data_8Y31
# 
_entry.id   8Y31 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8Y31         pdb_00008y31 10.2210/pdb8y31/pdb 
WWPDB D_1300044727 ?            ?                   
# 
_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       2024-12-04 
# 
_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                        8Y31 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              wfeng@ibp.ac.cn 
_pdbx_contact_author.name_first         Wei 
_pdbx_contact_author.name_last          Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9738-9398 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, W.'   1 0000-0001-6016-8399 
'Feng, W.' 2 0000-0001-9738-9398 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Int.J.Biol.Macromol. 
_citation.journal_id_ASTM           IJBMDR 
_citation.journal_id_CSD            0708 
_citation.journal_id_ISSN           0141-8130 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            268 
_citation.language                  ? 
_citation.page_first                131721 
_citation.page_last                 131721 
_citation.title                     
;Structural basis for the recognition of IFNAR1 by the humanized therapeutic monoclonal antibody QX006N for the treatment of systemic lupus erythematosus.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2024.131721 
_citation.pdbx_database_id_PubMed   38649079 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, X.' 1 ? 
primary 'Ke, H.'   2 ? 
primary 'Li, W.'   3 ? 
primary 'Yin, L.'  4 ? 
primary 'Chen, W.' 5 ? 
primary 'Chen, T.' 6 ? 
primary 'Wu, Y.'   7 ? 
primary 'Qiu, J.'  8 ? 
primary 'Feng, W.' 9 ? 
# 
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 QX006N-Fab-LC                      23200.725 2  ? ? ? ? 
2 polymer man QX006N-Fab-HC                      24517.518 2  ? ? ? ? 
3 polymer man 'Interferon alpha/beta receptor 1' 39767.223 2  ? ? ? ? 
4 water   nat water                              18.015    68 ? ? ? ? 
# 
_entity_name_com.entity_id   3 
_entity_name_com.name        
;IFN-R-1,IFN-alpha/beta receptor 1,Cytokine receptor class-II member 1,Cytokine receptor family 2 member 1,CRF2-1,Type I interferon receptor 1
;
# 
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 
;AIQMTQSPSSLSASVGDRVTITCQASQSISNQLSWYQQKPGKAPKLLIYDASSLASGVPSRFSGSRSGTKFTLTISSLQP
EDFATYYCLGIYGDGADDGIAFGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQS
GNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTQGTTSVTKSFNRGEC
;
;AIQMTQSPSSLSASVGDRVTITCQASQSISNQLSWYQQKPGKAPKLLIYDASSLASGVPSRFSGSRSGTKFTLTISSLQP
EDFATYYCLGIYGDGADDGIAFGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQS
GNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTQGTTSVTKSFNRGEC
;
A,C ? 
2 'polypeptide(L)' no no 
;EVQLVESGGGLVQPGGSLRLSCAASGFSLSSYYMTWVRQAPGKGLEWVSVINVYGGTYYASWAKGRFTISRDNSKNTLYL
QMNSLRAEDTAVYYCAREDVAVYMAIDLWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSW
NSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCGGHHHHHH
;
;EVQLVESGGGLVQPGGSLRLSCAASGFSLSSYYMTWVRQAPGKGLEWVSVINVYGGTYYASWAKGRFTISRDNSKNTLYL
QMNSLRAEDTAVYYCAREDVAVYMAIDLWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSW
NSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCGGHHHHHH
;
B,D ? 
3 'polypeptide(L)' no no 
;MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQ
NITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDG
LSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQ
NQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSE
EIKFDTEIQAFLLEVLFQGPHHHHHH
;
;MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQ
NITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDG
LSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQ
NQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSE
EIKFDTEIQAFLLEVLFQGPHHHHHH
;
E,F ? 
# 
_pdbx_entity_nonpoly.entity_id   4 
_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   ALA n 
1 2   ILE n 
1 3   GLN n 
1 4   MET n 
1 5   THR n 
1 6   GLN n 
1 7   SER n 
1 8   PRO n 
1 9   SER n 
1 10  SER n 
1 11  LEU n 
1 12  SER n 
1 13  ALA n 
1 14  SER n 
1 15  VAL n 
1 16  GLY n 
1 17  ASP n 
1 18  ARG n 
1 19  VAL n 
1 20  THR n 
1 21  ILE n 
1 22  THR n 
1 23  CYS n 
1 24  GLN n 
1 25  ALA n 
1 26  SER n 
1 27  GLN n 
1 28  SER n 
1 29  ILE n 
1 30  SER n 
1 31  ASN n 
1 32  GLN n 
1 33  LEU n 
1 34  SER n 
1 35  TRP n 
1 36  TYR n 
1 37  GLN n 
1 38  GLN n 
1 39  LYS n 
1 40  PRO n 
1 41  GLY n 
1 42  LYS n 
1 43  ALA n 
1 44  PRO n 
1 45  LYS n 
1 46  LEU n 
1 47  LEU n 
1 48  ILE n 
1 49  TYR n 
1 50  ASP n 
1 51  ALA n 
1 52  SER n 
1 53  SER n 
1 54  LEU n 
1 55  ALA n 
1 56  SER n 
1 57  GLY n 
1 58  VAL n 
1 59  PRO n 
1 60  SER n 
1 61  ARG n 
1 62  PHE n 
1 63  SER n 
1 64  GLY n 
1 65  SER n 
1 66  ARG n 
1 67  SER n 
1 68  GLY n 
1 69  THR n 
1 70  LYS n 
1 71  PHE n 
1 72  THR n 
1 73  LEU n 
1 74  THR n 
1 75  ILE n 
1 76  SER n 
1 77  SER n 
1 78  LEU n 
1 79  GLN n 
1 80  PRO n 
1 81  GLU n 
1 82  ASP n 
1 83  PHE n 
1 84  ALA n 
1 85  THR n 
1 86  TYR n 
1 87  TYR n 
1 88  CYS n 
1 89  LEU n 
1 90  GLY n 
1 91  ILE n 
1 92  TYR n 
1 93  GLY n 
1 94  ASP n 
1 95  GLY n 
1 96  ALA n 
1 97  ASP n 
1 98  ASP n 
1 99  GLY n 
1 100 ILE n 
1 101 ALA n 
1 102 PHE n 
1 103 GLY n 
1 104 GLY n 
1 105 GLY n 
1 106 THR n 
1 107 LYS n 
1 108 VAL n 
1 109 GLU n 
1 110 ILE n 
1 111 LYS n 
1 112 ARG n 
1 113 THR n 
1 114 VAL n 
1 115 ALA n 
1 116 ALA n 
1 117 PRO n 
1 118 SER n 
1 119 VAL n 
1 120 PHE n 
1 121 ILE n 
1 122 PHE n 
1 123 PRO n 
1 124 PRO n 
1 125 SER n 
1 126 ASP n 
1 127 GLU n 
1 128 GLN n 
1 129 LEU n 
1 130 LYS n 
1 131 SER n 
1 132 GLY n 
1 133 THR n 
1 134 ALA n 
1 135 SER n 
1 136 VAL n 
1 137 VAL n 
1 138 CYS n 
1 139 LEU n 
1 140 LEU n 
1 141 ASN n 
1 142 ASN n 
1 143 PHE n 
1 144 TYR n 
1 145 PRO n 
1 146 ARG n 
1 147 GLU n 
1 148 ALA n 
1 149 LYS n 
1 150 VAL n 
1 151 GLN n 
1 152 TRP n 
1 153 LYS n 
1 154 VAL n 
1 155 ASP n 
1 156 ASN n 
1 157 ALA n 
1 158 LEU n 
1 159 GLN n 
1 160 SER n 
1 161 GLY n 
1 162 ASN n 
1 163 SER n 
1 164 GLN n 
1 165 GLU n 
1 166 SER n 
1 167 VAL n 
1 168 THR n 
1 169 GLU n 
1 170 GLN n 
1 171 ASP n 
1 172 SER n 
1 173 LYS n 
1 174 ASP n 
1 175 SER n 
1 176 THR n 
1 177 TYR n 
1 178 SER n 
1 179 LEU n 
1 180 SER n 
1 181 SER n 
1 182 THR n 
1 183 LEU n 
1 184 THR n 
1 185 LEU n 
1 186 SER n 
1 187 LYS n 
1 188 ALA n 
1 189 ASP n 
1 190 TYR n 
1 191 GLU n 
1 192 LYS n 
1 193 HIS n 
1 194 LYS n 
1 195 VAL n 
1 196 TYR n 
1 197 ALA n 
1 198 CYS n 
1 199 GLU n 
1 200 VAL n 
1 201 THR n 
1 202 GLN n 
1 203 GLY n 
1 204 THR n 
1 205 THR n 
1 206 SER n 
1 207 VAL n 
1 208 THR n 
1 209 LYS n 
1 210 SER n 
1 211 PHE n 
1 212 ASN n 
1 213 ARG n 
1 214 GLY n 
1 215 GLU n 
1 216 CYS n 
2 1   GLU n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   VAL n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   GLY n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  GLN n 
2 14  PRO n 
2 15  GLY n 
2 16  GLY n 
2 17  SER n 
2 18  LEU n 
2 19  ARG n 
2 20  LEU n 
2 21  SER n 
2 22  CYS n 
2 23  ALA n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  PHE n 
2 28  SER n 
2 29  LEU n 
2 30  SER n 
2 31  SER n 
2 32  TYR n 
2 33  TYR n 
2 34  MET n 
2 35  THR n 
2 36  TRP n 
2 37  VAL n 
2 38  ARG n 
2 39  GLN n 
2 40  ALA n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  GLY n 
2 45  LEU n 
2 46  GLU n 
2 47  TRP n 
2 48  VAL n 
2 49  SER n 
2 50  VAL n 
2 51  ILE n 
2 52  ASN n 
2 53  VAL n 
2 54  TYR n 
2 55  GLY n 
2 56  GLY n 
2 57  THR n 
2 58  TYR n 
2 59  TYR n 
2 60  ALA n 
2 61  SER n 
2 62  TRP n 
2 63  ALA n 
2 64  LYS n 
2 65  GLY n 
2 66  ARG n 
2 67  PHE n 
2 68  THR n 
2 69  ILE n 
2 70  SER n 
2 71  ARG n 
2 72  ASP n 
2 73  ASN n 
2 74  SER n 
2 75  LYS n 
2 76  ASN n 
2 77  THR n 
2 78  LEU n 
2 79  TYR n 
2 80  LEU n 
2 81  GLN n 
2 82  MET n 
2 83  ASN n 
2 84  SER n 
2 85  LEU n 
2 86  ARG n 
2 87  ALA n 
2 88  GLU n 
2 89  ASP n 
2 90  THR n 
2 91  ALA n 
2 92  VAL n 
2 93  TYR n 
2 94  TYR n 
2 95  CYS n 
2 96  ALA n 
2 97  ARG n 
2 98  GLU n 
2 99  ASP n 
2 100 VAL n 
2 101 ALA n 
2 102 VAL n 
2 103 TYR n 
2 104 MET n 
2 105 ALA n 
2 106 ILE n 
2 107 ASP n 
2 108 LEU n 
2 109 TRP n 
2 110 GLY n 
2 111 GLN n 
2 112 GLY n 
2 113 THR n 
2 114 LEU n 
2 115 VAL n 
2 116 THR n 
2 117 VAL n 
2 118 SER n 
2 119 SER n 
2 120 ALA n 
2 121 SER n 
2 122 THR n 
2 123 LYS n 
2 124 GLY n 
2 125 PRO n 
2 126 SER n 
2 127 VAL n 
2 128 PHE n 
2 129 PRO n 
2 130 LEU n 
2 131 ALA n 
2 132 PRO n 
2 133 SER n 
2 134 SER n 
2 135 LYS n 
2 136 SER n 
2 137 THR n 
2 138 SER n 
2 139 GLY n 
2 140 GLY n 
2 141 THR n 
2 142 ALA n 
2 143 ALA n 
2 144 LEU n 
2 145 GLY n 
2 146 CYS n 
2 147 LEU n 
2 148 VAL n 
2 149 LYS n 
2 150 ASP n 
2 151 TYR n 
2 152 PHE n 
2 153 PRO n 
2 154 GLU n 
2 155 PRO n 
2 156 VAL n 
2 157 THR n 
2 158 VAL n 
2 159 SER n 
2 160 TRP n 
2 161 ASN n 
2 162 SER n 
2 163 GLY n 
2 164 ALA n 
2 165 LEU n 
2 166 THR n 
2 167 SER n 
2 168 GLY n 
2 169 VAL n 
2 170 HIS n 
2 171 THR n 
2 172 PHE n 
2 173 PRO n 
2 174 ALA n 
2 175 VAL n 
2 176 LEU n 
2 177 GLN n 
2 178 SER n 
2 179 SER n 
2 180 GLY n 
2 181 LEU n 
2 182 TYR n 
2 183 SER n 
2 184 LEU n 
2 185 SER n 
2 186 SER n 
2 187 VAL n 
2 188 VAL n 
2 189 THR n 
2 190 VAL n 
2 191 PRO n 
2 192 SER n 
2 193 SER n 
2 194 SER n 
2 195 LEU n 
2 196 GLY n 
2 197 THR n 
2 198 GLN n 
2 199 THR n 
2 200 TYR n 
2 201 ILE n 
2 202 CYS n 
2 203 ASN n 
2 204 VAL n 
2 205 ASN n 
2 206 HIS n 
2 207 LYS n 
2 208 PRO n 
2 209 SER n 
2 210 ASN n 
2 211 THR n 
2 212 LYS n 
2 213 VAL n 
2 214 ASP n 
2 215 LYS n 
2 216 LYS n 
2 217 VAL n 
2 218 GLU n 
2 219 PRO n 
2 220 LYS n 
2 221 SER n 
2 222 CYS n 
2 223 GLY n 
2 224 GLY n 
2 225 HIS n 
2 226 HIS n 
2 227 HIS n 
2 228 HIS n 
2 229 HIS n 
2 230 HIS n 
3 1   MET n 
3 2   MET n 
3 3   VAL n 
3 4   VAL n 
3 5   LEU n 
3 6   LEU n 
3 7   GLY n 
3 8   ALA n 
3 9   THR n 
3 10  THR n 
3 11  LEU n 
3 12  VAL n 
3 13  LEU n 
3 14  VAL n 
3 15  ALA n 
3 16  VAL n 
3 17  ALA n 
3 18  PRO n 
3 19  TRP n 
3 20  VAL n 
3 21  LEU n 
3 22  SER n 
3 23  ALA n 
3 24  ALA n 
3 25  ALA n 
3 26  GLY n 
3 27  GLY n 
3 28  LYS n 
3 29  ASN n 
3 30  LEU n 
3 31  LYS n 
3 32  SER n 
3 33  PRO n 
3 34  GLN n 
3 35  LYS n 
3 36  VAL n 
3 37  GLU n 
3 38  VAL n 
3 39  ASP n 
3 40  ILE n 
3 41  ILE n 
3 42  ASP n 
3 43  ASP n 
3 44  ASN n 
3 45  PHE n 
3 46  ILE n 
3 47  LEU n 
3 48  ARG n 
3 49  TRP n 
3 50  ASN n 
3 51  ARG n 
3 52  SER n 
3 53  ASP n 
3 54  GLU n 
3 55  SER n 
3 56  VAL n 
3 57  GLY n 
3 58  ASN n 
3 59  VAL n 
3 60  THR n 
3 61  PHE n 
3 62  SER n 
3 63  PHE n 
3 64  ASP n 
3 65  TYR n 
3 66  GLN n 
3 67  LYS n 
3 68  THR n 
3 69  GLY n 
3 70  MET n 
3 71  ASP n 
3 72  ASN n 
3 73  TRP n 
3 74  ILE n 
3 75  LYS n 
3 76  LEU n 
3 77  SER n 
3 78  GLY n 
3 79  CYS n 
3 80  GLN n 
3 81  ASN n 
3 82  ILE n 
3 83  THR n 
3 84  SER n 
3 85  THR n 
3 86  LYS n 
3 87  CYS n 
3 88  ASN n 
3 89  PHE n 
3 90  SER n 
3 91  SER n 
3 92  LEU n 
3 93  LYS n 
3 94  LEU n 
3 95  ASN n 
3 96  VAL n 
3 97  TYR n 
3 98  GLU n 
3 99  GLU n 
3 100 ILE n 
3 101 LYS n 
3 102 LEU n 
3 103 ARG n 
3 104 ILE n 
3 105 ARG n 
3 106 ALA n 
3 107 GLU n 
3 108 LYS n 
3 109 GLU n 
3 110 ASN n 
3 111 THR n 
3 112 SER n 
3 113 SER n 
3 114 TRP n 
3 115 TYR n 
3 116 GLU n 
3 117 VAL n 
3 118 ASP n 
3 119 SER n 
3 120 PHE n 
3 121 THR n 
3 122 PRO n 
3 123 PHE n 
3 124 ARG n 
3 125 LYS n 
3 126 ALA n 
3 127 GLN n 
3 128 ILE n 
3 129 GLY n 
3 130 PRO n 
3 131 PRO n 
3 132 GLU n 
3 133 VAL n 
3 134 HIS n 
3 135 LEU n 
3 136 GLU n 
3 137 ALA n 
3 138 GLU n 
3 139 ASP n 
3 140 LYS n 
3 141 ALA n 
3 142 ILE n 
3 143 VAL n 
3 144 ILE n 
3 145 HIS n 
3 146 ILE n 
3 147 SER n 
3 148 PRO n 
3 149 GLY n 
3 150 THR n 
3 151 LYS n 
3 152 ASP n 
3 153 SER n 
3 154 VAL n 
3 155 MET n 
3 156 TRP n 
3 157 ALA n 
3 158 LEU n 
3 159 ASP n 
3 160 GLY n 
3 161 LEU n 
3 162 SER n 
3 163 PHE n 
3 164 THR n 
3 165 TYR n 
3 166 SER n 
3 167 LEU n 
3 168 VAL n 
3 169 ILE n 
3 170 TRP n 
3 171 LYS n 
3 172 ASN n 
3 173 SER n 
3 174 SER n 
3 175 GLY n 
3 176 VAL n 
3 177 GLU n 
3 178 GLU n 
3 179 ARG n 
3 180 ILE n 
3 181 GLU n 
3 182 ASN n 
3 183 ILE n 
3 184 TYR n 
3 185 SER n 
3 186 ARG n 
3 187 HIS n 
3 188 LYS n 
3 189 ILE n 
3 190 TYR n 
3 191 LYS n 
3 192 LEU n 
3 193 SER n 
3 194 PRO n 
3 195 GLU n 
3 196 THR n 
3 197 THR n 
3 198 TYR n 
3 199 CYS n 
3 200 LEU n 
3 201 LYS n 
3 202 VAL n 
3 203 LYS n 
3 204 ALA n 
3 205 ALA n 
3 206 LEU n 
3 207 LEU n 
3 208 THR n 
3 209 SER n 
3 210 TRP n 
3 211 LYS n 
3 212 ILE n 
3 213 GLY n 
3 214 VAL n 
3 215 TYR n 
3 216 SER n 
3 217 PRO n 
3 218 VAL n 
3 219 HIS n 
3 220 CYS n 
3 221 ILE n 
3 222 LYS n 
3 223 THR n 
3 224 THR n 
3 225 VAL n 
3 226 GLU n 
3 227 ASN n 
3 228 GLU n 
3 229 LEU n 
3 230 PRO n 
3 231 PRO n 
3 232 PRO n 
3 233 GLU n 
3 234 ASN n 
3 235 ILE n 
3 236 GLU n 
3 237 VAL n 
3 238 SER n 
3 239 VAL n 
3 240 GLN n 
3 241 ASN n 
3 242 GLN n 
3 243 ASN n 
3 244 TYR n 
3 245 VAL n 
3 246 LEU n 
3 247 LYS n 
3 248 TRP n 
3 249 ASP n 
3 250 TYR n 
3 251 THR n 
3 252 TYR n 
3 253 ALA n 
3 254 ASN n 
3 255 MET n 
3 256 THR n 
3 257 PHE n 
3 258 GLN n 
3 259 VAL n 
3 260 GLN n 
3 261 TRP n 
3 262 LEU n 
3 263 HIS n 
3 264 ALA n 
3 265 PHE n 
3 266 LEU n 
3 267 LYS n 
3 268 ARG n 
3 269 ASN n 
3 270 PRO n 
3 271 GLY n 
3 272 ASN n 
3 273 HIS n 
3 274 LEU n 
3 275 TYR n 
3 276 LYS n 
3 277 TRP n 
3 278 LYS n 
3 279 GLN n 
3 280 ILE n 
3 281 PRO n 
3 282 ASP n 
3 283 CYS n 
3 284 GLU n 
3 285 ASN n 
3 286 VAL n 
3 287 LYS n 
3 288 THR n 
3 289 THR n 
3 290 GLN n 
3 291 CYS n 
3 292 VAL n 
3 293 PHE n 
3 294 PRO n 
3 295 GLN n 
3 296 ASN n 
3 297 VAL n 
3 298 PHE n 
3 299 GLN n 
3 300 LYS n 
3 301 GLY n 
3 302 ILE n 
3 303 TYR n 
3 304 LEU n 
3 305 LEU n 
3 306 ARG n 
3 307 VAL n 
3 308 GLN n 
3 309 ALA n 
3 310 SER n 
3 311 ASP n 
3 312 GLY n 
3 313 ASN n 
3 314 ASN n 
3 315 THR n 
3 316 SER n 
3 317 PHE n 
3 318 TRP n 
3 319 SER n 
3 320 GLU n 
3 321 GLU n 
3 322 ILE n 
3 323 LYS n 
3 324 PHE n 
3 325 ASP n 
3 326 THR n 
3 327 GLU n 
3 328 ILE n 
3 329 GLN n 
3 330 ALA n 
3 331 PHE n 
3 332 LEU n 
3 333 LEU n 
3 334 GLU n 
3 335 VAL n 
3 336 LEU n 
3 337 PHE n 
3 338 GLN n 
3 339 GLY n 
3 340 PRO n 
3 341 HIS n 
3 342 HIS n 
3 343 HIS n 
3 344 HIS n 
3 345 HIS n 
3 346 HIS 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' 1 216 human ? ?               ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 230 human ? ?               ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 346 human ? 'IFNAR1, IFNAR' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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   ALA 1   1   1   ALA ALA A . n 
A 1 2   ILE 2   2   2   ILE ILE A . n 
A 1 3   GLN 3   3   3   GLN GLN A . n 
A 1 4   MET 4   4   4   MET MET A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   GLN 6   6   6   GLN GLN A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   SER 9   9   9   SER SER A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  SER 12  12  12  SER SER A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ASP 17  17  17  ASP ASP A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  THR 20  20  20  THR THR A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  CYS 23  23  23  CYS CYS A . n 
A 1 24  GLN 24  24  24  GLN GLN A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  SER 30  30  30  SER SER A . n 
A 1 31  ASN 31  31  31  ASN ASN A . n 
A 1 32  GLN 32  32  32  GLN GLN A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  TRP 35  35  35  TRP TRP A . n 
A 1 36  TYR 36  36  36  TYR TYR A . n 
A 1 37  GLN 37  37  37  GLN GLN A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  ILE 48  48  48  ILE ILE A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  PRO 59  59  59  PRO PRO A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  PHE 62  62  62  PHE PHE A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  THR 69  69  69  THR THR A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  PHE 71  71  71  PHE PHE A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  PRO 80  80  80  PRO PRO A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  PHE 83  83  83  PHE PHE A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  TYR 86  86  86  TYR TYR A . n 
A 1 87  TYR 87  87  87  TYR TYR A . n 
A 1 88  CYS 88  88  88  CYS CYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  TYR 92  92  92  TYR TYR A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 PHE 102 102 102 PHE PHE A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 VAL 108 108 108 VAL VAL A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 THR 113 113 113 THR THR A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 PHE 120 120 120 PHE PHE A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 PRO 123 123 123 PRO PRO A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 SER 125 125 125 SER SER A . n 
A 1 126 ASP 126 126 126 ASP ASP A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 LYS 130 130 130 LYS LYS A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 THR 133 133 133 THR THR A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 SER 135 135 135 SER SER A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 CYS 138 138 138 CYS CYS A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ASN 141 141 141 ASN ASN A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 PHE 143 143 143 PHE PHE A . n 
A 1 144 TYR 144 144 144 TYR TYR A . n 
A 1 145 PRO 145 145 145 PRO PRO A . n 
A 1 146 ARG 146 146 146 ARG ARG A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 LYS 149 149 149 LYS LYS A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 GLN 151 151 151 GLN GLN A . n 
A 1 152 TRP 152 152 152 TRP TRP A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 VAL 154 154 154 VAL VAL A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 ALA 157 157 157 ALA ALA A . n 
A 1 158 LEU 158 158 158 LEU LEU A . n 
A 1 159 GLN 159 159 159 GLN GLN A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 GLN 164 164 164 GLN GLN A . n 
A 1 165 GLU 165 165 165 GLU GLU A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 GLU 169 169 169 GLU GLU A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 LYS 173 173 173 LYS LYS A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 TYR 177 177 177 TYR TYR A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 THR 184 184 184 THR THR A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 LYS 187 187 187 LYS LYS A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 LYS 192 192 192 LYS LYS A . n 
A 1 193 HIS 193 193 193 HIS HIS A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 CYS 198 198 198 CYS CYS A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 GLN 202 202 202 GLN GLN A . n 
A 1 203 GLY 203 203 203 GLY GLY A . n 
A 1 204 THR 204 204 204 THR THR A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 THR 208 208 208 THR THR A . n 
A 1 209 LYS 209 209 209 LYS LYS A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 ASN 212 212 212 ASN ASN A . n 
A 1 213 ARG 213 213 213 ARG ARG A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 CYS 216 216 ?   ?   ?   A . n 
B 2 1   GLU 1   1   1   GLU GLU B . n 
B 2 2   VAL 2   2   2   VAL VAL B . n 
B 2 3   GLN 3   3   3   GLN GLN B . n 
B 2 4   LEU 4   4   4   LEU LEU B . n 
B 2 5   VAL 5   5   5   VAL VAL B . n 
B 2 6   GLU 6   6   6   GLU GLU B . n 
B 2 7   SER 7   7   7   SER SER B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   GLY 9   9   9   GLY GLY B . n 
B 2 10  GLY 10  10  10  GLY GLY B . n 
B 2 11  LEU 11  11  11  LEU LEU B . n 
B 2 12  VAL 12  12  12  VAL VAL B . n 
B 2 13  GLN 13  13  13  GLN GLN B . n 
B 2 14  PRO 14  14  14  PRO PRO B . n 
B 2 15  GLY 15  15  15  GLY GLY B . n 
B 2 16  GLY 16  16  16  GLY GLY B . n 
B 2 17  SER 17  17  17  SER SER B . n 
B 2 18  LEU 18  18  18  LEU LEU B . n 
B 2 19  ARG 19  19  19  ARG ARG B . n 
B 2 20  LEU 20  20  20  LEU LEU B . n 
B 2 21  SER 21  21  21  SER SER B . n 
B 2 22  CYS 22  22  22  CYS CYS B . n 
B 2 23  ALA 23  23  23  ALA ALA B . n 
B 2 24  ALA 24  24  24  ALA ALA B . n 
B 2 25  SER 25  25  25  SER SER B . n 
B 2 26  GLY 26  26  26  GLY GLY B . n 
B 2 27  PHE 27  27  27  PHE PHE B . n 
B 2 28  SER 28  28  28  SER SER B . n 
B 2 29  LEU 29  29  29  LEU LEU B . n 
B 2 30  SER 30  30  30  SER SER B . n 
B 2 31  SER 31  31  31  SER SER B . n 
B 2 32  TYR 32  32  32  TYR TYR B . n 
B 2 33  TYR 33  33  33  TYR TYR B . n 
B 2 34  MET 34  34  34  MET MET B . n 
B 2 35  THR 35  35  35  THR THR B . n 
B 2 36  TRP 36  36  36  TRP TRP B . n 
B 2 37  VAL 37  37  37  VAL VAL B . n 
B 2 38  ARG 38  38  38  ARG ARG B . n 
B 2 39  GLN 39  39  39  GLN GLN B . n 
B 2 40  ALA 40  40  40  ALA ALA B . n 
B 2 41  PRO 41  41  41  PRO PRO B . n 
B 2 42  GLY 42  42  42  GLY GLY B . n 
B 2 43  LYS 43  43  43  LYS LYS B . n 
B 2 44  GLY 44  44  44  GLY GLY B . n 
B 2 45  LEU 45  45  45  LEU LEU B . n 
B 2 46  GLU 46  46  46  GLU GLU B . n 
B 2 47  TRP 47  47  47  TRP TRP B . n 
B 2 48  VAL 48  48  48  VAL VAL B . n 
B 2 49  SER 49  49  49  SER SER B . n 
B 2 50  VAL 50  50  50  VAL VAL B . n 
B 2 51  ILE 51  51  51  ILE ILE B . n 
B 2 52  ASN 52  52  52  ASN ASN B . n 
B 2 53  VAL 53  53  53  VAL VAL B . n 
B 2 54  TYR 54  54  54  TYR TYR B . n 
B 2 55  GLY 55  55  55  GLY GLY B . n 
B 2 56  GLY 56  56  56  GLY GLY B . n 
B 2 57  THR 57  57  57  THR THR B . n 
B 2 58  TYR 58  58  58  TYR TYR B . n 
B 2 59  TYR 59  59  59  TYR TYR B . n 
B 2 60  ALA 60  60  60  ALA ALA B . n 
B 2 61  SER 61  61  61  SER SER B . n 
B 2 62  TRP 62  62  62  TRP TRP B . n 
B 2 63  ALA 63  63  63  ALA ALA B . n 
B 2 64  LYS 64  64  64  LYS LYS B . n 
B 2 65  GLY 65  65  65  GLY GLY B . n 
B 2 66  ARG 66  66  66  ARG ARG B . n 
B 2 67  PHE 67  67  67  PHE PHE B . n 
B 2 68  THR 68  68  68  THR THR B . n 
B 2 69  ILE 69  69  69  ILE ILE B . n 
B 2 70  SER 70  70  70  SER SER B . n 
B 2 71  ARG 71  71  71  ARG ARG B . n 
B 2 72  ASP 72  72  72  ASP ASP B . n 
B 2 73  ASN 73  73  73  ASN ASN B . n 
B 2 74  SER 74  74  74  SER SER B . n 
B 2 75  LYS 75  75  75  LYS LYS B . n 
B 2 76  ASN 76  76  76  ASN ASN B . n 
B 2 77  THR 77  77  77  THR THR B . n 
B 2 78  LEU 78  78  78  LEU LEU B . n 
B 2 79  TYR 79  79  79  TYR TYR B . n 
B 2 80  LEU 80  80  80  LEU LEU B . n 
B 2 81  GLN 81  81  81  GLN GLN B . n 
B 2 82  MET 82  82  82  MET MET B . n 
B 2 83  ASN 83  83  83  ASN ASN B . n 
B 2 84  SER 84  84  84  SER SER B . n 
B 2 85  LEU 85  85  85  LEU LEU B . n 
B 2 86  ARG 86  86  86  ARG ARG B . n 
B 2 87  ALA 87  87  87  ALA ALA B . n 
B 2 88  GLU 88  88  88  GLU GLU B . n 
B 2 89  ASP 89  89  89  ASP ASP B . n 
B 2 90  THR 90  90  90  THR THR B . n 
B 2 91  ALA 91  91  91  ALA ALA B . n 
B 2 92  VAL 92  92  92  VAL VAL B . n 
B 2 93  TYR 93  93  93  TYR TYR B . n 
B 2 94  TYR 94  94  94  TYR TYR B . n 
B 2 95  CYS 95  95  95  CYS CYS B . n 
B 2 96  ALA 96  96  96  ALA ALA B . n 
B 2 97  ARG 97  97  97  ARG ARG B . n 
B 2 98  GLU 98  98  98  GLU GLU B . n 
B 2 99  ASP 99  99  99  ASP ASP B . n 
B 2 100 VAL 100 100 100 VAL VAL B . n 
B 2 101 ALA 101 101 101 ALA ALA B . n 
B 2 102 VAL 102 102 102 VAL VAL B . n 
B 2 103 TYR 103 103 103 TYR TYR B . n 
B 2 104 MET 104 104 104 MET MET B . n 
B 2 105 ALA 105 105 105 ALA ALA B . n 
B 2 106 ILE 106 106 106 ILE ILE B . n 
B 2 107 ASP 107 107 107 ASP ASP B . n 
B 2 108 LEU 108 108 108 LEU LEU B . n 
B 2 109 TRP 109 109 109 TRP TRP B . n 
B 2 110 GLY 110 110 110 GLY GLY B . n 
B 2 111 GLN 111 111 111 GLN GLN B . n 
B 2 112 GLY 112 112 112 GLY GLY B . n 
B 2 113 THR 113 113 113 THR THR B . n 
B 2 114 LEU 114 114 114 LEU LEU B . n 
B 2 115 VAL 115 115 115 VAL VAL B . n 
B 2 116 THR 116 116 116 THR THR B . n 
B 2 117 VAL 117 117 117 VAL VAL B . n 
B 2 118 SER 118 118 118 SER SER B . n 
B 2 119 SER 119 119 119 SER SER B . n 
B 2 120 ALA 120 120 120 ALA ALA B . n 
B 2 121 SER 121 121 121 SER SER B . n 
B 2 122 THR 122 122 122 THR THR B . n 
B 2 123 LYS 123 123 123 LYS LYS B . n 
B 2 124 GLY 124 124 124 GLY GLY B . n 
B 2 125 PRO 125 125 125 PRO PRO B . n 
B 2 126 SER 126 126 126 SER SER B . n 
B 2 127 VAL 127 127 127 VAL VAL B . n 
B 2 128 PHE 128 128 128 PHE PHE B . n 
B 2 129 PRO 129 129 129 PRO PRO B . n 
B 2 130 LEU 130 130 130 LEU LEU B . n 
B 2 131 ALA 131 131 131 ALA ALA B . n 
B 2 132 PRO 132 132 132 PRO PRO B . n 
B 2 133 SER 133 133 133 SER SER B . n 
B 2 134 SER 134 134 134 SER SER B . n 
B 2 135 LYS 135 135 135 LYS LYS B . n 
B 2 136 SER 136 136 136 SER SER B . n 
B 2 137 THR 137 137 137 THR THR B . n 
B 2 138 SER 138 138 138 SER SER B . n 
B 2 139 GLY 139 139 139 GLY GLY B . n 
B 2 140 GLY 140 140 140 GLY GLY B . n 
B 2 141 THR 141 141 141 THR THR B . n 
B 2 142 ALA 142 142 142 ALA ALA B . n 
B 2 143 ALA 143 143 143 ALA ALA B . n 
B 2 144 LEU 144 144 144 LEU LEU B . n 
B 2 145 GLY 145 145 145 GLY GLY B . n 
B 2 146 CYS 146 146 146 CYS CYS B . n 
B 2 147 LEU 147 147 147 LEU LEU B . n 
B 2 148 VAL 148 148 148 VAL VAL B . n 
B 2 149 LYS 149 149 149 LYS LYS B . n 
B 2 150 ASP 150 150 150 ASP ASP B . n 
B 2 151 TYR 151 151 151 TYR TYR B . n 
B 2 152 PHE 152 152 152 PHE PHE B . n 
B 2 153 PRO 153 153 153 PRO PRO B . n 
B 2 154 GLU 154 154 154 GLU GLU B . n 
B 2 155 PRO 155 155 155 PRO PRO B . n 
B 2 156 VAL 156 156 156 VAL VAL B . n 
B 2 157 THR 157 157 157 THR THR B . n 
B 2 158 VAL 158 158 158 VAL VAL B . n 
B 2 159 SER 159 159 159 SER SER B . n 
B 2 160 TRP 160 160 160 TRP TRP B . n 
B 2 161 ASN 161 161 161 ASN ASN B . n 
B 2 162 SER 162 162 162 SER SER B . n 
B 2 163 GLY 163 163 163 GLY GLY B . n 
B 2 164 ALA 164 164 164 ALA ALA B . n 
B 2 165 LEU 165 165 165 LEU LEU B . n 
B 2 166 THR 166 166 166 THR THR B . n 
B 2 167 SER 167 167 167 SER SER B . n 
B 2 168 GLY 168 168 168 GLY GLY B . n 
B 2 169 VAL 169 169 169 VAL VAL B . n 
B 2 170 HIS 170 170 170 HIS HIS B . n 
B 2 171 THR 171 171 171 THR THR B . n 
B 2 172 PHE 172 172 172 PHE PHE B . n 
B 2 173 PRO 173 173 173 PRO PRO B . n 
B 2 174 ALA 174 174 174 ALA ALA B . n 
B 2 175 VAL 175 175 175 VAL VAL B . n 
B 2 176 LEU 176 176 176 LEU LEU B . n 
B 2 177 GLN 177 177 177 GLN GLN B . n 
B 2 178 SER 178 178 178 SER SER B . n 
B 2 179 SER 179 179 179 SER SER B . n 
B 2 180 GLY 180 180 180 GLY GLY B . n 
B 2 181 LEU 181 181 181 LEU LEU B . n 
B 2 182 TYR 182 182 182 TYR TYR B . n 
B 2 183 SER 183 183 183 SER SER B . n 
B 2 184 LEU 184 184 184 LEU LEU B . n 
B 2 185 SER 185 185 185 SER SER B . n 
B 2 186 SER 186 186 186 SER SER B . n 
B 2 187 VAL 187 187 187 VAL VAL B . n 
B 2 188 VAL 188 188 188 VAL VAL B . n 
B 2 189 THR 189 189 189 THR THR B . n 
B 2 190 VAL 190 190 190 VAL VAL B . n 
B 2 191 PRO 191 191 191 PRO PRO B . n 
B 2 192 SER 192 192 192 SER SER B . n 
B 2 193 SER 193 193 193 SER SER B . n 
B 2 194 SER 194 194 194 SER SER B . n 
B 2 195 LEU 195 195 195 LEU LEU B . n 
B 2 196 GLY 196 196 196 GLY GLY B . n 
B 2 197 THR 197 197 197 THR THR B . n 
B 2 198 GLN 198 198 198 GLN GLN B . n 
B 2 199 THR 199 199 199 THR THR B . n 
B 2 200 TYR 200 200 200 TYR TYR B . n 
B 2 201 ILE 201 201 201 ILE ILE B . n 
B 2 202 CYS 202 202 202 CYS CYS B . n 
B 2 203 ASN 203 203 203 ASN ASN B . n 
B 2 204 VAL 204 204 204 VAL VAL B . n 
B 2 205 ASN 205 205 205 ASN ASN B . n 
B 2 206 HIS 206 206 206 HIS HIS B . n 
B 2 207 LYS 207 207 207 LYS LYS B . n 
B 2 208 PRO 208 208 208 PRO PRO B . n 
B 2 209 SER 209 209 209 SER SER B . n 
B 2 210 ASN 210 210 210 ASN ASN B . n 
B 2 211 THR 211 211 211 THR THR B . n 
B 2 212 LYS 212 212 212 LYS LYS B . n 
B 2 213 VAL 213 213 213 VAL VAL B . n 
B 2 214 ASP 214 214 214 ASP ASP B . n 
B 2 215 LYS 215 215 215 LYS LYS B . n 
B 2 216 LYS 216 216 216 LYS LYS B . n 
B 2 217 VAL 217 217 217 VAL VAL B . n 
B 2 218 GLU 218 218 218 GLU GLU B . n 
B 2 219 PRO 219 219 219 PRO PRO B . n 
B 2 220 LYS 220 220 220 LYS LYS B . n 
B 2 221 SER 221 221 221 SER SER B . n 
B 2 222 CYS 222 222 ?   ?   ?   B . n 
B 2 223 GLY 223 223 ?   ?   ?   B . n 
B 2 224 GLY 224 224 ?   ?   ?   B . n 
B 2 225 HIS 225 225 ?   ?   ?   B . n 
B 2 226 HIS 226 226 ?   ?   ?   B . n 
B 2 227 HIS 227 227 ?   ?   ?   B . n 
B 2 228 HIS 228 228 ?   ?   ?   B . n 
B 2 229 HIS 229 229 ?   ?   ?   B . n 
B 2 230 HIS 230 230 ?   ?   ?   B . n 
C 1 1   ALA 1   1   1   ALA ALA C . n 
C 1 2   ILE 2   2   2   ILE ILE C . n 
C 1 3   GLN 3   3   3   GLN GLN C . n 
C 1 4   MET 4   4   4   MET MET C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   GLN 6   6   6   GLN GLN C . n 
C 1 7   SER 7   7   7   SER SER C . n 
C 1 8   PRO 8   8   8   PRO PRO C . n 
C 1 9   SER 9   9   9   SER SER C . n 
C 1 10  SER 10  10  10  SER SER C . n 
C 1 11  LEU 11  11  11  LEU LEU C . n 
C 1 12  SER 12  12  12  SER SER C . n 
C 1 13  ALA 13  13  13  ALA ALA C . n 
C 1 14  SER 14  14  14  SER SER C . n 
C 1 15  VAL 15  15  15  VAL VAL C . n 
C 1 16  GLY 16  16  16  GLY GLY C . n 
C 1 17  ASP 17  17  17  ASP ASP C . n 
C 1 18  ARG 18  18  18  ARG ARG C . n 
C 1 19  VAL 19  19  19  VAL VAL C . n 
C 1 20  THR 20  20  20  THR THR C . n 
C 1 21  ILE 21  21  21  ILE ILE C . n 
C 1 22  THR 22  22  22  THR THR C . n 
C 1 23  CYS 23  23  23  CYS CYS C . n 
C 1 24  GLN 24  24  24  GLN GLN C . n 
C 1 25  ALA 25  25  25  ALA ALA C . n 
C 1 26  SER 26  26  26  SER SER C . n 
C 1 27  GLN 27  27  27  GLN GLN C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  ILE 29  29  29  ILE ILE C . n 
C 1 30  SER 30  30  30  SER SER C . n 
C 1 31  ASN 31  31  31  ASN ASN C . n 
C 1 32  GLN 32  32  32  GLN GLN C . n 
C 1 33  LEU 33  33  33  LEU LEU C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  TRP 35  35  35  TRP TRP C . n 
C 1 36  TYR 36  36  36  TYR TYR C . n 
C 1 37  GLN 37  37  37  GLN GLN C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  LYS 39  39  39  LYS LYS C . n 
C 1 40  PRO 40  40  40  PRO PRO C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  LYS 42  42  42  LYS LYS C . n 
C 1 43  ALA 43  43  43  ALA ALA C . n 
C 1 44  PRO 44  44  44  PRO PRO C . n 
C 1 45  LYS 45  45  45  LYS LYS C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  LEU 47  47  47  LEU LEU C . n 
C 1 48  ILE 48  48  48  ILE ILE C . n 
C 1 49  TYR 49  49  49  TYR TYR C . n 
C 1 50  ASP 50  50  50  ASP ASP C . n 
C 1 51  ALA 51  51  51  ALA ALA C . n 
C 1 52  SER 52  52  52  SER SER C . n 
C 1 53  SER 53  53  53  SER SER C . n 
C 1 54  LEU 54  54  54  LEU LEU C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  SER 56  56  56  SER SER C . n 
C 1 57  GLY 57  57  57  GLY GLY C . n 
C 1 58  VAL 58  58  58  VAL VAL C . n 
C 1 59  PRO 59  59  59  PRO PRO C . n 
C 1 60  SER 60  60  60  SER SER C . n 
C 1 61  ARG 61  61  61  ARG ARG C . n 
C 1 62  PHE 62  62  62  PHE PHE C . n 
C 1 63  SER 63  63  63  SER SER C . n 
C 1 64  GLY 64  64  64  GLY GLY C . n 
C 1 65  SER 65  65  65  SER SER C . n 
C 1 66  ARG 66  66  66  ARG ARG C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  GLY 68  68  68  GLY GLY C . n 
C 1 69  THR 69  69  69  THR THR C . n 
C 1 70  LYS 70  70  70  LYS LYS C . n 
C 1 71  PHE 71  71  71  PHE PHE C . n 
C 1 72  THR 72  72  72  THR THR C . n 
C 1 73  LEU 73  73  73  LEU LEU C . n 
C 1 74  THR 74  74  74  THR THR C . n 
C 1 75  ILE 75  75  75  ILE ILE C . n 
C 1 76  SER 76  76  76  SER SER C . n 
C 1 77  SER 77  77  77  SER SER C . n 
C 1 78  LEU 78  78  78  LEU LEU C . n 
C 1 79  GLN 79  79  79  GLN GLN C . n 
C 1 80  PRO 80  80  80  PRO PRO C . n 
C 1 81  GLU 81  81  81  GLU GLU C . n 
C 1 82  ASP 82  82  82  ASP ASP C . n 
C 1 83  PHE 83  83  83  PHE PHE C . n 
C 1 84  ALA 84  84  84  ALA ALA C . n 
C 1 85  THR 85  85  85  THR THR C . n 
C 1 86  TYR 86  86  86  TYR TYR C . n 
C 1 87  TYR 87  87  87  TYR TYR C . n 
C 1 88  CYS 88  88  88  CYS CYS C . n 
C 1 89  LEU 89  89  89  LEU LEU C . n 
C 1 90  GLY 90  90  90  GLY GLY C . n 
C 1 91  ILE 91  91  91  ILE ILE C . n 
C 1 92  TYR 92  92  92  TYR TYR C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  ASP 94  94  94  ASP ASP C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  ALA 96  96  96  ALA ALA C . n 
C 1 97  ASP 97  97  97  ASP ASP C . n 
C 1 98  ASP 98  98  98  ASP ASP C . n 
C 1 99  GLY 99  99  99  GLY GLY C . n 
C 1 100 ILE 100 100 100 ILE ILE C . n 
C 1 101 ALA 101 101 101 ALA ALA C . n 
C 1 102 PHE 102 102 102 PHE PHE C . n 
C 1 103 GLY 103 103 103 GLY GLY C . n 
C 1 104 GLY 104 104 104 GLY GLY C . n 
C 1 105 GLY 105 105 105 GLY GLY C . n 
C 1 106 THR 106 106 106 THR THR C . n 
C 1 107 LYS 107 107 107 LYS LYS C . n 
C 1 108 VAL 108 108 108 VAL VAL C . n 
C 1 109 GLU 109 109 109 GLU GLU C . n 
C 1 110 ILE 110 110 110 ILE ILE C . n 
C 1 111 LYS 111 111 111 LYS LYS C . n 
C 1 112 ARG 112 112 112 ARG ARG C . n 
C 1 113 THR 113 113 113 THR THR C . n 
C 1 114 VAL 114 114 114 VAL VAL C . n 
C 1 115 ALA 115 115 115 ALA ALA C . n 
C 1 116 ALA 116 116 116 ALA ALA C . n 
C 1 117 PRO 117 117 117 PRO PRO C . n 
C 1 118 SER 118 118 118 SER SER C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 PHE 120 120 120 PHE PHE C . n 
C 1 121 ILE 121 121 121 ILE ILE C . n 
C 1 122 PHE 122 122 122 PHE PHE C . n 
C 1 123 PRO 123 123 123 PRO PRO C . n 
C 1 124 PRO 124 124 124 PRO PRO C . n 
C 1 125 SER 125 125 125 SER SER C . n 
C 1 126 ASP 126 126 126 ASP ASP C . n 
C 1 127 GLU 127 127 127 GLU GLU C . n 
C 1 128 GLN 128 128 128 GLN GLN C . n 
C 1 129 LEU 129 129 129 LEU LEU C . n 
C 1 130 LYS 130 130 130 LYS LYS C . n 
C 1 131 SER 131 131 131 SER SER C . n 
C 1 132 GLY 132 132 132 GLY GLY C . n 
C 1 133 THR 133 133 133 THR THR C . n 
C 1 134 ALA 134 134 134 ALA ALA C . n 
C 1 135 SER 135 135 135 SER SER C . n 
C 1 136 VAL 136 136 136 VAL VAL C . n 
C 1 137 VAL 137 137 137 VAL VAL C . n 
C 1 138 CYS 138 138 138 CYS CYS C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 LEU 140 140 140 LEU LEU C . n 
C 1 141 ASN 141 141 141 ASN ASN C . n 
C 1 142 ASN 142 142 142 ASN ASN C . n 
C 1 143 PHE 143 143 143 PHE PHE C . n 
C 1 144 TYR 144 144 144 TYR TYR C . n 
C 1 145 PRO 145 145 145 PRO PRO C . n 
C 1 146 ARG 146 146 146 ARG ARG C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 ALA 148 148 148 ALA ALA C . n 
C 1 149 LYS 149 149 149 LYS LYS C . n 
C 1 150 VAL 150 150 150 VAL VAL C . n 
C 1 151 GLN 151 151 151 GLN GLN C . n 
C 1 152 TRP 152 152 152 TRP TRP C . n 
C 1 153 LYS 153 153 153 LYS LYS C . n 
C 1 154 VAL 154 154 154 VAL VAL C . n 
C 1 155 ASP 155 155 155 ASP ASP C . n 
C 1 156 ASN 156 156 156 ASN ASN C . n 
C 1 157 ALA 157 157 157 ALA ALA C . n 
C 1 158 LEU 158 158 158 LEU LEU C . n 
C 1 159 GLN 159 159 159 GLN GLN C . n 
C 1 160 SER 160 160 160 SER SER C . n 
C 1 161 GLY 161 161 161 GLY GLY C . n 
C 1 162 ASN 162 162 162 ASN ASN C . n 
C 1 163 SER 163 163 163 SER SER C . n 
C 1 164 GLN 164 164 164 GLN GLN C . n 
C 1 165 GLU 165 165 165 GLU GLU C . n 
C 1 166 SER 166 166 166 SER SER C . n 
C 1 167 VAL 167 167 167 VAL VAL C . n 
C 1 168 THR 168 168 168 THR THR C . n 
C 1 169 GLU 169 169 169 GLU GLU C . n 
C 1 170 GLN 170 170 170 GLN GLN C . n 
C 1 171 ASP 171 171 171 ASP ASP C . n 
C 1 172 SER 172 172 172 SER SER C . n 
C 1 173 LYS 173 173 173 LYS LYS C . n 
C 1 174 ASP 174 174 174 ASP ASP C . n 
C 1 175 SER 175 175 175 SER SER C . n 
C 1 176 THR 176 176 176 THR THR C . n 
C 1 177 TYR 177 177 177 TYR TYR C . n 
C 1 178 SER 178 178 178 SER SER C . n 
C 1 179 LEU 179 179 179 LEU LEU C . n 
C 1 180 SER 180 180 180 SER SER C . n 
C 1 181 SER 181 181 181 SER SER C . n 
C 1 182 THR 182 182 182 THR THR C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 THR 184 184 184 THR THR C . n 
C 1 185 LEU 185 185 185 LEU LEU C . n 
C 1 186 SER 186 186 186 SER SER C . n 
C 1 187 LYS 187 187 187 LYS LYS C . n 
C 1 188 ALA 188 188 188 ALA ALA C . n 
C 1 189 ASP 189 189 189 ASP ASP C . n 
C 1 190 TYR 190 190 190 TYR TYR C . n 
C 1 191 GLU 191 191 191 GLU GLU C . n 
C 1 192 LYS 192 192 192 LYS LYS C . n 
C 1 193 HIS 193 193 193 HIS HIS C . n 
C 1 194 LYS 194 194 194 LYS LYS C . n 
C 1 195 VAL 195 195 195 VAL VAL C . n 
C 1 196 TYR 196 196 196 TYR TYR C . n 
C 1 197 ALA 197 197 197 ALA ALA C . n 
C 1 198 CYS 198 198 198 CYS CYS C . n 
C 1 199 GLU 199 199 199 GLU GLU C . n 
C 1 200 VAL 200 200 200 VAL VAL C . n 
C 1 201 THR 201 201 201 THR THR C . n 
C 1 202 GLN 202 202 202 GLN GLN C . n 
C 1 203 GLY 203 203 203 GLY GLY C . n 
C 1 204 THR 204 204 204 THR THR C . n 
C 1 205 THR 205 205 205 THR THR C . n 
C 1 206 SER 206 206 206 SER SER C . n 
C 1 207 VAL 207 207 207 VAL VAL C . n 
C 1 208 THR 208 208 208 THR THR C . n 
C 1 209 LYS 209 209 209 LYS LYS C . n 
C 1 210 SER 210 210 210 SER SER C . n 
C 1 211 PHE 211 211 211 PHE PHE C . n 
C 1 212 ASN 212 212 212 ASN ASN C . n 
C 1 213 ARG 213 213 213 ARG ARG C . n 
C 1 214 GLY 214 214 214 GLY GLY C . n 
C 1 215 GLU 215 215 215 GLU GLU C . n 
C 1 216 CYS 216 216 ?   ?   ?   C . n 
D 2 1   GLU 1   1   1   GLU GLU D . n 
D 2 2   VAL 2   2   2   VAL VAL D . n 
D 2 3   GLN 3   3   3   GLN GLN D . n 
D 2 4   LEU 4   4   4   LEU LEU D . n 
D 2 5   VAL 5   5   5   VAL VAL D . n 
D 2 6   GLU 6   6   6   GLU GLU D . n 
D 2 7   SER 7   7   7   SER SER D . n 
D 2 8   GLY 8   8   8   GLY GLY D . n 
D 2 9   GLY 9   9   9   GLY GLY D . n 
D 2 10  GLY 10  10  10  GLY GLY D . n 
D 2 11  LEU 11  11  11  LEU LEU D . n 
D 2 12  VAL 12  12  12  VAL VAL D . n 
D 2 13  GLN 13  13  13  GLN GLN D . n 
D 2 14  PRO 14  14  14  PRO PRO D . n 
D 2 15  GLY 15  15  15  GLY GLY D . n 
D 2 16  GLY 16  16  16  GLY GLY D . n 
D 2 17  SER 17  17  17  SER SER D . n 
D 2 18  LEU 18  18  18  LEU LEU D . n 
D 2 19  ARG 19  19  19  ARG ARG D . n 
D 2 20  LEU 20  20  20  LEU LEU D . n 
D 2 21  SER 21  21  21  SER SER D . n 
D 2 22  CYS 22  22  22  CYS CYS D . n 
D 2 23  ALA 23  23  23  ALA ALA D . n 
D 2 24  ALA 24  24  24  ALA ALA D . n 
D 2 25  SER 25  25  25  SER SER D . n 
D 2 26  GLY 26  26  26  GLY GLY D . n 
D 2 27  PHE 27  27  27  PHE PHE D . n 
D 2 28  SER 28  28  28  SER SER D . n 
D 2 29  LEU 29  29  29  LEU LEU D . n 
D 2 30  SER 30  30  30  SER SER D . n 
D 2 31  SER 31  31  31  SER SER D . n 
D 2 32  TYR 32  32  32  TYR TYR D . n 
D 2 33  TYR 33  33  33  TYR TYR D . n 
D 2 34  MET 34  34  34  MET MET D . n 
D 2 35  THR 35  35  35  THR THR D . n 
D 2 36  TRP 36  36  36  TRP TRP D . n 
D 2 37  VAL 37  37  37  VAL VAL D . n 
D 2 38  ARG 38  38  38  ARG ARG D . n 
D 2 39  GLN 39  39  39  GLN GLN D . n 
D 2 40  ALA 40  40  40  ALA ALA D . n 
D 2 41  PRO 41  41  41  PRO PRO D . n 
D 2 42  GLY 42  42  42  GLY GLY D . n 
D 2 43  LYS 43  43  43  LYS LYS D . n 
D 2 44  GLY 44  44  44  GLY GLY D . n 
D 2 45  LEU 45  45  45  LEU LEU D . n 
D 2 46  GLU 46  46  46  GLU GLU D . n 
D 2 47  TRP 47  47  47  TRP TRP D . n 
D 2 48  VAL 48  48  48  VAL VAL D . n 
D 2 49  SER 49  49  49  SER SER D . n 
D 2 50  VAL 50  50  50  VAL VAL D . n 
D 2 51  ILE 51  51  51  ILE ILE D . n 
D 2 52  ASN 52  52  52  ASN ASN D . n 
D 2 53  VAL 53  53  53  VAL VAL D . n 
D 2 54  TYR 54  54  54  TYR TYR D . n 
D 2 55  GLY 55  55  55  GLY GLY D . n 
D 2 56  GLY 56  56  56  GLY GLY D . n 
D 2 57  THR 57  57  57  THR THR D . n 
D 2 58  TYR 58  58  58  TYR TYR D . n 
D 2 59  TYR 59  59  59  TYR TYR D . n 
D 2 60  ALA 60  60  60  ALA ALA D . n 
D 2 61  SER 61  61  61  SER SER D . n 
D 2 62  TRP 62  62  62  TRP TRP D . n 
D 2 63  ALA 63  63  63  ALA ALA D . n 
D 2 64  LYS 64  64  64  LYS LYS D . n 
D 2 65  GLY 65  65  65  GLY GLY D . n 
D 2 66  ARG 66  66  66  ARG ARG D . n 
D 2 67  PHE 67  67  67  PHE PHE D . n 
D 2 68  THR 68  68  68  THR THR D . n 
D 2 69  ILE 69  69  69  ILE ILE D . n 
D 2 70  SER 70  70  70  SER SER D . n 
D 2 71  ARG 71  71  71  ARG ARG D . n 
D 2 72  ASP 72  72  72  ASP ASP D . n 
D 2 73  ASN 73  73  73  ASN ASN D . n 
D 2 74  SER 74  74  74  SER SER D . n 
D 2 75  LYS 75  75  75  LYS LYS D . n 
D 2 76  ASN 76  76  76  ASN ASN D . n 
D 2 77  THR 77  77  77  THR THR D . n 
D 2 78  LEU 78  78  78  LEU LEU D . n 
D 2 79  TYR 79  79  79  TYR TYR D . n 
D 2 80  LEU 80  80  80  LEU LEU D . n 
D 2 81  GLN 81  81  81  GLN GLN D . n 
D 2 82  MET 82  82  82  MET MET D . n 
D 2 83  ASN 83  83  83  ASN ASN D . n 
D 2 84  SER 84  84  84  SER SER D . n 
D 2 85  LEU 85  85  85  LEU LEU D . n 
D 2 86  ARG 86  86  86  ARG ARG D . n 
D 2 87  ALA 87  87  87  ALA ALA D . n 
D 2 88  GLU 88  88  88  GLU GLU D . n 
D 2 89  ASP 89  89  89  ASP ASP D . n 
D 2 90  THR 90  90  90  THR THR D . n 
D 2 91  ALA 91  91  91  ALA ALA D . n 
D 2 92  VAL 92  92  92  VAL VAL D . n 
D 2 93  TYR 93  93  93  TYR TYR D . n 
D 2 94  TYR 94  94  94  TYR TYR D . n 
D 2 95  CYS 95  95  95  CYS CYS D . n 
D 2 96  ALA 96  96  96  ALA ALA D . n 
D 2 97  ARG 97  97  97  ARG ARG D . n 
D 2 98  GLU 98  98  98  GLU GLU D . n 
D 2 99  ASP 99  99  99  ASP ASP D . n 
D 2 100 VAL 100 100 100 VAL VAL D . n 
D 2 101 ALA 101 101 101 ALA ALA D . n 
D 2 102 VAL 102 102 102 VAL VAL D . n 
D 2 103 TYR 103 103 103 TYR TYR D . n 
D 2 104 MET 104 104 104 MET MET D . n 
D 2 105 ALA 105 105 105 ALA ALA D . n 
D 2 106 ILE 106 106 106 ILE ILE D . n 
D 2 107 ASP 107 107 107 ASP ASP D . n 
D 2 108 LEU 108 108 108 LEU LEU D . n 
D 2 109 TRP 109 109 109 TRP TRP D . n 
D 2 110 GLY 110 110 110 GLY GLY D . n 
D 2 111 GLN 111 111 111 GLN GLN D . n 
D 2 112 GLY 112 112 112 GLY GLY D . n 
D 2 113 THR 113 113 113 THR THR D . n 
D 2 114 LEU 114 114 114 LEU LEU D . n 
D 2 115 VAL 115 115 115 VAL VAL D . n 
D 2 116 THR 116 116 116 THR THR D . n 
D 2 117 VAL 117 117 117 VAL VAL D . n 
D 2 118 SER 118 118 118 SER SER D . n 
D 2 119 SER 119 119 119 SER SER D . n 
D 2 120 ALA 120 120 120 ALA ALA D . n 
D 2 121 SER 121 121 121 SER SER D . n 
D 2 122 THR 122 122 122 THR THR D . n 
D 2 123 LYS 123 123 123 LYS LYS D . n 
D 2 124 GLY 124 124 124 GLY GLY D . n 
D 2 125 PRO 125 125 125 PRO PRO D . n 
D 2 126 SER 126 126 126 SER SER D . n 
D 2 127 VAL 127 127 127 VAL VAL D . n 
D 2 128 PHE 128 128 128 PHE PHE D . n 
D 2 129 PRO 129 129 129 PRO PRO D . n 
D 2 130 LEU 130 130 130 LEU LEU D . n 
D 2 131 ALA 131 131 131 ALA ALA D . n 
D 2 132 PRO 132 132 132 PRO PRO D . n 
D 2 133 SER 133 133 133 SER SER D . n 
D 2 134 SER 134 134 134 SER SER D . n 
D 2 135 LYS 135 135 135 LYS LYS D . n 
D 2 136 SER 136 136 136 SER SER D . n 
D 2 137 THR 137 137 137 THR THR D . n 
D 2 138 SER 138 138 138 SER SER D . n 
D 2 139 GLY 139 139 139 GLY GLY D . n 
D 2 140 GLY 140 140 140 GLY GLY D . n 
D 2 141 THR 141 141 141 THR THR D . n 
D 2 142 ALA 142 142 142 ALA ALA D . n 
D 2 143 ALA 143 143 143 ALA ALA D . n 
D 2 144 LEU 144 144 144 LEU LEU D . n 
D 2 145 GLY 145 145 145 GLY GLY D . n 
D 2 146 CYS 146 146 146 CYS CYS D . n 
D 2 147 LEU 147 147 147 LEU LEU D . n 
D 2 148 VAL 148 148 148 VAL VAL D . n 
D 2 149 LYS 149 149 149 LYS LYS D . n 
D 2 150 ASP 150 150 150 ASP ASP D . n 
D 2 151 TYR 151 151 151 TYR TYR D . n 
D 2 152 PHE 152 152 152 PHE PHE D . n 
D 2 153 PRO 153 153 153 PRO PRO D . n 
D 2 154 GLU 154 154 154 GLU GLU D . n 
D 2 155 PRO 155 155 155 PRO PRO D . n 
D 2 156 VAL 156 156 156 VAL VAL D . n 
D 2 157 THR 157 157 157 THR THR D . n 
D 2 158 VAL 158 158 158 VAL VAL D . n 
D 2 159 SER 159 159 159 SER SER D . n 
D 2 160 TRP 160 160 160 TRP TRP D . n 
D 2 161 ASN 161 161 161 ASN ASN D . n 
D 2 162 SER 162 162 162 SER SER D . n 
D 2 163 GLY 163 163 163 GLY GLY D . n 
D 2 164 ALA 164 164 164 ALA ALA D . n 
D 2 165 LEU 165 165 165 LEU LEU D . n 
D 2 166 THR 166 166 166 THR THR D . n 
D 2 167 SER 167 167 167 SER SER D . n 
D 2 168 GLY 168 168 168 GLY GLY D . n 
D 2 169 VAL 169 169 169 VAL VAL D . n 
D 2 170 HIS 170 170 170 HIS HIS D . n 
D 2 171 THR 171 171 171 THR THR D . n 
D 2 172 PHE 172 172 172 PHE PHE D . n 
D 2 173 PRO 173 173 173 PRO PRO D . n 
D 2 174 ALA 174 174 174 ALA ALA D . n 
D 2 175 VAL 175 175 175 VAL VAL D . n 
D 2 176 LEU 176 176 176 LEU LEU D . n 
D 2 177 GLN 177 177 177 GLN GLN D . n 
D 2 178 SER 178 178 178 SER SER D . n 
D 2 179 SER 179 179 179 SER SER D . n 
D 2 180 GLY 180 180 180 GLY GLY D . n 
D 2 181 LEU 181 181 181 LEU LEU D . n 
D 2 182 TYR 182 182 182 TYR TYR D . n 
D 2 183 SER 183 183 183 SER SER D . n 
D 2 184 LEU 184 184 184 LEU LEU D . n 
D 2 185 SER 185 185 185 SER SER D . n 
D 2 186 SER 186 186 186 SER SER D . n 
D 2 187 VAL 187 187 187 VAL VAL D . n 
D 2 188 VAL 188 188 188 VAL VAL D . n 
D 2 189 THR 189 189 189 THR THR D . n 
D 2 190 VAL 190 190 190 VAL VAL D . n 
D 2 191 PRO 191 191 191 PRO PRO D . n 
D 2 192 SER 192 192 192 SER SER D . n 
D 2 193 SER 193 193 193 SER SER D . n 
D 2 194 SER 194 194 194 SER SER D . n 
D 2 195 LEU 195 195 195 LEU LEU D . n 
D 2 196 GLY 196 196 196 GLY GLY D . n 
D 2 197 THR 197 197 197 THR THR D . n 
D 2 198 GLN 198 198 198 GLN GLN D . n 
D 2 199 THR 199 199 199 THR THR D . n 
D 2 200 TYR 200 200 200 TYR TYR D . n 
D 2 201 ILE 201 201 201 ILE ILE D . n 
D 2 202 CYS 202 202 202 CYS CYS D . n 
D 2 203 ASN 203 203 203 ASN ASN D . n 
D 2 204 VAL 204 204 204 VAL VAL D . n 
D 2 205 ASN 205 205 205 ASN ASN D . n 
D 2 206 HIS 206 206 206 HIS HIS D . n 
D 2 207 LYS 207 207 207 LYS LYS D . n 
D 2 208 PRO 208 208 208 PRO PRO D . n 
D 2 209 SER 209 209 209 SER SER D . n 
D 2 210 ASN 210 210 210 ASN ASN D . n 
D 2 211 THR 211 211 211 THR THR D . n 
D 2 212 LYS 212 212 212 LYS LYS D . n 
D 2 213 VAL 213 213 213 VAL VAL D . n 
D 2 214 ASP 214 214 214 ASP ASP D . n 
D 2 215 LYS 215 215 215 LYS LYS D . n 
D 2 216 LYS 216 216 216 LYS LYS D . n 
D 2 217 VAL 217 217 217 VAL VAL D . n 
D 2 218 GLU 218 218 218 GLU GLU D . n 
D 2 219 PRO 219 219 219 PRO PRO D . n 
D 2 220 LYS 220 220 220 LYS LYS D . n 
D 2 221 SER 221 221 221 SER SER D . n 
D 2 222 CYS 222 222 ?   ?   ?   D . n 
D 2 223 GLY 223 223 ?   ?   ?   D . n 
D 2 224 GLY 224 224 ?   ?   ?   D . n 
D 2 225 HIS 225 225 ?   ?   ?   D . n 
D 2 226 HIS 226 226 ?   ?   ?   D . n 
D 2 227 HIS 227 227 ?   ?   ?   D . n 
D 2 228 HIS 228 228 ?   ?   ?   D . n 
D 2 229 HIS 229 229 ?   ?   ?   D . n 
D 2 230 HIS 230 230 ?   ?   ?   D . n 
E 3 1   MET 1   1   ?   ?   ?   E . n 
E 3 2   MET 2   2   ?   ?   ?   E . n 
E 3 3   VAL 3   3   ?   ?   ?   E . n 
E 3 4   VAL 4   4   ?   ?   ?   E . n 
E 3 5   LEU 5   5   ?   ?   ?   E . n 
E 3 6   LEU 6   6   ?   ?   ?   E . n 
E 3 7   GLY 7   7   ?   ?   ?   E . n 
E 3 8   ALA 8   8   ?   ?   ?   E . n 
E 3 9   THR 9   9   ?   ?   ?   E . n 
E 3 10  THR 10  10  ?   ?   ?   E . n 
E 3 11  LEU 11  11  ?   ?   ?   E . n 
E 3 12  VAL 12  12  ?   ?   ?   E . n 
E 3 13  LEU 13  13  ?   ?   ?   E . n 
E 3 14  VAL 14  14  ?   ?   ?   E . n 
E 3 15  ALA 15  15  ?   ?   ?   E . n 
E 3 16  VAL 16  16  ?   ?   ?   E . n 
E 3 17  ALA 17  17  ?   ?   ?   E . n 
E 3 18  PRO 18  18  ?   ?   ?   E . n 
E 3 19  TRP 19  19  ?   ?   ?   E . n 
E 3 20  VAL 20  20  ?   ?   ?   E . n 
E 3 21  LEU 21  21  ?   ?   ?   E . n 
E 3 22  SER 22  22  ?   ?   ?   E . n 
E 3 23  ALA 23  23  ?   ?   ?   E . n 
E 3 24  ALA 24  24  ?   ?   ?   E . n 
E 3 25  ALA 25  25  ?   ?   ?   E . n 
E 3 26  GLY 26  26  ?   ?   ?   E . n 
E 3 27  GLY 27  27  ?   ?   ?   E . n 
E 3 28  LYS 28  28  ?   ?   ?   E . n 
E 3 29  ASN 29  29  ?   ?   ?   E . n 
E 3 30  LEU 30  30  ?   ?   ?   E . n 
E 3 31  LYS 31  31  ?   ?   ?   E . n 
E 3 32  SER 32  32  ?   ?   ?   E . n 
E 3 33  PRO 33  33  ?   ?   ?   E . n 
E 3 34  GLN 34  34  ?   ?   ?   E . n 
E 3 35  LYS 35  35  ?   ?   ?   E . n 
E 3 36  VAL 36  36  ?   ?   ?   E . n 
E 3 37  GLU 37  37  ?   ?   ?   E . n 
E 3 38  VAL 38  38  ?   ?   ?   E . n 
E 3 39  ASP 39  39  ?   ?   ?   E . n 
E 3 40  ILE 40  40  ?   ?   ?   E . n 
E 3 41  ILE 41  41  ?   ?   ?   E . n 
E 3 42  ASP 42  42  ?   ?   ?   E . n 
E 3 43  ASP 43  43  ?   ?   ?   E . n 
E 3 44  ASN 44  44  ?   ?   ?   E . n 
E 3 45  PHE 45  45  ?   ?   ?   E . n 
E 3 46  ILE 46  46  ?   ?   ?   E . n 
E 3 47  LEU 47  47  ?   ?   ?   E . n 
E 3 48  ARG 48  48  ?   ?   ?   E . n 
E 3 49  TRP 49  49  ?   ?   ?   E . n 
E 3 50  ASN 50  50  ?   ?   ?   E . n 
E 3 51  ARG 51  51  ?   ?   ?   E . n 
E 3 52  SER 52  52  ?   ?   ?   E . n 
E 3 53  ASP 53  53  ?   ?   ?   E . n 
E 3 54  GLU 54  54  ?   ?   ?   E . n 
E 3 55  SER 55  55  ?   ?   ?   E . n 
E 3 56  VAL 56  56  ?   ?   ?   E . n 
E 3 57  GLY 57  57  ?   ?   ?   E . n 
E 3 58  ASN 58  58  ?   ?   ?   E . n 
E 3 59  VAL 59  59  ?   ?   ?   E . n 
E 3 60  THR 60  60  ?   ?   ?   E . n 
E 3 61  PHE 61  61  ?   ?   ?   E . n 
E 3 62  SER 62  62  ?   ?   ?   E . n 
E 3 63  PHE 63  63  ?   ?   ?   E . n 
E 3 64  ASP 64  64  ?   ?   ?   E . n 
E 3 65  TYR 65  65  ?   ?   ?   E . n 
E 3 66  GLN 66  66  ?   ?   ?   E . n 
E 3 67  LYS 67  67  ?   ?   ?   E . n 
E 3 68  THR 68  68  ?   ?   ?   E . n 
E 3 69  GLY 69  69  ?   ?   ?   E . n 
E 3 70  MET 70  70  ?   ?   ?   E . n 
E 3 71  ASP 71  71  ?   ?   ?   E . n 
E 3 72  ASN 72  72  ?   ?   ?   E . n 
E 3 73  TRP 73  73  ?   ?   ?   E . n 
E 3 74  ILE 74  74  ?   ?   ?   E . n 
E 3 75  LYS 75  75  ?   ?   ?   E . n 
E 3 76  LEU 76  76  ?   ?   ?   E . n 
E 3 77  SER 77  77  ?   ?   ?   E . n 
E 3 78  GLY 78  78  ?   ?   ?   E . n 
E 3 79  CYS 79  79  ?   ?   ?   E . n 
E 3 80  GLN 80  80  ?   ?   ?   E . n 
E 3 81  ASN 81  81  ?   ?   ?   E . n 
E 3 82  ILE 82  82  ?   ?   ?   E . n 
E 3 83  THR 83  83  ?   ?   ?   E . n 
E 3 84  SER 84  84  ?   ?   ?   E . n 
E 3 85  THR 85  85  ?   ?   ?   E . n 
E 3 86  LYS 86  86  ?   ?   ?   E . n 
E 3 87  CYS 87  87  ?   ?   ?   E . n 
E 3 88  ASN 88  88  ?   ?   ?   E . n 
E 3 89  PHE 89  89  ?   ?   ?   E . n 
E 3 90  SER 90  90  ?   ?   ?   E . n 
E 3 91  SER 91  91  ?   ?   ?   E . n 
E 3 92  LEU 92  92  ?   ?   ?   E . n 
E 3 93  LYS 93  93  ?   ?   ?   E . n 
E 3 94  LEU 94  94  ?   ?   ?   E . n 
E 3 95  ASN 95  95  ?   ?   ?   E . n 
E 3 96  VAL 96  96  ?   ?   ?   E . n 
E 3 97  TYR 97  97  ?   ?   ?   E . n 
E 3 98  GLU 98  98  ?   ?   ?   E . n 
E 3 99  GLU 99  99  ?   ?   ?   E . n 
E 3 100 ILE 100 100 ?   ?   ?   E . n 
E 3 101 LYS 101 101 ?   ?   ?   E . n 
E 3 102 LEU 102 102 ?   ?   ?   E . n 
E 3 103 ARG 103 103 ?   ?   ?   E . n 
E 3 104 ILE 104 104 ?   ?   ?   E . n 
E 3 105 ARG 105 105 ?   ?   ?   E . n 
E 3 106 ALA 106 106 ?   ?   ?   E . n 
E 3 107 GLU 107 107 ?   ?   ?   E . n 
E 3 108 LYS 108 108 ?   ?   ?   E . n 
E 3 109 GLU 109 109 ?   ?   ?   E . n 
E 3 110 ASN 110 110 ?   ?   ?   E . n 
E 3 111 THR 111 111 ?   ?   ?   E . n 
E 3 112 SER 112 112 ?   ?   ?   E . n 
E 3 113 SER 113 113 ?   ?   ?   E . n 
E 3 114 TRP 114 114 ?   ?   ?   E . n 
E 3 115 TYR 115 115 ?   ?   ?   E . n 
E 3 116 GLU 116 116 ?   ?   ?   E . n 
E 3 117 VAL 117 117 ?   ?   ?   E . n 
E 3 118 ASP 118 118 ?   ?   ?   E . n 
E 3 119 SER 119 119 ?   ?   ?   E . n 
E 3 120 PHE 120 120 ?   ?   ?   E . n 
E 3 121 THR 121 121 ?   ?   ?   E . n 
E 3 122 PRO 122 122 ?   ?   ?   E . n 
E 3 123 PHE 123 123 ?   ?   ?   E . n 
E 3 124 ARG 124 124 ?   ?   ?   E . n 
E 3 125 LYS 125 125 ?   ?   ?   E . n 
E 3 126 ALA 126 126 ?   ?   ?   E . n 
E 3 127 GLN 127 127 ?   ?   ?   E . n 
E 3 128 ILE 128 128 ?   ?   ?   E . n 
E 3 129 GLY 129 129 ?   ?   ?   E . n 
E 3 130 PRO 130 130 ?   ?   ?   E . n 
E 3 131 PRO 131 131 ?   ?   ?   E . n 
E 3 132 GLU 132 132 ?   ?   ?   E . n 
E 3 133 VAL 133 133 ?   ?   ?   E . n 
E 3 134 HIS 134 134 ?   ?   ?   E . n 
E 3 135 LEU 135 135 ?   ?   ?   E . n 
E 3 136 GLU 136 136 ?   ?   ?   E . n 
E 3 137 ALA 137 137 ?   ?   ?   E . n 
E 3 138 GLU 138 138 ?   ?   ?   E . n 
E 3 139 ASP 139 139 ?   ?   ?   E . n 
E 3 140 LYS 140 140 ?   ?   ?   E . n 
E 3 141 ALA 141 141 ?   ?   ?   E . n 
E 3 142 ILE 142 142 ?   ?   ?   E . n 
E 3 143 VAL 143 143 ?   ?   ?   E . n 
E 3 144 ILE 144 144 ?   ?   ?   E . n 
E 3 145 HIS 145 145 ?   ?   ?   E . n 
E 3 146 ILE 146 146 ?   ?   ?   E . n 
E 3 147 SER 147 147 ?   ?   ?   E . n 
E 3 148 PRO 148 148 ?   ?   ?   E . n 
E 3 149 GLY 149 149 ?   ?   ?   E . n 
E 3 150 THR 150 150 ?   ?   ?   E . n 
E 3 151 LYS 151 151 ?   ?   ?   E . n 
E 3 152 ASP 152 152 ?   ?   ?   E . n 
E 3 153 SER 153 153 ?   ?   ?   E . n 
E 3 154 VAL 154 154 ?   ?   ?   E . n 
E 3 155 MET 155 155 ?   ?   ?   E . n 
E 3 156 TRP 156 156 ?   ?   ?   E . n 
E 3 157 ALA 157 157 ?   ?   ?   E . n 
E 3 158 LEU 158 158 ?   ?   ?   E . n 
E 3 159 ASP 159 159 ?   ?   ?   E . n 
E 3 160 GLY 160 160 ?   ?   ?   E . n 
E 3 161 LEU 161 161 ?   ?   ?   E . n 
E 3 162 SER 162 162 ?   ?   ?   E . n 
E 3 163 PHE 163 163 ?   ?   ?   E . n 
E 3 164 THR 164 164 ?   ?   ?   E . n 
E 3 165 TYR 165 165 ?   ?   ?   E . n 
E 3 166 SER 166 166 ?   ?   ?   E . n 
E 3 167 LEU 167 167 ?   ?   ?   E . n 
E 3 168 VAL 168 168 ?   ?   ?   E . n 
E 3 169 ILE 169 169 ?   ?   ?   E . n 
E 3 170 TRP 170 170 ?   ?   ?   E . n 
E 3 171 LYS 171 171 ?   ?   ?   E . n 
E 3 172 ASN 172 172 ?   ?   ?   E . n 
E 3 173 SER 173 173 ?   ?   ?   E . n 
E 3 174 SER 174 174 ?   ?   ?   E . n 
E 3 175 GLY 175 175 ?   ?   ?   E . n 
E 3 176 VAL 176 176 ?   ?   ?   E . n 
E 3 177 GLU 177 177 ?   ?   ?   E . n 
E 3 178 GLU 178 178 ?   ?   ?   E . n 
E 3 179 ARG 179 179 ?   ?   ?   E . n 
E 3 180 ILE 180 180 ?   ?   ?   E . n 
E 3 181 GLU 181 181 ?   ?   ?   E . n 
E 3 182 ASN 182 182 ?   ?   ?   E . n 
E 3 183 ILE 183 183 ?   ?   ?   E . n 
E 3 184 TYR 184 184 ?   ?   ?   E . n 
E 3 185 SER 185 185 ?   ?   ?   E . n 
E 3 186 ARG 186 186 ?   ?   ?   E . n 
E 3 187 HIS 187 187 ?   ?   ?   E . n 
E 3 188 LYS 188 188 ?   ?   ?   E . n 
E 3 189 ILE 189 189 ?   ?   ?   E . n 
E 3 190 TYR 190 190 ?   ?   ?   E . n 
E 3 191 LYS 191 191 ?   ?   ?   E . n 
E 3 192 LEU 192 192 ?   ?   ?   E . n 
E 3 193 SER 193 193 ?   ?   ?   E . n 
E 3 194 PRO 194 194 ?   ?   ?   E . n 
E 3 195 GLU 195 195 ?   ?   ?   E . n 
E 3 196 THR 196 196 ?   ?   ?   E . n 
E 3 197 THR 197 197 ?   ?   ?   E . n 
E 3 198 TYR 198 198 ?   ?   ?   E . n 
E 3 199 CYS 199 199 ?   ?   ?   E . n 
E 3 200 LEU 200 200 ?   ?   ?   E . n 
E 3 201 LYS 201 201 ?   ?   ?   E . n 
E 3 202 VAL 202 202 ?   ?   ?   E . n 
E 3 203 LYS 203 203 ?   ?   ?   E . n 
E 3 204 ALA 204 204 ?   ?   ?   E . n 
E 3 205 ALA 205 205 ?   ?   ?   E . n 
E 3 206 LEU 206 206 ?   ?   ?   E . n 
E 3 207 LEU 207 207 ?   ?   ?   E . n 
E 3 208 THR 208 208 ?   ?   ?   E . n 
E 3 209 SER 209 209 ?   ?   ?   E . n 
E 3 210 TRP 210 210 ?   ?   ?   E . n 
E 3 211 LYS 211 211 ?   ?   ?   E . n 
E 3 212 ILE 212 212 ?   ?   ?   E . n 
E 3 213 GLY 213 213 ?   ?   ?   E . n 
E 3 214 VAL 214 214 ?   ?   ?   E . n 
E 3 215 TYR 215 215 ?   ?   ?   E . n 
E 3 216 SER 216 216 ?   ?   ?   E . n 
E 3 217 PRO 217 217 ?   ?   ?   E . n 
E 3 218 VAL 218 218 ?   ?   ?   E . n 
E 3 219 HIS 219 219 ?   ?   ?   E . n 
E 3 220 CYS 220 220 ?   ?   ?   E . n 
E 3 221 ILE 221 221 ?   ?   ?   E . n 
E 3 222 LYS 222 222 ?   ?   ?   E . n 
E 3 223 THR 223 223 ?   ?   ?   E . n 
E 3 224 THR 224 224 ?   ?   ?   E . n 
E 3 225 VAL 225 225 ?   ?   ?   E . n 
E 3 226 GLU 226 226 ?   ?   ?   E . n 
E 3 227 ASN 227 227 ?   ?   ?   E . n 
E 3 228 GLU 228 228 228 GLU GLU E . n 
E 3 229 LEU 229 229 229 LEU LEU E . n 
E 3 230 PRO 230 230 230 PRO PRO E . n 
E 3 231 PRO 231 231 231 PRO PRO E . n 
E 3 232 PRO 232 232 232 PRO PRO E . n 
E 3 233 GLU 233 233 233 GLU GLU E . n 
E 3 234 ASN 234 234 234 ASN ASN E . n 
E 3 235 ILE 235 235 235 ILE ILE E . n 
E 3 236 GLU 236 236 236 GLU GLU E . n 
E 3 237 VAL 237 237 237 VAL VAL E . n 
E 3 238 SER 238 238 238 SER SER E . n 
E 3 239 VAL 239 239 239 VAL VAL E . n 
E 3 240 GLN 240 240 240 GLN GLN E . n 
E 3 241 ASN 241 241 241 ASN ASN E . n 
E 3 242 GLN 242 242 242 GLN GLN E . n 
E 3 243 ASN 243 243 243 ASN ASN E . n 
E 3 244 TYR 244 244 244 TYR TYR E . n 
E 3 245 VAL 245 245 245 VAL VAL E . n 
E 3 246 LEU 246 246 246 LEU LEU E . n 
E 3 247 LYS 247 247 247 LYS LYS E . n 
E 3 248 TRP 248 248 248 TRP TRP E . n 
E 3 249 ASP 249 249 249 ASP ASP E . n 
E 3 250 TYR 250 250 250 TYR TYR E . n 
E 3 251 THR 251 251 251 THR THR E . n 
E 3 252 TYR 252 252 252 TYR TYR E . n 
E 3 253 ALA 253 253 253 ALA ALA E . n 
E 3 254 ASN 254 254 254 ASN ASN E . n 
E 3 255 MET 255 255 255 MET MET E . n 
E 3 256 THR 256 256 256 THR THR E . n 
E 3 257 PHE 257 257 257 PHE PHE E . n 
E 3 258 GLN 258 258 258 GLN GLN E . n 
E 3 259 VAL 259 259 259 VAL VAL E . n 
E 3 260 GLN 260 260 260 GLN GLN E . n 
E 3 261 TRP 261 261 261 TRP TRP E . n 
E 3 262 LEU 262 262 262 LEU LEU E . n 
E 3 263 HIS 263 263 263 HIS HIS E . n 
E 3 264 ALA 264 264 264 ALA ALA E . n 
E 3 265 PHE 265 265 265 PHE PHE E . n 
E 3 266 LEU 266 266 266 LEU LEU E . n 
E 3 267 LYS 267 267 267 LYS LYS E . n 
E 3 268 ARG 268 268 268 ARG ARG E . n 
E 3 269 ASN 269 269 269 ASN ASN E . n 
E 3 270 PRO 270 270 270 PRO PRO E . n 
E 3 271 GLY 271 271 271 GLY GLY E . n 
E 3 272 ASN 272 272 272 ASN ASN E . n 
E 3 273 HIS 273 273 273 HIS HIS E . n 
E 3 274 LEU 274 274 274 LEU LEU E . n 
E 3 275 TYR 275 275 275 TYR TYR E . n 
E 3 276 LYS 276 276 276 LYS LYS E . n 
E 3 277 TRP 277 277 277 TRP TRP E . n 
E 3 278 LYS 278 278 278 LYS LYS E . n 
E 3 279 GLN 279 279 279 GLN GLN E . n 
E 3 280 ILE 280 280 280 ILE ILE E . n 
E 3 281 PRO 281 281 281 PRO PRO E . n 
E 3 282 ASP 282 282 282 ASP ASP E . n 
E 3 283 CYS 283 283 283 CYS CYS E . n 
E 3 284 GLU 284 284 284 GLU GLU E . n 
E 3 285 ASN 285 285 285 ASN ASN E . n 
E 3 286 VAL 286 286 286 VAL VAL E . n 
E 3 287 LYS 287 287 287 LYS LYS E . n 
E 3 288 THR 288 288 288 THR THR E . n 
E 3 289 THR 289 289 289 THR THR E . n 
E 3 290 GLN 290 290 290 GLN GLN E . n 
E 3 291 CYS 291 291 291 CYS CYS E . n 
E 3 292 VAL 292 292 292 VAL VAL E . n 
E 3 293 PHE 293 293 293 PHE PHE E . n 
E 3 294 PRO 294 294 294 PRO PRO E . n 
E 3 295 GLN 295 295 295 GLN GLN E . n 
E 3 296 ASN 296 296 296 ASN ASN E . n 
E 3 297 VAL 297 297 297 VAL VAL E . n 
E 3 298 PHE 298 298 298 PHE PHE E . n 
E 3 299 GLN 299 299 299 GLN GLN E . n 
E 3 300 LYS 300 300 300 LYS LYS E . n 
E 3 301 GLY 301 301 301 GLY GLY E . n 
E 3 302 ILE 302 302 302 ILE ILE E . n 
E 3 303 TYR 303 303 303 TYR TYR E . n 
E 3 304 LEU 304 304 304 LEU LEU E . n 
E 3 305 LEU 305 305 305 LEU LEU E . n 
E 3 306 ARG 306 306 306 ARG ARG E . n 
E 3 307 VAL 307 307 307 VAL VAL E . n 
E 3 308 GLN 308 308 308 GLN GLN E . n 
E 3 309 ALA 309 309 309 ALA ALA E . n 
E 3 310 SER 310 310 310 SER SER E . n 
E 3 311 ASP 311 311 311 ASP ASP E . n 
E 3 312 GLY 312 312 312 GLY GLY E . n 
E 3 313 ASN 313 313 313 ASN ASN E . n 
E 3 314 ASN 314 314 314 ASN ASN E . n 
E 3 315 THR 315 315 315 THR THR E . n 
E 3 316 SER 316 316 316 SER SER E . n 
E 3 317 PHE 317 317 317 PHE PHE E . n 
E 3 318 TRP 318 318 318 TRP TRP E . n 
E 3 319 SER 319 319 319 SER SER E . n 
E 3 320 GLU 320 320 320 GLU GLU E . n 
E 3 321 GLU 321 321 321 GLU GLU E . n 
E 3 322 ILE 322 322 322 ILE ILE E . n 
E 3 323 LYS 323 323 323 LYS LYS E . n 
E 3 324 PHE 324 324 324 PHE PHE E . n 
E 3 325 ASP 325 325 325 ASP ASP E . n 
E 3 326 THR 326 326 326 THR THR E . n 
E 3 327 GLU 327 327 327 GLU GLU E . n 
E 3 328 ILE 328 328 328 ILE ILE E . n 
E 3 329 GLN 329 329 329 GLN GLN E . n 
E 3 330 ALA 330 330 ?   ?   ?   E . n 
E 3 331 PHE 331 331 ?   ?   ?   E . n 
E 3 332 LEU 332 332 ?   ?   ?   E . n 
E 3 333 LEU 333 333 ?   ?   ?   E . n 
E 3 334 GLU 334 334 ?   ?   ?   E . n 
E 3 335 VAL 335 335 ?   ?   ?   E . n 
E 3 336 LEU 336 336 ?   ?   ?   E . n 
E 3 337 PHE 337 337 ?   ?   ?   E . n 
E 3 338 GLN 338 338 ?   ?   ?   E . n 
E 3 339 GLY 339 339 ?   ?   ?   E . n 
E 3 340 PRO 340 340 ?   ?   ?   E . n 
E 3 341 HIS 341 341 ?   ?   ?   E . n 
E 3 342 HIS 342 342 ?   ?   ?   E . n 
E 3 343 HIS 343 343 ?   ?   ?   E . n 
E 3 344 HIS 344 344 ?   ?   ?   E . n 
E 3 345 HIS 345 345 ?   ?   ?   E . n 
E 3 346 HIS 346 346 ?   ?   ?   E . n 
F 3 1   MET 1   1   ?   ?   ?   F . n 
F 3 2   MET 2   2   ?   ?   ?   F . n 
F 3 3   VAL 3   3   ?   ?   ?   F . n 
F 3 4   VAL 4   4   ?   ?   ?   F . n 
F 3 5   LEU 5   5   ?   ?   ?   F . n 
F 3 6   LEU 6   6   ?   ?   ?   F . n 
F 3 7   GLY 7   7   ?   ?   ?   F . n 
F 3 8   ALA 8   8   ?   ?   ?   F . n 
F 3 9   THR 9   9   ?   ?   ?   F . n 
F 3 10  THR 10  10  ?   ?   ?   F . n 
F 3 11  LEU 11  11  ?   ?   ?   F . n 
F 3 12  VAL 12  12  ?   ?   ?   F . n 
F 3 13  LEU 13  13  ?   ?   ?   F . n 
F 3 14  VAL 14  14  ?   ?   ?   F . n 
F 3 15  ALA 15  15  ?   ?   ?   F . n 
F 3 16  VAL 16  16  ?   ?   ?   F . n 
F 3 17  ALA 17  17  ?   ?   ?   F . n 
F 3 18  PRO 18  18  ?   ?   ?   F . n 
F 3 19  TRP 19  19  ?   ?   ?   F . n 
F 3 20  VAL 20  20  ?   ?   ?   F . n 
F 3 21  LEU 21  21  ?   ?   ?   F . n 
F 3 22  SER 22  22  ?   ?   ?   F . n 
F 3 23  ALA 23  23  ?   ?   ?   F . n 
F 3 24  ALA 24  24  ?   ?   ?   F . n 
F 3 25  ALA 25  25  ?   ?   ?   F . n 
F 3 26  GLY 26  26  ?   ?   ?   F . n 
F 3 27  GLY 27  27  ?   ?   ?   F . n 
F 3 28  LYS 28  28  ?   ?   ?   F . n 
F 3 29  ASN 29  29  ?   ?   ?   F . n 
F 3 30  LEU 30  30  ?   ?   ?   F . n 
F 3 31  LYS 31  31  ?   ?   ?   F . n 
F 3 32  SER 32  32  ?   ?   ?   F . n 
F 3 33  PRO 33  33  ?   ?   ?   F . n 
F 3 34  GLN 34  34  ?   ?   ?   F . n 
F 3 35  LYS 35  35  ?   ?   ?   F . n 
F 3 36  VAL 36  36  ?   ?   ?   F . n 
F 3 37  GLU 37  37  ?   ?   ?   F . n 
F 3 38  VAL 38  38  ?   ?   ?   F . n 
F 3 39  ASP 39  39  ?   ?   ?   F . n 
F 3 40  ILE 40  40  ?   ?   ?   F . n 
F 3 41  ILE 41  41  ?   ?   ?   F . n 
F 3 42  ASP 42  42  ?   ?   ?   F . n 
F 3 43  ASP 43  43  ?   ?   ?   F . n 
F 3 44  ASN 44  44  ?   ?   ?   F . n 
F 3 45  PHE 45  45  ?   ?   ?   F . n 
F 3 46  ILE 46  46  ?   ?   ?   F . n 
F 3 47  LEU 47  47  ?   ?   ?   F . n 
F 3 48  ARG 48  48  ?   ?   ?   F . n 
F 3 49  TRP 49  49  ?   ?   ?   F . n 
F 3 50  ASN 50  50  ?   ?   ?   F . n 
F 3 51  ARG 51  51  ?   ?   ?   F . n 
F 3 52  SER 52  52  ?   ?   ?   F . n 
F 3 53  ASP 53  53  ?   ?   ?   F . n 
F 3 54  GLU 54  54  ?   ?   ?   F . n 
F 3 55  SER 55  55  ?   ?   ?   F . n 
F 3 56  VAL 56  56  ?   ?   ?   F . n 
F 3 57  GLY 57  57  ?   ?   ?   F . n 
F 3 58  ASN 58  58  ?   ?   ?   F . n 
F 3 59  VAL 59  59  ?   ?   ?   F . n 
F 3 60  THR 60  60  ?   ?   ?   F . n 
F 3 61  PHE 61  61  ?   ?   ?   F . n 
F 3 62  SER 62  62  ?   ?   ?   F . n 
F 3 63  PHE 63  63  ?   ?   ?   F . n 
F 3 64  ASP 64  64  ?   ?   ?   F . n 
F 3 65  TYR 65  65  ?   ?   ?   F . n 
F 3 66  GLN 66  66  ?   ?   ?   F . n 
F 3 67  LYS 67  67  ?   ?   ?   F . n 
F 3 68  THR 68  68  ?   ?   ?   F . n 
F 3 69  GLY 69  69  ?   ?   ?   F . n 
F 3 70  MET 70  70  ?   ?   ?   F . n 
F 3 71  ASP 71  71  ?   ?   ?   F . n 
F 3 72  ASN 72  72  ?   ?   ?   F . n 
F 3 73  TRP 73  73  ?   ?   ?   F . n 
F 3 74  ILE 74  74  ?   ?   ?   F . n 
F 3 75  LYS 75  75  ?   ?   ?   F . n 
F 3 76  LEU 76  76  ?   ?   ?   F . n 
F 3 77  SER 77  77  ?   ?   ?   F . n 
F 3 78  GLY 78  78  ?   ?   ?   F . n 
F 3 79  CYS 79  79  ?   ?   ?   F . n 
F 3 80  GLN 80  80  ?   ?   ?   F . n 
F 3 81  ASN 81  81  ?   ?   ?   F . n 
F 3 82  ILE 82  82  ?   ?   ?   F . n 
F 3 83  THR 83  83  ?   ?   ?   F . n 
F 3 84  SER 84  84  ?   ?   ?   F . n 
F 3 85  THR 85  85  ?   ?   ?   F . n 
F 3 86  LYS 86  86  ?   ?   ?   F . n 
F 3 87  CYS 87  87  ?   ?   ?   F . n 
F 3 88  ASN 88  88  ?   ?   ?   F . n 
F 3 89  PHE 89  89  ?   ?   ?   F . n 
F 3 90  SER 90  90  ?   ?   ?   F . n 
F 3 91  SER 91  91  ?   ?   ?   F . n 
F 3 92  LEU 92  92  ?   ?   ?   F . n 
F 3 93  LYS 93  93  ?   ?   ?   F . n 
F 3 94  LEU 94  94  ?   ?   ?   F . n 
F 3 95  ASN 95  95  ?   ?   ?   F . n 
F 3 96  VAL 96  96  ?   ?   ?   F . n 
F 3 97  TYR 97  97  ?   ?   ?   F . n 
F 3 98  GLU 98  98  ?   ?   ?   F . n 
F 3 99  GLU 99  99  ?   ?   ?   F . n 
F 3 100 ILE 100 100 ?   ?   ?   F . n 
F 3 101 LYS 101 101 ?   ?   ?   F . n 
F 3 102 LEU 102 102 ?   ?   ?   F . n 
F 3 103 ARG 103 103 ?   ?   ?   F . n 
F 3 104 ILE 104 104 ?   ?   ?   F . n 
F 3 105 ARG 105 105 ?   ?   ?   F . n 
F 3 106 ALA 106 106 ?   ?   ?   F . n 
F 3 107 GLU 107 107 ?   ?   ?   F . n 
F 3 108 LYS 108 108 ?   ?   ?   F . n 
F 3 109 GLU 109 109 ?   ?   ?   F . n 
F 3 110 ASN 110 110 ?   ?   ?   F . n 
F 3 111 THR 111 111 ?   ?   ?   F . n 
F 3 112 SER 112 112 ?   ?   ?   F . n 
F 3 113 SER 113 113 ?   ?   ?   F . n 
F 3 114 TRP 114 114 ?   ?   ?   F . n 
F 3 115 TYR 115 115 ?   ?   ?   F . n 
F 3 116 GLU 116 116 ?   ?   ?   F . n 
F 3 117 VAL 117 117 ?   ?   ?   F . n 
F 3 118 ASP 118 118 ?   ?   ?   F . n 
F 3 119 SER 119 119 ?   ?   ?   F . n 
F 3 120 PHE 120 120 ?   ?   ?   F . n 
F 3 121 THR 121 121 ?   ?   ?   F . n 
F 3 122 PRO 122 122 ?   ?   ?   F . n 
F 3 123 PHE 123 123 ?   ?   ?   F . n 
F 3 124 ARG 124 124 ?   ?   ?   F . n 
F 3 125 LYS 125 125 ?   ?   ?   F . n 
F 3 126 ALA 126 126 ?   ?   ?   F . n 
F 3 127 GLN 127 127 ?   ?   ?   F . n 
F 3 128 ILE 128 128 ?   ?   ?   F . n 
F 3 129 GLY 129 129 ?   ?   ?   F . n 
F 3 130 PRO 130 130 ?   ?   ?   F . n 
F 3 131 PRO 131 131 ?   ?   ?   F . n 
F 3 132 GLU 132 132 ?   ?   ?   F . n 
F 3 133 VAL 133 133 ?   ?   ?   F . n 
F 3 134 HIS 134 134 ?   ?   ?   F . n 
F 3 135 LEU 135 135 ?   ?   ?   F . n 
F 3 136 GLU 136 136 ?   ?   ?   F . n 
F 3 137 ALA 137 137 ?   ?   ?   F . n 
F 3 138 GLU 138 138 ?   ?   ?   F . n 
F 3 139 ASP 139 139 ?   ?   ?   F . n 
F 3 140 LYS 140 140 ?   ?   ?   F . n 
F 3 141 ALA 141 141 ?   ?   ?   F . n 
F 3 142 ILE 142 142 ?   ?   ?   F . n 
F 3 143 VAL 143 143 ?   ?   ?   F . n 
F 3 144 ILE 144 144 ?   ?   ?   F . n 
F 3 145 HIS 145 145 ?   ?   ?   F . n 
F 3 146 ILE 146 146 ?   ?   ?   F . n 
F 3 147 SER 147 147 ?   ?   ?   F . n 
F 3 148 PRO 148 148 ?   ?   ?   F . n 
F 3 149 GLY 149 149 ?   ?   ?   F . n 
F 3 150 THR 150 150 ?   ?   ?   F . n 
F 3 151 LYS 151 151 ?   ?   ?   F . n 
F 3 152 ASP 152 152 ?   ?   ?   F . n 
F 3 153 SER 153 153 ?   ?   ?   F . n 
F 3 154 VAL 154 154 ?   ?   ?   F . n 
F 3 155 MET 155 155 ?   ?   ?   F . n 
F 3 156 TRP 156 156 ?   ?   ?   F . n 
F 3 157 ALA 157 157 ?   ?   ?   F . n 
F 3 158 LEU 158 158 ?   ?   ?   F . n 
F 3 159 ASP 159 159 ?   ?   ?   F . n 
F 3 160 GLY 160 160 ?   ?   ?   F . n 
F 3 161 LEU 161 161 ?   ?   ?   F . n 
F 3 162 SER 162 162 ?   ?   ?   F . n 
F 3 163 PHE 163 163 ?   ?   ?   F . n 
F 3 164 THR 164 164 ?   ?   ?   F . n 
F 3 165 TYR 165 165 ?   ?   ?   F . n 
F 3 166 SER 166 166 ?   ?   ?   F . n 
F 3 167 LEU 167 167 ?   ?   ?   F . n 
F 3 168 VAL 168 168 ?   ?   ?   F . n 
F 3 169 ILE 169 169 ?   ?   ?   F . n 
F 3 170 TRP 170 170 ?   ?   ?   F . n 
F 3 171 LYS 171 171 ?   ?   ?   F . n 
F 3 172 ASN 172 172 ?   ?   ?   F . n 
F 3 173 SER 173 173 ?   ?   ?   F . n 
F 3 174 SER 174 174 ?   ?   ?   F . n 
F 3 175 GLY 175 175 ?   ?   ?   F . n 
F 3 176 VAL 176 176 ?   ?   ?   F . n 
F 3 177 GLU 177 177 ?   ?   ?   F . n 
F 3 178 GLU 178 178 ?   ?   ?   F . n 
F 3 179 ARG 179 179 ?   ?   ?   F . n 
F 3 180 ILE 180 180 ?   ?   ?   F . n 
F 3 181 GLU 181 181 ?   ?   ?   F . n 
F 3 182 ASN 182 182 ?   ?   ?   F . n 
F 3 183 ILE 183 183 ?   ?   ?   F . n 
F 3 184 TYR 184 184 ?   ?   ?   F . n 
F 3 185 SER 185 185 ?   ?   ?   F . n 
F 3 186 ARG 186 186 ?   ?   ?   F . n 
F 3 187 HIS 187 187 ?   ?   ?   F . n 
F 3 188 LYS 188 188 ?   ?   ?   F . n 
F 3 189 ILE 189 189 ?   ?   ?   F . n 
F 3 190 TYR 190 190 ?   ?   ?   F . n 
F 3 191 LYS 191 191 ?   ?   ?   F . n 
F 3 192 LEU 192 192 ?   ?   ?   F . n 
F 3 193 SER 193 193 ?   ?   ?   F . n 
F 3 194 PRO 194 194 ?   ?   ?   F . n 
F 3 195 GLU 195 195 ?   ?   ?   F . n 
F 3 196 THR 196 196 ?   ?   ?   F . n 
F 3 197 THR 197 197 ?   ?   ?   F . n 
F 3 198 TYR 198 198 ?   ?   ?   F . n 
F 3 199 CYS 199 199 ?   ?   ?   F . n 
F 3 200 LEU 200 200 ?   ?   ?   F . n 
F 3 201 LYS 201 201 ?   ?   ?   F . n 
F 3 202 VAL 202 202 ?   ?   ?   F . n 
F 3 203 LYS 203 203 ?   ?   ?   F . n 
F 3 204 ALA 204 204 ?   ?   ?   F . n 
F 3 205 ALA 205 205 ?   ?   ?   F . n 
F 3 206 LEU 206 206 ?   ?   ?   F . n 
F 3 207 LEU 207 207 ?   ?   ?   F . n 
F 3 208 THR 208 208 ?   ?   ?   F . n 
F 3 209 SER 209 209 ?   ?   ?   F . n 
F 3 210 TRP 210 210 ?   ?   ?   F . n 
F 3 211 LYS 211 211 ?   ?   ?   F . n 
F 3 212 ILE 212 212 ?   ?   ?   F . n 
F 3 213 GLY 213 213 ?   ?   ?   F . n 
F 3 214 VAL 214 214 ?   ?   ?   F . n 
F 3 215 TYR 215 215 ?   ?   ?   F . n 
F 3 216 SER 216 216 ?   ?   ?   F . n 
F 3 217 PRO 217 217 ?   ?   ?   F . n 
F 3 218 VAL 218 218 ?   ?   ?   F . n 
F 3 219 HIS 219 219 ?   ?   ?   F . n 
F 3 220 CYS 220 220 ?   ?   ?   F . n 
F 3 221 ILE 221 221 ?   ?   ?   F . n 
F 3 222 LYS 222 222 ?   ?   ?   F . n 
F 3 223 THR 223 223 ?   ?   ?   F . n 
F 3 224 THR 224 224 ?   ?   ?   F . n 
F 3 225 VAL 225 225 ?   ?   ?   F . n 
F 3 226 GLU 226 226 ?   ?   ?   F . n 
F 3 227 ASN 227 227 ?   ?   ?   F . n 
F 3 228 GLU 228 228 228 GLU GLU F . n 
F 3 229 LEU 229 229 229 LEU LEU F . n 
F 3 230 PRO 230 230 230 PRO PRO F . n 
F 3 231 PRO 231 231 231 PRO PRO F . n 
F 3 232 PRO 232 232 232 PRO PRO F . n 
F 3 233 GLU 233 233 233 GLU GLU F . n 
F 3 234 ASN 234 234 234 ASN ASN F . n 
F 3 235 ILE 235 235 235 ILE ILE F . n 
F 3 236 GLU 236 236 236 GLU GLU F . n 
F 3 237 VAL 237 237 237 VAL VAL F . n 
F 3 238 SER 238 238 238 SER SER F . n 
F 3 239 VAL 239 239 239 VAL VAL F . n 
F 3 240 GLN 240 240 240 GLN GLN F . n 
F 3 241 ASN 241 241 241 ASN ASN F . n 
F 3 242 GLN 242 242 242 GLN GLN F . n 
F 3 243 ASN 243 243 243 ASN ASN F . n 
F 3 244 TYR 244 244 244 TYR TYR F . n 
F 3 245 VAL 245 245 245 VAL VAL F . n 
F 3 246 LEU 246 246 246 LEU LEU F . n 
F 3 247 LYS 247 247 247 LYS LYS F . n 
F 3 248 TRP 248 248 248 TRP TRP F . n 
F 3 249 ASP 249 249 249 ASP ASP F . n 
F 3 250 TYR 250 250 250 TYR TYR F . n 
F 3 251 THR 251 251 251 THR THR F . n 
F 3 252 TYR 252 252 252 TYR TYR F . n 
F 3 253 ALA 253 253 253 ALA ALA F . n 
F 3 254 ASN 254 254 254 ASN ASN F . n 
F 3 255 MET 255 255 255 MET MET F . n 
F 3 256 THR 256 256 256 THR THR F . n 
F 3 257 PHE 257 257 257 PHE PHE F . n 
F 3 258 GLN 258 258 258 GLN GLN F . n 
F 3 259 VAL 259 259 259 VAL VAL F . n 
F 3 260 GLN 260 260 260 GLN GLN F . n 
F 3 261 TRP 261 261 261 TRP TRP F . n 
F 3 262 LEU 262 262 262 LEU LEU F . n 
F 3 263 HIS 263 263 263 HIS HIS F . n 
F 3 264 ALA 264 264 264 ALA ALA F . n 
F 3 265 PHE 265 265 265 PHE PHE F . n 
F 3 266 LEU 266 266 266 LEU LEU F . n 
F 3 267 LYS 267 267 267 LYS LYS F . n 
F 3 268 ARG 268 268 268 ARG ARG F . n 
F 3 269 ASN 269 269 269 ASN ASN F . n 
F 3 270 PRO 270 270 270 PRO PRO F . n 
F 3 271 GLY 271 271 271 GLY GLY F . n 
F 3 272 ASN 272 272 272 ASN ASN F . n 
F 3 273 HIS 273 273 273 HIS HIS F . n 
F 3 274 LEU 274 274 274 LEU LEU F . n 
F 3 275 TYR 275 275 275 TYR TYR F . n 
F 3 276 LYS 276 276 276 LYS LYS F . n 
F 3 277 TRP 277 277 277 TRP TRP F . n 
F 3 278 LYS 278 278 278 LYS LYS F . n 
F 3 279 GLN 279 279 279 GLN GLN F . n 
F 3 280 ILE 280 280 280 ILE ILE F . n 
F 3 281 PRO 281 281 281 PRO PRO F . n 
F 3 282 ASP 282 282 282 ASP ASP F . n 
F 3 283 CYS 283 283 283 CYS CYS F . n 
F 3 284 GLU 284 284 284 GLU GLU F . n 
F 3 285 ASN 285 285 285 ASN ASN F . n 
F 3 286 VAL 286 286 286 VAL VAL F . n 
F 3 287 LYS 287 287 287 LYS LYS F . n 
F 3 288 THR 288 288 288 THR THR F . n 
F 3 289 THR 289 289 289 THR THR F . n 
F 3 290 GLN 290 290 290 GLN GLN F . n 
F 3 291 CYS 291 291 291 CYS CYS F . n 
F 3 292 VAL 292 292 292 VAL VAL F . n 
F 3 293 PHE 293 293 293 PHE PHE F . n 
F 3 294 PRO 294 294 294 PRO PRO F . n 
F 3 295 GLN 295 295 295 GLN GLN F . n 
F 3 296 ASN 296 296 296 ASN ASN F . n 
F 3 297 VAL 297 297 297 VAL VAL F . n 
F 3 298 PHE 298 298 298 PHE PHE F . n 
F 3 299 GLN 299 299 299 GLN GLN F . n 
F 3 300 LYS 300 300 300 LYS LYS F . n 
F 3 301 GLY 301 301 301 GLY GLY F . n 
F 3 302 ILE 302 302 302 ILE ILE F . n 
F 3 303 TYR 303 303 303 TYR TYR F . n 
F 3 304 LEU 304 304 304 LEU LEU F . n 
F 3 305 LEU 305 305 305 LEU LEU F . n 
F 3 306 ARG 306 306 306 ARG ARG F . n 
F 3 307 VAL 307 307 307 VAL VAL F . n 
F 3 308 GLN 308 308 308 GLN GLN F . n 
F 3 309 ALA 309 309 309 ALA ALA F . n 
F 3 310 SER 310 310 310 SER SER F . n 
F 3 311 ASP 311 311 311 ASP ASP F . n 
F 3 312 GLY 312 312 312 GLY GLY F . n 
F 3 313 ASN 313 313 313 ASN ASN F . n 
F 3 314 ASN 314 314 314 ASN ASN F . n 
F 3 315 THR 315 315 315 THR THR F . n 
F 3 316 SER 316 316 316 SER SER F . n 
F 3 317 PHE 317 317 317 PHE PHE F . n 
F 3 318 TRP 318 318 318 TRP TRP F . n 
F 3 319 SER 319 319 319 SER SER F . n 
F 3 320 GLU 320 320 320 GLU GLU F . n 
F 3 321 GLU 321 321 321 GLU GLU F . n 
F 3 322 ILE 322 322 322 ILE ILE F . n 
F 3 323 LYS 323 323 323 LYS LYS F . n 
F 3 324 PHE 324 324 324 PHE PHE F . n 
F 3 325 ASP 325 325 325 ASP ASP F . n 
F 3 326 THR 326 326 326 THR THR F . n 
F 3 327 GLU 327 327 327 GLU GLU F . n 
F 3 328 ILE 328 328 328 ILE ILE F . n 
F 3 329 GLN 329 329 329 GLN GLN F . n 
F 3 330 ALA 330 330 ?   ?   ?   F . n 
F 3 331 PHE 331 331 ?   ?   ?   F . n 
F 3 332 LEU 332 332 ?   ?   ?   F . n 
F 3 333 LEU 333 333 ?   ?   ?   F . n 
F 3 334 GLU 334 334 ?   ?   ?   F . n 
F 3 335 VAL 335 335 ?   ?   ?   F . n 
F 3 336 LEU 336 336 ?   ?   ?   F . n 
F 3 337 PHE 337 337 ?   ?   ?   F . n 
F 3 338 GLN 338 338 ?   ?   ?   F . n 
F 3 339 GLY 339 339 ?   ?   ?   F . n 
F 3 340 PRO 340 340 ?   ?   ?   F . n 
F 3 341 HIS 341 341 ?   ?   ?   F . n 
F 3 342 HIS 342 342 ?   ?   ?   F . n 
F 3 343 HIS 343 343 ?   ?   ?   F . n 
F 3 344 HIS 344 344 ?   ?   ?   F . n 
F 3 345 HIS 345 345 ?   ?   ?   F . n 
F 3 346 HIS 346 346 ?   ?   ?   F . 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 
G 4 HOH 1  301 78 HOH HOH A . 
G 4 HOH 2  302 44 HOH HOH A . 
G 4 HOH 3  303 3  HOH HOH A . 
G 4 HOH 4  304 35 HOH HOH A . 
G 4 HOH 5  305 8  HOH HOH A . 
G 4 HOH 6  306 30 HOH HOH A . 
G 4 HOH 7  307 1  HOH HOH A . 
G 4 HOH 8  308 5  HOH HOH A . 
G 4 HOH 9  309 65 HOH HOH A . 
G 4 HOH 10 310 20 HOH HOH A . 
G 4 HOH 11 311 22 HOH HOH A . 
G 4 HOH 12 312 56 HOH HOH A . 
G 4 HOH 13 313 70 HOH HOH A . 
G 4 HOH 14 314 77 HOH HOH A . 
G 4 HOH 15 315 67 HOH HOH A . 
G 4 HOH 16 316 75 HOH HOH A . 
G 4 HOH 17 317 48 HOH HOH A . 
G 4 HOH 18 318 41 HOH HOH A . 
G 4 HOH 19 319 47 HOH HOH A . 
H 4 HOH 1  301 66 HOH HOH B . 
H 4 HOH 2  302 11 HOH HOH B . 
H 4 HOH 3  303 64 HOH HOH B . 
H 4 HOH 4  304 9  HOH HOH B . 
H 4 HOH 5  305 68 HOH HOH B . 
H 4 HOH 6  306 58 HOH HOH B . 
H 4 HOH 7  307 39 HOH HOH B . 
H 4 HOH 8  308 29 HOH HOH B . 
H 4 HOH 9  309 25 HOH HOH B . 
H 4 HOH 10 310 40 HOH HOH B . 
H 4 HOH 11 311 14 HOH HOH B . 
H 4 HOH 12 312 46 HOH HOH B . 
H 4 HOH 13 313 62 HOH HOH B . 
H 4 HOH 14 314 19 HOH HOH B . 
H 4 HOH 15 315 53 HOH HOH B . 
H 4 HOH 16 316 74 HOH HOH B . 
I 4 HOH 1  301 24 HOH HOH C . 
I 4 HOH 2  302 37 HOH HOH C . 
I 4 HOH 3  303 71 HOH HOH C . 
I 4 HOH 4  304 4  HOH HOH C . 
I 4 HOH 5  305 45 HOH HOH C . 
I 4 HOH 6  306 33 HOH HOH C . 
I 4 HOH 7  307 42 HOH HOH C . 
I 4 HOH 8  308 18 HOH HOH C . 
I 4 HOH 9  309 15 HOH HOH C . 
I 4 HOH 10 310 51 HOH HOH C . 
I 4 HOH 11 311 31 HOH HOH C . 
I 4 HOH 12 312 27 HOH HOH C . 
I 4 HOH 13 313 10 HOH HOH C . 
I 4 HOH 14 314 28 HOH HOH C . 
I 4 HOH 15 315 54 HOH HOH C . 
I 4 HOH 16 316 34 HOH HOH C . 
J 4 HOH 1  301 16 HOH HOH D . 
J 4 HOH 2  302 23 HOH HOH D . 
J 4 HOH 3  303 12 HOH HOH D . 
J 4 HOH 4  304 7  HOH HOH D . 
J 4 HOH 5  305 43 HOH HOH D . 
J 4 HOH 6  306 76 HOH HOH D . 
J 4 HOH 7  307 32 HOH HOH D . 
J 4 HOH 8  308 26 HOH HOH D . 
J 4 HOH 9  309 17 HOH HOH D . 
J 4 HOH 10 310 38 HOH HOH D . 
J 4 HOH 11 311 36 HOH HOH D . 
J 4 HOH 12 312 69 HOH HOH D . 
K 4 HOH 1  401 72 HOH HOH E . 
K 4 HOH 2  402 52 HOH HOH E . 
K 4 HOH 3  403 60 HOH HOH E . 
L 4 HOH 1  401 13 HOH HOH F . 
L 4 HOH 2  402 21 HOH HOH F . 
# 
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   ? ? ? '(1.18.2_3874: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   111.51 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Y31 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     73.155 
_cell.length_a_esd                 ? 
_cell.length_b                     121.031 
_cell.length_b_esd                 ? 
_cell.length_c                     79.738 
_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                         8Y31 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Y31 
_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             1.93 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          36.41 
_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          'EVAPORATION, RECRYSTALLIZATION' 
_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    
'8%(w/v) PEG3350  50 mM Na-Citrate pH 5.5, 100 mM (NH4)2Citrate, 250 mM NaCl, 5 mM Hexadecyltrimethylammonium Bromide' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 300 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-12-23 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_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                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Y31 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.68 
_reflns.d_resolution_low                               68.06 
_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                                     35675 
_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                           98.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.8 
_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                                   0.993 
_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                                    2.68 
_reflns_shell.d_res_low                                     2.83 
_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                             3527 
_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                                  0.672 
_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                                 8Y31 
_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                            2.68 
_refine.ls_d_res_low                             46.89 
_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                     35675 
_refine.ls_number_reflns_R_free                  1747 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.70 
_refine.ls_percent_reflns_R_free                 4.90 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1965 
_refine.ls_R_factor_R_free                       0.2392 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1944 
_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             1.11 
_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                 26.09 
_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                            0.35 
_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.details                          ? 
_refine_hist.d_res_high                       2.68 
_refine_hist.d_res_low                        46.89 
_refine_hist.number_atoms_solvent             68 
_refine_hist.number_atoms_total               8330 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        8262 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  ? 8452  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.775  ? 11496 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 20.209 ? 3022  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.049  ? 1288  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 1470  ? 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' 2.68 2.76  . . 149 2784 98.00 . . . . 0.2816 . . . . . . . . . . . 0.3764 
'X-RAY DIFFRACTION' 2.76 2.85  . . 160 2799 99.00 . . . . 0.2446 . . . . . . . . . . . 0.2806 
'X-RAY DIFFRACTION' 2.85 2.95  . . 153 2822 99.00 . . . . 0.2384 . . . . . . . . . . . 0.3102 
'X-RAY DIFFRACTION' 2.95 3.07  . . 169 2812 99.00 . . . . 0.2290 . . . . . . . . . . . 0.2613 
'X-RAY DIFFRACTION' 3.07 3.21  . . 151 2813 99.00 . . . . 0.2142 . . . . . . . . . . . 0.2956 
'X-RAY DIFFRACTION' 3.21 3.38  . . 113 2856 99.00 . . . . 0.2125 . . . . . . . . . . . 0.2614 
'X-RAY DIFFRACTION' 3.38 3.59  . . 151 2779 98.00 . . . . 0.2167 . . . . . . . . . . . 0.2647 
'X-RAY DIFFRACTION' 3.59 3.87  . . 131 2827 99.00 . . . . 0.2013 . . . . . . . . . . . 0.2599 
'X-RAY DIFFRACTION' 3.87 4.26  . . 150 2824 98.00 . . . . 0.1824 . . . . . . . . . . . 0.2192 
'X-RAY DIFFRACTION' 4.26 4.88  . . 130 2860 99.00 . . . . 0.1560 . . . . . . . . . . . 0.2239 
'X-RAY DIFFRACTION' 4.88 6.14  . . 168 2843 99.00 . . . . 0.1755 . . . . . . . . . . . 0.2002 
'X-RAY DIFFRACTION' 6.14 46.89 . . 122 2909 99.00 . . . . 0.1732 . . . . . . . . . . . 0.1738 
# 
_struct.entry_id                     8Y31 
_struct.title                        'The crystal structure of the QX006N-Fab/IFNAR1-SD123 complex' 
_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        8Y31 
_struct_keywords.text            'IFNAR1, QX006N, the QX006N-Fab-IFNAR1-SD123 complex, 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 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
# 
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 8Y31        8Y31   ? 1 ? 1 
2 PDB 8Y31        8Y31   ? 2 ? 1 
3 UNP INAR1_HUMAN P17181 ? 3 
;MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQ
NITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDG
LSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQ
NQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSE
EIKFDTEIQAFLL
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8Y31 A 1 ? 216 ? 8Y31   1 ? 216 ? 1 216 
2 2 8Y31 B 1 ? 230 ? 8Y31   1 ? 230 ? 1 230 
3 1 8Y31 C 1 ? 216 ? 8Y31   1 ? 216 ? 1 216 
4 2 8Y31 D 1 ? 230 ? 8Y31   1 ? 230 ? 1 230 
5 3 8Y31 E 1 ? 333 ? P17181 1 ? 333 ? 1 333 
6 3 8Y31 F 1 ? 333 ? P17181 1 ? 333 ? 1 333 
# 
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 
5 8Y31 GLU E 334 ? UNP P17181 ? ? 'expression tag' 334 1  
5 8Y31 VAL E 335 ? UNP P17181 ? ? 'expression tag' 335 2  
5 8Y31 LEU E 336 ? UNP P17181 ? ? 'expression tag' 336 3  
5 8Y31 PHE E 337 ? UNP P17181 ? ? 'expression tag' 337 4  
5 8Y31 GLN E 338 ? UNP P17181 ? ? 'expression tag' 338 5  
5 8Y31 GLY E 339 ? UNP P17181 ? ? 'expression tag' 339 6  
5 8Y31 PRO E 340 ? UNP P17181 ? ? 'expression tag' 340 7  
5 8Y31 HIS E 341 ? UNP P17181 ? ? 'expression tag' 341 8  
5 8Y31 HIS E 342 ? UNP P17181 ? ? 'expression tag' 342 9  
5 8Y31 HIS E 343 ? UNP P17181 ? ? 'expression tag' 343 10 
5 8Y31 HIS E 344 ? UNP P17181 ? ? 'expression tag' 344 11 
5 8Y31 HIS E 345 ? UNP P17181 ? ? 'expression tag' 345 12 
5 8Y31 HIS E 346 ? UNP P17181 ? ? 'expression tag' 346 13 
6 8Y31 GLU F 334 ? UNP P17181 ? ? 'expression tag' 334 14 
6 8Y31 VAL F 335 ? UNP P17181 ? ? 'expression tag' 335 15 
6 8Y31 LEU F 336 ? UNP P17181 ? ? 'expression tag' 336 16 
6 8Y31 PHE F 337 ? UNP P17181 ? ? 'expression tag' 337 17 
6 8Y31 GLN F 338 ? UNP P17181 ? ? 'expression tag' 338 18 
6 8Y31 GLY F 339 ? UNP P17181 ? ? 'expression tag' 339 19 
6 8Y31 PRO F 340 ? UNP P17181 ? ? 'expression tag' 340 20 
6 8Y31 HIS F 341 ? UNP P17181 ? ? 'expression tag' 341 21 
6 8Y31 HIS F 342 ? UNP P17181 ? ? 'expression tag' 342 22 
6 8Y31 HIS F 343 ? UNP P17181 ? ? 'expression tag' 343 23 
6 8Y31 HIS F 344 ? UNP P17181 ? ? 'expression tag' 344 24 
6 8Y31 HIS F 345 ? UNP P17181 ? ? 'expression tag' 345 25 
6 8Y31 HIS F 346 ? UNP P17181 ? ? 'expression tag' 346 26 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? trimeric 3 
2 author_defined_assembly ? trimeric 3 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,G,H,K 
2 1 C,D,F,I,J,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 79  ? PHE A 83  ? GLN A 79  PHE A 83  5 ? 5 
HELX_P HELX_P2  AA2 SER A 125 ? GLY A 132 ? SER A 125 GLY A 132 1 ? 8 
HELX_P HELX_P3  AA3 LYS A 187 ? LYS A 192 ? LYS A 187 LYS A 192 1 ? 6 
HELX_P HELX_P4  AA4 SER B 28  ? TYR B 32  ? SER B 28  TYR B 32  5 ? 5 
HELX_P HELX_P5  AA5 ALA B 60  ? GLY B 65  ? ALA B 60  GLY B 65  1 ? 6 
HELX_P HELX_P6  AA6 ARG B 86  ? THR B 90  ? ARG B 86  THR B 90  5 ? 5 
HELX_P HELX_P7  AA7 SER B 162 ? ALA B 164 ? SER B 162 ALA B 164 5 ? 3 
HELX_P HELX_P8  AA8 SER B 193 ? LEU B 195 ? SER B 193 LEU B 195 5 ? 3 
HELX_P HELX_P9  AA9 LYS B 207 ? ASN B 210 ? LYS B 207 ASN B 210 5 ? 4 
HELX_P HELX_P10 AB1 GLN C 79  ? PHE C 83  ? GLN C 79  PHE C 83  5 ? 5 
HELX_P HELX_P11 AB2 SER C 125 ? GLY C 132 ? SER C 125 GLY C 132 1 ? 8 
HELX_P HELX_P12 AB3 LYS C 187 ? LYS C 192 ? LYS C 187 LYS C 192 1 ? 6 
HELX_P HELX_P13 AB4 SER D 28  ? TYR D 32  ? SER D 28  TYR D 32  5 ? 5 
HELX_P HELX_P14 AB5 SER D 61  ? LYS D 64  ? SER D 61  LYS D 64  5 ? 4 
HELX_P HELX_P15 AB6 ARG D 86  ? THR D 90  ? ARG D 86  THR D 90  5 ? 5 
HELX_P HELX_P16 AB7 SER D 162 ? ALA D 164 ? SER D 162 ALA D 164 5 ? 3 
HELX_P HELX_P17 AB8 SER D 193 ? LEU D 195 ? SER D 193 LEU D 195 5 ? 3 
HELX_P HELX_P18 AB9 LYS D 207 ? ASN D 210 ? LYS D 207 ASN D 210 5 ? 4 
HELX_P HELX_P19 AC1 PHE E 265 ? ARG E 268 ? PHE E 265 ARG E 268 5 ? 4 
HELX_P HELX_P20 AC2 ASN E 296 ? PHE E 298 ? ASN E 296 PHE E 298 5 ? 3 
HELX_P HELX_P21 AC3 PHE F 265 ? ARG F 268 ? PHE F 265 ARG F 268 5 ? 4 
HELX_P HELX_P22 AC4 ASN F 296 ? PHE F 298 ? ASN F 296 PHE F 298 5 ? 3 
# 
_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 23  SG ? ? ? 1_555 A CYS 88  SG ? ? A CYS 23  A CYS 88  1_555 ? ? ? ? ? ? ? 2.052 ? ? 
disulf2  disulf ? ? A CYS 138 SG ? ? ? 1_555 A CYS 198 SG ? ? A CYS 138 A CYS 198 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
disulf3  disulf ? ? B CYS 22  SG ? ? ? 1_555 B CYS 95  SG ? ? B CYS 22  B CYS 95  1_555 ? ? ? ? ? ? ? 2.043 ? ? 
disulf4  disulf ? ? B CYS 146 SG ? ? ? 1_555 B CYS 202 SG ? ? B CYS 146 B CYS 202 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf5  disulf ? ? C CYS 23  SG ? ? ? 1_555 C CYS 88  SG ? ? C CYS 23  C CYS 88  1_555 ? ? ? ? ? ? ? 2.048 ? ? 
disulf6  disulf ? ? C CYS 138 SG ? ? ? 1_555 C CYS 198 SG ? ? C CYS 138 C CYS 198 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
disulf7  disulf ? ? D CYS 22  SG ? ? ? 1_555 D CYS 95  SG ? ? D CYS 22  D CYS 95  1_555 ? ? ? ? ? ? ? 2.039 ? ? 
disulf8  disulf ? ? D CYS 146 SG ? ? ? 1_555 D CYS 202 SG ? ? D CYS 146 D CYS 202 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
disulf9  disulf ? ? E CYS 283 SG ? ? ? 1_555 E CYS 291 SG ? ? E CYS 283 E CYS 291 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf10 disulf ? ? F CYS 283 SG ? ? ? 1_555 F CYS 291 SG ? ? F CYS 283 F CYS 291 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
# 
_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 23  ? CYS A 88  ? CYS A 23  ? 1_555 CYS A 88  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2  CYS A 138 ? CYS A 198 ? CYS A 138 ? 1_555 CYS A 198 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3  CYS B 22  ? CYS B 95  ? CYS B 22  ? 1_555 CYS B 95  ? 1_555 SG SG . . . None 'Disulfide bridge' 
4  CYS B 146 ? CYS B 202 ? CYS B 146 ? 1_555 CYS B 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5  CYS C 23  ? CYS C 88  ? CYS C 23  ? 1_555 CYS C 88  ? 1_555 SG SG . . . None 'Disulfide bridge' 
6  CYS C 138 ? CYS C 198 ? CYS C 138 ? 1_555 CYS C 198 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7  CYS D 22  ? CYS D 95  ? CYS D 22  ? 1_555 CYS D 95  ? 1_555 SG SG . . . None 'Disulfide bridge' 
8  CYS D 146 ? CYS D 202 ? CYS D 146 ? 1_555 CYS D 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
9  CYS E 283 ? CYS E 291 ? CYS E 283 ? 1_555 CYS E 291 ? 1_555 SG SG . . . None 'Disulfide bridge' 
10 CYS F 283 ? CYS F 291 ? CYS F 283 ? 1_555 CYS F 291 ? 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 SER 7   A . ? SER 7   A PRO 8   A ? PRO 8   A 1 -4.26 
2 TYR 144 A . ? TYR 144 A PRO 145 A ? PRO 145 A 1 6.22  
3 PHE 152 B . ? PHE 152 B PRO 153 B ? PRO 153 B 1 -3.33 
4 GLU 154 B . ? GLU 154 B PRO 155 B ? PRO 155 B 1 0.57  
5 SER 7   C . ? SER 7   C PRO 8   C ? PRO 8   C 1 -4.69 
6 TYR 144 C . ? TYR 144 C PRO 145 C ? PRO 145 C 1 6.51  
7 PHE 152 D . ? PHE 152 D PRO 153 D ? PRO 153 D 1 -4.25 
8 GLU 154 D . ? GLU 154 D PRO 155 D ? PRO 155 D 1 2.31  
# 
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 ? 4 ? 
AA7 ? 6 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 3 ? 
AB3 ? 4 ? 
AB4 ? 6 ? 
AB5 ? 4 ? 
AB6 ? 4 ? 
AB7 ? 4 ? 
AB8 ? 4 ? 
AB9 ? 6 ? 
AC1 ? 4 ? 
AC2 ? 4 ? 
AC3 ? 4 ? 
AC4 ? 3 ? 
AC5 ? 3 ? 
AC6 ? 4 ? 
AC7 ? 3 ? 
AC8 ? 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 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-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 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB4 5 6 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AB9 5 6 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC6 3 4 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC7 2 3 ? anti-parallel 
AC8 1 2 ? anti-parallel 
AC8 2 3 ? anti-parallel 
AC8 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 MET A 4   ? SER A 7   ? MET A 4   SER A 7   
AA1 2 VAL A 19  ? ALA A 25  ? VAL A 19  ALA A 25  
AA1 3 LYS A 70  ? ILE A 75  ? LYS A 70  ILE A 75  
AA1 4 PHE A 62  ? SER A 67  ? PHE A 62  SER A 67  
AA2 1 SER A 10  ? SER A 14  ? SER A 10  SER A 14  
AA2 2 THR A 106 ? LYS A 111 ? THR A 106 LYS A 111 
AA2 3 ALA A 84  ? ILE A 91  ? ALA A 84  ILE A 91  
AA2 4 LEU A 33  ? GLN A 38  ? LEU A 33  GLN A 38  
AA2 5 LYS A 45  ? TYR A 49  ? LYS A 45  TYR A 49  
AA2 6 SER A 53  ? LEU A 54  ? SER A 53  LEU A 54  
AA3 1 SER A 10  ? SER A 14  ? SER A 10  SER A 14  
AA3 2 THR A 106 ? LYS A 111 ? THR A 106 LYS A 111 
AA3 3 ALA A 84  ? ILE A 91  ? ALA A 84  ILE A 91  
AA3 4 ILE A 100 ? PHE A 102 ? ILE A 100 PHE A 102 
AA4 1 SER A 118 ? PHE A 122 ? SER A 118 PHE A 122 
AA4 2 THR A 133 ? PHE A 143 ? THR A 133 PHE A 143 
AA4 3 TYR A 177 ? SER A 186 ? TYR A 177 SER A 186 
AA4 4 SER A 163 ? VAL A 167 ? SER A 163 VAL A 167 
AA5 1 ALA A 157 ? LEU A 158 ? ALA A 157 LEU A 158 
AA5 2 LYS A 149 ? VAL A 154 ? LYS A 149 VAL A 154 
AA5 3 VAL A 195 ? GLN A 202 ? VAL A 195 GLN A 202 
AA5 4 THR A 205 ? ASN A 212 ? THR A 205 ASN A 212 
AA6 1 GLN B 3   ? SER B 7   ? GLN B 3   SER B 7   
AA6 2 LEU B 18  ? SER B 25  ? LEU B 18  SER B 25  
AA6 3 THR B 77  ? MET B 82  ? THR B 77  MET B 82  
AA6 4 PHE B 67  ? ASP B 72  ? PHE B 67  ASP B 72  
AA7 1 LEU B 11  ? VAL B 12  ? LEU B 11  VAL B 12  
AA7 2 THR B 113 ? VAL B 117 ? THR B 113 VAL B 117 
AA7 3 ALA B 91  ? GLU B 98  ? ALA B 91  GLU B 98  
AA7 4 TYR B 33  ? GLN B 39  ? TYR B 33  GLN B 39  
AA7 5 LEU B 45  ? ILE B 51  ? LEU B 45  ILE B 51  
AA7 6 THR B 57  ? TYR B 59  ? THR B 57  TYR B 59  
AA8 1 LEU B 11  ? VAL B 12  ? LEU B 11  VAL B 12  
AA8 2 THR B 113 ? VAL B 117 ? THR B 113 VAL B 117 
AA8 3 ALA B 91  ? GLU B 98  ? ALA B 91  GLU B 98  
AA8 4 ILE B 106 ? TRP B 109 ? ILE B 106 TRP B 109 
AA9 1 SER B 126 ? LEU B 130 ? SER B 126 LEU B 130 
AA9 2 THR B 141 ? TYR B 151 ? THR B 141 TYR B 151 
AA9 3 TYR B 182 ? PRO B 191 ? TYR B 182 PRO B 191 
AA9 4 VAL B 169 ? THR B 171 ? VAL B 169 THR B 171 
AB1 1 SER B 126 ? LEU B 130 ? SER B 126 LEU B 130 
AB1 2 THR B 141 ? TYR B 151 ? THR B 141 TYR B 151 
AB1 3 TYR B 182 ? PRO B 191 ? TYR B 182 PRO B 191 
AB1 4 VAL B 175 ? LEU B 176 ? VAL B 175 LEU B 176 
AB2 1 THR B 157 ? TRP B 160 ? THR B 157 TRP B 160 
AB2 2 TYR B 200 ? HIS B 206 ? TYR B 200 HIS B 206 
AB2 3 THR B 211 ? VAL B 217 ? THR B 211 VAL B 217 
AB3 1 MET C 4   ? SER C 7   ? MET C 4   SER C 7   
AB3 2 VAL C 19  ? ALA C 25  ? VAL C 19  ALA C 25  
AB3 3 LYS C 70  ? ILE C 75  ? LYS C 70  ILE C 75  
AB3 4 PHE C 62  ? SER C 67  ? PHE C 62  SER C 67  
AB4 1 SER C 10  ? SER C 14  ? SER C 10  SER C 14  
AB4 2 THR C 106 ? LYS C 111 ? THR C 106 LYS C 111 
AB4 3 ALA C 84  ? ILE C 91  ? ALA C 84  ILE C 91  
AB4 4 LEU C 33  ? GLN C 38  ? LEU C 33  GLN C 38  
AB4 5 LYS C 45  ? TYR C 49  ? LYS C 45  TYR C 49  
AB4 6 SER C 53  ? LEU C 54  ? SER C 53  LEU C 54  
AB5 1 SER C 10  ? SER C 14  ? SER C 10  SER C 14  
AB5 2 THR C 106 ? LYS C 111 ? THR C 106 LYS C 111 
AB5 3 ALA C 84  ? ILE C 91  ? ALA C 84  ILE C 91  
AB5 4 ILE C 100 ? PHE C 102 ? ILE C 100 PHE C 102 
AB6 1 SER C 118 ? PHE C 122 ? SER C 118 PHE C 122 
AB6 2 THR C 133 ? PHE C 143 ? THR C 133 PHE C 143 
AB6 3 TYR C 177 ? SER C 186 ? TYR C 177 SER C 186 
AB6 4 SER C 163 ? VAL C 167 ? SER C 163 VAL C 167 
AB7 1 ALA C 157 ? LEU C 158 ? ALA C 157 LEU C 158 
AB7 2 LYS C 149 ? VAL C 154 ? LYS C 149 VAL C 154 
AB7 3 VAL C 195 ? GLN C 202 ? VAL C 195 GLN C 202 
AB7 4 THR C 205 ? ASN C 212 ? THR C 205 ASN C 212 
AB8 1 GLN D 3   ? SER D 7   ? GLN D 3   SER D 7   
AB8 2 LEU D 18  ? SER D 25  ? LEU D 18  SER D 25  
AB8 3 THR D 77  ? MET D 82  ? THR D 77  MET D 82  
AB8 4 PHE D 67  ? ASP D 72  ? PHE D 67  ASP D 72  
AB9 1 LEU D 11  ? VAL D 12  ? LEU D 11  VAL D 12  
AB9 2 THR D 113 ? VAL D 117 ? THR D 113 VAL D 117 
AB9 3 ALA D 91  ? GLU D 98  ? ALA D 91  GLU D 98  
AB9 4 TYR D 33  ? GLN D 39  ? TYR D 33  GLN D 39  
AB9 5 LEU D 45  ? ILE D 51  ? LEU D 45  ILE D 51  
AB9 6 THR D 57  ? TYR D 59  ? THR D 57  TYR D 59  
AC1 1 LEU D 11  ? VAL D 12  ? LEU D 11  VAL D 12  
AC1 2 THR D 113 ? VAL D 117 ? THR D 113 VAL D 117 
AC1 3 ALA D 91  ? GLU D 98  ? ALA D 91  GLU D 98  
AC1 4 ILE D 106 ? TRP D 109 ? ILE D 106 TRP D 109 
AC2 1 SER D 126 ? LEU D 130 ? SER D 126 LEU D 130 
AC2 2 THR D 141 ? TYR D 151 ? THR D 141 TYR D 151 
AC2 3 TYR D 182 ? PRO D 191 ? TYR D 182 PRO D 191 
AC2 4 VAL D 169 ? THR D 171 ? VAL D 169 THR D 171 
AC3 1 THR D 137 ? SER D 138 ? THR D 137 SER D 138 
AC3 2 THR D 141 ? TYR D 151 ? THR D 141 TYR D 151 
AC3 3 TYR D 182 ? PRO D 191 ? TYR D 182 PRO D 191 
AC3 4 VAL D 175 ? LEU D 176 ? VAL D 175 LEU D 176 
AC4 1 THR D 157 ? TRP D 160 ? THR D 157 TRP D 160 
AC4 2 TYR D 200 ? HIS D 206 ? TYR D 200 HIS D 206 
AC4 3 THR D 211 ? VAL D 217 ? THR D 211 VAL D 217 
AC5 1 GLU E 233 ? GLN E 240 ? GLU E 233 GLN E 240 
AC5 2 ASN E 243 ? ASP E 249 ? ASN E 243 ASP E 249 
AC5 3 GLN E 290 ? PRO E 294 ? GLN E 290 PRO E 294 
AC6 1 LYS E 278 ? GLN E 279 ? LYS E 278 GLN E 279 
AC6 2 THR E 256 ? HIS E 263 ? THR E 256 HIS E 263 
AC6 3 ILE E 302 ? SER E 310 ? ILE E 302 SER E 310 
AC6 4 ILE E 322 ? ASP E 325 ? ILE E 322 ASP E 325 
AC7 1 GLU F 233 ? GLN F 240 ? GLU F 233 GLN F 240 
AC7 2 ASN F 243 ? ASP F 249 ? ASN F 243 ASP F 249 
AC7 3 GLN F 290 ? PRO F 294 ? GLN F 290 PRO F 294 
AC8 1 LYS F 278 ? GLN F 279 ? LYS F 278 GLN F 279 
AC8 2 THR F 256 ? HIS F 263 ? THR F 256 HIS F 263 
AC8 3 ILE F 302 ? SER F 310 ? ILE F 302 SER F 310 
AC8 4 ILE F 322 ? ASP F 325 ? ILE F 322 ASP F 325 
# 
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 SER A 7   ? N SER A 7   O THR A 22  ? O THR A 22  
AA1 2 3 N ILE A 21  ? N ILE A 21  O LEU A 73  ? O LEU A 73  
AA1 3 4 O THR A 74  ? O THR A 74  N SER A 63  ? N SER A 63  
AA2 1 2 N ALA A 13  ? N ALA A 13  O LYS A 111 ? O LYS A 111 
AA2 2 3 O VAL A 108 ? O VAL A 108 N ALA A 84  ? N ALA A 84  
AA2 3 4 O TYR A 87  ? O TYR A 87  N TYR A 36  ? N TYR A 36  
AA2 4 5 N TRP A 35  ? N TRP A 35  O LEU A 47  ? O LEU A 47  
AA2 5 6 N TYR A 49  ? N TYR A 49  O SER A 53  ? O SER A 53  
AA3 1 2 N ALA A 13  ? N ALA A 13  O LYS A 111 ? O LYS A 111 
AA3 2 3 O VAL A 108 ? O VAL A 108 N ALA A 84  ? N ALA A 84  
AA3 3 4 N GLY A 90  ? N GLY A 90  O ALA A 101 ? O ALA A 101 
AA4 1 2 N PHE A 122 ? N PHE A 122 O VAL A 137 ? O VAL A 137 
AA4 2 3 N LEU A 140 ? N LEU A 140 O LEU A 179 ? O LEU A 179 
AA4 3 4 O THR A 182 ? O THR A 182 N GLN A 164 ? N GLN A 164 
AA5 1 2 O ALA A 157 ? O ALA A 157 N VAL A 154 ? N VAL A 154 
AA5 2 3 N LYS A 153 ? N LYS A 153 O ALA A 197 ? O ALA A 197 
AA5 3 4 N VAL A 200 ? N VAL A 200 O VAL A 207 ? O VAL A 207 
AA6 1 2 N VAL B 5   ? N VAL B 5   O ALA B 23  ? O ALA B 23  
AA6 2 3 N LEU B 18  ? N LEU B 18  O MET B 82  ? O MET B 82  
AA6 3 4 O TYR B 79  ? O TYR B 79  N SER B 70  ? N SER B 70  
AA7 1 2 N VAL B 12  ? N VAL B 12  O THR B 116 ? O THR B 116 
AA7 2 3 O THR B 113 ? O THR B 113 N TYR B 93  ? N TYR B 93  
AA7 3 4 O TYR B 94  ? O TYR B 94  N VAL B 37  ? N VAL B 37  
AA7 4 5 N ARG B 38  ? N ARG B 38  O GLU B 46  ? O GLU B 46  
AA7 5 6 N VAL B 50  ? N VAL B 50  O TYR B 58  ? O TYR B 58  
AA8 1 2 N VAL B 12  ? N VAL B 12  O THR B 116 ? O THR B 116 
AA8 2 3 O THR B 113 ? O THR B 113 N TYR B 93  ? N TYR B 93  
AA8 3 4 N ARG B 97  ? N ARG B 97  O LEU B 108 ? O LEU B 108 
AA9 1 2 N LEU B 130 ? N LEU B 130 O GLY B 145 ? O GLY B 145 
AA9 2 3 N TYR B 151 ? N TYR B 151 O TYR B 182 ? O TYR B 182 
AA9 3 4 O VAL B 187 ? O VAL B 187 N HIS B 170 ? N HIS B 170 
AB1 1 2 N LEU B 130 ? N LEU B 130 O GLY B 145 ? O GLY B 145 
AB1 2 3 N TYR B 151 ? N TYR B 151 O TYR B 182 ? O TYR B 182 
AB1 3 4 O SER B 183 ? O SER B 183 N VAL B 175 ? N VAL B 175 
AB2 1 2 N SER B 159 ? N SER B 159 O ASN B 203 ? O ASN B 203 
AB2 2 3 N HIS B 206 ? N HIS B 206 O THR B 211 ? O THR B 211 
AB3 1 2 N SER C 7   ? N SER C 7   O THR C 22  ? O THR C 22  
AB3 2 3 N CYS C 23  ? N CYS C 23  O PHE C 71  ? O PHE C 71  
AB3 3 4 O THR C 74  ? O THR C 74  N SER C 63  ? N SER C 63  
AB4 1 2 N ALA C 13  ? N ALA C 13  O LYS C 111 ? O LYS C 111 
AB4 2 3 O VAL C 108 ? O VAL C 108 N ALA C 84  ? N ALA C 84  
AB4 3 4 O TYR C 87  ? O TYR C 87  N TYR C 36  ? N TYR C 36  
AB4 4 5 N TRP C 35  ? N TRP C 35  O LEU C 47  ? O LEU C 47  
AB4 5 6 N TYR C 49  ? N TYR C 49  O SER C 53  ? O SER C 53  
AB5 1 2 N ALA C 13  ? N ALA C 13  O LYS C 111 ? O LYS C 111 
AB5 2 3 O VAL C 108 ? O VAL C 108 N ALA C 84  ? N ALA C 84  
AB5 3 4 N GLY C 90  ? N GLY C 90  O ALA C 101 ? O ALA C 101 
AB6 1 2 N PHE C 122 ? N PHE C 122 O VAL C 137 ? O VAL C 137 
AB6 2 3 N LEU C 140 ? N LEU C 140 O LEU C 179 ? O LEU C 179 
AB6 3 4 O SER C 180 ? O SER C 180 N SER C 166 ? N SER C 166 
AB7 1 2 O ALA C 157 ? O ALA C 157 N VAL C 154 ? N VAL C 154 
AB7 2 3 N GLN C 151 ? N GLN C 151 O GLU C 199 ? O GLU C 199 
AB7 3 4 N VAL C 200 ? N VAL C 200 O VAL C 207 ? O VAL C 207 
AB8 1 2 N GLN D 3   ? N GLN D 3   O SER D 25  ? O SER D 25  
AB8 2 3 N LEU D 18  ? N LEU D 18  O MET D 82  ? O MET D 82  
AB8 3 4 O TYR D 79  ? O TYR D 79  N SER D 70  ? N SER D 70  
AB9 1 2 N VAL D 12  ? N VAL D 12  O THR D 116 ? O THR D 116 
AB9 2 3 O THR D 113 ? O THR D 113 N TYR D 93  ? N TYR D 93  
AB9 3 4 O TYR D 94  ? O TYR D 94  N VAL D 37  ? N VAL D 37  
AB9 4 5 N ARG D 38  ? N ARG D 38  O GLU D 46  ? O GLU D 46  
AB9 5 6 N VAL D 50  ? N VAL D 50  O TYR D 58  ? O TYR D 58  
AC1 1 2 N VAL D 12  ? N VAL D 12  O THR D 116 ? O THR D 116 
AC1 2 3 O THR D 113 ? O THR D 113 N TYR D 93  ? N TYR D 93  
AC1 3 4 N ARG D 97  ? N ARG D 97  O LEU D 108 ? O LEU D 108 
AC2 1 2 N SER D 126 ? N SER D 126 O LYS D 149 ? O LYS D 149 
AC2 2 3 N TYR D 151 ? N TYR D 151 O TYR D 182 ? O TYR D 182 
AC2 3 4 O VAL D 187 ? O VAL D 187 N HIS D 170 ? N HIS D 170 
AC3 1 2 N SER D 138 ? N SER D 138 O THR D 141 ? O THR D 141 
AC3 2 3 N TYR D 151 ? N TYR D 151 O TYR D 182 ? O TYR D 182 
AC3 3 4 O SER D 183 ? O SER D 183 N VAL D 175 ? N VAL D 175 
AC4 1 2 N SER D 159 ? N SER D 159 O ASN D 203 ? O ASN D 203 
AC4 2 3 N HIS D 206 ? N HIS D 206 O THR D 211 ? O THR D 211 
AC5 1 2 N GLU E 233 ? N GLU E 233 O ASP E 249 ? O ASP E 249 
AC5 2 3 N TYR E 244 ? N TYR E 244 O PHE E 293 ? O PHE E 293 
AC6 1 2 O LYS E 278 ? O LYS E 278 N TRP E 261 ? N TRP E 261 
AC6 2 3 N GLN E 260 ? N GLN E 260 O ARG E 306 ? O ARG E 306 
AC6 3 4 N TYR E 303 ? N TYR E 303 O PHE E 324 ? O PHE E 324 
AC7 1 2 N GLU F 236 ? N GLU F 236 O LYS F 247 ? O LYS F 247 
AC7 2 3 N LEU F 246 ? N LEU F 246 O CYS F 291 ? O CYS F 291 
AC8 1 2 O LYS F 278 ? O LYS F 278 N TRP F 261 ? N TRP F 261 
AC8 2 3 N LEU F 262 ? N LEU F 262 O LEU F 304 ? O LEU F 304 
AC8 3 4 N TYR F 303 ? N TYR F 303 O PHE F 324 ? O PHE F 324 
# 
_pdbx_entry_details.entry_id                   8Y31 
_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 SER A 30  ? ? 57.43   -136.32 
2  1 ALA A 51  ? ? 75.45   -39.74  
3  1 VAL B 102 ? ? -126.64 -56.22  
4  1 SER B 134 ? ? -130.80 -93.36  
5  1 SER C 30  ? ? 57.47   -135.54 
6  1 ALA C 51  ? ? 77.45   -52.44  
7  1 VAL D 102 ? ? -128.05 -55.45  
8  1 SER D 134 ? ? -132.79 -83.97  
9  1 ASN E 241 ? ? 55.42   -127.34 
10 1 LEU E 274 ? ? -86.88  49.31   
11 1 ASN E 313 ? ? -123.53 -58.25  
12 1 ILE E 328 ? ? 80.17   13.34   
13 1 ASN F 241 ? ? 55.39   -128.07 
14 1 ASN F 272 ? ? 38.61   32.74   
15 1 LEU F 274 ? ? -85.33  48.46   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A CYS 216 ? A CYS 216 
2   1 Y 1 B CYS 222 ? B CYS 222 
3   1 Y 1 B GLY 223 ? B GLY 223 
4   1 Y 1 B GLY 224 ? B GLY 224 
5   1 Y 1 B HIS 225 ? B HIS 225 
6   1 Y 1 B HIS 226 ? B HIS 226 
7   1 Y 1 B HIS 227 ? B HIS 227 
8   1 Y 1 B HIS 228 ? B HIS 228 
9   1 Y 1 B HIS 229 ? B HIS 229 
10  1 Y 1 B HIS 230 ? B HIS 230 
11  1 Y 1 C CYS 216 ? C CYS 216 
12  1 Y 1 D CYS 222 ? D CYS 222 
13  1 Y 1 D GLY 223 ? D GLY 223 
14  1 Y 1 D GLY 224 ? D GLY 224 
15  1 Y 1 D HIS 225 ? D HIS 225 
16  1 Y 1 D HIS 226 ? D HIS 226 
17  1 Y 1 D HIS 227 ? D HIS 227 
18  1 Y 1 D HIS 228 ? D HIS 228 
19  1 Y 1 D HIS 229 ? D HIS 229 
20  1 Y 1 D HIS 230 ? D HIS 230 
21  1 Y 1 E MET 1   ? E MET 1   
22  1 Y 1 E MET 2   ? E MET 2   
23  1 Y 1 E VAL 3   ? E VAL 3   
24  1 Y 1 E VAL 4   ? E VAL 4   
25  1 Y 1 E LEU 5   ? E LEU 5   
26  1 Y 1 E LEU 6   ? E LEU 6   
27  1 Y 1 E GLY 7   ? E GLY 7   
28  1 Y 1 E ALA 8   ? E ALA 8   
29  1 Y 1 E THR 9   ? E THR 9   
30  1 Y 1 E THR 10  ? E THR 10  
31  1 Y 1 E LEU 11  ? E LEU 11  
32  1 Y 1 E VAL 12  ? E VAL 12  
33  1 Y 1 E LEU 13  ? E LEU 13  
34  1 Y 1 E VAL 14  ? E VAL 14  
35  1 Y 1 E ALA 15  ? E ALA 15  
36  1 Y 1 E VAL 16  ? E VAL 16  
37  1 Y 1 E ALA 17  ? E ALA 17  
38  1 Y 1 E PRO 18  ? E PRO 18  
39  1 Y 1 E TRP 19  ? E TRP 19  
40  1 Y 1 E VAL 20  ? E VAL 20  
41  1 Y 1 E LEU 21  ? E LEU 21  
42  1 Y 1 E SER 22  ? E SER 22  
43  1 Y 1 E ALA 23  ? E ALA 23  
44  1 Y 1 E ALA 24  ? E ALA 24  
45  1 Y 1 E ALA 25  ? E ALA 25  
46  1 Y 1 E GLY 26  ? E GLY 26  
47  1 Y 1 E GLY 27  ? E GLY 27  
48  1 Y 1 E LYS 28  ? E LYS 28  
49  1 Y 1 E ASN 29  ? E ASN 29  
50  1 Y 1 E LEU 30  ? E LEU 30  
51  1 Y 1 E LYS 31  ? E LYS 31  
52  1 Y 1 E SER 32  ? E SER 32  
53  1 Y 1 E PRO 33  ? E PRO 33  
54  1 Y 1 E GLN 34  ? E GLN 34  
55  1 Y 1 E LYS 35  ? E LYS 35  
56  1 Y 1 E VAL 36  ? E VAL 36  
57  1 Y 1 E GLU 37  ? E GLU 37  
58  1 Y 1 E VAL 38  ? E VAL 38  
59  1 Y 1 E ASP 39  ? E ASP 39  
60  1 Y 1 E ILE 40  ? E ILE 40  
61  1 Y 1 E ILE 41  ? E ILE 41  
62  1 Y 1 E ASP 42  ? E ASP 42  
63  1 Y 1 E ASP 43  ? E ASP 43  
64  1 Y 1 E ASN 44  ? E ASN 44  
65  1 Y 1 E PHE 45  ? E PHE 45  
66  1 Y 1 E ILE 46  ? E ILE 46  
67  1 Y 1 E LEU 47  ? E LEU 47  
68  1 Y 1 E ARG 48  ? E ARG 48  
69  1 Y 1 E TRP 49  ? E TRP 49  
70  1 Y 1 E ASN 50  ? E ASN 50  
71  1 Y 1 E ARG 51  ? E ARG 51  
72  1 Y 1 E SER 52  ? E SER 52  
73  1 Y 1 E ASP 53  ? E ASP 53  
74  1 Y 1 E GLU 54  ? E GLU 54  
75  1 Y 1 E SER 55  ? E SER 55  
76  1 Y 1 E VAL 56  ? E VAL 56  
77  1 Y 1 E GLY 57  ? E GLY 57  
78  1 Y 1 E ASN 58  ? E ASN 58  
79  1 Y 1 E VAL 59  ? E VAL 59  
80  1 Y 1 E THR 60  ? E THR 60  
81  1 Y 1 E PHE 61  ? E PHE 61  
82  1 Y 1 E SER 62  ? E SER 62  
83  1 Y 1 E PHE 63  ? E PHE 63  
84  1 Y 1 E ASP 64  ? E ASP 64  
85  1 Y 1 E TYR 65  ? E TYR 65  
86  1 Y 1 E GLN 66  ? E GLN 66  
87  1 Y 1 E LYS 67  ? E LYS 67  
88  1 Y 1 E THR 68  ? E THR 68  
89  1 Y 1 E GLY 69  ? E GLY 69  
90  1 Y 1 E MET 70  ? E MET 70  
91  1 Y 1 E ASP 71  ? E ASP 71  
92  1 Y 1 E ASN 72  ? E ASN 72  
93  1 Y 1 E TRP 73  ? E TRP 73  
94  1 Y 1 E ILE 74  ? E ILE 74  
95  1 Y 1 E LYS 75  ? E LYS 75  
96  1 Y 1 E LEU 76  ? E LEU 76  
97  1 Y 1 E SER 77  ? E SER 77  
98  1 Y 1 E GLY 78  ? E GLY 78  
99  1 Y 1 E CYS 79  ? E CYS 79  
100 1 Y 1 E GLN 80  ? E GLN 80  
101 1 Y 1 E ASN 81  ? E ASN 81  
102 1 Y 1 E ILE 82  ? E ILE 82  
103 1 Y 1 E THR 83  ? E THR 83  
104 1 Y 1 E SER 84  ? E SER 84  
105 1 Y 1 E THR 85  ? E THR 85  
106 1 Y 1 E LYS 86  ? E LYS 86  
107 1 Y 1 E CYS 87  ? E CYS 87  
108 1 Y 1 E ASN 88  ? E ASN 88  
109 1 Y 1 E PHE 89  ? E PHE 89  
110 1 Y 1 E SER 90  ? E SER 90  
111 1 Y 1 E SER 91  ? E SER 91  
112 1 Y 1 E LEU 92  ? E LEU 92  
113 1 Y 1 E LYS 93  ? E LYS 93  
114 1 Y 1 E LEU 94  ? E LEU 94  
115 1 Y 1 E ASN 95  ? E ASN 95  
116 1 Y 1 E VAL 96  ? E VAL 96  
117 1 Y 1 E TYR 97  ? E TYR 97  
118 1 Y 1 E GLU 98  ? E GLU 98  
119 1 Y 1 E GLU 99  ? E GLU 99  
120 1 Y 1 E ILE 100 ? E ILE 100 
121 1 Y 1 E LYS 101 ? E LYS 101 
122 1 Y 1 E LEU 102 ? E LEU 102 
123 1 Y 1 E ARG 103 ? E ARG 103 
124 1 Y 1 E ILE 104 ? E ILE 104 
125 1 Y 1 E ARG 105 ? E ARG 105 
126 1 Y 1 E ALA 106 ? E ALA 106 
127 1 Y 1 E GLU 107 ? E GLU 107 
128 1 Y 1 E LYS 108 ? E LYS 108 
129 1 Y 1 E GLU 109 ? E GLU 109 
130 1 Y 1 E ASN 110 ? E ASN 110 
131 1 Y 1 E THR 111 ? E THR 111 
132 1 Y 1 E SER 112 ? E SER 112 
133 1 Y 1 E SER 113 ? E SER 113 
134 1 Y 1 E TRP 114 ? E TRP 114 
135 1 Y 1 E TYR 115 ? E TYR 115 
136 1 Y 1 E GLU 116 ? E GLU 116 
137 1 Y 1 E VAL 117 ? E VAL 117 
138 1 Y 1 E ASP 118 ? E ASP 118 
139 1 Y 1 E SER 119 ? E SER 119 
140 1 Y 1 E PHE 120 ? E PHE 120 
141 1 Y 1 E THR 121 ? E THR 121 
142 1 Y 1 E PRO 122 ? E PRO 122 
143 1 Y 1 E PHE 123 ? E PHE 123 
144 1 Y 1 E ARG 124 ? E ARG 124 
145 1 Y 1 E LYS 125 ? E LYS 125 
146 1 Y 1 E ALA 126 ? E ALA 126 
147 1 Y 1 E GLN 127 ? E GLN 127 
148 1 Y 1 E ILE 128 ? E ILE 128 
149 1 Y 1 E GLY 129 ? E GLY 129 
150 1 Y 1 E PRO 130 ? E PRO 130 
151 1 Y 1 E PRO 131 ? E PRO 131 
152 1 Y 1 E GLU 132 ? E GLU 132 
153 1 Y 1 E VAL 133 ? E VAL 133 
154 1 Y 1 E HIS 134 ? E HIS 134 
155 1 Y 1 E LEU 135 ? E LEU 135 
156 1 Y 1 E GLU 136 ? E GLU 136 
157 1 Y 1 E ALA 137 ? E ALA 137 
158 1 Y 1 E GLU 138 ? E GLU 138 
159 1 Y 1 E ASP 139 ? E ASP 139 
160 1 Y 1 E LYS 140 ? E LYS 140 
161 1 Y 1 E ALA 141 ? E ALA 141 
162 1 Y 1 E ILE 142 ? E ILE 142 
163 1 Y 1 E VAL 143 ? E VAL 143 
164 1 Y 1 E ILE 144 ? E ILE 144 
165 1 Y 1 E HIS 145 ? E HIS 145 
166 1 Y 1 E ILE 146 ? E ILE 146 
167 1 Y 1 E SER 147 ? E SER 147 
168 1 Y 1 E PRO 148 ? E PRO 148 
169 1 Y 1 E GLY 149 ? E GLY 149 
170 1 Y 1 E THR 150 ? E THR 150 
171 1 Y 1 E LYS 151 ? E LYS 151 
172 1 Y 1 E ASP 152 ? E ASP 152 
173 1 Y 1 E SER 153 ? E SER 153 
174 1 Y 1 E VAL 154 ? E VAL 154 
175 1 Y 1 E MET 155 ? E MET 155 
176 1 Y 1 E TRP 156 ? E TRP 156 
177 1 Y 1 E ALA 157 ? E ALA 157 
178 1 Y 1 E LEU 158 ? E LEU 158 
179 1 Y 1 E ASP 159 ? E ASP 159 
180 1 Y 1 E GLY 160 ? E GLY 160 
181 1 Y 1 E LEU 161 ? E LEU 161 
182 1 Y 1 E SER 162 ? E SER 162 
183 1 Y 1 E PHE 163 ? E PHE 163 
184 1 Y 1 E THR 164 ? E THR 164 
185 1 Y 1 E TYR 165 ? E TYR 165 
186 1 Y 1 E SER 166 ? E SER 166 
187 1 Y 1 E LEU 167 ? E LEU 167 
188 1 Y 1 E VAL 168 ? E VAL 168 
189 1 Y 1 E ILE 169 ? E ILE 169 
190 1 Y 1 E TRP 170 ? E TRP 170 
191 1 Y 1 E LYS 171 ? E LYS 171 
192 1 Y 1 E ASN 172 ? E ASN 172 
193 1 Y 1 E SER 173 ? E SER 173 
194 1 Y 1 E SER 174 ? E SER 174 
195 1 Y 1 E GLY 175 ? E GLY 175 
196 1 Y 1 E VAL 176 ? E VAL 176 
197 1 Y 1 E GLU 177 ? E GLU 177 
198 1 Y 1 E GLU 178 ? E GLU 178 
199 1 Y 1 E ARG 179 ? E ARG 179 
200 1 Y 1 E ILE 180 ? E ILE 180 
201 1 Y 1 E GLU 181 ? E GLU 181 
202 1 Y 1 E ASN 182 ? E ASN 182 
203 1 Y 1 E ILE 183 ? E ILE 183 
204 1 Y 1 E TYR 184 ? E TYR 184 
205 1 Y 1 E SER 185 ? E SER 185 
206 1 Y 1 E ARG 186 ? E ARG 186 
207 1 Y 1 E HIS 187 ? E HIS 187 
208 1 Y 1 E LYS 188 ? E LYS 188 
209 1 Y 1 E ILE 189 ? E ILE 189 
210 1 Y 1 E TYR 190 ? E TYR 190 
211 1 Y 1 E LYS 191 ? E LYS 191 
212 1 Y 1 E LEU 192 ? E LEU 192 
213 1 Y 1 E SER 193 ? E SER 193 
214 1 Y 1 E PRO 194 ? E PRO 194 
215 1 Y 1 E GLU 195 ? E GLU 195 
216 1 Y 1 E THR 196 ? E THR 196 
217 1 Y 1 E THR 197 ? E THR 197 
218 1 Y 1 E TYR 198 ? E TYR 198 
219 1 Y 1 E CYS 199 ? E CYS 199 
220 1 Y 1 E LEU 200 ? E LEU 200 
221 1 Y 1 E LYS 201 ? E LYS 201 
222 1 Y 1 E VAL 202 ? E VAL 202 
223 1 Y 1 E LYS 203 ? E LYS 203 
224 1 Y 1 E ALA 204 ? E ALA 204 
225 1 Y 1 E ALA 205 ? E ALA 205 
226 1 Y 1 E LEU 206 ? E LEU 206 
227 1 Y 1 E LEU 207 ? E LEU 207 
228 1 Y 1 E THR 208 ? E THR 208 
229 1 Y 1 E SER 209 ? E SER 209 
230 1 Y 1 E TRP 210 ? E TRP 210 
231 1 Y 1 E LYS 211 ? E LYS 211 
232 1 Y 1 E ILE 212 ? E ILE 212 
233 1 Y 1 E GLY 213 ? E GLY 213 
234 1 Y 1 E VAL 214 ? E VAL 214 
235 1 Y 1 E TYR 215 ? E TYR 215 
236 1 Y 1 E SER 216 ? E SER 216 
237 1 Y 1 E PRO 217 ? E PRO 217 
238 1 Y 1 E VAL 218 ? E VAL 218 
239 1 Y 1 E HIS 219 ? E HIS 219 
240 1 Y 1 E CYS 220 ? E CYS 220 
241 1 Y 1 E ILE 221 ? E ILE 221 
242 1 Y 1 E LYS 222 ? E LYS 222 
243 1 Y 1 E THR 223 ? E THR 223 
244 1 Y 1 E THR 224 ? E THR 224 
245 1 Y 1 E VAL 225 ? E VAL 225 
246 1 Y 1 E GLU 226 ? E GLU 226 
247 1 Y 1 E ASN 227 ? E ASN 227 
248 1 Y 1 E ALA 330 ? E ALA 330 
249 1 Y 1 E PHE 331 ? E PHE 331 
250 1 Y 1 E LEU 332 ? E LEU 332 
251 1 Y 1 E LEU 333 ? E LEU 333 
252 1 Y 1 E GLU 334 ? E GLU 334 
253 1 Y 1 E VAL 335 ? E VAL 335 
254 1 Y 1 E LEU 336 ? E LEU 336 
255 1 Y 1 E PHE 337 ? E PHE 337 
256 1 Y 1 E GLN 338 ? E GLN 338 
257 1 Y 1 E GLY 339 ? E GLY 339 
258 1 Y 1 E PRO 340 ? E PRO 340 
259 1 Y 1 E HIS 341 ? E HIS 341 
260 1 Y 1 E HIS 342 ? E HIS 342 
261 1 Y 1 E HIS 343 ? E HIS 343 
262 1 Y 1 E HIS 344 ? E HIS 344 
263 1 Y 1 E HIS 345 ? E HIS 345 
264 1 Y 1 E HIS 346 ? E HIS 346 
265 1 Y 1 F MET 1   ? F MET 1   
266 1 Y 1 F MET 2   ? F MET 2   
267 1 Y 1 F VAL 3   ? F VAL 3   
268 1 Y 1 F VAL 4   ? F VAL 4   
269 1 Y 1 F LEU 5   ? F LEU 5   
270 1 Y 1 F LEU 6   ? F LEU 6   
271 1 Y 1 F GLY 7   ? F GLY 7   
272 1 Y 1 F ALA 8   ? F ALA 8   
273 1 Y 1 F THR 9   ? F THR 9   
274 1 Y 1 F THR 10  ? F THR 10  
275 1 Y 1 F LEU 11  ? F LEU 11  
276 1 Y 1 F VAL 12  ? F VAL 12  
277 1 Y 1 F LEU 13  ? F LEU 13  
278 1 Y 1 F VAL 14  ? F VAL 14  
279 1 Y 1 F ALA 15  ? F ALA 15  
280 1 Y 1 F VAL 16  ? F VAL 16  
281 1 Y 1 F ALA 17  ? F ALA 17  
282 1 Y 1 F PRO 18  ? F PRO 18  
283 1 Y 1 F TRP 19  ? F TRP 19  
284 1 Y 1 F VAL 20  ? F VAL 20  
285 1 Y 1 F LEU 21  ? F LEU 21  
286 1 Y 1 F SER 22  ? F SER 22  
287 1 Y 1 F ALA 23  ? F ALA 23  
288 1 Y 1 F ALA 24  ? F ALA 24  
289 1 Y 1 F ALA 25  ? F ALA 25  
290 1 Y 1 F GLY 26  ? F GLY 26  
291 1 Y 1 F GLY 27  ? F GLY 27  
292 1 Y 1 F LYS 28  ? F LYS 28  
293 1 Y 1 F ASN 29  ? F ASN 29  
294 1 Y 1 F LEU 30  ? F LEU 30  
295 1 Y 1 F LYS 31  ? F LYS 31  
296 1 Y 1 F SER 32  ? F SER 32  
297 1 Y 1 F PRO 33  ? F PRO 33  
298 1 Y 1 F GLN 34  ? F GLN 34  
299 1 Y 1 F LYS 35  ? F LYS 35  
300 1 Y 1 F VAL 36  ? F VAL 36  
301 1 Y 1 F GLU 37  ? F GLU 37  
302 1 Y 1 F VAL 38  ? F VAL 38  
303 1 Y 1 F ASP 39  ? F ASP 39  
304 1 Y 1 F ILE 40  ? F ILE 40  
305 1 Y 1 F ILE 41  ? F ILE 41  
306 1 Y 1 F ASP 42  ? F ASP 42  
307 1 Y 1 F ASP 43  ? F ASP 43  
308 1 Y 1 F ASN 44  ? F ASN 44  
309 1 Y 1 F PHE 45  ? F PHE 45  
310 1 Y 1 F ILE 46  ? F ILE 46  
311 1 Y 1 F LEU 47  ? F LEU 47  
312 1 Y 1 F ARG 48  ? F ARG 48  
313 1 Y 1 F TRP 49  ? F TRP 49  
314 1 Y 1 F ASN 50  ? F ASN 50  
315 1 Y 1 F ARG 51  ? F ARG 51  
316 1 Y 1 F SER 52  ? F SER 52  
317 1 Y 1 F ASP 53  ? F ASP 53  
318 1 Y 1 F GLU 54  ? F GLU 54  
319 1 Y 1 F SER 55  ? F SER 55  
320 1 Y 1 F VAL 56  ? F VAL 56  
321 1 Y 1 F GLY 57  ? F GLY 57  
322 1 Y 1 F ASN 58  ? F ASN 58  
323 1 Y 1 F VAL 59  ? F VAL 59  
324 1 Y 1 F THR 60  ? F THR 60  
325 1 Y 1 F PHE 61  ? F PHE 61  
326 1 Y 1 F SER 62  ? F SER 62  
327 1 Y 1 F PHE 63  ? F PHE 63  
328 1 Y 1 F ASP 64  ? F ASP 64  
329 1 Y 1 F TYR 65  ? F TYR 65  
330 1 Y 1 F GLN 66  ? F GLN 66  
331 1 Y 1 F LYS 67  ? F LYS 67  
332 1 Y 1 F THR 68  ? F THR 68  
333 1 Y 1 F GLY 69  ? F GLY 69  
334 1 Y 1 F MET 70  ? F MET 70  
335 1 Y 1 F ASP 71  ? F ASP 71  
336 1 Y 1 F ASN 72  ? F ASN 72  
337 1 Y 1 F TRP 73  ? F TRP 73  
338 1 Y 1 F ILE 74  ? F ILE 74  
339 1 Y 1 F LYS 75  ? F LYS 75  
340 1 Y 1 F LEU 76  ? F LEU 76  
341 1 Y 1 F SER 77  ? F SER 77  
342 1 Y 1 F GLY 78  ? F GLY 78  
343 1 Y 1 F CYS 79  ? F CYS 79  
344 1 Y 1 F GLN 80  ? F GLN 80  
345 1 Y 1 F ASN 81  ? F ASN 81  
346 1 Y 1 F ILE 82  ? F ILE 82  
347 1 Y 1 F THR 83  ? F THR 83  
348 1 Y 1 F SER 84  ? F SER 84  
349 1 Y 1 F THR 85  ? F THR 85  
350 1 Y 1 F LYS 86  ? F LYS 86  
351 1 Y 1 F CYS 87  ? F CYS 87  
352 1 Y 1 F ASN 88  ? F ASN 88  
353 1 Y 1 F PHE 89  ? F PHE 89  
354 1 Y 1 F SER 90  ? F SER 90  
355 1 Y 1 F SER 91  ? F SER 91  
356 1 Y 1 F LEU 92  ? F LEU 92  
357 1 Y 1 F LYS 93  ? F LYS 93  
358 1 Y 1 F LEU 94  ? F LEU 94  
359 1 Y 1 F ASN 95  ? F ASN 95  
360 1 Y 1 F VAL 96  ? F VAL 96  
361 1 Y 1 F TYR 97  ? F TYR 97  
362 1 Y 1 F GLU 98  ? F GLU 98  
363 1 Y 1 F GLU 99  ? F GLU 99  
364 1 Y 1 F ILE 100 ? F ILE 100 
365 1 Y 1 F LYS 101 ? F LYS 101 
366 1 Y 1 F LEU 102 ? F LEU 102 
367 1 Y 1 F ARG 103 ? F ARG 103 
368 1 Y 1 F ILE 104 ? F ILE 104 
369 1 Y 1 F ARG 105 ? F ARG 105 
370 1 Y 1 F ALA 106 ? F ALA 106 
371 1 Y 1 F GLU 107 ? F GLU 107 
372 1 Y 1 F LYS 108 ? F LYS 108 
373 1 Y 1 F GLU 109 ? F GLU 109 
374 1 Y 1 F ASN 110 ? F ASN 110 
375 1 Y 1 F THR 111 ? F THR 111 
376 1 Y 1 F SER 112 ? F SER 112 
377 1 Y 1 F SER 113 ? F SER 113 
378 1 Y 1 F TRP 114 ? F TRP 114 
379 1 Y 1 F TYR 115 ? F TYR 115 
380 1 Y 1 F GLU 116 ? F GLU 116 
381 1 Y 1 F VAL 117 ? F VAL 117 
382 1 Y 1 F ASP 118 ? F ASP 118 
383 1 Y 1 F SER 119 ? F SER 119 
384 1 Y 1 F PHE 120 ? F PHE 120 
385 1 Y 1 F THR 121 ? F THR 121 
386 1 Y 1 F PRO 122 ? F PRO 122 
387 1 Y 1 F PHE 123 ? F PHE 123 
388 1 Y 1 F ARG 124 ? F ARG 124 
389 1 Y 1 F LYS 125 ? F LYS 125 
390 1 Y 1 F ALA 126 ? F ALA 126 
391 1 Y 1 F GLN 127 ? F GLN 127 
392 1 Y 1 F ILE 128 ? F ILE 128 
393 1 Y 1 F GLY 129 ? F GLY 129 
394 1 Y 1 F PRO 130 ? F PRO 130 
395 1 Y 1 F PRO 131 ? F PRO 131 
396 1 Y 1 F GLU 132 ? F GLU 132 
397 1 Y 1 F VAL 133 ? F VAL 133 
398 1 Y 1 F HIS 134 ? F HIS 134 
399 1 Y 1 F LEU 135 ? F LEU 135 
400 1 Y 1 F GLU 136 ? F GLU 136 
401 1 Y 1 F ALA 137 ? F ALA 137 
402 1 Y 1 F GLU 138 ? F GLU 138 
403 1 Y 1 F ASP 139 ? F ASP 139 
404 1 Y 1 F LYS 140 ? F LYS 140 
405 1 Y 1 F ALA 141 ? F ALA 141 
406 1 Y 1 F ILE 142 ? F ILE 142 
407 1 Y 1 F VAL 143 ? F VAL 143 
408 1 Y 1 F ILE 144 ? F ILE 144 
409 1 Y 1 F HIS 145 ? F HIS 145 
410 1 Y 1 F ILE 146 ? F ILE 146 
411 1 Y 1 F SER 147 ? F SER 147 
412 1 Y 1 F PRO 148 ? F PRO 148 
413 1 Y 1 F GLY 149 ? F GLY 149 
414 1 Y 1 F THR 150 ? F THR 150 
415 1 Y 1 F LYS 151 ? F LYS 151 
416 1 Y 1 F ASP 152 ? F ASP 152 
417 1 Y 1 F SER 153 ? F SER 153 
418 1 Y 1 F VAL 154 ? F VAL 154 
419 1 Y 1 F MET 155 ? F MET 155 
420 1 Y 1 F TRP 156 ? F TRP 156 
421 1 Y 1 F ALA 157 ? F ALA 157 
422 1 Y 1 F LEU 158 ? F LEU 158 
423 1 Y 1 F ASP 159 ? F ASP 159 
424 1 Y 1 F GLY 160 ? F GLY 160 
425 1 Y 1 F LEU 161 ? F LEU 161 
426 1 Y 1 F SER 162 ? F SER 162 
427 1 Y 1 F PHE 163 ? F PHE 163 
428 1 Y 1 F THR 164 ? F THR 164 
429 1 Y 1 F TYR 165 ? F TYR 165 
430 1 Y 1 F SER 166 ? F SER 166 
431 1 Y 1 F LEU 167 ? F LEU 167 
432 1 Y 1 F VAL 168 ? F VAL 168 
433 1 Y 1 F ILE 169 ? F ILE 169 
434 1 Y 1 F TRP 170 ? F TRP 170 
435 1 Y 1 F LYS 171 ? F LYS 171 
436 1 Y 1 F ASN 172 ? F ASN 172 
437 1 Y 1 F SER 173 ? F SER 173 
438 1 Y 1 F SER 174 ? F SER 174 
439 1 Y 1 F GLY 175 ? F GLY 175 
440 1 Y 1 F VAL 176 ? F VAL 176 
441 1 Y 1 F GLU 177 ? F GLU 177 
442 1 Y 1 F GLU 178 ? F GLU 178 
443 1 Y 1 F ARG 179 ? F ARG 179 
444 1 Y 1 F ILE 180 ? F ILE 180 
445 1 Y 1 F GLU 181 ? F GLU 181 
446 1 Y 1 F ASN 182 ? F ASN 182 
447 1 Y 1 F ILE 183 ? F ILE 183 
448 1 Y 1 F TYR 184 ? F TYR 184 
449 1 Y 1 F SER 185 ? F SER 185 
450 1 Y 1 F ARG 186 ? F ARG 186 
451 1 Y 1 F HIS 187 ? F HIS 187 
452 1 Y 1 F LYS 188 ? F LYS 188 
453 1 Y 1 F ILE 189 ? F ILE 189 
454 1 Y 1 F TYR 190 ? F TYR 190 
455 1 Y 1 F LYS 191 ? F LYS 191 
456 1 Y 1 F LEU 192 ? F LEU 192 
457 1 Y 1 F SER 193 ? F SER 193 
458 1 Y 1 F PRO 194 ? F PRO 194 
459 1 Y 1 F GLU 195 ? F GLU 195 
460 1 Y 1 F THR 196 ? F THR 196 
461 1 Y 1 F THR 197 ? F THR 197 
462 1 Y 1 F TYR 198 ? F TYR 198 
463 1 Y 1 F CYS 199 ? F CYS 199 
464 1 Y 1 F LEU 200 ? F LEU 200 
465 1 Y 1 F LYS 201 ? F LYS 201 
466 1 Y 1 F VAL 202 ? F VAL 202 
467 1 Y 1 F LYS 203 ? F LYS 203 
468 1 Y 1 F ALA 204 ? F ALA 204 
469 1 Y 1 F ALA 205 ? F ALA 205 
470 1 Y 1 F LEU 206 ? F LEU 206 
471 1 Y 1 F LEU 207 ? F LEU 207 
472 1 Y 1 F THR 208 ? F THR 208 
473 1 Y 1 F SER 209 ? F SER 209 
474 1 Y 1 F TRP 210 ? F TRP 210 
475 1 Y 1 F LYS 211 ? F LYS 211 
476 1 Y 1 F ILE 212 ? F ILE 212 
477 1 Y 1 F GLY 213 ? F GLY 213 
478 1 Y 1 F VAL 214 ? F VAL 214 
479 1 Y 1 F TYR 215 ? F TYR 215 
480 1 Y 1 F SER 216 ? F SER 216 
481 1 Y 1 F PRO 217 ? F PRO 217 
482 1 Y 1 F VAL 218 ? F VAL 218 
483 1 Y 1 F HIS 219 ? F HIS 219 
484 1 Y 1 F CYS 220 ? F CYS 220 
485 1 Y 1 F ILE 221 ? F ILE 221 
486 1 Y 1 F LYS 222 ? F LYS 222 
487 1 Y 1 F THR 223 ? F THR 223 
488 1 Y 1 F THR 224 ? F THR 224 
489 1 Y 1 F VAL 225 ? F VAL 225 
490 1 Y 1 F GLU 226 ? F GLU 226 
491 1 Y 1 F ASN 227 ? F ASN 227 
492 1 Y 1 F ALA 330 ? F ALA 330 
493 1 Y 1 F PHE 331 ? F PHE 331 
494 1 Y 1 F LEU 332 ? F LEU 332 
495 1 Y 1 F LEU 333 ? F LEU 333 
496 1 Y 1 F GLU 334 ? F GLU 334 
497 1 Y 1 F VAL 335 ? F VAL 335 
498 1 Y 1 F LEU 336 ? F LEU 336 
499 1 Y 1 F PHE 337 ? F PHE 337 
500 1 Y 1 F GLN 338 ? F GLN 338 
501 1 Y 1 F GLY 339 ? F GLY 339 
502 1 Y 1 F PRO 340 ? F PRO 340 
503 1 Y 1 F HIS 341 ? F HIS 341 
504 1 Y 1 F HIS 342 ? F HIS 342 
505 1 Y 1 F HIS 343 ? F HIS 343 
506 1 Y 1 F HIS 344 ? F HIS 344 
507 1 Y 1 F HIS 345 ? F HIS 345 
508 1 Y 1 F HIS 346 ? F HIS 346 
# 
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 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 32071191 1 
'National Natural Science Foundation of China (NSFC)' China 31971160 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8Y2K 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8Y31 
_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]   0.013670 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005387 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008262 
_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]   0.013480 
_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   . ALA A 1 1   ? 2.084   24.359  49.067  1.00 62.99  ?  1   ALA A N   1 
ATOM   2    C CA  . ALA A 1 1   ? 1.720   23.960  47.710  1.00 63.61  ?  1   ALA A CA  1 
ATOM   3    C C   . ALA A 1 1   ? 0.260   24.284  47.435  1.00 64.79  ?  1   ALA A C   1 
ATOM   4    O O   . ALA A 1 1   ? -0.597  24.072  48.290  1.00 70.27  ?  1   ALA A O   1 
ATOM   5    C CB  . ALA A 1 1   ? 1.981   22.479  47.501  1.00 57.77  ?  1   ALA A CB  1 
ATOM   6    N N   . ILE A 1 2   ? -0.022  24.806  46.244  1.00 64.39  ?  2   ILE A N   1 
ATOM   7    C CA  . ILE A 1 2   ? -1.375  25.196  45.873  1.00 63.39  ?  2   ILE A CA  1 
ATOM   8    C C   . ILE A 1 2   ? -1.763  24.485  44.584  1.00 60.50  ?  2   ILE A C   1 
ATOM   9    O O   . ILE A 1 2   ? -0.926  24.228  43.712  1.00 56.53  ?  2   ILE A O   1 
ATOM   10   C CB  . ILE A 1 2   ? -1.519  26.725  45.705  1.00 58.91  ?  2   ILE A CB  1 
ATOM   11   C CG1 . ILE A 1 2   ? -0.481  27.248  44.715  1.00 51.86  ?  2   ILE A CG1 1 
ATOM   12   C CG2 . ILE A 1 2   ? -1.387  27.427  47.048  1.00 53.93  ?  2   ILE A CG2 1 
ATOM   13   C CD1 . ILE A 1 2   ? -0.856  28.572  44.086  1.00 48.18  ?  2   ILE A CD1 1 
ATOM   14   N N   . GLN A 1 3   ? -3.049  24.165  44.473  1.00 57.97  ?  3   GLN A N   1 
ATOM   15   C CA  . GLN A 1 3   ? -3.612  23.537  43.288  1.00 54.54  ?  3   GLN A CA  1 
ATOM   16   C C   . GLN A 1 3   ? -4.838  24.323  42.856  1.00 56.66  ?  3   GLN A C   1 
ATOM   17   O O   . GLN A 1 3   ? -5.590  24.821  43.698  1.00 59.65  ?  3   GLN A O   1 
ATOM   18   C CB  . GLN A 1 3   ? -4.003  22.068  43.531  1.00 57.70  ?  3   GLN A CB  1 
ATOM   19   C CG  . GLN A 1 3   ? -2.867  21.125  43.931  1.00 71.49  ?  3   GLN A CG  1 
ATOM   20   C CD  . GLN A 1 3   ? -2.733  20.931  45.437  1.00 78.16  ?  3   GLN A CD  1 
ATOM   21   O OE1 . GLN A 1 3   ? -2.851  21.880  46.216  1.00 75.77  ?  3   GLN A OE1 1 
ATOM   22   N NE2 . GLN A 1 3   ? -2.493  19.687  45.852  1.00 78.69  ?  3   GLN A NE2 1 
ATOM   23   N N   . MET A 1 4   ? -5.038  24.438  41.548  1.00 54.57  ?  4   MET A N   1 
ATOM   24   C CA  . MET A 1 4   ? -6.243  25.041  40.997  1.00 50.74  ?  4   MET A CA  1 
ATOM   25   C C   . MET A 1 4   ? -7.086  23.938  40.375  1.00 51.47  ?  4   MET A C   1 
ATOM   26   O O   . MET A 1 4   ? -6.611  23.201  39.504  1.00 49.72  ?  4   MET A O   1 
ATOM   27   C CB  . MET A 1 4   ? -5.919  26.113  39.957  1.00 52.98  ?  4   MET A CB  1 
ATOM   28   C CG  . MET A 1 4   ? -4.885  27.124  40.392  1.00 52.56  ?  4   MET A CG  1 
ATOM   29   S SD  . MET A 1 4   ? -5.323  28.048  41.878  1.00 49.91  ?  4   MET A SD  1 
ATOM   30   C CE  . MET A 1 4   ? -6.998  28.529  41.536  1.00 53.61  ?  4   MET A CE  1 
ATOM   31   N N   . THR A 1 5   ? -8.334  23.839  40.810  1.00 51.63  ?  5   THR A N   1 
ATOM   32   C CA  . THR A 1 5   ? -9.285  22.882  40.267  1.00 48.26  ?  5   THR A CA  1 
ATOM   33   C C   . THR A 1 5   ? -10.206 23.633  39.315  1.00 46.60  ?  5   THR A C   1 
ATOM   34   O O   . THR A 1 5   ? -11.030 24.439  39.751  1.00 52.77  ?  5   THR A O   1 
ATOM   35   C CB  . THR A 1 5   ? -10.074 22.216  41.392  1.00 52.79  ?  5   THR A CB  1 
ATOM   36   O OG1 . THR A 1 5   ? -9.165  21.615  42.321  1.00 58.34  ?  5   THR A OG1 1 
ATOM   37   C CG2 . THR A 1 5   ? -10.991 21.145  40.834  1.00 49.30  ?  5   THR A CG2 1 
ATOM   38   N N   . GLN A 1 6   ? -10.050 23.383  38.021  1.00 46.71  ?  6   GLN A N   1 
ATOM   39   C CA  . GLN A 1 6   ? -10.842 24.030  36.988  1.00 48.26  ?  6   GLN A CA  1 
ATOM   40   C C   . GLN A 1 6   ? -12.015 23.149  36.579  1.00 46.53  ?  6   GLN A C   1 
ATOM   41   O O   . GLN A 1 6   ? -11.908 21.923  36.549  1.00 49.68  ?  6   GLN A O   1 
ATOM   42   C CB  . GLN A 1 6   ? -9.982  24.335  35.764  1.00 46.32  ?  6   GLN A CB  1 
ATOM   43   C CG  . GLN A 1 6   ? -10.530 25.434  34.891  1.00 51.43  ?  6   GLN A CG  1 
ATOM   44   C CD  . GLN A 1 6   ? -9.522  25.897  33.867  1.00 49.62  ?  6   GLN A CD  1 
ATOM   45   O OE1 . GLN A 1 6   ? -8.320  25.926  34.137  1.00 46.38  ?  6   GLN A OE1 1 
ATOM   46   N NE2 . GLN A 1 6   ? -10.001 26.267  32.685  1.00 48.21  ?  6   GLN A NE2 1 
ATOM   47   N N   . SER A 1 7   ? -13.132 23.793  36.228  1.00 54.01  ?  7   SER A N   1 
ATOM   48   C CA  . SER A 1 7   ? -14.362 23.106  35.849  1.00 48.62  ?  7   SER A CA  1 
ATOM   49   C C   . SER A 1 7   ? -15.186 23.989  34.924  1.00 47.76  ?  7   SER A C   1 
ATOM   50   O O   . SER A 1 7   ? -15.222 25.210  35.119  1.00 47.73  ?  7   SER A O   1 
ATOM   51   C CB  . SER A 1 7   ? -15.189 22.739  37.086  1.00 52.15  ?  7   SER A CB  1 
ATOM   52   O OG  . SER A 1 7   ? -16.295 21.928  36.734  1.00 64.12  ?  7   SER A OG  1 
ATOM   53   N N   . PRO A 1 8   ? -15.839 23.423  33.902  1.00 47.44  ?  8   PRO A N   1 
ATOM   54   C CA  . PRO A 1 8   ? -15.764 22.012  33.531  1.00 45.32  ?  8   PRO A CA  1 
ATOM   55   C C   . PRO A 1 8   ? -14.517 21.727  32.722  1.00 46.93  ?  8   PRO A C   1 
ATOM   56   O O   . PRO A 1 8   ? -13.858 22.658  32.272  1.00 48.59  ?  8   PRO A O   1 
ATOM   57   C CB  . PRO A 1 8   ? -17.018 21.813  32.680  1.00 50.55  ?  8   PRO A CB  1 
ATOM   58   C CG  . PRO A 1 8   ? -17.219 23.143  32.023  1.00 47.43  ?  8   PRO A CG  1 
ATOM   59   C CD  . PRO A 1 8   ? -16.763 24.174  33.029  1.00 49.02  ?  8   PRO A CD  1 
ATOM   60   N N   . SER A 1 9   ? -14.199 20.444  32.550  1.00 54.99  ?  9   SER A N   1 
ATOM   61   C CA  . SER A 1 9   ? -13.056 20.066  31.726  1.00 47.53  ?  9   SER A CA  1 
ATOM   62   C C   . SER A 1 9   ? -13.265 20.465  30.269  1.00 47.96  ?  9   SER A C   1 
ATOM   63   O O   . SER A 1 9   ? -12.305 20.818  29.572  1.00 47.36  ?  9   SER A O   1 
ATOM   64   C CB  . SER A 1 9   ? -12.804 18.566  31.845  1.00 50.38  ?  9   SER A CB  1 
ATOM   65   O OG  . SER A 1 9   ? -11.709 18.188  31.038  1.00 67.20  ?  9   SER A OG  1 
ATOM   66   N N   . SER A 1 10  ? -14.504 20.383  29.785  1.00 47.41  ?  10  SER A N   1 
ATOM   67   C CA  . SER A 1 10  ? -14.860 20.840  28.448  1.00 48.57  ?  10  SER A CA  1 
ATOM   68   C C   . SER A 1 10  ? -16.310 21.299  28.455  1.00 49.63  ?  10  SER A C   1 
ATOM   69   O O   . SER A 1 10  ? -17.067 21.007  29.385  1.00 53.62  ?  10  SER A O   1 
ATOM   70   C CB  . SER A 1 10  ? -14.668 19.747  27.390  1.00 45.35  ?  10  SER A CB  1 
ATOM   71   O OG  . SER A 1 10  ? -15.292 18.542  27.796  1.00 58.84  ?  10  SER A OG  1 
ATOM   72   N N   . LEU A 1 11  ? -16.694 22.017  27.401  1.00 43.59  ?  11  LEU A N   1 
ATOM   73   C CA  . LEU A 1 11  ? -18.078 22.447  27.257  1.00 42.35  ?  11  LEU A CA  1 
ATOM   74   C C   . LEU A 1 11  ? -18.359 22.805  25.805  1.00 43.86  ?  11  LEU A C   1 
ATOM   75   O O   . LEU A 1 11  ? -17.465 23.234  25.072  1.00 46.52  ?  11  LEU A O   1 
ATOM   76   C CB  . LEU A 1 11  ? -18.394 23.639  28.172  1.00 41.56  ?  11  LEU A CB  1 
ATOM   77   C CG  . LEU A 1 11  ? -17.673 24.973  27.955  1.00 47.11  ?  11  LEU A CG  1 
ATOM   78   C CD1 . LEU A 1 11  ? -18.325 25.836  26.874  1.00 44.21  ?  11  LEU A CD1 1 
ATOM   79   C CD2 . LEU A 1 11  ? -17.609 25.718  29.272  1.00 42.65  ?  11  LEU A CD2 1 
ATOM   80   N N   . SER A 1 12  ? -19.618 22.629  25.409  1.00 42.27  ?  12  SER A N   1 
ATOM   81   C CA  . SER A 1 12  ? -20.118 23.075  24.118  1.00 46.07  ?  12  SER A CA  1 
ATOM   82   C C   . SER A 1 12  ? -21.272 24.046  24.345  1.00 52.44  ?  12  SER A C   1 
ATOM   83   O O   . SER A 1 12  ? -22.072 23.867  25.270  1.00 51.13  ?  12  SER A O   1 
ATOM   84   C CB  . SER A 1 12  ? -20.573 21.883  23.264  1.00 48.06  ?  12  SER A CB  1 
ATOM   85   O OG  . SER A 1 12  ? -21.025 22.307  21.990  1.00 54.68  ?  12  SER A OG  1 
ATOM   86   N N   . ALA A 1 13  ? -21.361 25.072  23.498  1.00 48.23  ?  13  ALA A N   1 
ATOM   87   C CA  . ALA A 1 13  ? -22.384 26.099  23.653  1.00 49.14  ?  13  ALA A CA  1 
ATOM   88   C C   . ALA A 1 13  ? -22.579 26.816  22.324  1.00 52.75  ?  13  ALA A C   1 
ATOM   89   O O   . ALA A 1 13  ? -21.669 26.869  21.494  1.00 53.16  ?  13  ALA A O   1 
ATOM   90   C CB  . ALA A 1 13  ? -22.011 27.098  24.754  1.00 46.72  ?  13  ALA A CB  1 
ATOM   91   N N   . SER A 1 14  ? -23.778 27.364  22.133  1.00 51.63  ?  14  SER A N   1 
ATOM   92   C CA  . SER A 1 14  ? -24.120 28.030  20.884  1.00 54.30  ?  14  SER A CA  1 
ATOM   93   C C   . SER A 1 14  ? -23.571 29.455  20.849  1.00 53.75  ?  14  SER A C   1 
ATOM   94   O O   . SER A 1 14  ? -23.241 30.053  21.878  1.00 51.84  ?  14  SER A O   1 
ATOM   95   C CB  . SER A 1 14  ? -25.636 28.052  20.683  1.00 46.56  ?  14  SER A CB  1 
ATOM   96   O OG  . SER A 1 14  ? -26.185 26.758  20.868  1.00 56.53  ?  14  SER A OG  1 
ATOM   97   N N   . VAL A 1 15  ? -23.471 29.997  19.633  1.00 47.43  ?  15  VAL A N   1 
ATOM   98   C CA  . VAL A 1 15  ? -23.101 31.396  19.472  1.00 47.46  ?  15  VAL A CA  1 
ATOM   99   C C   . VAL A 1 15  ? -24.149 32.266  20.150  1.00 55.64  ?  15  VAL A C   1 
ATOM   100  O O   . VAL A 1 15  ? -25.347 32.154  19.869  1.00 59.61  ?  15  VAL A O   1 
ATOM   101  C CB  . VAL A 1 15  ? -22.958 31.744  17.983  1.00 49.52  ?  15  VAL A CB  1 
ATOM   102  C CG1 . VAL A 1 15  ? -22.758 33.246  17.799  1.00 49.23  ?  15  VAL A CG1 1 
ATOM   103  C CG2 . VAL A 1 15  ? -21.808 30.971  17.367  1.00 45.76  ?  15  VAL A CG2 1 
ATOM   104  N N   . GLY A 1 16  ? -23.700 33.138  21.056  1.00 58.87  ?  16  GLY A N   1 
ATOM   105  C CA  . GLY A 1 16  ? -24.583 33.998  21.814  1.00 44.12  ?  16  GLY A CA  1 
ATOM   106  C C   . GLY A 1 16  ? -24.856 33.549  23.235  1.00 52.76  ?  16  GLY A C   1 
ATOM   107  O O   . GLY A 1 16  ? -25.432 34.322  24.008  1.00 60.15  ?  16  GLY A O   1 
ATOM   108  N N   . ASP A 1 17  ? -24.461 32.335  23.607  1.00 54.50  ?  17  ASP A N   1 
ATOM   109  C CA  . ASP A 1 17  ? -24.707 31.867  24.963  1.00 54.33  ?  17  ASP A CA  1 
ATOM   110  C C   . ASP A 1 17  ? -23.768 32.546  25.960  1.00 53.91  ?  17  ASP A C   1 
ATOM   111  O O   . ASP A 1 17  ? -22.745 33.136  25.600  1.00 56.96  ?  17  ASP A O   1 
ATOM   112  C CB  . ASP A 1 17  ? -24.536 30.348  25.057  1.00 53.48  ?  17  ASP A CB  1 
ATOM   113  C CG  . ASP A 1 17  ? -25.638 29.586  24.348  1.00 64.23  ?  17  ASP A CG  1 
ATOM   114  O OD1 . ASP A 1 17  ? -26.713 30.177  24.104  1.00 67.61  ?  17  ASP A OD1 1 
ATOM   115  O OD2 . ASP A 1 17  ? -25.440 28.384  24.056  1.00 68.44  ?  17  ASP A OD2 1 
ATOM   116  N N   . ARG A 1 18  ? -24.131 32.447  27.236  1.00 53.08  ?  18  ARG A N   1 
ATOM   117  C CA  . ARG A 1 18  ? -23.300 32.906  28.342  1.00 51.28  ?  18  ARG A CA  1 
ATOM   118  C C   . ARG A 1 18  ? -22.667 31.672  28.968  1.00 55.03  ?  18  ARG A C   1 
ATOM   119  O O   . ARG A 1 18  ? -23.372 30.802  29.491  1.00 53.74  ?  18  ARG A O   1 
ATOM   120  C CB  . ARG A 1 18  ? -24.119 33.683  29.372  1.00 62.77  ?  18  ARG A CB  1 
ATOM   121  C CG  . ARG A 1 18  ? -23.392 33.950  30.695  1.00 66.74  ?  18  ARG A CG  1 
ATOM   122  C CD  . ARG A 1 18  ? -24.254 34.746  31.681  1.00 61.64  ?  18  ARG A CD  1 
ATOM   123  N NE  . ARG A 1 18  ? -24.850 35.925  31.058  1.00 70.94  ?  18  ARG A NE  1 
ATOM   124  C CZ  . ARG A 1 18  ? -24.275 37.124  31.014  1.00 81.23  ?  18  ARG A CZ  1 
ATOM   125  N NH1 . ARG A 1 18  ? -23.081 37.313  31.564  1.00 78.33  ?  18  ARG A NH1 1 
ATOM   126  N NH2 . ARG A 1 18  ? -24.895 38.139  30.420  1.00 80.50  ?  18  ARG A NH2 1 
ATOM   127  N N   . VAL A 1 19  ? -21.345 31.577  28.883  1.00 54.12  ?  19  VAL A N   1 
ATOM   128  C CA  . VAL A 1 19  ? -20.625 30.418  29.388  1.00 49.21  ?  19  VAL A CA  1 
ATOM   129  C C   . VAL A 1 19  ? -19.793 30.847  30.584  1.00 48.44  ?  19  VAL A C   1 
ATOM   130  O O   . VAL A 1 19  ? -19.326 31.991  30.667  1.00 48.73  ?  19  VAL A O   1 
ATOM   131  C CB  . VAL A 1 19  ? -19.758 29.760  28.295  1.00 50.29  ?  19  VAL A CB  1 
ATOM   132  C CG1 . VAL A 1 19  ? -20.553 29.643  27.008  1.00 51.83  ?  19  VAL A CG1 1 
ATOM   133  C CG2 . VAL A 1 19  ? -18.484 30.543  28.063  1.00 56.97  ?  19  VAL A CG2 1 
ATOM   134  N N   . THR A 1 20  ? -19.614 29.918  31.522  1.00 47.40  ?  20  THR A N   1 
ATOM   135  C CA  . THR A 1 20  ? -18.940 30.199  32.783  1.00 48.06  ?  20  THR A CA  1 
ATOM   136  C C   . THR A 1 20  ? -17.945 29.092  33.092  1.00 48.33  ?  20  THR A C   1 
ATOM   137  O O   . THR A 1 20  ? -18.312 27.914  33.138  1.00 51.66  ?  20  THR A O   1 
ATOM   138  C CB  . THR A 1 20  ? -19.943 30.349  33.932  1.00 45.22  ?  20  THR A CB  1 
ATOM   139  O OG1 . THR A 1 20  ? -20.924 29.310  33.846  1.00 58.61  ?  20  THR A OG1 1 
ATOM   140  C CG2 . THR A 1 20  ? -20.635 31.703  33.867  1.00 48.43  ?  20  THR A CG2 1 
ATOM   141  N N   . ILE A 1 21  ? -16.692 29.482  33.302  1.00 50.25  ?  21  ILE A N   1 
ATOM   142  C CA  . ILE A 1 21  ? -15.626 28.610  33.768  1.00 45.47  ?  21  ILE A CA  1 
ATOM   143  C C   . ILE A 1 21  ? -15.417 28.923  35.239  1.00 47.43  ?  21  ILE A C   1 
ATOM   144  O O   . ILE A 1 21  ? -15.400 30.093  35.634  1.00 51.42  ?  21  ILE A O   1 
ATOM   145  C CB  . ILE A 1 21  ? -14.315 28.855  32.991  1.00 50.88  ?  21  ILE A CB  1 
ATOM   146  C CG1 . ILE A 1 21  ? -14.547 28.907  31.482  1.00 45.59  ?  21  ILE A CG1 1 
ATOM   147  C CG2 . ILE A 1 21  ? -13.286 27.789  33.328  1.00 51.64  ?  21  ILE A CG2 1 
ATOM   148  C CD1 . ILE A 1 21  ? -15.198 27.709  30.938  1.00 49.33  ?  21  ILE A CD1 1 
ATOM   149  N N   . THR A 1 22  ? -15.249 27.893  36.052  1.00 52.28  ?  22  THR A N   1 
ATOM   150  C CA  . THR A 1 22  ? -14.961 28.057  37.462  1.00 49.21  ?  22  THR A CA  1 
ATOM   151  C C   . THR A 1 22  ? -13.582 27.484  37.742  1.00 52.35  ?  22  THR A C   1 
ATOM   152  O O   . THR A 1 22  ? -13.122 26.561  37.062  1.00 52.50  ?  22  THR A O   1 
ATOM   153  C CB  . THR A 1 22  ? -16.007 27.362  38.334  1.00 51.76  ?  22  THR A CB  1 
ATOM   154  O OG1 . THR A 1 22  ? -17.318 27.718  37.879  1.00 58.12  ?  22  THR A OG1 1 
ATOM   155  C CG2 . THR A 1 22  ? -15.850 27.783  39.786  1.00 55.62  ?  22  THR A CG2 1 
ATOM   156  N N   . CYS A 1 23  ? -12.921 28.053  38.738  1.00 50.61  ?  23  CYS A N   1 
ATOM   157  C CA  . CYS A 1 23  ? -11.587 27.620  39.122  1.00 52.20  ?  23  CYS A CA  1 
ATOM   158  C C   . CYS A 1 23  ? -11.468 27.849  40.620  1.00 57.47  ?  23  CYS A C   1 
ATOM   159  O O   . CYS A 1 23  ? -11.627 28.977  41.092  1.00 60.19  ?  23  CYS A O   1 
ATOM   160  C CB  . CYS A 1 23  ? -10.523 28.394  38.319  1.00 56.82  ?  23  CYS A CB  1 
ATOM   161  S SG  . CYS A 1 23  ? -8.774  28.135  38.742  1.00 81.55  ?  23  CYS A SG  1 
ATOM   162  N N   . GLN A 1 24  ? -11.233 26.790  41.378  1.00 53.49  ?  24  GLN A N   1 
ATOM   163  C CA  . GLN A 1 24  ? -11.173 26.889  42.827  1.00 57.14  ?  24  GLN A CA  1 
ATOM   164  C C   . GLN A 1 24  ? -9.750  26.663  43.307  1.00 55.97  ?  24  GLN A C   1 
ATOM   165  O O   . GLN A 1 24  ? -9.069  25.742  42.847  1.00 58.29  ?  24  GLN A O   1 
ATOM   166  C CB  . GLN A 1 24  ? -12.115 25.896  43.498  1.00 61.08  ?  24  GLN A CB  1 
ATOM   167  C CG  . GLN A 1 24  ? -12.123 26.049  45.005  1.00 64.15  ?  24  GLN A CG  1 
ATOM   168  C CD  . GLN A 1 24  ? -13.435 25.648  45.615  1.00 77.66  ?  24  GLN A CD  1 
ATOM   169  O OE1 . GLN A 1 24  ? -14.393 25.340  44.906  1.00 86.04  ?  24  GLN A OE1 1 
ATOM   170  N NE2 . GLN A 1 24  ? -13.498 25.666  46.941  1.00 83.86  ?  24  GLN A NE2 1 
ATOM   171  N N   . ALA A 1 25  ? -9.302  27.515  44.217  1.00 55.25  ?  25  ALA A N   1 
ATOM   172  C CA  . ALA A 1 25  ? -7.973  27.394  44.788  1.00 58.17  ?  25  ALA A CA  1 
ATOM   173  C C   . ALA A 1 25  ? -8.011  26.517  46.032  1.00 57.68  ?  25  ALA A C   1 
ATOM   174  O O   . ALA A 1 25  ? -8.989  26.518  46.786  1.00 62.66  ?  25  ALA A O   1 
ATOM   175  C CB  . ALA A 1 25  ? -7.412  28.774  45.131  1.00 52.02  ?  25  ALA A CB  1 
ATOM   176  N N   . SER A 1 26  ? -6.927  25.762  46.240  1.00 53.54  ?  26  SER A N   1 
ATOM   177  C CA  . SER A 1 26  ? -6.818  24.934  47.436  1.00 54.45  ?  26  SER A CA  1 
ATOM   178  C C   . SER A 1 26  ? -6.791  25.784  48.700  1.00 51.78  ?  26  SER A C   1 
ATOM   179  O O   . SER A 1 26  ? -7.180  25.313  49.774  1.00 54.01  ?  26  SER A O   1 
ATOM   180  C CB  . SER A 1 26  ? -5.576  24.045  47.347  1.00 50.91  ?  26  SER A CB  1 
ATOM   181  O OG  . SER A 1 26  ? -4.394  24.817  47.262  1.00 59.31  ?  26  SER A OG  1 
ATOM   182  N N   . GLN A 1 27  ? -6.349  27.031  48.590  1.00 48.08  ?  27  GLN A N   1 
ATOM   183  C CA  . GLN A 1 27  ? -6.425  27.973  49.696  1.00 53.03  ?  27  GLN A CA  1 
ATOM   184  C C   . GLN A 1 27  ? -6.441  29.379  49.113  1.00 51.10  ?  27  GLN A C   1 
ATOM   185  O O   . GLN A 1 27  ? -6.236  29.576  47.915  1.00 53.51  ?  27  GLN A O   1 
ATOM   186  C CB  . GLN A 1 27  ? -5.262  27.800  50.668  1.00 44.47  ?  27  GLN A CB  1 
ATOM   187  C CG  . GLN A 1 27  ? -3.910  27.902  50.018  1.00 47.87  ?  27  GLN A CG  1 
ATOM   188  C CD  . GLN A 1 27  ? -2.810  27.573  50.985  1.00 49.17  ?  27  GLN A CD  1 
ATOM   189  O OE1 . GLN A 1 27  ? -2.487  28.365  51.866  1.00 51.42  ?  27  GLN A OE1 1 
ATOM   190  N NE2 . GLN A 1 27  ? -2.238  26.382  50.845  1.00 49.52  ?  27  GLN A NE2 1 
ATOM   191  N N   . SER A 1 28  ? -6.684  30.356  49.977  1.00 46.89  ?  28  SER A N   1 
ATOM   192  C CA  . SER A 1 28  ? -6.847  31.722  49.505  1.00 49.97  ?  28  SER A CA  1 
ATOM   193  C C   . SER A 1 28  ? -5.568  32.219  48.848  1.00 56.15  ?  28  SER A C   1 
ATOM   194  O O   . SER A 1 28  ? -4.458  31.975  49.332  1.00 54.42  ?  28  SER A O   1 
ATOM   195  C CB  . SER A 1 28  ? -7.243  32.649  50.645  1.00 51.40  ?  28  SER A CB  1 
ATOM   196  O OG  . SER A 1 28  ? -7.551  33.940  50.153  1.00 61.03  ?  28  SER A OG  1 
ATOM   197  N N   . ILE A 1 29  ? -5.739  32.905  47.722  1.00 53.56  ?  29  ILE A N   1 
ATOM   198  C CA  . ILE A 1 29  ? -4.640  33.482  46.962  1.00 52.36  ?  29  ILE A CA  1 
ATOM   199  C C   . ILE A 1 29  ? -4.943  34.950  46.701  1.00 49.99  ?  29  ILE A C   1 
ATOM   200  O O   . ILE A 1 29  ? -4.371  35.559  45.788  1.00 51.47  ?  29  ILE A O   1 
ATOM   201  C CB  . ILE A 1 29  ? -4.414  32.711  45.648  1.00 47.84  ?  29  ILE A CB  1 
ATOM   202  C CG1 . ILE A 1 29  ? -5.732  32.580  44.877  1.00 42.76  ?  29  ILE A CG1 1 
ATOM   203  C CG2 . ILE A 1 29  ? -3.815  31.350  45.937  1.00 44.50  ?  29  ILE A CG2 1 
ATOM   204  C CD1 . ILE A 1 29  ? -5.580  32.057  43.465  1.00 36.81  ?  29  ILE A CD1 1 
ATOM   205  N N   . SER A 1 30  ? -5.848  35.516  47.493  1.00 50.55  ?  30  SER A N   1 
ATOM   206  C CA  . SER A 1 30  ? -6.335  36.899  47.329  1.00 49.21  ?  30  SER A CA  1 
ATOM   207  C C   . SER A 1 30  ? -6.911  37.004  45.915  1.00 45.52  ?  30  SER A C   1 
ATOM   208  O O   . SER A 1 30  ? -7.610  36.083  45.469  1.00 47.58  ?  30  SER A O   1 
ATOM   209  C CB  . SER A 1 30  ? -5.232  37.882  47.641  1.00 54.91  ?  30  SER A CB  1 
ATOM   210  O OG  . SER A 1 30  ? -4.757  37.702  48.961  1.00 66.65  ?  30  SER A OG  1 
ATOM   211  N N   . ASN A 1 31  ? -6.624  38.078  45.184  1.00 45.49  ?  31  ASN A N   1 
ATOM   212  C CA  . ASN A 1 31  ? -7.124  38.247  43.828  1.00 46.48  ?  31  ASN A CA  1 
ATOM   213  C C   . ASN A 1 31  ? -6.141  37.763  42.774  1.00 48.06  ?  31  ASN A C   1 
ATOM   214  O O   . ASN A 1 31  ? -6.413  37.926  41.581  1.00 47.81  ?  31  ASN A O   1 
ATOM   215  C CB  . ASN A 1 31  ? -7.466  39.719  43.550  1.00 54.76  ?  31  ASN A CB  1 
ATOM   216  C CG  . ASN A 1 31  ? -8.426  40.301  44.565  1.00 53.45  ?  31  ASN A CG  1 
ATOM   217  O OD1 . ASN A 1 31  ? -9.389  39.649  44.975  1.00 51.28  ?  31  ASN A OD1 1 
ATOM   218  N ND2 . ASN A 1 31  ? -8.187  41.547  44.953  1.00 58.94  ?  31  ASN A ND2 1 
ATOM   219  N N   . GLN A 1 32  ? -5.013  37.174  43.181  1.00 49.20  ?  32  GLN A N   1 
ATOM   220  C CA  . GLN A 1 32  ? -3.928  36.832  42.261  1.00 41.29  ?  32  GLN A CA  1 
ATOM   221  C C   . GLN A 1 32  ? -4.270  35.582  41.446  1.00 41.44  ?  32  GLN A C   1 
ATOM   222  O O   . GLN A 1 32  ? -3.625  34.536  41.531  1.00 46.64  ?  32  GLN A O   1 
ATOM   223  C CB  . GLN A 1 32  ? -2.619  36.663  43.019  1.00 36.36  ?  32  GLN A CB  1 
ATOM   224  C CG  . GLN A 1 32  ? -2.079  37.954  43.591  1.00 37.35  ?  32  GLN A CG  1 
ATOM   225  C CD  . GLN A 1 32  ? -0.783  37.769  44.354  1.00 44.43  ?  32  GLN A CD  1 
ATOM   226  O OE1 . GLN A 1 32  ? -0.318  38.687  45.027  1.00 45.71  ?  32  GLN A OE1 1 
ATOM   227  N NE2 . GLN A 1 32  ? -0.187  36.579  44.249  1.00 40.35  ?  32  GLN A NE2 1 
ATOM   228  N N   . LEU A 1 33  ? -5.321  35.711  40.644  1.00 36.69  ?  33  LEU A N   1 
ATOM   229  C CA  . LEU A 1 33  ? -5.708  34.689  39.687  1.00 36.93  ?  33  LEU A CA  1 
ATOM   230  C C   . LEU A 1 33  ? -5.909  35.344  38.336  1.00 37.13  ?  33  LEU A C   1 
ATOM   231  O O   . LEU A 1 33  ? -6.587  36.369  38.231  1.00 40.81  ?  33  LEU A O   1 
ATOM   232  C CB  . LEU A 1 33  ? -6.979  33.947  40.107  1.00 40.25  ?  33  LEU A CB  1 
ATOM   233  C CG  . LEU A 1 33  ? -7.343  32.790  39.170  1.00 43.82  ?  33  LEU A CG  1 
ATOM   234  C CD1 . LEU A 1 33  ? -7.813  31.610  39.975  1.00 46.13  ?  33  LEU A CD1 1 
ATOM   235  C CD2 . LEU A 1 33  ? -8.421  33.204  38.169  1.00 42.45  ?  33  LEU A CD2 1 
ATOM   236  N N   . SER A 1 34  ? -5.313  34.758  37.311  1.00 38.24  ?  34  SER A N   1 
ATOM   237  C CA  . SER A 1 34  ? -5.411  35.283  35.963  1.00 38.24  ?  34  SER A CA  1 
ATOM   238  C C   . SER A 1 34  ? -5.980  34.212  35.036  1.00 40.46  ?  34  SER A C   1 
ATOM   239  O O   . SER A 1 34  ? -5.925  33.016  35.324  1.00 40.42  ?  34  SER A O   1 
ATOM   240  C CB  . SER A 1 34  ? -4.040  35.815  35.498  1.00 39.01  ?  34  SER A CB  1 
ATOM   241  O OG  . SER A 1 34  ? -3.000  34.874  35.700  1.00 40.07  ?  34  SER A OG  1 
ATOM   242  N N   . TRP A 1 35  ? -6.580  34.663  33.941  1.00 39.29  ?  35  TRP A N   1 
ATOM   243  C CA  . TRP A 1 35  ? -7.219  33.797  32.962  1.00 37.52  ?  35  TRP A CA  1 
ATOM   244  C C   . TRP A 1 35  ? -6.565  33.999  31.610  1.00 39.85  ?  35  TRP A C   1 
ATOM   245  O O   . TRP A 1 35  ? -6.340  35.143  31.188  1.00 39.42  ?  35  TRP A O   1 
ATOM   246  C CB  . TRP A 1 35  ? -8.726  34.065  32.826  1.00 40.85  ?  35  TRP A CB  1 
ATOM   247  C CG  . TRP A 1 35  ? -9.538  33.667  34.002  1.00 42.44  ?  35  TRP A CG  1 
ATOM   248  C CD1 . TRP A 1 35  ? -9.974  34.475  35.004  1.00 47.29  ?  35  TRP A CD1 1 
ATOM   249  C CD2 . TRP A 1 35  ? -10.024 32.352  34.304  1.00 47.17  ?  35  TRP A CD2 1 
ATOM   250  N NE1 . TRP A 1 35  ? -10.702 33.751  35.915  1.00 51.24  ?  35  TRP A NE1 1 
ATOM   251  C CE2 . TRP A 1 35  ? -10.745 32.443  35.510  1.00 46.39  ?  35  TRP A CE2 1 
ATOM   252  C CE3 . TRP A 1 35  ? -9.910  31.106  33.676  1.00 38.80  ?  35  TRP A CE3 1 
ATOM   253  C CZ2 . TRP A 1 35  ? -11.352 31.341  36.101  1.00 48.54  ?  35  TRP A CZ2 1 
ATOM   254  C CZ3 . TRP A 1 35  ? -10.511 30.012  34.265  1.00 48.66  ?  35  TRP A CZ3 1 
ATOM   255  C CH2 . TRP A 1 35  ? -11.227 30.137  35.464  1.00 55.16  ?  35  TRP A CH2 1 
ATOM   256  N N   . TYR A 1 36  ? -6.308  32.869  30.937  1.00 40.88  ?  36  TYR A N   1 
ATOM   257  C CA  . TYR A 1 36  ? -5.598  32.795  29.671  1.00 41.24  ?  36  TYR A CA  1 
ATOM   258  C C   . TYR A 1 36  ? -6.419  32.011  28.660  1.00 38.20  ?  36  TYR A C   1 
ATOM   259  O O   . TYR A 1 36  ? -7.119  31.057  29.009  1.00 41.43  ?  36  TYR A O   1 
ATOM   260  C CB  . TYR A 1 36  ? -4.215  32.128  29.845  1.00 34.79  ?  36  TYR A CB  1 
ATOM   261  C CG  . TYR A 1 36  ? -3.327  32.874  30.808  1.00 39.53  ?  36  TYR A CG  1 
ATOM   262  C CD1 . TYR A 1 36  ? -2.517  33.915  30.365  1.00 38.49  ?  36  TYR A CD1 1 
ATOM   263  C CD2 . TYR A 1 36  ? -3.326  32.570  32.164  1.00 38.14  ?  36  TYR A CD2 1 
ATOM   264  C CE1 . TYR A 1 36  ? -1.718  34.627  31.240  1.00 37.85  ?  36  TYR A CE1 1 
ATOM   265  C CE2 . TYR A 1 36  ? -2.530  33.278  33.053  1.00 38.63  ?  36  TYR A CE2 1 
ATOM   266  C CZ  . TYR A 1 36  ? -1.725  34.307  32.585  1.00 40.47  ?  36  TYR A CZ  1 
ATOM   267  O OH  . TYR A 1 36  ? -0.927  35.010  33.463  1.00 39.88  ?  36  TYR A OH  1 
ATOM   268  N N   . GLN A 1 37  ? -6.313  32.427  27.402  1.00 37.57  ?  37  GLN A N   1 
ATOM   269  C CA  . GLN A 1 37  ? -6.916  31.759  26.256  1.00 36.26  ?  37  GLN A CA  1 
ATOM   270  C C   . GLN A 1 37  ? -5.815  31.211  25.358  1.00 39.93  ?  37  GLN A C   1 
ATOM   271  O O   . GLN A 1 37  ? -4.886  31.941  24.994  1.00 38.05  ?  37  GLN A O   1 
ATOM   272  C CB  . GLN A 1 37  ? -7.791  32.734  25.469  1.00 36.51  ?  37  GLN A CB  1 
ATOM   273  C CG  . GLN A 1 37  ? -8.127  32.301  24.053  1.00 41.51  ?  37  GLN A CG  1 
ATOM   274  C CD  . GLN A 1 37  ? -8.752  33.436  23.250  1.00 49.43  ?  37  GLN A CD  1 
ATOM   275  O OE1 . GLN A 1 37  ? -8.050  34.330  22.754  1.00 49.41  ?  37  GLN A OE1 1 
ATOM   276  N NE2 . GLN A 1 37  ? -10.072 33.398  23.104  1.00 45.36  ?  37  GLN A NE2 1 
ATOM   277  N N   . GLN A 1 38  ? -5.932  29.939  24.976  1.00 38.50  ?  38  GLN A N   1 
ATOM   278  C CA  . GLN A 1 38  ? -4.971  29.296  24.091  1.00 44.29  ?  38  GLN A CA  1 
ATOM   279  C C   . GLN A 1 38  ? -5.700  28.779  22.864  1.00 40.35  ?  38  GLN A C   1 
ATOM   280  O O   . GLN A 1 38  ? -6.507  27.845  22.958  1.00 39.64  ?  38  GLN A O   1 
ATOM   281  C CB  . GLN A 1 38  ? -4.228  28.166  24.787  1.00 41.28  ?  38  GLN A CB  1 
ATOM   282  C CG  . GLN A 1 38  ? -3.118  27.609  23.927  1.00 37.06  ?  38  GLN A CG  1 
ATOM   283  C CD  . GLN A 1 38  ? -2.253  26.623  24.668  1.00 47.32  ?  38  GLN A CD  1 
ATOM   284  O OE1 . GLN A 1 38  ? -2.751  25.802  25.442  1.00 49.88  ?  38  GLN A OE1 1 
ATOM   285  N NE2 . GLN A 1 38  ? -0.941  26.708  24.453  1.00 45.96  ?  38  GLN A NE2 1 
ATOM   286  N N   . LYS A 1 39  ? -5.415  29.405  21.729  1.00 46.03  ?  39  LYS A N   1 
ATOM   287  C CA  . LYS A 1 39  ? -5.898  28.986  20.433  1.00 48.37  ?  39  LYS A CA  1 
ATOM   288  C C   . LYS A 1 39  ? -5.030  27.846  19.919  1.00 50.36  ?  39  LYS A C   1 
ATOM   289  O O   . LYS A 1 39  ? -3.910  27.644  20.395  1.00 52.00  ?  39  LYS A O   1 
ATOM   290  C CB  . LYS A 1 39  ? -5.855  30.163  19.460  1.00 48.94  ?  39  LYS A CB  1 
ATOM   291  C CG  . LYS A 1 39  ? -6.703  31.357  19.858  1.00 41.83  ?  39  LYS A CG  1 
ATOM   292  C CD  . LYS A 1 39  ? -8.179  31.105  19.596  1.00 47.30  ?  39  LYS A CD  1 
ATOM   293  C CE  . LYS A 1 39  ? -9.045  32.298  19.998  1.00 50.89  ?  39  LYS A CE  1 
ATOM   294  N NZ  . LYS A 1 39  ? -8.880  33.505  19.124  1.00 57.26  ?  39  LYS A NZ  1 
ATOM   295  N N   . PRO A 1 40  ? -5.533  27.062  18.969  1.00 54.87  ?  40  PRO A N   1 
ATOM   296  C CA  . PRO A 1 40  ? -4.737  25.942  18.449  1.00 52.57  ?  40  PRO A CA  1 
ATOM   297  C C   . PRO A 1 40  ? -3.410  26.416  17.870  1.00 53.09  ?  40  PRO A C   1 
ATOM   298  O O   . PRO A 1 40  ? -3.360  27.331  17.044  1.00 51.09  ?  40  PRO A O   1 
ATOM   299  C CB  . PRO A 1 40  ? -5.645  25.339  17.374  1.00 46.55  ?  40  PRO A CB  1 
ATOM   300  C CG  . PRO A 1 40  ? -7.014  25.663  17.841  1.00 52.62  ?  40  PRO A CG  1 
ATOM   301  C CD  . PRO A 1 40  ? -6.921  27.025  18.477  1.00 52.89  ?  40  PRO A CD  1 
ATOM   302  N N   . GLY A 1 41  ? -2.329  25.780  18.318  1.00 50.50  ?  41  GLY A N   1 
ATOM   303  C CA  . GLY A 1 41  ? -1.011  26.074  17.785  1.00 48.26  ?  41  GLY A CA  1 
ATOM   304  C C   . GLY A 1 41  ? -0.509  27.472  18.060  1.00 56.93  ?  41  GLY A C   1 
ATOM   305  O O   . GLY A 1 41  ? 0.237   28.024  17.246  1.00 68.45  ?  41  GLY A O   1 
ATOM   306  N N   . LYS A 1 42  ? -0.894  28.065  19.188  1.00 57.65  ?  42  LYS A N   1 
ATOM   307  C CA  . LYS A 1 42  ? -0.401  29.378  19.578  1.00 49.28  ?  42  LYS A CA  1 
ATOM   308  C C   . LYS A 1 42  ? -0.117  29.379  21.073  1.00 48.22  ?  42  LYS A C   1 
ATOM   309  O O   . LYS A 1 42  ? -0.598  28.524  21.822  1.00 47.90  ?  42  LYS A O   1 
ATOM   310  C CB  . LYS A 1 42  ? -1.395  30.495  19.233  1.00 48.00  ?  42  LYS A CB  1 
ATOM   311  C CG  . LYS A 1 42  ? -1.567  30.745  17.746  1.00 52.20  ?  42  LYS A CG  1 
ATOM   312  C CD  . LYS A 1 42  ? -2.540  31.890  17.502  1.00 65.97  ?  42  LYS A CD  1 
ATOM   313  C CE  . LYS A 1 42  ? -2.770  32.118  16.015  1.00 82.51  ?  42  LYS A CE  1 
ATOM   314  N NZ  . LYS A 1 42  ? -3.854  33.110  15.760  1.00 88.35  ?  42  LYS A NZ  1 
ATOM   315  N N   . ALA A 1 43  ? 0.684   30.347  21.500  1.00 47.82  ?  43  ALA A N   1 
ATOM   316  C CA  . ALA A 1 43  ? 0.965   30.495  22.910  1.00 39.28  ?  43  ALA A CA  1 
ATOM   317  C C   . ALA A 1 43  ? -0.249  31.103  23.601  1.00 40.67  ?  43  ALA A C   1 
ATOM   318  O O   . ALA A 1 43  ? -1.077  31.759  22.962  1.00 39.85  ?  43  ALA A O   1 
ATOM   319  C CB  . ALA A 1 43  ? 2.204   31.364  23.122  1.00 34.89  ?  43  ALA A CB  1 
ATOM   320  N N   . PRO A 1 44  ? -0.386  30.889  24.903  1.00 37.39  ?  44  PRO A N   1 
ATOM   321  C CA  . PRO A 1 44  ? -1.532  31.454  25.617  1.00 39.32  ?  44  PRO A CA  1 
ATOM   322  C C   . PRO A 1 44  ? -1.527  32.975  25.563  1.00 41.02  ?  44  PRO A C   1 
ATOM   323  O O   . PRO A 1 44  ? -0.478  33.619  25.469  1.00 41.07  ?  44  PRO A O   1 
ATOM   324  C CB  . PRO A 1 44  ? -1.340  30.947  27.050  1.00 43.23  ?  44  PRO A CB  1 
ATOM   325  C CG  . PRO A 1 44  ? -0.468  29.748  26.916  1.00 39.22  ?  44  PRO A CG  1 
ATOM   326  C CD  . PRO A 1 44  ? 0.436   30.026  25.766  1.00 36.68  ?  44  PRO A CD  1 
ATOM   327  N N   . LYS A 1 45  ? -2.725  33.545  25.614  1.00 40.47  ?  45  LYS A N   1 
ATOM   328  C CA  . LYS A 1 45  ? -2.929  34.985  25.615  1.00 40.04  ?  45  LYS A CA  1 
ATOM   329  C C   . LYS A 1 45  ? -3.587  35.398  26.924  1.00 42.89  ?  45  LYS A C   1 
ATOM   330  O O   . LYS A 1 45  ? -4.579  34.789  27.341  1.00 38.62  ?  45  LYS A O   1 
ATOM   331  C CB  . LYS A 1 45  ? -3.798  35.399  24.425  1.00 41.13  ?  45  LYS A CB  1 
ATOM   332  C CG  . LYS A 1 45  ? -4.166  36.876  24.377  1.00 53.22  ?  45  LYS A CG  1 
ATOM   333  C CD  . LYS A 1 45  ? -5.419  37.070  23.528  1.00 61.37  ?  45  LYS A CD  1 
ATOM   334  C CE  . LYS A 1 45  ? -5.915  38.508  23.534  1.00 70.88  ?  45  LYS A CE  1 
ATOM   335  N NZ  . LYS A 1 45  ? -7.174  38.641  22.737  1.00 67.94  ?  45  LYS A NZ  1 
ATOM   336  N N   . LEU A 1 46  ? -3.038  36.431  27.567  1.00 44.30  ?  46  LEU A N   1 
ATOM   337  C CA  . LEU A 1 46  ? -3.597  36.928  28.821  1.00 42.18  ?  46  LEU A CA  1 
ATOM   338  C C   . LEU A 1 46  ? -4.938  37.601  28.562  1.00 40.94  ?  46  LEU A C   1 
ATOM   339  O O   . LEU A 1 46  ? -5.022  38.541  27.768  1.00 47.70  ?  46  LEU A O   1 
ATOM   340  C CB  . LEU A 1 46  ? -2.636  37.912  29.480  1.00 40.66  ?  46  LEU A CB  1 
ATOM   341  C CG  . LEU A 1 46  ? -3.163  38.615  30.734  1.00 41.70  ?  46  LEU A CG  1 
ATOM   342  C CD1 . LEU A 1 46  ? -3.342  37.637  31.895  1.00 38.33  ?  46  LEU A CD1 1 
ATOM   343  C CD2 . LEU A 1 46  ? -2.255  39.762  31.132  1.00 44.64  ?  46  LEU A CD2 1 
ATOM   344  N N   . LEU A 1 47  ? -5.985  37.121  29.231  1.00 41.44  ?  47  LEU A N   1 
ATOM   345  C CA  . LEU A 1 47  ? -7.309  37.727  29.165  1.00 45.21  ?  47  LEU A CA  1 
ATOM   346  C C   . LEU A 1 47  ? -7.617  38.568  30.392  1.00 46.51  ?  47  LEU A C   1 
ATOM   347  O O   . LEU A 1 47  ? -8.082  39.704  30.264  1.00 43.82  ?  47  LEU A O   1 
ATOM   348  C CB  . LEU A 1 47  ? -8.404  36.664  29.019  1.00 43.56  ?  47  LEU A CB  1 
ATOM   349  C CG  . LEU A 1 47  ? -8.506  35.824  27.752  1.00 45.33  ?  47  LEU A CG  1 
ATOM   350  C CD1 . LEU A 1 47  ? -9.575  34.760  27.960  1.00 43.86  ?  47  LEU A CD1 1 
ATOM   351  C CD2 . LEU A 1 47  ? -8.829  36.701  26.557  1.00 46.89  ?  47  LEU A CD2 1 
ATOM   352  N N   . ILE A 1 48  ? -7.403  38.021  31.585  1.00 45.08  ?  48  ILE A N   1 
ATOM   353  C CA  . ILE A 1 48  ? -7.858  38.684  32.804  1.00 45.29  ?  48  ILE A CA  1 
ATOM   354  C C   . ILE A 1 48  ? -6.797  38.542  33.884  1.00 42.85  ?  48  ILE A C   1 
ATOM   355  O O   . ILE A 1 48  ? -6.179  37.484  34.015  1.00 44.58  ?  48  ILE A O   1 
ATOM   356  C CB  . ILE A 1 48  ? -9.222  38.117  33.266  1.00 48.33  ?  48  ILE A CB  1 
ATOM   357  C CG1 . ILE A 1 48  ? -10.325 38.564  32.306  1.00 48.16  ?  48  ILE A CG1 1 
ATOM   358  C CG2 . ILE A 1 48  ? -9.561  38.534  34.688  1.00 44.54  ?  48  ILE A CG2 1 
ATOM   359  C CD1 . ILE A 1 48  ? -11.703 38.203  32.757  1.00 49.52  ?  48  ILE A CD1 1 
ATOM   360  N N   . TYR A 1 49  ? -6.629  39.614  34.666  1.00 44.38  ?  49  TYR A N   1 
ATOM   361  C CA  . TYR A 1 49  ? -5.665  39.635  35.793  1.00 42.03  ?  49  TYR A CA  1 
ATOM   362  C C   . TYR A 1 49  ? -6.326  40.188  37.055  1.00 46.67  ?  49  TYR A C   1 
ATOM   363  O O   . TYR A 1 49  ? -7.299  40.928  36.949  1.00 46.03  ?  49  TYR A O   1 
ATOM   364  C CB  . TYR A 1 49  ? -4.417  40.433  35.416  1.00 39.30  ?  49  TYR A CB  1 
ATOM   365  C CG  . TYR A 1 49  ? -4.557  41.920  35.241  1.00 45.79  ?  49  TYR A CG  1 
ATOM   366  C CD1 . TYR A 1 49  ? -4.908  42.457  34.017  1.00 45.21  ?  49  TYR A CD1 1 
ATOM   367  C CD2 . TYR A 1 49  ? -4.271  42.791  36.275  1.00 49.48  ?  49  TYR A CD2 1 
ATOM   368  C CE1 . TYR A 1 49  ? -5.017  43.823  33.836  1.00 49.52  ?  49  TYR A CE1 1 
ATOM   369  C CE2 . TYR A 1 49  ? -4.376  44.161  36.111  1.00 46.02  ?  49  TYR A CE2 1 
ATOM   370  C CZ  . TYR A 1 49  ? -4.751  44.678  34.887  1.00 48.22  ?  49  TYR A CZ  1 
ATOM   371  O OH  . TYR A 1 49  ? -4.853  46.024  34.707  1.00 39.41  ?  49  TYR A OH  1 
ATOM   372  N N   . ASP A 1 50  ? -5.810  39.807  38.212  1.00 43.28  ?  50  ASP A N   1 
ATOM   373  C CA  . ASP A 1 50  ? -6.350  40.249  39.522  1.00 43.39  ?  50  ASP A CA  1 
ATOM   374  C C   . ASP A 1 50  ? -7.820  39.856  39.649  1.00 49.90  ?  50  ASP A C   1 
ATOM   375  O O   . ASP A 1 50  ? -8.565  40.627  40.260  1.00 52.57  ?  50  ASP A O   1 
ATOM   376  C CB  . ASP A 1 50  ? -6.059  41.724  39.781  1.00 51.45  ?  50  ASP A CB  1 
ATOM   377  C CG  . ASP A 1 50  ? -4.593  41.996  40.061  1.00 71.63  ?  50  ASP A CG  1 
ATOM   378  O OD1 . ASP A 1 50  ? -3.859  41.026  40.335  1.00 73.83  ?  50  ASP A OD1 1 
ATOM   379  O OD2 . ASP A 1 50  ? -4.195  43.174  39.995  1.00 68.79  ?  50  ASP A OD2 1 
ATOM   380  N N   . ALA A 1 51  ? -8.191  38.706  39.094  1.00 47.60  ?  51  ALA A N   1 
ATOM   381  C CA  . ALA A 1 51  ? -9.557  38.150  39.200  1.00 44.74  ?  51  ALA A CA  1 
ATOM   382  C C   . ALA A 1 51  ? -10.569 38.858  38.309  1.00 46.07  ?  51  ALA A C   1 
ATOM   383  O O   . ALA A 1 51  ? -11.376 38.151  37.728  1.00 48.48  ?  51  ALA A O   1 
ATOM   384  C CB  . ALA A 1 51  ? -10.001 38.139  40.624  1.00 44.39  ?  51  ALA A CB  1 
ATOM   385  N N   . SER A 1 52  ? -10.512 40.179  38.181  1.00 43.89  ?  52  SER A N   1 
ATOM   386  C CA  . SER A 1 52  ? -11.575 40.892  37.428  1.00 47.94  ?  52  SER A CA  1 
ATOM   387  C C   . SER A 1 52  ? -11.064 41.910  36.423  1.00 46.84  ?  52  SER A C   1 
ATOM   388  O O   . SER A 1 52  ? -11.893 42.462  35.715  1.00 53.48  ?  52  SER A O   1 
ATOM   389  C CB  . SER A 1 52  ? -12.453 41.597  38.397  1.00 47.39  ?  52  SER A CB  1 
ATOM   390  O OG  . SER A 1 52  ? -11.741 42.601  39.100  1.00 58.62  ?  52  SER A OG  1 
ATOM   391  N N   . SER A 1 53  ? -9.770  42.165  36.364  1.00 47.74  ?  53  SER A N   1 
ATOM   392  C CA  . SER A 1 53  ? -9.283  43.260  35.493  1.00 48.61  ?  53  SER A CA  1 
ATOM   393  C C   . SER A 1 53  ? -8.994  42.748  34.086  1.00 48.93  ?  53  SER A C   1 
ATOM   394  O O   . SER A 1 53  ? -8.167  41.856  33.936  1.00 46.52  ?  53  SER A O   1 
ATOM   395  C CB  . SER A 1 53  ? -8.112  43.941  36.100  1.00 48.78  ?  53  SER A CB  1 
ATOM   396  O OG  . SER A 1 53  ? -8.455  44.487  37.362  1.00 52.67  ?  53  SER A OG  1 
ATOM   397  N N   . LEU A 1 54  ? -9.686  43.314  33.104  1.00 49.10  ?  54  LEU A N   1 
ATOM   398  C CA  . LEU A 1 54  ? -9.433  42.925  31.723  1.00 45.35  ?  54  LEU A CA  1 
ATOM   399  C C   . LEU A 1 54  ? -8.082  43.431  31.250  1.00 47.47  ?  54  LEU A C   1 
ATOM   400  O O   . LEU A 1 54  ? -7.700  44.576  31.508  1.00 50.80  ?  54  LEU A O   1 
ATOM   401  C CB  . LEU A 1 54  ? -10.517 43.459  30.795  1.00 44.23  ?  54  LEU A CB  1 
ATOM   402  C CG  . LEU A 1 54  ? -11.759 42.614  30.544  1.00 50.46  ?  54  LEU A CG  1 
ATOM   403  C CD1 . LEU A 1 54  ? -12.625 42.522  31.794  1.00 57.30  ?  54  LEU A CD1 1 
ATOM   404  C CD2 . LEU A 1 54  ? -12.530 43.211  29.380  1.00 54.94  ?  54  LEU A CD2 1 
ATOM   405  N N   . ALA A 1 55  ? -7.362  42.570  30.541  1.00 49.50  ?  55  ALA A N   1 
ATOM   406  C CA  . ALA A 1 55  ? -6.112  42.973  29.925  1.00 45.66  ?  55  ALA A CA  1 
ATOM   407  C C   . ALA A 1 55  ? -6.381  43.789  28.664  1.00 52.52  ?  55  ALA A C   1 
ATOM   408  O O   . ALA A 1 55  ? -7.489  43.801  28.115  1.00 51.02  ?  55  ALA A O   1 
ATOM   409  C CB  . ALA A 1 55  ? -5.254  41.754  29.595  1.00 39.15  ?  55  ALA A CB  1 
ATOM   410  N N   . SER A 1 56  ? -5.339  44.478  28.209  1.00 54.21  ?  56  SER A N   1 
ATOM   411  C CA  . SER A 1 56  ? -5.458  45.373  27.068  1.00 55.96  ?  56  SER A CA  1 
ATOM   412  C C   . SER A 1 56  ? -5.795  44.599  25.799  1.00 57.53  ?  56  SER A C   1 
ATOM   413  O O   . SER A 1 56  ? -5.141  43.606  25.471  1.00 54.66  ?  56  SER A O   1 
ATOM   414  C CB  . SER A 1 56  ? -4.154  46.149  26.883  1.00 64.45  ?  56  SER A CB  1 
ATOM   415  O OG  . SER A 1 56  ? -4.131  46.834  25.643  1.00 73.11  ?  56  SER A OG  1 
ATOM   416  N N   . GLY A 1 57  ? -6.826  45.059  25.090  1.00 61.60  ?  57  GLY A N   1 
ATOM   417  C CA  . GLY A 1 57  ? -7.201  44.464  23.822  1.00 54.12  ?  57  GLY A CA  1 
ATOM   418  C C   . GLY A 1 57  ? -8.077  43.239  23.917  1.00 58.18  ?  57  GLY A C   1 
ATOM   419  O O   . GLY A 1 57  ? -8.134  42.455  22.965  1.00 64.24  ?  57  GLY A O   1 
ATOM   420  N N   . VAL A 1 58  ? -8.787  43.061  25.021  1.00 54.24  ?  58  VAL A N   1 
ATOM   421  C CA  . VAL A 1 58  ? -9.654  41.907  25.231  1.00 55.22  ?  58  VAL A CA  1 
ATOM   422  C C   . VAL A 1 58  ? -11.096 42.379  25.092  1.00 52.68  ?  58  VAL A C   1 
ATOM   423  O O   . VAL A 1 58  ? -11.503 43.312  25.795  1.00 52.21  ?  58  VAL A O   1 
ATOM   424  C CB  . VAL A 1 58  ? -9.412  41.257  26.600  1.00 56.99  ?  58  VAL A CB  1 
ATOM   425  C CG1 . VAL A 1 58  ? -10.359 40.084  26.805  1.00 52.08  ?  58  VAL A CG1 1 
ATOM   426  C CG2 . VAL A 1 58  ? -7.959  40.802  26.717  1.00 53.37  ?  58  VAL A CG2 1 
ATOM   427  N N   . PRO A 1 59  ? -11.895 41.774  24.211  1.00 54.27  ?  59  PRO A N   1 
ATOM   428  C CA  . PRO A 1 59  ? -13.282 42.218  24.048  1.00 50.43  ?  59  PRO A CA  1 
ATOM   429  C C   . PRO A 1 59  ? -14.039 42.180  25.366  1.00 52.54  ?  59  PRO A C   1 
ATOM   430  O O   . PRO A 1 59  ? -13.743 41.390  26.266  1.00 53.02  ?  59  PRO A O   1 
ATOM   431  C CB  . PRO A 1 59  ? -13.865 41.219  23.036  1.00 55.63  ?  59  PRO A CB  1 
ATOM   432  C CG  . PRO A 1 59  ? -12.909 40.076  23.006  1.00 48.93  ?  59  PRO A CG  1 
ATOM   433  C CD  . PRO A 1 59  ? -11.566 40.657  23.312  1.00 51.78  ?  59  PRO A CD  1 
ATOM   434  N N   . SER A 1 60  ? -15.048 43.044  25.458  1.00 52.66  ?  60  SER A N   1 
ATOM   435  C CA  . SER A 1 60  ? -15.774 43.253  26.702  1.00 51.40  ?  60  SER A CA  1 
ATOM   436  C C   . SER A 1 60  ? -16.653 42.073  27.105  1.00 47.50  ?  60  SER A C   1 
ATOM   437  O O   . SER A 1 60  ? -17.227 42.108  28.198  1.00 47.52  ?  60  SER A O   1 
ATOM   438  C CB  . SER A 1 60  ? -16.609 44.526  26.581  1.00 53.07  ?  60  SER A CB  1 
ATOM   439  O OG  . SER A 1 60  ? -17.393 44.491  25.404  1.00 55.36  ?  60  SER A OG  1 
ATOM   440  N N   . ARG A 1 61  ? -16.790 41.041  26.267  1.00 46.33  ?  61  ARG A N   1 
ATOM   441  C CA  . ARG A 1 61  ? -17.611 39.903  26.670  1.00 45.98  ?  61  ARG A CA  1 
ATOM   442  C C   . ARG A 1 61  ? -16.924 39.012  27.699  1.00 47.66  ?  61  ARG A C   1 
ATOM   443  O O   . ARG A 1 61  ? -17.588 38.148  28.282  1.00 49.20  ?  61  ARG A O   1 
ATOM   444  C CB  . ARG A 1 61  ? -17.994 39.050  25.461  1.00 44.77  ?  61  ARG A CB  1 
ATOM   445  C CG  . ARG A 1 61  ? -16.821 38.542  24.655  1.00 51.50  ?  61  ARG A CG  1 
ATOM   446  C CD  . ARG A 1 61  ? -17.298 37.787  23.424  1.00 53.51  ?  61  ARG A CD  1 
ATOM   447  N NE  . ARG A 1 61  ? -16.201 37.449  22.523  1.00 55.27  ?  61  ARG A NE  1 
ATOM   448  C CZ  . ARG A 1 61  ? -15.773 38.224  21.532  1.00 64.19  ?  61  ARG A CZ  1 
ATOM   449  N NH1 . ARG A 1 61  ? -16.355 39.396  21.298  1.00 66.19  ?  61  ARG A NH1 1 
ATOM   450  N NH2 . ARG A 1 61  ? -14.763 37.821  20.772  1.00 60.34  ?  61  ARG A NH2 1 
ATOM   451  N N   . PHE A 1 62  ? -15.626 39.191  27.936  1.00 45.79  ?  62  PHE A N   1 
ATOM   452  C CA  . PHE A 1 62  ? -14.918 38.445  28.969  1.00 44.67  ?  62  PHE A CA  1 
ATOM   453  C C   . PHE A 1 62  ? -14.967 39.210  30.285  1.00 45.07  ?  62  PHE A C   1 
ATOM   454  O O   . PHE A 1 62  ? -14.690 40.414  30.324  1.00 47.10  ?  62  PHE A O   1 
ATOM   455  C CB  . PHE A 1 62  ? -13.464 38.184  28.564  1.00 45.62  ?  62  PHE A CB  1 
ATOM   456  C CG  . PHE A 1 62  ? -13.316 37.287  27.365  1.00 47.86  ?  62  PHE A CG  1 
ATOM   457  C CD1 . PHE A 1 62  ? -13.310 35.912  27.509  1.00 46.41  ?  62  PHE A CD1 1 
ATOM   458  C CD2 . PHE A 1 62  ? -13.169 37.819  26.096  1.00 51.88  ?  62  PHE A CD2 1 
ATOM   459  C CE1 . PHE A 1 62  ? -13.173 35.088  26.409  1.00 45.25  ?  62  PHE A CE1 1 
ATOM   460  C CE2 . PHE A 1 62  ? -13.030 36.994  24.992  1.00 46.17  ?  62  PHE A CE2 1 
ATOM   461  C CZ  . PHE A 1 62  ? -13.033 35.632  25.151  1.00 43.10  ?  62  PHE A CZ  1 
ATOM   462  N N   . SER A 1 63  ? -15.296 38.503  31.363  1.00 41.35  ?  63  SER A N   1 
ATOM   463  C CA  . SER A 1 63  ? -15.346 39.121  32.680  1.00 45.01  ?  63  SER A CA  1 
ATOM   464  C C   . SER A 1 63  ? -14.917 38.097  33.718  1.00 43.84  ?  63  SER A C   1 
ATOM   465  O O   . SER A 1 63  ? -14.964 36.892  33.482  1.00 44.38  ?  63  SER A O   1 
ATOM   466  C CB  . SER A 1 63  ? -16.747 39.659  33.002  1.00 41.02  ?  63  SER A CB  1 
ATOM   467  O OG  . SER A 1 63  ? -17.748 38.678  32.773  1.00 48.05  ?  63  SER A OG  1 
ATOM   468  N N   . GLY A 1 64  ? -14.494 38.589  34.870  1.00 45.37  ?  64  GLY A N   1 
ATOM   469  C CA  . GLY A 1 64  ? -13.997 37.722  35.922  1.00 43.75  ?  64  GLY A CA  1 
ATOM   470  C C   . GLY A 1 64  ? -14.521 38.157  37.271  1.00 45.99  ?  64  GLY A C   1 
ATOM   471  O O   . GLY A 1 64  ? -14.743 39.343  37.526  1.00 51.73  ?  64  GLY A O   1 
ATOM   472  N N   . SER A 1 65  ? -14.719 37.172  38.141  1.00 45.40  ?  65  SER A N   1 
ATOM   473  C CA  . SER A 1 65  ? -15.303 37.407  39.451  1.00 48.43  ?  65  SER A CA  1 
ATOM   474  C C   . SER A 1 65  ? -14.638 36.506  40.482  1.00 44.43  ?  65  SER A C   1 
ATOM   475  O O   . SER A 1 65  ? -14.161 35.416  40.160  1.00 47.70  ?  65  SER A O   1 
ATOM   476  C CB  . SER A 1 65  ? -16.823 37.170  39.425  1.00 48.63  ?  65  SER A CB  1 
ATOM   477  O OG  . SER A 1 65  ? -17.350 37.044  40.735  1.00 55.90  ?  65  SER A OG  1 
ATOM   478  N N   . ARG A 1 66  ? -14.622 36.973  41.729  1.00 43.82  ?  66  ARG A N   1 
ATOM   479  C CA  . ARG A 1 66  ? -14.048 36.244  42.848  1.00 46.52  ?  66  ARG A CA  1 
ATOM   480  C C   . ARG A 1 66  ? -15.078 36.065  43.961  1.00 50.93  ?  66  ARG A C   1 
ATOM   481  O O   . ARG A 1 66  ? -15.967 36.898  44.151  1.00 48.04  ?  66  ARG A O   1 
ATOM   482  C CB  . ARG A 1 66  ? -12.819 36.972  43.407  1.00 45.38  ?  66  ARG A CB  1 
ATOM   483  C CG  . ARG A 1 66  ? -12.165 36.248  44.572  1.00 49.12  ?  66  ARG A CG  1 
ATOM   484  C CD  . ARG A 1 66  ? -11.226 37.122  45.368  1.00 44.06  ?  66  ARG A CD  1 
ATOM   485  N NE  . ARG A 1 66  ? -10.829 36.421  46.582  1.00 45.08  ?  66  ARG A NE  1 
ATOM   486  C CZ  . ARG A 1 66  ? -10.130 36.965  47.569  1.00 47.75  ?  66  ARG A CZ  1 
ATOM   487  N NH1 . ARG A 1 66  ? -9.814  36.234  48.632  1.00 48.67  ?  66  ARG A NH1 1 
ATOM   488  N NH2 . ARG A 1 66  ? -9.756  38.236  47.494  1.00 40.93  ?  66  ARG A NH2 1 
ATOM   489  N N   . SER A 1 67  ? -14.955 34.948  44.686  1.00 54.64  ?  67  SER A N   1 
ATOM   490  C CA  . SER A 1 67  ? -15.734 34.714  45.900  1.00 52.92  ?  67  SER A CA  1 
ATOM   491  C C   . SER A 1 67  ? -14.918 33.732  46.741  1.00 51.26  ?  67  SER A C   1 
ATOM   492  O O   . SER A 1 67  ? -14.975 32.521  46.510  1.00 55.09  ?  67  SER A O   1 
ATOM   493  C CB  . SER A 1 67  ? -17.119 34.177  45.588  1.00 61.63  ?  67  SER A CB  1 
ATOM   494  O OG  . SER A 1 67  ? -17.867 33.992  46.779  1.00 72.25  ?  67  SER A OG  1 
ATOM   495  N N   . GLY A 1 68  ? -14.139 34.267  47.678  1.00 55.73  ?  68  GLY A N   1 
ATOM   496  C CA  . GLY A 1 68  ? -13.245 33.463  48.490  1.00 51.91  ?  68  GLY A CA  1 
ATOM   497  C C   . GLY A 1 68  ? -12.134 32.811  47.693  1.00 54.65  ?  68  GLY A C   1 
ATOM   498  O O   . GLY A 1 68  ? -11.223 33.493  47.216  1.00 59.59  ?  68  GLY A O   1 
ATOM   499  N N   . THR A 1 69  ? -12.194 31.487  47.546  1.00 58.57  ?  69  THR A N   1 
ATOM   500  C CA  . THR A 1 69  ? -11.248 30.746  46.723  1.00 55.31  ?  69  THR A CA  1 
ATOM   501  C C   . THR A 1 69  ? -11.873 30.270  45.418  1.00 55.92  ?  69  THR A C   1 
ATOM   502  O O   . THR A 1 69  ? -11.244 29.494  44.688  1.00 56.65  ?  69  THR A O   1 
ATOM   503  C CB  . THR A 1 69  ? -10.681 29.544  47.487  1.00 58.32  ?  69  THR A CB  1 
ATOM   504  O OG1 . THR A 1 69  ? -11.724 28.595  47.748  1.00 57.37  ?  69  THR A OG1 1 
ATOM   505  C CG2 . THR A 1 69  ? -10.069 29.990  48.810  1.00 55.69  ?  69  THR A CG2 1 
ATOM   506  N N   . LYS A 1 70  ? -13.096 30.698  45.112  1.00 54.11  ?  70  LYS A N   1 
ATOM   507  C CA  . LYS A 1 70  ? -13.761 30.330  43.868  1.00 54.99  ?  70  LYS A CA  1 
ATOM   508  C C   . LYS A 1 70  ? -13.708 31.517  42.912  1.00 57.02  ?  70  LYS A C   1 
ATOM   509  O O   . LYS A 1 70  ? -14.159 32.615  43.248  1.00 54.08  ?  70  LYS A O   1 
ATOM   510  C CB  . LYS A 1 70  ? -15.200 29.890  44.137  1.00 52.26  ?  70  LYS A CB  1 
ATOM   511  C CG  . LYS A 1 70  ? -15.288 28.755  45.151  1.00 65.93  ?  70  LYS A CG  1 
ATOM   512  C CD  . LYS A 1 70  ? -16.652 28.072  45.176  1.00 80.08  ?  70  LYS A CD  1 
ATOM   513  C CE  . LYS A 1 70  ? -16.940 27.293  43.899  1.00 82.74  ?  70  LYS A CE  1 
ATOM   514  N NZ  . LYS A 1 70  ? -18.184 26.468  44.028  1.00 69.23  ?  70  LYS A NZ  1 
ATOM   515  N N   . PHE A 1 71  ? -13.146 31.302  41.730  1.00 53.52  ?  71  PHE A N   1 
ATOM   516  C CA  . PHE A 1 71  ? -13.043 32.327  40.709  1.00 46.24  ?  71  PHE A CA  1 
ATOM   517  C C   . PHE A 1 71  ? -13.852 31.895  39.497  1.00 48.86  ?  71  PHE A C   1 
ATOM   518  O O   . PHE A 1 71  ? -14.012 30.699  39.232  1.00 52.20  ?  71  PHE A O   1 
ATOM   519  C CB  . PHE A 1 71  ? -11.577 32.577  40.329  1.00 47.82  ?  71  PHE A CB  1 
ATOM   520  C CG  . PHE A 1 71  ? -10.741 33.071  41.473  1.00 47.91  ?  71  PHE A CG  1 
ATOM   521  C CD1 . PHE A 1 71  ? -10.309 32.199  42.459  1.00 42.08  ?  71  PHE A CD1 1 
ATOM   522  C CD2 . PHE A 1 71  ? -10.407 34.410  41.577  1.00 44.22  ?  71  PHE A CD2 1 
ATOM   523  C CE1 . PHE A 1 71  ? -9.557  32.648  43.518  1.00 39.99  ?  71  PHE A CE1 1 
ATOM   524  C CE2 . PHE A 1 71  ? -9.652  34.863  42.636  1.00 40.14  ?  71  PHE A CE2 1 
ATOM   525  C CZ  . PHE A 1 71  ? -9.228  33.978  43.608  1.00 40.47  ?  71  PHE A CZ  1 
ATOM   526  N N   . THR A 1 72  ? -14.381 32.876  38.774  1.00 45.75  ?  72  THR A N   1 
ATOM   527  C CA  . THR A 1 72  ? -15.237 32.604  37.630  1.00 44.74  ?  72  THR A CA  1 
ATOM   528  C C   . THR A 1 72  ? -14.828 33.485  36.463  1.00 49.51  ?  72  THR A C   1 
ATOM   529  O O   . THR A 1 72  ? -14.689 34.703  36.616  1.00 52.53  ?  72  THR A O   1 
ATOM   530  C CB  . THR A 1 72  ? -16.715 32.839  37.961  1.00 47.77  ?  72  THR A CB  1 
ATOM   531  O OG1 . THR A 1 72  ? -17.132 31.921  38.976  1.00 53.50  ?  72  THR A OG1 1 
ATOM   532  C CG2 . THR A 1 72  ? -17.576 32.622  36.726  1.00 49.88  ?  72  THR A CG2 1 
ATOM   533  N N   . LEU A 1 73  ? -14.608 32.855  35.315  1.00 46.41  ?  73  LEU A N   1 
ATOM   534  C CA  . LEU A 1 73  ? -14.461 33.543  34.042  1.00 47.69  ?  73  LEU A CA  1 
ATOM   535  C C   . LEU A 1 73  ? -15.770 33.389  33.285  1.00 47.51  ?  73  LEU A C   1 
ATOM   536  O O   . LEU A 1 73  ? -16.327 32.293  33.230  1.00 45.55  ?  73  LEU A O   1 
ATOM   537  C CB  . LEU A 1 73  ? -13.298 32.972  33.231  1.00 49.92  ?  73  LEU A CB  1 
ATOM   538  C CG  . LEU A 1 73  ? -13.197 33.436  31.778  1.00 46.57  ?  73  LEU A CG  1 
ATOM   539  C CD1 . LEU A 1 73  ? -12.792 34.892  31.716  1.00 39.19  ?  73  LEU A CD1 1 
ATOM   540  C CD2 . LEU A 1 73  ? -12.220 32.566  30.996  1.00 44.46  ?  73  LEU A CD2 1 
ATOM   541  N N   . THR A 1 74  ? -16.278 34.483  32.735  1.00 48.85  ?  74  THR A N   1 
ATOM   542  C CA  . THR A 1 74  ? -17.573 34.472  32.075  1.00 47.60  ?  74  THR A CA  1 
ATOM   543  C C   . THR A 1 74  ? -17.447 35.098  30.701  1.00 49.18  ?  74  THR A C   1 
ATOM   544  O O   . THR A 1 74  ? -16.906 36.200  30.560  1.00 52.21  ?  74  THR A O   1 
ATOM   545  C CB  . THR A 1 74  ? -18.626 35.221  32.894  1.00 47.75  ?  74  THR A CB  1 
ATOM   546  O OG1 . THR A 1 74  ? -18.753 34.606  34.182  1.00 55.50  ?  74  THR A OG1 1 
ATOM   547  C CG2 . THR A 1 74  ? -19.970 35.191  32.182  1.00 48.47  ?  74  THR A CG2 1 
ATOM   548  N N   . ILE A 1 75  ? -17.959 34.396  29.698  1.00 48.49  ?  75  ILE A N   1 
ATOM   549  C CA  . ILE A 1 75  ? -18.111 34.930  28.355  1.00 45.91  ?  75  ILE A CA  1 
ATOM   550  C C   . ILE A 1 75  ? -19.594 35.197  28.164  1.00 54.22  ?  75  ILE A C   1 
ATOM   551  O O   . ILE A 1 75  ? -20.412 34.272  28.256  1.00 57.91  ?  75  ILE A O   1 
ATOM   552  C CB  . ILE A 1 75  ? -17.568 33.961  27.295  1.00 47.54  ?  75  ILE A CB  1 
ATOM   553  C CG1 . ILE A 1 75  ? -16.190 33.447  27.715  1.00 48.68  ?  75  ILE A CG1 1 
ATOM   554  C CG2 . ILE A 1 75  ? -17.504 34.631  25.932  1.00 50.11  ?  75  ILE A CG2 1 
ATOM   555  C CD1 . ILE A 1 75  ? -15.586 32.448  26.753  1.00 47.66  ?  75  ILE A CD1 1 
ATOM   556  N N   . SER A 1 76  ? -19.942 36.467  27.926  1.00 53.07  ?  76  SER A N   1 
ATOM   557  C CA  . SER A 1 76  ? -21.344 36.876  27.918  1.00 53.48  ?  76  SER A CA  1 
ATOM   558  C C   . SER A 1 76  ? -22.051 36.472  26.629  1.00 58.51  ?  76  SER A C   1 
ATOM   559  O O   . SER A 1 76  ? -23.187 35.983  26.667  1.00 64.99  ?  76  SER A O   1 
ATOM   560  C CB  . SER A 1 76  ? -21.445 38.383  28.120  1.00 49.42  ?  76  SER A CB  1 
ATOM   561  O OG  . SER A 1 76  ? -20.807 39.065  27.056  1.00 55.36  ?  76  SER A OG  1 
ATOM   562  N N   . SER A 1 77  ? -21.400 36.667  25.486  1.00 57.43  ?  77  SER A N   1 
ATOM   563  C CA  . SER A 1 77  ? -21.946 36.306  24.178  1.00 54.54  ?  77  SER A CA  1 
ATOM   564  C C   . SER A 1 77  ? -20.876 35.525  23.424  1.00 56.80  ?  77  SER A C   1 
ATOM   565  O O   . SER A 1 77  ? -19.973 36.123  22.830  1.00 54.06  ?  77  SER A O   1 
ATOM   566  C CB  . SER A 1 77  ? -22.368 37.542  23.394  1.00 57.26  ?  77  SER A CB  1 
ATOM   567  O OG  . SER A 1 77  ? -22.705 37.190  22.063  1.00 61.95  ?  77  SER A OG  1 
ATOM   568  N N   . LEU A 1 78  ? -20.986 34.198  23.437  1.00 54.29  ?  78  LEU A N   1 
ATOM   569  C CA  . LEU A 1 78  ? -19.959 33.356  22.836  1.00 51.07  ?  78  LEU A CA  1 
ATOM   570  C C   . LEU A 1 78  ? -19.916 33.577  21.328  1.00 54.69  ?  78  LEU A C   1 
ATOM   571  O O   . LEU A 1 78  ? -20.956 33.601  20.662  1.00 53.41  ?  78  LEU A O   1 
ATOM   572  C CB  . LEU A 1 78  ? -20.231 31.887  23.154  1.00 52.30  ?  78  LEU A CB  1 
ATOM   573  C CG  . LEU A 1 78  ? -19.190 30.828  22.778  1.00 55.93  ?  78  LEU A CG  1 
ATOM   574  C CD1 . LEU A 1 78  ? -17.921 30.982  23.605  1.00 49.55  ?  78  LEU A CD1 1 
ATOM   575  C CD2 . LEU A 1 78  ? -19.775 29.434  22.947  1.00 52.62  ?  78  LEU A CD2 1 
ATOM   576  N N   . GLN A 1 79  ? -18.711 33.751  20.794  1.00 53.16  ?  79  GLN A N   1 
ATOM   577  C CA  . GLN A 1 79  ? -18.472 34.015  19.385  1.00 53.02  ?  79  GLN A CA  1 
ATOM   578  C C   . GLN A 1 79  ? -17.715 32.857  18.742  1.00 58.32  ?  79  GLN A C   1 
ATOM   579  O O   . GLN A 1 79  ? -17.038 32.088  19.433  1.00 57.32  ?  79  GLN A O   1 
ATOM   580  C CB  . GLN A 1 79  ? -17.678 35.317  19.214  1.00 52.86  ?  79  GLN A CB  1 
ATOM   581  C CG  . GLN A 1 79  ? -18.337 36.518  19.872  1.00 57.45  ?  79  GLN A CG  1 
ATOM   582  C CD  . GLN A 1 79  ? -19.759 36.737  19.389  1.00 57.78  ?  79  GLN A CD  1 
ATOM   583  O OE1 . GLN A 1 79  ? -20.695 36.833  20.191  1.00 53.44  ?  79  GLN A OE1 1 
ATOM   584  N NE2 . GLN A 1 79  ? -19.931 36.819  18.073  1.00 53.94  ?  79  GLN A NE2 1 
ATOM   585  N N   . PRO A 1 80  ? -17.819 32.689  17.417  1.00 60.31  ?  80  PRO A N   1 
ATOM   586  C CA  . PRO A 1 80  ? -17.133 31.556  16.773  1.00 54.74  ?  80  PRO A CA  1 
ATOM   587  C C   . PRO A 1 80  ? -15.630 31.578  16.965  1.00 54.32  ?  80  PRO A C   1 
ATOM   588  O O   . PRO A 1 80  ? -15.004 30.512  17.026  1.00 54.24  ?  80  PRO A O   1 
ATOM   589  C CB  . PRO A 1 80  ? -17.505 31.713  15.291  1.00 55.58  ?  80  PRO A CB  1 
ATOM   590  C CG  . PRO A 1 80  ? -18.737 32.552  15.287  1.00 55.12  ?  80  PRO A CG  1 
ATOM   591  C CD  . PRO A 1 80  ? -18.586 33.487  16.444  1.00 58.84  ?  80  PRO A CD  1 
ATOM   592  N N   . GLU A 1 81  ? -15.029 32.760  17.060  1.00 50.45  ?  81  GLU A N   1 
ATOM   593  C CA  . GLU A 1 81  ? -13.594 32.865  17.266  1.00 49.06  ?  81  GLU A CA  1 
ATOM   594  C C   . GLU A 1 81  ? -13.181 32.612  18.712  1.00 48.88  ?  81  GLU A C   1 
ATOM   595  O O   . GLU A 1 81  ? -12.000 32.769  19.030  1.00 50.59  ?  81  GLU A O   1 
ATOM   596  C CB  . GLU A 1 81  ? -13.091 34.243  16.824  1.00 49.39  ?  81  GLU A CB  1 
ATOM   597  C CG  . GLU A 1 81  ? -13.586 35.406  17.677  1.00 55.80  ?  81  GLU A CG  1 
ATOM   598  C CD  . GLU A 1 81  ? -14.794 36.106  17.084  1.00 67.11  ?  81  GLU A CD  1 
ATOM   599  O OE1 . GLU A 1 81  ? -15.679 35.413  16.529  1.00 67.24  ?  81  GLU A OE1 1 
ATOM   600  O OE2 . GLU A 1 81  ? -14.859 37.354  17.184  1.00 73.99  ?  81  GLU A OE2 1 
ATOM   601  N N   . ASP A 1 82  ? -14.105 32.225  19.591  1.00 47.06  ?  82  ASP A N   1 
ATOM   602  C CA  . ASP A 1 82  ? -13.770 31.947  20.982  1.00 45.11  ?  82  ASP A CA  1 
ATOM   603  C C   . ASP A 1 82  ? -13.447 30.480  21.241  1.00 44.79  ?  82  ASP A C   1 
ATOM   604  O O   . ASP A 1 82  ? -13.127 30.127  22.382  1.00 42.95  ?  82  ASP A O   1 
ATOM   605  C CB  . ASP A 1 82  ? -14.906 32.391  21.914  1.00 49.14  ?  82  ASP A CB  1 
ATOM   606  C CG  . ASP A 1 82  ? -15.123 33.897  21.902  1.00 54.18  ?  82  ASP A CG  1 
ATOM   607  O OD1 . ASP A 1 82  ? -16.295 34.322  21.987  1.00 55.97  ?  82  ASP A OD1 1 
ATOM   608  O OD2 . ASP A 1 82  ? -14.130 34.655  21.804  1.00 53.25  ?  82  ASP A OD2 1 
ATOM   609  N N   . PHE A 1 83  ? -13.537 29.622  20.225  1.00 45.69  ?  83  PHE A N   1 
ATOM   610  C CA  . PHE A 1 83  ? -13.091 28.239  20.358  1.00 46.76  ?  83  PHE A CA  1 
ATOM   611  C C   . PHE A 1 83  ? -11.654 28.198  20.842  1.00 43.48  ?  83  PHE A C   1 
ATOM   612  O O   . PHE A 1 83  ? -10.752 28.707  20.169  1.00 44.09  ?  83  PHE A O   1 
ATOM   613  C CB  . PHE A 1 83  ? -13.204 27.511  19.017  1.00 42.33  ?  83  PHE A CB  1 
ATOM   614  C CG  . PHE A 1 83  ? -12.375 26.258  18.943  1.00 47.66  ?  83  PHE A CG  1 
ATOM   615  C CD1 . PHE A 1 83  ? -11.151 26.253  18.292  1.00 46.43  ?  83  PHE A CD1 1 
ATOM   616  C CD2 . PHE A 1 83  ? -12.814 25.082  19.543  1.00 54.10  ?  83  PHE A CD2 1 
ATOM   617  C CE1 . PHE A 1 83  ? -10.388 25.102  18.228  1.00 49.48  ?  83  PHE A CE1 1 
ATOM   618  C CE2 . PHE A 1 83  ? -12.052 23.923  19.483  1.00 52.57  ?  83  PHE A CE2 1 
ATOM   619  C CZ  . PHE A 1 83  ? -10.838 23.935  18.825  1.00 52.19  ?  83  PHE A CZ  1 
ATOM   620  N N   . ALA A 1 84  ? -11.434 27.594  22.006  1.00 43.67  ?  84  ALA A N   1 
ATOM   621  C CA  . ALA A 1 84  ? -10.083 27.658  22.567  1.00 39.79  ?  84  ALA A CA  1 
ATOM   622  C C   . ALA A 1 84  ? -10.050 26.842  23.847  1.00 38.98  ?  84  ALA A C   1 
ATOM   623  O O   . ALA A 1 84  ? -11.075 26.338  24.313  1.00 37.90  ?  84  ALA A O   1 
ATOM   624  C CB  . ALA A 1 84  ? -9.634  29.090  22.865  1.00 36.23  ?  84  ALA A CB  1 
ATOM   625  N N   . THR A 1 85  ? -8.859  26.718  24.419  1.00 36.83  ?  85  THR A N   1 
ATOM   626  C CA  . THR A 1 85  ? -8.722  26.156  25.755  1.00 40.40  ?  85  THR A CA  1 
ATOM   627  C C   . THR A 1 85  ? -8.394  27.285  26.728  1.00 38.09  ?  85  THR A C   1 
ATOM   628  O O   . THR A 1 85  ? -7.543  28.128  26.446  1.00 37.32  ?  85  THR A O   1 
ATOM   629  C CB  . THR A 1 85  ? -7.663  25.051  25.788  1.00 40.77  ?  85  THR A CB  1 
ATOM   630  O OG1 . THR A 1 85  ? -7.933  24.105  24.744  1.00 39.09  ?  85  THR A OG1 1 
ATOM   631  C CG2 . THR A 1 85  ? -7.690  24.331  27.129  1.00 33.68  ?  85  THR A CG2 1 
ATOM   632  N N   . TYR A 1 86  ? -9.087  27.315  27.856  1.00 40.70  ?  86  TYR A N   1 
ATOM   633  C CA  . TYR A 1 86  ? -8.949  28.390  28.826  1.00 36.36  ?  86  TYR A CA  1 
ATOM   634  C C   . TYR A 1 86  ? -8.302  27.854  30.093  1.00 38.71  ?  86  TYR A C   1 
ATOM   635  O O   . TYR A 1 86  ? -8.666  26.778  30.576  1.00 42.43  ?  86  TYR A O   1 
ATOM   636  C CB  . TYR A 1 86  ? -10.313 29.021  29.119  1.00 35.49  ?  86  TYR A CB  1 
ATOM   637  C CG  . TYR A 1 86  ? -10.853 29.712  27.892  1.00 35.67  ?  86  TYR A CG  1 
ATOM   638  C CD1 . TYR A 1 86  ? -11.523 28.997  26.911  1.00 32.24  ?  86  TYR A CD1 1 
ATOM   639  C CD2 . TYR A 1 86  ? -10.637 31.074  27.683  1.00 37.00  ?  86  TYR A CD2 1 
ATOM   640  C CE1 . TYR A 1 86  ? -11.988 29.617  25.767  1.00 37.86  ?  86  TYR A CE1 1 
ATOM   641  C CE2 . TYR A 1 86  ? -11.100 31.707  26.542  1.00 33.49  ?  86  TYR A CE2 1 
ATOM   642  C CZ  . TYR A 1 86  ? -11.775 30.970  25.588  1.00 38.64  ?  86  TYR A CZ  1 
ATOM   643  O OH  . TYR A 1 86  ? -12.242 31.574  24.448  1.00 42.22  ?  86  TYR A OH  1 
ATOM   644  N N   . TYR A 1 87  ? -7.324  28.590  30.610  1.00 40.73  ?  87  TYR A N   1 
ATOM   645  C CA  . TYR A 1 87  ? -6.600  28.190  31.809  1.00 38.89  ?  87  TYR A CA  1 
ATOM   646  C C   . TYR A 1 87  ? -6.675  29.293  32.850  1.00 41.35  ?  87  TYR A C   1 
ATOM   647  O O   . TYR A 1 87  ? -6.648  30.483  32.513  1.00 42.02  ?  87  TYR A O   1 
ATOM   648  C CB  . TYR A 1 87  ? -5.123  27.878  31.511  1.00 35.63  ?  87  TYR A CB  1 
ATOM   649  C CG  . TYR A 1 87  ? -4.902  26.702  30.587  1.00 38.88  ?  87  TYR A CG  1 
ATOM   650  C CD1 . TYR A 1 87  ? -4.715  25.417  31.088  1.00 39.48  ?  87  TYR A CD1 1 
ATOM   651  C CD2 . TYR A 1 87  ? -4.878  26.880  29.215  1.00 37.25  ?  87  TYR A CD2 1 
ATOM   652  C CE1 . TYR A 1 87  ? -4.510  24.339  30.232  1.00 43.58  ?  87  TYR A CE1 1 
ATOM   653  C CE2 . TYR A 1 87  ? -4.675  25.823  28.358  1.00 42.28  ?  87  TYR A CE2 1 
ATOM   654  C CZ  . TYR A 1 87  ? -4.492  24.551  28.862  1.00 46.74  ?  87  TYR A CZ  1 
ATOM   655  O OH  . TYR A 1 87  ? -4.299  23.508  27.975  1.00 39.98  ?  87  TYR A OH  1 
ATOM   656  N N   . CYS A 1 88  ? -6.761  28.898  34.113  1.00 38.91  ?  88  CYS A N   1 
ATOM   657  C CA  . CYS A 1 88  ? -6.524  29.828  35.203  1.00 44.45  ?  88  CYS A CA  1 
ATOM   658  C C   . CYS A 1 88  ? -5.108  29.633  35.729  1.00 46.75  ?  88  CYS A C   1 
ATOM   659  O O   . CYS A 1 88  ? -4.526  28.549  35.632  1.00 43.44  ?  88  CYS A O   1 
ATOM   660  C CB  . CYS A 1 88  ? -7.539  29.657  36.342  1.00 44.85  ?  88  CYS A CB  1 
ATOM   661  S SG  . CYS A 1 88  ? -7.738  27.974  36.978  1.00 63.07  ?  88  CYS A SG  1 
ATOM   662  N N   . LEU A 1 89  ? -4.558  30.710  36.280  1.00 42.45  ?  89  LEU A N   1 
ATOM   663  C CA  . LEU A 1 89  ? -3.230  30.714  36.872  1.00 37.64  ?  89  LEU A CA  1 
ATOM   664  C C   . LEU A 1 89  ? -3.326  31.390  38.225  1.00 37.87  ?  89  LEU A C   1 
ATOM   665  O O   . LEU A 1 89  ? -3.645  32.581  38.301  1.00 46.05  ?  89  LEU A O   1 
ATOM   666  C CB  . LEU A 1 89  ? -2.230  31.453  35.989  1.00 36.46  ?  89  LEU A CB  1 
ATOM   667  C CG  . LEU A 1 89  ? -0.844  31.509  36.619  1.00 40.63  ?  89  LEU A CG  1 
ATOM   668  C CD1 . LEU A 1 89  ? -0.189  30.133  36.526  1.00 36.97  ?  89  LEU A CD1 1 
ATOM   669  C CD2 . LEU A 1 89  ? 0.008   32.584  35.958  1.00 41.34  ?  89  LEU A CD2 1 
ATOM   670  N N   . GLY A 1 90  ? -3.054  30.637  39.284  1.00 37.49  ?  90  GLY A N   1 
ATOM   671  C CA  . GLY A 1 90  ? -3.061  31.159  40.632  1.00 37.89  ?  90  GLY A CA  1 
ATOM   672  C C   . GLY A 1 90  ? -1.633  31.261  41.139  1.00 43.56  ?  90  GLY A C   1 
ATOM   673  O O   . GLY A 1 90  ? -0.843  30.324  40.999  1.00 49.74  ?  90  GLY A O   1 
ATOM   674  N N   . ILE A 1 91  ? -1.322  32.407  41.727  1.00 36.62  ?  91  ILE A N   1 
ATOM   675  C CA  . ILE A 1 91  ? -0.013  32.665  42.300  1.00 39.61  ?  91  ILE A CA  1 
ATOM   676  C C   . ILE A 1 91  ? -0.222  32.973  43.774  1.00 44.86  ?  91  ILE A C   1 
ATOM   677  O O   . ILE A 1 91  ? -0.806  34.006  44.127  1.00 46.51  ?  91  ILE A O   1 
ATOM   678  C CB  . ILE A 1 91  ? 0.713   33.808  41.583  1.00 39.58  ?  91  ILE A CB  1 
ATOM   679  C CG1 . ILE A 1 91  ? 0.939   33.442  40.116  1.00 37.71  ?  91  ILE A CG1 1 
ATOM   680  C CG2 . ILE A 1 91  ? 2.018   34.144  42.278  1.00 39.51  ?  91  ILE A CG2 1 
ATOM   681  C CD1 . ILE A 1 91  ? 1.704   34.483  39.350  1.00 39.17  ?  91  ILE A CD1 1 
ATOM   682  N N   . TYR A 1 92  ? 0.248   32.075  44.632  1.00 43.57  ?  92  TYR A N   1 
ATOM   683  C CA  . TYR A 1 92  ? 0.180   32.288  46.068  1.00 45.10  ?  92  TYR A CA  1 
ATOM   684  C C   . TYR A 1 92  ? 1.345   33.161  46.513  1.00 38.41  ?  92  TYR A C   1 
ATOM   685  O O   . TYR A 1 92  ? 2.509   32.841  46.257  1.00 44.42  ?  92  TYR A O   1 
ATOM   686  C CB  . TYR A 1 92  ? 0.198   30.950  46.806  1.00 42.98  ?  92  TYR A CB  1 
ATOM   687  C CG  . TYR A 1 92  ? 0.241   31.076  48.309  1.00 46.55  ?  92  TYR A CG  1 
ATOM   688  C CD1 . TYR A 1 92  ? -0.917  31.308  49.039  1.00 46.80  ?  92  TYR A CD1 1 
ATOM   689  C CD2 . TYR A 1 92  ? 1.439   30.948  49.003  1.00 48.61  ?  92  TYR A CD2 1 
ATOM   690  C CE1 . TYR A 1 92  ? -0.885  31.417  50.416  1.00 46.81  ?  92  TYR A CE1 1 
ATOM   691  C CE2 . TYR A 1 92  ? 1.481   31.056  50.383  1.00 51.42  ?  92  TYR A CE2 1 
ATOM   692  C CZ  . TYR A 1 92  ? 0.315   31.293  51.083  1.00 51.93  ?  92  TYR A CZ  1 
ATOM   693  O OH  . TYR A 1 92  ? 0.352   31.402  52.455  1.00 52.12  ?  92  TYR A OH  1 
ATOM   694  N N   . GLY A 1 93  ? 1.026   34.260  47.187  1.00 39.48  ?  93  GLY A N   1 
ATOM   695  C CA  . GLY A 1 93  ? 2.053   35.197  47.611  1.00 39.43  ?  93  GLY A CA  1 
ATOM   696  C C   . GLY A 1 93  ? 2.873   35.679  46.432  1.00 42.30  ?  93  GLY A C   1 
ATOM   697  O O   . GLY A 1 93  ? 2.344   36.156  45.421  1.00 42.02  ?  93  GLY A O   1 
ATOM   698  N N   . ASP A 1 94  ? 4.193   35.563  46.567  1.00 41.39  ?  94  ASP A N   1 
ATOM   699  C CA  . ASP A 1 94  ? 5.128   35.925  45.513  1.00 39.95  ?  94  ASP A CA  1 
ATOM   700  C C   . ASP A 1 94  ? 5.626   34.702  44.740  1.00 41.96  ?  94  ASP A C   1 
ATOM   701  O O   . ASP A 1 94  ? 6.748   34.703  44.220  1.00 39.41  ?  94  ASP A O   1 
ATOM   702  C CB  . ASP A 1 94  ? 6.299   36.712  46.101  1.00 41.79  ?  94  ASP A CB  1 
ATOM   703  C CG  . ASP A 1 94  ? 7.084   37.455  45.041  1.00 47.00  ?  94  ASP A CG  1 
ATOM   704  O OD1 . ASP A 1 94  ? 6.494   37.754  43.980  1.00 46.73  ?  94  ASP A OD1 1 
ATOM   705  O OD2 . ASP A 1 94  ? 8.296   37.701  45.250  1.00 46.66  ?  94  ASP A OD2 1 
ATOM   706  N N   . GLY A 1 95  ? 4.823   33.640  44.683  1.00 41.51  ?  95  GLY A N   1 
ATOM   707  C CA  . GLY A 1 95  ? 5.137   32.478  43.869  1.00 41.34  ?  95  GLY A CA  1 
ATOM   708  C C   . GLY A 1 95  ? 6.476   31.825  44.136  1.00 42.81  ?  95  GLY A C   1 
ATOM   709  O O   . GLY A 1 95  ? 7.332   31.772  43.251  1.00 43.12  ?  95  GLY A O   1 
ATOM   710  N N   . ALA A 1 96  ? 6.679   31.340  45.355  1.00 45.78  ?  96  ALA A N   1 
ATOM   711  C CA  . ALA A 1 96  ? 7.864   30.569  45.705  1.00 39.06  ?  96  ALA A CA  1 
ATOM   712  C C   . ALA A 1 96  ? 7.596   29.104  45.351  1.00 40.90  ?  96  ALA A C   1 
ATOM   713  O O   . ALA A 1 96  ? 6.682   28.804  44.579  1.00 38.50  ?  96  ALA A O   1 
ATOM   714  C CB  . ALA A 1 96  ? 8.190   30.766  47.189  1.00 35.93  ?  96  ALA A CB  1 
ATOM   715  N N   . ASP A 1 97  ? 8.393   28.183  45.890  1.00 46.40  ?  97  ASP A N   1 
ATOM   716  C CA  . ASP A 1 97  ? 8.288   26.766  45.547  1.00 43.52  ?  97  ASP A CA  1 
ATOM   717  C C   . ASP A 1 97  ? 6.846   26.282  45.638  1.00 46.10  ?  97  ASP A C   1 
ATOM   718  O O   . ASP A 1 97  ? 6.205   26.403  46.688  1.00 46.75  ?  97  ASP A O   1 
ATOM   719  C CB  . ASP A 1 97  ? 9.185   25.936  46.470  1.00 42.47  ?  97  ASP A CB  1 
ATOM   720  C CG  . ASP A 1 97  ? 10.659  26.006  46.084  1.00 50.16  ?  97  ASP A CG  1 
ATOM   721  O OD1 . ASP A 1 97  ? 10.972  26.398  44.938  1.00 50.58  ?  97  ASP A OD1 1 
ATOM   722  O OD2 . ASP A 1 97  ? 11.510  25.665  46.930  1.00 58.74  ?  97  ASP A OD2 1 
ATOM   723  N N   . ASP A 1 98  ? 6.341   25.743  44.523  1.00 43.44  ?  98  ASP A N   1 
ATOM   724  C CA  . ASP A 1 98  ? 4.944   25.310  44.386  1.00 44.64  ?  98  ASP A CA  1 
ATOM   725  C C   . ASP A 1 98  ? 3.954   26.436  44.677  1.00 48.66  ?  98  ASP A C   1 
ATOM   726  O O   . ASP A 1 98  ? 2.817   26.183  45.084  1.00 51.28  ?  98  ASP A O   1 
ATOM   727  C CB  . ASP A 1 98  ? 4.639   24.106  45.280  1.00 48.03  ?  98  ASP A CB  1 
ATOM   728  C CG  . ASP A 1 98  ? 5.526   22.921  44.979  1.00 51.46  ?  98  ASP A CG  1 
ATOM   729  O OD1 . ASP A 1 98  ? 6.365   22.578  45.837  1.00 51.89  ?  98  ASP A OD1 1 
ATOM   730  O OD2 . ASP A 1 98  ? 5.403   22.353  43.873  1.00 51.30  ?  98  ASP A OD2 1 
ATOM   731  N N   . GLY A 1 99  ? 4.362   27.683  44.463  1.00 44.05  ?  99  GLY A N   1 
ATOM   732  C CA  . GLY A 1 99  ? 3.499   28.822  44.670  1.00 42.90  ?  99  GLY A CA  1 
ATOM   733  C C   . GLY A 1 99  ? 2.779   29.315  43.441  1.00 44.14  ?  99  GLY A C   1 
ATOM   734  O O   . GLY A 1 99  ? 2.061   30.317  43.524  1.00 45.16  ?  99  GLY A O   1 
ATOM   735  N N   . ILE A 1 100 ? 2.961   28.658  42.298  1.00 42.97  ?  100 ILE A N   1 
ATOM   736  C CA  . ILE A 1 100 ? 2.323   29.037  41.043  1.00 42.62  ?  100 ILE A CA  1 
ATOM   737  C C   . ILE A 1 100 ? 1.712   27.787  40.433  1.00 46.01  ?  100 ILE A C   1 
ATOM   738  O O   . ILE A 1 100 ? 2.395   26.769  40.277  1.00 44.20  ?  100 ILE A O   1 
ATOM   739  C CB  . ILE A 1 100 ? 3.315   29.678  40.055  1.00 40.32  ?  100 ILE A CB  1 
ATOM   740  C CG1 . ILE A 1 100 ? 3.918   30.954  40.647  1.00 45.07  ?  100 ILE A CG1 1 
ATOM   741  C CG2 . ILE A 1 100 ? 2.637   29.941  38.728  1.00 36.25  ?  100 ILE A CG2 1 
ATOM   742  C CD1 . ILE A 1 100 ? 5.122   31.475  39.882  1.00 41.30  ?  100 ILE A CD1 1 
ATOM   743  N N   . ALA A 1 101 ? 0.433   27.858  40.089  1.00 42.86  ?  101 ALA A N   1 
ATOM   744  C CA  . ALA A 1 101 ? -0.244  26.672  39.597  1.00 42.57  ?  101 ALA A CA  1 
ATOM   745  C C   . ALA A 1 101 ? -1.245  27.064  38.528  1.00 45.59  ?  101 ALA A C   1 
ATOM   746  O O   . ALA A 1 101 ? -2.041  27.986  38.725  1.00 42.23  ?  101 ALA A O   1 
ATOM   747  C CB  . ALA A 1 101 ? -0.942  25.926  40.736  1.00 46.21  ?  101 ALA A CB  1 
ATOM   748  N N   . PHE A 1 102 ? -1.180  26.379  37.393  1.00 44.21  ?  102 PHE A N   1 
ATOM   749  C CA  . PHE A 1 102 ? -2.221  26.486  36.387  1.00 41.42  ?  102 PHE A CA  1 
ATOM   750  C C   . PHE A 1 102 ? -3.359  25.531  36.724  1.00 46.25  ?  102 PHE A C   1 
ATOM   751  O O   . PHE A 1 102 ? -3.141  24.437  37.253  1.00 49.37  ?  102 PHE A O   1 
ATOM   752  C CB  . PHE A 1 102 ? -1.679  26.131  35.002  1.00 39.76  ?  102 PHE A CB  1 
ATOM   753  C CG  . PHE A 1 102 ? -0.859  27.210  34.360  1.00 41.91  ?  102 PHE A CG  1 
ATOM   754  C CD1 . PHE A 1 102 ? -1.461  28.205  33.604  1.00 42.81  ?  102 PHE A CD1 1 
ATOM   755  C CD2 . PHE A 1 102 ? 0.521   27.207  34.479  1.00 34.62  ?  102 PHE A CD2 1 
ATOM   756  C CE1 . PHE A 1 102 ? -0.703  29.185  32.995  1.00 41.46  ?  102 PHE A CE1 1 
ATOM   757  C CE2 . PHE A 1 102 ? 1.281   28.182  33.872  1.00 35.77  ?  102 PHE A CE2 1 
ATOM   758  C CZ  . PHE A 1 102 ? 0.670   29.175  33.129  1.00 39.60  ?  102 PHE A CZ  1 
ATOM   759  N N   . GLY A 1 103 ? -4.578  25.942  36.394  1.00 44.09  ?  103 GLY A N   1 
ATOM   760  C CA  . GLY A 1 103 ? -5.691  25.020  36.424  1.00 38.32  ?  103 GLY A CA  1 
ATOM   761  C C   . GLY A 1 103 ? -5.628  24.058  35.251  1.00 44.73  ?  103 GLY A C   1 
ATOM   762  O O   . GLY A 1 103 ? -4.872  24.235  34.293  1.00 44.35  ?  103 GLY A O   1 
ATOM   763  N N   . GLY A 1 104 ? -6.464  23.021  35.322  1.00 41.59  ?  104 GLY A N   1 
ATOM   764  C CA  . GLY A 1 104 ? -6.433  21.959  34.331  1.00 32.53  ?  104 GLY A CA  1 
ATOM   765  C C   . GLY A 1 104 ? -6.854  22.376  32.936  1.00 38.49  ?  104 GLY A C   1 
ATOM   766  O O   . GLY A 1 104 ? -6.563  21.660  31.972  1.00 33.01  ?  104 GLY A O   1 
ATOM   767  N N   . GLY A 1 105 ? -7.553  23.493  32.802  1.00 40.94  ?  105 GLY A N   1 
ATOM   768  C CA  . GLY A 1 105 ? -7.982  23.913  31.487  1.00 43.77  ?  105 GLY A CA  1 
ATOM   769  C C   . GLY A 1 105 ? -9.426  23.527  31.192  1.00 46.88  ?  105 GLY A C   1 
ATOM   770  O O   . GLY A 1 105 ? -9.999  22.607  31.787  1.00 41.97  ?  105 GLY A O   1 
ATOM   771  N N   . THR A 1 106 ? -10.019 24.254  30.248  1.00 43.03  ?  106 THR A N   1 
ATOM   772  C CA  . THR A 1 106 ? -11.385 24.007  29.808  1.00 44.93  ?  106 THR A CA  1 
ATOM   773  C C   . THR A 1 106 ? -11.436 24.197  28.302  1.00 42.48  ?  106 THR A C   1 
ATOM   774  O O   . THR A 1 106 ? -11.153 25.293  27.809  1.00 38.99  ?  106 THR A O   1 
ATOM   775  C CB  . THR A 1 106 ? -12.380 24.951  30.495  1.00 45.44  ?  106 THR A CB  1 
ATOM   776  O OG1 . THR A 1 106 ? -12.404 24.695  31.905  1.00 44.19  ?  106 THR A OG1 1 
ATOM   777  C CG2 . THR A 1 106 ? -13.770 24.741  29.923  1.00 43.32  ?  106 THR A CG2 1 
ATOM   778  N N   . LYS A 1 107 ? -11.751 23.130  27.574  1.00 41.19  ?  107 LYS A N   1 
ATOM   779  C CA  . LYS A 1 107 ? -11.944 23.239  26.135  1.00 39.30  ?  107 LYS A CA  1 
ATOM   780  C C   . LYS A 1 107 ? -13.332 23.797  25.851  1.00 42.43  ?  107 LYS A C   1 
ATOM   781  O O   . LYS A 1 107 ? -14.326 23.326  26.412  1.00 44.52  ?  107 LYS A O   1 
ATOM   782  C CB  . LYS A 1 107 ? -11.752 21.884  25.452  1.00 44.42  ?  107 LYS A CB  1 
ATOM   783  C CG  . LYS A 1 107 ? -10.381 21.249  25.692  1.00 53.69  ?  107 LYS A CG  1 
ATOM   784  C CD  . LYS A 1 107 ? -10.204 19.965  24.886  1.00 50.03  ?  107 LYS A CD  1 
ATOM   785  C CE  . LYS A 1 107 ? -8.876  19.286  25.200  1.00 56.51  ?  107 LYS A CE  1 
ATOM   786  N NZ  . LYS A 1 107 ? -8.958  18.403  26.403  1.00 54.54  ?  107 LYS A NZ  1 
ATOM   787  N N   . VAL A 1 108 ? -13.392 24.824  25.007  1.00 44.65  ?  108 VAL A N   1 
ATOM   788  C CA  . VAL A 1 108 ? -14.630 25.506  24.652  1.00 45.00  ?  108 VAL A CA  1 
ATOM   789  C C   . VAL A 1 108 ? -14.816 25.369  23.148  1.00 45.25  ?  108 VAL A C   1 
ATOM   790  O O   . VAL A 1 108 ? -14.015 25.904  22.359  1.00 50.63  ?  108 VAL A O   1 
ATOM   791  C CB  . VAL A 1 108 ? -14.616 26.981  25.075  1.00 42.62  ?  108 VAL A CB  1 
ATOM   792  C CG1 . VAL A 1 108 ? -15.785 27.723  24.451  1.00 42.61  ?  108 VAL A CG1 1 
ATOM   793  C CG2 . VAL A 1 108 ? -14.648 27.090  26.591  1.00 43.62  ?  108 VAL A CG2 1 
ATOM   794  N N   . GLU A 1 109 ? -15.869 24.645  22.764  1.00 44.90  ?  109 GLU A N   1 
ATOM   795  C CA  . GLU A 1 109 ? -16.261 24.395  21.384  1.00 54.18  ?  109 GLU A CA  1 
ATOM   796  C C   . GLU A 1 109 ? -17.604 25.064  21.101  1.00 51.56  ?  109 GLU A C   1 
ATOM   797  O O   . GLU A 1 109 ? -18.505 25.044  21.946  1.00 47.21  ?  109 GLU A O   1 
ATOM   798  C CB  . GLU A 1 109 ? -16.382 22.891  21.116  1.00 53.24  ?  109 GLU A CB  1 
ATOM   799  C CG  . GLU A 1 109 ? -17.012 22.562  19.771  1.00 58.47  ?  109 GLU A CG  1 
ATOM   800  C CD  . GLU A 1 109 ? -17.771 21.257  19.767  1.00 61.51  ?  109 GLU A CD  1 
ATOM   801  O OE1 . GLU A 1 109 ? -17.350 20.326  19.041  1.00 62.66  ?  109 GLU A OE1 1 
ATOM   802  O OE2 . GLU A 1 109 ? -18.778 21.159  20.506  1.00 59.05  ?  109 GLU A OE2 1 
ATOM   803  N N   . ILE A 1 110 ? -17.743 25.641  19.910  1.00 50.52  ?  110 ILE A N   1 
ATOM   804  C CA  . ILE A 1 110 ? -18.981 26.310  19.524  1.00 50.11  ?  110 ILE A CA  1 
ATOM   805  C C   . ILE A 1 110 ? -19.959 25.283  18.959  1.00 52.58  ?  110 ILE A C   1 
ATOM   806  O O   . ILE A 1 110 ? -19.612 24.498  18.071  1.00 49.81  ?  110 ILE A O   1 
ATOM   807  C CB  . ILE A 1 110 ? -18.704 27.428  18.506  1.00 51.29  ?  110 ILE A CB  1 
ATOM   808  C CG1 . ILE A 1 110 ? -18.151 28.676  19.194  1.00 54.07  ?  110 ILE A CG1 1 
ATOM   809  C CG2 . ILE A 1 110 ? -19.975 27.795  17.759  1.00 49.84  ?  110 ILE A CG2 1 
ATOM   810  C CD1 . ILE A 1 110 ? -16.709 28.576  19.593  1.00 52.03  ?  110 ILE A CD1 1 
ATOM   811  N N   . LYS A 1 111 ? -21.193 25.298  19.463  1.00 59.22  ?  111 LYS A N   1 
ATOM   812  C CA  . LYS A 1 111 ? -22.268 24.449  18.951  1.00 55.54  ?  111 LYS A CA  1 
ATOM   813  C C   . LYS A 1 111 ? -22.962 25.180  17.807  1.00 55.80  ?  111 LYS A C   1 
ATOM   814  O O   . LYS A 1 111 ? -23.576 26.232  18.015  1.00 53.78  ?  111 LYS A O   1 
ATOM   815  C CB  . LYS A 1 111 ? -23.265 24.113  20.057  1.00 53.62  ?  111 LYS A CB  1 
ATOM   816  C CG  . LYS A 1 111 ? -24.359 23.141  19.649  1.00 57.79  ?  111 LYS A CG  1 
ATOM   817  C CD  . LYS A 1 111 ? -25.346 22.911  20.791  1.00 62.14  ?  111 LYS A CD  1 
ATOM   818  C CE  . LYS A 1 111 ? -24.684 22.226  21.977  1.00 64.77  ?  111 LYS A CE  1 
ATOM   819  N NZ  . LYS A 1 111 ? -25.637 21.962  23.093  1.00 67.92  ?  111 LYS A NZ  1 
ATOM   820  N N   . ARG A 1 112 ? -22.858 24.634  16.603  1.00 56.21  ?  112 ARG A N   1 
ATOM   821  C CA  . ARG A 1 112 ? -23.506 25.200  15.429  1.00 51.15  ?  112 ARG A CA  1 
ATOM   822  C C   . ARG A 1 112 ? -24.488 24.182  14.858  1.00 56.78  ?  112 ARG A C   1 
ATOM   823  O O   . ARG A 1 112 ? -24.732 23.125  15.447  1.00 61.34  ?  112 ARG A O   1 
ATOM   824  C CB  . ARG A 1 112 ? -22.467 25.621  14.392  1.00 48.46  ?  112 ARG A CB  1 
ATOM   825  C CG  . ARG A 1 112 ? -21.630 24.476  13.868  1.00 50.90  ?  112 ARG A CG  1 
ATOM   826  C CD  . ARG A 1 112 ? -21.094 24.793  12.485  1.00 52.30  ?  112 ARG A CD  1 
ATOM   827  N NE  . ARG A 1 112 ? -22.068 24.542  11.426  1.00 52.55  ?  112 ARG A NE  1 
ATOM   828  C CZ  . ARG A 1 112 ? -21.952 25.003  10.184  1.00 48.85  ?  112 ARG A CZ  1 
ATOM   829  N NH1 . ARG A 1 112 ? -22.878 24.725  9.282   1.00 48.88  ?  112 ARG A NH1 1 
ATOM   830  N NH2 . ARG A 1 112 ? -20.914 25.754  9.846   1.00 54.03  ?  112 ARG A NH2 1 
ATOM   831  N N   . THR A 1 113 ? -25.049 24.506  13.697  1.00 57.76  ?  113 THR A N   1 
ATOM   832  C CA  . THR A 1 113 ? -25.981 23.602  13.039  1.00 60.33  ?  113 THR A CA  1 
ATOM   833  C C   . THR A 1 113 ? -25.247 22.400  12.447  1.00 61.58  ?  113 THR A C   1 
ATOM   834  O O   . THR A 1 113 ? -24.067 22.479  12.091  1.00 62.54  ?  113 THR A O   1 
ATOM   835  C CB  . THR A 1 113 ? -26.746 24.341  11.946  1.00 61.31  ?  113 THR A CB  1 
ATOM   836  O OG1 . THR A 1 113 ? -25.838 24.730  10.909  1.00 63.80  ?  113 THR A OG1 1 
ATOM   837  C CG2 . THR A 1 113 ? -27.413 25.580  12.519  1.00 55.52  ?  113 THR A CG2 1 
ATOM   838  N N   . VAL A 1 114 ? -25.965 21.274  12.345  1.00 59.01  ?  114 VAL A N   1 
ATOM   839  C CA  . VAL A 1 114 ? -25.379 20.054  11.797  1.00 53.98  ?  114 VAL A CA  1 
ATOM   840  C C   . VAL A 1 114 ? -24.998 20.274  10.340  1.00 56.53  ?  114 VAL A C   1 
ATOM   841  O O   . VAL A 1 114 ? -25.788 20.798  9.545   1.00 62.88  ?  114 VAL A O   1 
ATOM   842  C CB  . VAL A 1 114 ? -26.352 18.876  11.951  1.00 54.18  ?  114 VAL A CB  1 
ATOM   843  C CG1 . VAL A 1 114 ? -25.877 17.689  11.129  1.00 54.57  ?  114 VAL A CG1 1 
ATOM   844  C CG2 . VAL A 1 114 ? -26.480 18.478  13.416  1.00 52.13  ?  114 VAL A CG2 1 
ATOM   845  N N   . ALA A 1 115 ? -23.779 19.870  9.983   1.00 48.61  ?  115 ALA A N   1 
ATOM   846  C CA  . ALA A 1 115 ? -23.278 19.986  8.620   1.00 52.88  ?  115 ALA A CA  1 
ATOM   847  C C   . ALA A 1 115 ? -22.770 18.630  8.159   1.00 53.87  ?  115 ALA A C   1 
ATOM   848  O O   . ALA A 1 115 ? -22.011 17.972  8.878   1.00 51.18  ?  115 ALA A O   1 
ATOM   849  C CB  . ALA A 1 115 ? -22.157 21.029  8.519   1.00 49.86  ?  115 ALA A CB  1 
ATOM   850  N N   . ALA A 1 116 ? -23.192 18.214  6.967   1.00 54.24  ?  116 ALA A N   1 
ATOM   851  C CA  . ALA A 1 116 ? -22.715 16.950  6.426   1.00 47.98  ?  116 ALA A CA  1 
ATOM   852  C C   . ALA A 1 116 ? -21.331 17.141  5.810   1.00 48.81  ?  116 ALA A C   1 
ATOM   853  O O   . ALA A 1 116 ? -21.065 18.173  5.186   1.00 48.37  ?  116 ALA A O   1 
ATOM   854  C CB  . ALA A 1 116 ? -23.680 16.409  5.375   1.00 42.66  ?  116 ALA A CB  1 
ATOM   855  N N   . PRO A 1 117 ? -20.430 16.179  5.990   1.00 51.36  ?  117 PRO A N   1 
ATOM   856  C CA  . PRO A 1 117 ? -19.071 16.339  5.465   1.00 52.53  ?  117 PRO A CA  1 
ATOM   857  C C   . PRO A 1 117 ? -19.031 16.151  3.961   1.00 55.62  ?  117 PRO A C   1 
ATOM   858  O O   . PRO A 1 117 ? -19.868 15.461  3.373   1.00 56.23  ?  117 PRO A O   1 
ATOM   859  C CB  . PRO A 1 117 ? -18.288 15.228  6.173   1.00 49.96  ?  117 PRO A CB  1 
ATOM   860  C CG  . PRO A 1 117 ? -19.320 14.173  6.437   1.00 42.82  ?  117 PRO A CG  1 
ATOM   861  C CD  . PRO A 1 117 ? -20.590 14.922  6.742   1.00 49.27  ?  117 PRO A CD  1 
ATOM   862  N N   . SER A 1 118 ? -18.030 16.764  3.338   1.00 54.43  ?  118 SER A N   1 
ATOM   863  C CA  . SER A 1 118 ? -17.685 16.450  1.957   1.00 52.94  ?  118 SER A CA  1 
ATOM   864  C C   . SER A 1 118 ? -16.629 15.352  1.978   1.00 53.85  ?  118 SER A C   1 
ATOM   865  O O   . SER A 1 118 ? -15.557 15.537  2.560   1.00 52.78  ?  118 SER A O   1 
ATOM   866  C CB  . SER A 1 118 ? -17.173 17.690  1.228   1.00 52.46  ?  118 SER A CB  1 
ATOM   867  O OG  . SER A 1 118 ? -18.253 18.490  0.784   1.00 62.99  ?  118 SER A OG  1 
ATOM   868  N N   . VAL A 1 119 ? -16.933 14.208  1.370   1.00 49.94  ?  119 VAL A N   1 
ATOM   869  C CA  . VAL A 1 119 ? -16.092 13.022  1.491   1.00 50.44  ?  119 VAL A CA  1 
ATOM   870  C C   . VAL A 1 119 ? -15.364 12.791  0.175   1.00 51.14  ?  119 VAL A C   1 
ATOM   871  O O   . VAL A 1 119 ? -15.996 12.605  -0.872  1.00 52.87  ?  119 VAL A O   1 
ATOM   872  C CB  . VAL A 1 119 ? -16.906 11.787  1.887   1.00 45.60  ?  119 VAL A CB  1 
ATOM   873  C CG1 . VAL A 1 119 ? -15.982 10.593  2.041   1.00 45.58  ?  119 VAL A CG1 1 
ATOM   874  C CG2 . VAL A 1 119 ? -17.666 12.059  3.166   1.00 44.24  ?  119 VAL A CG2 1 
ATOM   875  N N   . PHE A 1 120 ? -14.036 12.796  0.237   1.00 49.13  ?  120 PHE A N   1 
ATOM   876  C CA  . PHE A 1 120 ? -13.183 12.489  -0.900  1.00 49.42  ?  120 PHE A CA  1 
ATOM   877  C C   . PHE A 1 120 ? -12.334 11.277  -0.557  1.00 49.50  ?  120 PHE A C   1 
ATOM   878  O O   . PHE A 1 120 ? -11.989 11.059  0.605   1.00 50.76  ?  120 PHE A O   1 
ATOM   879  C CB  . PHE A 1 120 ? -12.266 13.662  -1.258  1.00 51.46  ?  120 PHE A CB  1 
ATOM   880  C CG  . PHE A 1 120 ? -12.981 14.970  -1.444  1.00 44.71  ?  120 PHE A CG  1 
ATOM   881  C CD1 . PHE A 1 120 ? -13.258 15.445  -2.713  1.00 49.50  ?  120 PHE A CD1 1 
ATOM   882  C CD2 . PHE A 1 120 ? -13.360 15.736  -0.348  1.00 49.96  ?  120 PHE A CD2 1 
ATOM   883  C CE1 . PHE A 1 120 ? -13.908 16.655  -2.887  1.00 57.42  ?  120 PHE A CE1 1 
ATOM   884  C CE2 . PHE A 1 120 ? -14.009 16.950  -0.515  1.00 46.88  ?  120 PHE A CE2 1 
ATOM   885  C CZ  . PHE A 1 120 ? -14.281 17.410  -1.786  1.00 48.56  ?  120 PHE A CZ  1 
ATOM   886  N N   . ILE A 1 121 ? -11.986 10.491  -1.572  1.00 53.16  ?  121 ILE A N   1 
ATOM   887  C CA  . ILE A 1 121 ? -11.148 9.313   -1.378  1.00 43.92  ?  121 ILE A CA  1 
ATOM   888  C C   . ILE A 1 121 ? -10.003 9.349   -2.384  1.00 46.12  ?  121 ILE A C   1 
ATOM   889  O O   . ILE A 1 121 ? -10.224 9.543   -3.585  1.00 48.59  ?  121 ILE A O   1 
ATOM   890  C CB  . ILE A 1 121 ? -11.961 8.005   -1.488  1.00 50.96  ?  121 ILE A CB  1 
ATOM   891  C CG1 . ILE A 1 121 ? -11.084 6.792   -1.176  1.00 51.61  ?  121 ILE A CG1 1 
ATOM   892  C CG2 . ILE A 1 121 ? -12.647 7.869   -2.849  1.00 50.23  ?  121 ILE A CG2 1 
ATOM   893  C CD1 . ILE A 1 121 ? -11.875 5.589   -0.709  1.00 46.33  ?  121 ILE A CD1 1 
ATOM   894  N N   . PHE A 1 122 ? -8.777  9.180   -1.881  1.00 47.75  ?  122 PHE A N   1 
ATOM   895  C CA  . PHE A 1 122 ? -7.552  9.209   -2.667  1.00 45.11  ?  122 PHE A CA  1 
ATOM   896  C C   . PHE A 1 122 ? -6.935  7.817   -2.693  1.00 46.64  ?  122 PHE A C   1 
ATOM   897  O O   . PHE A 1 122 ? -6.581  7.284   -1.624  1.00 44.82  ?  122 PHE A O   1 
ATOM   898  C CB  . PHE A 1 122 ? -6.549  10.202  -2.075  1.00 45.15  ?  122 PHE A CB  1 
ATOM   899  C CG  . PHE A 1 122 ? -6.986  11.636  -2.117  1.00 43.83  ?  122 PHE A CG  1 
ATOM   900  C CD1 . PHE A 1 122 ? -6.750  12.415  -3.233  1.00 46.75  ?  122 PHE A CD1 1 
ATOM   901  C CD2 . PHE A 1 122 ? -7.584  12.218  -1.018  1.00 42.93  ?  122 PHE A CD2 1 
ATOM   902  C CE1 . PHE A 1 122 ? -7.136  13.737  -3.262  1.00 49.57  ?  122 PHE A CE1 1 
ATOM   903  C CE2 . PHE A 1 122 ? -7.969  13.540  -1.040  1.00 46.75  ?  122 PHE A CE2 1 
ATOM   904  C CZ  . PHE A 1 122 ? -7.746  14.301  -2.162  1.00 46.51  ?  122 PHE A CZ  1 
ATOM   905  N N   . PRO A 1 123 ? -6.781  7.201   -3.863  1.00 43.84  ?  123 PRO A N   1 
ATOM   906  C CA  . PRO A 1 123 ? -6.016  5.955   -3.952  1.00 43.87  ?  123 PRO A CA  1 
ATOM   907  C C   . PRO A 1 123 ? -4.541  6.237   -3.737  1.00 43.43  ?  123 PRO A C   1 
ATOM   908  O O   . PRO A 1 123 ? -4.108  7.397   -3.805  1.00 47.00  ?  123 PRO A O   1 
ATOM   909  C CB  . PRO A 1 123 ? -6.288  5.467   -5.387  1.00 41.28  ?  123 PRO A CB  1 
ATOM   910  C CG  . PRO A 1 123 ? -7.442  6.274   -5.874  1.00 46.18  ?  123 PRO A CG  1 
ATOM   911  C CD  . PRO A 1 123 ? -7.337  7.593   -5.167  1.00 39.92  ?  123 PRO A CD  1 
ATOM   912  N N   . PRO A 1 124 ? -3.739  5.217   -3.460  1.00 43.74  ?  124 PRO A N   1 
ATOM   913  C CA  . PRO A 1 124 ? -2.304  5.451   -3.302  1.00 44.05  ?  124 PRO A CA  1 
ATOM   914  C C   . PRO A 1 124 ? -1.677  5.899   -4.608  1.00 46.94  ?  124 PRO A C   1 
ATOM   915  O O   . PRO A 1 124 ? -2.139  5.550   -5.697  1.00 47.78  ?  124 PRO A O   1 
ATOM   916  C CB  . PRO A 1 124 ? -1.765  4.083   -2.869  1.00 47.09  ?  124 PRO A CB  1 
ATOM   917  C CG  . PRO A 1 124 ? -2.761  3.112   -3.364  1.00 45.21  ?  124 PRO A CG  1 
ATOM   918  C CD  . PRO A 1 124 ? -4.087  3.800   -3.265  1.00 44.80  ?  124 PRO A CD  1 
ATOM   919  N N   . SER A 1 125 ? -0.624  6.701   -4.485  1.00 46.52  ?  125 SER A N   1 
ATOM   920  C CA  . SER A 1 125 ? 0.134   7.133   -5.645  1.00 46.20  ?  125 SER A CA  1 
ATOM   921  C C   . SER A 1 125 ? 1.049   6.015   -6.135  1.00 52.90  ?  125 SER A C   1 
ATOM   922  O O   . SER A 1 125 ? 1.361   5.066   -5.408  1.00 54.99  ?  125 SER A O   1 
ATOM   923  C CB  . SER A 1 125 ? 0.970   8.362   -5.310  1.00 47.20  ?  125 SER A CB  1 
ATOM   924  O OG  . SER A 1 125 ? 2.077   7.992   -4.515  1.00 48.56  ?  125 SER A OG  1 
ATOM   925  N N   . ASP A 1 126 ? 1.489   6.140   -7.390  1.00 57.02  ?  126 ASP A N   1 
ATOM   926  C CA  . ASP A 1 126 ? 2.401   5.139   -7.935  1.00 58.89  ?  126 ASP A CA  1 
ATOM   927  C C   . ASP A 1 126 ? 3.761   5.196   -7.264  1.00 61.54  ?  126 ASP A C   1 
ATOM   928  O O   . ASP A 1 126 ? 4.413   4.161   -7.116  1.00 63.17  ?  126 ASP A O   1 
ATOM   929  C CB  . ASP A 1 126 ? 2.557   5.298   -9.446  1.00 62.11  ?  126 ASP A CB  1 
ATOM   930  C CG  . ASP A 1 126 ? 1.443   4.628   -10.218 1.00 74.81  ?  126 ASP A CG  1 
ATOM   931  O OD1 . ASP A 1 126 ? 0.427   4.251   -9.598  1.00 80.94  ?  126 ASP A OD1 1 
ATOM   932  O OD2 . ASP A 1 126 ? 1.594   4.465   -11.450 1.00 79.09  ?  126 ASP A OD2 1 
ATOM   933  N N   . GLU A 1 127 ? 4.210   6.386   -6.868  1.00 57.06  ?  127 GLU A N   1 
ATOM   934  C CA  . GLU A 1 127 ? 5.491   6.497   -6.176  1.00 62.14  ?  127 GLU A CA  1 
ATOM   935  C C   . GLU A 1 127 ? 5.501   5.646   -4.911  1.00 62.31  ?  127 GLU A C   1 
ATOM   936  O O   . GLU A 1 127 ? 6.406   4.822   -4.700  1.00 63.76  ?  127 GLU A O   1 
ATOM   937  C CB  . GLU A 1 127 ? 5.779   7.965   -5.862  1.00 62.74  ?  127 GLU A CB  1 
ATOM   938  C CG  . GLU A 1 127 ? 5.075   8.924   -6.824  1.00 67.01  ?  127 GLU A CG  1 
ATOM   939  C CD  . GLU A 1 127 ? 5.421   10.381  -6.576  1.00 70.29  ?  127 GLU A CD  1 
ATOM   940  O OE1 . GLU A 1 127 ? 4.907   11.248  -7.317  1.00 77.03  ?  127 GLU A OE1 1 
ATOM   941  O OE2 . GLU A 1 127 ? 6.206   10.660  -5.642  1.00 66.67  ?  127 GLU A OE2 1 
ATOM   942  N N   . GLN A 1 128 ? 4.485   5.819   -4.060  1.00 58.36  ?  128 GLN A N   1 
ATOM   943  C CA  . GLN A 1 128 ? 4.414   5.026   -2.840  1.00 54.51  ?  128 GLN A CA  1 
ATOM   944  C C   . GLN A 1 128 ? 4.258   3.543   -3.149  1.00 56.00  ?  128 GLN A C   1 
ATOM   945  O O   . GLN A 1 128 ? 4.810   2.698   -2.434  1.00 54.68  ?  128 GLN A O   1 
ATOM   946  C CB  . GLN A 1 128 ? 3.271   5.522   -1.958  1.00 44.92  ?  128 GLN A CB  1 
ATOM   947  C CG  . GLN A 1 128 ? 3.353   5.019   -0.536  1.00 45.80  ?  128 GLN A CG  1 
ATOM   948  C CD  . GLN A 1 128 ? 2.030   5.094   0.195   1.00 49.86  ?  128 GLN A CD  1 
ATOM   949  O OE1 . GLN A 1 128 ? 1.038   5.600   -0.334  1.00 47.17  ?  128 GLN A OE1 1 
ATOM   950  N NE2 . GLN A 1 128 ? 2.007   4.582   1.419   1.00 51.39  ?  128 GLN A NE2 1 
ATOM   951  N N   . LEU A 1 129 ? 3.543   3.209   -4.225  1.00 53.94  ?  129 LEU A N   1 
ATOM   952  C CA  . LEU A 1 129 ? 3.397   1.809   -4.603  1.00 58.33  ?  129 LEU A CA  1 
ATOM   953  C C   . LEU A 1 129 ? 4.740   1.207   -4.998  1.00 66.63  ?  129 LEU A C   1 
ATOM   954  O O   . LEU A 1 129 ? 5.030   0.049   -4.669  1.00 66.19  ?  129 LEU A O   1 
ATOM   955  C CB  . LEU A 1 129 ? 2.377   1.684   -5.731  1.00 56.94  ?  129 LEU A CB  1 
ATOM   956  C CG  . LEU A 1 129 ? 0.954   1.414   -5.239  1.00 54.49  ?  129 LEU A CG  1 
ATOM   957  C CD1 . LEU A 1 129 ? 0.007   1.106   -6.391  1.00 48.28  ?  129 LEU A CD1 1 
ATOM   958  C CD2 . LEU A 1 129 ? 0.958   0.281   -4.230  1.00 50.35  ?  129 LEU A CD2 1 
ATOM   959  N N   . LYS A 1 130 ? 5.565   1.973   -5.723  1.00 67.81  ?  130 LYS A N   1 
ATOM   960  C CA  . LYS A 1 130 ? 6.943   1.563   -5.984  1.00 64.69  ?  130 LYS A CA  1 
ATOM   961  C C   . LYS A 1 130 ? 7.694   1.319   -4.682  1.00 62.16  ?  130 LYS A C   1 
ATOM   962  O O   . LYS A 1 130 ? 8.418   0.325   -4.552  1.00 63.74  ?  130 LYS A O   1 
ATOM   963  C CB  . LYS A 1 130 ? 7.675   2.623   -6.813  1.00 65.04  ?  130 LYS A CB  1 
ATOM   964  C CG  . LYS A 1 130 ? 7.109   2.888   -8.202  1.00 65.98  ?  130 LYS A CG  1 
ATOM   965  C CD  . LYS A 1 130 ? 7.817   4.081   -8.847  1.00 65.66  ?  130 LYS A CD  1 
ATOM   966  C CE  . LYS A 1 130 ? 7.398   4.283   -10.298 1.00 69.85  ?  130 LYS A CE  1 
ATOM   967  N NZ  . LYS A 1 130 ? 6.538   5.487   -10.466 1.00 74.65  ?  130 LYS A NZ  1 
ATOM   968  N N   . SER A 1 131 ? 7.529   2.216   -3.705  1.00 60.84  ?  131 SER A N   1 
ATOM   969  C CA  . SER A 1 131 ? 8.144   1.998   -2.396  1.00 59.38  ?  131 SER A CA  1 
ATOM   970  C C   . SER A 1 131 ? 7.748   0.653   -1.796  1.00 62.81  ?  131 SER A C   1 
ATOM   971  O O   . SER A 1 131 ? 8.477   0.111   -0.960  1.00 64.27  ?  131 SER A O   1 
ATOM   972  C CB  . SER A 1 131 ? 7.764   3.127   -1.438  1.00 63.52  ?  131 SER A CB  1 
ATOM   973  O OG  . SER A 1 131 ? 8.270   4.368   -1.893  1.00 71.02  ?  131 SER A OG  1 
ATOM   974  N N   . GLY A 1 132 ? 6.598   0.112   -2.188  1.00 60.93  ?  132 GLY A N   1 
ATOM   975  C CA  . GLY A 1 132 ? 6.113   -1.152  -1.677  1.00 57.52  ?  132 GLY A CA  1 
ATOM   976  C C   . GLY A 1 132 ? 5.053   -1.058  -0.605  1.00 53.82  ?  132 GLY A C   1 
ATOM   977  O O   . GLY A 1 132 ? 4.732   -2.077  0.015   1.00 50.52  ?  132 GLY A O   1 
ATOM   978  N N   . THR A 1 133 ? 4.487   0.121   -0.380  1.00 57.09  ?  133 THR A N   1 
ATOM   979  C CA  . THR A 1 133 ? 3.428   0.310   0.597   1.00 56.67  ?  133 THR A CA  1 
ATOM   980  C C   . THR A 1 133 ? 2.293   1.087   -0.060  1.00 53.49  ?  133 THR A C   1 
ATOM   981  O O   . THR A 1 133 ? 2.507   1.830   -1.021  1.00 52.27  ?  133 THR A O   1 
ATOM   982  C CB  . THR A 1 133 ? 3.959   1.028   1.855   1.00 54.07  ?  133 THR A CB  1 
ATOM   983  O OG1 . THR A 1 133 ? 2.892   1.228   2.789   1.00 60.93  ?  133 THR A OG1 1 
ATOM   984  C CG2 . THR A 1 133 ? 4.597   2.367   1.492   1.00 59.62  ?  133 THR A CG2 1 
ATOM   985  N N   . ALA A 1 134 ? 1.071   0.876   0.426   1.00 52.78  ?  134 ALA A N   1 
ATOM   986  C CA  . ALA A 1 134 ? -0.115  1.489   -0.161  1.00 52.28  ?  134 ALA A CA  1 
ATOM   987  C C   . ALA A 1 134 ? -0.900  2.206   0.924   1.00 48.09  ?  134 ALA A C   1 
ATOM   988  O O   . ALA A 1 134 ? -1.397  1.567   1.856   1.00 48.60  ?  134 ALA A O   1 
ATOM   989  C CB  . ALA A 1 134 ? -0.992  0.444   -0.855  1.00 45.64  ?  134 ALA A CB  1 
ATOM   990  N N   . SER A 1 135 ? -1.005  3.525   0.806   1.00 44.16  ?  135 SER A N   1 
ATOM   991  C CA  . SER A 1 135 ? -1.806  4.338   1.711   1.00 44.71  ?  135 SER A CA  1 
ATOM   992  C C   . SER A 1 135 ? -2.991  4.904   0.937   1.00 43.83  ?  135 SER A C   1 
ATOM   993  O O   . SER A 1 135 ? -2.802  5.625   -0.048  1.00 45.79  ?  135 SER A O   1 
ATOM   994  C CB  . SER A 1 135 ? -0.971  5.466   2.317   1.00 47.81  ?  135 SER A CB  1 
ATOM   995  O OG  . SER A 1 135 ? -0.005  4.973   3.229   1.00 48.01  ?  135 SER A OG  1 
ATOM   996  N N   . VAL A 1 136 ? -4.203  4.565   1.369   1.00 38.95  ?  136 VAL A N   1 
ATOM   997  C CA  . VAL A 1 136 ? -5.434  5.118   0.806   1.00 40.31  ?  136 VAL A CA  1 
ATOM   998  C C   . VAL A 1 136 ? -6.051  6.062   1.831   1.00 37.05  ?  136 VAL A C   1 
ATOM   999  O O   . VAL A 1 136 ? -6.156  5.720   3.018   1.00 33.65  ?  136 VAL A O   1 
ATOM   1000 C CB  . VAL A 1 136 ? -6.411  4.004   0.384   1.00 42.08  ?  136 VAL A CB  1 
ATOM   1001 C CG1 . VAL A 1 136 ? -6.586  3.025   1.495   1.00 46.34  ?  136 VAL A CG1 1 
ATOM   1002 C CG2 . VAL A 1 136 ? -7.761  4.592   0.016   1.00 42.05  ?  136 VAL A CG2 1 
ATOM   1003 N N   . VAL A 1 137 ? -6.446  7.256   1.378   1.00 41.35  ?  137 VAL A N   1 
ATOM   1004 C CA  . VAL A 1 137 ? -6.785  8.356   2.278   1.00 42.17  ?  137 VAL A CA  1 
ATOM   1005 C C   . VAL A 1 137 ? -8.238  8.781   2.075   1.00 42.00  ?  137 VAL A C   1 
ATOM   1006 O O   . VAL A 1 137 ? -8.683  9.008   0.946   1.00 41.19  ?  137 VAL A O   1 
ATOM   1007 C CB  . VAL A 1 137 ? -5.831  9.550   2.090   1.00 37.19  ?  137 VAL A CB  1 
ATOM   1008 C CG1 . VAL A 1 137 ? -6.175  10.664  3.063   1.00 38.52  ?  137 VAL A CG1 1 
ATOM   1009 C CG2 . VAL A 1 137 ? -4.394  9.114   2.284   1.00 42.57  ?  137 VAL A CG2 1 
ATOM   1010 N N   . CYS A 1 138 ? -8.968  8.902   3.174   1.00 41.71  ?  138 CYS A N   1 
ATOM   1011 C CA  . CYS A 1 138 ? -10.351 9.350   3.189   1.00 45.33  ?  138 CYS A CA  1 
ATOM   1012 C C   . CYS A 1 138 ? -10.383 10.706  3.874   1.00 46.26  ?  138 CYS A C   1 
ATOM   1013 O O   . CYS A 1 138 ? -9.908  10.836  5.005   1.00 49.62  ?  138 CYS A O   1 
ATOM   1014 C CB  . CYS A 1 138 ? -11.221 8.337   3.935   1.00 52.51  ?  138 CYS A CB  1 
ATOM   1015 S SG  . CYS A 1 138 ? -13.012 8.580   3.944   1.00 60.64  ?  138 CYS A SG  1 
ATOM   1016 N N   . LEU A 1 139 ? -10.899 11.718  3.182   1.00 45.74  ?  139 LEU A N   1 
ATOM   1017 C CA  . LEU A 1 139 ? -10.983 13.075  3.706   1.00 46.63  ?  139 LEU A CA  1 
ATOM   1018 C C   . LEU A 1 139 ? -12.444 13.455  3.907   1.00 47.20  ?  139 LEU A C   1 
ATOM   1019 O O   . LEU A 1 139 ? -13.266 13.271  3.002   1.00 48.29  ?  139 LEU A O   1 
ATOM   1020 C CB  . LEU A 1 139 ? -10.299 14.070  2.762   1.00 48.78  ?  139 LEU A CB  1 
ATOM   1021 C CG  . LEU A 1 139 ? -10.582 15.558  2.995   1.00 49.36  ?  139 LEU A CG  1 
ATOM   1022 C CD1 . LEU A 1 139 ? -10.152 15.984  4.391   1.00 43.76  ?  139 LEU A CD1 1 
ATOM   1023 C CD2 . LEU A 1 139 ? -9.898  16.420  1.935   1.00 47.67  ?  139 LEU A CD2 1 
ATOM   1024 N N   . LEU A 1 140 ? -12.763 13.956  5.102   1.00 46.67  ?  140 LEU A N   1 
ATOM   1025 C CA  . LEU A 1 140 ? -14.081 14.472  5.468   1.00 44.47  ?  140 LEU A CA  1 
ATOM   1026 C C   . LEU A 1 140 ? -13.923 15.959  5.747   1.00 48.79  ?  140 LEU A C   1 
ATOM   1027 O O   . LEU A 1 140 ? -13.234 16.342  6.697   1.00 51.68  ?  140 LEU A O   1 
ATOM   1028 C CB  . LEU A 1 140 ? -14.631 13.766  6.701   1.00 43.05  ?  140 LEU A CB  1 
ATOM   1029 C CG  . LEU A 1 140 ? -15.241 12.376  6.612   1.00 46.48  ?  140 LEU A CG  1 
ATOM   1030 C CD1 . LEU A 1 140 ? -14.229 11.360  6.119   1.00 49.27  ?  140 LEU A CD1 1 
ATOM   1031 C CD2 . LEU A 1 140 ? -15.700 12.023  7.998   1.00 48.85  ?  140 LEU A CD2 1 
ATOM   1032 N N   . ASN A 1 141 ? -14.553 16.797  4.938   1.00 46.51  ?  141 ASN A N   1 
ATOM   1033 C CA  . ASN A 1 141 ? -14.329 18.233  4.993   1.00 50.49  ?  141 ASN A CA  1 
ATOM   1034 C C   . ASN A 1 141 ? -15.551 18.952  5.548   1.00 54.67  ?  141 ASN A C   1 
ATOM   1035 O O   . ASN A 1 141 ? -16.679 18.710  5.098   1.00 58.43  ?  141 ASN A O   1 
ATOM   1036 C CB  . ASN A 1 141 ? -13.981 18.778  3.609   1.00 54.53  ?  141 ASN A CB  1 
ATOM   1037 C CG  . ASN A 1 141 ? -12.944 19.877  3.666   1.00 58.76  ?  141 ASN A CG  1 
ATOM   1038 O OD1 . ASN A 1 141 ? -12.051 19.861  4.515   1.00 58.30  ?  141 ASN A OD1 1 
ATOM   1039 N ND2 . ASN A 1 141 ? -13.064 20.850  2.770   1.00 66.55  ?  141 ASN A ND2 1 
ATOM   1040 N N   . ASN A 1 142 ? -15.311 19.819  6.536   1.00 46.68  ?  142 ASN A N   1 
ATOM   1041 C CA  . ASN A 1 142 ? -16.235 20.864  6.980   1.00 52.09  ?  142 ASN A CA  1 
ATOM   1042 C C   . ASN A 1 142 ? -17.609 20.334  7.399   1.00 49.64  ?  142 ASN A C   1 
ATOM   1043 O O   . ASN A 1 142 ? -18.631 20.564  6.749   1.00 46.06  ?  142 ASN A O   1 
ATOM   1044 C CB  . ASN A 1 142 ? -16.370 21.954  5.911   1.00 56.64  ?  142 ASN A CB  1 
ATOM   1045 C CG  . ASN A 1 142 ? -15.041 22.624  5.599   1.00 62.08  ?  142 ASN A CG  1 
ATOM   1046 O OD1 . ASN A 1 142 ? -14.584 22.632  4.457   1.00 62.35  ?  142 ASN A OD1 1 
ATOM   1047 N ND2 . ASN A 1 142 ? -14.407 23.179  6.629   1.00 65.78  ?  142 ASN A ND2 1 
ATOM   1048 N N   . PHE A 1 143 ? -17.595 19.624  8.529   1.00 47.25  ?  143 PHE A N   1 
ATOM   1049 C CA  . PHE A 1 143 ? -18.785 19.002  9.090   1.00 48.41  ?  143 PHE A CA  1 
ATOM   1050 C C   . PHE A 1 143 ? -18.923 19.363  10.566  1.00 47.98  ?  143 PHE A C   1 
ATOM   1051 O O   . PHE A 1 143 ? -18.024 19.942  11.180  1.00 47.25  ?  143 PHE A O   1 
ATOM   1052 C CB  . PHE A 1 143 ? -18.751 17.476  8.919   1.00 48.93  ?  143 PHE A CB  1 
ATOM   1053 C CG  . PHE A 1 143 ? -17.581 16.807  9.588   1.00 45.02  ?  143 PHE A CG  1 
ATOM   1054 C CD1 . PHE A 1 143 ? -17.709 16.268  10.859  1.00 44.06  ?  143 PHE A CD1 1 
ATOM   1055 C CD2 . PHE A 1 143 ? -16.359 16.707  8.942   1.00 46.12  ?  143 PHE A CD2 1 
ATOM   1056 C CE1 . PHE A 1 143 ? -16.636 15.643  11.479  1.00 41.41  ?  143 PHE A CE1 1 
ATOM   1057 C CE2 . PHE A 1 143 ? -15.282 16.084  9.556   1.00 45.60  ?  143 PHE A CE2 1 
ATOM   1058 C CZ  . PHE A 1 143 ? -15.421 15.550  10.824  1.00 44.29  ?  143 PHE A CZ  1 
ATOM   1059 N N   . TYR A 1 144 ? -20.070 18.988  11.131  1.00 49.67  ?  144 TYR A N   1 
ATOM   1060 C CA  . TYR A 1 144 ? -20.420 19.175  12.535  1.00 49.59  ?  144 TYR A CA  1 
ATOM   1061 C C   . TYR A 1 144 ? -21.620 18.291  12.857  1.00 47.96  ?  144 TYR A C   1 
ATOM   1062 O O   . TYR A 1 144 ? -22.554 18.203  12.050  1.00 50.35  ?  144 TYR A O   1 
ATOM   1063 C CB  . TYR A 1 144 ? -20.723 20.646  12.858  1.00 49.48  ?  144 TYR A CB  1 
ATOM   1064 C CG  . TYR A 1 144 ? -20.850 20.871  14.347  1.00 50.45  ?  144 TYR A CG  1 
ATOM   1065 C CD1 . TYR A 1 144 ? -22.093 20.832  14.972  1.00 45.85  ?  144 TYR A CD1 1 
ATOM   1066 C CD2 . TYR A 1 144 ? -19.722 21.059  15.139  1.00 48.44  ?  144 TYR A CD2 1 
ATOM   1067 C CE1 . TYR A 1 144 ? -22.209 20.996  16.339  1.00 46.36  ?  144 TYR A CE1 1 
ATOM   1068 C CE2 . TYR A 1 144 ? -19.830 21.225  16.507  1.00 49.18  ?  144 TYR A CE2 1 
ATOM   1069 C CZ  . TYR A 1 144 ? -21.075 21.195  17.100  1.00 51.27  ?  144 TYR A CZ  1 
ATOM   1070 O OH  . TYR A 1 144 ? -21.185 21.363  18.459  1.00 54.20  ?  144 TYR A OH  1 
ATOM   1071 N N   . PRO A 1 145 ? -21.641 17.619  14.020  1.00 45.31  ?  145 PRO A N   1 
ATOM   1072 C CA  . PRO A 1 145 ? -20.665 17.738  15.107  1.00 46.37  ?  145 PRO A CA  1 
ATOM   1073 C C   . PRO A 1 145 ? -19.374 16.966  14.903  1.00 50.73  ?  145 PRO A C   1 
ATOM   1074 O O   . PRO A 1 145 ? -19.119 16.393  13.843  1.00 53.66  ?  145 PRO A O   1 
ATOM   1075 C CB  . PRO A 1 145 ? -21.418 17.167  16.306  1.00 40.39  ?  145 PRO A CB  1 
ATOM   1076 C CG  . PRO A 1 145 ? -22.283 16.146  15.712  1.00 39.87  ?  145 PRO A CG  1 
ATOM   1077 C CD  . PRO A 1 145 ? -22.737 16.707  14.386  1.00 40.67  ?  145 PRO A CD  1 
ATOM   1078 N N   . ARG A 1 146 ? -18.564 16.951  15.960  1.00 50.59  ?  146 ARG A N   1 
ATOM   1079 C CA  . ARG A 1 146 ? -17.222 16.407  15.847  1.00 47.86  ?  146 ARG A CA  1 
ATOM   1080 C C   . ARG A 1 146 ? -17.259 14.897  15.657  1.00 57.11  ?  146 ARG A C   1 
ATOM   1081 O O   . ARG A 1 146 ? -16.557 14.360  14.795  1.00 62.58  ?  146 ARG A O   1 
ATOM   1082 C CB  . ARG A 1 146 ? -16.409 16.776  17.084  1.00 49.77  ?  146 ARG A CB  1 
ATOM   1083 C CG  . ARG A 1 146 ? -14.932 16.463  16.959  1.00 54.99  ?  146 ARG A CG  1 
ATOM   1084 C CD  . ARG A 1 146 ? -14.150 17.096  18.090  1.00 60.89  ?  146 ARG A CD  1 
ATOM   1085 N NE  . ARG A 1 146 ? -12.769 16.630  18.131  1.00 58.74  ?  146 ARG A NE  1 
ATOM   1086 C CZ  . ARG A 1 146 ? -12.393 15.492  18.698  1.00 59.26  ?  146 ARG A CZ  1 
ATOM   1087 N NH1 . ARG A 1 146 ? -13.300 14.712  19.268  1.00 63.92  ?  146 ARG A NH1 1 
ATOM   1088 N NH2 . ARG A 1 146 ? -11.115 15.136  18.701  1.00 69.69  ?  146 ARG A NH2 1 
ATOM   1089 N N   . GLU A 1 147 ? -18.079 14.201  16.441  1.00 54.17  ?  147 GLU A N   1 
ATOM   1090 C CA  . GLU A 1 147 ? -18.074 12.745  16.444  1.00 55.41  ?  147 GLU A CA  1 
ATOM   1091 C C   . GLU A 1 147 ? -18.528 12.191  15.097  1.00 55.67  ?  147 GLU A C   1 
ATOM   1092 O O   . GLU A 1 147 ? -19.515 12.657  14.517  1.00 58.60  ?  147 GLU A O   1 
ATOM   1093 C CB  . GLU A 1 147 ? -18.977 12.235  17.559  1.00 56.61  ?  147 GLU A CB  1 
ATOM   1094 C CG  . GLU A 1 147 ? -18.805 13.025  18.847  1.00 68.57  ?  147 GLU A CG  1 
ATOM   1095 C CD  . GLU A 1 147 ? -17.356 13.136  19.279  1.00 74.45  ?  147 GLU A CD  1 
ATOM   1096 O OE1 . GLU A 1 147 ? -16.907 14.266  19.575  1.00 74.15  ?  147 GLU A OE1 1 
ATOM   1097 O OE2 . GLU A 1 147 ? -16.658 12.101  19.305  1.00 84.68  ?  147 GLU A OE2 1 
ATOM   1098 N N   . ALA A 1 148 ? -17.792 11.200  14.598  1.00 53.71  ?  148 ALA A N   1 
ATOM   1099 C CA  . ALA A 1 148 ? -18.106 10.549  13.333  1.00 56.05  ?  148 ALA A CA  1 
ATOM   1100 C C   . ALA A 1 148 ? -17.351 9.230   13.277  1.00 53.85  ?  148 ALA A C   1 
ATOM   1101 O O   . ALA A 1 148 ? -16.138 9.203   13.507  1.00 59.78  ?  148 ALA A O   1 
ATOM   1102 C CB  . ALA A 1 148 ? -17.732 11.435  12.141  1.00 54.49  ?  148 ALA A CB  1 
ATOM   1103 N N   . LYS A 1 149 ? -18.063 8.146   12.979  1.00 51.98  ?  149 LYS A N   1 
ATOM   1104 C CA  . LYS A 1 149 ? -17.445 6.835   12.830  1.00 53.69  ?  149 LYS A CA  1 
ATOM   1105 C C   . LYS A 1 149 ? -16.948 6.662   11.398  1.00 54.99  ?  149 LYS A C   1 
ATOM   1106 O O   . LYS A 1 149 ? -17.692 6.899   10.442  1.00 56.53  ?  149 LYS A O   1 
ATOM   1107 C CB  . LYS A 1 149 ? -18.429 5.727   13.212  1.00 56.99  ?  149 LYS A CB  1 
ATOM   1108 C CG  . LYS A 1 149 ? -17.934 4.307   12.906  1.00 71.08  ?  149 LYS A CG  1 
ATOM   1109 C CD  . LYS A 1 149 ? -18.844 3.225   13.506  1.00 75.98  ?  149 LYS A CD  1 
ATOM   1110 C CE  . LYS A 1 149 ? -20.262 3.258   12.939  1.00 78.72  ?  149 LYS A CE  1 
ATOM   1111 N NZ  . LYS A 1 149 ? -20.433 2.361   11.762  1.00 82.11  ?  149 LYS A NZ  1 
ATOM   1112 N N   . VAL A 1 150 ? -15.674 6.307   11.254  1.00 54.69  ?  150 VAL A N   1 
ATOM   1113 C CA  . VAL A 1 150 ? -15.058 6.063   9.952   1.00 55.71  ?  150 VAL A CA  1 
ATOM   1114 C C   . VAL A 1 150 ? -14.577 4.619   9.904   1.00 53.80  ?  150 VAL A C   1 
ATOM   1115 O O   . VAL A 1 150 ? -13.792 4.191   10.759  1.00 57.50  ?  150 VAL A O   1 
ATOM   1116 C CB  . VAL A 1 150 ? -13.893 7.027   9.675   1.00 54.38  ?  150 VAL A CB  1 
ATOM   1117 C CG1 . VAL A 1 150 ? -13.288 6.741   8.308   1.00 54.43  ?  150 VAL A CG1 1 
ATOM   1118 C CG2 . VAL A 1 150 ? -14.363 8.467   9.767   1.00 51.21  ?  150 VAL A CG2 1 
ATOM   1119 N N   . GLN A 1 151 ? -15.041 3.872   8.907   1.00 55.86  ?  151 GLN A N   1 
ATOM   1120 C CA  . GLN A 1 151 ? -14.650 2.482   8.732   1.00 54.14  ?  151 GLN A CA  1 
ATOM   1121 C C   . GLN A 1 151 ? -14.192 2.255   7.300   1.00 50.06  ?  151 GLN A C   1 
ATOM   1122 O O   . GLN A 1 151 ? -14.655 2.912   6.365   1.00 54.07  ?  151 GLN A O   1 
ATOM   1123 C CB  . GLN A 1 151 ? -15.784 1.500   9.079   1.00 51.71  ?  151 GLN A CB  1 
ATOM   1124 C CG  . GLN A 1 151 ? -16.286 1.612   10.507  1.00 64.76  ?  151 GLN A CG  1 
ATOM   1125 C CD  . GLN A 1 151 ? -17.065 0.383   10.949  1.00 77.24  ?  151 GLN A CD  1 
ATOM   1126 O OE1 . GLN A 1 151 ? -18.267 0.261   10.698  1.00 86.11  ?  151 GLN A OE1 1 
ATOM   1127 N NE2 . GLN A 1 151 ? -16.375 -0.539  11.609  1.00 70.47  ?  151 GLN A NE2 1 
ATOM   1128 N N   . TRP A 1 152 ? -13.265 1.321   7.140   1.00 43.86  ?  152 TRP A N   1 
ATOM   1129 C CA  . TRP A 1 152 ? -12.738 0.951   5.839   1.00 48.85  ?  152 TRP A CA  1 
ATOM   1130 C C   . TRP A 1 152 ? -13.261 -0.425  5.460   1.00 50.33  ?  152 TRP A C   1 
ATOM   1131 O O   . TRP A 1 152 ? -13.290 -1.338  6.289   1.00 52.48  ?  152 TRP A O   1 
ATOM   1132 C CB  . TRP A 1 152 ? -11.207 0.954   5.841   1.00 48.10  ?  152 TRP A CB  1 
ATOM   1133 C CG  . TRP A 1 152 ? -10.616 2.328   5.882   1.00 44.03  ?  152 TRP A CG  1 
ATOM   1134 C CD1 . TRP A 1 152 ? -10.239 3.022   6.991   1.00 41.04  ?  152 TRP A CD1 1 
ATOM   1135 C CD2 . TRP A 1 152 ? -10.341 3.176   4.764   1.00 40.18  ?  152 TRP A CD2 1 
ATOM   1136 N NE1 . TRP A 1 152 ? -9.739  4.248   6.634   1.00 43.00  ?  152 TRP A NE1 1 
ATOM   1137 C CE2 . TRP A 1 152 ? -9.790  4.368   5.271   1.00 42.09  ?  152 TRP A CE2 1 
ATOM   1138 C CE3 . TRP A 1 152 ? -10.503 3.043   3.383   1.00 41.49  ?  152 TRP A CE3 1 
ATOM   1139 C CZ2 . TRP A 1 152 ? -9.405  5.425   4.446   1.00 43.70  ?  152 TRP A CZ2 1 
ATOM   1140 C CZ3 . TRP A 1 152 ? -10.115 4.093   2.563   1.00 44.53  ?  152 TRP A CZ3 1 
ATOM   1141 C CH2 . TRP A 1 152 ? -9.574  5.267   3.098   1.00 44.04  ?  152 TRP A CH2 1 
ATOM   1142 N N   . LYS A 1 153 ? -13.672 -0.564  4.204   1.00 51.38  ?  153 LYS A N   1 
ATOM   1143 C CA  . LYS A 1 153 ? -14.098 -1.843  3.653   1.00 54.51  ?  153 LYS A CA  1 
ATOM   1144 C C   . LYS A 1 153 ? -13.346 -2.070  2.357   1.00 57.55  ?  153 LYS A C   1 
ATOM   1145 O O   . LYS A 1 153 ? -13.415 -1.237  1.448   1.00 62.54  ?  153 LYS A O   1 
ATOM   1146 C CB  . LYS A 1 153 ? -15.598 -1.846  3.372   1.00 58.06  ?  153 LYS A CB  1 
ATOM   1147 C CG  . LYS A 1 153 ? -16.458 -1.423  4.524   1.00 64.75  ?  153 LYS A CG  1 
ATOM   1148 C CD  . LYS A 1 153 ? -17.888 -1.280  4.048   1.00 71.47  ?  153 LYS A CD  1 
ATOM   1149 C CE  . LYS A 1 153 ? -18.647 -0.305  4.920   1.00 74.82  ?  153 LYS A CE  1 
ATOM   1150 N NZ  . LYS A 1 153 ? -20.082 -0.225  4.539   1.00 74.17  ?  153 LYS A NZ  1 
ATOM   1151 N N   . VAL A 1 154 ? -12.636 -3.186  2.262   1.00 59.37  ?  154 VAL A N   1 
ATOM   1152 C CA  . VAL A 1 154 ? -11.971 -3.574  1.025   1.00 59.20  ?  154 VAL A CA  1 
ATOM   1153 C C   . VAL A 1 154 ? -12.549 -4.913  0.585   1.00 58.58  ?  154 VAL A C   1 
ATOM   1154 O O   . VAL A 1 154 ? -12.405 -5.922  1.289   1.00 59.56  ?  154 VAL A O   1 
ATOM   1155 C CB  . VAL A 1 154 ? -10.440 -3.618  1.182   1.00 59.39  ?  154 VAL A CB  1 
ATOM   1156 C CG1 . VAL A 1 154 ? -10.030 -4.397  2.411   1.00 65.05  ?  154 VAL A CG1 1 
ATOM   1157 C CG2 . VAL A 1 154 ? -9.808  -4.220  -0.043  1.00 58.35  ?  154 VAL A CG2 1 
ATOM   1158 N N   . ASP A 1 155 ? -13.223 -4.911  -0.566  1.00 60.87  ?  155 ASP A N   1 
ATOM   1159 C CA  . ASP A 1 155 ? -13.987 -6.061  -1.053  1.00 60.98  ?  155 ASP A CA  1 
ATOM   1160 C C   . ASP A 1 155 ? -14.928 -6.596  0.024   1.00 61.31  ?  155 ASP A C   1 
ATOM   1161 O O   . ASP A 1 155 ? -14.945 -7.788  0.335   1.00 68.85  ?  155 ASP A O   1 
ATOM   1162 C CB  . ASP A 1 155 ? -13.069 -7.165  -1.577  1.00 56.58  ?  155 ASP A CB  1 
ATOM   1163 C CG  . ASP A 1 155 ? -12.362 -6.774  -2.858  1.00 58.58  ?  155 ASP A CG  1 
ATOM   1164 O OD1 . ASP A 1 155 ? -11.264 -7.305  -3.122  1.00 66.36  ?  155 ASP A OD1 1 
ATOM   1165 O OD2 . ASP A 1 155 ? -12.901 -5.928  -3.601  1.00 61.04  ?  155 ASP A OD2 1 
ATOM   1166 N N   . ASN A 1 156 ? -15.693 -5.685  0.626   1.00 61.55  ?  156 ASN A N   1 
ATOM   1167 C CA  . ASN A 1 156 ? -16.703 -6.031  1.628   1.00 71.81  ?  156 ASN A CA  1 
ATOM   1168 C C   . ASN A 1 156 ? -16.105 -6.742  2.841   1.00 72.90  ?  156 ASN A C   1 
ATOM   1169 O O   . ASN A 1 156 ? -16.787 -7.520  3.514   1.00 84.39  ?  156 ASN A O   1 
ATOM   1170 C CB  . ASN A 1 156 ? -17.834 -6.867  1.022   1.00 76.96  ?  156 ASN A CB  1 
ATOM   1171 C CG  . ASN A 1 156 ? -18.630 -6.096  -0.010  1.00 87.34  ?  156 ASN A CG  1 
ATOM   1172 O OD1 . ASN A 1 156 ? -18.543 -6.364  -1.209  1.00 93.73  ?  156 ASN A OD1 1 
ATOM   1173 N ND2 . ASN A 1 156 ? -19.402 -5.115  0.452   1.00 81.17  ?  156 ASN A ND2 1 
ATOM   1174 N N   . ALA A 1 157 ? -14.828 -6.499  3.126   1.00 64.91  ?  157 ALA A N   1 
ATOM   1175 C CA  . ALA A 1 157 ? -14.177 -7.012  4.327   1.00 62.13  ?  157 ALA A CA  1 
ATOM   1176 C C   . ALA A 1 157 ? -13.815 -5.810  5.193   1.00 60.06  ?  157 ALA A C   1 
ATOM   1177 O O   . ALA A 1 157 ? -12.970 -4.994  4.807   1.00 58.21  ?  157 ALA A O   1 
ATOM   1178 C CB  . ALA A 1 157 ? -12.941 -7.836  3.980   1.00 51.82  ?  157 ALA A CB  1 
ATOM   1179 N N   . LEU A 1 158 ? -14.454 -5.701  6.354   1.00 59.57  ?  158 LEU A N   1 
ATOM   1180 C CA  . LEU A 1 158 ? -14.179 -4.582  7.242   1.00 57.62  ?  158 LEU A CA  1 
ATOM   1181 C C   . LEU A 1 158 ? -12.743 -4.653  7.730   1.00 59.75  ?  158 LEU A C   1 
ATOM   1182 O O   . LEU A 1 158 ? -12.250 -5.721  8.096   1.00 55.66  ?  158 LEU A O   1 
ATOM   1183 C CB  . LEU A 1 158 ? -15.137 -4.577  8.431   1.00 66.82  ?  158 LEU A CB  1 
ATOM   1184 C CG  . LEU A 1 158 ? -14.789 -3.585  9.547   1.00 72.21  ?  158 LEU A CG  1 
ATOM   1185 C CD1 . LEU A 1 158 ? -14.843 -2.133  9.055   1.00 66.34  ?  158 LEU A CD1 1 
ATOM   1186 C CD2 . LEU A 1 158 ? -15.700 -3.787  10.750  1.00 75.01  ?  158 LEU A CD2 1 
ATOM   1187 N N   . GLN A 1 159 ? -12.069 -3.509  7.723   1.00 64.18  ?  159 GLN A N   1 
ATOM   1188 C CA  . GLN A 1 159 ? -10.681 -3.448  8.139   1.00 59.89  ?  159 GLN A CA  1 
ATOM   1189 C C   . GLN A 1 159 ? -10.591 -3.110  9.619   1.00 65.00  ?  159 GLN A C   1 
ATOM   1190 O O   . GLN A 1 159 ? -11.447 -2.417  10.175  1.00 70.99  ?  159 GLN A O   1 
ATOM   1191 C CB  . GLN A 1 159 ? -9.921  -2.411  7.317   1.00 58.17  ?  159 GLN A CB  1 
ATOM   1192 C CG  . GLN A 1 159 ? -9.760  -2.811  5.873   1.00 56.82  ?  159 GLN A CG  1 
ATOM   1193 C CD  . GLN A 1 159 ? -9.069  -4.146  5.737   1.00 59.51  ?  159 GLN A CD  1 
ATOM   1194 O OE1 . GLN A 1 159 ? -7.849  -4.244  5.867   1.00 61.50  ?  159 GLN A OE1 1 
ATOM   1195 N NE2 . GLN A 1 159 ? -9.849  -5.190  5.487   1.00 61.40  ?  159 GLN A NE2 1 
ATOM   1196 N N   . SER A 1 160 ? -9.544  -3.619  10.256  1.00 63.96  ?  160 SER A N   1 
ATOM   1197 C CA  . SER A 1 160 ? -9.329  -3.380  11.674  1.00 64.60  ?  160 SER A CA  1 
ATOM   1198 C C   . SER A 1 160 ? -7.833  -3.367  11.923  1.00 67.83  ?  160 SER A C   1 
ATOM   1199 O O   . SER A 1 160 ? -7.131  -4.294  11.509  1.00 70.36  ?  160 SER A O   1 
ATOM   1200 C CB  . SER A 1 160 ? -10.009 -4.452  12.531  1.00 76.43  ?  160 SER A CB  1 
ATOM   1201 O OG  . SER A 1 160 ? -11.404 -4.511  12.273  1.00 85.31  ?  160 SER A OG  1 
ATOM   1202 N N   . GLY A 1 161 ? -7.352  -2.312  12.579  1.00 64.23  ?  161 GLY A N   1 
ATOM   1203 C CA  . GLY A 1 161 ? -5.976  -2.248  13.020  1.00 53.00  ?  161 GLY A CA  1 
ATOM   1204 C C   . GLY A 1 161 ? -4.989  -1.735  11.999  1.00 52.85  ?  161 GLY A C   1 
ATOM   1205 O O   . GLY A 1 161 ? -3.791  -1.662  12.303  1.00 61.93  ?  161 GLY A O   1 
ATOM   1206 N N   . ASN A 1 162 ? -5.439  -1.378  10.799  1.00 52.29  ?  162 ASN A N   1 
ATOM   1207 C CA  . ASN A 1 162 ? -4.547  -0.861  9.770   1.00 55.34  ?  162 ASN A CA  1 
ATOM   1208 C C   . ASN A 1 162 ? -5.007  0.497   9.240   1.00 52.80  ?  162 ASN A C   1 
ATOM   1209 O O   . ASN A 1 162 ? -4.739  0.839   8.085   1.00 52.94  ?  162 ASN A O   1 
ATOM   1210 C CB  . ASN A 1 162 ? -4.402  -1.862  8.623   1.00 54.96  ?  162 ASN A CB  1 
ATOM   1211 C CG  . ASN A 1 162 ? -5.736  -2.383  8.122   1.00 54.60  ?  162 ASN A CG  1 
ATOM   1212 O OD1 . ASN A 1 162 ? -6.798  -2.020  8.631   1.00 55.40  ?  162 ASN A OD1 1 
ATOM   1213 N ND2 . ASN A 1 162 ? -5.686  -3.221  7.093   1.00 54.21  ?  162 ASN A ND2 1 
ATOM   1214 N N   . SER A 1 163 ? -5.695  1.288   10.068  1.00 45.54  ?  163 SER A N   1 
ATOM   1215 C CA  . SER A 1 163 ? -6.056  2.651   9.698   1.00 46.10  ?  163 SER A CA  1 
ATOM   1216 C C   . SER A 1 163 ? -5.941  3.552   10.917  1.00 47.14  ?  163 SER A C   1 
ATOM   1217 O O   . SER A 1 163 ? -6.041  3.095   12.059  1.00 48.39  ?  163 SER A O   1 
ATOM   1218 C CB  . SER A 1 163 ? -7.481  2.753   9.121   1.00 47.32  ?  163 SER A CB  1 
ATOM   1219 O OG  . SER A 1 163 ? -8.467  2.535   10.112  1.00 49.87  ?  163 SER A OG  1 
ATOM   1220 N N   . GLN A 1 164 ? -5.725  4.840   10.659  1.00 48.65  ?  164 GLN A N   1 
ATOM   1221 C CA  . GLN A 1 164 ? -5.638  5.842   11.713  1.00 42.70  ?  164 GLN A CA  1 
ATOM   1222 C C   . GLN A 1 164 ? -6.383  7.097   11.296  1.00 44.48  ?  164 GLN A C   1 
ATOM   1223 O O   . GLN A 1 164 ? -6.486  7.415   10.110  1.00 42.84  ?  164 GLN A O   1 
ATOM   1224 C CB  . GLN A 1 164 ? -4.192  6.199   12.059  1.00 45.91  ?  164 GLN A CB  1 
ATOM   1225 C CG  . GLN A 1 164 ? -3.448  5.088   12.760  1.00 54.77  ?  164 GLN A CG  1 
ATOM   1226 C CD  . GLN A 1 164 ? -2.141  5.559   13.348  1.00 55.61  ?  164 GLN A CD  1 
ATOM   1227 O OE1 . GLN A 1 164 ? -1.291  6.105   12.643  1.00 64.86  ?  164 GLN A OE1 1 
ATOM   1228 N NE2 . GLN A 1 164 ? -1.972  5.358   14.651  1.00 50.99  ?  164 GLN A NE2 1 
ATOM   1229 N N   . GLU A 1 165 ? -6.892  7.817   12.290  1.00 46.72  ?  165 GLU A N   1 
ATOM   1230 C CA  . GLU A 1 165 ? -7.684  9.014   12.061  1.00 47.82  ?  165 GLU A CA  1 
ATOM   1231 C C   . GLU A 1 165 ? -7.030  10.217  12.727  1.00 43.93  ?  165 GLU A C   1 
ATOM   1232 O O   . GLU A 1 165 ? -6.330  10.090  13.737  1.00 41.62  ?  165 GLU A O   1 
ATOM   1233 C CB  . GLU A 1 165 ? -9.109  8.831   12.584  1.00 46.78  ?  165 GLU A CB  1 
ATOM   1234 C CG  . GLU A 1 165 ? -9.860  7.725   11.868  1.00 55.53  ?  165 GLU A CG  1 
ATOM   1235 C CD  . GLU A 1 165 ? -11.226 7.449   12.470  1.00 72.57  ?  165 GLU A CD  1 
ATOM   1236 O OE1 . GLU A 1 165 ? -11.714 8.278   13.275  1.00 77.73  ?  165 GLU A OE1 1 
ATOM   1237 O OE2 . GLU A 1 165 ? -11.807 6.391   12.141  1.00 73.89  ?  165 GLU A OE2 1 
ATOM   1238 N N   . SER A 1 166 ? -7.281  11.388  12.151  1.00 44.56  ?  166 SER A N   1 
ATOM   1239 C CA  . SER A 1 166 ? -6.788  12.650  12.682  1.00 42.79  ?  166 SER A CA  1 
ATOM   1240 C C   . SER A 1 166 ? -7.834  13.714  12.388  1.00 45.69  ?  166 SER A C   1 
ATOM   1241 O O   . SER A 1 166 ? -8.376  13.766  11.283  1.00 49.77  ?  166 SER A O   1 
ATOM   1242 C CB  . SER A 1 166 ? -5.431  13.014  12.059  1.00 40.43  ?  166 SER A CB  1 
ATOM   1243 O OG  . SER A 1 166 ? -4.975  14.283  12.487  1.00 42.15  ?  166 SER A OG  1 
ATOM   1244 N N   . VAL A 1 167 ? -8.127  14.556  13.371  1.00 40.32  ?  167 VAL A N   1 
ATOM   1245 C CA  . VAL A 1 167 ? -9.159  15.576  13.225  1.00 49.22  ?  167 VAL A CA  1 
ATOM   1246 C C   . VAL A 1 167 ? -8.558  16.946  13.507  1.00 49.07  ?  167 VAL A C   1 
ATOM   1247 O O   . VAL A 1 167 ? -7.764  17.109  14.442  1.00 51.61  ?  167 VAL A O   1 
ATOM   1248 C CB  . VAL A 1 167 ? -10.367 15.291  14.145  1.00 47.86  ?  167 VAL A CB  1 
ATOM   1249 C CG1 . VAL A 1 167 ? -9.919  15.134  15.584  1.00 58.45  ?  167 VAL A CG1 1 
ATOM   1250 C CG2 . VAL A 1 167 ? -11.403 16.387  14.022  1.00 39.20  ?  167 VAL A CG2 1 
ATOM   1251 N N   . THR A 1 168 ? -8.912  17.923  12.672  1.00 46.51  ?  168 THR A N   1 
ATOM   1252 C CA  . THR A 1 168 ? -8.475  19.295  12.883  1.00 48.15  ?  168 THR A CA  1 
ATOM   1253 C C   . THR A 1 168 ? -9.173  19.897  14.099  1.00 52.95  ?  168 THR A C   1 
ATOM   1254 O O   . THR A 1 168 ? -10.155 19.365  14.623  1.00 56.57  ?  168 THR A O   1 
ATOM   1255 C CB  . THR A 1 168 ? -8.775  20.172  11.662  1.00 45.84  ?  168 THR A CB  1 
ATOM   1256 O OG1 . THR A 1 168 ? -10.191 20.381  11.556  1.00 47.25  ?  168 THR A OG1 1 
ATOM   1257 C CG2 . THR A 1 168 ? -8.256  19.543  10.389  1.00 46.27  ?  168 THR A CG2 1 
ATOM   1258 N N   . GLU A 1 169 ? -8.652  21.029  14.547  1.00 53.93  ?  169 GLU A N   1 
ATOM   1259 C CA  . GLU A 1 169 ? -9.387  21.809  15.520  1.00 50.18  ?  169 GLU A CA  1 
ATOM   1260 C C   . GLU A 1 169 ? -10.542 22.526  14.828  1.00 53.51  ?  169 GLU A C   1 
ATOM   1261 O O   . GLU A 1 169 ? -10.605 22.628  13.598  1.00 48.88  ?  169 GLU A O   1 
ATOM   1262 C CB  . GLU A 1 169 ? -8.463  22.793  16.231  1.00 56.59  ?  169 GLU A CB  1 
ATOM   1263 C CG  . GLU A 1 169 ? -7.268  22.131  16.938  1.00 63.85  ?  169 GLU A CG  1 
ATOM   1264 C CD  . GLU A 1 169 ? -7.610  21.544  18.306  1.00 65.83  ?  169 GLU A CD  1 
ATOM   1265 O OE1 . GLU A 1 169 ? -8.764  21.106  18.514  1.00 64.76  ?  169 GLU A OE1 1 
ATOM   1266 O OE2 . GLU A 1 169 ? -6.717  21.528  19.181  1.00 67.80  ?  169 GLU A OE2 1 
ATOM   1267 N N   . GLN A 1 170 ? -11.469 23.028  15.636  1.00 53.00  ?  170 GLN A N   1 
ATOM   1268 C CA  . GLN A 1 170 ? -12.659 23.658  15.086  1.00 54.36  ?  170 GLN A CA  1 
ATOM   1269 C C   . GLN A 1 170 ? -12.300 24.931  14.328  1.00 52.46  ?  170 GLN A C   1 
ATOM   1270 O O   . GLN A 1 170 ? -11.548 25.773  14.824  1.00 54.72  ?  170 GLN A O   1 
ATOM   1271 C CB  . GLN A 1 170 ? -13.660 23.955  16.197  1.00 51.31  ?  170 GLN A CB  1 
ATOM   1272 C CG  . GLN A 1 170 ? -14.998 24.388  15.657  1.00 51.44  ?  170 GLN A CG  1 
ATOM   1273 C CD  . GLN A 1 170 ? -16.100 24.308  16.681  1.00 48.95  ?  170 GLN A CD  1 
ATOM   1274 O OE1 . GLN A 1 170 ? -15.902 24.634  17.849  1.00 51.96  ?  170 GLN A OE1 1 
ATOM   1275 N NE2 . GLN A 1 170 ? -17.274 23.873  16.247  1.00 42.77  ?  170 GLN A NE2 1 
ATOM   1276 N N   . ASP A 1 171 ? -12.831 25.055  13.115  1.00 55.38  ?  171 ASP A N   1 
ATOM   1277 C CA  . ASP A 1 171 ? -12.587 26.232  12.293  1.00 54.98  ?  171 ASP A CA  1 
ATOM   1278 C C   . ASP A 1 171 ? -13.120 27.482  12.989  1.00 63.76  ?  171 ASP A C   1 
ATOM   1279 O O   . ASP A 1 171 ? -14.294 27.546  13.368  1.00 63.74  ?  171 ASP A O   1 
ATOM   1280 C CB  . ASP A 1 171 ? -13.254 26.044  10.929  1.00 56.21  ?  171 ASP A CB  1 
ATOM   1281 C CG  . ASP A 1 171 ? -12.790 27.054  9.898   1.00 66.92  ?  171 ASP A CG  1 
ATOM   1282 O OD1 . ASP A 1 171 ? -12.077 26.647  8.956   1.00 73.37  ?  171 ASP A OD1 1 
ATOM   1283 O OD2 . ASP A 1 171 ? -13.127 28.252  10.029  1.00 66.04  ?  171 ASP A OD2 1 
ATOM   1284 N N   . SER A 1 172 ? -12.248 28.480  13.158  1.00 62.91  ?  172 SER A N   1 
ATOM   1285 C CA  . SER A 1 172 ? -12.600 29.688  13.898  1.00 61.64  ?  172 SER A CA  1 
ATOM   1286 C C   . SER A 1 172 ? -13.595 30.576  13.164  1.00 59.04  ?  172 SER A C   1 
ATOM   1287 O O   . SER A 1 172 ? -14.105 31.526  13.767  1.00 57.91  ?  172 SER A O   1 
ATOM   1288 C CB  . SER A 1 172 ? -11.340 30.493  14.216  1.00 63.39  ?  172 SER A CB  1 
ATOM   1289 O OG  . SER A 1 172 ? -10.592 30.735  13.037  1.00 71.01  ?  172 SER A OG  1 
ATOM   1290 N N   . LYS A 1 173 ? -13.878 30.306  11.892  1.00 61.76  ?  173 LYS A N   1 
ATOM   1291 C CA  . LYS A 1 173 ? -14.848 31.101  11.144  1.00 61.59  ?  173 LYS A CA  1 
ATOM   1292 C C   . LYS A 1 173 ? -16.237 30.470  11.180  1.00 62.19  ?  173 LYS A C   1 
ATOM   1293 O O   . LYS A 1 173 ? -17.199 31.102  11.628  1.00 67.25  ?  173 LYS A O   1 
ATOM   1294 C CB  . LYS A 1 173 ? -14.377 31.289  9.696   1.00 68.94  ?  173 LYS A CB  1 
ATOM   1295 C CG  . LYS A 1 173 ? -13.255 32.314  9.522   1.00 73.31  ?  173 LYS A CG  1 
ATOM   1296 C CD  . LYS A 1 173 ? -11.873 31.734  9.830   1.00 71.69  ?  173 LYS A CD  1 
ATOM   1297 C CE  . LYS A 1 173 ? -11.457 30.680  8.809   1.00 75.15  ?  173 LYS A CE  1 
ATOM   1298 N NZ  . LYS A 1 173 ? -10.204 29.966  9.204   1.00 69.73  ?  173 LYS A NZ  1 
ATOM   1299 N N   . ASP A 1 174 ? -16.357 29.227  10.714  1.00 59.10  ?  174 ASP A N   1 
ATOM   1300 C CA  . ASP A 1 174 ? -17.651 28.577  10.557  1.00 59.14  ?  174 ASP A CA  1 
ATOM   1301 C C   . ASP A 1 174 ? -17.876 27.415  11.516  1.00 56.93  ?  174 ASP A C   1 
ATOM   1302 O O   . ASP A 1 174 ? -18.903 26.738  11.406  1.00 53.78  ?  174 ASP A O   1 
ATOM   1303 C CB  . ASP A 1 174 ? -17.821 28.095  9.114   1.00 57.80  ?  174 ASP A CB  1 
ATOM   1304 C CG  . ASP A 1 174 ? -16.951 26.904  8.794   1.00 62.17  ?  174 ASP A CG  1 
ATOM   1305 O OD1 . ASP A 1 174 ? -15.881 26.758  9.418   1.00 62.01  ?  174 ASP A OD1 1 
ATOM   1306 O OD2 . ASP A 1 174 ? -17.334 26.112  7.908   1.00 78.27  ?  174 ASP A OD2 1 
ATOM   1307 N N   . SER A 1 175 ? -16.944 27.153  12.433  1.00 53.59  ?  175 SER A N   1 
ATOM   1308 C CA  . SER A 1 175 ? -17.130 26.186  13.514  1.00 53.98  ?  175 SER A CA  1 
ATOM   1309 C C   . SER A 1 175 ? -17.264 24.748  13.014  1.00 52.97  ?  175 SER A C   1 
ATOM   1310 O O   . SER A 1 175 ? -17.848 23.902  13.697  1.00 43.74  ?  175 SER A O   1 
ATOM   1311 C CB  . SER A 1 175 ? -18.339 26.551  14.384  1.00 49.32  ?  175 SER A CB  1 
ATOM   1312 O OG  . SER A 1 175 ? -18.209 27.846  14.934  1.00 52.64  ?  175 SER A OG  1 
ATOM   1313 N N   . THR A 1 176 ? -16.711 24.434  11.848  1.00 56.61  ?  176 THR A N   1 
ATOM   1314 C CA  . THR A 1 176 ? -16.750 23.072  11.338  1.00 55.16  ?  176 THR A CA  1 
ATOM   1315 C C   . THR A 1 176 ? -15.422 22.367  11.594  1.00 54.81  ?  176 THR A C   1 
ATOM   1316 O O   . THR A 1 176 ? -14.398 22.994  11.877  1.00 50.47  ?  176 THR A O   1 
ATOM   1317 C CB  . THR A 1 176 ? -17.063 23.040  9.839   1.00 51.99  ?  176 THR A CB  1 
ATOM   1318 O OG1 . THR A 1 176 ? -16.099 23.827  9.129   1.00 54.78  ?  176 THR A OG1 1 
ATOM   1319 C CG2 . THR A 1 176 ? -18.460 23.569  9.575   1.00 48.00  ?  176 THR A CG2 1 
ATOM   1320 N N   . TYR A 1 177 ? -15.459 21.041  11.478  1.00 50.40  ?  177 TYR A N   1 
ATOM   1321 C CA  . TYR A 1 177 ? -14.300 20.181  11.631  1.00 41.88  ?  177 TYR A CA  1 
ATOM   1322 C C   . TYR A 1 177 ? -13.955 19.519  10.304  1.00 46.73  ?  177 TYR A C   1 
ATOM   1323 O O   . TYR A 1 177 ? -14.779 19.431  9.388   1.00 46.28  ?  177 TYR A O   1 
ATOM   1324 C CB  . TYR A 1 177 ? -14.555 19.090  12.673  1.00 43.41  ?  177 TYR A CB  1 
ATOM   1325 C CG  . TYR A 1 177 ? -14.651 19.562  14.101  1.00 50.91  ?  177 TYR A CG  1 
ATOM   1326 C CD1 . TYR A 1 177 ? -15.867 19.972  14.640  1.00 50.34  ?  177 TYR A CD1 1 
ATOM   1327 C CD2 . TYR A 1 177 ? -13.535 19.566  14.922  1.00 47.63  ?  177 TYR A CD2 1 
ATOM   1328 C CE1 . TYR A 1 177 ? -15.960 20.389  15.954  1.00 49.06  ?  177 TYR A CE1 1 
ATOM   1329 C CE2 . TYR A 1 177 ? -13.617 19.981  16.232  1.00 51.85  ?  177 TYR A CE2 1 
ATOM   1330 C CZ  . TYR A 1 177 ? -14.828 20.391  16.744  1.00 53.14  ?  177 TYR A CZ  1 
ATOM   1331 O OH  . TYR A 1 177 ? -14.896 20.800  18.054  1.00 55.62  ?  177 TYR A OH  1 
ATOM   1332 N N   . SER A 1 178 ? -12.717 19.041  10.219  1.00 47.32  ?  178 SER A N   1 
ATOM   1333 C CA  . SER A 1 178 ? -12.282 18.173  9.138   1.00 42.15  ?  178 SER A CA  1 
ATOM   1334 C C   . SER A 1 178 ? -11.562 16.971  9.727   1.00 43.99  ?  178 SER A C   1 
ATOM   1335 O O   . SER A 1 178 ? -10.931 17.062  10.783  1.00 46.60  ?  178 SER A O   1 
ATOM   1336 C CB  . SER A 1 178 ? -11.365 18.912  8.161   1.00 44.77  ?  178 SER A CB  1 
ATOM   1337 O OG  . SER A 1 178 ? -12.104 19.831  7.376   1.00 48.18  ?  178 SER A OG  1 
ATOM   1338 N N   . LEU A 1 179 ? -11.658 15.839  9.037   1.00 43.19  ?  179 LEU A N   1 
ATOM   1339 C CA  . LEU A 1 179 ? -11.059 14.600  9.507   1.00 43.36  ?  179 LEU A CA  1 
ATOM   1340 C C   . LEU A 1 179 ? -10.380 13.902  8.337   1.00 46.70  ?  179 LEU A C   1 
ATOM   1341 O O   . LEU A 1 179 ? -10.835 13.983  7.194   1.00 48.58  ?  179 LEU A O   1 
ATOM   1342 C CB  . LEU A 1 179 ? -12.117 13.691  10.154  1.00 45.60  ?  179 LEU A CB  1 
ATOM   1343 C CG  . LEU A 1 179 ? -11.733 12.268  10.567  1.00 46.95  ?  179 LEU A CG  1 
ATOM   1344 C CD1 . LEU A 1 179 ? -12.442 11.867  11.847  1.00 46.45  ?  179 LEU A CD1 1 
ATOM   1345 C CD2 . LEU A 1 179 ? -12.063 11.283  9.460   1.00 46.14  ?  179 LEU A CD2 1 
ATOM   1346 N N   . SER A 1 180 ? -9.276  13.225  8.625   1.00 42.42  ?  180 SER A N   1 
ATOM   1347 C CA  . SER A 1 180 ? -8.618  12.384  7.640   1.00 48.07  ?  180 SER A CA  1 
ATOM   1348 C C   . SER A 1 180 ? -8.420  11.001  8.239   1.00 46.68  ?  180 SER A C   1 
ATOM   1349 O O   . SER A 1 180 ? -8.108  10.865  9.426   1.00 45.43  ?  180 SER A O   1 
ATOM   1350 C CB  . SER A 1 180 ? -7.273  12.970  7.182   1.00 48.25  ?  180 SER A CB  1 
ATOM   1351 O OG  . SER A 1 180 ? -6.288  12.879  8.201   1.00 61.25  ?  180 SER A OG  1 
ATOM   1352 N N   . SER A 1 181 ? -8.648  9.979   7.422   1.00 42.57  ?  181 SER A N   1 
ATOM   1353 C CA  . SER A 1 181 ? -8.434  8.594   7.806   1.00 44.12  ?  181 SER A CA  1 
ATOM   1354 C C   . SER A 1 181 ? -7.503  7.963   6.785   1.00 43.07  ?  181 SER A C   1 
ATOM   1355 O O   . SER A 1 181 ? -7.694  8.133   5.579   1.00 43.89  ?  181 SER A O   1 
ATOM   1356 C CB  . SER A 1 181 ? -9.757  7.828   7.881   1.00 47.45  ?  181 SER A CB  1 
ATOM   1357 O OG  . SER A 1 181 ? -9.571  6.535   8.426   1.00 47.13  ?  181 SER A OG  1 
ATOM   1358 N N   . THR A 1 182 ? -6.484  7.259   7.258   1.00 43.26  ?  182 THR A N   1 
ATOM   1359 C CA  . THR A 1 182 ? -5.484  6.662   6.384   1.00 44.92  ?  182 THR A CA  1 
ATOM   1360 C C   . THR A 1 182 ? -5.447  5.163   6.637   1.00 44.41  ?  182 THR A C   1 
ATOM   1361 O O   . THR A 1 182 ? -5.312  4.728   7.784   1.00 44.64  ?  182 THR A O   1 
ATOM   1362 C CB  . THR A 1 182 ? -4.099  7.290   6.606   1.00 40.91  ?  182 THR A CB  1 
ATOM   1363 O OG1 . THR A 1 182 ? -4.181  8.707   6.409   1.00 47.79  ?  182 THR A OG1 1 
ATOM   1364 C CG2 . THR A 1 182 ? -3.098  6.735   5.612   1.00 40.87  ?  182 THR A CG2 1 
ATOM   1365 N N   . LEU A 1 183 ? -5.610  4.384   5.571   1.00 42.77  ?  183 LEU A N   1 
ATOM   1366 C CA  . LEU A 1 183 ? -5.504  2.932   5.606   1.00 44.09  ?  183 LEU A CA  1 
ATOM   1367 C C   . LEU A 1 183 ? -4.236  2.510   4.877   1.00 45.68  ?  183 LEU A C   1 
ATOM   1368 O O   . LEU A 1 183 ? -4.041  2.877   3.714   1.00 47.77  ?  183 LEU A O   1 
ATOM   1369 C CB  . LEU A 1 183 ? -6.730  2.289   4.954   1.00 43.76  ?  183 LEU A CB  1 
ATOM   1370 C CG  . LEU A 1 183 ? -6.750  0.775   4.759   1.00 43.04  ?  183 LEU A CG  1 
ATOM   1371 C CD1 . LEU A 1 183 ? -7.167  0.088   6.042   1.00 45.06  ?  183 LEU A CD1 1 
ATOM   1372 C CD2 . LEU A 1 183 ? -7.692  0.413   3.627   1.00 38.62  ?  183 LEU A CD2 1 
ATOM   1373 N N   . THR A 1 184 ? -3.380  1.739   5.547   1.00 47.26  ?  184 THR A N   1 
ATOM   1374 C CA  . THR A 1 184 ? -2.094  1.348   4.981   1.00 46.43  ?  184 THR A CA  1 
ATOM   1375 C C   . THR A 1 184 ? -1.985  -0.168  4.868   1.00 50.94  ?  184 THR A C   1 
ATOM   1376 O O   . THR A 1 184 ? -2.184  -0.891  5.849   1.00 48.54  ?  184 THR A O   1 
ATOM   1377 C CB  . THR A 1 184 ? -0.936  1.898   5.816   1.00 50.91  ?  184 THR A CB  1 
ATOM   1378 O OG1 . THR A 1 184 ? -1.116  3.308   6.010   1.00 61.28  ?  184 THR A OG1 1 
ATOM   1379 C CG2 . THR A 1 184 ? 0.387   1.664   5.100   1.00 51.38  ?  184 THR A CG2 1 
ATOM   1380 N N   . LEU A 1 185 ? -1.639  -0.635  3.673   1.00 45.92  ?  185 LEU A N   1 
ATOM   1381 C CA  . LEU A 1 185 ? -1.415  -2.037  3.374   1.00 47.31  ?  185 LEU A CA  1 
ATOM   1382 C C   . LEU A 1 185 ? -0.055  -2.183  2.713   1.00 54.12  ?  185 LEU A C   1 
ATOM   1383 O O   . LEU A 1 185 ? 0.591   -1.200  2.345   1.00 50.66  ?  185 LEU A O   1 
ATOM   1384 C CB  . LEU A 1 185 ? -2.490  -2.602  2.441   1.00 46.74  ?  185 LEU A CB  1 
ATOM   1385 C CG  . LEU A 1 185 ? -3.931  -2.292  2.804   1.00 51.00  ?  185 LEU A CG  1 
ATOM   1386 C CD1 . LEU A 1 185 ? -4.844  -2.779  1.700   1.00 54.33  ?  185 LEU A CD1 1 
ATOM   1387 C CD2 . LEU A 1 185 ? -4.275  -2.944  4.127   1.00 53.00  ?  185 LEU A CD2 1 
ATOM   1388 N N   . SER A 1 186 ? 0.383   -3.429  2.573   1.00 52.85  ?  186 SER A N   1 
ATOM   1389 C CA  . SER A 1 186 ? 1.495   -3.705  1.685   1.00 49.98  ?  186 SER A CA  1 
ATOM   1390 C C   . SER A 1 186 ? 1.035   -3.593  0.234   1.00 51.08  ?  186 SER A C   1 
ATOM   1391 O O   . SER A 1 186 ? -0.157  -3.657  -0.072  1.00 53.01  ?  186 SER A O   1 
ATOM   1392 C CB  . SER A 1 186 ? 2.050   -5.099  1.945   1.00 53.97  ?  186 SER A CB  1 
ATOM   1393 O OG  . SER A 1 186 ? 1.125   -6.078  1.513   1.00 60.86  ?  186 SER A OG  1 
ATOM   1394 N N   . LYS A 1 187 ? 2.001   -3.409  -0.668  1.00 54.00  ?  187 LYS A N   1 
ATOM   1395 C CA  . LYS A 1 187 ? 1.682   -3.380  -2.093  1.00 55.08  ?  187 LYS A CA  1 
ATOM   1396 C C   . LYS A 1 187 ? 0.998   -4.671  -2.534  1.00 54.46  ?  187 LYS A C   1 
ATOM   1397 O O   . LYS A 1 187 ? 0.032   -4.638  -3.307  1.00 56.97  ?  187 LYS A O   1 
ATOM   1398 C CB  . LYS A 1 187 ? 2.956   -3.140  -2.907  1.00 57.05  ?  187 LYS A CB  1 
ATOM   1399 C CG  . LYS A 1 187 ? 2.767   -3.183  -4.420  1.00 59.54  ?  187 LYS A CG  1 
ATOM   1400 C CD  . LYS A 1 187 ? 4.114   -3.154  -5.140  1.00 61.84  ?  187 LYS A CD  1 
ATOM   1401 C CE  . LYS A 1 187 ? 3.954   -3.213  -6.654  1.00 66.02  ?  187 LYS A CE  1 
ATOM   1402 N NZ  . LYS A 1 187 ? 3.472   -4.543  -7.122  1.00 69.44  ?  187 LYS A NZ  1 
ATOM   1403 N N   . ALA A 1 188 ? 1.467   -5.815  -2.031  1.00 50.44  ?  188 ALA A N   1 
ATOM   1404 C CA  . ALA A 1 188 ? 0.875   -7.094  -2.412  1.00 57.20  ?  188 ALA A CA  1 
ATOM   1405 C C   . ALA A 1 188 ? -0.593  -7.162  -2.008  1.00 64.09  ?  188 ALA A C   1 
ATOM   1406 O O   . ALA A 1 188 ? -1.461  -7.516  -2.820  1.00 66.52  ?  188 ALA A O   1 
ATOM   1407 C CB  . ALA A 1 188 ? 1.662   -8.241  -1.781  1.00 60.29  ?  188 ALA A CB  1 
ATOM   1408 N N   . ASP A 1 189 ? -0.884  -6.841  -0.744  1.00 62.90  ?  189 ASP A N   1 
ATOM   1409 C CA  . ASP A 1 189 ? -2.266  -6.812  -0.278  1.00 59.49  ?  189 ASP A CA  1 
ATOM   1410 C C   . ASP A 1 189 ? -3.111  -5.886  -1.141  1.00 56.69  ?  189 ASP A C   1 
ATOM   1411 O O   . ASP A 1 189 ? -4.204  -6.254  -1.583  1.00 61.57  ?  189 ASP A O   1 
ATOM   1412 C CB  . ASP A 1 189 ? -2.319  -6.359  1.181   1.00 63.14  ?  189 ASP A CB  1 
ATOM   1413 C CG  . ASP A 1 189 ? -1.654  -7.337  2.124   1.00 71.65  ?  189 ASP A CG  1 
ATOM   1414 O OD1 . ASP A 1 189 ? -1.267  -8.439  1.675   1.00 73.38  ?  189 ASP A OD1 1 
ATOM   1415 O OD2 . ASP A 1 189 ? -1.511  -6.991  3.319   1.00 76.27  ?  189 ASP A OD2 1 
ATOM   1416 N N   . TYR A 1 190 ? -2.601  -4.683  -1.414  1.00 55.23  ?  190 TYR A N   1 
ATOM   1417 C CA  . TYR A 1 190 ? -3.363  -3.715  -2.194  1.00 56.20  ?  190 TYR A CA  1 
ATOM   1418 C C   . TYR A 1 190 ? -3.689  -4.259  -3.576  1.00 58.00  ?  190 TYR A C   1 
ATOM   1419 O O   . TYR A 1 190 ? -4.788  -4.034  -4.096  1.00 56.56  ?  190 TYR A O   1 
ATOM   1420 C CB  . TYR A 1 190 ? -2.597  -2.399  -2.300  1.00 48.01  ?  190 TYR A CB  1 
ATOM   1421 C CG  . TYR A 1 190 ? -3.289  -1.375  -3.159  1.00 48.64  ?  190 TYR A CG  1 
ATOM   1422 C CD1 . TYR A 1 190 ? -4.430  -0.719  -2.706  1.00 45.88  ?  190 TYR A CD1 1 
ATOM   1423 C CD2 . TYR A 1 190 ? -2.801  -1.053  -4.419  1.00 50.57  ?  190 TYR A CD2 1 
ATOM   1424 C CE1 . TYR A 1 190 ? -5.073  0.223   -3.493  1.00 44.97  ?  190 TYR A CE1 1 
ATOM   1425 C CE2 . TYR A 1 190 ? -3.431  -0.109  -5.212  1.00 47.18  ?  190 TYR A CE2 1 
ATOM   1426 C CZ  . TYR A 1 190 ? -4.567  0.527   -4.744  1.00 48.18  ?  190 TYR A CZ  1 
ATOM   1427 O OH  . TYR A 1 190 ? -5.202  1.463   -5.531  1.00 51.52  ?  190 TYR A OH  1 
ATOM   1428 N N   . GLU A 1 191 ? -2.748  -4.977  -4.189  1.00 63.08  ?  191 GLU A N   1 
ATOM   1429 C CA  . GLU A 1 191 ? -3.000  -5.550  -5.505  1.00 62.42  ?  191 GLU A CA  1 
ATOM   1430 C C   . GLU A 1 191 ? -3.825  -6.830  -5.447  1.00 57.88  ?  191 GLU A C   1 
ATOM   1431 O O   . GLU A 1 191 ? -4.234  -7.325  -6.502  1.00 61.39  ?  191 GLU A O   1 
ATOM   1432 C CB  . GLU A 1 191 ? -1.679  -5.831  -6.223  1.00 61.81  ?  191 GLU A CB  1 
ATOM   1433 C CG  . GLU A 1 191 ? -0.805  -4.610  -6.431  1.00 67.20  ?  191 GLU A CG  1 
ATOM   1434 C CD  . GLU A 1 191 ? 0.420   -4.910  -7.282  1.00 82.31  ?  191 GLU A CD  1 
ATOM   1435 O OE1 . GLU A 1 191 ? 0.862   -4.011  -8.035  1.00 86.11  ?  191 GLU A OE1 1 
ATOM   1436 O OE2 . GLU A 1 191 ? 0.951   -6.042  -7.182  1.00 70.16  ?  191 GLU A OE2 1 
ATOM   1437 N N   . LYS A 1 192 ? -4.074  -7.381  -4.254  1.00 59.57  ?  192 LYS A N   1 
ATOM   1438 C CA  . LYS A 1 192 ? -4.946  -8.549  -4.127  1.00 62.62  ?  192 LYS A CA  1 
ATOM   1439 C C   . LYS A 1 192 ? -6.435  -8.207  -4.091  1.00 62.41  ?  192 LYS A C   1 
ATOM   1440 O O   . LYS A 1 192 ? -7.255  -9.124  -3.965  1.00 62.80  ?  192 LYS A O   1 
ATOM   1441 C CB  . LYS A 1 192 ? -4.621  -9.336  -2.852  1.00 63.78  ?  192 LYS A CB  1 
ATOM   1442 C CG  . LYS A 1 192 ? -3.304  -10.079 -2.832  1.00 66.15  ?  192 LYS A CG  1 
ATOM   1443 C CD  . LYS A 1 192 ? -3.292  -11.070 -1.672  1.00 72.17  ?  192 LYS A CD  1 
ATOM   1444 C CE  . LYS A 1 192 ? -3.708  -10.397 -0.366  1.00 76.63  ?  192 LYS A CE  1 
ATOM   1445 N NZ  . LYS A 1 192 ? -3.814  -11.350 0.779   1.00 88.89  ?  192 LYS A NZ  1 
ATOM   1446 N N   . HIS A 1 193 ? -6.812  -6.933  -4.196  1.00 63.75  ?  193 HIS A N   1 
ATOM   1447 C CA  . HIS A 1 193 ? -8.195  -6.528  -3.982  1.00 57.21  ?  193 HIS A CA  1 
ATOM   1448 C C   . HIS A 1 193 ? -8.590  -5.435  -4.965  1.00 61.01  ?  193 HIS A C   1 
ATOM   1449 O O   . HIS A 1 193 ? -7.741  -4.732  -5.523  1.00 54.67  ?  193 HIS A O   1 
ATOM   1450 C CB  . HIS A 1 193 ? -8.414  -6.051  -2.545  1.00 55.83  ?  193 HIS A CB  1 
ATOM   1451 C CG  . HIS A 1 193 ? -8.124  -7.091  -1.507  1.00 63.49  ?  193 HIS A CG  1 
ATOM   1452 N ND1 . HIS A 1 193 ? -8.894  -8.226  -1.356  1.00 64.42  ?  193 HIS A ND1 1 
ATOM   1453 C CD2 . HIS A 1 193 ? -7.159  -7.164  -0.560  1.00 60.44  ?  193 HIS A CD2 1 
ATOM   1454 C CE1 . HIS A 1 193 ? -8.412  -8.956  -0.366  1.00 65.13  ?  193 HIS A CE1 1 
ATOM   1455 N NE2 . HIS A 1 193 ? -7.359  -8.335  0.134   1.00 64.15  ?  193 HIS A NE2 1 
ATOM   1456 N N   . LYS A 1 194 ? -9.906  -5.281  -5.151  1.00 56.53  ?  194 LYS A N   1 
ATOM   1457 C CA  . LYS A 1 194 ? -10.445 -4.410  -6.188  1.00 56.60  ?  194 LYS A CA  1 
ATOM   1458 C C   . LYS A 1 194 ? -11.139 -3.177  -5.623  1.00 58.24  ?  194 LYS A C   1 
ATOM   1459 O O   . LYS A 1 194 ? -10.762 -2.050  -5.956  1.00 61.71  ?  194 LYS A O   1 
ATOM   1460 C CB  . LYS A 1 194 ? -11.407 -5.202  -7.088  1.00 56.52  ?  194 LYS A CB  1 
ATOM   1461 C CG  . LYS A 1 194 ? -11.790 -4.476  -8.371  1.00 64.45  ?  194 LYS A CG  1 
ATOM   1462 C CD  . LYS A 1 194 ? -12.659 -5.340  -9.284  1.00 79.16  ?  194 LYS A CD  1 
ATOM   1463 C CE  . LYS A 1 194 ? -14.150 -5.103  -9.057  1.00 89.16  ?  194 LYS A CE  1 
ATOM   1464 N NZ  . LYS A 1 194 ? -14.987 -5.608  -10.189 1.00 77.34  ?  194 LYS A NZ  1 
ATOM   1465 N N   . VAL A 1 195 ? -12.157 -3.351  -4.788  1.00 58.31  ?  195 VAL A N   1 
ATOM   1466 C CA  . VAL A 1 195 ? -13.008 -2.248  -4.351  1.00 59.92  ?  195 VAL A CA  1 
ATOM   1467 C C   . VAL A 1 195 ? -12.539 -1.756  -2.989  1.00 56.66  ?  195 VAL A C   1 
ATOM   1468 O O   . VAL A 1 195 ? -12.418 -2.543  -2.041  1.00 51.89  ?  195 VAL A O   1 
ATOM   1469 C CB  . VAL A 1 195 ? -14.488 -2.666  -4.312  1.00 55.13  ?  195 VAL A CB  1 
ATOM   1470 C CG1 . VAL A 1 195 ? -15.351 -1.520  -3.814  1.00 52.80  ?  195 VAL A CG1 1 
ATOM   1471 C CG2 . VAL A 1 195 ? -14.946 -3.088  -5.691  1.00 58.89  ?  195 VAL A CG2 1 
ATOM   1472 N N   . TYR A 1 196 ? -12.294 -0.451  -2.885  1.00 56.59  ?  196 TYR A N   1 
ATOM   1473 C CA  . TYR A 1 196 ? -11.879 0.180   -1.640  1.00 57.77  ?  196 TYR A CA  1 
ATOM   1474 C C   . TYR A 1 196 ? -12.892 1.254   -1.278  1.00 52.31  ?  196 TYR A C   1 
ATOM   1475 O O   . TYR A 1 196 ? -13.285 2.047   -2.139  1.00 56.81  ?  196 TYR A O   1 
ATOM   1476 C CB  . TYR A 1 196 ? -10.467 0.773   -1.769  1.00 52.79  ?  196 TYR A CB  1 
ATOM   1477 C CG  . TYR A 1 196 ? -9.388  -0.284  -1.840  1.00 50.31  ?  196 TYR A CG  1 
ATOM   1478 C CD1 . TYR A 1 196 ? -8.661  -0.632  -0.712  1.00 47.12  ?  196 TYR A CD1 1 
ATOM   1479 C CD2 . TYR A 1 196 ? -9.120  -0.957  -3.024  1.00 49.13  ?  196 TYR A CD2 1 
ATOM   1480 C CE1 . TYR A 1 196 ? -7.686  -1.605  -0.765  1.00 48.82  ?  196 TYR A CE1 1 
ATOM   1481 C CE2 . TYR A 1 196 ? -8.148  -1.932  -3.086  1.00 48.41  ?  196 TYR A CE2 1 
ATOM   1482 C CZ  . TYR A 1 196 ? -7.432  -2.254  -1.953  1.00 52.55  ?  196 TYR A CZ  1 
ATOM   1483 O OH  . TYR A 1 196 ? -6.457  -3.227  -2.002  1.00 52.89  ?  196 TYR A OH  1 
ATOM   1484 N N   . ALA A 1 197 ? -13.317 1.282   -0.013  1.00 46.40  ?  197 ALA A N   1 
ATOM   1485 C CA  . ALA A 1 197 ? -14.360 2.212   0.403   1.00 53.77  ?  197 ALA A CA  1 
ATOM   1486 C C   . ALA A 1 197 ? -14.193 2.608   1.862   1.00 49.33  ?  197 ALA A C   1 
ATOM   1487 O O   . ALA A 1 197 ? -13.884 1.768   2.713   1.00 48.33  ?  197 ALA A O   1 
ATOM   1488 C CB  . ALA A 1 197 ? -15.756 1.613   0.206   1.00 50.25  ?  197 ALA A CB  1 
ATOM   1489 N N   . CYS A 1 198 ? -14.416 3.892   2.140   1.00 43.55  ?  198 CYS A N   1 
ATOM   1490 C CA  . CYS A 1 198 ? -14.547 4.383   3.504   1.00 49.91  ?  198 CYS A CA  1 
ATOM   1491 C C   . CYS A 1 198 ? -15.985 4.816   3.734   1.00 49.61  ?  198 CYS A C   1 
ATOM   1492 O O   . CYS A 1 198 ? -16.593 5.478   2.883   1.00 48.72  ?  198 CYS A O   1 
ATOM   1493 C CB  . CYS A 1 198 ? -13.582 5.543   3.822   1.00 48.61  ?  198 CYS A CB  1 
ATOM   1494 S SG  . CYS A 1 198 ? -13.725 7.034   2.809   1.00 73.16  ?  198 CYS A SG  1 
ATOM   1495 N N   . GLU A 1 199 ? -16.519 4.422   4.887   1.00 50.56  ?  199 GLU A N   1 
ATOM   1496 C CA  . GLU A 1 199 ? -17.903 4.668   5.265   1.00 54.76  ?  199 GLU A CA  1 
ATOM   1497 C C   . GLU A 1 199 ? -17.913 5.572   6.487   1.00 48.69  ?  199 GLU A C   1 
ATOM   1498 O O   . GLU A 1 199 ? -17.299 5.250   7.509   1.00 51.45  ?  199 GLU A O   1 
ATOM   1499 C CB  . GLU A 1 199 ? -18.639 3.351   5.529   1.00 57.27  ?  199 GLU A CB  1 
ATOM   1500 C CG  . GLU A 1 199 ? -19.819 3.447   6.484   1.00 57.15  ?  199 GLU A CG  1 
ATOM   1501 C CD  . GLU A 1 199 ? -20.561 2.124   6.633   1.00 75.11  ?  199 GLU A CD  1 
ATOM   1502 O OE1 . GLU A 1 199 ? -21.011 1.574   5.603   1.00 74.67  ?  199 GLU A OE1 1 
ATOM   1503 O OE2 . GLU A 1 199 ? -20.661 1.613   7.771   1.00 80.99  ?  199 GLU A OE2 1 
ATOM   1504 N N   . VAL A 1 200 ? -18.587 6.710   6.361   1.00 46.25  ?  200 VAL A N   1 
ATOM   1505 C CA  . VAL A 1 200 ? -18.716 7.718   7.403   1.00 51.53  ?  200 VAL A CA  1 
ATOM   1506 C C   . VAL A 1 200 ? -20.122 7.635   7.975   1.00 49.48  ?  200 VAL A C   1 
ATOM   1507 O O   . VAL A 1 200 ? -21.101 7.603   7.223   1.00 42.11  ?  200 VAL A O   1 
ATOM   1508 C CB  . VAL A 1 200 ? -18.454 9.127   6.843   1.00 49.42  ?  200 VAL A CB  1 
ATOM   1509 C CG1 . VAL A 1 200 ? -18.602 10.171  7.937   1.00 43.79  ?  200 VAL A CG1 1 
ATOM   1510 C CG2 . VAL A 1 200 ? -17.098 9.188   6.175   1.00 50.36  ?  200 VAL A CG2 1 
ATOM   1511 N N   . THR A 1 201 ? -20.230 7.616   9.298   1.00 50.72  ?  201 THR A N   1 
ATOM   1512 C CA  . THR A 1 201 ? -21.530 7.584   9.949   1.00 53.34  ?  201 THR A CA  1 
ATOM   1513 C C   . THR A 1 201 ? -21.617 8.715   10.957  1.00 52.75  ?  201 THR A C   1 
ATOM   1514 O O   . THR A 1 201 ? -20.697 8.913   11.757  1.00 55.81  ?  201 THR A O   1 
ATOM   1515 C CB  . THR A 1 201 ? -21.790 6.242   10.652  1.00 57.42  ?  201 THR A CB  1 
ATOM   1516 O OG1 . THR A 1 201 ? -21.673 5.165   9.713   1.00 55.57  ?  201 THR A OG1 1 
ATOM   1517 C CG2 . THR A 1 201 ? -23.192 6.230   11.262  1.00 49.68  ?  201 THR A CG2 1 
ATOM   1518 N N   . GLN A 1 202 ? -22.710 9.467   10.904  1.00 55.02  ?  202 GLN A N   1 
ATOM   1519 C CA  . GLN A 1 202 ? -23.011 10.384  11.992  1.00 57.73  ?  202 GLN A CA  1 
ATOM   1520 C C   . GLN A 1 202 ? -24.523 10.456  12.136  1.00 57.24  ?  202 GLN A C   1 
ATOM   1521 O O   . GLN A 1 202 ? -25.248 10.584  11.141  1.00 53.20  ?  202 GLN A O   1 
ATOM   1522 C CB  . GLN A 1 202 ? -22.391 11.777  11.784  1.00 58.49  ?  202 GLN A CB  1 
ATOM   1523 C CG  . GLN A 1 202 ? -22.909 12.620  10.625  1.00 59.81  ?  202 GLN A CG  1 
ATOM   1524 C CD  . GLN A 1 202 ? -22.431 14.071  10.726  1.00 68.21  ?  202 GLN A CD  1 
ATOM   1525 O OE1 . GLN A 1 202 ? -21.529 14.386  11.510  1.00 68.03  ?  202 GLN A OE1 1 
ATOM   1526 N NE2 . GLN A 1 202 ? -23.045 14.961  9.946   1.00 55.55  ?  202 GLN A NE2 1 
ATOM   1527 N N   . GLY A 1 203 ? -24.984 10.338  13.376  1.00 61.35  ?  203 GLY A N   1 
ATOM   1528 C CA  . GLY A 1 203 ? -26.412 10.300  13.627  1.00 59.12  ?  203 GLY A CA  1 
ATOM   1529 C C   . GLY A 1 203 ? -27.054 9.152   12.877  1.00 60.06  ?  203 GLY A C   1 
ATOM   1530 O O   . GLY A 1 203 ? -26.639 7.992   12.980  1.00 56.29  ?  203 GLY A O   1 
ATOM   1531 N N   . THR A 1 204 ? -28.072 9.483   12.093  1.00 60.24  ?  204 THR A N   1 
ATOM   1532 C CA  . THR A 1 204 ? -28.831 8.515   11.318  1.00 59.19  ?  204 THR A CA  1 
ATOM   1533 C C   . THR A 1 204 ? -28.300 8.341   9.904   1.00 56.78  ?  204 THR A C   1 
ATOM   1534 O O   . THR A 1 204 ? -28.935 7.648   9.104   1.00 57.87  ?  204 THR A O   1 
ATOM   1535 C CB  . THR A 1 204 ? -30.303 8.933   11.261  1.00 65.29  ?  204 THR A CB  1 
ATOM   1536 O OG1 . THR A 1 204 ? -30.400 10.293  10.800  1.00 64.98  ?  204 THR A OG1 1 
ATOM   1537 C CG2 . THR A 1 204 ? -30.954 8.802   12.634  1.00 65.42  ?  204 THR A CG2 1 
ATOM   1538 N N   . THR A 1 205 ? -27.170 8.955   9.570   1.00 55.20  ?  205 THR A N   1 
ATOM   1539 C CA  . THR A 1 205 ? -26.700 9.001   8.194   1.00 56.17  ?  205 THR A CA  1 
ATOM   1540 C C   . THR A 1 205 ? -25.405 8.210   8.062   1.00 52.40  ?  205 THR A C   1 
ATOM   1541 O O   . THR A 1 205 ? -24.561 8.220   8.966   1.00 56.97  ?  205 THR A O   1 
ATOM   1542 C CB  . THR A 1 205 ? -26.478 10.448  7.735   1.00 57.62  ?  205 THR A CB  1 
ATOM   1543 O OG1 . THR A 1 205 ? -27.663 11.212  7.973   1.00 58.24  ?  205 THR A OG1 1 
ATOM   1544 C CG2 . THR A 1 205 ? -26.158 10.499  6.247   1.00 54.46  ?  205 THR A CG2 1 
ATOM   1545 N N   . SER A 1 206 ? -25.282 7.492   6.945   1.00 49.96  ?  206 SER A N   1 
ATOM   1546 C CA  . SER A 1 206 ? -24.048 6.842   6.524   1.00 49.72  ?  206 SER A CA  1 
ATOM   1547 C C   . SER A 1 206 ? -23.776 7.214   5.076   1.00 48.14  ?  206 SER A C   1 
ATOM   1548 O O   . SER A 1 206 ? -24.684 7.159   4.242   1.00 51.95  ?  206 SER A O   1 
ATOM   1549 C CB  . SER A 1 206 ? -24.130 5.319   6.665   1.00 47.13  ?  206 SER A CB  1 
ATOM   1550 O OG  . SER A 1 206 ? -23.991 4.931   8.018   1.00 51.01  ?  206 SER A OG  1 
ATOM   1551 N N   . VAL A 1 207 ? -22.545 7.622   4.790   1.00 45.69  ?  207 VAL A N   1 
ATOM   1552 C CA  . VAL A 1 207 ? -22.091 7.941   3.442   1.00 45.77  ?  207 VAL A CA  1 
ATOM   1553 C C   . VAL A 1 207 ? -20.888 7.062   3.133   1.00 48.37  ?  207 VAL A C   1 
ATOM   1554 O O   . VAL A 1 207 ? -19.957 6.981   3.936   1.00 45.65  ?  207 VAL A O   1 
ATOM   1555 C CB  . VAL A 1 207 ? -21.727 9.428   3.302   1.00 43.36  ?  207 VAL A CB  1 
ATOM   1556 C CG1 . VAL A 1 207 ? -21.280 9.724   1.884   1.00 50.28  ?  207 VAL A CG1 1 
ATOM   1557 C CG2 . VAL A 1 207 ? -22.900 10.301  3.694   1.00 44.71  ?  207 VAL A CG2 1 
ATOM   1558 N N   . THR A 1 208 ? -20.898 6.407   1.980   1.00 51.29  ?  208 THR A N   1 
ATOM   1559 C CA  . THR A 1 208 ? -19.826 5.486   1.619   1.00 49.91  ?  208 THR A CA  1 
ATOM   1560 C C   . THR A 1 208 ? -19.204 5.910   0.297   1.00 54.37  ?  208 THR A C   1 
ATOM   1561 O O   . THR A 1 208 ? -19.881 5.918   -0.738  1.00 55.44  ?  208 THR A O   1 
ATOM   1562 C CB  . THR A 1 208 ? -20.344 4.053   1.540   1.00 48.51  ?  208 THR A CB  1 
ATOM   1563 O OG1 . THR A 1 208 ? -20.688 3.613   2.858   1.00 53.77  ?  208 THR A OG1 1 
ATOM   1564 C CG2 . THR A 1 208 ? -19.282 3.137   0.965   1.00 52.83  ?  208 THR A CG2 1 
ATOM   1565 N N   . LYS A 1 209 ? -17.909 6.233   0.331   1.00 56.69  ?  209 LYS A N   1 
ATOM   1566 C CA  . LYS A 1 209 ? -17.161 6.629   -0.855  1.00 48.72  ?  209 LYS A CA  1 
ATOM   1567 C C   . LYS A 1 209 ? -16.186 5.519   -1.219  1.00 49.98  ?  209 LYS A C   1 
ATOM   1568 O O   . LYS A 1 209 ? -15.533 4.942   -0.343  1.00 52.63  ?  209 LYS A O   1 
ATOM   1569 C CB  . LYS A 1 209 ? -16.416 7.948   -0.619  1.00 50.12  ?  209 LYS A CB  1 
ATOM   1570 C CG  . LYS A 1 209 ? -16.251 8.829   -1.860  1.00 55.45  ?  209 LYS A CG  1 
ATOM   1571 C CD  . LYS A 1 209 ? -17.588 9.409   -2.317  1.00 62.46  ?  209 LYS A CD  1 
ATOM   1572 C CE  . LYS A 1 209 ? -17.430 10.737  -3.072  1.00 62.72  ?  209 LYS A CE  1 
ATOM   1573 N NZ  . LYS A 1 209 ? -16.755 10.611  -4.396  1.00 65.74  ?  209 LYS A NZ  1 
ATOM   1574 N N   . SER A 1 210 ? -16.103 5.204   -2.511  1.00 49.81  ?  210 SER A N   1 
ATOM   1575 C CA  . SER A 1 210 ? -15.350 4.043   -2.961  1.00 51.46  ?  210 SER A CA  1 
ATOM   1576 C C   . SER A 1 210 ? -14.639 4.323   -4.281  1.00 54.16  ?  210 SER A C   1 
ATOM   1577 O O   . SER A 1 210 ? -14.854 5.348   -4.936  1.00 57.01  ?  210 SER A O   1 
ATOM   1578 C CB  . SER A 1 210 ? -16.265 2.830   -3.120  1.00 46.66  ?  210 SER A CB  1 
ATOM   1579 O OG  . SER A 1 210 ? -17.301 3.125   -4.035  1.00 56.90  ?  210 SER A OG  1 
ATOM   1580 N N   . PHE A 1 211 ? -13.765 3.387   -4.649  1.00 52.65  ?  211 PHE A N   1 
ATOM   1581 C CA  . PHE A 1 211 ? -13.162 3.337   -5.974  1.00 56.00  ?  211 PHE A CA  1 
ATOM   1582 C C   . PHE A 1 211 ? -12.775 1.895   -6.285  1.00 58.18  ?  211 PHE A C   1 
ATOM   1583 O O   . PHE A 1 211 ? -12.538 1.086   -5.379  1.00 58.81  ?  211 PHE A O   1 
ATOM   1584 C CB  . PHE A 1 211 ? -11.943 4.273   -6.115  1.00 50.19  ?  211 PHE A CB  1 
ATOM   1585 C CG  . PHE A 1 211 ? -10.723 3.839   -5.337  1.00 53.57  ?  211 PHE A CG  1 
ATOM   1586 C CD1 . PHE A 1 211 ? -10.481 4.336   -4.064  1.00 52.37  ?  211 PHE A CD1 1 
ATOM   1587 C CD2 . PHE A 1 211 ? -9.795  2.965   -5.894  1.00 54.37  ?  211 PHE A CD2 1 
ATOM   1588 C CE1 . PHE A 1 211 ? -9.353  3.950   -3.348  1.00 48.83  ?  211 PHE A CE1 1 
ATOM   1589 C CE2 . PHE A 1 211 ? -8.666  2.574   -5.184  1.00 51.45  ?  211 PHE A CE2 1 
ATOM   1590 C CZ  . PHE A 1 211 ? -8.445  3.070   -3.909  1.00 46.56  ?  211 PHE A CZ  1 
ATOM   1591 N N   . ASN A 1 212 ? -12.731 1.574   -7.576  1.00 63.45  ?  212 ASN A N   1 
ATOM   1592 C CA  . ASN A 1 212 ? -12.352 0.218   -8.025  1.00 58.89  ?  212 ASN A CA  1 
ATOM   1593 C C   . ASN A 1 212 ? -11.003 0.300   -8.721  1.00 61.73  ?  212 ASN A C   1 
ATOM   1594 O O   . ASN A 1 212 ? -10.890 1.051   -9.680  1.00 66.25  ?  212 ASN A O   1 
ATOM   1595 C CB  . ASN A 1 212 ? -13.398 -0.359  -8.965  1.00 65.43  ?  212 ASN A CB  1 
ATOM   1596 C CG  . ASN A 1 212 ? -14.766 -0.476  -8.336  1.00 73.39  ?  212 ASN A CG  1 
ATOM   1597 O OD1 . ASN A 1 212 ? -14.961 -0.102  -7.183  1.00 76.67  ?  212 ASN A OD1 1 
ATOM   1598 N ND2 . ASN A 1 212 ? -15.722 -0.991  -9.089  1.00 81.04  ?  212 ASN A ND2 1 
ATOM   1599 N N   . ARG A 1 213 ? -10.027 -0.450  -8.218  1.00 65.89  ?  213 ARG A N   1 
ATOM   1600 C CA  . ARG A 1 213 ? -8.659  -0.447  -8.792  1.00 66.48  ?  213 ARG A CA  1 
ATOM   1601 C C   . ARG A 1 213 ? -8.734  -0.709  -10.293 1.00 71.41  ?  213 ARG A C   1 
ATOM   1602 O O   . ARG A 1 213 ? -9.565  -1.526  -10.715 1.00 71.92  ?  213 ARG A O   1 
ATOM   1603 C CB  . ARG A 1 213 ? -7.783  -1.467  -8.068  1.00 57.61  ?  213 ARG A CB  1 
ATOM   1604 C CG  . ARG A 1 213 ? -7.305  -1.009  -6.700  1.00 58.70  ?  213 ARG A CG  1 
ATOM   1605 C CD  . ARG A 1 213 ? -6.342  -2.004  -6.090  1.00 59.93  ?  213 ARG A CD  1 
ATOM   1606 N NE  . ARG A 1 213 ? -5.251  -2.340  -6.987  1.00 57.75  ?  213 ARG A NE  1 
ATOM   1607 C CZ  . ARG A 1 213 ? -5.111  -3.513  -7.587  1.00 60.74  ?  213 ARG A CZ  1 
ATOM   1608 N NH1 . ARG A 1 213 ? -6.000  -4.469  -7.393  1.00 55.22  ?  213 ARG A NH1 1 
ATOM   1609 N NH2 . ARG A 1 213 ? -4.085  -3.728  -8.384  1.00 69.28  ?  213 ARG A NH2 1 
ATOM   1610 N N   . GLY A 1 214 ? -7.893  -0.023  -11.061 1.00 30.00  ?  214 GLY A N   1 
ATOM   1611 C CA  . GLY A 1 214 ? -7.941  -0.150  -12.523 1.00 30.00  ?  214 GLY A CA  1 
ATOM   1612 C C   . GLY A 1 214 ? -9.133  0.182   -13.384 1.00 30.00  ?  214 GLY A C   1 
ATOM   1613 O O   . GLY A 1 214 ? -9.123  -0.200  -14.563 1.00 30.00  ?  214 GLY A O   1 
ATOM   1614 N N   . GLU A 1 215 ? -10.130 0.851   -12.809 1.00 30.00  ?  215 GLU A N   1 
ATOM   1615 C CA  . GLU A 1 215 ? -11.544 0.892   -13.255 1.00 30.00  ?  215 GLU A CA  1 
ATOM   1616 C C   . GLU A 1 215 ? -12.149 2.217   -12.794 1.00 30.00  ?  215 GLU A C   1 
ATOM   1617 O O   . GLU A 1 215 ? -11.378 3.029   -12.255 1.00 30.00  ?  215 GLU A O   1 
ATOM   1618 C CB  . GLU A 1 215 ? -12.313 -0.313  -12.711 1.00 30.00  ?  215 GLU A CB  1 
ATOM   1619 C CG  . GLU A 1 215 ? -11.870 -1.648  -13.283 1.00 30.00  ?  215 GLU A CG  1 
ATOM   1620 C CD  . GLU A 1 215 ? -12.554 -2.886  -12.724 1.00 30.00  ?  215 GLU A CD  1 
ATOM   1621 O OE1 . GLU A 1 215 ? -13.280 -2.756  -11.719 1.00 30.00  ?  215 GLU A OE1 1 
ATOM   1622 O OE2 . GLU A 1 215 ? -12.378 -3.975  -13.309 1.00 30.00  ?  215 GLU A OE2 1 
ATOM   1623 N N   . GLU B 2 1   ? 7.316   45.757  20.485  1.00 80.58  ?  1   GLU B N   1 
ATOM   1624 C CA  . GLU B 2 1   ? 8.506   45.255  19.805  1.00 78.74  ?  1   GLU B CA  1 
ATOM   1625 C C   . GLU B 2 1   ? 9.293   44.283  20.675  1.00 69.64  ?  1   GLU B C   1 
ATOM   1626 O O   . GLU B 2 1   ? 10.266  43.684  20.213  1.00 64.25  ?  1   GLU B O   1 
ATOM   1627 C CB  . GLU B 2 1   ? 9.419   46.406  19.376  1.00 83.84  ?  1   GLU B CB  1 
ATOM   1628 C CG  . GLU B 2 1   ? 8.792   47.381  18.397  1.00 99.89  ?  1   GLU B CG  1 
ATOM   1629 C CD  . GLU B 2 1   ? 9.781   48.423  17.906  1.00 113.68 ?  1   GLU B CD  1 
ATOM   1630 O OE1 . GLU B 2 1   ? 9.415   49.617  17.857  1.00 115.48 ?  1   GLU B OE1 1 
ATOM   1631 O OE2 . GLU B 2 1   ? 10.932  48.048  17.586  1.00 108.98 ?  1   GLU B OE2 1 
ATOM   1632 N N   . VAL B 2 2   ? 8.878   44.124  21.935  1.00 65.56  ?  2   VAL B N   1 
ATOM   1633 C CA  . VAL B 2 2   ? 9.527   43.148  22.800  1.00 56.13  ?  2   VAL B CA  1 
ATOM   1634 C C   . VAL B 2 2   ? 9.134   41.746  22.360  1.00 49.18  ?  2   VAL B C   1 
ATOM   1635 O O   . VAL B 2 2   ? 8.000   41.502  21.925  1.00 52.01  ?  2   VAL B O   1 
ATOM   1636 C CB  . VAL B 2 2   ? 9.152   43.393  24.272  1.00 50.46  ?  2   VAL B CB  1 
ATOM   1637 C CG1 . VAL B 2 2   ? 9.596   44.783  24.704  1.00 47.13  ?  2   VAL B CG1 1 
ATOM   1638 C CG2 . VAL B 2 2   ? 7.662   43.213  24.483  1.00 48.62  ?  2   VAL B CG2 1 
ATOM   1639 N N   . GLN B 2 3   ? 10.074  40.812  22.465  1.00 52.21  ?  3   GLN B N   1 
ATOM   1640 C CA  . GLN B 2 3   ? 9.781   39.432  22.107  1.00 48.33  ?  3   GLN B CA  1 
ATOM   1641 C C   . GLN B 2 3   ? 10.721  38.496  22.854  1.00 44.59  ?  3   GLN B C   1 
ATOM   1642 O O   . GLN B 2 3   ? 11.815  38.880  23.282  1.00 46.16  ?  3   GLN B O   1 
ATOM   1643 C CB  . GLN B 2 3   ? 9.876   39.218  20.591  1.00 49.98  ?  3   GLN B CB  1 
ATOM   1644 C CG  . GLN B 2 3   ? 11.275  39.400  20.014  1.00 61.98  ?  3   GLN B CG  1 
ATOM   1645 C CD  . GLN B 2 3   ? 11.343  39.091  18.527  1.00 63.59  ?  3   GLN B CD  1 
ATOM   1646 O OE1 . GLN B 2 3   ? 10.353  38.675  17.919  1.00 61.70  ?  3   GLN B OE1 1 
ATOM   1647 N NE2 . GLN B 2 3   ? 12.516  39.291  17.935  1.00 63.80  ?  3   GLN B NE2 1 
ATOM   1648 N N   . LEU B 2 4   ? 10.263  37.258  23.014  1.00 46.02  ?  4   LEU B N   1 
ATOM   1649 C CA  . LEU B 2 4   ? 11.044  36.178  23.597  1.00 46.08  ?  4   LEU B CA  1 
ATOM   1650 C C   . LEU B 2 4   ? 11.217  35.094  22.545  1.00 48.41  ?  4   LEU B C   1 
ATOM   1651 O O   . LEU B 2 4   ? 10.228  34.621  21.972  1.00 47.12  ?  4   LEU B O   1 
ATOM   1652 C CB  . LEU B 2 4   ? 10.358  35.608  24.840  1.00 40.84  ?  4   LEU B CB  1 
ATOM   1653 C CG  . LEU B 2 4   ? 10.321  36.479  26.092  1.00 39.74  ?  4   LEU B CG  1 
ATOM   1654 C CD1 . LEU B 2 4   ? 9.304   35.941  27.081  1.00 36.38  ?  4   LEU B CD1 1 
ATOM   1655 C CD2 . LEU B 2 4   ? 11.706  36.527  26.725  1.00 36.63  ?  4   LEU B CD2 1 
ATOM   1656 N N   . VAL B 2 5   ? 12.462  34.711  22.277  1.00 45.33  ?  5   VAL B N   1 
ATOM   1657 C CA  . VAL B 2 5   ? 12.751  33.705  21.259  1.00 52.42  ?  5   VAL B CA  1 
ATOM   1658 C C   . VAL B 2 5   ? 13.515  32.565  21.920  1.00 48.43  ?  5   VAL B C   1 
ATOM   1659 O O   . VAL B 2 5   ? 14.669  32.743  22.330  1.00 46.65  ?  5   VAL B O   1 
ATOM   1660 C CB  . VAL B 2 5   ? 13.544  34.299  20.088  1.00 50.06  ?  5   VAL B CB  1 
ATOM   1661 C CG1 . VAL B 2 5   ? 13.813  33.233  19.038  1.00 50.72  ?  5   VAL B CG1 1 
ATOM   1662 C CG2 . VAL B 2 5   ? 12.793  35.485  19.492  1.00 45.44  ?  5   VAL B CG2 1 
ATOM   1663 N N   . GLU B 2 6   ? 12.880  31.401  22.044  1.00 44.07  ?  6   GLU B N   1 
ATOM   1664 C CA  . GLU B 2 6   ? 13.583  30.259  22.611  1.00 46.11  ?  6   GLU B CA  1 
ATOM   1665 C C   . GLU B 2 6   ? 14.226  29.414  21.519  1.00 46.16  ?  6   GLU B C   1 
ATOM   1666 O O   . GLU B 2 6   ? 13.814  29.416  20.357  1.00 49.18  ?  6   GLU B O   1 
ATOM   1667 C CB  . GLU B 2 6   ? 12.678  29.384  23.488  1.00 41.22  ?  6   GLU B CB  1 
ATOM   1668 C CG  . GLU B 2 6   ? 11.304  29.103  22.961  1.00 45.25  ?  6   GLU B CG  1 
ATOM   1669 C CD  . GLU B 2 6   ? 10.290  30.089  23.488  1.00 48.91  ?  6   GLU B CD  1 
ATOM   1670 O OE1 . GLU B 2 6   ? 10.382  31.275  23.114  1.00 56.08  ?  6   GLU B OE1 1 
ATOM   1671 O OE2 . GLU B 2 6   ? 9.413   29.686  24.287  1.00 44.22  ?  6   GLU B OE2 1 
ATOM   1672 N N   . SER B 2 7   ? 15.268  28.699  21.919  1.00 44.43  ?  7   SER B N   1 
ATOM   1673 C CA  . SER B 2 7   ? 15.967  27.778  21.044  1.00 47.72  ?  7   SER B CA  1 
ATOM   1674 C C   . SER B 2 7   ? 16.593  26.686  21.902  1.00 45.07  ?  7   SER B C   1 
ATOM   1675 O O   . SER B 2 7   ? 16.517  26.705  23.137  1.00 44.57  ?  7   SER B O   1 
ATOM   1676 C CB  . SER B 2 7   ? 17.006  28.513  20.193  1.00 44.75  ?  7   SER B CB  1 
ATOM   1677 O OG  . SER B 2 7   ? 18.228  28.636  20.891  1.00 41.87  ?  7   SER B OG  1 
ATOM   1678 N N   . GLY B 2 8   ? 17.259  25.760  21.240  1.00 43.39  ?  8   GLY B N   1 
ATOM   1679 C CA  . GLY B 2 8   ? 17.519  24.484  21.843  1.00 42.27  ?  8   GLY B CA  1 
ATOM   1680 C C   . GLY B 2 8   ? 16.302  23.618  21.607  1.00 51.54  ?  8   GLY B C   1 
ATOM   1681 O O   . GLY B 2 8   ? 15.406  23.948  20.824  1.00 64.08  ?  8   GLY B O   1 
ATOM   1682 N N   . GLY B 2 9   ? 16.261  22.497  22.300  1.00 42.82  ?  9   GLY B N   1 
ATOM   1683 C CA  . GLY B 2 9   ? 15.123  21.623  22.139  1.00 46.95  ?  9   GLY B CA  1 
ATOM   1684 C C   . GLY B 2 9   ? 15.181  20.871  20.829  1.00 49.70  ?  9   GLY B C   1 
ATOM   1685 O O   . GLY B 2 9   ? 15.651  21.389  19.811  1.00 51.43  ?  9   GLY B O   1 
ATOM   1686 N N   . GLY B 2 10  ? 14.669  19.659  20.845  1.00 42.97  ?  10  GLY B N   1 
ATOM   1687 C CA  . GLY B 2 10  ? 14.853  18.729  19.760  1.00 39.08  ?  10  GLY B CA  1 
ATOM   1688 C C   . GLY B 2 10  ? 14.882  17.324  20.316  1.00 44.03  ?  10  GLY B C   1 
ATOM   1689 O O   . GLY B 2 10  ? 14.390  17.072  21.414  1.00 43.94  ?  10  GLY B O   1 
ATOM   1690 N N   . LEU B 2 11  ? 15.473  16.419  19.542  1.00 41.53  ?  11  LEU B N   1 
ATOM   1691 C CA  . LEU B 2 11  ? 15.547  15.023  19.942  1.00 38.63  ?  11  LEU B CA  1 
ATOM   1692 C C   . LEU B 2 11  ? 16.683  14.848  20.940  1.00 39.17  ?  11  LEU B C   1 
ATOM   1693 O O   . LEU B 2 11  ? 17.826  15.220  20.657  1.00 43.66  ?  11  LEU B O   1 
ATOM   1694 C CB  . LEU B 2 11  ? 15.758  14.144  18.714  1.00 40.16  ?  11  LEU B CB  1 
ATOM   1695 C CG  . LEU B 2 11  ? 15.707  12.630  18.908  1.00 38.52  ?  11  LEU B CG  1 
ATOM   1696 C CD1 . LEU B 2 11  ? 14.498  12.236  19.744  1.00 34.64  ?  11  LEU B CD1 1 
ATOM   1697 C CD2 . LEU B 2 11  ? 15.657  11.954  17.549  1.00 40.50  ?  11  LEU B CD2 1 
ATOM   1698 N N   . VAL B 2 12  ? 16.375  14.294  22.106  1.00 36.18  ?  12  VAL B N   1 
ATOM   1699 C CA  . VAL B 2 12  ? 17.383  14.019  23.124  1.00 38.32  ?  12  VAL B CA  1 
ATOM   1700 C C   . VAL B 2 12  ? 17.119  12.622  23.677  1.00 38.69  ?  12  VAL B C   1 
ATOM   1701 O O   . VAL B 2 12  ? 15.967  12.243  23.913  1.00 42.48  ?  12  VAL B O   1 
ATOM   1702 C CB  . VAL B 2 12  ? 17.374  15.099  24.232  1.00 38.72  ?  12  VAL B CB  1 
ATOM   1703 C CG1 . VAL B 2 12  ? 16.002  15.193  24.889  1.00 39.41  ?  12  VAL B CG1 1 
ATOM   1704 C CG2 . VAL B 2 12  ? 18.458  14.837  25.265  1.00 37.13  ?  12  VAL B CG2 1 
ATOM   1705 N N   . GLN B 2 13  ? 18.183  11.851  23.872  1.00 39.32  ?  13  GLN B N   1 
ATOM   1706 C CA  . GLN B 2 13  ? 18.013  10.498  24.374  1.00 46.40  ?  13  GLN B CA  1 
ATOM   1707 C C   . GLN B 2 13  ? 17.669  10.491  25.859  1.00 44.27  ?  13  GLN B C   1 
ATOM   1708 O O   . GLN B 2 13  ? 18.077  11.383  26.608  1.00 40.58  ?  13  GLN B O   1 
ATOM   1709 C CB  . GLN B 2 13  ? 19.253  9.649   24.120  1.00 45.02  ?  13  GLN B CB  1 
ATOM   1710 C CG  . GLN B 2 13  ? 19.458  9.368   22.656  1.00 57.36  ?  13  GLN B CG  1 
ATOM   1711 C CD  . GLN B 2 13  ? 20.656  8.503   22.395  1.00 67.55  ?  13  GLN B CD  1 
ATOM   1712 O OE1 . GLN B 2 13  ? 21.336  8.071   23.326  1.00 76.59  ?  13  GLN B OE1 1 
ATOM   1713 N NE2 . GLN B 2 13  ? 20.932  8.245   21.123  1.00 74.17  ?  13  GLN B NE2 1 
ATOM   1714 N N   . PRO B 2 14  ? 16.883  9.508   26.295  1.00 38.66  ?  14  PRO B N   1 
ATOM   1715 C CA  . PRO B 2 14  ? 16.564  9.385   27.718  1.00 36.40  ?  14  PRO B CA  1 
ATOM   1716 C C   . PRO B 2 14  ? 17.825  9.344   28.564  1.00 39.59  ?  14  PRO B C   1 
ATOM   1717 O O   . PRO B 2 14  ? 18.822  8.718   28.199  1.00 45.42  ?  14  PRO B O   1 
ATOM   1718 C CB  . PRO B 2 14  ? 15.791  8.065   27.787  1.00 35.20  ?  14  PRO B CB  1 
ATOM   1719 C CG  . PRO B 2 14  ? 15.188  7.924   26.420  1.00 34.62  ?  14  PRO B CG  1 
ATOM   1720 C CD  . PRO B 2 14  ? 16.203  8.484   25.481  1.00 37.01  ?  14  PRO B CD  1 
ATOM   1721 N N   . GLY B 2 15  ? 17.777  10.035  29.700  1.00 39.05  ?  15  GLY B N   1 
ATOM   1722 C CA  . GLY B 2 15  ? 18.927  10.192  30.561  1.00 42.12  ?  15  GLY B CA  1 
ATOM   1723 C C   . GLY B 2 15  ? 19.872  11.311  30.181  1.00 44.18  ?  15  GLY B C   1 
ATOM   1724 O O   . GLY B 2 15  ? 20.668  11.741  31.025  1.00 52.70  ?  15  GLY B O   1 
ATOM   1725 N N   . GLY B 2 16  ? 19.802  11.815  28.950  1.00 39.66  ?  16  GLY B N   1 
ATOM   1726 C CA  . GLY B 2 16  ? 20.691  12.866  28.507  1.00 42.31  ?  16  GLY B CA  1 
ATOM   1727 C C   . GLY B 2 16  ? 20.335  14.240  29.053  1.00 44.13  ?  16  GLY B C   1 
ATOM   1728 O O   . GLY B 2 16  ? 19.364  14.440  29.782  1.00 44.41  ?  16  GLY B O   1 
ATOM   1729 N N   . SER B 2 17  ? 21.151  15.214  28.669  1.00 45.06  ?  17  SER B N   1 
ATOM   1730 C CA  . SER B 2 17  ? 20.989  16.588  29.111  1.00 45.52  ?  17  SER B CA  1 
ATOM   1731 C C   . SER B 2 17  ? 20.713  17.499  27.927  1.00 44.69  ?  17  SER B C   1 
ATOM   1732 O O   . SER B 2 17  ? 21.067  17.209  26.780  1.00 44.20  ?  17  SER B O   1 
ATOM   1733 C CB  . SER B 2 17  ? 22.227  17.090  29.860  1.00 42.35  ?  17  SER B CB  1 
ATOM   1734 O OG  . SER B 2 17  ? 22.102  16.827  31.245  1.00 54.03  ?  17  SER B OG  1 
ATOM   1735 N N   . LEU B 2 18  ? 20.117  18.640  28.240  1.00 38.17  ?  18  LEU B N   1 
ATOM   1736 C CA  . LEU B 2 18  ? 19.769  19.617  27.226  1.00 42.18  ?  18  LEU B CA  1 
ATOM   1737 C C   . LEU B 2 18  ? 19.779  20.990  27.878  1.00 43.64  ?  18  LEU B C   1 
ATOM   1738 O O   . LEU B 2 18  ? 19.561  21.118  29.084  1.00 44.25  ?  18  LEU B O   1 
ATOM   1739 C CB  . LEU B 2 18  ? 18.401  19.293  26.621  1.00 37.62  ?  18  LEU B CB  1 
ATOM   1740 C CG  . LEU B 2 18  ? 18.093  19.879  25.251  1.00 46.90  ?  18  LEU B CG  1 
ATOM   1741 C CD1 . LEU B 2 18  ? 19.175  19.482  24.258  1.00 48.71  ?  18  LEU B CD1 1 
ATOM   1742 C CD2 . LEU B 2 18  ? 16.717  19.416  24.786  1.00 40.87  ?  18  LEU B CD2 1 
ATOM   1743 N N   . ARG B 2 19  ? 20.085  22.016  27.094  1.00 40.85  ?  19  ARG B N   1 
ATOM   1744 C CA  . ARG B 2 19  ? 19.982  23.383  27.592  1.00 38.15  ?  19  ARG B CA  1 
ATOM   1745 C C   . ARG B 2 19  ? 19.113  24.183  26.637  1.00 36.91  ?  19  ARG B C   1 
ATOM   1746 O O   . ARG B 2 19  ? 19.484  24.387  25.477  1.00 36.67  ?  19  ARG B O   1 
ATOM   1747 C CB  . ARG B 2 19  ? 21.350  24.041  27.762  1.00 41.74  ?  19  ARG B CB  1 
ATOM   1748 C CG  . ARG B 2 19  ? 21.293  25.283  28.649  1.00 42.29  ?  19  ARG B CG  1 
ATOM   1749 C CD  . ARG B 2 19  ? 22.663  25.858  28.974  1.00 45.45  ?  19  ARG B CD  1 
ATOM   1750 N NE  . ARG B 2 19  ? 23.089  26.871  28.010  1.00 58.39  ?  19  ARG B NE  1 
ATOM   1751 C CZ  . ARG B 2 19  ? 24.142  26.754  27.204  1.00 70.74  ?  19  ARG B CZ  1 
ATOM   1752 N NH1 . ARG B 2 19  ? 24.895  25.658  27.240  1.00 72.30  ?  19  ARG B NH1 1 
ATOM   1753 N NH2 . ARG B 2 19  ? 24.449  27.742  26.365  1.00 64.30  ?  19  ARG B NH2 1 
ATOM   1754 N N   . LEU B 2 20  ? 17.955  24.617  27.121  1.00 35.11  ?  20  LEU B N   1 
ATOM   1755 C CA  . LEU B 2 20  ? 17.113  25.545  26.389  1.00 39.26  ?  20  LEU B CA  1 
ATOM   1756 C C   . LEU B 2 20  ? 17.560  26.969  26.688  1.00 40.40  ?  20  LEU B C   1 
ATOM   1757 O O   . LEU B 2 20  ? 17.928  27.293  27.822  1.00 37.06  ?  20  LEU B O   1 
ATOM   1758 C CB  . LEU B 2 20  ? 15.650  25.367  26.785  1.00 31.69  ?  20  LEU B CB  1 
ATOM   1759 C CG  . LEU B 2 20  ? 15.045  23.992  26.542  1.00 36.20  ?  20  LEU B CG  1 
ATOM   1760 C CD1 . LEU B 2 20  ? 13.579  24.000  26.937  1.00 30.89  ?  20  LEU B CD1 1 
ATOM   1761 C CD2 . LEU B 2 20  ? 15.213  23.594  25.097  1.00 35.31  ?  20  LEU B CD2 1 
ATOM   1762 N N   . SER B 2 21  ? 17.524  27.821  25.671  1.00 40.00  ?  21  SER B N   1 
ATOM   1763 C CA  . SER B 2 21  ? 17.866  29.221  25.855  1.00 41.79  ?  21  SER B CA  1 
ATOM   1764 C C   . SER B 2 21  ? 16.718  30.073  25.345  1.00 38.86  ?  21  SER B C   1 
ATOM   1765 O O   . SER B 2 21  ? 15.888  29.624  24.556  1.00 44.45  ?  21  SER B O   1 
ATOM   1766 C CB  . SER B 2 21  ? 19.173  29.606  25.142  1.00 42.58  ?  21  SER B CB  1 
ATOM   1767 O OG  . SER B 2 21  ? 19.105  29.330  23.758  1.00 48.73  ?  21  SER B OG  1 
ATOM   1768 N N   . CYS B 2 22  ? 16.675  31.309  25.819  1.00 40.92  ?  22  CYS B N   1 
ATOM   1769 C CA  . CYS B 2 22  ? 15.589  32.224  25.481  1.00 44.67  ?  22  CYS B CA  1 
ATOM   1770 C C   . CYS B 2 22  ? 16.181  33.626  25.423  1.00 41.27  ?  22  CYS B C   1 
ATOM   1771 O O   . CYS B 2 22  ? 16.581  34.180  26.451  1.00 37.25  ?  22  CYS B O   1 
ATOM   1772 C CB  . CYS B 2 22  ? 14.461  32.128  26.507  1.00 42.85  ?  22  CYS B CB  1 
ATOM   1773 S SG  . CYS B 2 22  ? 13.100  33.294  26.286  1.00 60.85  ?  22  CYS B SG  1 
ATOM   1774 N N   . ALA B 2 23  ? 16.256  34.185  24.223  1.00 40.87  ?  23  ALA B N   1 
ATOM   1775 C CA  . ALA B 2 23  ? 16.774  35.531  24.026  1.00 41.97  ?  23  ALA B CA  1 
ATOM   1776 C C   . ALA B 2 23  ? 15.630  36.531  24.152  1.00 39.31  ?  23  ALA B C   1 
ATOM   1777 O O   . ALA B 2 23  ? 14.606  36.408  23.465  1.00 48.60  ?  23  ALA B O   1 
ATOM   1778 C CB  . ALA B 2 23  ? 17.464  35.650  22.669  1.00 36.40  ?  23  ALA B CB  1 
ATOM   1779 N N   . ALA B 2 24  ? 15.789  37.488  25.059  1.00 37.58  ?  24  ALA B N   1 
ATOM   1780 C CA  . ALA B 2 24  ? 14.853  38.593  25.198  1.00 45.08  ?  24  ALA B CA  1 
ATOM   1781 C C   . ALA B 2 24  ? 15.304  39.729  24.296  1.00 43.65  ?  24  ALA B C   1 
ATOM   1782 O O   . ALA B 2 24  ? 16.471  40.130  24.329  1.00 42.94  ?  24  ALA B O   1 
ATOM   1783 C CB  . ALA B 2 24  ? 14.782  39.079  26.648  1.00 45.08  ?  24  ALA B CB  1 
ATOM   1784 N N   . SER B 2 25  ? 14.383  40.246  23.495  1.00 44.03  ?  25  SER B N   1 
ATOM   1785 C CA  . SER B 2 25  ? 14.683  41.322  22.566  1.00 43.82  ?  25  SER B CA  1 
ATOM   1786 C C   . SER B 2 25  ? 13.754  42.482  22.881  1.00 48.46  ?  25  SER B C   1 
ATOM   1787 O O   . SER B 2 25  ? 12.529  42.319  22.871  1.00 49.22  ?  25  SER B O   1 
ATOM   1788 C CB  . SER B 2 25  ? 14.517  40.859  21.119  1.00 53.91  ?  25  SER B CB  1 
ATOM   1789 O OG  . SER B 2 25  ? 14.617  41.948  20.221  1.00 68.20  ?  25  SER B OG  1 
ATOM   1790 N N   . GLY B 2 26  ? 14.342  43.639  23.184  1.00 43.33  ?  26  GLY B N   1 
ATOM   1791 C CA  . GLY B 2 26  ? 13.604  44.863  23.386  1.00 35.28  ?  26  GLY B CA  1 
ATOM   1792 C C   . GLY B 2 26  ? 13.382  45.272  24.824  1.00 36.79  ?  26  GLY B C   1 
ATOM   1793 O O   . GLY B 2 26  ? 12.801  46.339  25.056  1.00 40.65  ?  26  GLY B O   1 
ATOM   1794 N N   . PHE B 2 27  ? 13.825  44.482  25.799  1.00 35.49  ?  27  PHE B N   1 
ATOM   1795 C CA  . PHE B 2 27  ? 13.628  44.871  27.188  1.00 38.11  ?  27  PHE B CA  1 
ATOM   1796 C C   . PHE B 2 27  ? 14.733  44.271  28.044  1.00 35.42  ?  27  PHE B C   1 
ATOM   1797 O O   . PHE B 2 27  ? 15.521  43.443  27.590  1.00 35.13  ?  27  PHE B O   1 
ATOM   1798 C CB  . PHE B 2 27  ? 12.235  44.474  27.701  1.00 35.95  ?  27  PHE B CB  1 
ATOM   1799 C CG  . PHE B 2 27  ? 12.038  42.998  27.868  1.00 41.66  ?  27  PHE B CG  1 
ATOM   1800 C CD1 . PHE B 2 27  ? 11.768  42.188  26.772  1.00 42.04  ?  27  PHE B CD1 1 
ATOM   1801 C CD2 . PHE B 2 27  ? 12.107  42.419  29.126  1.00 39.77  ?  27  PHE B CD2 1 
ATOM   1802 C CE1 . PHE B 2 27  ? 11.581  40.826  26.929  1.00 38.54  ?  27  PHE B CE1 1 
ATOM   1803 C CE2 . PHE B 2 27  ? 11.923  41.053  29.290  1.00 39.89  ?  27  PHE B CE2 1 
ATOM   1804 C CZ  . PHE B 2 27  ? 11.661  40.258  28.190  1.00 36.41  ?  27  PHE B CZ  1 
ATOM   1805 N N   . SER B 2 28  ? 14.793  44.728  29.292  1.00 36.37  ?  28  SER B N   1 
ATOM   1806 C CA  . SER B 2 28  ? 15.852  44.353  30.224  1.00 40.31  ?  28  SER B CA  1 
ATOM   1807 C C   . SER B 2 28  ? 15.422  43.091  30.961  1.00 40.07  ?  28  SER B C   1 
ATOM   1808 O O   . SER B 2 28  ? 14.606  43.144  31.884  1.00 42.99  ?  28  SER B O   1 
ATOM   1809 C CB  . SER B 2 28  ? 16.130  45.502  31.185  1.00 39.40  ?  28  SER B CB  1 
ATOM   1810 O OG  . SER B 2 28  ? 17.297  45.260  31.944  1.00 46.76  ?  28  SER B OG  1 
ATOM   1811 N N   . LEU B 2 29  ? 15.997  41.952  30.559  1.00 37.30  ?  29  LEU B N   1 
ATOM   1812 C CA  . LEU B 2 29  ? 15.558  40.649  31.059  1.00 37.82  ?  29  LEU B CA  1 
ATOM   1813 C C   . LEU B 2 29  ? 15.680  40.528  32.574  1.00 39.51  ?  29  LEU B C   1 
ATOM   1814 O O   . LEU B 2 29  ? 14.818  39.930  33.226  1.00 38.01  ?  29  LEU B O   1 
ATOM   1815 C CB  . LEU B 2 29  ? 16.365  39.545  30.391  1.00 39.03  ?  29  LEU B CB  1 
ATOM   1816 C CG  . LEU B 2 29  ? 15.996  38.121  30.785  1.00 37.23  ?  29  LEU B CG  1 
ATOM   1817 C CD1 . LEU B 2 29  ? 14.698  37.740  30.116  1.00 36.29  ?  29  LEU B CD1 1 
ATOM   1818 C CD2 . LEU B 2 29  ? 17.119  37.173  30.404  1.00 34.91  ?  29  LEU B CD2 1 
ATOM   1819 N N   . SER B 2 30  ? 16.760  41.052  33.152  1.00 40.39  ?  30  SER B N   1 
ATOM   1820 C CA  . SER B 2 30  ? 17.035  40.812  34.564  1.00 35.15  ?  30  SER B CA  1 
ATOM   1821 C C   . SER B 2 30  ? 16.119  41.587  35.501  1.00 40.78  ?  30  SER B C   1 
ATOM   1822 O O   . SER B 2 30  ? 16.220  41.396  36.717  1.00 47.24  ?  30  SER B O   1 
ATOM   1823 C CB  . SER B 2 30  ? 18.490  41.157  34.881  1.00 43.51  ?  30  SER B CB  1 
ATOM   1824 O OG  . SER B 2 30  ? 18.725  42.550  34.734  1.00 48.10  ?  30  SER B OG  1 
ATOM   1825 N N   . SER B 2 31  ? 15.232  42.441  34.992  1.00 34.35  ?  31  SER B N   1 
ATOM   1826 C CA  . SER B 2 31  ? 14.341  43.220  35.844  1.00 44.36  ?  31  SER B CA  1 
ATOM   1827 C C   . SER B 2 31  ? 12.912  42.691  35.822  1.00 43.69  ?  31  SER B C   1 
ATOM   1828 O O   . SER B 2 31  ? 11.984  43.402  36.218  1.00 39.83  ?  31  SER B O   1 
ATOM   1829 C CB  . SER B 2 31  ? 14.360  44.694  35.438  1.00 43.59  ?  31  SER B CB  1 
ATOM   1830 O OG  . SER B 2 31  ? 13.844  44.855  34.130  1.00 50.90  ?  31  SER B OG  1 
ATOM   1831 N N   . TYR B 2 32  ? 12.719  41.456  35.374  1.00 44.28  ?  32  TYR B N   1 
ATOM   1832 C CA  . TYR B 2 32  ? 11.427  40.795  35.430  1.00 38.98  ?  32  TYR B CA  1 
ATOM   1833 C C   . TYR B 2 32  ? 11.581  39.428  36.077  1.00 39.22  ?  32  TYR B C   1 
ATOM   1834 O O   . TYR B 2 32  ? 12.670  38.846  36.105  1.00 41.68  ?  32  TYR B O   1 
ATOM   1835 C CB  . TYR B 2 32  ? 10.815  40.632  34.038  1.00 37.66  ?  32  TYR B CB  1 
ATOM   1836 C CG  . TYR B 2 32  ? 10.340  41.921  33.417  1.00 37.21  ?  32  TYR B CG  1 
ATOM   1837 C CD1 . TYR B 2 32  ? 9.009   42.298  33.495  1.00 37.41  ?  32  TYR B CD1 1 
ATOM   1838 C CD2 . TYR B 2 32  ? 11.222  42.760  32.749  1.00 41.53  ?  32  TYR B CD2 1 
ATOM   1839 C CE1 . TYR B 2 32  ? 8.566   43.468  32.926  1.00 36.36  ?  32  TYR B CE1 1 
ATOM   1840 C CE2 . TYR B 2 32  ? 10.788  43.935  32.171  1.00 41.57  ?  32  TYR B CE2 1 
ATOM   1841 C CZ  . TYR B 2 32  ? 9.458   44.285  32.265  1.00 40.99  ?  32  TYR B CZ  1 
ATOM   1842 O OH  . TYR B 2 32  ? 9.022   45.461  31.699  1.00 45.48  ?  32  TYR B OH  1 
ATOM   1843 N N   . TYR B 2 33  ? 10.474  38.931  36.623  1.00 35.99  ?  33  TYR B N   1 
ATOM   1844 C CA  . TYR B 2 33  ? 10.376  37.523  36.974  1.00 34.06  ?  33  TYR B CA  1 
ATOM   1845 C C   . TYR B 2 33  ? 10.215  36.718  35.688  1.00 35.29  ?  33  TYR B C   1 
ATOM   1846 O O   . TYR B 2 33  ? 9.293   36.964  34.908  1.00 39.14  ?  33  TYR B O   1 
ATOM   1847 C CB  . TYR B 2 33  ? 9.193   37.293  37.913  1.00 35.28  ?  33  TYR B CB  1 
ATOM   1848 C CG  . TYR B 2 33  ? 9.443   37.677  39.362  1.00 39.19  ?  33  TYR B CG  1 
ATOM   1849 C CD1 . TYR B 2 33  ? 9.077   36.825  40.397  1.00 38.48  ?  33  TYR B CD1 1 
ATOM   1850 C CD2 . TYR B 2 33  ? 10.044  38.887  39.697  1.00 40.95  ?  33  TYR B CD2 1 
ATOM   1851 C CE1 . TYR B 2 33  ? 9.301   37.164  41.722  1.00 42.11  ?  33  TYR B CE1 1 
ATOM   1852 C CE2 . TYR B 2 33  ? 10.274  39.236  41.023  1.00 39.59  ?  33  TYR B CE2 1 
ATOM   1853 C CZ  . TYR B 2 33  ? 9.900   38.369  42.030  1.00 40.18  ?  33  TYR B CZ  1 
ATOM   1854 O OH  . TYR B 2 33  ? 10.127  38.702  43.348  1.00 37.19  ?  33  TYR B OH  1 
ATOM   1855 N N   . MET B 2 34  ? 11.134  35.797  35.424  1.00 34.29  ?  34  MET B N   1 
ATOM   1856 C CA  . MET B 2 34  ? 11.085  35.008  34.201  1.00 36.66  ?  34  MET B CA  1 
ATOM   1857 C C   . MET B 2 34  ? 10.849  33.548  34.554  1.00 40.77  ?  34  MET B C   1 
ATOM   1858 O O   . MET B 2 34  ? 11.441  33.030  35.506  1.00 37.60  ?  34  MET B O   1 
ATOM   1859 C CB  . MET B 2 34  ? 12.376  35.149  33.393  1.00 36.33  ?  34  MET B CB  1 
ATOM   1860 C CG  . MET B 2 34  ? 12.628  36.545  32.841  1.00 39.68  ?  34  MET B CG  1 
ATOM   1861 S SD  . MET B 2 34  ? 11.437  37.125  31.618  1.00 40.26  ?  34  MET B SD  1 
ATOM   1862 C CE  . MET B 2 34  ? 11.459  35.774  30.445  1.00 38.18  ?  34  MET B CE  1 
ATOM   1863 N N   . THR B 2 35  ? 10.017  32.876  33.757  1.00 36.24  ?  35  THR B N   1 
ATOM   1864 C CA  . THR B 2 35  ? 9.511   31.559  34.097  1.00 35.30  ?  35  THR B CA  1 
ATOM   1865 C C   . THR B 2 35  ? 9.583   30.668  32.871  1.00 35.09  ?  35  THR B C   1 
ATOM   1866 O O   . THR B 2 35  ? 9.566   31.137  31.726  1.00 35.77  ?  35  THR B O   1 
ATOM   1867 C CB  . THR B 2 35  ? 8.042   31.557  34.588  1.00 37.66  ?  35  THR B CB  1 
ATOM   1868 O OG1 . THR B 2 35  ? 7.159   31.825  33.488  1.00 37.07  ?  35  THR B OG1 1 
ATOM   1869 C CG2 . THR B 2 35  ? 7.806   32.579  35.675  1.00 37.81  ?  35  THR B CG2 1 
ATOM   1870 N N   . TRP B 2 36  ? 9.669   29.372  33.137  1.00 33.83  ?  36  TRP B N   1 
ATOM   1871 C CA  . TRP B 2 36  ? 9.486   28.336  32.138  1.00 30.37  ?  36  TRP B CA  1 
ATOM   1872 C C   . TRP B 2 36  ? 8.191   27.614  32.462  1.00 36.87  ?  36  TRP B C   1 
ATOM   1873 O O   . TRP B 2 36  ? 7.965   27.236  33.625  1.00 36.06  ?  36  TRP B O   1 
ATOM   1874 C CB  . TRP B 2 36  ? 10.658  27.354  32.122  1.00 32.56  ?  36  TRP B CB  1 
ATOM   1875 C CG  . TRP B 2 36  ? 11.915  27.895  31.509  1.00 36.60  ?  36  TRP B CG  1 
ATOM   1876 C CD1 . TRP B 2 36  ? 13.007  28.382  32.167  1.00 32.27  ?  36  TRP B CD1 1 
ATOM   1877 C CD2 . TRP B 2 36  ? 12.215  27.990  30.111  1.00 33.35  ?  36  TRP B CD2 1 
ATOM   1878 N NE1 . TRP B 2 36  ? 13.962  28.778  31.269  1.00 32.62  ?  36  TRP B NE1 1 
ATOM   1879 C CE2 . TRP B 2 36  ? 13.501  28.549  29.999  1.00 32.49  ?  36  TRP B CE2 1 
ATOM   1880 C CE3 . TRP B 2 36  ? 11.520  27.657  28.944  1.00 32.30  ?  36  TRP B CE3 1 
ATOM   1881 C CZ2 . TRP B 2 36  ? 14.109  28.781  28.768  1.00 33.38  ?  36  TRP B CZ2 1 
ATOM   1882 C CZ3 . TRP B 2 36  ? 12.123  27.889  27.723  1.00 31.92  ?  36  TRP B CZ3 1 
ATOM   1883 C CH2 . TRP B 2 36  ? 13.406  28.448  27.644  1.00 34.22  ?  36  TRP B CH2 1 
ATOM   1884 N N   . VAL B 2 37  ? 7.346   27.463  31.436  1.00 35.61  ?  37  VAL B N   1 
ATOM   1885 C CA  . VAL B 2 37  ? 6.080   26.737  31.495  1.00 35.21  ?  37  VAL B CA  1 
ATOM   1886 C C   . VAL B 2 37  ? 6.084   25.675  30.403  1.00 34.27  ?  37  VAL B C   1 
ATOM   1887 O O   . VAL B 2 37  ? 6.432   25.962  29.256  1.00 35.95  ?  37  VAL B O   1 
ATOM   1888 C CB  . VAL B 2 37  ? 4.873   27.687  31.305  1.00 34.75  ?  37  VAL B CB  1 
ATOM   1889 C CG1 . VAL B 2 37  ? 3.590   26.897  31.131  1.00 33.05  ?  37  VAL B CG1 1 
ATOM   1890 C CG2 . VAL B 2 37  ? 4.746   28.635  32.484  1.00 32.11  ?  37  VAL B CG2 1 
ATOM   1891 N N   . ARG B 2 38  ? 5.665   24.459  30.727  1.00 34.82  ?  38  ARG B N   1 
ATOM   1892 C CA  . ARG B 2 38  ? 5.690   23.409  29.719  1.00 36.59  ?  38  ARG B CA  1 
ATOM   1893 C C   . ARG B 2 38  ? 4.294   22.859  29.470  1.00 35.39  ?  38  ARG B C   1 
ATOM   1894 O O   . ARG B 2 38  ? 3.389   22.974  30.301  1.00 36.30  ?  38  ARG B O   1 
ATOM   1895 C CB  . ARG B 2 38  ? 6.635   22.261  30.104  1.00 37.10  ?  38  ARG B CB  1 
ATOM   1896 C CG  . ARG B 2 38  ? 6.040   21.248  31.062  1.00 37.42  ?  38  ARG B CG  1 
ATOM   1897 C CD  . ARG B 2 38  ? 7.007   20.112  31.304  1.00 39.93  ?  38  ARG B CD  1 
ATOM   1898 N NE  . ARG B 2 38  ? 6.441   19.103  32.189  1.00 49.84  ?  38  ARG B NE  1 
ATOM   1899 C CZ  . ARG B 2 38  ? 7.098   18.030  32.617  1.00 48.96  ?  38  ARG B CZ  1 
ATOM   1900 N NH1 . ARG B 2 38  ? 6.500   17.165  33.427  1.00 49.86  ?  38  ARG B NH1 1 
ATOM   1901 N NH2 . ARG B 2 38  ? 8.353   17.824  32.239  1.00 45.38  ?  38  ARG B NH2 1 
ATOM   1902 N N   . GLN B 2 39  ? 4.137   22.263  28.293  1.00 35.09  ?  39  GLN B N   1 
ATOM   1903 C CA  . GLN B 2 39  ? 2.881   21.643  27.885  1.00 42.18  ?  39  GLN B CA  1 
ATOM   1904 C C   . GLN B 2 39  ? 3.193   20.314  27.204  1.00 41.63  ?  39  GLN B C   1 
ATOM   1905 O O   . GLN B 2 39  ? 3.746   20.286  26.099  1.00 36.64  ?  39  GLN B O   1 
ATOM   1906 C CB  . GLN B 2 39  ? 2.085   22.564  26.964  1.00 42.50  ?  39  GLN B CB  1 
ATOM   1907 C CG  . GLN B 2 39  ? 0.652   22.112  26.743  1.00 43.29  ?  39  GLN B CG  1 
ATOM   1908 C CD  . GLN B 2 39  ? -0.182  23.157  26.031  1.00 45.92  ?  39  GLN B CD  1 
ATOM   1909 O OE1 . GLN B 2 39  ? 0.305   23.869  25.155  1.00 46.54  ?  39  GLN B OE1 1 
ATOM   1910 N NE2 . GLN B 2 39  ? -1.444  23.263  26.417  1.00 55.72  ?  39  GLN B NE2 1 
ATOM   1911 N N   . ALA B 2 40  ? 2.857   19.216  27.875  1.00 43.86  ?  40  ALA B N   1 
ATOM   1912 C CA  . ALA B 2 40  ? 3.002   17.899  27.291  1.00 42.60  ?  40  ALA B CA  1 
ATOM   1913 C C   . ALA B 2 40  ? 2.005   17.736  26.145  1.00 47.57  ?  40  ALA B C   1 
ATOM   1914 O O   . ALA B 2 40  ? 1.002   18.448  26.084  1.00 46.82  ?  40  ALA B O   1 
ATOM   1915 C CB  . ALA B 2 40  ? 2.784   16.832  28.359  1.00 42.85  ?  40  ALA B CB  1 
ATOM   1916 N N   . PRO B 2 41  ? 2.262   16.810  25.220  1.00 54.47  ?  41  PRO B N   1 
ATOM   1917 C CA  . PRO B 2 41  ? 1.366   16.664  24.062  1.00 51.33  ?  41  PRO B CA  1 
ATOM   1918 C C   . PRO B 2 41  ? -0.058  16.334  24.487  1.00 57.70  ?  41  PRO B C   1 
ATOM   1919 O O   . PRO B 2 41  ? -0.302  15.363  25.209  1.00 58.87  ?  41  PRO B O   1 
ATOM   1920 C CB  . PRO B 2 41  ? 1.998   15.512  23.269  1.00 59.52  ?  41  PRO B CB  1 
ATOM   1921 C CG  . PRO B 2 41  ? 3.431   15.499  23.689  1.00 57.76  ?  41  PRO B CG  1 
ATOM   1922 C CD  . PRO B 2 41  ? 3.424   15.905  25.132  1.00 53.77  ?  41  PRO B CD  1 
ATOM   1923 N N   . GLY B 2 42  ? -1.000  17.151  24.023  1.00 56.17  ?  42  GLY B N   1 
ATOM   1924 C CA  . GLY B 2 42  ? -2.399  16.954  24.351  1.00 50.00  ?  42  GLY B CA  1 
ATOM   1925 C C   . GLY B 2 42  ? -2.755  17.130  25.813  1.00 56.86  ?  42  GLY B C   1 
ATOM   1926 O O   . GLY B 2 42  ? -3.756  16.570  26.267  1.00 64.24  ?  42  GLY B O   1 
ATOM   1927 N N   . LYS B 2 43  ? -1.973  17.898  26.564  1.00 58.41  ?  43  LYS B N   1 
ATOM   1928 C CA  . LYS B 2 43  ? -2.251  18.142  27.974  1.00 55.51  ?  43  LYS B CA  1 
ATOM   1929 C C   . LYS B 2 43  ? -2.235  19.643  28.245  1.00 55.76  ?  43  LYS B C   1 
ATOM   1930 O O   . LYS B 2 43  ? -2.102  20.467  27.330  1.00 50.43  ?  43  LYS B O   1 
ATOM   1931 C CB  . LYS B 2 43  ? -1.254  17.412  28.881  1.00 55.40  ?  43  LYS B CB  1 
ATOM   1932 C CG  . LYS B 2 43  ? -1.438  15.906  28.908  1.00 57.76  ?  43  LYS B CG  1 
ATOM   1933 C CD  . LYS B 2 43  ? -0.254  15.225  29.574  1.00 65.29  ?  43  LYS B CD  1 
ATOM   1934 C CE  . LYS B 2 43  ? -0.041  15.749  30.995  1.00 70.10  ?  43  LYS B CE  1 
ATOM   1935 N NZ  . LYS B 2 43  ? 1.087   15.061  31.695  1.00 66.05  ?  43  LYS B NZ  1 
ATOM   1936 N N   . GLY B 2 44  ? -2.399  19.997  29.523  1.00 51.43  ?  44  GLY B N   1 
ATOM   1937 C CA  . GLY B 2 44  ? -2.516  21.382  29.922  1.00 46.84  ?  44  GLY B CA  1 
ATOM   1938 C C   . GLY B 2 44  ? -1.178  22.031  30.227  1.00 44.77  ?  44  GLY B C   1 
ATOM   1939 O O   . GLY B 2 44  ? -0.117  21.413  30.179  1.00 40.53  ?  44  GLY B O   1 
ATOM   1940 N N   . LEU B 2 45  ? -1.248  23.317  30.557  1.00 44.91  ?  45  LEU B N   1 
ATOM   1941 C CA  . LEU B 2 45  ? -0.063  24.073  30.918  1.00 35.23  ?  45  LEU B CA  1 
ATOM   1942 C C   . LEU B 2 45  ? 0.403   23.698  32.314  1.00 34.08  ?  45  LEU B C   1 
ATOM   1943 O O   . LEU B 2 45  ? -0.402  23.489  33.223  1.00 38.11  ?  45  LEU B O   1 
ATOM   1944 C CB  . LEU B 2 45  ? -0.352  25.567  30.848  1.00 41.77  ?  45  LEU B CB  1 
ATOM   1945 C CG  . LEU B 2 45  ? -0.832  26.066  29.491  1.00 40.81  ?  45  LEU B CG  1 
ATOM   1946 C CD1 . LEU B 2 45  ? -1.371  27.470  29.638  1.00 41.15  ?  45  LEU B CD1 1 
ATOM   1947 C CD2 . LEU B 2 45  ? 0.307   26.023  28.490  1.00 36.96  ?  45  LEU B CD2 1 
ATOM   1948 N N   . GLU B 2 46  ? 1.717   23.632  32.485  1.00 38.78  ?  46  GLU B N   1 
ATOM   1949 C CA  . GLU B 2 46  ? 2.320   23.179  33.729  1.00 38.39  ?  46  GLU B CA  1 
ATOM   1950 C C   . GLU B 2 46  ? 3.491   24.097  34.043  1.00 41.22  ?  46  GLU B C   1 
ATOM   1951 O O   . GLU B 2 46  ? 4.434   24.189  33.252  1.00 41.84  ?  46  GLU B O   1 
ATOM   1952 C CB  . GLU B 2 46  ? 2.774   21.724  33.595  1.00 38.93  ?  46  GLU B CB  1 
ATOM   1953 C CG  . GLU B 2 46  ? 3.093   21.011  34.890  1.00 50.54  ?  46  GLU B CG  1 
ATOM   1954 C CD  . GLU B 2 46  ? 3.320   19.522  34.679  1.00 59.62  ?  46  GLU B CD  1 
ATOM   1955 O OE1 . GLU B 2 46  ? 3.142   18.748  35.644  1.00 69.11  ?  46  GLU B OE1 1 
ATOM   1956 O OE2 . GLU B 2 46  ? 3.682   19.126  33.550  1.00 54.79  ?  46  GLU B OE2 1 
ATOM   1957 N N   . TRP B 2 47  ? 3.427   24.788  35.179  1.00 39.73  ?  47  TRP B N   1 
ATOM   1958 C CA  . TRP B 2 47  ? 4.487   25.721  35.537  1.00 35.39  ?  47  TRP B CA  1 
ATOM   1959 C C   . TRP B 2 47  ? 5.727   24.963  35.994  1.00 38.69  ?  47  TRP B C   1 
ATOM   1960 O O   . TRP B 2 47  ? 5.646   24.078  36.850  1.00 41.53  ?  47  TRP B O   1 
ATOM   1961 C CB  . TRP B 2 47  ? 4.022   26.678  36.635  1.00 36.60  ?  47  TRP B CB  1 
ATOM   1962 C CG  . TRP B 2 47  ? 5.148   27.520  37.177  1.00 40.73  ?  47  TRP B CG  1 
ATOM   1963 C CD1 . TRP B 2 47  ? 5.807   28.518  36.523  1.00 36.09  ?  47  TRP B CD1 1 
ATOM   1964 C CD2 . TRP B 2 47  ? 5.760   27.420  38.474  1.00 42.32  ?  47  TRP B CD2 1 
ATOM   1965 N NE1 . TRP B 2 47  ? 6.787   29.047  37.328  1.00 39.01  ?  47  TRP B NE1 1 
ATOM   1966 C CE2 . TRP B 2 47  ? 6.778   28.394  38.531  1.00 39.20  ?  47  TRP B CE2 1 
ATOM   1967 C CE3 . TRP B 2 47  ? 5.544   26.605  39.591  1.00 38.94  ?  47  TRP B CE3 1 
ATOM   1968 C CZ2 . TRP B 2 47  ? 7.573   28.581  39.661  1.00 37.37  ?  47  TRP B CZ2 1 
ATOM   1969 C CZ3 . TRP B 2 47  ? 6.333   26.791  40.710  1.00 40.88  ?  47  TRP B CZ3 1 
ATOM   1970 C CH2 . TRP B 2 47  ? 7.336   27.775  40.738  1.00 40.27  ?  47  TRP B CH2 1 
ATOM   1971 N N   . VAL B 2 48  ? 6.880   25.326  35.430  1.00 40.66  ?  48  VAL B N   1 
ATOM   1972 C CA  . VAL B 2 48  ? 8.127   24.625  35.710  1.00 40.54  ?  48  VAL B CA  1 
ATOM   1973 C C   . VAL B 2 48  ? 8.997   25.408  36.682  1.00 41.05  ?  48  VAL B C   1 
ATOM   1974 O O   . VAL B 2 48  ? 9.404   24.872  37.720  1.00 40.93  ?  48  VAL B O   1 
ATOM   1975 C CB  . VAL B 2 48  ? 8.905   24.329  34.420  1.00 36.71  ?  48  VAL B CB  1 
ATOM   1976 C CG1 . VAL B 2 48  ? 10.233  23.682  34.757  1.00 34.82  ?  48  VAL B CG1 1 
ATOM   1977 C CG2 . VAL B 2 48  ? 8.072   23.431  33.514  1.00 41.37  ?  48  VAL B CG2 1 
ATOM   1978 N N   . SER B 2 49  ? 9.313   26.665  36.365  1.00 40.44  ?  49  SER B N   1 
ATOM   1979 C CA  . SER B 2 49  ? 10.238  27.359  37.265  1.00 39.28  ?  49  SER B CA  1 
ATOM   1980 C C   . SER B 2 49  ? 10.224  28.864  37.038  1.00 39.49  ?  49  SER B C   1 
ATOM   1981 O O   . SER B 2 49  ? 9.763   29.356  36.008  1.00 39.21  ?  49  SER B O   1 
ATOM   1982 C CB  . SER B 2 49  ? 11.670  26.833  37.111  1.00 36.97  ?  49  SER B CB  1 
ATOM   1983 O OG  . SER B 2 49  ? 12.219  27.220  35.866  1.00 39.32  ?  49  SER B OG  1 
ATOM   1984 N N   . VAL B 2 50  ? 10.821  29.581  37.995  1.00 34.21  ?  50  VAL B N   1 
ATOM   1985 C CA  . VAL B 2 50  ? 10.876  31.036  37.976  1.00 36.55  ?  50  VAL B CA  1 
ATOM   1986 C C   . VAL B 2 50  ? 12.210  31.490  38.559  1.00 38.40  ?  50  VAL B C   1 
ATOM   1987 O O   . VAL B 2 50  ? 12.774  30.851  39.453  1.00 38.80  ?  50  VAL B O   1 
ATOM   1988 C CB  . VAL B 2 50  ? 9.689   31.660  38.755  1.00 36.14  ?  50  VAL B CB  1 
ATOM   1989 C CG1 . VAL B 2 50  ? 9.801   31.350  40.239  1.00 29.49  ?  50  VAL B CG1 1 
ATOM   1990 C CG2 . VAL B 2 50  ? 9.625   33.166  38.534  1.00 32.08  ?  50  VAL B CG2 1 
ATOM   1991 N N   . ILE B 2 51  ? 12.723  32.592  38.019  1.00 39.69  ?  51  ILE B N   1 
ATOM   1992 C CA  . ILE B 2 51  ? 13.876  33.303  38.558  1.00 39.91  ?  51  ILE B CA  1 
ATOM   1993 C C   . ILE B 2 51  ? 13.486  34.770  38.695  1.00 39.39  ?  51  ILE B C   1 
ATOM   1994 O O   . ILE B 2 51  ? 12.895  35.349  37.772  1.00 38.90  ?  51  ILE B O   1 
ATOM   1995 C CB  . ILE B 2 51  ? 15.132  33.138  37.676  1.00 35.74  ?  51  ILE B CB  1 
ATOM   1996 C CG1 . ILE B 2 51  ? 16.320  33.886  38.292  1.00 40.20  ?  51  ILE B CG1 1 
ATOM   1997 C CG2 . ILE B 2 51  ? 14.869  33.604  36.256  1.00 34.82  ?  51  ILE B CG2 1 
ATOM   1998 C CD1 . ILE B 2 51  ? 17.652  33.597  37.627  1.00 34.32  ?  51  ILE B CD1 1 
ATOM   1999 N N   . ASN B 2 52  ? 13.778  35.356  39.859  1.00 34.32  ?  52  ASN B N   1 
ATOM   2000 C CA  . ASN B 2 52  ? 13.371  36.715  40.170  1.00 40.61  ?  52  ASN B CA  1 
ATOM   2001 C C   . ASN B 2 52  ? 14.511  37.692  39.862  1.00 46.41  ?  52  ASN B C   1 
ATOM   2002 O O   . ASN B 2 52  ? 15.560  37.314  39.329  1.00 43.93  ?  52  ASN B O   1 
ATOM   2003 C CB  . ASN B 2 52  ? 12.879  36.797  41.625  1.00 37.14  ?  52  ASN B CB  1 
ATOM   2004 C CG  . ASN B 2 52  ? 13.974  36.507  42.659  1.00 44.81  ?  52  ASN B CG  1 
ATOM   2005 O OD1 . ASN B 2 52  ? 15.153  36.819  42.464  1.00 39.83  ?  52  ASN B OD1 1 
ATOM   2006 N ND2 . ASN B 2 52  ? 13.570  35.920  43.780  1.00 42.42  ?  52  ASN B ND2 1 
ATOM   2007 N N   . VAL B 2 53  ? 14.307  38.968  40.205  1.00 44.25  ?  53  VAL B N   1 
ATOM   2008 C CA  . VAL B 2 53  ? 15.241  40.009  39.788  1.00 45.28  ?  53  VAL B CA  1 
ATOM   2009 C C   . VAL B 2 53  ? 16.570  39.893  40.521  1.00 44.70  ?  53  VAL B C   1 
ATOM   2010 O O   . VAL B 2 53  ? 17.607  40.312  39.995  1.00 45.55  ?  53  VAL B O   1 
ATOM   2011 C CB  . VAL B 2 53  ? 14.616  41.403  39.983  1.00 48.26  ?  53  VAL B CB  1 
ATOM   2012 C CG1 . VAL B 2 53  ? 13.396  41.558  39.101  1.00 42.30  ?  53  VAL B CG1 1 
ATOM   2013 C CG2 . VAL B 2 53  ? 14.248  41.623  41.441  1.00 52.55  ?  53  VAL B CG2 1 
ATOM   2014 N N   . TYR B 2 54  ? 16.572  39.344  41.739  1.00 48.22  ?  54  TYR B N   1 
ATOM   2015 C CA  . TYR B 2 54  ? 17.816  39.137  42.474  1.00 48.53  ?  54  TYR B CA  1 
ATOM   2016 C C   . TYR B 2 54  ? 18.549  37.869  42.048  1.00 50.47  ?  54  TYR B C   1 
ATOM   2017 O O   . TYR B 2 54  ? 19.684  37.652  42.486  1.00 60.28  ?  54  TYR B O   1 
ATOM   2018 C CB  . TYR B 2 54  ? 17.551  39.090  43.985  1.00 49.79  ?  54  TYR B CB  1 
ATOM   2019 C CG  . TYR B 2 54  ? 16.722  40.246  44.518  1.00 61.91  ?  54  TYR B CG  1 
ATOM   2020 C CD1 . TYR B 2 54  ? 15.342  40.118  44.678  1.00 64.69  ?  54  TYR B CD1 1 
ATOM   2021 C CD2 . TYR B 2 54  ? 17.314  41.461  44.867  1.00 57.27  ?  54  TYR B CD2 1 
ATOM   2022 C CE1 . TYR B 2 54  ? 14.568  41.168  45.165  1.00 63.98  ?  54  TYR B CE1 1 
ATOM   2023 C CE2 . TYR B 2 54  ? 16.546  42.520  45.355  1.00 65.54  ?  54  TYR B CE2 1 
ATOM   2024 C CZ  . TYR B 2 54  ? 15.170  42.364  45.500  1.00 69.85  ?  54  TYR B CZ  1 
ATOM   2025 O OH  . TYR B 2 54  ? 14.382  43.393  45.980  1.00 64.99  ?  54  TYR B OH  1 
ATOM   2026 N N   . GLY B 2 55  ? 17.935  37.033  41.217  1.00 49.46  ?  55  GLY B N   1 
ATOM   2027 C CA  . GLY B 2 55  ? 18.528  35.786  40.784  1.00 46.35  ?  55  GLY B CA  1 
ATOM   2028 C C   . GLY B 2 55  ? 18.129  34.555  41.570  1.00 48.48  ?  55  GLY B C   1 
ATOM   2029 O O   . GLY B 2 55  ? 18.678  33.479  41.313  1.00 49.60  ?  55  GLY B O   1 
ATOM   2030 N N   . GLY B 2 56  ? 17.189  34.671  42.504  1.00 41.97  ?  56  GLY B N   1 
ATOM   2031 C CA  . GLY B 2 56  ? 16.734  33.502  43.233  1.00 41.06  ?  56  GLY B CA  1 
ATOM   2032 C C   . GLY B 2 56  ? 15.853  32.617  42.368  1.00 42.66  ?  56  GLY B C   1 
ATOM   2033 O O   . GLY B 2 56  ? 15.053  33.091  41.561  1.00 41.62  ?  56  GLY B O   1 
ATOM   2034 N N   . THR B 2 57  ? 15.997  31.312  42.553  1.00 46.78  ?  57  THR B N   1 
ATOM   2035 C CA  . THR B 2 57  ? 15.326  30.315  41.733  1.00 43.85  ?  57  THR B CA  1 
ATOM   2036 C C   . THR B 2 57  ? 14.261  29.605  42.554  1.00 38.66  ?  57  THR B C   1 
ATOM   2037 O O   . THR B 2 57  ? 14.469  29.329  43.740  1.00 37.94  ?  57  THR B O   1 
ATOM   2038 C CB  . THR B 2 57  ? 16.334  29.299  41.191  1.00 43.92  ?  57  THR B CB  1 
ATOM   2039 O OG1 . THR B 2 57  ? 17.007  28.661  42.287  1.00 41.31  ?  57  THR B OG1 1 
ATOM   2040 C CG2 . THR B 2 57  ? 17.355  29.997  40.313  1.00 41.25  ?  57  THR B CG2 1 
ATOM   2041 N N   . TYR B 2 58  ? 13.107  29.349  41.934  1.00 36.12  ?  58  TYR B N   1 
ATOM   2042 C CA  . TYR B 2 58  ? 12.021  28.636  42.593  1.00 36.81  ?  58  TYR B CA  1 
ATOM   2043 C C   . TYR B 2 58  ? 11.375  27.704  41.578  1.00 38.33  ?  58  TYR B C   1 
ATOM   2044 O O   . TYR B 2 58  ? 11.308  28.011  40.384  1.00 39.89  ?  58  TYR B O   1 
ATOM   2045 C CB  . TYR B 2 58  ? 11.010  29.612  43.221  1.00 35.88  ?  58  TYR B CB  1 
ATOM   2046 C CG  . TYR B 2 58  ? 11.679  30.454  44.281  1.00 41.96  ?  58  TYR B CG  1 
ATOM   2047 C CD1 . TYR B 2 58  ? 11.745  30.026  45.599  1.00 39.10  ?  58  TYR B CD1 1 
ATOM   2048 C CD2 . TYR B 2 58  ? 12.307  31.652  43.947  1.00 43.49  ?  58  TYR B CD2 1 
ATOM   2049 C CE1 . TYR B 2 58  ? 12.398  30.777  46.563  1.00 40.01  ?  58  TYR B CE1 1 
ATOM   2050 C CE2 . TYR B 2 58  ? 12.965  32.406  44.897  1.00 44.23  ?  58  TYR B CE2 1 
ATOM   2051 C CZ  . TYR B 2 58  ? 13.008  31.968  46.206  1.00 45.77  ?  58  TYR B CZ  1 
ATOM   2052 O OH  . TYR B 2 58  ? 13.663  32.730  47.152  1.00 43.91  ?  58  TYR B OH  1 
ATOM   2053 N N   . TYR B 2 59  ? 10.926  26.546  42.060  1.00 37.17  ?  59  TYR B N   1 
ATOM   2054 C CA  . TYR B 2 59  ? 10.573  25.437  41.186  1.00 40.05  ?  59  TYR B CA  1 
ATOM   2055 C C   . TYR B 2 59  ? 9.269   24.790  41.634  1.00 42.91  ?  59  TYR B C   1 
ATOM   2056 O O   . TYR B 2 59  ? 8.851   24.907  42.789  1.00 43.84  ?  59  TYR B O   1 
ATOM   2057 C CB  . TYR B 2 59  ? 11.687  24.378  41.165  1.00 35.16  ?  59  TYR B CB  1 
ATOM   2058 C CG  . TYR B 2 59  ? 13.023  24.877  40.662  1.00 39.30  ?  59  TYR B CG  1 
ATOM   2059 C CD1 . TYR B 2 59  ? 13.397  24.709  39.332  1.00 34.12  ?  59  TYR B CD1 1 
ATOM   2060 C CD2 . TYR B 2 59  ? 13.911  25.518  41.516  1.00 41.14  ?  59  TYR B CD2 1 
ATOM   2061 C CE1 . TYR B 2 59  ? 14.611  25.167  38.869  1.00 31.74  ?  59  TYR B CE1 1 
ATOM   2062 C CE2 . TYR B 2 59  ? 15.133  25.982  41.062  1.00 37.45  ?  59  TYR B CE2 1 
ATOM   2063 C CZ  . TYR B 2 59  ? 15.480  25.805  39.740  1.00 37.28  ?  59  TYR B CZ  1 
ATOM   2064 O OH  . TYR B 2 59  ? 16.700  26.272  39.297  1.00 33.63  ?  59  TYR B OH  1 
ATOM   2065 N N   . ALA B 2 60  ? 8.629   24.094  40.700  1.00 38.01  ?  60  ALA B N   1 
ATOM   2066 C CA  . ALA B 2 60  ? 7.654   23.082  41.072  1.00 45.93  ?  60  ALA B CA  1 
ATOM   2067 C C   . ALA B 2 60  ? 8.378   21.869  41.650  1.00 49.18  ?  60  ALA B C   1 
ATOM   2068 O O   . ALA B 2 60  ? 9.489   21.532  41.233  1.00 47.05  ?  60  ALA B O   1 
ATOM   2069 C CB  . ALA B 2 60  ? 6.808   22.675  39.865  1.00 44.07  ?  60  ALA B CB  1 
ATOM   2070 N N   . SER B 2 61  ? 7.731   21.206  42.617  1.00 52.16  ?  61  SER B N   1 
ATOM   2071 C CA  . SER B 2 61  ? 8.367   20.104  43.341  1.00 45.96  ?  61  SER B CA  1 
ATOM   2072 C C   . SER B 2 61  ? 8.946   19.059  42.398  1.00 49.48  ?  61  SER B C   1 
ATOM   2073 O O   . SER B 2 61  ? 10.104  18.653  42.539  1.00 57.79  ?  61  SER B O   1 
ATOM   2074 C CB  . SER B 2 61  ? 7.370   19.457  44.301  1.00 46.50  ?  61  SER B CB  1 
ATOM   2075 O OG  . SER B 2 61  ? 7.186   20.259  45.454  1.00 52.16  ?  61  SER B OG  1 
ATOM   2076 N N   . TRP B 2 62  ? 8.153   18.609  41.427  1.00 49.04  ?  62  TRP B N   1 
ATOM   2077 C CA  . TRP B 2 62  ? 8.622   17.569  40.524  1.00 44.05  ?  62  TRP B CA  1 
ATOM   2078 C C   . TRP B 2 62  ? 9.812   18.010  39.677  1.00 50.50  ?  62  TRP B C   1 
ATOM   2079 O O   . TRP B 2 62  ? 10.574  17.157  39.209  1.00 58.21  ?  62  TRP B O   1 
ATOM   2080 C CB  . TRP B 2 62  ? 7.479   17.120  39.616  1.00 48.00  ?  62  TRP B CB  1 
ATOM   2081 C CG  . TRP B 2 62  ? 6.864   18.220  38.822  1.00 51.97  ?  62  TRP B CG  1 
ATOM   2082 C CD1 . TRP B 2 62  ? 5.745   18.932  39.139  1.00 55.90  ?  62  TRP B CD1 1 
ATOM   2083 C CD2 . TRP B 2 62  ? 7.322   18.730  37.566  1.00 50.24  ?  62  TRP B CD2 1 
ATOM   2084 N NE1 . TRP B 2 62  ? 5.479   19.857  38.158  1.00 56.92  ?  62  TRP B NE1 1 
ATOM   2085 C CE2 . TRP B 2 62  ? 6.435   19.754  37.182  1.00 52.72  ?  62  TRP B CE2 1 
ATOM   2086 C CE3 . TRP B 2 62  ? 8.396   18.419  36.728  1.00 47.98  ?  62  TRP B CE3 1 
ATOM   2087 C CZ2 . TRP B 2 62  ? 6.589   20.469  35.999  1.00 51.77  ?  62  TRP B CZ2 1 
ATOM   2088 C CZ3 . TRP B 2 62  ? 8.549   19.130  35.555  1.00 47.80  ?  62  TRP B CZ3 1 
ATOM   2089 C CH2 . TRP B 2 62  ? 7.652   20.145  35.201  1.00 52.17  ?  62  TRP B CH2 1 
ATOM   2090 N N   . ALA B 2 63  ? 10.008  19.313  39.485  1.00 52.84  ?  63  ALA B N   1 
ATOM   2091 C CA  . ALA B 2 63  ? 11.059  19.790  38.597  1.00 48.12  ?  63  ALA B CA  1 
ATOM   2092 C C   . ALA B 2 63  ? 12.360  20.113  39.314  1.00 47.40  ?  63  ALA B C   1 
ATOM   2093 O O   . ALA B 2 63  ? 13.401  20.209  38.653  1.00 50.70  ?  63  ALA B O   1 
ATOM   2094 C CB  . ALA B 2 63  ? 10.584  21.032  37.837  1.00 44.03  ?  63  ALA B CB  1 
ATOM   2095 N N   . LYS B 2 64  ? 12.333  20.246  40.644  1.00 46.20  ?  64  LYS B N   1 
ATOM   2096 C CA  . LYS B 2 64  ? 13.483  20.791  41.362  1.00 51.92  ?  64  LYS B CA  1 
ATOM   2097 C C   . LYS B 2 64  ? 14.713  19.899  41.242  1.00 59.27  ?  64  LYS B C   1 
ATOM   2098 O O   . LYS B 2 64  ? 15.843  20.400  41.228  1.00 63.86  ?  64  LYS B O   1 
ATOM   2099 C CB  . LYS B 2 64  ? 13.126  21.000  42.835  1.00 54.05  ?  64  LYS B CB  1 
ATOM   2100 C CG  . LYS B 2 64  ? 14.045  21.964  43.573  1.00 50.92  ?  64  LYS B CG  1 
ATOM   2101 C CD  . LYS B 2 64  ? 13.365  22.524  44.816  1.00 49.02  ?  64  LYS B CD  1 
ATOM   2102 C CE  . LYS B 2 64  ? 14.280  23.479  45.567  1.00 51.33  ?  64  LYS B CE  1 
ATOM   2103 N NZ  . LYS B 2 64  ? 13.677  23.906  46.858  1.00 52.53  ?  64  LYS B NZ  1 
ATOM   2104 N N   . GLY B 2 65  ? 14.519  18.584  41.138  1.00 57.35  ?  65  GLY B N   1 
ATOM   2105 C CA  . GLY B 2 65  ? 15.654  17.680  41.145  1.00 62.03  ?  65  GLY B CA  1 
ATOM   2106 C C   . GLY B 2 65  ? 16.485  17.707  39.878  1.00 62.19  ?  65  GLY B C   1 
ATOM   2107 O O   . GLY B 2 65  ? 17.704  17.532  39.932  1.00 64.98  ?  65  GLY B O   1 
ATOM   2108 N N   . ARG B 2 66  ? 15.851  17.910  38.725  1.00 58.22  ?  66  ARG B N   1 
ATOM   2109 C CA  . ARG B 2 66  ? 16.522  17.719  37.448  1.00 49.18  ?  66  ARG B CA  1 
ATOM   2110 C C   . ARG B 2 66  ? 16.570  18.964  36.575  1.00 53.90  ?  66  ARG B C   1 
ATOM   2111 O O   . ARG B 2 66  ? 17.316  18.971  35.588  1.00 50.89  ?  66  ARG B O   1 
ATOM   2112 C CB  . ARG B 2 66  ? 15.853  16.579  36.662  1.00 50.34  ?  66  ARG B CB  1 
ATOM   2113 C CG  . ARG B 2 66  ? 15.751  15.267  37.442  1.00 51.77  ?  66  ARG B CG  1 
ATOM   2114 C CD  . ARG B 2 66  ? 14.910  14.230  36.701  1.00 50.70  ?  66  ARG B CD  1 
ATOM   2115 N NE  . ARG B 2 66  ? 13.523  14.650  36.524  1.00 50.95  ?  66  ARG B NE  1 
ATOM   2116 C CZ  . ARG B 2 66  ? 12.956  14.862  35.340  1.00 50.48  ?  66  ARG B CZ  1 
ATOM   2117 N NH1 . ARG B 2 66  ? 11.681  15.236  35.257  1.00 44.54  ?  66  ARG B NH1 1 
ATOM   2118 N NH2 . ARG B 2 66  ? 13.673  14.710  34.236  1.00 45.37  ?  66  ARG B NH2 1 
ATOM   2119 N N   . PHE B 2 67  ? 15.804  20.005  36.897  1.00 52.17  ?  67  PHE B N   1 
ATOM   2120 C CA  . PHE B 2 67  ? 15.759  21.226  36.108  1.00 38.41  ?  67  PHE B CA  1 
ATOM   2121 C C   . PHE B 2 67  ? 16.443  22.348  36.876  1.00 41.63  ?  67  PHE B C   1 
ATOM   2122 O O   . PHE B 2 67  ? 16.328  22.434  38.103  1.00 44.85  ?  67  PHE B O   1 
ATOM   2123 C CB  . PHE B 2 67  ? 14.323  21.640  35.786  1.00 41.25  ?  67  PHE B CB  1 
ATOM   2124 C CG  . PHE B 2 67  ? 13.611  20.721  34.838  1.00 41.41  ?  67  PHE B CG  1 
ATOM   2125 C CD1 . PHE B 2 67  ? 13.402  21.091  33.521  1.00 42.83  ?  67  PHE B CD1 1 
ATOM   2126 C CD2 . PHE B 2 67  ? 13.154  19.484  35.258  1.00 51.73  ?  67  PHE B CD2 1 
ATOM   2127 C CE1 . PHE B 2 67  ? 12.739  20.246  32.637  1.00 43.27  ?  67  PHE B CE1 1 
ATOM   2128 C CE2 . PHE B 2 67  ? 12.489  18.633  34.380  1.00 52.24  ?  67  PHE B CE2 1 
ATOM   2129 C CZ  . PHE B 2 67  ? 12.285  19.017  33.067  1.00 45.04  ?  67  PHE B CZ  1 
ATOM   2130 N N   . THR B 2 68  ? 17.146  23.215  36.148  1.00 38.14  ?  68  THR B N   1 
ATOM   2131 C CA  . THR B 2 68  ? 17.783  24.388  36.738  1.00 38.02  ?  68  THR B CA  1 
ATOM   2132 C C   . THR B 2 68  ? 17.539  25.585  35.837  1.00 37.95  ?  68  THR B C   1 
ATOM   2133 O O   . THR B 2 68  ? 17.931  25.569  34.668  1.00 37.20  ?  68  THR B O   1 
ATOM   2134 C CB  . THR B 2 68  ? 19.286  24.179  36.922  1.00 38.53  ?  68  THR B CB  1 
ATOM   2135 O OG1 . THR B 2 68  ? 19.508  23.165  37.907  1.00 50.03  ?  68  THR B OG1 1 
ATOM   2136 C CG2 . THR B 2 68  ? 19.941  25.483  37.374  1.00 33.91  ?  68  THR B CG2 1 
ATOM   2137 N N   . ILE B 2 69  ? 16.914  26.614  36.372  1.00 37.55  ?  69  ILE B N   1 
ATOM   2138 C CA  . ILE B 2 69  ? 16.727  27.859  35.637  1.00 37.51  ?  69  ILE B CA  1 
ATOM   2139 C C   . ILE B 2 69  ? 17.882  28.799  35.966  1.00 34.97  ?  69  ILE B C   1 
ATOM   2140 O O   . ILE B 2 69  ? 18.426  28.782  37.077  1.00 38.19  ?  69  ILE B O   1 
ATOM   2141 C CB  . ILE B 2 69  ? 15.352  28.482  35.965  1.00 34.81  ?  69  ILE B CB  1 
ATOM   2142 C CG1 . ILE B 2 69  ? 15.021  29.607  34.986  1.00 38.80  ?  69  ILE B CG1 1 
ATOM   2143 C CG2 . ILE B 2 69  ? 15.308  28.986  37.405  1.00 31.70  ?  69  ILE B CG2 1 
ATOM   2144 C CD1 . ILE B 2 69  ? 13.625  30.166  35.155  1.00 36.57  ?  69  ILE B CD1 1 
ATOM   2145 N N   . SER B 2 70  ? 18.290  29.606  34.988  1.00 32.68  ?  70  SER B N   1 
ATOM   2146 C CA  . SER B 2 70  ? 19.356  30.583  35.205  1.00 36.83  ?  70  SER B CA  1 
ATOM   2147 C C   . SER B 2 70  ? 19.267  31.661  34.130  1.00 33.12  ?  70  SER B C   1 
ATOM   2148 O O   . SER B 2 70  ? 18.446  31.584  33.218  1.00 32.66  ?  70  SER B O   1 
ATOM   2149 C CB  . SER B 2 70  ? 20.742  29.923  35.207  1.00 33.33  ?  70  SER B CB  1 
ATOM   2150 O OG  . SER B 2 70  ? 21.149  29.576  33.895  1.00 40.14  ?  70  SER B OG  1 
ATOM   2151 N N   . ARG B 2 71  ? 20.113  32.682  34.251  1.00 33.04  ?  71  ARG B N   1 
ATOM   2152 C CA  . ARG B 2 71  ? 20.155  33.704  33.214  1.00 37.58  ?  71  ARG B CA  1 
ATOM   2153 C C   . ARG B 2 71  ? 21.549  34.304  33.117  1.00 39.23  ?  71  ARG B C   1 
ATOM   2154 O O   . ARG B 2 71  ? 22.264  34.430  34.114  1.00 43.01  ?  71  ARG B O   1 
ATOM   2155 C CB  . ARG B 2 71  ? 19.123  34.811  33.454  1.00 37.80  ?  71  ARG B CB  1 
ATOM   2156 C CG  . ARG B 2 71  ? 19.305  35.566  34.756  1.00 41.52  ?  71  ARG B CG  1 
ATOM   2157 C CD  . ARG B 2 71  ? 18.597  36.916  34.717  1.00 41.72  ?  71  ARG B CD  1 
ATOM   2158 N NE  . ARG B 2 71  ? 18.864  37.681  35.932  1.00 43.66  ?  71  ARG B NE  1 
ATOM   2159 C CZ  . ARG B 2 71  ? 17.949  37.973  36.849  1.00 46.83  ?  71  ARG B CZ  1 
ATOM   2160 N NH1 . ARG B 2 71  ? 16.686  37.592  36.677  1.00 41.15  ?  71  ARG B NH1 1 
ATOM   2161 N NH2 . ARG B 2 71  ? 18.295  38.666  37.925  1.00 48.46  ?  71  ARG B NH2 1 
ATOM   2162 N N   . ASP B 2 72  ? 21.923  34.671  31.893  1.00 37.45  ?  72  ASP B N   1 
ATOM   2163 C CA  . ASP B 2 72  ? 23.141  35.422  31.620  1.00 43.07  ?  72  ASP B CA  1 
ATOM   2164 C C   . ASP B 2 72  ? 22.744  36.868  31.325  1.00 44.78  ?  72  ASP B C   1 
ATOM   2165 O O   . ASP B 2 72  ? 22.095  37.152  30.305  1.00 46.84  ?  72  ASP B O   1 
ATOM   2166 C CB  . ASP B 2 72  ? 23.913  34.810  30.453  1.00 42.58  ?  72  ASP B CB  1 
ATOM   2167 C CG  . ASP B 2 72  ? 25.354  35.286  30.392  1.00 48.58  ?  72  ASP B CG  1 
ATOM   2168 O OD1 . ASP B 2 72  ? 26.222  34.479  30.004  1.00 59.49  ?  72  ASP B OD1 1 
ATOM   2169 O OD2 . ASP B 2 72  ? 25.627  36.457  30.749  1.00 47.60  ?  72  ASP B OD2 1 
ATOM   2170 N N   . ASN B 2 73  ? 23.115  37.769  32.241  1.00 41.73  ?  73  ASN B N   1 
ATOM   2171 C CA  . ASN B 2 73  ? 22.829  39.191  32.072  1.00 43.26  ?  73  ASN B CA  1 
ATOM   2172 C C   . ASN B 2 73  ? 23.679  39.812  30.969  1.00 41.30  ?  73  ASN B C   1 
ATOM   2173 O O   . ASN B 2 73  ? 23.237  40.756  30.304  1.00 40.17  ?  73  ASN B O   1 
ATOM   2174 C CB  . ASN B 2 73  ? 23.070  39.936  33.390  1.00 41.69  ?  73  ASN B CB  1 
ATOM   2175 C CG  . ASN B 2 73  ? 22.221  39.406  34.530  1.00 41.65  ?  73  ASN B CG  1 
ATOM   2176 O OD1 . ASN B 2 73  ? 21.078  38.983  34.328  1.00 38.61  ?  73  ASN B OD1 1 
ATOM   2177 N ND2 . ASN B 2 73  ? 22.778  39.432  35.742  1.00 38.23  ?  73  ASN B ND2 1 
ATOM   2178 N N   . SER B 2 74  ? 24.899  39.313  30.765  1.00 38.85  ?  74  SER B N   1 
ATOM   2179 C CA  . SER B 2 74  ? 25.739  39.841  29.700  1.00 41.09  ?  74  SER B CA  1 
ATOM   2180 C C   . SER B 2 74  ? 25.252  39.444  28.312  1.00 41.07  ?  74  SER B C   1 
ATOM   2181 O O   . SER B 2 74  ? 25.736  40.002  27.321  1.00 35.51  ?  74  SER B O   1 
ATOM   2182 C CB  . SER B 2 74  ? 27.179  39.380  29.902  1.00 34.49  ?  74  SER B CB  1 
ATOM   2183 O OG  . SER B 2 74  ? 27.305  38.012  29.606  1.00 41.91  ?  74  SER B OG  1 
ATOM   2184 N N   . LYS B 2 75  ? 24.300  38.517  28.215  1.00 40.76  ?  75  LYS B N   1 
ATOM   2185 C CA  . LYS B 2 75  ? 23.717  38.138  26.937  1.00 41.39  ?  75  LYS B CA  1 
ATOM   2186 C C   . LYS B 2 75  ? 22.223  38.430  26.853  1.00 41.43  ?  75  LYS B C   1 
ATOM   2187 O O   . LYS B 2 75  ? 21.621  38.198  25.795  1.00 32.99  ?  75  LYS B O   1 
ATOM   2188 C CB  . LYS B 2 75  ? 23.953  36.648  26.660  1.00 47.79  ?  75  LYS B CB  1 
ATOM   2189 C CG  . LYS B 2 75  ? 25.411  36.228  26.582  1.00 45.59  ?  75  LYS B CG  1 
ATOM   2190 C CD  . LYS B 2 75  ? 25.514  34.856  25.941  1.00 47.77  ?  75  LYS B CD  1 
ATOM   2191 C CE  . LYS B 2 75  ? 26.922  34.314  26.009  1.00 52.43  ?  75  LYS B CE  1 
ATOM   2192 N NZ  . LYS B 2 75  ? 27.279  34.039  27.425  1.00 68.07  ?  75  LYS B NZ  1 
ATOM   2193 N N   . ASN B 2 76  ? 21.616  38.939  27.933  1.00 41.41  ?  76  ASN B N   1 
ATOM   2194 C CA  . ASN B 2 76  ? 20.173  39.178  28.016  1.00 39.11  ?  76  ASN B CA  1 
ATOM   2195 C C   . ASN B 2 76  ? 19.387  37.898  27.742  1.00 39.54  ?  76  ASN B C   1 
ATOM   2196 O O   . ASN B 2 76  ? 18.354  37.919  27.065  1.00 38.12  ?  76  ASN B O   1 
ATOM   2197 C CB  . ASN B 2 76  ? 19.738  40.297  27.064  1.00 38.59  ?  76  ASN B CB  1 
ATOM   2198 C CG  . ASN B 2 76  ? 18.548  41.089  27.588  1.00 39.18  ?  76  ASN B CG  1 
ATOM   2199 O OD1 . ASN B 2 76  ? 18.364  41.230  28.795  1.00 37.64  ?  76  ASN B OD1 1 
ATOM   2200 N ND2 . ASN B 2 76  ? 17.738  41.615  26.674  1.00 33.74  ?  76  ASN B ND2 1 
ATOM   2201 N N   . THR B 2 77  ? 19.873  36.766  28.271  1.00 42.37  ?  77  THR B N   1 
ATOM   2202 C CA  . THR B 2 77  ? 19.337  35.465  27.881  1.00 36.86  ?  77  THR B CA  1 
ATOM   2203 C C   . THR B 2 77  ? 18.978  34.630  29.102  1.00 37.22  ?  77  THR B C   1 
ATOM   2204 O O   . THR B 2 77  ? 19.723  34.595  30.084  1.00 37.25  ?  77  THR B O   1 
ATOM   2205 C CB  . THR B 2 77  ? 20.337  34.695  27.001  1.00 44.41  ?  77  THR B CB  1 
ATOM   2206 O OG1 . THR B 2 77  ? 20.593  35.434  25.801  1.00 43.45  ?  77  THR B OG1 1 
ATOM   2207 C CG2 . THR B 2 77  ? 19.785  33.322  26.624  1.00 42.40  ?  77  THR B CG2 1 
ATOM   2208 N N   . LEU B 2 78  ? 17.830  33.962  29.034  1.00 35.54  ?  78  LEU B N   1 
ATOM   2209 C CA  . LEU B 2 78  ? 17.383  33.008  30.040  1.00 41.39  ?  78  LEU B CA  1 
ATOM   2210 C C   . LEU B 2 78  ? 17.724  31.577  29.611  1.00 35.35  ?  78  LEU B C   1 
ATOM   2211 O O   . LEU B 2 78  ? 17.782  31.271  28.421  1.00 31.44  ?  78  LEU B O   1 
ATOM   2212 C CB  . LEU B 2 78  ? 15.875  33.145  30.255  1.00 35.35  ?  78  LEU B CB  1 
ATOM   2213 C CG  . LEU B 2 78  ? 15.281  32.552  31.526  1.00 37.07  ?  78  LEU B CG  1 
ATOM   2214 C CD1 . LEU B 2 78  ? 15.583  33.461  32.698  1.00 33.87  ?  78  LEU B CD1 1 
ATOM   2215 C CD2 . LEU B 2 78  ? 13.780  32.329  31.360  1.00 34.91  ?  78  LEU B CD2 1 
ATOM   2216 N N   . TYR B 2 79  ? 17.956  30.697  30.586  1.00 33.89  ?  79  TYR B N   1 
ATOM   2217 C CA  . TYR B 2 79  ? 18.331  29.315  30.302  1.00 40.07  ?  79  TYR B CA  1 
ATOM   2218 C C   . TYR B 2 79  ? 17.552  28.356  31.190  1.00 37.22  ?  79  TYR B C   1 
ATOM   2219 O O   . TYR B 2 79  ? 17.299  28.641  32.367  1.00 36.80  ?  79  TYR B O   1 
ATOM   2220 C CB  . TYR B 2 79  ? 19.831  29.046  30.518  1.00 34.24  ?  79  TYR B CB  1 
ATOM   2221 C CG  . TYR B 2 79  ? 20.765  29.868  29.660  1.00 40.35  ?  79  TYR B CG  1 
ATOM   2222 C CD1 . TYR B 2 79  ? 20.996  29.536  28.330  1.00 35.20  ?  79  TYR B CD1 1 
ATOM   2223 C CD2 . TYR B 2 79  ? 21.447  30.960  30.196  1.00 40.93  ?  79  TYR B CD2 1 
ATOM   2224 C CE1 . TYR B 2 79  ? 21.859  30.278  27.554  1.00 41.77  ?  79  TYR B CE1 1 
ATOM   2225 C CE2 . TYR B 2 79  ? 22.311  31.712  29.427  1.00 37.51  ?  79  TYR B CE2 1 
ATOM   2226 C CZ  . TYR B 2 79  ? 22.514  31.368  28.107  1.00 44.58  ?  79  TYR B CZ  1 
ATOM   2227 O OH  . TYR B 2 79  ? 23.378  32.116  27.339  1.00 48.92  ?  79  TYR B OH  1 
ATOM   2228 N N   . LEU B 2 80  ? 17.206  27.206  30.620  1.00 33.97  ?  80  LEU B N   1 
ATOM   2229 C CA  . LEU B 2 80  ? 16.661  26.074  31.364  1.00 36.53  ?  80  LEU B CA  1 
ATOM   2230 C C   . LEU B 2 80  ? 17.536  24.863  31.075  1.00 36.09  ?  80  LEU B C   1 
ATOM   2231 O O   . LEU B 2 80  ? 17.517  24.335  29.958  1.00 35.22  ?  80  LEU B O   1 
ATOM   2232 C CB  . LEU B 2 80  ? 15.210  25.794  30.981  1.00 34.18  ?  80  LEU B CB  1 
ATOM   2233 C CG  . LEU B 2 80  ? 14.568  24.657  31.779  1.00 37.76  ?  80  LEU B CG  1 
ATOM   2234 C CD1 . LEU B 2 80  ? 14.586  24.974  33.270  1.00 33.86  ?  80  LEU B CD1 1 
ATOM   2235 C CD2 . LEU B 2 80  ? 13.154  24.371  31.298  1.00 36.88  ?  80  LEU B CD2 1 
ATOM   2236 N N   . GLN B 2 81  ? 18.307  24.435  32.075  1.00 34.47  ?  81  GLN B N   1 
ATOM   2237 C CA  . GLN B 2 81  ? 19.130  23.237  31.976  1.00 44.49  ?  81  GLN B CA  1 
ATOM   2238 C C   . GLN B 2 81  ? 18.323  22.039  32.456  1.00 38.29  ?  81  GLN B C   1 
ATOM   2239 O O   . GLN B 2 81  ? 17.762  22.064  33.556  1.00 37.75  ?  81  GLN B O   1 
ATOM   2240 C CB  . GLN B 2 81  ? 20.406  23.391  32.809  1.00 41.20  ?  81  GLN B CB  1 
ATOM   2241 C CG  . GLN B 2 81  ? 21.325  22.177  32.823  1.00 45.33  ?  81  GLN B CG  1 
ATOM   2242 C CD  . GLN B 2 81  ? 22.137  22.021  31.544  1.00 50.46  ?  81  GLN B CD  1 
ATOM   2243 O OE1 . GLN B 2 81  ? 22.629  23.000  30.981  1.00 51.54  ?  81  GLN B OE1 1 
ATOM   2244 N NE2 . GLN B 2 81  ? 22.287  20.781  31.087  1.00 53.85  ?  81  GLN B NE2 1 
ATOM   2245 N N   . MET B 2 82  ? 18.275  20.992  31.636  1.00 40.58  ?  82  MET B N   1 
ATOM   2246 C CA  . MET B 2 82  ? 17.514  19.782  31.920  1.00 42.47  ?  82  MET B CA  1 
ATOM   2247 C C   . MET B 2 82  ? 18.473  18.601  31.953  1.00 40.41  ?  82  MET B C   1 
ATOM   2248 O O   . MET B 2 82  ? 19.089  18.269  30.934  1.00 40.28  ?  82  MET B O   1 
ATOM   2249 C CB  . MET B 2 82  ? 16.435  19.563  30.857  1.00 42.68  ?  82  MET B CB  1 
ATOM   2250 C CG  . MET B 2 82  ? 15.508  20.756  30.644  1.00 47.28  ?  82  MET B CG  1 
ATOM   2251 S SD  . MET B 2 82  ? 14.231  20.480  29.392  1.00 48.34  ?  82  MET B SD  1 
ATOM   2252 C CE  . MET B 2 82  ? 15.197  20.616  27.897  1.00 38.48  ?  82  MET B CE  1 
ATOM   2253 N N   . ASN B 2 83  ? 18.593  17.972  33.117  1.00 42.02  ?  83  ASN B N   1 
ATOM   2254 C CA  . ASN B 2 83  ? 19.437  16.802  33.311  1.00 44.27  ?  83  ASN B CA  1 
ATOM   2255 C C   . ASN B 2 83  ? 18.587  15.556  33.507  1.00 45.87  ?  83  ASN B C   1 
ATOM   2256 O O   . ASN B 2 83  ? 17.445  15.632  33.970  1.00 45.67  ?  83  ASN B O   1 
ATOM   2257 C CB  . ASN B 2 83  ? 20.350  16.972  34.522  1.00 43.20  ?  83  ASN B CB  1 
ATOM   2258 C CG  . ASN B 2 83  ? 21.265  18.155  34.389  1.00 55.36  ?  83  ASN B CG  1 
ATOM   2259 O OD1 . ASN B 2 83  ? 21.827  18.403  33.322  1.00 54.19  ?  83  ASN B OD1 1 
ATOM   2260 N ND2 . ASN B 2 83  ? 21.410  18.912  35.471  1.00 61.44  ?  83  ASN B ND2 1 
ATOM   2261 N N   . SER B 2 84  ? 19.173  14.408  33.179  1.00 47.23  ?  84  SER B N   1 
ATOM   2262 C CA  . SER B 2 84  ? 18.534  13.103  33.351  1.00 52.94  ?  84  SER B CA  1 
ATOM   2263 C C   . SER B 2 84  ? 17.085  13.133  32.854  1.00 51.41  ?  84  SER B C   1 
ATOM   2264 O O   . SER B 2 84  ? 16.129  12.893  33.597  1.00 45.27  ?  84  SER B O   1 
ATOM   2265 C CB  . SER B 2 84  ? 18.607  12.659  34.817  1.00 55.65  ?  84  SER B CB  1 
ATOM   2266 O OG  . SER B 2 84  ? 19.928  12.304  35.200  1.00 59.90  ?  84  SER B OG  1 
ATOM   2267 N N   . LEU B 2 85  ? 16.944  13.438  31.567  1.00 49.85  ?  85  LEU B N   1 
ATOM   2268 C CA  . LEU B 2 85  ? 15.627  13.644  30.984  1.00 43.30  ?  85  LEU B CA  1 
ATOM   2269 C C   . LEU B 2 85  ? 14.844  12.341  30.914  1.00 45.47  ?  85  LEU B C   1 
ATOM   2270 O O   . LEU B 2 85  ? 15.398  11.266  30.665  1.00 44.92  ?  85  LEU B O   1 
ATOM   2271 C CB  . LEU B 2 85  ? 15.754  14.266  29.597  1.00 46.40  ?  85  LEU B CB  1 
ATOM   2272 C CG  . LEU B 2 85  ? 16.064  15.765  29.642  1.00 45.27  ?  85  LEU B CG  1 
ATOM   2273 C CD1 . LEU B 2 85  ? 16.601  16.245  28.312  1.00 40.95  ?  85  LEU B CD1 1 
ATOM   2274 C CD2 . LEU B 2 85  ? 14.810  16.533  30.021  1.00 42.46  ?  85  LEU B CD2 1 
ATOM   2275 N N   . ARG B 2 86  ? 13.538  12.458  31.115  1.00 46.28  ?  86  ARG B N   1 
ATOM   2276 C CA  . ARG B 2 86  ? 12.598  11.352  31.081  1.00 45.98  ?  86  ARG B CA  1 
ATOM   2277 C C   . ARG B 2 86  ? 11.706  11.472  29.856  1.00 46.11  ?  86  ARG B C   1 
ATOM   2278 O O   . ARG B 2 86  ? 11.498  12.567  29.327  1.00 46.17  ?  86  ARG B O   1 
ATOM   2279 C CB  . ARG B 2 86  ? 11.710  11.378  32.324  1.00 39.17  ?  86  ARG B CB  1 
ATOM   2280 C CG  . ARG B 2 86  ? 12.441  11.314  33.641  1.00 44.80  ?  86  ARG B CG  1 
ATOM   2281 C CD  . ARG B 2 86  ? 11.452  11.477  34.775  1.00 44.45  ?  86  ARG B CD  1 
ATOM   2282 N NE  . ARG B 2 86  ? 10.572  10.325  34.899  1.00 52.30  ?  86  ARG B NE  1 
ATOM   2283 C CZ  . ARG B 2 86  ? 9.577   10.246  35.772  1.00 60.37  ?  86  ARG B CZ  1 
ATOM   2284 N NH1 . ARG B 2 86  ? 9.335   11.257  36.597  1.00 61.38  ?  86  ARG B NH1 1 
ATOM   2285 N NH2 . ARG B 2 86  ? 8.824   9.157   35.814  1.00 68.74  ?  86  ARG B NH2 1 
ATOM   2286 N N   . ALA B 2 87  ? 11.197  10.331  29.391  1.00 47.63  ?  87  ALA B N   1 
ATOM   2287 C CA  . ALA B 2 87  ? 10.240  10.368  28.292  1.00 46.64  ?  87  ALA B CA  1 
ATOM   2288 C C   . ALA B 2 87  ? 9.044   11.241  28.648  1.00 45.49  ?  87  ALA B C   1 
ATOM   2289 O O   . ALA B 2 87  ? 8.485   11.921  27.779  1.00 40.46  ?  87  ALA B O   1 
ATOM   2290 C CB  . ALA B 2 87  ? 9.781   8.952   27.941  1.00 35.54  ?  87  ALA B CB  1 
ATOM   2291 N N   . GLU B 2 88  ? 8.660   11.255  29.927  1.00 43.87  ?  88  GLU B N   1 
ATOM   2292 C CA  . GLU B 2 88  ? 7.578   12.098  30.412  1.00 42.52  ?  88  GLU B CA  1 
ATOM   2293 C C   . GLU B 2 88  ? 7.917   13.583  30.358  1.00 49.06  ?  88  GLU B C   1 
ATOM   2294 O O   . GLU B 2 88  ? 7.018   14.411  30.541  1.00 52.67  ?  88  GLU B O   1 
ATOM   2295 C CB  . GLU B 2 88  ? 7.214   11.709  31.852  1.00 48.65  ?  88  GLU B CB  1 
ATOM   2296 C CG  . GLU B 2 88  ? 6.674   10.282  32.030  1.00 55.87  ?  88  GLU B CG  1 
ATOM   2297 C CD  . GLU B 2 88  ? 7.756   9.208   31.906  1.00 53.97  ?  88  GLU B CD  1 
ATOM   2298 O OE1 . GLU B 2 88  ? 8.950   9.541   32.030  1.00 55.27  ?  88  GLU B OE1 1 
ATOM   2299 O OE2 . GLU B 2 88  ? 7.418   8.031   31.671  1.00 62.56  ?  88  GLU B OE2 1 
ATOM   2300 N N   . ASP B 2 89  ? 9.182   13.945  30.134  1.00 45.55  ?  89  ASP B N   1 
ATOM   2301 C CA  . ASP B 2 89  ? 9.535   15.349  29.975  1.00 40.49  ?  89  ASP B CA  1 
ATOM   2302 C C   . ASP B 2 89  ? 9.284   15.864  28.567  1.00 40.23  ?  89  ASP B C   1 
ATOM   2303 O O   . ASP B 2 89  ? 9.390   17.075  28.346  1.00 45.07  ?  89  ASP B O   1 
ATOM   2304 C CB  . ASP B 2 89  ? 11.002  15.589  30.337  1.00 40.77  ?  89  ASP B CB  1 
ATOM   2305 C CG  . ASP B 2 89  ? 11.314  15.252  31.780  1.00 46.62  ?  89  ASP B CG  1 
ATOM   2306 O OD1 . ASP B 2 89  ? 12.382  14.660  32.031  1.00 47.96  ?  89  ASP B OD1 1 
ATOM   2307 O OD2 . ASP B 2 89  ? 10.492  15.575  32.663  1.00 49.79  ?  89  ASP B OD2 1 
ATOM   2308 N N   . THR B 2 90  ? 8.957   14.984  27.625  1.00 36.35  ?  90  THR B N   1 
ATOM   2309 C CA  . THR B 2 90  ? 8.637   15.399  26.266  1.00 37.54  ?  90  THR B CA  1 
ATOM   2310 C C   . THR B 2 90  ? 7.485   16.395  26.291  1.00 38.82  ?  90  THR B C   1 
ATOM   2311 O O   . THR B 2 90  ? 6.397   16.083  26.784  1.00 43.94  ?  90  THR B O   1 
ATOM   2312 C CB  . THR B 2 90  ? 8.279   14.171  25.422  1.00 39.03  ?  90  THR B CB  1 
ATOM   2313 O OG1 . THR B 2 90  ? 9.436   13.335  25.288  1.00 35.87  ?  90  THR B OG1 1 
ATOM   2314 C CG2 . THR B 2 90  ? 7.768   14.573  24.040  1.00 31.69  ?  90  THR B CG2 1 
ATOM   2315 N N   . ALA B 2 91  ? 7.729   17.599  25.782  1.00 41.74  ?  91  ALA B N   1 
ATOM   2316 C CA  . ALA B 2 91  ? 6.740   18.668  25.894  1.00 39.00  ?  91  ALA B CA  1 
ATOM   2317 C C   . ALA B 2 91  ? 7.208   19.859  25.074  1.00 37.26  ?  91  ALA B C   1 
ATOM   2318 O O   . ALA B 2 91  ? 8.370   19.941  24.670  1.00 37.12  ?  91  ALA B O   1 
ATOM   2319 C CB  . ALA B 2 91  ? 6.522   19.091  27.351  1.00 36.49  ?  91  ALA B CB  1 
ATOM   2320 N N   . VAL B 2 92  ? 6.286   20.789  24.840  1.00 35.99  ?  92  VAL B N   1 
ATOM   2321 C CA  . VAL B 2 92  ? 6.663   22.121  24.383  1.00 32.06  ?  92  VAL B CA  1 
ATOM   2322 C C   . VAL B 2 92  ? 7.052   22.946  25.601  1.00 33.13  ?  92  VAL B C   1 
ATOM   2323 O O   . VAL B 2 92  ? 6.337   22.957  26.610  1.00 32.33  ?  92  VAL B O   1 
ATOM   2324 C CB  . VAL B 2 92  ? 5.520   22.785  23.602  1.00 31.49  ?  92  VAL B CB  1 
ATOM   2325 C CG1 . VAL B 2 92  ? 5.871   24.247  23.287  1.00 32.81  ?  92  VAL B CG1 1 
ATOM   2326 C CG2 . VAL B 2 92  ? 5.245   22.023  22.326  1.00 26.91  ?  92  VAL B CG2 1 
ATOM   2327 N N   . TYR B 2 93  ? 8.204   23.606  25.527  1.00 32.38  ?  93  TYR B N   1 
ATOM   2328 C CA  . TYR B 2 93  ? 8.692   24.457  26.603  1.00 35.90  ?  93  TYR B CA  1 
ATOM   2329 C C   . TYR B 2 93  ? 8.614   25.916  26.167  1.00 40.25  ?  93  TYR B C   1 
ATOM   2330 O O   . TYR B 2 93  ? 9.162   26.287  25.117  1.00 42.82  ?  93  TYR B O   1 
ATOM   2331 C CB  . TYR B 2 93  ? 10.113  24.062  26.997  1.00 34.00  ?  93  TYR B CB  1 
ATOM   2332 C CG  . TYR B 2 93  ? 10.142  22.758  27.756  1.00 38.67  ?  93  TYR B CG  1 
ATOM   2333 C CD1 . TYR B 2 93  ? 10.268  22.740  29.138  1.00 36.35  ?  93  TYR B CD1 1 
ATOM   2334 C CD2 . TYR B 2 93  ? 10.015  21.541  27.091  1.00 35.60  ?  93  TYR B CD2 1 
ATOM   2335 C CE1 . TYR B 2 93  ? 10.274  21.542  29.838  1.00 38.45  ?  93  TYR B CE1 1 
ATOM   2336 C CE2 . TYR B 2 93  ? 10.022  20.344  27.779  1.00 39.50  ?  93  TYR B CE2 1 
ATOM   2337 C CZ  . TYR B 2 93  ? 10.153  20.348  29.153  1.00 42.05  ?  93  TYR B CZ  1 
ATOM   2338 O OH  . TYR B 2 93  ? 10.160  19.153  29.838  1.00 40.75  ?  93  TYR B OH  1 
ATOM   2339 N N   . TYR B 2 94  ? 7.907   26.722  26.965  1.00 38.91  ?  94  TYR B N   1 
ATOM   2340 C CA  . TYR B 2 94  ? 7.680   28.142  26.737  1.00 35.89  ?  94  TYR B CA  1 
ATOM   2341 C C   . TYR B 2 94  ? 8.491   28.960  27.728  1.00 34.49  ?  94  TYR B C   1 
ATOM   2342 O O   . TYR B 2 94  ? 8.462   28.703  28.943  1.00 33.87  ?  94  TYR B O   1 
ATOM   2343 C CB  . TYR B 2 94  ? 6.205   28.533  26.904  1.00 33.47  ?  94  TYR B CB  1 
ATOM   2344 C CG  . TYR B 2 94  ? 5.250   28.020  25.860  1.00 34.32  ?  94  TYR B CG  1 
ATOM   2345 C CD1 . TYR B 2 94  ? 4.418   26.942  26.123  1.00 35.56  ?  94  TYR B CD1 1 
ATOM   2346 C CD2 . TYR B 2 94  ? 5.157   28.635  24.622  1.00 33.72  ?  94  TYR B CD2 1 
ATOM   2347 C CE1 . TYR B 2 94  ? 3.533   26.479  25.170  1.00 37.68  ?  94  TYR B CE1 1 
ATOM   2348 C CE2 . TYR B 2 94  ? 4.277   28.181  23.666  1.00 34.06  ?  94  TYR B CE2 1 
ATOM   2349 C CZ  . TYR B 2 94  ? 3.467   27.105  23.943  1.00 38.42  ?  94  TYR B CZ  1 
ATOM   2350 O OH  . TYR B 2 94  ? 2.589   26.653  22.985  1.00 47.10  ?  94  TYR B OH  1 
ATOM   2351 N N   . CYS B 2 95  ? 9.203   29.936  27.188  1.00 39.42  ?  95  CYS B N   1 
ATOM   2352 C CA  . CYS B 2 95  ? 9.667   31.092  27.932  1.00 39.37  ?  95  CYS B CA  1 
ATOM   2353 C C   . CYS B 2 95  ? 8.482   32.012  28.228  1.00 39.49  ?  95  CYS B C   1 
ATOM   2354 O O   . CYS B 2 95  ? 7.643   32.255  27.356  1.00 31.51  ?  95  CYS B O   1 
ATOM   2355 C CB  . CYS B 2 95  ? 10.700  31.803  27.070  1.00 32.74  ?  95  CYS B CB  1 
ATOM   2356 S SG  . CYS B 2 95  ? 11.830  32.884  27.833  1.00 66.85  ?  95  CYS B SG  1 
ATOM   2357 N N   . ALA B 2 96  ? 8.402   32.533  29.455  1.00 35.40  ?  96  ALA B N   1 
ATOM   2358 C CA  . ALA B 2 96  ? 7.278   33.398  29.797  1.00 38.41  ?  96  ALA B CA  1 
ATOM   2359 C C   . ALA B 2 96  ? 7.698   34.451  30.815  1.00 38.92  ?  96  ALA B C   1 
ATOM   2360 O O   . ALA B 2 96  ? 8.392   34.151  31.788  1.00 45.69  ?  96  ALA B O   1 
ATOM   2361 C CB  . ALA B 2 96  ? 6.095   32.588  30.344  1.00 37.22  ?  96  ALA B CB  1 
ATOM   2362 N N   . ARG B 2 97  ? 7.258   35.683  30.593  1.00 34.60  ?  97  ARG B N   1 
ATOM   2363 C CA  . ARG B 2 97  ? 7.589   36.807  31.456  1.00 36.36  ?  97  ARG B CA  1 
ATOM   2364 C C   . ARG B 2 97  ? 6.425   37.082  32.401  1.00 35.12  ?  97  ARG B C   1 
ATOM   2365 O O   . ARG B 2 97  ? 5.288   37.260  31.954  1.00 33.27  ?  97  ARG B O   1 
ATOM   2366 C CB  . ARG B 2 97  ? 7.908   38.049  30.619  1.00 37.85  ?  97  ARG B CB  1 
ATOM   2367 C CG  . ARG B 2 97  ? 8.325   39.258  31.437  1.00 37.95  ?  97  ARG B CG  1 
ATOM   2368 C CD  . ARG B 2 97  ? 8.612   40.467  30.564  1.00 37.39  ?  97  ARG B CD  1 
ATOM   2369 N NE  . ARG B 2 97  ? 7.395   41.128  30.106  1.00 37.40  ?  97  ARG B NE  1 
ATOM   2370 C CZ  . ARG B 2 97  ? 7.385   42.231  29.363  1.00 39.20  ?  97  ARG B CZ  1 
ATOM   2371 N NH1 . ARG B 2 97  ? 6.236   42.775  28.987  1.00 42.06  ?  97  ARG B NH1 1 
ATOM   2372 N NH2 . ARG B 2 97  ? 8.526   42.806  29.012  1.00 35.93  ?  97  ARG B NH2 1 
ATOM   2373 N N   . GLU B 2 98  ? 6.710   37.114  33.701  1.00 36.83  ?  98  GLU B N   1 
ATOM   2374 C CA  . GLU B 2 98  ? 5.730   37.430  34.727  1.00 39.41  ?  98  GLU B CA  1 
ATOM   2375 C C   . GLU B 2 98  ? 5.895   38.886  35.148  1.00 44.26  ?  98  GLU B C   1 
ATOM   2376 O O   . GLU B 2 98  ? 6.985   39.303  35.558  1.00 47.14  ?  98  GLU B O   1 
ATOM   2377 C CB  . GLU B 2 98  ? 5.896   36.507  35.930  1.00 38.90  ?  98  GLU B CB  1 
ATOM   2378 C CG  . GLU B 2 98  ? 5.105   36.956  37.142  1.00 49.72  ?  98  GLU B CG  1 
ATOM   2379 C CD  . GLU B 2 98  ? 5.451   36.165  38.388  1.00 52.14  ?  98  GLU B CD  1 
ATOM   2380 O OE1 . GLU B 2 98  ? 4.895   36.469  39.466  1.00 53.07  ?  98  GLU B OE1 1 
ATOM   2381 O OE2 . GLU B 2 98  ? 6.268   35.225  38.281  1.00 51.89  ?  98  GLU B OE2 1 
ATOM   2382 N N   . ASP B 2 99  ? 4.818   39.653  35.057  1.00 46.07  ?  99  ASP B N   1 
ATOM   2383 C CA  . ASP B 2 99  ? 4.827   41.038  35.508  1.00 48.79  ?  99  ASP B CA  1 
ATOM   2384 C C   . ASP B 2 99  ? 4.401   41.074  36.969  1.00 48.16  ?  99  ASP B C   1 
ATOM   2385 O O   . ASP B 2 99  ? 3.252   40.760  37.294  1.00 48.20  ?  99  ASP B O   1 
ATOM   2386 C CB  . ASP B 2 99  ? 3.898   41.889  34.653  1.00 51.85  ?  99  ASP B CB  1 
ATOM   2387 C CG  . ASP B 2 99  ? 3.833   43.312  35.127  1.00 50.76  ?  99  ASP B CG  1 
ATOM   2388 O OD1 . ASP B 2 99  ? 4.849   44.026  34.980  1.00 43.74  ?  99  ASP B OD1 1 
ATOM   2389 O OD2 . ASP B 2 99  ? 2.774   43.700  35.669  1.00 55.84  ?  99  ASP B OD2 1 
ATOM   2390 N N   . VAL B 2 100 ? 5.333   41.442  37.855  1.00 50.66  ?  100 VAL B N   1 
ATOM   2391 C CA  . VAL B 2 100 ? 5.007   41.585  39.272  1.00 50.32  ?  100 VAL B CA  1 
ATOM   2392 C C   . VAL B 2 100 ? 4.642   43.009  39.659  1.00 47.59  ?  100 VAL B C   1 
ATOM   2393 O O   . VAL B 2 100 ? 4.118   43.222  40.763  1.00 47.52  ?  100 VAL B O   1 
ATOM   2394 C CB  . VAL B 2 100 ? 6.166   41.123  40.176  1.00 48.00  ?  100 VAL B CB  1 
ATOM   2395 C CG1 . VAL B 2 100 ? 6.507   39.673  39.896  1.00 47.80  ?  100 VAL B CG1 1 
ATOM   2396 C CG2 . VAL B 2 100 ? 7.370   42.019  39.984  1.00 47.42  ?  100 VAL B CG2 1 
ATOM   2397 N N   . ALA B 2 101 ? 4.904   43.992  38.798  1.00 48.34  ?  101 ALA B N   1 
ATOM   2398 C CA  . ALA B 2 101 ? 4.611   45.375  39.157  1.00 52.44  ?  101 ALA B CA  1 
ATOM   2399 C C   . ALA B 2 101 ? 3.119   45.571  39.390  1.00 50.83  ?  101 ALA B C   1 
ATOM   2400 O O   . ALA B 2 101 ? 2.706   46.104  40.425  1.00 50.76  ?  101 ALA B O   1 
ATOM   2401 C CB  . ALA B 2 101 ? 5.124   46.325  38.074  1.00 51.16  ?  101 ALA B CB  1 
ATOM   2402 N N   . VAL B 2 102 ? 2.293   45.114  38.452  1.00 51.28  ?  102 VAL B N   1 
ATOM   2403 C CA  . VAL B 2 102 ? 0.853   45.347  38.511  1.00 53.80  ?  102 VAL B CA  1 
ATOM   2404 C C   . VAL B 2 102 ? 0.078   44.041  38.396  1.00 48.35  ?  102 VAL B C   1 
ATOM   2405 O O   . VAL B 2 102 ? -0.731  43.702  39.267  1.00 48.19  ?  102 VAL B O   1 
ATOM   2406 C CB  . VAL B 2 102 ? 0.418   46.319  37.400  1.00 49.38  ?  102 VAL B CB  1 
ATOM   2407 C CG1 . VAL B 2 102 ? -1.090  46.514  37.425  1.00 42.33  ?  102 VAL B CG1 1 
ATOM   2408 C CG2 . VAL B 2 102 ? 1.148   47.637  37.540  1.00 48.23  ?  102 VAL B CG2 1 
ATOM   2409 N N   . TYR B 2 103 ? 0.330   43.305  37.312  1.00 46.61  ?  103 TYR B N   1 
ATOM   2410 C CA  . TYR B 2 103 ? -0.527  42.184  36.941  1.00 48.90  ?  103 TYR B CA  1 
ATOM   2411 C C   . TYR B 2 103 ? -0.467  41.049  37.954  1.00 46.41  ?  103 TYR B C   1 
ATOM   2412 O O   . TYR B 2 103 ? -1.503  40.469  38.300  1.00 47.84  ?  103 TYR B O   1 
ATOM   2413 C CB  . TYR B 2 103 ? -0.129  41.669  35.562  1.00 50.33  ?  103 TYR B CB  1 
ATOM   2414 C CG  . TYR B 2 103 ? -0.337  42.654  34.438  1.00 54.13  ?  103 TYR B CG  1 
ATOM   2415 C CD1 . TYR B 2 103 ? -1.381  43.565  34.469  1.00 53.95  ?  103 TYR B CD1 1 
ATOM   2416 C CD2 . TYR B 2 103 ? 0.515   42.669  33.341  1.00 54.14  ?  103 TYR B CD2 1 
ATOM   2417 C CE1 . TYR B 2 103 ? -1.574  44.460  33.435  1.00 61.87  ?  103 TYR B CE1 1 
ATOM   2418 C CE2 . TYR B 2 103 ? 0.330   43.558  32.304  1.00 58.61  ?  103 TYR B CE2 1 
ATOM   2419 C CZ  . TYR B 2 103 ? -0.713  44.452  32.354  1.00 67.20  ?  103 TYR B CZ  1 
ATOM   2420 O OH  . TYR B 2 103 ? -0.893  45.340  31.319  1.00 86.10  ?  103 TYR B OH  1 
ATOM   2421 N N   . MET B 2 104 ? 0.734   40.707  38.422  1.00 42.31  ?  104 MET B N   1 
ATOM   2422 C CA  . MET B 2 104 ? 0.982   39.427  39.083  1.00 42.67  ?  104 MET B CA  1 
ATOM   2423 C C   . MET B 2 104 ? 0.477   38.281  38.206  1.00 41.57  ?  104 MET B C   1 
ATOM   2424 O O   . MET B 2 104 ? -0.169  37.341  38.668  1.00 40.37  ?  104 MET B O   1 
ATOM   2425 C CB  . MET B 2 104 ? 0.360   39.384  40.479  1.00 41.36  ?  104 MET B CB  1 
ATOM   2426 C CG  . MET B 2 104 ? 1.057   40.286  41.501  1.00 48.29  ?  104 MET B CG  1 
ATOM   2427 S SD  . MET B 2 104 ? 2.789   39.848  41.810  1.00 49.52  ?  104 MET B SD  1 
ATOM   2428 C CE  . MET B 2 104 ? 2.596   38.294  42.678  1.00 46.21  ?  104 MET B CE  1 
ATOM   2429 N N   . ALA B 2 105 ? 0.798   38.369  36.917  1.00 41.04  ?  105 ALA B N   1 
ATOM   2430 C CA  . ALA B 2 105 ? 0.367   37.402  35.920  1.00 38.12  ?  105 ALA B CA  1 
ATOM   2431 C C   . ALA B 2 105 ? 1.436   37.336  34.836  1.00 39.67  ?  105 ALA B C   1 
ATOM   2432 O O   . ALA B 2 105 ? 2.438   38.055  34.885  1.00 41.09  ?  105 ALA B O   1 
ATOM   2433 C CB  . ALA B 2 105 ? -1.000  37.779  35.342  1.00 36.91  ?  105 ALA B CB  1 
ATOM   2434 N N   . ILE B 2 106 ? 1.231   36.452  33.865  1.00 35.97  ?  106 ILE B N   1 
ATOM   2435 C CA  . ILE B 2 106 ? 2.162   36.286  32.752  1.00 38.15  ?  106 ILE B CA  1 
ATOM   2436 C C   . ILE B 2 106 ? 1.682   37.140  31.586  1.00 40.80  ?  106 ILE B C   1 
ATOM   2437 O O   . ILE B 2 106 ? 0.554   36.975  31.107  1.00 46.74  ?  106 ILE B O   1 
ATOM   2438 C CB  . ILE B 2 106 ? 2.282   34.812  32.338  1.00 38.77  ?  106 ILE B CB  1 
ATOM   2439 C CG1 . ILE B 2 106 ? 2.956   33.999  33.443  1.00 38.57  ?  106 ILE B CG1 1 
ATOM   2440 C CG2 . ILE B 2 106 ? 3.059   34.690  31.031  1.00 37.43  ?  106 ILE B CG2 1 
ATOM   2441 C CD1 . ILE B 2 106 ? 3.068   32.522  33.126  1.00 37.77  ?  106 ILE B CD1 1 
ATOM   2442 N N   . ASP B 2 107 ? 2.541   38.038  31.108  1.00 36.89  ?  107 ASP B N   1 
ATOM   2443 C CA  . ASP B 2 107 ? 2.138   38.990  30.085  1.00 42.79  ?  107 ASP B CA  1 
ATOM   2444 C C   . ASP B 2 107 ? 2.877   38.846  28.760  1.00 42.87  ?  107 ASP B C   1 
ATOM   2445 O O   . ASP B 2 107 ? 2.564   39.580  27.819  1.00 46.47  ?  107 ASP B O   1 
ATOM   2446 C CB  . ASP B 2 107 ? 2.299   40.425  30.617  1.00 42.37  ?  107 ASP B CB  1 
ATOM   2447 C CG  . ASP B 2 107 ? 3.738   40.920  30.567  1.00 44.68  ?  107 ASP B CG  1 
ATOM   2448 O OD1 . ASP B 2 107 ? 3.929   42.137  30.372  1.00 50.88  ?  107 ASP B OD1 1 
ATOM   2449 O OD2 . ASP B 2 107 ? 4.678   40.108  30.708  1.00 43.09  ?  107 ASP B OD2 1 
ATOM   2450 N N   . LEU B 2 108 ? 3.824   37.920  28.639  1.00 39.90  ?  108 LEU B N   1 
ATOM   2451 C CA  . LEU B 2 108 ? 4.569   37.796  27.392  1.00 39.70  ?  108 LEU B CA  1 
ATOM   2452 C C   . LEU B 2 108 ? 5.096   36.376  27.283  1.00 36.83  ?  108 LEU B C   1 
ATOM   2453 O O   . LEU B 2 108 ? 5.762   35.894  28.197  1.00 39.97  ?  108 LEU B O   1 
ATOM   2454 C CB  . LEU B 2 108 ? 5.716   38.817  27.339  1.00 38.79  ?  108 LEU B CB  1 
ATOM   2455 C CG  . LEU B 2 108 ? 6.689   38.835  26.157  1.00 37.31  ?  108 LEU B CG  1 
ATOM   2456 C CD1 . LEU B 2 108 ? 6.005   39.272  24.881  1.00 33.04  ?  108 LEU B CD1 1 
ATOM   2457 C CD2 . LEU B 2 108 ? 7.860   39.747  26.461  1.00 34.62  ?  108 LEU B CD2 1 
ATOM   2458 N N   . TRP B 2 109 ? 4.803   35.709  26.176  1.00 37.14  ?  109 TRP B N   1 
ATOM   2459 C CA  . TRP B 2 109 ? 5.237   34.336  25.979  1.00 37.71  ?  109 TRP B CA  1 
ATOM   2460 C C   . TRP B 2 109 ? 6.200   34.247  24.803  1.00 38.32  ?  109 TRP B C   1 
ATOM   2461 O O   . TRP B 2 109 ? 6.146   35.058  23.874  1.00 42.07  ?  109 TRP B O   1 
ATOM   2462 C CB  . TRP B 2 109 ? 4.051   33.404  25.716  1.00 35.74  ?  109 TRP B CB  1 
ATOM   2463 C CG  . TRP B 2 109 ? 3.059   33.304  26.823  1.00 37.64  ?  109 TRP B CG  1 
ATOM   2464 C CD1 . TRP B 2 109 ? 2.156   34.254  27.209  1.00 40.55  ?  109 TRP B CD1 1 
ATOM   2465 C CD2 . TRP B 2 109 ? 2.839   32.173  27.672  1.00 42.34  ?  109 TRP B CD2 1 
ATOM   2466 N NE1 . TRP B 2 109 ? 1.397   33.788  28.256  1.00 39.67  ?  109 TRP B NE1 1 
ATOM   2467 C CE2 . TRP B 2 109 ? 1.793   32.512  28.559  1.00 41.90  ?  109 TRP B CE2 1 
ATOM   2468 C CE3 . TRP B 2 109 ? 3.424   30.903  27.771  1.00 38.27  ?  109 TRP B CE3 1 
ATOM   2469 C CZ2 . TRP B 2 109 ? 1.325   31.629  29.536  1.00 43.42  ?  109 TRP B CZ2 1 
ATOM   2470 C CZ3 . TRP B 2 109 ? 2.952   30.022  28.741  1.00 37.33  ?  109 TRP B CZ3 1 
ATOM   2471 C CH2 . TRP B 2 109 ? 1.916   30.391  29.611  1.00 40.05  ?  109 TRP B CH2 1 
ATOM   2472 N N   . GLY B 2 110 ? 7.079   33.243  24.843  1.00 38.26  ?  110 GLY B N   1 
ATOM   2473 C CA  . GLY B 2 110 ? 7.835   32.865  23.670  1.00 39.08  ?  110 GLY B CA  1 
ATOM   2474 C C   . GLY B 2 110 ? 7.003   32.003  22.737  1.00 41.40  ?  110 GLY B C   1 
ATOM   2475 O O   . GLY B 2 110 ? 5.846   31.679  23.002  1.00 33.10  ?  110 GLY B O   1 
ATOM   2476 N N   . GLN B 2 111 ? 7.622   31.589  21.631  1.00 43.41  ?  111 GLN B N   1 
ATOM   2477 C CA  . GLN B 2 111 ? 6.895   30.753  20.682  1.00 43.81  ?  111 GLN B CA  1 
ATOM   2478 C C   . GLN B 2 111 ? 6.909   29.273  21.059  1.00 46.99  ?  111 GLN B C   1 
ATOM   2479 O O   . GLN B 2 111 ? 6.109   28.509  20.509  1.00 44.96  ?  111 GLN B O   1 
ATOM   2480 C CB  . GLN B 2 111 ? 7.462   30.937  19.270  1.00 45.45  ?  111 GLN B CB  1 
ATOM   2481 C CG  . GLN B 2 111 ? 8.574   29.962  18.884  1.00 63.14  ?  111 GLN B CG  1 
ATOM   2482 C CD  . GLN B 2 111 ? 9.962   30.436  19.301  1.00 65.19  ?  111 GLN B CD  1 
ATOM   2483 O OE1 . GLN B 2 111 ? 10.104  31.433  20.013  1.00 63.32  ?  111 GLN B OE1 1 
ATOM   2484 N NE2 . GLN B 2 111 ? 10.994  29.730  18.842  1.00 63.60  ?  111 GLN B NE2 1 
ATOM   2485 N N   . GLY B 2 112 ? 7.760   28.856  21.992  1.00 44.75  ?  112 GLY B N   1 
ATOM   2486 C CA  . GLY B 2 112 ? 7.864   27.468  22.425  1.00 41.31  ?  112 GLY B CA  1 
ATOM   2487 C C   . GLY B 2 112 ? 8.824   26.670  21.564  1.00 47.15  ?  112 GLY B C   1 
ATOM   2488 O O   . GLY B 2 112 ? 8.969   26.887  20.359  1.00 48.74  ?  112 GLY B O   1 
ATOM   2489 N N   . THR B 2 113 ? 9.521   25.735  22.210  1.00 42.64  ?  113 THR B N   1 
ATOM   2490 C CA  . THR B 2 113 ? 10.324  24.749  21.495  1.00 42.80  ?  113 THR B CA  1 
ATOM   2491 C C   . THR B 2 113 ? 9.936   23.358  21.960  1.00 39.39  ?  113 THR B C   1 
ATOM   2492 O O   . THR B 2 113 ? 9.742   23.119  23.159  1.00 36.88  ?  113 THR B O   1 
ATOM   2493 C CB  . THR B 2 113 ? 11.840  24.936  21.693  1.00 43.64  ?  113 THR B CB  1 
ATOM   2494 O OG1 . THR B 2 113 ? 12.161  24.982  23.085  1.00 44.84  ?  113 THR B OG1 1 
ATOM   2495 C CG2 . THR B 2 113 ? 12.329  26.201  21.017  1.00 54.70  ?  113 THR B CG2 1 
ATOM   2496 N N   . LEU B 2 114 ? 9.826   22.446  21.006  1.00 40.85  ?  114 LEU B N   1 
ATOM   2497 C CA  . LEU B 2 114 ? 9.477   21.075  21.324  1.00 33.70  ?  114 LEU B CA  1 
ATOM   2498 C C   . LEU B 2 114 ? 10.723  20.341  21.798  1.00 38.10  ?  114 LEU B C   1 
ATOM   2499 O O   . LEU B 2 114 ? 11.784  20.432  21.171  1.00 34.45  ?  114 LEU B O   1 
ATOM   2500 C CB  . LEU B 2 114 ? 8.890   20.379  20.105  1.00 32.62  ?  114 LEU B CB  1 
ATOM   2501 C CG  . LEU B 2 114 ? 8.575   18.896  20.347  1.00 43.51  ?  114 LEU B CG  1 
ATOM   2502 C CD1 . LEU B 2 114 ? 7.529   18.719  21.449  1.00 36.76  ?  114 LEU B CD1 1 
ATOM   2503 C CD2 . LEU B 2 114 ? 8.135   18.230  19.069  1.00 42.84  ?  114 LEU B CD2 1 
ATOM   2504 N N   . VAL B 2 115 ? 10.599  19.638  22.920  1.00 37.54  ?  115 VAL B N   1 
ATOM   2505 C CA  . VAL B 2 115 ? 11.628  18.747  23.438  1.00 39.54  ?  115 VAL B CA  1 
ATOM   2506 C C   . VAL B 2 115 ? 11.075  17.332  23.377  1.00 39.72  ?  115 VAL B C   1 
ATOM   2507 O O   . VAL B 2 115 ? 10.074  17.020  24.041  1.00 39.21  ?  115 VAL B O   1 
ATOM   2508 C CB  . VAL B 2 115 ? 12.031  19.112  24.873  1.00 38.92  ?  115 VAL B CB  1 
ATOM   2509 C CG1 . VAL B 2 115 ? 12.970  18.059  25.428  1.00 35.67  ?  115 VAL B CG1 1 
ATOM   2510 C CG2 . VAL B 2 115 ? 12.676  20.490  24.906  1.00 34.03  ?  115 VAL B CG2 1 
ATOM   2511 N N   . THR B 2 116 ? 11.721  16.487  22.577  1.00 36.14  ?  116 THR B N   1 
ATOM   2512 C CA  . THR B 2 116 ? 11.361  15.082  22.435  1.00 37.25  ?  116 THR B CA  1 
ATOM   2513 C C   . THR B 2 116 ? 12.433  14.247  23.119  1.00 41.34  ?  116 THR B C   1 
ATOM   2514 O O   . THR B 2 116 ? 13.603  14.275  22.713  1.00 37.38  ?  116 THR B O   1 
ATOM   2515 C CB  . THR B 2 116 ? 11.246  14.675  20.966  1.00 40.29  ?  116 THR B CB  1 
ATOM   2516 O OG1 . THR B 2 116 ? 10.391  15.590  20.274  1.00 47.93  ?  116 THR B OG1 1 
ATOM   2517 C CG2 . THR B 2 116 ? 10.664  13.276  20.853  1.00 37.05  ?  116 THR B CG2 1 
ATOM   2518 N N   . VAL B 2 117 ? 12.039  13.514  24.151  1.00 34.78  ?  117 VAL B N   1 
ATOM   2519 C CA  . VAL B 2 117 ? 12.957  12.658  24.887  1.00 42.74  ?  117 VAL B CA  1 
ATOM   2520 C C   . VAL B 2 117 ? 12.689  11.233  24.418  1.00 42.54  ?  117 VAL B C   1 
ATOM   2521 O O   . VAL B 2 117 ? 11.746  10.582  24.871  1.00 44.41  ?  117 VAL B O   1 
ATOM   2522 C CB  . VAL B 2 117 ? 12.783  12.805  26.399  1.00 46.43  ?  117 VAL B CB  1 
ATOM   2523 C CG1 . VAL B 2 117 ? 13.852  12.003  27.132  1.00 43.71  ?  117 VAL B CG1 1 
ATOM   2524 C CG2 . VAL B 2 117 ? 12.816  14.279  26.800  1.00 38.63  ?  117 VAL B CG2 1 
ATOM   2525 N N   . SER B 2 118 ? 13.522  10.739  23.510  1.00 42.71  ?  118 SER B N   1 
ATOM   2526 C CA  . SER B 2 118 ? 13.288  9.425   22.938  1.00 44.11  ?  118 SER B CA  1 
ATOM   2527 C C   . SER B 2 118 ? 14.612  8.808   22.516  1.00 48.18  ?  118 SER B C   1 
ATOM   2528 O O   . SER B 2 118 ? 15.598  9.506   22.258  1.00 51.50  ?  118 SER B O   1 
ATOM   2529 C CB  . SER B 2 118 ? 12.331  9.509   21.745  1.00 44.20  ?  118 SER B CB  1 
ATOM   2530 O OG  . SER B 2 118 ? 12.132  8.236   21.158  1.00 50.90  ?  118 SER B OG  1 
ATOM   2531 N N   . SER B 2 119 ? 14.614  7.481   22.423  1.00 49.79  ?  119 SER B N   1 
ATOM   2532 C CA  . SER B 2 119 ? 15.771  6.745   21.940  1.00 49.65  ?  119 SER B CA  1 
ATOM   2533 C C   . SER B 2 119 ? 15.675  6.420   20.456  1.00 46.59  ?  119 SER B C   1 
ATOM   2534 O O   . SER B 2 119 ? 16.647  5.916   19.883  1.00 47.67  ?  119 SER B O   1 
ATOM   2535 C CB  . SER B 2 119 ? 15.957  5.453   22.749  1.00 42.93  ?  119 SER B CB  1 
ATOM   2536 O OG  . SER B 2 119 ? 14.719  4.789   22.956  1.00 51.40  ?  119 SER B OG  1 
ATOM   2537 N N   . ALA B 2 120 ? 14.543  6.718   19.823  1.00 45.69  ?  120 ALA B N   1 
ATOM   2538 C CA  . ALA B 2 120 ? 14.403  6.516   18.390  1.00 47.33  ?  120 ALA B CA  1 
ATOM   2539 C C   . ALA B 2 120 ? 15.321  7.468   17.626  1.00 47.58  ?  120 ALA B C   1 
ATOM   2540 O O   . ALA B 2 120 ? 15.820  8.463   18.159  1.00 49.12  ?  120 ALA B O   1 
ATOM   2541 C CB  . ALA B 2 120 ? 12.946  6.710   17.961  1.00 43.91  ?  120 ALA B CB  1 
ATOM   2542 N N   . SER B 2 121 ? 15.522  7.166   16.350  1.00 49.32  ?  121 SER B N   1 
ATOM   2543 C CA  . SER B 2 121 ? 16.452  7.916   15.522  1.00 46.04  ?  121 SER B CA  1 
ATOM   2544 C C   . SER B 2 121 ? 15.719  8.906   14.629  1.00 44.32  ?  121 SER B C   1 
ATOM   2545 O O   . SER B 2 121 ? 14.579  8.682   14.215  1.00 47.08  ?  121 SER B O   1 
ATOM   2546 C CB  . SER B 2 121 ? 17.298  6.974   14.662  1.00 55.53  ?  121 SER B CB  1 
ATOM   2547 O OG  . SER B 2 121 ? 18.222  6.251   15.460  1.00 65.68  ?  121 SER B OG  1 
ATOM   2548 N N   . THR B 2 122 ? 16.392  10.014  14.345  1.00 44.49  ?  122 THR B N   1 
ATOM   2549 C CA  . THR B 2 122 ? 15.859  10.989  13.412  1.00 44.02  ?  122 THR B CA  1 
ATOM   2550 C C   . THR B 2 122 ? 15.672  10.353  12.040  1.00 49.27  ?  122 THR B C   1 
ATOM   2551 O O   . THR B 2 122 ? 16.552  9.644   11.543  1.00 48.97  ?  122 THR B O   1 
ATOM   2552 C CB  . THR B 2 122 ? 16.792  12.198  13.332  1.00 39.71  ?  122 THR B CB  1 
ATOM   2553 O OG1 . THR B 2 122 ? 16.784  12.880  14.592  1.00 49.62  ?  122 THR B OG1 1 
ATOM   2554 C CG2 . THR B 2 122 ? 16.339  13.165  12.249  1.00 37.34  ?  122 THR B CG2 1 
ATOM   2555 N N   . LYS B 2 123 ? 14.504  10.584  11.444  1.00 47.38  ?  123 LYS B N   1 
ATOM   2556 C CA  . LYS B 2 123 ? 14.224  10.142  10.086  1.00 46.01  ?  123 LYS B CA  1 
ATOM   2557 C C   . LYS B 2 123 ? 13.450  11.237  9.372   1.00 44.05  ?  123 LYS B C   1 
ATOM   2558 O O   . LYS B 2 123 ? 12.478  11.765  9.915   1.00 44.31  ?  123 LYS B O   1 
ATOM   2559 C CB  . LYS B 2 123 ? 13.425  8.836   10.082  1.00 50.84  ?  123 LYS B CB  1 
ATOM   2560 C CG  . LYS B 2 123 ? 13.188  8.246   8.697   1.00 57.67  ?  123 LYS B CG  1 
ATOM   2561 C CD  . LYS B 2 123 ? 12.460  6.911   8.790   1.00 59.45  ?  123 LYS B CD  1 
ATOM   2562 C CE  . LYS B 2 123 ? 12.105  6.365   7.416   1.00 56.25  ?  123 LYS B CE  1 
ATOM   2563 N NZ  . LYS B 2 123 ? 13.319  6.095   6.600   1.00 64.55  ?  123 LYS B NZ  1 
ATOM   2564 N N   . GLY B 2 124 ? 13.886  11.575  8.163   1.00 42.80  ?  124 GLY B N   1 
ATOM   2565 C CA  . GLY B 2 124 ? 13.199  12.543  7.346   1.00 40.90  ?  124 GLY B CA  1 
ATOM   2566 C C   . GLY B 2 124 ? 11.979  11.945  6.680   1.00 42.76  ?  124 GLY B C   1 
ATOM   2567 O O   . GLY B 2 124 ? 11.859  10.727  6.536   1.00 44.89  ?  124 GLY B O   1 
ATOM   2568 N N   . PRO B 2 125 ? 11.055  12.794  6.241   1.00 48.05  ?  125 PRO B N   1 
ATOM   2569 C CA  . PRO B 2 125 ? 9.769   12.305  5.739   1.00 46.72  ?  125 PRO B CA  1 
ATOM   2570 C C   . PRO B 2 125 ? 9.760   11.955  4.259   1.00 47.78  ?  125 PRO B C   1 
ATOM   2571 O O   . PRO B 2 125 ? 10.466  12.539  3.434   1.00 46.53  ?  125 PRO B O   1 
ATOM   2572 C CB  . PRO B 2 125 ? 8.838   13.493  6.006   1.00 43.21  ?  125 PRO B CB  1 
ATOM   2573 C CG  . PRO B 2 125 ? 9.721   14.675  5.805   1.00 42.72  ?  125 PRO B CG  1 
ATOM   2574 C CD  . PRO B 2 125 ? 11.091  14.266  6.309   1.00 47.06  ?  125 PRO B CD  1 
ATOM   2575 N N   . SER B 2 126 ? 8.915   10.981  3.934   1.00 47.58  ?  126 SER B N   1 
ATOM   2576 C CA  . SER B 2 126 ? 8.540   10.705  2.558   1.00 42.51  ?  126 SER B CA  1 
ATOM   2577 C C   . SER B 2 126 ? 7.296   11.518  2.234   1.00 46.18  ?  126 SER B C   1 
ATOM   2578 O O   . SER B 2 126 ? 6.392   11.638  3.063   1.00 46.75  ?  126 SER B O   1 
ATOM   2579 C CB  . SER B 2 126 ? 8.258   9.215   2.357   1.00 47.05  ?  126 SER B CB  1 
ATOM   2580 O OG  . SER B 2 126 ? 9.269   8.413   2.946   1.00 53.17  ?  126 SER B OG  1 
ATOM   2581 N N   . VAL B 2 127 ? 7.268   12.118  1.049   1.00 44.43  ?  127 VAL B N   1 
ATOM   2582 C CA  . VAL B 2 127 ? 6.159   12.977  0.645   1.00 39.95  ?  127 VAL B CA  1 
ATOM   2583 C C   . VAL B 2 127 ? 5.559   12.402  -0.627  1.00 43.01  ?  127 VAL B C   1 
ATOM   2584 O O   . VAL B 2 127 ? 6.241   12.296  -1.652  1.00 48.63  ?  127 VAL B O   1 
ATOM   2585 C CB  . VAL B 2 127 ? 6.596   14.435  0.444   1.00 42.75  ?  127 VAL B CB  1 
ATOM   2586 C CG1 . VAL B 2 127 ? 5.411   15.287  0.039   1.00 41.69  ?  127 VAL B CG1 1 
ATOM   2587 C CG2 . VAL B 2 127 ? 7.227   14.975  1.717   1.00 42.56  ?  127 VAL B CG2 1 
ATOM   2588 N N   . PHE B 2 128 ? 4.293   12.025  -0.557  1.00 44.62  ?  128 PHE B N   1 
ATOM   2589 C CA  . PHE B 2 128 ? 3.556   11.482  -1.683  1.00 40.82  ?  128 PHE B CA  1 
ATOM   2590 C C   . PHE B 2 128 ? 2.409   12.412  -2.044  1.00 46.30  ?  128 PHE B C   1 
ATOM   2591 O O   . PHE B 2 128 ? 1.938   13.189  -1.204  1.00 47.53  ?  128 PHE B O   1 
ATOM   2592 C CB  . PHE B 2 128 ? 3.026   10.078  -1.359  1.00 40.46  ?  128 PHE B CB  1 
ATOM   2593 C CG  . PHE B 2 128 ? 4.103   9.120   -0.943  1.00 48.35  ?  128 PHE B CG  1 
ATOM   2594 C CD1 . PHE B 2 128 ? 5.043   8.678   -1.861  1.00 51.68  ?  128 PHE B CD1 1 
ATOM   2595 C CD2 . PHE B 2 128 ? 4.183   8.663   0.366   1.00 47.06  ?  128 PHE B CD2 1 
ATOM   2596 C CE1 . PHE B 2 128 ? 6.045   7.800   -1.485  1.00 50.82  ?  128 PHE B CE1 1 
ATOM   2597 C CE2 . PHE B 2 128 ? 5.181   7.787   0.749   1.00 47.68  ?  128 PHE B CE2 1 
ATOM   2598 C CZ  . PHE B 2 128 ? 6.114   7.352   -0.180  1.00 46.85  ?  128 PHE B CZ  1 
ATOM   2599 N N   . PRO B 2 129 ? 1.949   12.383  -3.294  1.00 50.18  ?  129 PRO B N   1 
ATOM   2600 C CA  . PRO B 2 129 ? 0.849   13.265  -3.697  1.00 44.24  ?  129 PRO B CA  1 
ATOM   2601 C C   . PRO B 2 129 ? -0.511  12.593  -3.591  1.00 51.17  ?  129 PRO B C   1 
ATOM   2602 O O   . PRO B 2 129 ? -0.682  11.412  -3.905  1.00 55.37  ?  129 PRO B O   1 
ATOM   2603 C CB  . PRO B 2 129 ? 1.190   13.576  -5.159  1.00 46.60  ?  129 PRO B CB  1 
ATOM   2604 C CG  . PRO B 2 129 ? 2.049   12.396  -5.625  1.00 47.72  ?  129 PRO B CG  1 
ATOM   2605 C CD  . PRO B 2 129 ? 2.435   11.574  -4.423  1.00 47.47  ?  129 PRO B CD  1 
ATOM   2606 N N   . LEU B 2 130 ? -1.489  13.359  -3.105  1.00 45.94  ?  130 LEU B N   1 
ATOM   2607 C CA  . LEU B 2 130 ? -2.904  12.996  -3.155  1.00 45.43  ?  130 LEU B CA  1 
ATOM   2608 C C   . LEU B 2 130 ? -3.532  13.805  -4.288  1.00 49.61  ?  130 LEU B C   1 
ATOM   2609 O O   . LEU B 2 130 ? -3.855  14.983  -4.109  1.00 53.80  ?  130 LEU B O   1 
ATOM   2610 C CB  . LEU B 2 130 ? -3.572  13.280  -1.815  1.00 47.24  ?  130 LEU B CB  1 
ATOM   2611 C CG  . LEU B 2 130 ? -2.901  12.652  -0.593  1.00 42.50  ?  130 LEU B CG  1 
ATOM   2612 C CD1 . LEU B 2 130 ? -3.299  13.380  0.679   1.00 40.01  ?  130 LEU B CD1 1 
ATOM   2613 C CD2 . LEU B 2 130 ? -3.274  11.187  -0.503  1.00 40.45  ?  130 LEU B CD2 1 
ATOM   2614 N N   . ALA B 2 131 ? -3.670  13.185  -5.462  1.00 49.74  ?  131 ALA B N   1 
ATOM   2615 C CA  . ALA B 2 131 ? -4.031  13.804  -6.736  1.00 52.21  ?  131 ALA B CA  1 
ATOM   2616 C C   . ALA B 2 131 ? -5.546  13.905  -6.903  1.00 59.53  ?  131 ALA B C   1 
ATOM   2617 O O   . ALA B 2 131 ? -6.276  12.980  -6.533  1.00 60.39  ?  131 ALA B O   1 
ATOM   2618 C CB  . ALA B 2 131 ? -3.450  13.010  -7.902  1.00 60.28  ?  131 ALA B CB  1 
ATOM   2619 N N   . PRO B 2 132 ? -6.020  15.029  -7.460  1.00 67.85  ?  132 PRO B N   1 
ATOM   2620 C CA  . PRO B 2 132 ? -7.455  15.189  -7.743  1.00 72.26  ?  132 PRO B CA  1 
ATOM   2621 C C   . PRO B 2 132 ? -7.854  14.719  -9.138  1.00 79.87  ?  132 PRO B C   1 
ATOM   2622 O O   . PRO B 2 132 ? -7.085  14.028  -9.813  1.00 82.37  ?  132 PRO B O   1 
ATOM   2623 C CB  . PRO B 2 132 ? -7.660  16.699  -7.585  1.00 70.91  ?  132 PRO B CB  1 
ATOM   2624 C CG  . PRO B 2 132 ? -6.355  17.280  -8.050  1.00 66.87  ?  132 PRO B CG  1 
ATOM   2625 C CD  . PRO B 2 132 ? -5.279  16.291  -7.645  1.00 63.91  ?  132 PRO B CD  1 
ATOM   2626 N N   . SER B 2 133 ? -9.076  15.077  -9.557  1.00 87.71  ?  133 SER B N   1 
ATOM   2627 C CA  . SER B 2 133 ? -9.577  14.901  -10.928 1.00 91.75  ?  133 SER B CA  1 
ATOM   2628 C C   . SER B 2 133 ? -9.866  13.444  -11.274 1.00 97.46  ?  133 SER B C   1 
ATOM   2629 O O   . SER B 2 133 ? -9.809  13.054  -12.444 1.00 102.88 ?  133 SER B O   1 
ATOM   2630 C CB  . SER B 2 133 ? -8.628  15.502  -11.972 1.00 88.37  ?  133 SER B CB  1 
ATOM   2631 O OG  . SER B 2 133 ? -9.333  15.828  -13.161 1.00 89.89  ?  133 SER B OG  1 
ATOM   2632 N N   . SER B 2 134 ? -10.183 12.629  -10.272 1.00 94.07  ?  134 SER B N   1 
ATOM   2633 C CA  . SER B 2 134 ? -10.503 11.226  -10.501 1.00 100.24 ?  134 SER B CA  1 
ATOM   2634 C C   . SER B 2 134 ? -11.800 11.109  -9.709  1.00 103.08 ?  134 SER B C   1 
ATOM   2635 O O   . SER B 2 134 ? -12.870 11.508  -10.181 1.00 100.57 ?  134 SER B O   1 
ATOM   2636 C CB  . SER B 2 134 ? -9.333  10.341  -10.051 1.00 100.97 ?  134 SER B CB  1 
ATOM   2637 O OG  . SER B 2 134 ? -8.952  10.626  -8.708  1.00 91.69  ?  134 SER B OG  1 
ATOM   2638 N N   . LYS B 2 135 ? -11.652 10.687  -8.431  1.00 100.23 ?  135 LYS B N   1 
ATOM   2639 C CA  . LYS B 2 135 ? -12.801 10.449  -7.565  1.00 94.10  ?  135 LYS B CA  1 
ATOM   2640 C C   . LYS B 2 135 ? -12.667 11.464  -6.439  1.00 87.48  ?  135 LYS B C   1 
ATOM   2641 O O   . LYS B 2 135 ? -13.163 11.256  -5.327  1.00 72.82  ?  135 LYS B O   1 
ATOM   2642 C CB  . LYS B 2 135 ? -12.965 9.016   -7.056  1.00 83.10  ?  135 LYS B CB  1 
ATOM   2643 C CG  . LYS B 2 135 ? -13.034 8.054   -8.225  1.00 82.00  ?  135 LYS B CG  1 
ATOM   2644 C CD  . LYS B 2 135 ? -14.283 8.408   -9.047  1.00 91.55  ?  135 LYS B CD  1 
ATOM   2645 C CE  . LYS B 2 135 ? -14.307 7.771   -10.432 1.00 97.07  ?  135 LYS B CE  1 
ATOM   2646 N NZ  . LYS B 2 135 ? -15.707 7.539   -10.909 1.00 89.54  ?  135 LYS B NZ  1 
ATOM   2647 N N   . SER B 2 136 ? -11.955 12.554  -6.734  1.00 90.49  ?  136 SER B N   1 
ATOM   2648 C CA  . SER B 2 136 ? -11.728 13.665  -5.820  1.00 84.72  ?  136 SER B CA  1 
ATOM   2649 C C   . SER B 2 136 ? -12.368 14.949  -6.347  1.00 79.99  ?  136 SER B C   1 
ATOM   2650 O O   . SER B 2 136 ? -11.888 16.048  -6.061  1.00 72.70  ?  136 SER B O   1 
ATOM   2651 C CB  . SER B 2 136 ? -10.230 13.878  -5.590  1.00 73.07  ?  136 SER B CB  1 
ATOM   2652 O OG  . SER B 2 136 ? -9.539  12.640  -5.528  1.00 72.85  ?  136 SER B OG  1 
ATOM   2653 N N   . THR B 2 137 ? -13.437 14.825  -7.141  1.00 81.65  ?  137 THR B N   1 
ATOM   2654 C CA  . THR B 2 137 ? -14.165 15.971  -7.688  1.00 83.98  ?  137 THR B CA  1 
ATOM   2655 C C   . THR B 2 137 ? -15.665 15.750  -7.513  1.00 82.98  ?  137 THR B C   1 
ATOM   2656 O O   . THR B 2 137 ? -16.248 14.879  -8.168  1.00 82.02  ?  137 THR B O   1 
ATOM   2657 C CB  . THR B 2 137 ? -13.828 16.191  -9.167  1.00 87.38  ?  137 THR B CB  1 
ATOM   2658 O OG1 . THR B 2 137 ? -14.113 15.000  -9.912  1.00 88.87  ?  137 THR B OG1 1 
ATOM   2659 C CG2 . THR B 2 137 ? -12.358 16.564  -9.344  1.00 81.47  ?  137 THR B CG2 1 
ATOM   2660 N N   . SER B 2 138 ? -16.295 16.557  -6.654  1.00 79.66  ?  138 SER B N   1 
ATOM   2661 C CA  . SER B 2 138 ? -17.739 16.490  -6.425  1.00 86.87  ?  138 SER B CA  1 
ATOM   2662 C C   . SER B 2 138 ? -18.306 17.905  -6.421  1.00 86.69  ?  138 SER B C   1 
ATOM   2663 O O   . SER B 2 138 ? -18.036 18.682  -5.499  1.00 80.76  ?  138 SER B O   1 
ATOM   2664 C CB  . SER B 2 138 ? -18.081 15.767  -5.117  1.00 83.25  ?  138 SER B CB  1 
ATOM   2665 O OG  . SER B 2 138 ? -17.721 14.395  -5.162  1.00 85.88  ?  138 SER B OG  1 
ATOM   2666 N N   . GLY B 2 139 ? -19.087 18.235  -7.449  1.00 85.61  ?  139 GLY B N   1 
ATOM   2667 C CA  . GLY B 2 139 ? -19.681 19.552  -7.571  1.00 75.28  ?  139 GLY B CA  1 
ATOM   2668 C C   . GLY B 2 139 ? -18.710 20.671  -7.886  1.00 78.94  ?  139 GLY B C   1 
ATOM   2669 O O   . GLY B 2 139 ? -18.683 21.686  -7.184  1.00 84.23  ?  139 GLY B O   1 
ATOM   2670 N N   . GLY B 2 140 ? -17.904 20.499  -8.932  1.00 77.42  ?  140 GLY B N   1 
ATOM   2671 C CA  . GLY B 2 140 ? -16.989 21.535  -9.376  1.00 74.60  ?  140 GLY B CA  1 
ATOM   2672 C C   . GLY B 2 140 ? -15.885 21.876  -8.395  1.00 71.59  ?  140 GLY B C   1 
ATOM   2673 O O   . GLY B 2 140 ? -15.080 22.777  -8.643  1.00 72.86  ?  140 GLY B O   1 
ATOM   2674 N N   . THR B 2 141 ? -15.835 21.165  -7.276  1.00 72.86  ?  141 THR B N   1 
ATOM   2675 C CA  . THR B 2 141 ? -14.803 21.342  -6.265  1.00 68.60  ?  141 THR B CA  1 
ATOM   2676 C C   . THR B 2 141 ? -13.939 20.091  -6.219  1.00 68.76  ?  141 THR B C   1 
ATOM   2677 O O   . THR B 2 141 ? -14.458 18.981  -6.066  1.00 69.91  ?  141 THR B O   1 
ATOM   2678 C CB  . THR B 2 141 ? -15.411 21.610  -4.888  1.00 73.68  ?  141 THR B CB  1 
ATOM   2679 O OG1 . THR B 2 141 ? -16.007 22.912  -4.867  1.00 76.09  ?  141 THR B OG1 1 
ATOM   2680 C CG2 . THR B 2 141 ? -14.337 21.525  -3.813  1.00 68.00  ?  141 THR B CG2 1 
ATOM   2681 N N   . ALA B 2 142 ? -12.632 20.268  -6.362  1.00 68.33  ?  142 ALA B N   1 
ATOM   2682 C CA  . ALA B 2 142 ? -11.683 19.178  -6.230  1.00 62.62  ?  142 ALA B CA  1 
ATOM   2683 C C   . ALA B 2 142 ? -10.944 19.295  -4.905  1.00 56.62  ?  142 ALA B C   1 
ATOM   2684 O O   . ALA B 2 142 ? -10.887 20.361  -4.289  1.00 55.43  ?  142 ALA B O   1 
ATOM   2685 C CB  . ALA B 2 142 ? -10.682 19.172  -7.391  1.00 65.31  ?  142 ALA B CB  1 
ATOM   2686 N N   . ALA B 2 143 ? -10.397 18.171  -4.460  1.00 61.80  ?  143 ALA B N   1 
ATOM   2687 C CA  . ALA B 2 143 ? -9.539  18.120  -3.287  1.00 56.42  ?  143 ALA B CA  1 
ATOM   2688 C C   . ALA B 2 143 ? -8.208  17.503  -3.689  1.00 55.90  ?  143 ALA B C   1 
ATOM   2689 O O   . ALA B 2 143 ? -8.172  16.548  -4.473  1.00 53.67  ?  143 ALA B O   1 
ATOM   2690 C CB  . ALA B 2 143 ? -10.182 17.312  -2.155  1.00 50.35  ?  143 ALA B CB  1 
ATOM   2691 N N   . LEU B 2 144 ? -7.113  18.064  -3.174  1.00 52.86  ?  144 LEU B N   1 
ATOM   2692 C CA  . LEU B 2 144 ? -5.782  17.523  -3.425  1.00 47.75  ?  144 LEU B CA  1 
ATOM   2693 C C   . LEU B 2 144 ? -4.951  17.716  -2.166  1.00 47.92  ?  144 LEU B C   1 
ATOM   2694 O O   . LEU B 2 144 ? -5.379  18.381  -1.223  1.00 47.78  ?  144 LEU B O   1 
ATOM   2695 C CB  . LEU B 2 144 ? -5.119  18.184  -4.642  1.00 47.95  ?  144 LEU B CB  1 
ATOM   2696 C CG  . LEU B 2 144 ? -4.967  19.707  -4.625  1.00 50.34  ?  144 LEU B CG  1 
ATOM   2697 C CD1 . LEU B 2 144 ? -3.534  20.082  -4.305  1.00 54.27  ?  144 LEU B CD1 1 
ATOM   2698 C CD2 . LEU B 2 144 ? -5.401  20.331  -5.941  1.00 54.84  ?  144 LEU B CD2 1 
ATOM   2699 N N   . GLY B 2 145 ? -3.770  17.109  -2.129  1.00 50.79  ?  145 GLY B N   1 
ATOM   2700 C CA  . GLY B 2 145 ? -2.934  17.287  -0.954  1.00 46.93  ?  145 GLY B CA  1 
ATOM   2701 C C   . GLY B 2 145 ? -1.622  16.534  -1.027  1.00 45.56  ?  145 GLY B C   1 
ATOM   2702 O O   . GLY B 2 145 ? -1.220  16.027  -2.074  1.00 46.71  ?  145 GLY B O   1 
ATOM   2703 N N   . CYS B 2 146 ? -0.974  16.468  0.137   1.00 41.78  ?  146 CYS B N   1 
ATOM   2704 C CA  . CYS B 2 146 ? 0.316   15.821  0.343   1.00 46.53  ?  146 CYS B CA  1 
ATOM   2705 C C   . CYS B 2 146 ? 0.247   14.902  1.555   1.00 43.02  ?  146 CYS B C   1 
ATOM   2706 O O   . CYS B 2 146 ? -0.247  15.298  2.619   1.00 40.10  ?  146 CYS B O   1 
ATOM   2707 C CB  . CYS B 2 146 ? 1.427   16.855  0.560   1.00 46.00  ?  146 CYS B CB  1 
ATOM   2708 S SG  . CYS B 2 146 ? 2.073   17.562  -0.950  1.00 67.23  ?  146 CYS B SG  1 
ATOM   2709 N N   . LEU B 2 147 ? 0.770   13.691  1.396   1.00 44.97  ?  147 LEU B N   1 
ATOM   2710 C CA  . LEU B 2 147 ? 0.915   12.735  2.486   1.00 42.72  ?  147 LEU B CA  1 
ATOM   2711 C C   . LEU B 2 147 ? 2.372   12.739  2.934   1.00 39.35  ?  147 LEU B C   1 
ATOM   2712 O O   . LEU B 2 147 ? 3.269   12.450  2.134   1.00 37.11  ?  147 LEU B O   1 
ATOM   2713 C CB  . LEU B 2 147 ? 0.476   11.340  2.039   1.00 44.41  ?  147 LEU B CB  1 
ATOM   2714 C CG  . LEU B 2 147 ? 0.579   10.178  3.027   1.00 44.25  ?  147 LEU B CG  1 
ATOM   2715 C CD1 . LEU B 2 147 ? -0.412  10.336  4.168   1.00 47.39  ?  147 LEU B CD1 1 
ATOM   2716 C CD2 . LEU B 2 147 ? 0.351   8.878   2.290   1.00 40.47  ?  147 LEU B CD2 1 
ATOM   2717 N N   . VAL B 2 148 ? 2.606   13.117  4.189   1.00 36.92  ?  148 VAL B N   1 
ATOM   2718 C CA  . VAL B 2 148 ? 3.939   13.211  4.770   1.00 38.32  ?  148 VAL B CA  1 
ATOM   2719 C C   . VAL B 2 148 ? 4.069   12.057  5.758   1.00 39.02  ?  148 VAL B C   1 
ATOM   2720 O O   . VAL B 2 148 ? 3.536   12.112  6.869   1.00 40.15  ?  148 VAL B O   1 
ATOM   2721 C CB  . VAL B 2 148 ? 4.164   14.570  5.443   1.00 39.53  ?  148 VAL B CB  1 
ATOM   2722 C CG1 . VAL B 2 148 ? 5.540   14.644  6.062   1.00 41.42  ?  148 VAL B CG1 1 
ATOM   2723 C CG2 . VAL B 2 148 ? 3.974   15.696  4.434   1.00 34.13  ?  148 VAL B CG2 1 
ATOM   2724 N N   . LYS B 2 149 ? 4.798   11.015  5.366   1.00 41.34  ?  149 LYS B N   1 
ATOM   2725 C CA  . LYS B 2 149 ? 4.773   9.721   6.035   1.00 46.65  ?  149 LYS B CA  1 
ATOM   2726 C C   . LYS B 2 149 ? 6.163   9.340   6.528   1.00 44.47  ?  149 LYS B C   1 
ATOM   2727 O O   . LYS B 2 149 ? 7.162   9.616   5.854   1.00 45.60  ?  149 LYS B O   1 
ATOM   2728 C CB  . LYS B 2 149 ? 4.242   8.641   5.073   1.00 47.37  ?  149 LYS B CB  1 
ATOM   2729 C CG  . LYS B 2 149 ? 4.112   7.246   5.657   1.00 53.22  ?  149 LYS B CG  1 
ATOM   2730 C CD  . LYS B 2 149 ? 3.641   6.258   4.593   1.00 59.61  ?  149 LYS B CD  1 
ATOM   2731 C CE  . LYS B 2 149 ? 3.795   4.811   5.048   1.00 54.87  ?  149 LYS B CE  1 
ATOM   2732 N NZ  . LYS B 2 149 ? 2.808   4.457   6.103   1.00 63.98  ?  149 LYS B NZ  1 
ATOM   2733 N N   . ASP B 2 150 ? 6.213   8.714   7.713   1.00 47.75  ?  150 ASP B N   1 
ATOM   2734 C CA  . ASP B 2 150 ? 7.396   8.016   8.219   1.00 46.20  ?  150 ASP B CA  1 
ATOM   2735 C C   . ASP B 2 150 ? 8.548   8.956   8.539   1.00 47.87  ?  150 ASP B C   1 
ATOM   2736 O O   . ASP B 2 150 ? 9.660   8.780   8.023   1.00 48.49  ?  150 ASP B O   1 
ATOM   2737 C CB  . ASP B 2 150 ? 7.868   6.955   7.224   1.00 47.59  ?  150 ASP B CB  1 
ATOM   2738 C CG  . ASP B 2 150 ? 6.919   5.791   7.133   1.00 51.56  ?  150 ASP B CG  1 
ATOM   2739 O OD1 . ASP B 2 150 ? 6.185   5.553   8.114   1.00 58.12  ?  150 ASP B OD1 1 
ATOM   2740 O OD2 . ASP B 2 150 ? 6.910   5.111   6.088   1.00 60.88  ?  150 ASP B OD2 1 
ATOM   2741 N N   . TYR B 2 151 ? 8.296   9.941   9.401   1.00 41.76  ?  151 TYR B N   1 
ATOM   2742 C CA  . TYR B 2 151 ? 9.327   10.844  9.883   1.00 46.06  ?  151 TYR B CA  1 
ATOM   2743 C C   . TYR B 2 151 ? 9.387   10.835  11.406  1.00 43.09  ?  151 TYR B C   1 
ATOM   2744 O O   . TYR B 2 151 ? 8.456   10.394  12.088  1.00 39.17  ?  151 TYR B O   1 
ATOM   2745 C CB  . TYR B 2 151 ? 9.097   12.273  9.378   1.00 43.53  ?  151 TYR B CB  1 
ATOM   2746 C CG  . TYR B 2 151 ? 7.864   12.946  9.933   1.00 44.00  ?  151 TYR B CG  1 
ATOM   2747 C CD1 . TYR B 2 151 ? 6.648   12.872  9.262   1.00 43.95  ?  151 TYR B CD1 1 
ATOM   2748 C CD2 . TYR B 2 151 ? 7.917   13.673  11.112  1.00 44.30  ?  151 TYR B CD2 1 
ATOM   2749 C CE1 . TYR B 2 151 ? 5.521   13.492  9.758   1.00 36.29  ?  151 TYR B CE1 1 
ATOM   2750 C CE2 . TYR B 2 151 ? 6.796   14.291  11.616  1.00 46.58  ?  151 TYR B CE2 1 
ATOM   2751 C CZ  . TYR B 2 151 ? 5.603   14.199  10.936  1.00 43.68  ?  151 TYR B CZ  1 
ATOM   2752 O OH  . TYR B 2 151 ? 4.497   14.831  11.446  1.00 48.68  ?  151 TYR B OH  1 
ATOM   2753 N N   . PHE B 2 152 ? 10.499  11.360  11.930  1.00 43.34  ?  152 PHE B N   1 
ATOM   2754 C CA  . PHE B 2 152 ? 10.730  11.429  13.367  1.00 43.46  ?  152 PHE B CA  1 
ATOM   2755 C C   . PHE B 2 152 ? 11.908  12.355  13.645  1.00 46.18  ?  152 PHE B C   1 
ATOM   2756 O O   . PHE B 2 152 ? 12.917  12.314  12.927  1.00 50.67  ?  152 PHE B O   1 
ATOM   2757 C CB  . PHE B 2 152 ? 10.999  10.040  13.947  1.00 35.72  ?  152 PHE B CB  1 
ATOM   2758 C CG  . PHE B 2 152 ? 11.007  10.010  15.443  1.00 40.39  ?  152 PHE B CG  1 
ATOM   2759 C CD1 . PHE B 2 152 ? 12.185  10.180  16.151  1.00 39.24  ?  152 PHE B CD1 1 
ATOM   2760 C CD2 . PHE B 2 152 ? 9.822   9.827   16.147  1.00 41.36  ?  152 PHE B CD2 1 
ATOM   2761 C CE1 . PHE B 2 152 ? 12.186  10.155  17.535  1.00 39.86  ?  152 PHE B CE1 1 
ATOM   2762 C CE2 . PHE B 2 152 ? 9.813   9.806   17.530  1.00 37.94  ?  152 PHE B CE2 1 
ATOM   2763 C CZ  . PHE B 2 152 ? 10.999  9.971   18.225  1.00 39.52  ?  152 PHE B CZ  1 
ATOM   2764 N N   . PRO B 2 153 ? 11.820  13.217  14.666  1.00 47.98  ?  153 PRO B N   1 
ATOM   2765 C CA  . PRO B 2 153 ? 10.631  13.382  15.501  1.00 45.55  ?  153 PRO B CA  1 
ATOM   2766 C C   . PRO B 2 153 ? 9.748   14.501  14.984  1.00 47.29  ?  153 PRO B C   1 
ATOM   2767 O O   . PRO B 2 153 ? 9.914   14.968  13.856  1.00 45.81  ?  153 PRO B O   1 
ATOM   2768 C CB  . PRO B 2 153 ? 11.223  13.755  16.854  1.00 45.67  ?  153 PRO B CB  1 
ATOM   2769 C CG  . PRO B 2 153 ? 12.402  14.626  16.461  1.00 38.08  ?  153 PRO B CG  1 
ATOM   2770 C CD  . PRO B 2 153 ? 12.936  14.049  15.155  1.00 42.55  ?  153 PRO B CD  1 
ATOM   2771 N N   . GLU B 2 154 ? 8.801   14.918  15.810  1.00 45.65  ?  154 GLU B N   1 
ATOM   2772 C CA  . GLU B 2 154 ? 8.067   16.132  15.532  1.00 48.92  ?  154 GLU B CA  1 
ATOM   2773 C C   . GLU B 2 154 ? 8.989   17.344  15.677  1.00 46.82  ?  154 GLU B C   1 
ATOM   2774 O O   . GLU B 2 154 ? 9.979   17.301  16.411  1.00 44.70  ?  154 GLU B O   1 
ATOM   2775 C CB  . GLU B 2 154 ? 6.879   16.248  16.481  1.00 45.75  ?  154 GLU B CB  1 
ATOM   2776 C CG  . GLU B 2 154 ? 5.780   15.255  16.220  1.00 45.52  ?  154 GLU B CG  1 
ATOM   2777 C CD  . GLU B 2 154 ? 4.691   15.854  15.363  1.00 50.47  ?  154 GLU B CD  1 
ATOM   2778 O OE1 . GLU B 2 154 ? 5.000   16.296  14.231  1.00 45.02  ?  154 GLU B OE1 1 
ATOM   2779 O OE2 . GLU B 2 154 ? 3.535   15.912  15.837  1.00 52.27  -1 154 GLU B OE2 1 
ATOM   2780 N N   . PRO B 2 155 ? 8.673   18.454  15.000  1.00 49.16  ?  155 PRO B N   1 
ATOM   2781 C CA  . PRO B 2 155 ? 7.524   18.673  14.123  1.00 48.08  ?  155 PRO B CA  1 
ATOM   2782 C C   . PRO B 2 155 ? 7.896   18.824  12.655  1.00 48.25  ?  155 PRO B C   1 
ATOM   2783 O O   . PRO B 2 155 ? 9.060   19.068  12.328  1.00 47.74  ?  155 PRO B O   1 
ATOM   2784 C CB  . PRO B 2 155 ? 6.956   19.984  14.654  1.00 45.23  ?  155 PRO B CB  1 
ATOM   2785 C CG  . PRO B 2 155 ? 8.201   20.762  14.990  1.00 41.16  ?  155 PRO B CG  1 
ATOM   2786 C CD  . PRO B 2 155 ? 9.266   19.740  15.404  1.00 50.10  ?  155 PRO B CD  1 
ATOM   2787 N N   . VAL B 2 156 ? 6.904   18.671  11.783  1.00 49.94  ?  156 VAL B N   1 
ATOM   2788 C CA  . VAL B 2 156 ? 7.011   19.092  10.395  1.00 48.07  ?  156 VAL B CA  1 
ATOM   2789 C C   . VAL B 2 156 ? 6.001   20.207  10.198  1.00 49.21  ?  156 VAL B C   1 
ATOM   2790 O O   . VAL B 2 156 ? 4.944   20.227  10.838  1.00 48.72  ?  156 VAL B O   1 
ATOM   2791 C CB  . VAL B 2 156 ? 6.747   17.956  9.385   1.00 42.33  ?  156 VAL B CB  1 
ATOM   2792 C CG1 . VAL B 2 156 ? 7.813   16.897  9.478   1.00 50.67  ?  156 VAL B CG1 1 
ATOM   2793 C CG2 . VAL B 2 156 ? 5.405   17.358  9.622   1.00 51.18  ?  156 VAL B CG2 1 
ATOM   2794 N N   . THR B 2 157 ? 6.334   21.148  9.317   1.00 46.08  ?  157 THR B N   1 
ATOM   2795 C CA  . THR B 2 157 ? 5.422   22.225  8.960   1.00 45.59  ?  157 THR B CA  1 
ATOM   2796 C C   . THR B 2 157 ? 5.127   22.135  7.473   1.00 48.58  ?  157 THR B C   1 
ATOM   2797 O O   . THR B 2 157 ? 6.026   21.879  6.667   1.00 46.61  ?  157 THR B O   1 
ATOM   2798 C CB  . THR B 2 157 ? 5.986   23.609  9.295   1.00 49.56  ?  157 THR B CB  1 
ATOM   2799 O OG1 . THR B 2 157 ? 7.194   23.836  8.554   1.00 58.46  ?  157 THR B OG1 1 
ATOM   2800 C CG2 . THR B 2 157 ? 6.257   23.723  10.783  1.00 45.17  ?  157 THR B CG2 1 
ATOM   2801 N N   . VAL B 2 158 ? 3.865   22.337  7.109   1.00 43.61  ?  158 VAL B N   1 
ATOM   2802 C CA  . VAL B 2 158 ? 3.439   22.261  5.721   1.00 43.90  ?  158 VAL B CA  1 
ATOM   2803 C C   . VAL B 2 158 ? 2.833   23.595  5.326   1.00 46.20  ?  158 VAL B C   1 
ATOM   2804 O O   . VAL B 2 158 ? 1.941   24.108  6.011   1.00 54.89  ?  158 VAL B O   1 
ATOM   2805 C CB  . VAL B 2 158 ? 2.430   21.122  5.491   1.00 43.62  ?  158 VAL B CB  1 
ATOM   2806 C CG1 . VAL B 2 158 ? 2.168   20.934  4.001   1.00 39.92  ?  158 VAL B CG1 1 
ATOM   2807 C CG2 . VAL B 2 158 ? 2.933   19.837  6.108   1.00 42.50  ?  158 VAL B CG2 1 
ATOM   2808 N N   . SER B 2 159 ? 3.312   24.147  4.222   1.00 42.26  ?  159 SER B N   1 
ATOM   2809 C CA  . SER B 2 159 ? 2.703   25.307  3.598   1.00 43.78  ?  159 SER B CA  1 
ATOM   2810 C C   . SER B 2 159 ? 2.382   24.958  2.152   1.00 44.19  ?  159 SER B C   1 
ATOM   2811 O O   . SER B 2 159 ? 2.846   23.954  1.618   1.00 47.24  ?  159 SER B O   1 
ATOM   2812 C CB  . SER B 2 159 ? 3.623   26.533  3.670   1.00 41.45  ?  159 SER B CB  1 
ATOM   2813 O OG  . SER B 2 159 ? 4.709   26.409  2.767   1.00 48.48  ?  159 SER B OG  1 
ATOM   2814 N N   . TRP B 2 160 ? 1.573   25.787  1.508   1.00 47.57  ?  160 TRP B N   1 
ATOM   2815 C CA  . TRP B 2 160 ? 1.225   25.578  0.113   1.00 47.20  ?  160 TRP B CA  1 
ATOM   2816 C C   . TRP B 2 160 ? 1.627   26.813  -0.679  1.00 52.76  ?  160 TRP B C   1 
ATOM   2817 O O   . TRP B 2 160 ? 1.304   27.941  -0.286  1.00 57.07  ?  160 TRP B O   1 
ATOM   2818 C CB  . TRP B 2 160 ? -0.270  25.281  -0.037  1.00 47.06  ?  160 TRP B CB  1 
ATOM   2819 C CG  . TRP B 2 160 ? -0.612  23.897  0.406   1.00 42.45  ?  160 TRP B CG  1 
ATOM   2820 C CD1 . TRP B 2 160 ? -0.892  23.486  1.678   1.00 44.91  ?  160 TRP B CD1 1 
ATOM   2821 C CD2 . TRP B 2 160 ? -0.679  22.729  -0.416  1.00 41.85  ?  160 TRP B CD2 1 
ATOM   2822 N NE1 . TRP B 2 160 ? -1.141  22.134  1.697   1.00 44.85  ?  160 TRP B NE1 1 
ATOM   2823 C CE2 . TRP B 2 160 ? -1.012  21.645  0.423   1.00 43.58  ?  160 TRP B CE2 1 
ATOM   2824 C CE3 . TRP B 2 160 ? -0.492  22.493  -1.779  1.00 43.65  ?  160 TRP B CE3 1 
ATOM   2825 C CZ2 . TRP B 2 160 ? -1.163  20.349  -0.060  1.00 40.70  ?  160 TRP B CZ2 1 
ATOM   2826 C CZ3 . TRP B 2 160 ? -0.638  21.204  -2.254  1.00 45.56  ?  160 TRP B CZ3 1 
ATOM   2827 C CH2 . TRP B 2 160 ? -0.970  20.149  -1.397  1.00 43.62  ?  160 TRP B CH2 1 
ATOM   2828 N N   . ASN B 2 161 ? 2.329   26.591  -1.791  1.00 49.86  ?  161 ASN B N   1 
ATOM   2829 C CA  . ASN B 2 161 ? 2.848   27.669  -2.630  1.00 51.32  ?  161 ASN B CA  1 
ATOM   2830 C C   . ASN B 2 161 ? 3.530   28.744  -1.788  1.00 57.66  ?  161 ASN B C   1 
ATOM   2831 O O   . ASN B 2 161 ? 3.210   29.932  -1.868  1.00 55.46  ?  161 ASN B O   1 
ATOM   2832 C CB  . ASN B 2 161 ? 1.737   28.256  -3.494  1.00 55.34  ?  161 ASN B CB  1 
ATOM   2833 C CG  . ASN B 2 161 ? 1.178   27.245  -4.464  1.00 58.79  ?  161 ASN B CG  1 
ATOM   2834 O OD1 . ASN B 2 161 ? 1.499   26.061  -4.386  1.00 64.10  ?  161 ASN B OD1 1 
ATOM   2835 N ND2 . ASN B 2 161 ? 0.320   27.694  -5.368  1.00 65.90  ?  161 ASN B ND2 1 
ATOM   2836 N N   . SER B 2 162 ? 4.459   28.299  -0.942  1.00 57.69  ?  162 SER B N   1 
ATOM   2837 C CA  . SER B 2 162 ? 5.300   29.165  -0.118  1.00 58.70  ?  162 SER B CA  1 
ATOM   2838 C C   . SER B 2 162 ? 4.491   30.073  0.806   1.00 58.72  ?  162 SER B C   1 
ATOM   2839 O O   . SER B 2 162 ? 4.982   31.124  1.236   1.00 62.70  ?  162 SER B O   1 
ATOM   2840 C CB  . SER B 2 162 ? 6.240   29.995  -0.999  1.00 54.98  ?  162 SER B CB  1 
ATOM   2841 O OG  . SER B 2 162 ? 6.902   29.155  -1.932  1.00 64.75  ?  162 SER B OG  1 
ATOM   2842 N N   . GLY B 2 163 ? 3.271   29.670  1.155   1.00 57.28  ?  163 GLY B N   1 
ATOM   2843 C CA  . GLY B 2 163 ? 2.420   30.452  2.021   1.00 57.84  ?  163 GLY B CA  1 
ATOM   2844 C C   . GLY B 2 163 ? 1.384   31.278  1.297   1.00 61.43  ?  163 GLY B C   1 
ATOM   2845 O O   . GLY B 2 163 ? 0.532   31.889  1.956   1.00 59.86  ?  163 GLY B O   1 
ATOM   2846 N N   . ALA B 2 164 ? 1.426   31.306  -0.039  1.00 58.56  ?  164 ALA B N   1 
ATOM   2847 C CA  . ALA B 2 164 ? 0.468   32.102  -0.797  1.00 56.10  ?  164 ALA B CA  1 
ATOM   2848 C C   . ALA B 2 164 ? -0.931  31.514  -0.701  1.00 62.19  ?  164 ALA B C   1 
ATOM   2849 O O   . ALA B 2 164 ? -1.918  32.257  -0.668  1.00 70.47  ?  164 ALA B O   1 
ATOM   2850 C CB  . ALA B 2 164 ? 0.904   32.203  -2.258  1.00 60.31  ?  164 ALA B CB  1 
ATOM   2851 N N   . LEU B 2 165 ? -1.033  30.186  -0.653  1.00 61.83  ?  165 LEU B N   1 
ATOM   2852 C CA  . LEU B 2 165 ? -2.311  29.488  -0.593  1.00 54.58  ?  165 LEU B CA  1 
ATOM   2853 C C   . LEU B 2 165 ? -2.586  29.103  0.855   1.00 55.84  ?  165 LEU B C   1 
ATOM   2854 O O   . LEU B 2 165 ? -1.874  28.272  1.428   1.00 55.87  ?  165 LEU B O   1 
ATOM   2855 C CB  . LEU B 2 165 ? -2.292  28.259  -1.495  1.00 52.71  ?  165 LEU B CB  1 
ATOM   2856 C CG  . LEU B 2 165 ? -3.563  27.419  -1.499  1.00 60.51  ?  165 LEU B CG  1 
ATOM   2857 C CD1 . LEU B 2 165 ? -4.768  28.291  -1.782  1.00 57.26  ?  165 LEU B CD1 1 
ATOM   2858 C CD2 . LEU B 2 165 ? -3.445  26.307  -2.529  1.00 63.12  ?  165 LEU B CD2 1 
ATOM   2859 N N   . THR B 2 166 ? -3.620  29.709  1.445   1.00 57.73  ?  166 THR B N   1 
ATOM   2860 C CA  . THR B 2 166 ? -3.984  29.481  2.841   1.00 58.33  ?  166 THR B CA  1 
ATOM   2861 C C   . THR B 2 166 ? -5.450  29.117  3.030   1.00 56.64  ?  166 THR B C   1 
ATOM   2862 O O   . THR B 2 166 ? -5.769  28.328  3.923   1.00 56.60  ?  166 THR B O   1 
ATOM   2863 C CB  . THR B 2 166 ? -3.658  30.728  3.683   1.00 62.50  ?  166 THR B CB  1 
ATOM   2864 O OG1 . THR B 2 166 ? -4.339  31.866  3.140   1.00 67.46  ?  166 THR B OG1 1 
ATOM   2865 C CG2 . THR B 2 166 ? -2.161  30.998  3.677   1.00 59.28  ?  166 THR B CG2 1 
ATOM   2866 N N   . SER B 2 167 ? -6.350  29.685  2.234   1.00 60.75  ?  167 SER B N   1 
ATOM   2867 C CA  . SER B 2 167 ? -7.773  29.429  2.415   1.00 65.60  ?  167 SER B CA  1 
ATOM   2868 C C   . SER B 2 167 ? -8.125  28.036  1.917   1.00 60.57  ?  167 SER B C   1 
ATOM   2869 O O   . SER B 2 167 ? -7.741  27.647  0.809   1.00 61.57  ?  167 SER B O   1 
ATOM   2870 C CB  . SER B 2 167 ? -8.607  30.480  1.683   1.00 63.60  ?  167 SER B CB  1 
ATOM   2871 O OG  . SER B 2 167 ? -8.393  30.405  0.285   1.00 72.77  ?  167 SER B OG  1 
ATOM   2872 N N   . GLY B 2 168 ? -8.857  27.284  2.735   1.00 56.79  ?  168 GLY B N   1 
ATOM   2873 C CA  . GLY B 2 168 ? -9.235  25.937  2.368   1.00 58.03  ?  168 GLY B CA  1 
ATOM   2874 C C   . GLY B 2 168 ? -8.178  24.891  2.626   1.00 55.88  ?  168 GLY B C   1 
ATOM   2875 O O   . GLY B 2 168 ? -8.357  23.735  2.229   1.00 58.89  ?  168 GLY B O   1 
ATOM   2876 N N   . VAL B 2 169 ? -7.087  25.257  3.275   1.00 49.73  ?  169 VAL B N   1 
ATOM   2877 C CA  . VAL B 2 169 ? -6.013  24.325  3.577   1.00 54.34  ?  169 VAL B CA  1 
ATOM   2878 C C   . VAL B 2 169 ? -6.239  23.752  4.969   1.00 57.14  ?  169 VAL B C   1 
ATOM   2879 O O   . VAL B 2 169 ? -6.468  24.495  5.931   1.00 54.29  ?  169 VAL B O   1 
ATOM   2880 C CB  . VAL B 2 169 ? -4.642  25.013  3.473   1.00 50.64  ?  169 VAL B CB  1 
ATOM   2881 C CG1 . VAL B 2 169 ? -3.537  24.043  3.878   1.00 52.09  ?  169 VAL B CG1 1 
ATOM   2882 C CG2 . VAL B 2 169 ? -4.419  25.526  2.058   1.00 47.55  ?  169 VAL B CG2 1 
ATOM   2883 N N   . HIS B 2 170 ? -6.206  22.428  5.071   1.00 50.92  ?  170 HIS B N   1 
ATOM   2884 C CA  . HIS B 2 170 ? -6.274  21.726  6.344   1.00 44.29  ?  170 HIS B CA  1 
ATOM   2885 C C   . HIS B 2 170 ? -5.022  20.868  6.474   1.00 45.83  ?  170 HIS B C   1 
ATOM   2886 O O   . HIS B 2 170 ? -4.809  19.959  5.667   1.00 46.22  ?  170 HIS B O   1 
ATOM   2887 C CB  . HIS B 2 170 ? -7.540  20.865  6.428   1.00 41.98  ?  170 HIS B CB  1 
ATOM   2888 C CG  . HIS B 2 170 ? -8.818  21.648  6.351   1.00 57.56  ?  170 HIS B CG  1 
ATOM   2889 N ND1 . HIS B 2 170 ? -9.444  21.941  5.158   1.00 61.94  ?  170 HIS B ND1 1 
ATOM   2890 C CD2 . HIS B 2 170 ? -9.587  22.198  7.322   1.00 61.48  ?  170 HIS B CD2 1 
ATOM   2891 C CE1 . HIS B 2 170 ? -10.542 22.638  5.396   1.00 63.93  ?  170 HIS B CE1 1 
ATOM   2892 N NE2 . HIS B 2 170 ? -10.653 22.806  6.702   1.00 62.34  ?  170 HIS B NE2 1 
ATOM   2893 N N   . THR B 2 171 ? -4.179  21.170  7.460   1.00 43.77  ?  171 THR B N   1 
ATOM   2894 C CA  . THR B 2 171 ? -3.036  20.320  7.793   1.00 44.51  ?  171 THR B CA  1 
ATOM   2895 C C   . THR B 2 171 ? -3.377  19.600  9.090   1.00 44.71  ?  171 THR B C   1 
ATOM   2896 O O   . THR B 2 171 ? -3.465  20.229  10.150  1.00 47.46  ?  171 THR B O   1 
ATOM   2897 C CB  . THR B 2 171 ? -1.740  21.118  7.929   1.00 41.89  ?  171 THR B CB  1 
ATOM   2898 O OG1 . THR B 2 171 ? -1.445  21.780  6.695   1.00 52.09  ?  171 THR B OG1 1 
ATOM   2899 C CG2 . THR B 2 171 ? -0.594  20.197  8.267   1.00 33.71  ?  171 THR B CG2 1 
ATOM   2900 N N   . PHE B 2 172 ? -3.584  18.289  9.002   1.00 40.03  ?  172 PHE B N   1 
ATOM   2901 C CA  . PHE B 2 172 ? -4.067  17.528  10.140  1.00 42.03  ?  172 PHE B CA  1 
ATOM   2902 C C   . PHE B 2 172 ? -2.942  17.266  11.134  1.00 42.38  ?  172 PHE B C   1 
ATOM   2903 O O   . PHE B 2 172 ? -1.786  17.095  10.741  1.00 44.34  ?  172 PHE B O   1 
ATOM   2904 C CB  . PHE B 2 172 ? -4.657  16.209  9.669   1.00 41.10  ?  172 PHE B CB  1 
ATOM   2905 C CG  . PHE B 2 172 ? -5.848  16.376  8.791   1.00 44.54  ?  172 PHE B CG  1 
ATOM   2906 C CD1 . PHE B 2 172 ? -5.696  16.555  7.428   1.00 40.10  ?  172 PHE B CD1 1 
ATOM   2907 C CD2 . PHE B 2 172 ? -7.125  16.357  9.329   1.00 45.84  ?  172 PHE B CD2 1 
ATOM   2908 C CE1 . PHE B 2 172 ? -6.796  16.716  6.616   1.00 44.20  ?  172 PHE B CE1 1 
ATOM   2909 C CE2 . PHE B 2 172 ? -8.228  16.515  8.525   1.00 42.44  ?  172 PHE B CE2 1 
ATOM   2910 C CZ  . PHE B 2 172 ? -8.067  16.695  7.166   1.00 44.49  ?  172 PHE B CZ  1 
ATOM   2911 N N   . PRO B 2 173 ? -3.258  17.214  12.427  1.00 43.13  ?  173 PRO B N   1 
ATOM   2912 C CA  . PRO B 2 173 ? -2.229  16.866  13.412  1.00 38.05  ?  173 PRO B CA  1 
ATOM   2913 C C   . PRO B 2 173 ? -1.646  15.492  13.112  1.00 43.83  ?  173 PRO B C   1 
ATOM   2914 O O   . PRO B 2 173 ? -2.362  14.559  12.737  1.00 47.90  ?  173 PRO B O   1 
ATOM   2915 C CB  . PRO B 2 173 ? -2.990  16.879  14.745  1.00 43.51  ?  173 PRO B CB  1 
ATOM   2916 C CG  . PRO B 2 173 ? -4.214  17.700  14.492  1.00 43.30  ?  173 PRO B CG  1 
ATOM   2917 C CD  . PRO B 2 173 ? -4.567  17.470  13.053  1.00 43.96  ?  173 PRO B CD  1 
ATOM   2918 N N   . ALA B 2 174 ? -0.334  15.370  13.283  1.00 44.62  ?  174 ALA B N   1 
ATOM   2919 C CA  . ALA B 2 174 ? 0.320   14.098  13.021  1.00 43.68  ?  174 ALA B CA  1 
ATOM   2920 C C   . ALA B 2 174 ? -0.143  13.048  14.020  1.00 40.10  ?  174 ALA B C   1 
ATOM   2921 O O   . ALA B 2 174 ? -0.460  13.347  15.173  1.00 43.06  ?  174 ALA B O   1 
ATOM   2922 C CB  . ALA B 2 174 ? 1.838   14.243  13.091  1.00 41.46  ?  174 ALA B CB  1 
ATOM   2923 N N   . VAL B 2 175 ? -0.178  11.804  13.565  1.00 39.96  ?  175 VAL B N   1 
ATOM   2924 C CA  . VAL B 2 175 ? -0.501  10.673  14.418  1.00 45.38  ?  175 VAL B CA  1 
ATOM   2925 C C   . VAL B 2 175 ? 0.704   9.746   14.446  1.00 48.63  ?  175 VAL B C   1 
ATOM   2926 O O   . VAL B 2 175 ? 1.363   9.532   13.422  1.00 52.35  ?  175 VAL B O   1 
ATOM   2927 C CB  . VAL B 2 175 ? -1.766  9.931   13.936  1.00 48.66  ?  175 VAL B CB  1 
ATOM   2928 C CG1 . VAL B 2 175 ? -1.636  9.517   12.475  1.00 52.09  ?  175 VAL B CG1 1 
ATOM   2929 C CG2 . VAL B 2 175 ? -2.034  8.722   14.818  1.00 55.92  ?  175 VAL B CG2 1 
ATOM   2930 N N   . LEU B 2 176 ? 1.002   9.212   15.625  1.00 46.46  ?  176 LEU B N   1 
ATOM   2931 C CA  . LEU B 2 176 ? 2.098   8.267   15.773  1.00 45.13  ?  176 LEU B CA  1 
ATOM   2932 C C   . LEU B 2 176 ? 1.654   6.903   15.264  1.00 45.25  ?  176 LEU B C   1 
ATOM   2933 O O   . LEU B 2 176 ? 0.678   6.338   15.767  1.00 44.93  ?  176 LEU B O   1 
ATOM   2934 C CB  . LEU B 2 176 ? 2.530   8.189   17.233  1.00 46.10  ?  176 LEU B CB  1 
ATOM   2935 C CG  . LEU B 2 176 ? 3.813   7.417   17.516  1.00 48.47  ?  176 LEU B CG  1 
ATOM   2936 C CD1 . LEU B 2 176 ? 4.996   8.040   16.770  1.00 45.75  ?  176 LEU B CD1 1 
ATOM   2937 C CD2 . LEU B 2 176 ? 4.048   7.411   19.009  1.00 45.87  ?  176 LEU B CD2 1 
ATOM   2938 N N   . GLN B 2 177 ? 2.364   6.373   14.275  1.00 47.57  ?  177 GLN B N   1 
ATOM   2939 C CA  . GLN B 2 177 ? 2.021   5.074   13.723  1.00 48.19  ?  177 GLN B CA  1 
ATOM   2940 C C   . GLN B 2 177 ? 2.569   3.953   14.608  1.00 50.36  ?  177 GLN B C   1 
ATOM   2941 O O   . GLN B 2 177 ? 3.412   4.168   15.483  1.00 51.81  ?  177 GLN B O   1 
ATOM   2942 C CB  . GLN B 2 177 ? 2.570   4.937   12.303  1.00 48.82  ?  177 GLN B CB  1 
ATOM   2943 C CG  . GLN B 2 177 ? 2.004   5.923   11.297  1.00 48.25  ?  177 GLN B CG  1 
ATOM   2944 C CD  . GLN B 2 177 ? 2.753   5.885   9.974   1.00 53.23  ?  177 GLN B CD  1 
ATOM   2945 O OE1 . GLN B 2 177 ? 2.153   5.795   8.902   1.00 57.41  ?  177 GLN B OE1 1 
ATOM   2946 N NE2 . GLN B 2 177 ? 4.076   5.969   10.047  1.00 49.08  ?  177 GLN B NE2 1 
ATOM   2947 N N   . SER B 2 178 ? 2.076   2.735   14.364  1.00 51.53  ?  178 SER B N   1 
ATOM   2948 C CA  . SER B 2 178 ? 2.529   1.583   15.138  1.00 54.30  ?  178 SER B CA  1 
ATOM   2949 C C   . SER B 2 178 ? 4.017   1.330   14.943  1.00 57.92  ?  178 SER B C   1 
ATOM   2950 O O   . SER B 2 178 ? 4.667   0.746   15.818  1.00 58.97  ?  178 SER B O   1 
ATOM   2951 C CB  . SER B 2 178 ? 1.719   0.337   14.772  1.00 54.05  ?  178 SER B CB  1 
ATOM   2952 O OG  . SER B 2 178 ? 1.945   -0.049  13.431  1.00 64.77  ?  178 SER B OG  1 
ATOM   2953 N N   . SER B 2 179 ? 4.571   1.744   13.801  1.00 52.95  ?  179 SER B N   1 
ATOM   2954 C CA  . SER B 2 179 ? 6.000   1.596   13.556  1.00 46.75  ?  179 SER B CA  1 
ATOM   2955 C C   . SER B 2 179 ? 6.849   2.498   14.442  1.00 51.28  ?  179 SER B C   1 
ATOM   2956 O O   . SER B 2 179 ? 8.075   2.340   14.458  1.00 50.44  ?  179 SER B O   1 
ATOM   2957 C CB  . SER B 2 179 ? 6.303   1.886   12.086  1.00 50.18  ?  179 SER B CB  1 
ATOM   2958 O OG  . SER B 2 179 ? 5.948   3.216   11.744  1.00 54.63  ?  179 SER B OG  1 
ATOM   2959 N N   . GLY B 2 180 ? 6.235   3.414   15.187  1.00 51.31  ?  180 GLY B N   1 
ATOM   2960 C CA  . GLY B 2 180 ? 6.963   4.417   15.937  1.00 50.35  ?  180 GLY B CA  1 
ATOM   2961 C C   . GLY B 2 180 ? 7.308   5.679   15.176  1.00 50.09  ?  180 GLY B C   1 
ATOM   2962 O O   . GLY B 2 180 ? 8.045   6.518   15.707  1.00 47.87  ?  180 GLY B O   1 
ATOM   2963 N N   . LEU B 2 181 ? 6.800   5.845   13.958  1.00 47.22  ?  181 LEU B N   1 
ATOM   2964 C CA  . LEU B 2 181 ? 7.054   7.021   13.141  1.00 44.86  ?  181 LEU B CA  1 
ATOM   2965 C C   . LEU B 2 181 ? 5.785   7.857   13.024  1.00 46.34  ?  181 LEU B C   1 
ATOM   2966 O O   . LEU B 2 181 ? 4.671   7.367   13.227  1.00 46.21  ?  181 LEU B O   1 
ATOM   2967 C CB  . LEU B 2 181 ? 7.551   6.620   11.748  1.00 43.32  ?  181 LEU B CB  1 
ATOM   2968 C CG  . LEU B 2 181 ? 8.856   5.829   11.770  1.00 44.26  ?  181 LEU B CG  1 
ATOM   2969 C CD1 . LEU B 2 181 ? 9.285   5.467   10.362  1.00 43.22  ?  181 LEU B CD1 1 
ATOM   2970 C CD2 . LEU B 2 181 ? 9.943   6.607   12.497  1.00 36.24  ?  181 LEU B CD2 1 
ATOM   2971 N N   . TYR B 2 182 ? 5.962   9.134   12.696  1.00 41.71  ?  182 TYR B N   1 
ATOM   2972 C CA  . TYR B 2 182 ? 4.828   10.036  12.564  1.00 39.23  ?  182 TYR B CA  1 
ATOM   2973 C C   . TYR B 2 182 ? 4.375   10.132  11.114  1.00 39.74  ?  182 TYR B C   1 
ATOM   2974 O O   . TYR B 2 182 ? 5.156   9.943   10.176  1.00 39.50  ?  182 TYR B O   1 
ATOM   2975 C CB  . TYR B 2 182 ? 5.163   11.429  13.088  1.00 38.43  ?  182 TYR B CB  1 
ATOM   2976 C CG  . TYR B 2 182 ? 5.233   11.512  14.591  1.00 42.15  ?  182 TYR B CG  1 
ATOM   2977 C CD1 . TYR B 2 182 ? 6.458   11.588  15.239  1.00 46.35  ?  182 TYR B CD1 1 
ATOM   2978 C CD2 . TYR B 2 182 ? 4.078   11.524  15.364  1.00 41.62  ?  182 TYR B CD2 1 
ATOM   2979 C CE1 . TYR B 2 182 ? 6.535   11.670  16.615  1.00 46.91  ?  182 TYR B CE1 1 
ATOM   2980 C CE2 . TYR B 2 182 ? 4.143   11.600  16.743  1.00 38.91  ?  182 TYR B CE2 1 
ATOM   2981 C CZ  . TYR B 2 182 ? 5.377   11.674  17.361  1.00 47.12  ?  182 TYR B CZ  1 
ATOM   2982 O OH  . TYR B 2 182 ? 5.467   11.753  18.729  1.00 50.75  ?  182 TYR B OH  1 
ATOM   2983 N N   . SER B 2 183 ? 3.099   10.460  10.944  1.00 40.23  ?  183 SER B N   1 
ATOM   2984 C CA  . SER B 2 183 ? 2.501   10.621  9.629   1.00 40.37  ?  183 SER B CA  1 
ATOM   2985 C C   . SER B 2 183 ? 1.417   11.684  9.708   1.00 41.44  ?  183 SER B C   1 
ATOM   2986 O O   . SER B 2 183 ? 0.690   11.765  10.701  1.00 47.39  ?  183 SER B O   1 
ATOM   2987 C CB  . SER B 2 183 ? 1.909   9.301   9.124   1.00 44.80  ?  183 SER B CB  1 
ATOM   2988 O OG  . SER B 2 183 ? 1.568   9.381   7.752   1.00 53.74  ?  183 SER B OG  1 
ATOM   2989 N N   . LEU B 2 184 ? 1.317   12.499  8.664   1.00 38.61  ?  184 LEU B N   1 
ATOM   2990 C CA  . LEU B 2 184 ? 0.266   13.498  8.597   1.00 42.78  ?  184 LEU B CA  1 
ATOM   2991 C C   . LEU B 2 184 ? -0.133  13.703  7.145   1.00 41.65  ?  184 LEU B C   1 
ATOM   2992 O O   . LEU B 2 184 ? 0.539   13.249  6.214   1.00 39.80  ?  184 LEU B O   1 
ATOM   2993 C CB  . LEU B 2 184 ? 0.686   14.829  9.249   1.00 44.19  ?  184 LEU B CB  1 
ATOM   2994 C CG  . LEU B 2 184 ? 1.766   15.793  8.731   1.00 45.53  ?  184 LEU B CG  1 
ATOM   2995 C CD1 . LEU B 2 184 ? 1.401   16.503  7.420   1.00 39.93  ?  184 LEU B CD1 1 
ATOM   2996 C CD2 . LEU B 2 184 ? 2.019   16.824  9.807   1.00 41.45  ?  184 LEU B CD2 1 
ATOM   2997 N N   . SER B 2 185 ? -1.244  14.407  6.968   1.00 41.79  ?  185 SER B N   1 
ATOM   2998 C CA  . SER B 2 185 ? -1.735  14.779  5.656   1.00 42.80  ?  185 SER B CA  1 
ATOM   2999 C C   . SER B 2 185 ? -2.058  16.261  5.661   1.00 41.76  ?  185 SER B C   1 
ATOM   3000 O O   . SER B 2 185 ? -2.465  16.822  6.682   1.00 41.02  ?  185 SER B O   1 
ATOM   3001 C CB  . SER B 2 185 ? -2.977  13.983  5.263   1.00 44.98  ?  185 SER B CB  1 
ATOM   3002 O OG  . SER B 2 185 ? -2.648  12.620  5.049   1.00 62.59  ?  185 SER B OG  1 
ATOM   3003 N N   . SER B 2 186 ? -1.838  16.893  4.516   1.00 41.20  ?  186 SER B N   1 
ATOM   3004 C CA  . SER B 2 186 ? -2.236  18.274  4.297   1.00 41.45  ?  186 SER B CA  1 
ATOM   3005 C C   . SER B 2 186 ? -3.061  18.300  3.023   1.00 41.70  ?  186 SER B C   1 
ATOM   3006 O O   . SER B 2 186 ? -2.644  17.746  2.005   1.00 41.42  ?  186 SER B O   1 
ATOM   3007 C CB  . SER B 2 186 ? -1.017  19.196  4.187   1.00 39.28  ?  186 SER B CB  1 
ATOM   3008 O OG  . SER B 2 186 ? -1.399  20.556  4.083   1.00 46.37  ?  186 SER B OG  1 
ATOM   3009 N N   . VAL B 2 187 ? -4.235  18.917  3.080   1.00 39.34  ?  187 VAL B N   1 
ATOM   3010 C CA  . VAL B 2 187 ? -5.150  18.925  1.950   1.00 44.04  ?  187 VAL B CA  1 
ATOM   3011 C C   . VAL B 2 187 ? -5.594  20.353  1.684   1.00 48.06  ?  187 VAL B C   1 
ATOM   3012 O O   . VAL B 2 187 ? -5.570  21.218  2.562   1.00 49.80  ?  187 VAL B O   1 
ATOM   3013 C CB  . VAL B 2 187 ? -6.384  18.028  2.188   1.00 43.31  ?  187 VAL B CB  1 
ATOM   3014 C CG1 . VAL B 2 187 ? -5.984  16.565  2.204   1.00 44.19  ?  187 VAL B CG1 1 
ATOM   3015 C CG2 . VAL B 2 187 ? -7.072  18.419  3.481   1.00 38.84  ?  187 VAL B CG2 1 
ATOM   3016 N N   . VAL B 2 188 ? -6.015  20.587  0.452   1.00 43.72  ?  188 VAL B N   1 
ATOM   3017 C CA  . VAL B 2 188 ? -6.601  21.855  0.060   1.00 49.81  ?  188 VAL B CA  1 
ATOM   3018 C C   . VAL B 2 188 ? -7.697  21.559  -0.952  1.00 53.34  ?  188 VAL B C   1 
ATOM   3019 O O   . VAL B 2 188 ? -7.557  20.673  -1.808  1.00 49.47  ?  188 VAL B O   1 
ATOM   3020 C CB  . VAL B 2 188 ? -5.539  22.831  -0.495  1.00 48.73  ?  188 VAL B CB  1 
ATOM   3021 C CG1 . VAL B 2 188 ? -4.764  22.202  -1.637  1.00 47.80  ?  188 VAL B CG1 1 
ATOM   3022 C CG2 . VAL B 2 188 ? -6.176  24.139  -0.921  1.00 52.36  ?  188 VAL B CG2 1 
ATOM   3023 N N   . THR B 2 189 ? -8.809  22.274  -0.812  1.00 57.49  ?  189 THR B N   1 
ATOM   3024 C CA  . THR B 2 189 ? -9.936  22.197  -1.730  1.00 60.85  ?  189 THR B CA  1 
ATOM   3025 C C   . THR B 2 189 ? -9.869  23.377  -2.688  1.00 58.23  ?  189 THR B C   1 
ATOM   3026 O O   . THR B 2 189 ? -9.688  24.522  -2.261  1.00 61.25  ?  189 THR B O   1 
ATOM   3027 C CB  . THR B 2 189 ? -11.266 22.190  -0.969  1.00 57.83  ?  189 THR B CB  1 
ATOM   3028 O OG1 . THR B 2 189 ? -11.188 23.082  0.152   1.00 59.81  ?  189 THR B OG1 1 
ATOM   3029 C CG2 . THR B 2 189 ? -11.583 20.793  -0.468  1.00 50.94  ?  189 THR B CG2 1 
ATOM   3030 N N   . VAL B 2 190 ? -9.983  23.088  -3.979  1.00 59.13  ?  190 VAL B N   1 
ATOM   3031 C CA  . VAL B 2 190 ? -9.825  24.098  -5.022  1.00 65.33  ?  190 VAL B CA  1 
ATOM   3032 C C   . VAL B 2 190 ? -10.986 23.977  -5.999  1.00 67.38  ?  190 VAL B C   1 
ATOM   3033 O O   . VAL B 2 190 ? -11.700 22.963  -6.019  1.00 64.27  ?  190 VAL B O   1 
ATOM   3034 C CB  . VAL B 2 190 ? -8.467  23.953  -5.747  1.00 63.77  ?  190 VAL B CB  1 
ATOM   3035 C CG1 . VAL B 2 190 ? -7.332  24.087  -4.755  1.00 59.74  ?  190 VAL B CG1 1 
ATOM   3036 C CG2 . VAL B 2 190 ? -8.391  22.611  -6.455  1.00 65.86  ?  190 VAL B CG2 1 
ATOM   3037 N N   . PRO B 2 191 ? -11.232 25.015  -6.798  1.00 69.49  ?  191 PRO B N   1 
ATOM   3038 C CA  . PRO B 2 191 ? -12.179 24.864  -7.909  1.00 67.24  ?  191 PRO B CA  1 
ATOM   3039 C C   . PRO B 2 191 ? -11.675 23.823  -8.897  1.00 68.67  ?  191 PRO B C   1 
ATOM   3040 O O   . PRO B 2 191 ? -10.485 23.762  -9.209  1.00 68.71  ?  191 PRO B O   1 
ATOM   3041 C CB  . PRO B 2 191 ? -12.225 26.262  -8.534  1.00 65.98  ?  191 PRO B CB  1 
ATOM   3042 C CG  . PRO B 2 191 ? -11.790 27.179  -7.445  1.00 64.65  ?  191 PRO B CG  1 
ATOM   3043 C CD  . PRO B 2 191 ? -10.790 26.411  -6.638  1.00 69.07  ?  191 PRO B CD  1 
ATOM   3044 N N   . SER B 2 192 ? -12.594 22.983  -9.378  1.00 72.02  ?  192 SER B N   1 
ATOM   3045 C CA  . SER B 2 192 ? -12.202 21.956  -10.337 1.00 70.43  ?  192 SER B CA  1 
ATOM   3046 C C   . SER B 2 192 ? -11.609 22.569  -11.599 1.00 73.24  ?  192 SER B C   1 
ATOM   3047 O O   . SER B 2 192 ? -10.736 21.966  -12.232 1.00 74.17  ?  192 SER B O   1 
ATOM   3048 C CB  . SER B 2 192 ? -13.403 21.076  -10.681 1.00 70.99  ?  192 SER B CB  1 
ATOM   3049 O OG  . SER B 2 192 ? -13.028 20.018  -11.543 1.00 84.24  ?  192 SER B OG  1 
ATOM   3050 N N   . SER B 2 193 ? -12.058 23.768  -11.972 1.00 80.63  ?  193 SER B N   1 
ATOM   3051 C CA  . SER B 2 193 ? -11.534 24.461  -13.143 1.00 80.73  ?  193 SER B CA  1 
ATOM   3052 C C   . SER B 2 193 ? -10.131 25.021  -12.930 1.00 81.89  ?  193 SER B C   1 
ATOM   3053 O O   . SER B 2 193 ? -9.496  25.439  -13.905 1.00 83.40  ?  193 SER B O   1 
ATOM   3054 C CB  . SER B 2 193 ? -12.489 25.589  -13.542 1.00 77.83  ?  193 SER B CB  1 
ATOM   3055 O OG  . SER B 2 193 ? -12.637 26.526  -12.488 1.00 76.00  ?  193 SER B OG  1 
ATOM   3056 N N   . SER B 2 194 ? -9.627  25.031  -11.693 1.00 82.34  ?  194 SER B N   1 
ATOM   3057 C CA  . SER B 2 194 ? -8.298  25.565  -11.421 1.00 74.91  ?  194 SER B CA  1 
ATOM   3058 C C   . SER B 2 194 ? -7.185  24.618  -11.839 1.00 78.75  ?  194 SER B C   1 
ATOM   3059 O O   . SER B 2 194 ? -6.047  25.066  -12.019 1.00 79.99  ?  194 SER B O   1 
ATOM   3060 C CB  . SER B 2 194 ? -8.144  25.895  -9.935  1.00 72.81  ?  194 SER B CB  1 
ATOM   3061 O OG  . SER B 2 194 ? -9.014  26.943  -9.545  1.00 75.36  ?  194 SER B OG  1 
ATOM   3062 N N   . LEU B 2 195 ? -7.474  23.328  -11.977 1.00 75.49  ?  195 LEU B N   1 
ATOM   3063 C CA  . LEU B 2 195 ? -6.451  22.396  -12.424 1.00 76.52  ?  195 LEU B CA  1 
ATOM   3064 C C   . LEU B 2 195 ? -5.978  22.789  -13.820 1.00 84.46  ?  195 LEU B C   1 
ATOM   3065 O O   . LEU B 2 195 ? -6.747  23.294  -14.642 1.00 88.66  ?  195 LEU B O   1 
ATOM   3066 C CB  . LEU B 2 195 ? -6.991  20.964  -12.410 1.00 73.94  ?  195 LEU B CB  1 
ATOM   3067 C CG  . LEU B 2 195 ? -7.819  20.597  -11.170 1.00 72.79  ?  195 LEU B CG  1 
ATOM   3068 C CD1 . LEU B 2 195 ? -8.283  19.144  -11.203 1.00 68.12  ?  195 LEU B CD1 1 
ATOM   3069 C CD2 . LEU B 2 195 ? -7.055  20.894  -9.884  1.00 67.70  ?  195 LEU B CD2 1 
ATOM   3070 N N   . GLY B 2 196 ? -4.690  22.578  -14.075 1.00 90.13  ?  196 GLY B N   1 
ATOM   3071 C CA  . GLY B 2 196 ? -4.096  23.025  -15.321 1.00 89.69  ?  196 GLY B CA  1 
ATOM   3072 C C   . GLY B 2 196 ? -3.689  24.483  -15.280 1.00 83.51  ?  196 GLY B C   1 
ATOM   3073 O O   . GLY B 2 196 ? -2.522  24.817  -15.508 1.00 83.78  ?  196 GLY B O   1 
ATOM   3074 N N   . THR B 2 197 ? -4.643  25.358  -14.965 1.00 76.91  ?  197 THR B N   1 
ATOM   3075 C CA  . THR B 2 197 ? -4.420  26.798  -14.904 1.00 86.76  ?  197 THR B CA  1 
ATOM   3076 C C   . THR B 2 197 ? -3.778  27.230  -13.588 1.00 86.51  ?  197 THR B C   1 
ATOM   3077 O O   . THR B 2 197 ? -3.519  28.424  -13.388 1.00 81.68  ?  197 THR B O   1 
ATOM   3078 C CB  . THR B 2 197 ? -5.757  27.526  -15.122 1.00 88.68  ?  197 THR B CB  1 
ATOM   3079 O OG1 . THR B 2 197 ? -6.422  26.959  -16.258 1.00 100.87 ?  197 THR B OG1 1 
ATOM   3080 C CG2 . THR B 2 197 ? -5.567  29.026  -15.367 1.00 80.98  ?  197 THR B CG2 1 
ATOM   3081 N N   . GLN B 2 198 ? -3.475  26.285  -12.702 1.00 82.95  ?  198 GLN B N   1 
ATOM   3082 C CA  . GLN B 2 198 ? -2.860  26.617  -11.426 1.00 77.08  ?  198 GLN B CA  1 
ATOM   3083 C C   . GLN B 2 198 ? -1.954  25.470  -11.000 1.00 75.54  ?  198 GLN B C   1 
ATOM   3084 O O   . GLN B 2 198 ? -2.328  24.299  -11.120 1.00 79.14  ?  198 GLN B O   1 
ATOM   3085 C CB  . GLN B 2 198 ? -3.931  26.889  -10.365 1.00 72.90  ?  198 GLN B CB  1 
ATOM   3086 C CG  . GLN B 2 198 ? -3.386  27.260  -9.004  1.00 75.58  ?  198 GLN B CG  1 
ATOM   3087 C CD  . GLN B 2 198 ? -2.837  28.664  -8.969  1.00 84.33  ?  198 GLN B CD  1 
ATOM   3088 O OE1 . GLN B 2 198 ? -3.413  29.581  -9.556  1.00 88.07  ?  198 GLN B OE1 1 
ATOM   3089 N NE2 . GLN B 2 198 ? -1.712  28.844  -8.284  1.00 86.44  ?  198 GLN B NE2 1 
ATOM   3090 N N   . THR B 2 199 ? -0.754  25.810  -10.542 1.00 75.25  ?  199 THR B N   1 
ATOM   3091 C CA  . THR B 2 199 ? 0.190   24.831  -10.026 1.00 73.14  ?  199 THR B CA  1 
ATOM   3092 C C   . THR B 2 199 ? 0.054   24.793  -8.512  1.00 68.33  ?  199 THR B C   1 
ATOM   3093 O O   . THR B 2 199 ? -0.008  25.842  -7.861  1.00 68.06  ?  199 THR B O   1 
ATOM   3094 C CB  . THR B 2 199 ? 1.632   25.157  -10.427 1.00 72.08  ?  199 THR B CB  1 
ATOM   3095 O OG1 . THR B 2 199 ? 1.963   26.487  -10.005 1.00 83.44  ?  199 THR B OG1 1 
ATOM   3096 C CG2 . THR B 2 199 ? 1.819   25.029  -11.937 1.00 65.34  ?  199 THR B CG2 1 
ATOM   3097 N N   . TYR B 2 200 ? -0.014  23.588  -7.960  1.00 65.17  ?  200 TYR B N   1 
ATOM   3098 C CA  . TYR B 2 200 ? -0.175  23.399  -6.527  1.00 60.81  ?  200 TYR B CA  1 
ATOM   3099 C C   . TYR B 2 200 ? 1.060   22.688  -5.998  1.00 58.26  ?  200 TYR B C   1 
ATOM   3100 O O   . TYR B 2 200 ? 1.374   21.572  -6.429  1.00 54.73  ?  200 TYR B O   1 
ATOM   3101 C CB  . TYR B 2 200 ? -1.454  22.616  -6.225  1.00 61.32  ?  200 TYR B CB  1 
ATOM   3102 C CG  . TYR B 2 200 ? -2.708  23.400  -6.557  1.00 63.84  ?  200 TYR B CG  1 
ATOM   3103 C CD1 . TYR B 2 200 ? -3.172  24.394  -5.702  1.00 60.89  ?  200 TYR B CD1 1 
ATOM   3104 C CD2 . TYR B 2 200 ? -3.414  23.162  -7.732  1.00 60.61  ?  200 TYR B CD2 1 
ATOM   3105 C CE1 . TYR B 2 200 ? -4.304  25.119  -5.998  1.00 53.50  ?  200 TYR B CE1 1 
ATOM   3106 C CE2 . TYR B 2 200 ? -4.549  23.884  -8.037  1.00 62.31  ?  200 TYR B CE2 1 
ATOM   3107 C CZ  . TYR B 2 200 ? -4.992  24.861  -7.164  1.00 63.98  ?  200 TYR B CZ  1 
ATOM   3108 O OH  . TYR B 2 200 ? -6.126  25.587  -7.454  1.00 66.46  ?  200 TYR B OH  1 
ATOM   3109 N N   . ILE B 2 201 ? 1.772   23.353  -5.095  1.00 50.84  ?  201 ILE B N   1 
ATOM   3110 C CA  . ILE B 2 201 ? 3.030   22.860  -4.554  1.00 54.56  ?  201 ILE B CA  1 
ATOM   3111 C C   . ILE B 2 201 ? 2.930   22.880  -3.041  1.00 47.82  ?  201 ILE B C   1 
ATOM   3112 O O   . ILE B 2 201 ? 2.610   23.917  -2.450  1.00 47.88  ?  201 ILE B O   1 
ATOM   3113 C CB  . ILE B 2 201 ? 4.231   23.709  -5.014  1.00 53.56  ?  201 ILE B CB  1 
ATOM   3114 C CG1 . ILE B 2 201 ? 4.331   23.732  -6.536  1.00 53.28  ?  201 ILE B CG1 1 
ATOM   3115 C CG2 . ILE B 2 201 ? 5.523   23.198  -4.385  1.00 50.84  ?  201 ILE B CG2 1 
ATOM   3116 C CD1 . ILE B 2 201 ? 5.381   24.678  -7.034  1.00 44.45  ?  201 ILE B CD1 1 
ATOM   3117 N N   . CYS B 2 202 ? 3.189   21.743  -2.413  1.00 45.87  ?  202 CYS B N   1 
ATOM   3118 C CA  . CYS B 2 202 ? 3.244   21.705  -0.962  1.00 48.65  ?  202 CYS B CA  1 
ATOM   3119 C C   . CYS B 2 202 ? 4.704   21.697  -0.514  1.00 45.15  ?  202 CYS B C   1 
ATOM   3120 O O   . CYS B 2 202 ? 5.564   21.058  -1.134  1.00 42.98  ?  202 CYS B O   1 
ATOM   3121 C CB  . CYS B 2 202 ? 2.473   20.507  -0.400  1.00 45.81  ?  202 CYS B CB  1 
ATOM   3122 S SG  . CYS B 2 202 ? 3.378   18.981  -0.314  1.00 60.57  ?  202 CYS B SG  1 
ATOM   3123 N N   . ASN B 2 203 ? 4.975   22.450  0.545   1.00 41.95  ?  203 ASN B N   1 
ATOM   3124 C CA  . ASN B 2 203 ? 6.307   22.666  1.087   1.00 46.63  ?  203 ASN B CA  1 
ATOM   3125 C C   . ASN B 2 203 ? 6.314   22.052  2.473   1.00 44.98  ?  203 ASN B C   1 
ATOM   3126 O O   . ASN B 2 203 ? 5.630   22.548  3.377   1.00 46.65  ?  203 ASN B O   1 
ATOM   3127 C CB  . ASN B 2 203 ? 6.651   24.156  1.163   1.00 46.79  ?  203 ASN B CB  1 
ATOM   3128 C CG  . ASN B 2 203 ? 6.023   24.960  0.048   1.00 48.88  ?  203 ASN B CG  1 
ATOM   3129 O OD1 . ASN B 2 203 ? 5.171   25.820  0.290   1.00 47.41  ?  203 ASN B OD1 1 
ATOM   3130 N ND2 . ASN B 2 203 ? 6.430   24.678  -1.186  1.00 47.84  ?  203 ASN B ND2 1 
ATOM   3131 N N   . VAL B 2 204 ? 7.054   20.961  2.623   1.00 40.21  ?  204 VAL B N   1 
ATOM   3132 C CA  . VAL B 2 204 ? 7.209   20.270  3.892   1.00 43.06  ?  204 VAL B CA  1 
ATOM   3133 C C   . VAL B 2 204 ? 8.579   20.632  4.442   1.00 41.69  ?  204 VAL B C   1 
ATOM   3134 O O   . VAL B 2 204 ? 9.584   20.569  3.722   1.00 43.02  ?  204 VAL B O   1 
ATOM   3135 C CB  . VAL B 2 204 ? 7.057   18.748  3.717   1.00 39.46  ?  204 VAL B CB  1 
ATOM   3136 C CG1 . VAL B 2 204 ? 6.968   18.055  5.069   1.00 36.90  ?  204 VAL B CG1 1 
ATOM   3137 C CG2 . VAL B 2 204 ? 5.845   18.431  2.859   1.00 34.39  ?  204 VAL B CG2 1 
ATOM   3138 N N   . ASN B 2 205 ? 8.622   21.042  5.702   1.00 40.25  ?  205 ASN B N   1 
ATOM   3139 C CA  . ASN B 2 205 ? 9.876   21.391  6.345   1.00 43.72  ?  205 ASN B CA  1 
ATOM   3140 C C   . ASN B 2 205 ? 9.994   20.566  7.611   1.00 47.19  ?  205 ASN B C   1 
ATOM   3141 O O   . ASN B 2 205 ? 9.083   20.573  8.447   1.00 47.74  ?  205 ASN B O   1 
ATOM   3142 C CB  . ASN B 2 205 ? 9.953   22.890  6.659   1.00 45.34  ?  205 ASN B CB  1 
ATOM   3143 C CG  . ASN B 2 205 ? 11.378  23.358  6.920   1.00 58.50  ?  205 ASN B CG  1 
ATOM   3144 O OD1 . ASN B 2 205 ? 11.755  23.644  8.057   1.00 61.31  ?  205 ASN B OD1 1 
ATOM   3145 N ND2 . ASN B 2 205 ? 12.181  23.426  5.864   1.00 60.77  ?  205 ASN B ND2 1 
ATOM   3146 N N   . HIS B 2 206 ? 11.105  19.838  7.736   1.00 44.89  ?  206 HIS B N   1 
ATOM   3147 C CA  . HIS B 2 206 ? 11.409  19.003  8.893   1.00 48.40  ?  206 HIS B CA  1 
ATOM   3148 C C   . HIS B 2 206 ? 12.784  19.462  9.365   1.00 48.19  ?  206 HIS B C   1 
ATOM   3149 O O   . HIS B 2 206 ? 13.810  18.901  8.956   1.00 45.94  ?  206 HIS B O   1 
ATOM   3150 C CB  . HIS B 2 206 ? 11.372  17.514  8.522   1.00 47.28  ?  206 HIS B CB  1 
ATOM   3151 C CG  . HIS B 2 206 ? 11.427  16.591  9.698   1.00 45.89  ?  206 HIS B CG  1 
ATOM   3152 N ND1 . HIS B 2 206 ? 12.279  15.509  9.753   1.00 45.23  ?  206 HIS B ND1 1 
ATOM   3153 C CD2 . HIS B 2 206 ? 10.738  16.585  10.864  1.00 44.04  ?  206 HIS B CD2 1 
ATOM   3154 C CE1 . HIS B 2 206 ? 12.113  14.877  10.902  1.00 43.64  ?  206 HIS B CE1 1 
ATOM   3155 N NE2 . HIS B 2 206 ? 11.181  15.508  11.593  1.00 48.15  ?  206 HIS B NE2 1 
ATOM   3156 N N   . LYS B 2 207 ? 12.792  20.515  10.188  1.00 48.74  ?  207 LYS B N   1 
ATOM   3157 C CA  . LYS B 2 207 ? 14.048  21.027  10.731  1.00 44.94  ?  207 LYS B CA  1 
ATOM   3158 C C   . LYS B 2 207 ? 14.850  19.983  11.500  1.00 49.38  ?  207 LYS B C   1 
ATOM   3159 O O   . LYS B 2 207 ? 16.083  19.961  11.337  1.00 51.33  ?  207 LYS B O   1 
ATOM   3160 C CB  . LYS B 2 207 ? 13.780  22.255  11.610  1.00 48.19  ?  207 LYS B CB  1 
ATOM   3161 C CG  . LYS B 2 207 ? 13.541  23.535  10.825  1.00 63.00  ?  207 LYS B CG  1 
ATOM   3162 C CD  . LYS B 2 207 ? 13.200  24.701  11.742  1.00 64.16  ?  207 LYS B CD  1 
ATOM   3163 C CE  . LYS B 2 207 ? 12.629  25.878  10.956  1.00 67.27  ?  207 LYS B CE  1 
ATOM   3164 N NZ  . LYS B 2 207 ? 13.503  26.295  9.822   1.00 76.64  ?  207 LYS B NZ  1 
ATOM   3165 N N   . PRO B 2 208 ? 14.259  19.117  12.336  1.00 49.03  ?  208 PRO B N   1 
ATOM   3166 C CA  . PRO B 2 208 ? 15.083  18.113  13.030  1.00 44.99  ?  208 PRO B CA  1 
ATOM   3167 C C   . PRO B 2 208 ? 15.820  17.165  12.102  1.00 43.97  ?  208 PRO B C   1 
ATOM   3168 O O   . PRO B 2 208 ? 16.774  16.522  12.548  1.00 49.56  ?  208 PRO B O   1 
ATOM   3169 C CB  . PRO B 2 208 ? 14.070  17.368  13.912  1.00 49.09  ?  208 PRO B CB  1 
ATOM   3170 C CG  . PRO B 2 208 ? 12.725  17.759  13.405  1.00 45.54  ?  208 PRO B CG  1 
ATOM   3171 C CD  . PRO B 2 208 ? 12.875  19.119  12.846  1.00 43.54  ?  208 PRO B CD  1 
ATOM   3172 N N   . SER B 2 209 ? 15.427  17.066  10.830  1.00 49.29  ?  209 SER B N   1 
ATOM   3173 C CA  . SER B 2 209 ? 16.202  16.346  9.823   1.00 46.29  ?  209 SER B CA  1 
ATOM   3174 C C   . SER B 2 209 ? 17.027  17.264  8.938   1.00 48.37  ?  209 SER B C   1 
ATOM   3175 O O   . SER B 2 209 ? 17.766  16.767  8.081   1.00 46.67  ?  209 SER B O   1 
ATOM   3176 C CB  . SER B 2 209 ? 15.294  15.521  8.909   1.00 40.07  ?  209 SER B CB  1 
ATOM   3177 O OG  . SER B 2 209 ? 15.030  14.256  9.463   1.00 59.00  ?  209 SER B OG  1 
ATOM   3178 N N   . ASN B 2 210 ? 16.893  18.578  9.097   1.00 45.62  ?  210 ASN B N   1 
ATOM   3179 C CA  . ASN B 2 210 ? 17.437  19.532  8.141   1.00 50.48  ?  210 ASN B CA  1 
ATOM   3180 C C   . ASN B 2 210 ? 16.959  19.205  6.728   1.00 49.41  ?  210 ASN B C   1 
ATOM   3181 O O   . ASN B 2 210 ? 17.727  19.249  5.765   1.00 51.97  ?  210 ASN B O   1 
ATOM   3182 C CB  . ASN B 2 210 ? 18.964  19.557  8.213   1.00 51.99  ?  210 ASN B CB  1 
ATOM   3183 C CG  . ASN B 2 210 ? 19.472  20.009  9.566   1.00 59.26  ?  210 ASN B CG  1 
ATOM   3184 O OD1 . ASN B 2 210 ? 19.175  21.116  10.015  1.00 58.59  ?  210 ASN B OD1 1 
ATOM   3185 N ND2 . ASN B 2 210 ? 20.240  19.147  10.230  1.00 55.95  ?  210 ASN B ND2 1 
ATOM   3186 N N   . THR B 2 211 ? 15.674  18.865  6.600   1.00 47.85  ?  211 THR B N   1 
ATOM   3187 C CA  . THR B 2 211 ? 15.116  18.430  5.325   1.00 43.21  ?  211 THR B CA  1 
ATOM   3188 C C   . THR B 2 211 ? 13.980  19.351  4.898   1.00 50.46  ?  211 THR B C   1 
ATOM   3189 O O   . THR B 2 211 ? 13.151  19.760  5.718   1.00 51.36  ?  211 THR B O   1 
ATOM   3190 C CB  . THR B 2 211 ? 14.603  16.980  5.394   1.00 46.73  ?  211 THR B CB  1 
ATOM   3191 O OG1 . THR B 2 211 ? 15.640  16.115  5.868   1.00 54.68  ?  211 THR B OG1 1 
ATOM   3192 C CG2 . THR B 2 211 ? 14.181  16.500  4.019   1.00 45.34  ?  211 THR B CG2 1 
ATOM   3193 N N   . LYS B 2 212 ? 13.953  19.691  3.611   1.00 47.95  ?  212 LYS B N   1 
ATOM   3194 C CA  . LYS B 2 212 ? 12.825  20.394  3.016   1.00 44.48  ?  212 LYS B CA  1 
ATOM   3195 C C   . LYS B 2 212 ? 12.431  19.681  1.733   1.00 45.26  ?  212 LYS B C   1 
ATOM   3196 O O   . LYS B 2 212 ? 13.294  19.322  0.927   1.00 46.96  ?  212 LYS B O   1 
ATOM   3197 C CB  . LYS B 2 212 ? 13.143  21.868  2.728   1.00 46.47  ?  212 LYS B CB  1 
ATOM   3198 C CG  . LYS B 2 212 ? 12.005  22.584  2.002   1.00 57.35  ?  212 LYS B CG  1 
ATOM   3199 C CD  . LYS B 2 212 ? 12.184  24.098  1.961   1.00 69.48  ?  212 LYS B CD  1 
ATOM   3200 C CE  . LYS B 2 212 ? 10.915  24.786  1.459   1.00 65.62  ?  212 LYS B CE  1 
ATOM   3201 N NZ  . LYS B 2 212 ? 11.041  26.273  1.406   1.00 82.94  ?  212 LYS B NZ  1 
ATOM   3202 N N   . VAL B 2 213 ? 11.134  19.444  1.568   1.00 45.41  ?  213 VAL B N   1 
ATOM   3203 C CA  . VAL B 2 213 ? 10.586  18.807  0.379   1.00 39.67  ?  213 VAL B CA  1 
ATOM   3204 C C   . VAL B 2 213 ? 9.594   19.761  -0.265  1.00 45.64  ?  213 VAL B C   1 
ATOM   3205 O O   . VAL B 2 213 ? 8.780   20.383  0.423   1.00 48.38  ?  213 VAL B O   1 
ATOM   3206 C CB  . VAL B 2 213 ? 9.905   17.466  0.715   1.00 41.90  ?  213 VAL B CB  1 
ATOM   3207 C CG1 . VAL B 2 213 ? 9.444   16.768  -0.562  1.00 41.46  ?  213 VAL B CG1 1 
ATOM   3208 C CG2 . VAL B 2 213 ? 10.840  16.585  1.528   1.00 40.88  ?  213 VAL B CG2 1 
ATOM   3209 N N   . ASP B 2 214 ? 9.670   19.888  -1.582  1.00 42.56  ?  214 ASP B N   1 
ATOM   3210 C CA  . ASP B 2 214 ? 8.704   20.658  -2.355  1.00 42.78  ?  214 ASP B CA  1 
ATOM   3211 C C   . ASP B 2 214 ? 8.119   19.710  -3.387  1.00 51.17  ?  214 ASP B C   1 
ATOM   3212 O O   . ASP B 2 214 ? 8.831   19.252  -4.286  1.00 53.92  ?  214 ASP B O   1 
ATOM   3213 C CB  . ASP B 2 214 ? 9.346   21.880  -3.012  1.00 46.85  ?  214 ASP B CB  1 
ATOM   3214 C CG  . ASP B 2 214 ? 9.800   22.922  -1.999  1.00 55.05  ?  214 ASP B CG  1 
ATOM   3215 O OD1 . ASP B 2 214 ? 9.010   23.255  -1.090  1.00 54.61  ?  214 ASP B OD1 1 
ATOM   3216 O OD2 . ASP B 2 214 ? 10.946  23.413  -2.111  1.00 65.06  ?  214 ASP B OD2 1 
ATOM   3217 N N   . LYS B 2 215 ? 6.833   19.401  -3.248  1.00 50.31  ?  215 LYS B N   1 
ATOM   3218 C CA  . LYS B 2 215 ? 6.179   18.417  -4.099  1.00 46.99  ?  215 LYS B CA  1 
ATOM   3219 C C   . LYS B 2 215 ? 5.065   19.094  -4.882  1.00 53.47  ?  215 LYS B C   1 
ATOM   3220 O O   . LYS B 2 215 ? 4.140   19.667  -4.290  1.00 54.49  ?  215 LYS B O   1 
ATOM   3221 C CB  . LYS B 2 215 ? 5.635   17.256  -3.265  1.00 50.56  ?  215 LYS B CB  1 
ATOM   3222 C CG  . LYS B 2 215 ? 4.622   16.384  -3.986  1.00 54.98  ?  215 LYS B CG  1 
ATOM   3223 C CD  . LYS B 2 215 ? 5.255   15.596  -5.108  1.00 56.93  ?  215 LYS B CD  1 
ATOM   3224 C CE  . LYS B 2 215 ? 6.013   14.400  -4.574  1.00 53.36  ?  215 LYS B CE  1 
ATOM   3225 N NZ  . LYS B 2 215 ? 6.443   13.529  -5.695  1.00 60.23  ?  215 LYS B NZ  1 
ATOM   3226 N N   . LYS B 2 216 ? 5.166   19.044  -6.208  1.00 56.77  ?  216 LYS B N   1 
ATOM   3227 C CA  . LYS B 2 216 ? 4.090   19.522  -7.062  1.00 61.54  ?  216 LYS B CA  1 
ATOM   3228 C C   . LYS B 2 216 ? 3.056   18.417  -7.221  1.00 55.21  ?  216 LYS B C   1 
ATOM   3229 O O   . LYS B 2 216 ? 3.391   17.296  -7.617  1.00 55.02  ?  216 LYS B O   1 
ATOM   3230 C CB  . LYS B 2 216 ? 4.616   19.955  -8.431  1.00 59.69  ?  216 LYS B CB  1 
ATOM   3231 C CG  . LYS B 2 216 ? 3.542   20.614  -9.285  1.00 64.01  ?  216 LYS B CG  1 
ATOM   3232 C CD  . LYS B 2 216 ? 3.932   20.757  -10.747 1.00 63.65  ?  216 LYS B CD  1 
ATOM   3233 C CE  . LYS B 2 216 ? 2.895   21.605  -11.488 1.00 68.54  ?  216 LYS B CE  1 
ATOM   3234 N NZ  . LYS B 2 216 ? 3.026   21.558  -12.975 1.00 69.23  ?  216 LYS B NZ  1 
ATOM   3235 N N   . VAL B 2 217 ? 1.804   18.732  -6.908  1.00 57.17  ?  217 VAL B N   1 
ATOM   3236 C CA  . VAL B 2 217 ? 0.706   17.778  -7.001  1.00 61.69  ?  217 VAL B CA  1 
ATOM   3237 C C   . VAL B 2 217 ? 0.024   17.978  -8.349  1.00 57.68  ?  217 VAL B C   1 
ATOM   3238 O O   . VAL B 2 217 ? -0.473  19.071  -8.644  1.00 60.39  ?  217 VAL B O   1 
ATOM   3239 C CB  . VAL B 2 217 ? -0.290  17.956  -5.845  1.00 59.15  ?  217 VAL B CB  1 
ATOM   3240 C CG1 . VAL B 2 217 ? -1.278  16.799  -5.813  1.00 58.13  ?  217 VAL B CG1 1 
ATOM   3241 C CG2 . VAL B 2 217 ? 0.442   18.102  -4.513  1.00 51.37  ?  217 VAL B CG2 1 
ATOM   3242 N N   . GLU B 2 218 ? 0.027   16.940  -9.182  1.00 59.58  ?  218 GLU B N   1 
ATOM   3243 C CA  . GLU B 2 218 ? -0.570  17.044  -10.501 1.00 67.02  ?  218 GLU B CA  1 
ATOM   3244 C C   . GLU B 2 218 ? -1.773  16.117  -10.624 1.00 68.74  ?  218 GLU B C   1 
ATOM   3245 O O   . GLU B 2 218 ? -1.752  14.998  -10.101 1.00 68.89  ?  218 GLU B O   1 
ATOM   3246 C CB  . GLU B 2 218 ? 0.450   16.731  -11.606 1.00 74.54  ?  218 GLU B CB  1 
ATOM   3247 C CG  . GLU B 2 218 ? 1.367   17.915  -11.908 1.00 76.85  ?  218 GLU B CG  1 
ATOM   3248 C CD  . GLU B 2 218 ? 2.403   17.618  -12.972 1.00 83.47  ?  218 GLU B CD  1 
ATOM   3249 O OE1 . GLU B 2 218 ? 2.803   16.439  -13.107 1.00 91.81  ?  218 GLU B OE1 1 
ATOM   3250 O OE2 . GLU B 2 218 ? 2.807   18.567  -13.680 1.00 72.77  ?  218 GLU B OE2 1 
ATOM   3251 N N   . PRO B 2 219 ? -2.841  16.561  -11.287 1.00 69.13  ?  219 PRO B N   1 
ATOM   3252 C CA  . PRO B 2 219 ? -4.048  15.729  -11.401 1.00 71.23  ?  219 PRO B CA  1 
ATOM   3253 C C   . PRO B 2 219 ? -3.825  14.543  -12.327 1.00 76.57  ?  219 PRO B C   1 
ATOM   3254 O O   . PRO B 2 219 ? -3.506  14.706  -13.506 1.00 82.17  ?  219 PRO B O   1 
ATOM   3255 C CB  . PRO B 2 219 ? -5.095  16.700  -11.959 1.00 77.97  ?  219 PRO B CB  1 
ATOM   3256 C CG  . PRO B 2 219 ? -4.305  17.746  -12.667 1.00 74.56  ?  219 PRO B CG  1 
ATOM   3257 C CD  . PRO B 2 219 ? -3.024  17.892  -11.894 1.00 74.16  ?  219 PRO B CD  1 
ATOM   3258 N N   . LYS B 2 220 ? -3.983  13.344  -11.775 1.00 82.29  ?  220 LYS B N   1 
ATOM   3259 C CA  . LYS B 2 220 ? -3.928  12.109  -12.540 1.00 83.45  ?  220 LYS B CA  1 
ATOM   3260 C C   . LYS B 2 220 ? -5.345  11.697  -12.908 1.00 85.94  ?  220 LYS B C   1 
ATOM   3261 O O   . LYS B 2 220 ? -6.292  11.919  -12.149 1.00 87.30  ?  220 LYS B O   1 
ATOM   3262 C CB  . LYS B 2 220 ? -3.250  10.967  -11.766 1.00 83.42  ?  220 LYS B CB  1 
ATOM   3263 C CG  . LYS B 2 220 ? -1.769  11.161  -11.413 1.00 86.18  ?  220 LYS B CG  1 
ATOM   3264 C CD  . LYS B 2 220 ? -1.034  12.100  -12.367 1.00 82.95  ?  220 LYS B CD  1 
ATOM   3265 C CE  . LYS B 2 220 ? 0.391   12.369  -11.879 1.00 78.89  ?  220 LYS B CE  1 
ATOM   3266 N NZ  . LYS B 2 220 ? 1.155   13.277  -12.793 1.00 81.96  ?  220 LYS B NZ  1 
ATOM   3267 N N   . SER B 2 221 ? -5.487  11.110  -14.091 1.00 96.90  ?  221 SER B N   1 
ATOM   3268 C CA  . SER B 2 221 ? -6.798  10.662  -14.555 1.00 98.92  ?  221 SER B CA  1 
ATOM   3269 C C   . SER B 2 221 ? -7.126  9.275   -14.004 1.00 94.22  ?  221 SER B C   1 
ATOM   3270 O O   . SER B 2 221 ? -8.108  9.106   -13.277 1.00 93.97  ?  221 SER B O   1 
ATOM   3271 C CB  . SER B 2 221 ? -6.852  10.648  -16.082 1.00 93.69  ?  221 SER B CB  1 
ATOM   3272 O OG  . SER B 2 221 ? -7.250  11.911  -16.581 1.00 96.02  ?  221 SER B OG  1 
ATOM   3273 N N   . ALA C 1 1   ? 9.743   3.359   26.593  1.00 41.17  ?  1   ALA C N   1 
ATOM   3274 C CA  . ALA C 1 1   ? 9.361   3.688   27.963  1.00 37.25  ?  1   ALA C CA  1 
ATOM   3275 C C   . ALA C 1 1   ? 7.895   3.359   28.208  1.00 45.18  ?  1   ALA C C   1 
ATOM   3276 O O   . ALA C 1 1   ? 7.036   3.606   27.358  1.00 49.28  ?  1   ALA C O   1 
ATOM   3277 C CB  . ALA C 1 1   ? 9.628   5.140   28.253  1.00 32.45  ?  1   ALA C CB  1 
ATOM   3278 N N   . ILE C 1 2   ? 7.605   2.801   29.375  1.00 42.58  ?  2   ILE C N   1 
ATOM   3279 C CA  . ILE C 1 2   ? 6.249   2.399   29.708  1.00 44.86  ?  2   ILE C CA  1 
ATOM   3280 C C   . ILE C 1 2   ? 5.833   3.099   30.987  1.00 44.24  ?  2   ILE C C   1 
ATOM   3281 O O   . ILE C 1 2   ? 6.647   3.358   31.879  1.00 49.34  ?  2   ILE C O   1 
ATOM   3282 C CB  . ILE C 1 2   ? 6.098   0.869   29.864  1.00 45.58  ?  2   ILE C CB  1 
ATOM   3283 C CG1 . ILE C 1 2   ? 7.141   0.339   30.847  1.00 47.42  ?  2   ILE C CG1 1 
ATOM   3284 C CG2 . ILE C 1 2   ? 6.163   0.175   28.506  1.00 38.96  ?  2   ILE C CG2 1 
ATOM   3285 C CD1 . ILE C 1 2   ? 6.765   -0.979  31.467  1.00 48.00  ?  2   ILE C CD1 1 
ATOM   3286 N N   . GLN C 1 3   ? 4.544   3.402   31.068  1.00 43.06  ?  3   GLN C N   1 
ATOM   3287 C CA  . GLN C 1 3   ? 3.956   4.050   32.223  1.00 44.84  ?  3   GLN C CA  1 
ATOM   3288 C C   . GLN C 1 3   ? 2.748   3.242   32.653  1.00 44.33  ?  3   GLN C C   1 
ATOM   3289 O O   . GLN C 1 3   ? 1.998   2.743   31.811  1.00 46.57  ?  3   GLN C O   1 
ATOM   3290 C CB  . GLN C 1 3   ? 3.527   5.499   31.899  1.00 48.99  ?  3   GLN C CB  1 
ATOM   3291 C CG  . GLN C 1 3   ? 4.657   6.422   31.441  1.00 50.73  ?  3   GLN C CG  1 
ATOM   3292 C CD  . GLN C 1 3   ? 4.810   6.495   29.919  1.00 53.96  ?  3   GLN C CD  1 
ATOM   3293 O OE1 . GLN C 1 3   ? 3.849   6.307   29.169  1.00 45.88  ?  3   GLN C OE1 1 
ATOM   3294 N NE2 . GLN C 1 3   ? 6.029   6.764   29.463  1.00 52.82  ?  3   GLN C NE2 1 
ATOM   3295 N N   . MET C 1 4   ? 2.562   3.116   33.961  1.00 42.57  ?  4   MET C N   1 
ATOM   3296 C CA  . MET C 1 4   ? 1.374   2.495   34.522  1.00 42.57  ?  4   MET C CA  1 
ATOM   3297 C C   . MET C 1 4   ? 0.538   3.569   35.204  1.00 47.42  ?  4   MET C C   1 
ATOM   3298 O O   . MET C 1 4   ? 1.039   4.295   36.068  1.00 48.50  ?  4   MET C O   1 
ATOM   3299 C CB  . MET C 1 4   ? 1.736   1.391   35.522  1.00 46.40  ?  4   MET C CB  1 
ATOM   3300 C CG  . MET C 1 4   ? 2.788   0.387   35.044  1.00 44.02  ?  4   MET C CG  1 
ATOM   3301 S SD  . MET C 1 4   ? 2.375   -0.508  33.526  1.00 52.62  ?  4   MET C SD  1 
ATOM   3302 C CE  . MET C 1 4   ? 0.693   -1.019  33.826  1.00 39.41  ?  4   MET C CE  1 
ATOM   3303 N N   . THR C 1 5   ? -0.727  3.676   34.810  1.00 51.46  ?  5   THR C N   1 
ATOM   3304 C CA  . THR C 1 5   ? -1.674  4.585   35.451  1.00 44.57  ?  5   THR C CA  1 
ATOM   3305 C C   . THR C 1 5   ? -2.576  3.762   36.360  1.00 42.17  ?  5   THR C C   1 
ATOM   3306 O O   . THR C 1 5   ? -3.407  2.990   35.879  1.00 48.40  ?  5   THR C O   1 
ATOM   3307 C CB  . THR C 1 5   ? -2.494  5.354   34.416  1.00 47.19  ?  5   THR C CB  1 
ATOM   3308 O OG1 . THR C 1 5   ? -1.619  6.077   33.538  1.00 54.57  ?  5   THR C OG1 1 
ATOM   3309 C CG2 . THR C 1 5   ? -3.443  6.323   35.102  1.00 40.70  ?  5   THR C CG2 1 
ATOM   3310 N N   . GLN C 1 6   ? -2.394  3.907   37.667  1.00 44.98  ?  6   GLN C N   1 
ATOM   3311 C CA  . GLN C 1 6   ? -3.182  3.192   38.659  1.00 41.04  ?  6   GLN C CA  1 
ATOM   3312 C C   . GLN C 1 6   ? -4.321  4.076   39.148  1.00 41.31  ?  6   GLN C C   1 
ATOM   3313 O O   . GLN C 1 6   ? -4.180  5.295   39.252  1.00 40.87  ?  6   GLN C O   1 
ATOM   3314 C CB  . GLN C 1 6   ? -2.306  2.754   39.836  1.00 40.76  ?  6   GLN C CB  1 
ATOM   3315 C CG  . GLN C 1 6   ? -2.872  1.591   40.629  1.00 46.58  ?  6   GLN C CG  1 
ATOM   3316 C CD  . GLN C 1 6   ? -1.858  0.982   41.579  1.00 46.37  ?  6   GLN C CD  1 
ATOM   3317 O OE1 . GLN C 1 6   ? -0.670  0.901   41.267  1.00 47.04  ?  6   GLN C OE1 1 
ATOM   3318 N NE2 . GLN C 1 6   ? -2.321  0.555   42.749  1.00 44.71  ?  6   GLN C NE2 1 
ATOM   3319 N N   . SER C 1 7   ? -5.453  3.446   39.463  1.00 48.54  ?  7   SER C N   1 
ATOM   3320 C CA  . SER C 1 7   ? -6.641  4.168   39.878  1.00 43.62  ?  7   SER C CA  1 
ATOM   3321 C C   . SER C 1 7   ? -7.522  3.291   40.754  1.00 46.95  ?  7   SER C C   1 
ATOM   3322 O O   . SER C 1 7   ? -7.600  2.075   40.520  1.00 45.19  ?  7   SER C O   1 
ATOM   3323 C CB  . SER C 1 7   ? -7.436  4.640   38.661  1.00 39.15  ?  7   SER C CB  1 
ATOM   3324 O OG  . SER C 1 7   ? -8.488  5.500   39.055  1.00 62.47  ?  7   SER C OG  1 
ATOM   3325 N N   . PRO C 1 8   ? -8.163  3.854   41.790  1.00 45.88  ?  8   PRO C N   1 
ATOM   3326 C CA  . PRO C 1 8   ? -8.060  5.235   42.272  1.00 46.10  ?  8   PRO C CA  1 
ATOM   3327 C C   . PRO C 1 8   ? -6.824  5.438   43.140  1.00 48.76  ?  8   PRO C C   1 
ATOM   3328 O O   . PRO C 1 8   ? -6.173  4.457   43.488  1.00 51.00  ?  8   PRO C O   1 
ATOM   3329 C CB  . PRO C 1 8   ? -9.331  5.410   43.098  1.00 40.36  ?  8   PRO C CB  1 
ATOM   3330 C CG  . PRO C 1 8   ? -9.589  4.046   43.639  1.00 48.65  ?  8   PRO C CG  1 
ATOM   3331 C CD  . PRO C 1 8   ? -9.136  3.074   42.576  1.00 42.51  ?  8   PRO C CD  1 
ATOM   3332 N N   . SER C 1 9   ? -6.494  6.692   43.463  1.00 52.33  ?  9   SER C N   1 
ATOM   3333 C CA  . SER C 1 9   ? -5.366  6.949   44.356  1.00 45.40  ?  9   SER C CA  1 
ATOM   3334 C C   . SER C 1 9   ? -5.628  6.388   45.750  1.00 41.06  ?  9   SER C C   1 
ATOM   3335 O O   . SER C 1 9   ? -4.708  5.909   46.418  1.00 46.92  ?  9   SER C O   1 
ATOM   3336 C CB  . SER C 1 9   ? -5.083  8.446   44.435  1.00 49.48  ?  9   SER C CB  1 
ATOM   3337 O OG  . SER C 1 9   ? -6.152  9.125   45.075  1.00 59.95  ?  9   SER C OG  1 
ATOM   3338 N N   . SER C 1 10  ? -6.874  6.449   46.211  1.00 47.51  ?  10  SER C N   1 
ATOM   3339 C CA  . SER C 1 10  ? -7.257  5.843   47.478  1.00 47.30  ?  10  SER C CA  1 
ATOM   3340 C C   . SER C 1 10  ? -8.709  5.401   47.388  1.00 46.92  ?  10  SER C C   1 
ATOM   3341 O O   . SER C 1 10  ? -9.442  5.784   46.473  1.00 46.76  ?  10  SER C O   1 
ATOM   3342 C CB  . SER C 1 10  ? -7.067  6.806   48.659  1.00 51.22  ?  10  SER C CB  1 
ATOM   3343 O OG  . SER C 1 10  ? -7.667  8.066   48.399  1.00 44.01  ?  10  SER C OG  1 
ATOM   3344 N N   . LEU C 1 11  ? -9.110  4.571   48.343  1.00 43.32  ?  11  LEU C N   1 
ATOM   3345 C CA  . LEU C 1 11  ? -10.495 4.140   48.419  1.00 44.96  ?  11  LEU C CA  1 
ATOM   3346 C C   . LEU C 1 11  ? -10.753 3.614   49.821  1.00 49.26  ?  11  LEU C C   1 
ATOM   3347 O O   . LEU C 1 11  ? -9.856  3.078   50.476  1.00 49.06  ?  11  LEU C O   1 
ATOM   3348 C CB  . LEU C 1 11  ? -10.822 3.074   47.360  1.00 42.78  ?  11  LEU C CB  1 
ATOM   3349 C CG  . LEU C 1 11  ? -10.146 1.694   47.413  1.00 46.25  ?  11  LEU C CG  1 
ATOM   3350 C CD1 . LEU C 1 11  ? -10.872 0.723   48.349  1.00 43.70  ?  11  LEU C CD1 1 
ATOM   3351 C CD2 . LEU C 1 11  ? -10.000 1.093   46.021  1.00 40.30  ?  11  LEU C CD2 1 
ATOM   3352 N N   . SER C 1 12  ? -11.993 3.763   50.264  1.00 53.26  ?  12  SER C N   1 
ATOM   3353 C CA  . SER C 1 12  ? -12.450 3.200   51.521  1.00 52.32  ?  12  SER C CA  1 
ATOM   3354 C C   . SER C 1 12  ? -13.614 2.257   51.255  1.00 52.80  ?  12  SER C C   1 
ATOM   3355 O O   . SER C 1 12  ? -14.410 2.472   50.336  1.00 57.20  ?  12  SER C O   1 
ATOM   3356 C CB  . SER C 1 12  ? -12.874 4.296   52.507  1.00 57.89  ?  12  SER C CB  1 
ATOM   3357 O OG  . SER C 1 12  ? -13.271 3.733   53.746  1.00 61.18  ?  12  SER C OG  1 
ATOM   3358 N N   . ALA C 1 13  ? -13.699 1.201   52.055  1.00 54.88  ?  13  ALA C N   1 
ATOM   3359 C CA  . ALA C 1 13  ? -14.751 0.215   51.872  1.00 52.50  ?  13  ALA C CA  1 
ATOM   3360 C C   . ALA C 1 13  ? -14.953 -0.532  53.179  1.00 57.93  ?  13  ALA C C   1 
ATOM   3361 O O   . ALA C 1 13  ? -14.037 -0.632  54.000  1.00 56.44  ?  13  ALA C O   1 
ATOM   3362 C CB  . ALA C 1 13  ? -14.418 -0.760  50.739  1.00 52.51  ?  13  ALA C CB  1 
ATOM   3363 N N   . SER C 1 14  ? -16.169 -1.045  53.363  1.00 60.88  ?  14  SER C N   1 
ATOM   3364 C CA  . SER C 1 14  ? -16.523 -1.758  54.578  1.00 58.62  ?  14  SER C CA  1 
ATOM   3365 C C   . SER C 1 14  ? -15.988 -3.183  54.522  1.00 58.87  ?  14  SER C C   1 
ATOM   3366 O O   . SER C 1 14  ? -15.688 -3.722  53.453  1.00 52.49  ?  14  SER C O   1 
ATOM   3367 C CB  . SER C 1 14  ? -18.041 -1.789  54.775  1.00 55.24  ?  14  SER C CB  1 
ATOM   3368 O OG  . SER C 1 14  ? -18.608 -0.497  54.659  1.00 59.14  ?  14  SER C OG  1 
ATOM   3369 N N   . VAL C 1 15  ? -15.869 -3.792  55.702  1.00 58.22  ?  15  VAL C N   1 
ATOM   3370 C CA  . VAL C 1 15  ? -15.503 -5.198  55.771  1.00 57.91  ?  15  VAL C CA  1 
ATOM   3371 C C   . VAL C 1 15  ? -16.567 -6.020  55.065  1.00 58.90  ?  15  VAL C C   1 
ATOM   3372 O O   . VAL C 1 15  ? -17.762 -5.912  55.367  1.00 59.45  ?  15  VAL C O   1 
ATOM   3373 C CB  . VAL C 1 15  ? -15.326 -5.636  57.231  1.00 63.74  ?  15  VAL C CB  1 
ATOM   3374 C CG1 . VAL C 1 15  ? -15.138 -7.141  57.311  1.00 51.85  ?  15  VAL C CG1 1 
ATOM   3375 C CG2 . VAL C 1 15  ? -14.142 -4.906  57.856  1.00 63.22  ?  15  VAL C CG2 1 
ATOM   3376 N N   . GLY C 1 16  ? -16.136 -6.840  54.108  1.00 60.97  ?  16  GLY C N   1 
ATOM   3377 C CA  . GLY C 1 16  ? -17.034 -7.647  53.315  1.00 56.74  ?  16  GLY C CA  1 
ATOM   3378 C C   . GLY C 1 16  ? -17.314 -7.112  51.926  1.00 59.51  ?  16  GLY C C   1 
ATOM   3379 O O   . GLY C 1 16  ? -17.918 -7.826  51.118  1.00 66.95  ?  16  GLY C O   1 
ATOM   3380 N N   . ASP C 1 17  ? -16.908 -5.882  51.627  1.00 55.18  ?  17  ASP C N   1 
ATOM   3381 C CA  . ASP C 1 17  ? -17.142 -5.328  50.305  1.00 57.29  ?  17  ASP C CA  1 
ATOM   3382 C C   . ASP C 1 17  ? -16.183 -5.938  49.280  1.00 58.27  ?  17  ASP C C   1 
ATOM   3383 O O   . ASP C 1 17  ? -15.160 -6.536  49.620  1.00 54.83  ?  17  ASP C O   1 
ATOM   3384 C CB  . ASP C 1 17  ? -16.988 -3.803  50.322  1.00 59.04  ?  17  ASP C CB  1 
ATOM   3385 C CG  . ASP C 1 17  ? -18.108 -3.108  51.081  1.00 70.65  ?  17  ASP C CG  1 
ATOM   3386 O OD1 . ASP C 1 17  ? -17.904 -1.958  51.527  1.00 69.01  ?  17  ASP C OD1 1 
ATOM   3387 O OD2 . ASP C 1 17  ? -19.186 -3.720  51.256  1.00 73.82  ?  17  ASP C OD2 1 
ATOM   3388 N N   . ARG C 1 18  ? -16.530 -5.762  48.006  1.00 57.82  ?  18  ARG C N   1 
ATOM   3389 C CA  . ARG C 1 18  ? -15.692 -6.159  46.883  1.00 53.31  ?  18  ARG C CA  1 
ATOM   3390 C C   . ARG C 1 18  ? -15.032 -4.918  46.302  1.00 55.51  ?  18  ARG C C   1 
ATOM   3391 O O   . ARG C 1 18  ? -15.721 -4.044  45.768  1.00 57.33  ?  18  ARG C O   1 
ATOM   3392 C CB  . ARG C 1 18  ? -16.516 -6.870  45.809  1.00 56.31  ?  18  ARG C CB  1 
ATOM   3393 C CG  . ARG C 1 18  ? -15.791 -7.063  44.485  1.00 63.11  ?  18  ARG C CG  1 
ATOM   3394 C CD  . ARG C 1 18  ? -16.661 -7.798  43.478  1.00 65.93  ?  18  ARG C CD  1 
ATOM   3395 N NE  . ARG C 1 18  ? -17.263 -8.996  44.061  1.00 82.75  ?  18  ARG C NE  1 
ATOM   3396 C CZ  . ARG C 1 18  ? -16.701 -10.204 44.060  1.00 82.06  ?  18  ARG C CZ  1 
ATOM   3397 N NH1 . ARG C 1 18  ? -15.513 -10.389 43.499  1.00 74.61  ?  18  ARG C NH1 1 
ATOM   3398 N NH2 . ARG C 1 18  ? -17.331 -11.231 44.621  1.00 78.01  ?  18  ARG C NH2 1 
ATOM   3399 N N   . VAL C 1 19  ? -13.706 -4.845  46.390  1.00 57.06  ?  19  VAL C N   1 
ATOM   3400 C CA  . VAL C 1 19  ? -12.977 -3.667  45.939  1.00 54.62  ?  19  VAL C CA  1 
ATOM   3401 C C   . VAL C 1 19  ? -12.179 -4.012  44.689  1.00 50.66  ?  19  VAL C C   1 
ATOM   3402 O O   . VAL C 1 19  ? -11.699 -5.139  44.511  1.00 52.33  ?  19  VAL C O   1 
ATOM   3403 C CB  . VAL C 1 19  ? -12.066 -3.096  47.047  1.00 51.89  ?  19  VAL C CB  1 
ATOM   3404 C CG1 . VAL C 1 19  ? -12.815 -3.039  48.367  1.00 56.30  ?  19  VAL C CG1 1 
ATOM   3405 C CG2 . VAL C 1 19  ? -10.807 -3.914  47.188  1.00 57.18  ?  19  VAL C CG2 1 
ATOM   3406 N N   . THR C 1 20  ? -12.049 -3.016  43.813  1.00 47.74  ?  20  THR C N   1 
ATOM   3407 C CA  . THR C 1 20  ? -11.415 -3.183  42.513  1.00 43.03  ?  20  THR C CA  1 
ATOM   3408 C C   . THR C 1 20  ? -10.491 -2.002  42.243  1.00 45.30  ?  20  THR C C   1 
ATOM   3409 O O   . THR C 1 20  ? -10.936 -0.849  42.230  1.00 41.52  ?  20  THR C O   1 
ATOM   3410 C CB  . THR C 1 20  ? -12.475 -3.301  41.415  1.00 46.33  ?  20  THR C CB  1 
ATOM   3411 O OG1 . THR C 1 20  ? -13.278 -4.462  41.659  1.00 51.76  ?  20  THR C OG1 1 
ATOM   3412 C CG2 . THR C 1 20  ? -11.826 -3.419  40.047  1.00 44.40  ?  20  THR C CG2 1 
ATOM   3413 N N   . ILE C 1 21  ? -9.211  -2.302  42.030  1.00 42.32  ?  21  ILE C N   1 
ATOM   3414 C CA  . ILE C 1 21  ? -8.199  -1.348  41.600  1.00 37.69  ?  21  ILE C CA  1 
ATOM   3415 C C   . ILE C 1 21  ? -7.860  -1.639  40.146  1.00 40.82  ?  21  ILE C C   1 
ATOM   3416 O O   . ILE C 1 21  ? -7.756  -2.801  39.748  1.00 46.55  ?  21  ILE C O   1 
ATOM   3417 C CB  . ILE C 1 21  ? -6.948  -1.441  42.495  1.00 42.43  ?  21  ILE C CB  1 
ATOM   3418 C CG1 . ILE C 1 21  ? -7.350  -1.349  43.968  1.00 37.57  ?  21  ILE C CG1 1 
ATOM   3419 C CG2 . ILE C 1 21  ? -5.911  -0.396  42.107  1.00 46.62  ?  21  ILE C CG2 1 
ATOM   3420 C CD1 . ILE C 1 21  ? -6.243  -1.716  44.921  1.00 35.39  ?  21  ILE C CD1 1 
ATOM   3421 N N   . THR C 1 22  ? -7.691  -0.593  39.352  1.00 43.25  ?  22  THR C N   1 
ATOM   3422 C CA  . THR C 1 22  ? -7.333  -0.750  37.954  1.00 44.22  ?  22  THR C CA  1 
ATOM   3423 C C   . THR C 1 22  ? -5.960  -0.146  37.701  1.00 48.84  ?  22  THR C C   1 
ATOM   3424 O O   . THR C 1 22  ? -5.514  0.755   38.414  1.00 49.22  ?  22  THR C O   1 
ATOM   3425 C CB  . THR C 1 22  ? -8.386  -0.110  37.044  1.00 41.18  ?  22  THR C CB  1 
ATOM   3426 O OG1 . THR C 1 22  ? -9.685  -0.555  37.457  1.00 49.45  ?  22  THR C OG1 1 
ATOM   3427 C CG2 . THR C 1 22  ? -8.175  -0.511  35.594  1.00 41.75  ?  22  THR C CG2 1 
ATOM   3428 N N   . CYS C 1 23  ? -5.285  -0.680  36.693  1.00 44.71  ?  23  CYS C N   1 
ATOM   3429 C CA  . CYS C 1 23  ? -3.947  -0.244  36.324  1.00 46.63  ?  23  CYS C CA  1 
ATOM   3430 C C   . CYS C 1 23  ? -3.845  -0.388  34.814  1.00 51.26  ?  23  CYS C C   1 
ATOM   3431 O O   . CYS C 1 23  ? -4.054  -1.476  34.277  1.00 59.17  ?  23  CYS C O   1 
ATOM   3432 C CB  . CYS C 1 23  ? -2.891  -1.082  37.069  1.00 48.52  ?  23  CYS C CB  1 
ATOM   3433 S SG  . CYS C 1 23  ? -1.126  -0.814  36.668  1.00 78.34  ?  23  CYS C SG  1 
ATOM   3434 N N   . GLN C 1 24  ? -3.589  0.709   34.118  1.00 48.86  ?  24  GLN C N   1 
ATOM   3435 C CA  . GLN C 1 24  ? -3.549  0.698   32.664  1.00 51.39  ?  24  GLN C CA  1 
ATOM   3436 C C   . GLN C 1 24  ? -2.129  0.931   32.179  1.00 50.05  ?  24  GLN C C   1 
ATOM   3437 O O   . GLN C 1 24  ? -1.443  1.839   32.659  1.00 54.54  ?  24  GLN C O   1 
ATOM   3438 C CB  . GLN C 1 24  ? -4.477  1.753   32.068  1.00 54.79  ?  24  GLN C CB  1 
ATOM   3439 C CG  . GLN C 1 24  ? -4.513  1.673   30.558  1.00 61.02  ?  24  GLN C CG  1 
ATOM   3440 C CD  . GLN C 1 24  ? -5.812  2.159   29.978  1.00 69.20  ?  24  GLN C CD  1 
ATOM   3441 O OE1 . GLN C 1 24  ? -6.748  2.489   30.706  1.00 79.12  ?  24  GLN C OE1 1 
ATOM   3442 N NE2 . GLN C 1 24  ? -5.890  2.182   28.653  1.00 70.11  ?  24  GLN C NE2 1 
ATOM   3443 N N   . ALA C 1 25  ? -1.706  0.125   31.215  1.00 41.57  ?  25  ALA C N   1 
ATOM   3444 C CA  . ALA C 1 25  ? -0.379  0.243   30.641  1.00 47.70  ?  25  ALA C CA  1 
ATOM   3445 C C   . ALA C 1 25  ? -0.396  1.213   29.466  1.00 51.46  ?  25  ALA C C   1 
ATOM   3446 O O   . ALA C 1 25  ? -1.385  1.311   28.736  1.00 52.38  ?  25  ALA C O   1 
ATOM   3447 C CB  . ALA C 1 25  ? 0.130   -1.126  30.192  1.00 50.23  ?  25  ALA C CB  1 
ATOM   3448 N N   . SER C 1 26  ? 0.716   1.941   29.298  1.00 48.33  ?  26  SER C N   1 
ATOM   3449 C CA  . SER C 1 26  ? 0.837   2.867   28.175  1.00 50.30  ?  26  SER C CA  1 
ATOM   3450 C C   . SER C 1 26  ? 0.823   2.136   26.838  1.00 54.39  ?  26  SER C C   1 
ATOM   3451 O O   . SER C 1 26  ? 0.420   2.708   25.819  1.00 50.05  ?  26  SER C O   1 
ATOM   3452 C CB  . SER C 1 26  ? 2.121   3.689   28.302  1.00 51.45  ?  26  SER C CB  1 
ATOM   3453 O OG  . SER C 1 26  ? 3.274   2.862   28.250  1.00 49.78  ?  26  SER C OG  1 
ATOM   3454 N N   . GLN C 1 27  ? 1.260   0.879   26.821  1.00 55.12  ?  27  GLN C N   1 
ATOM   3455 C CA  . GLN C 1 27  ? 1.190   0.041   25.634  1.00 50.95  ?  27  GLN C CA  1 
ATOM   3456 C C   . GLN C 1 27  ? 1.214   -1.411  26.081  1.00 49.68  ?  27  GLN C C   1 
ATOM   3457 O O   . GLN C 1 27  ? 1.378   -1.711  27.266  1.00 46.60  ?  27  GLN C O   1 
ATOM   3458 C CB  . GLN C 1 27  ? 2.319   0.361   24.655  1.00 50.07  ?  27  GLN C CB  1 
ATOM   3459 C CG  . GLN C 1 27  ? 3.704   0.297   25.243  1.00 49.20  ?  27  GLN C CG  1 
ATOM   3460 C CD  . GLN C 1 27  ? 4.738   0.828   24.277  1.00 55.23  ?  27  GLN C CD  1 
ATOM   3461 O OE1 . GLN C 1 27  ? 5.225   1.955   24.425  1.00 57.49  ?  27  GLN C OE1 1 
ATOM   3462 N NE2 . GLN C 1 27  ? 5.067   0.031   23.267  1.00 51.29  ?  27  GLN C NE2 1 
ATOM   3463 N N   . SER C 1 28  ? 1.034   -2.309  25.115  1.00 56.21  ?  28  SER C N   1 
ATOM   3464 C CA  . SER C 1 28  ? 0.886   -3.725  25.426  1.00 54.24  ?  28  SER C CA  1 
ATOM   3465 C C   . SER C 1 28  ? 2.128   -4.263  26.126  1.00 49.09  ?  28  SER C C   1 
ATOM   3466 O O   . SER C 1 28  ? 3.259   -3.988  25.714  1.00 49.91  ?  28  SER C O   1 
ATOM   3467 C CB  . SER C 1 28  ? 0.624   -4.516  24.146  1.00 54.59  ?  28  SER C CB  1 
ATOM   3468 O OG  . SER C 1 28  ? 0.313   -5.867  24.438  1.00 57.21  ?  28  SER C OG  1 
ATOM   3469 N N   . ILE C 1 29  ? 1.907   -5.030  27.193  1.00 44.59  ?  29  ILE C N   1 
ATOM   3470 C CA  . ILE C 1 29  ? 2.988   -5.662  27.938  1.00 46.39  ?  29  ILE C CA  1 
ATOM   3471 C C   . ILE C 1 29  ? 2.680   -7.144  28.100  1.00 51.72  ?  29  ILE C C   1 
ATOM   3472 O O   . ILE C 1 29  ? 3.289   -7.826  28.934  1.00 50.49  ?  29  ILE C O   1 
ATOM   3473 C CB  . ILE C 1 29  ? 3.188   -5.000  29.312  1.00 45.38  ?  29  ILE C CB  1 
ATOM   3474 C CG1 . ILE C 1 29  ? 1.863   -4.944  30.080  1.00 41.55  ?  29  ILE C CG1 1 
ATOM   3475 C CG2 . ILE C 1 29  ? 3.808   -3.613  29.149  1.00 47.17  ?  29  ILE C CG2 1 
ATOM   3476 C CD1 . ILE C 1 29  ? 1.998   -4.553  31.548  1.00 35.76  ?  29  ILE C CD1 1 
ATOM   3477 N N   . SER C 1 30  ? 1.756   -7.652  27.289  1.00 50.09  ?  30  SER C N   1 
ATOM   3478 C CA  . SER C 1 30  ? 1.271   -9.043  27.381  1.00 52.78  ?  30  SER C CA  1 
ATOM   3479 C C   . SER C 1 30  ? 0.725   -9.230  28.798  1.00 49.01  ?  30  SER C C   1 
ATOM   3480 O O   . SER C 1 30  ? 0.025   -8.346  29.316  1.00 46.60  ?  30  SER C O   1 
ATOM   3481 C CB  . SER C 1 30  ? 2.355   -10.025 26.998  1.00 57.03  ?  30  SER C CB  1 
ATOM   3482 O OG  . SER C 1 30  ? 2.815   -9.806  25.680  1.00 63.70  ?  30  SER C OG  1 
ATOM   3483 N N   . ASN C 1 31  ? 1.047   -10.341 29.451  1.00 48.02  ?  31  ASN C N   1 
ATOM   3484 C CA  . ASN C 1 31  ? 0.559   -10.640 30.789  1.00 49.23  ?  31  ASN C CA  1 
ATOM   3485 C C   . ASN C 1 31  ? 1.521   -10.227 31.896  1.00 51.57  ?  31  ASN C C   1 
ATOM   3486 O O   . ASN C 1 31  ? 1.226   -10.481 33.067  1.00 50.35  ?  31  ASN C O   1 
ATOM   3487 C CB  . ASN C 1 31  ? 0.272   -12.140 30.904  1.00 55.63  ?  31  ASN C CB  1 
ATOM   3488 C CG  . ASN C 1 31  ? -0.648  -12.637 29.813  1.00 57.13  ?  31  ASN C CG  1 
ATOM   3489 O OD1 . ASN C 1 31  ? -1.647  -11.994 29.488  1.00 55.45  ?  31  ASN C OD1 1 
ATOM   3490 N ND2 . ASN C 1 31  ? -0.302  -13.773 29.217  1.00 68.35  ?  31  ASN C ND2 1 
ATOM   3491 N N   . GLN C 1 32  ? 2.648   -9.586  31.566  1.00 48.52  ?  32  GLN C N   1 
ATOM   3492 C CA  . GLN C 1 32  ? 3.719   -9.337  32.536  1.00 42.32  ?  32  GLN C CA  1 
ATOM   3493 C C   . GLN C 1 32  ? 3.379   -8.178  33.478  1.00 47.95  ?  32  GLN C C   1 
ATOM   3494 O O   . GLN C 1 32  ? 4.086   -7.172  33.563  1.00 48.86  ?  32  GLN C O   1 
ATOM   3495 C CB  . GLN C 1 32  ? 5.026   -9.082  31.799  1.00 37.97  ?  32  GLN C CB  1 
ATOM   3496 C CG  . GLN C 1 32  ? 5.566   -10.298 31.082  1.00 39.58  ?  32  GLN C CG  1 
ATOM   3497 C CD  . GLN C 1 32  ? 6.837   -10.013 30.303  1.00 43.36  ?  32  GLN C CD  1 
ATOM   3498 O OE1 . GLN C 1 32  ? 7.288   -10.848 29.520  1.00 46.92  ?  32  GLN C OE1 1 
ATOM   3499 N NE2 . GLN C 1 32  ? 7.421   -8.836  30.511  1.00 36.58  ?  32  GLN C NE2 1 
ATOM   3500 N N   . LEU C 1 33  ? 2.292   -8.353  34.232  1.00 42.19  ?  33  LEU C N   1 
ATOM   3501 C CA  . LEU C 1 33  ? 1.892   -7.385  35.244  1.00 40.28  ?  33  LEU C CA  1 
ATOM   3502 C C   . LEU C 1 33  ? 1.637   -8.083  36.567  1.00 39.54  ?  33  LEU C C   1 
ATOM   3503 O O   . LEU C 1 33  ? 0.878   -9.052  36.632  1.00 46.25  ?  33  LEU C O   1 
ATOM   3504 C CB  . LEU C 1 33  ? 0.650   -6.603  34.829  1.00 44.03  ?  33  LEU C CB  1 
ATOM   3505 C CG  . LEU C 1 33  ? 0.323   -5.499  35.837  1.00 43.59  ?  33  LEU C CG  1 
ATOM   3506 C CD1 . LEU C 1 33  ? -0.083  -4.264  35.094  1.00 46.99  ?  33  LEU C CD1 1 
ATOM   3507 C CD2 . LEU C 1 33  ? -0.784  -5.910  36.800  1.00 42.97  ?  33  LEU C CD2 1 
ATOM   3508 N N   . SER C 1 34  ? 2.234   -7.553  37.619  1.00 38.44  ?  34  SER C N   1 
ATOM   3509 C CA  . SER C 1 34  ? 2.144   -8.136  38.942  1.00 39.85  ?  34  SER C CA  1 
ATOM   3510 C C   . SER C 1 34  ? 1.599   -7.109  39.928  1.00 39.97  ?  34  SER C C   1 
ATOM   3511 O O   . SER C 1 34  ? 1.647   -5.905  39.691  1.00 43.07  ?  34  SER C O   1 
ATOM   3512 C CB  . SER C 1 34  ? 3.512   -8.677  39.373  1.00 38.31  ?  34  SER C CB  1 
ATOM   3513 O OG  . SER C 1 34  ? 4.519   -7.696  39.229  1.00 42.41  ?  34  SER C OG  1 
ATOM   3514 N N   . TRP C 1 35  ? 1.036   -7.611  41.018  1.00 40.24  ?  35  TRP C N   1 
ATOM   3515 C CA  . TRP C 1 35  ? 0.412   -6.804  42.055  1.00 39.48  ?  35  TRP C CA  1 
ATOM   3516 C C   . TRP C 1 35  ? 1.089   -7.091  43.386  1.00 41.41  ?  35  TRP C C   1 
ATOM   3517 O O   . TRP C 1 35  ? 1.339   -8.262  43.722  1.00 39.69  ?  35  TRP C O   1 
ATOM   3518 C CB  . TRP C 1 35  ? -1.087  -7.107  42.165  1.00 44.14  ?  35  TRP C CB  1 
ATOM   3519 C CG  . TRP C 1 35  ? -1.898  -6.683  40.984  1.00 42.30  ?  35  TRP C CG  1 
ATOM   3520 C CD1 . TRP C 1 35  ? -2.273  -7.462  39.931  1.00 43.30  ?  35  TRP C CD1 1 
ATOM   3521 C CD2 . TRP C 1 35  ? -2.468  -5.391  40.750  1.00 44.90  ?  35  TRP C CD2 1 
ATOM   3522 N NE1 . TRP C 1 35  ? -3.025  -6.735  39.046  1.00 43.60  ?  35  TRP C NE1 1 
ATOM   3523 C CE2 . TRP C 1 35  ? -3.162  -5.460  39.525  1.00 45.69  ?  35  TRP C CE2 1 
ATOM   3524 C CE3 . TRP C 1 35  ? -2.453  -4.181  41.452  1.00 41.54  ?  35  TRP C CE3 1 
ATOM   3525 C CZ2 . TRP C 1 35  ? -3.837  -4.366  38.986  1.00 43.68  ?  35  TRP C CZ2 1 
ATOM   3526 C CZ3 . TRP C 1 35  ? -3.122  -3.097  40.915  1.00 43.91  ?  35  TRP C CZ3 1 
ATOM   3527 C CH2 . TRP C 1 35  ? -3.807  -3.198  39.695  1.00 46.36  ?  35  TRP C CH2 1 
ATOM   3528 N N   . TYR C 1 36  ? 1.352   -6.012  44.137  1.00 39.32  ?  36  TYR C N   1 
ATOM   3529 C CA  . TYR C 1 36  ? 2.080   -6.037  45.399  1.00 43.40  ?  36  TYR C CA  1 
ATOM   3530 C C   . TYR C 1 36  ? 1.283   -5.320  46.475  1.00 37.37  ?  36  TYR C C   1 
ATOM   3531 O O   . TYR C 1 36  ? 0.591   -4.336  46.202  1.00 42.00  ?  36  TYR C O   1 
ATOM   3532 C CB  . TYR C 1 36  ? 3.460   -5.363  45.278  1.00 35.99  ?  36  TYR C CB  1 
ATOM   3533 C CG  . TYR C 1 36  ? 4.331   -6.011  44.246  1.00 34.95  ?  36  TYR C CG  1 
ATOM   3534 C CD1 . TYR C 1 36  ? 4.207   -5.674  42.907  1.00 36.80  ?  36  TYR C CD1 1 
ATOM   3535 C CD2 . TYR C 1 36  ? 5.252   -6.984  44.601  1.00 33.12  ?  36  TYR C CD2 1 
ATOM   3536 C CE1 . TYR C 1 36  ? 4.982   -6.270  41.952  1.00 36.40  ?  36  TYR C CE1 1 
ATOM   3537 C CE2 . TYR C 1 36  ? 6.032   -7.596  43.649  1.00 35.10  ?  36  TYR C CE2 1 
ATOM   3538 C CZ  . TYR C 1 36  ? 5.892   -7.233  42.322  1.00 38.23  ?  36  TYR C CZ  1 
ATOM   3539 O OH  . TYR C 1 36  ? 6.662   -7.829  41.351  1.00 41.28  ?  36  TYR C OH  1 
ATOM   3540 N N   . GLN C 1 37  ? 1.408   -5.812  47.704  1.00 39.21  ?  37  GLN C N   1 
ATOM   3541 C CA  . GLN C 1 37  ? 0.809   -5.196  48.881  1.00 42.07  ?  37  GLN C CA  1 
ATOM   3542 C C   . GLN C 1 37  ? 1.918   -4.690  49.794  1.00 44.16  ?  37  GLN C C   1 
ATOM   3543 O O   . GLN C 1 37  ? 2.893   -5.409  50.046  1.00 42.09  ?  37  GLN C O   1 
ATOM   3544 C CB  . GLN C 1 37  ? -0.082  -6.190  49.635  1.00 39.60  ?  37  GLN C CB  1 
ATOM   3545 C CG  . GLN C 1 37  ? -0.459  -5.736  51.041  1.00 44.63  ?  37  GLN C CG  1 
ATOM   3546 C CD  . GLN C 1 37  ? -1.107  -6.836  51.868  1.00 48.64  ?  37  GLN C CD  1 
ATOM   3547 O OE1 . GLN C 1 37  ? -0.423  -7.684  52.443  1.00 45.58  ?  37  GLN C OE1 1 
ATOM   3548 N NE2 . GLN C 1 37  ? -2.434  -6.832  51.921  1.00 51.85  ?  37  GLN C NE2 1 
ATOM   3549 N N   . GLN C 1 38  ? 1.783   -3.450  50.266  1.00 44.04  ?  38  GLN C N   1 
ATOM   3550 C CA  . GLN C 1 38  ? 2.732   -2.847  51.194  1.00 47.23  ?  38  GLN C CA  1 
ATOM   3551 C C   . GLN C 1 38  ? 1.980   -2.402  52.441  1.00 42.30  ?  38  GLN C C   1 
ATOM   3552 O O   . GLN C 1 38  ? 1.162   -1.476  52.381  1.00 40.03  ?  38  GLN C O   1 
ATOM   3553 C CB  . GLN C 1 38  ? 3.468   -1.675  50.552  1.00 43.53  ?  38  GLN C CB  1 
ATOM   3554 C CG  . GLN C 1 38  ? 4.587   -1.137  51.416  1.00 44.00  ?  38  GLN C CG  1 
ATOM   3555 C CD  . GLN C 1 38  ? 5.422   -0.108  50.698  1.00 48.11  ?  38  GLN C CD  1 
ATOM   3556 O OE1 . GLN C 1 38  ? 4.896   0.720   49.953  1.00 57.06  ?  38  GLN C OE1 1 
ATOM   3557 N NE2 . GLN C 1 38  ? 6.733   -0.145  50.920  1.00 42.09  ?  38  GLN C NE2 1 
ATOM   3558 N N   . LYS C 1 39  ? 2.241   -3.090  53.553  1.00 43.86  ?  39  LYS C N   1 
ATOM   3559 C CA  . LYS C 1 39  ? 1.738   -2.733  54.865  1.00 45.78  ?  39  LYS C CA  1 
ATOM   3560 C C   . LYS C 1 39  ? 2.632   -1.668  55.487  1.00 51.05  ?  39  LYS C C   1 
ATOM   3561 O O   . LYS C 1 39  ? 3.785   -1.505  55.081  1.00 52.20  ?  39  LYS C O   1 
ATOM   3562 C CB  . LYS C 1 39  ? 1.670   -3.972  55.752  1.00 50.66  ?  39  LYS C CB  1 
ATOM   3563 C CG  . LYS C 1 39  ? 0.732   -5.050  55.233  1.00 49.07  ?  39  LYS C CG  1 
ATOM   3564 C CD  . LYS C 1 39  ? 0.330   -6.011  56.344  1.00 57.67  ?  39  LYS C CD  1 
ATOM   3565 C CE  . LYS C 1 39  ? -0.633  -7.074  55.842  1.00 52.89  ?  39  LYS C CE  1 
ATOM   3566 N NZ  . LYS C 1 39  ? -1.764  -6.458  55.107  1.00 60.54  ?  39  LYS C NZ  1 
ATOM   3567 N N   . PRO C 1 40  ? 2.128   -0.931  56.479  1.00 54.06  ?  40  PRO C N   1 
ATOM   3568 C CA  . PRO C 1 40  ? 2.921   0.155   57.074  1.00 54.37  ?  40  PRO C CA  1 
ATOM   3569 C C   . PRO C 1 40  ? 4.265   -0.320  57.610  1.00 51.66  ?  40  PRO C C   1 
ATOM   3570 O O   . PRO C 1 40  ? 4.347   -1.285  58.373  1.00 50.04  ?  40  PRO C O   1 
ATOM   3571 C CB  . PRO C 1 40  ? 2.018   0.668   58.200  1.00 51.51  ?  40  PRO C CB  1 
ATOM   3572 C CG  . PRO C 1 40  ? 0.650   0.370   57.725  1.00 59.39  ?  40  PRO C CG  1 
ATOM   3573 C CD  . PRO C 1 40  ? 0.745   -0.934  56.986  1.00 53.37  ?  40  PRO C CD  1 
ATOM   3574 N N   . GLY C 1 41  ? 5.324   0.377   57.198  1.00 56.23  ?  41  GLY C N   1 
ATOM   3575 C CA  . GLY C 1 41  ? 6.660   0.087   57.690  1.00 55.31  ?  41  GLY C CA  1 
ATOM   3576 C C   . GLY C 1 41  ? 7.189   -1.279  57.316  1.00 55.97  ?  41  GLY C C   1 
ATOM   3577 O O   . GLY C 1 41  ? 7.946   -1.873  58.089  1.00 61.72  ?  41  GLY C O   1 
ATOM   3578 N N   . LYS C 1 42  ? 6.804   -1.803  56.156  1.00 52.16  ?  42  LYS C N   1 
ATOM   3579 C CA  . LYS C 1 42  ? 7.307   -3.086  55.692  1.00 47.56  ?  42  LYS C CA  1 
ATOM   3580 C C   . LYS C 1 42  ? 7.577   -3.009  54.198  1.00 48.04  ?  42  LYS C C   1 
ATOM   3581 O O   . LYS C 1 42  ? 7.120   -2.096  53.503  1.00 47.75  ?  42  LYS C O   1 
ATOM   3582 C CB  . LYS C 1 42  ? 6.333   -4.228  56.004  1.00 48.24  ?  42  LYS C CB  1 
ATOM   3583 C CG  . LYS C 1 42  ? 6.212   -4.533  57.484  1.00 55.93  ?  42  LYS C CG  1 
ATOM   3584 C CD  . LYS C 1 42  ? 5.284   -5.703  57.737  1.00 65.93  ?  42  LYS C CD  1 
ATOM   3585 C CE  . LYS C 1 42  ? 5.129   -5.969  59.227  1.00 78.38  ?  42  LYS C CE  1 
ATOM   3586 N NZ  . LYS C 1 42  ? 4.085   -6.997  59.503  1.00 86.34  ?  42  LYS C NZ  1 
ATOM   3587 N N   . ALA C 1 43  ? 8.365   -3.959  53.721  1.00 44.67  ?  43  ALA C N   1 
ATOM   3588 C CA  . ALA C 1 43  ? 8.633   -4.063  52.302  1.00 43.91  ?  43  ALA C CA  1 
ATOM   3589 C C   . ALA C 1 43  ? 7.423   -4.663  51.593  1.00 42.38  ?  43  ALA C C   1 
ATOM   3590 O O   . ALA C 1 43  ? 6.609   -5.353  52.211  1.00 42.80  ?  43  ALA C O   1 
ATOM   3591 C CB  . ALA C 1 43  ? 9.873   -4.917  52.066  1.00 42.29  ?  43  ALA C CB  1 
ATOM   3592 N N   . PRO C 1 44  ? 7.270   -4.401  50.298  1.00 38.38  ?  44  PRO C N   1 
ATOM   3593 C CA  . PRO C 1 44  ? 6.131   -4.968  49.567  1.00 43.91  ?  44  PRO C CA  1 
ATOM   3594 C C   . PRO C 1 44  ? 6.180   -6.491  49.506  1.00 46.59  ?  44  PRO C C   1 
ATOM   3595 O O   . PRO C 1 44  ? 7.249   -7.105  49.490  1.00 44.71  ?  44  PRO C O   1 
ATOM   3596 C CB  . PRO C 1 44  ? 6.267   -4.352  48.170  1.00 41.86  ?  44  PRO C CB  1 
ATOM   3597 C CG  . PRO C 1 44  ? 7.082   -3.121  48.374  1.00 41.39  ?  44  PRO C CG  1 
ATOM   3598 C CD  . PRO C 1 44  ? 8.028   -3.436  49.484  1.00 39.36  ?  44  PRO C CD  1 
ATOM   3599 N N   . LYS C 1 45  ? 4.995   -7.097  49.458  1.00 44.00  ?  45  LYS C N   1 
ATOM   3600 C CA  . LYS C 1 45  ? 4.849   -8.539  49.320  1.00 42.39  ?  45  LYS C CA  1 
ATOM   3601 C C   . LYS C 1 45  ? 4.135   -8.836  48.007  1.00 45.54  ?  45  LYS C C   1 
ATOM   3602 O O   . LYS C 1 45  ? 3.130   -8.194  47.683  1.00 47.73  ?  45  LYS C O   1 
ATOM   3603 C CB  . LYS C 1 45  ? 4.077   -9.145  50.500  1.00 41.45  ?  45  LYS C CB  1 
ATOM   3604 C CG  . LYS C 1 45  ? 3.880   -10.646 50.365  1.00 53.14  ?  45  LYS C CG  1 
ATOM   3605 C CD  . LYS C 1 45  ? 2.734   -11.195 51.199  1.00 57.65  ?  45  LYS C CD  1 
ATOM   3606 C CE  . LYS C 1 45  ? 2.556   -12.690 50.907  1.00 72.37  ?  45  LYS C CE  1 
ATOM   3607 N NZ  . LYS C 1 45  ? 1.424   -13.328 51.641  1.00 75.62  ?  45  LYS C NZ  1 
ATOM   3608 N N   . LEU C 1 46  ? 4.662   -9.796  47.248  1.00 43.35  ?  46  LEU C N   1 
ATOM   3609 C CA  . LEU C 1 46  ? 4.058   -10.168 45.975  1.00 40.17  ?  46  LEU C CA  1 
ATOM   3610 C C   . LEU C 1 46  ? 2.716   -10.851 46.195  1.00 44.70  ?  46  LEU C C   1 
ATOM   3611 O O   . LEU C 1 46  ? 2.618   -11.826 46.942  1.00 50.54  ?  46  LEU C O   1 
ATOM   3612 C CB  . LEU C 1 46  ? 4.994   -11.085 45.191  1.00 40.76  ?  46  LEU C CB  1 
ATOM   3613 C CG  . LEU C 1 46  ? 4.449   -11.682 43.893  1.00 42.84  ?  46  LEU C CG  1 
ATOM   3614 C CD1 . LEU C 1 46  ? 4.212   -10.606 42.845  1.00 38.33  ?  46  LEU C CD1 1 
ATOM   3615 C CD2 . LEU C 1 46  ? 5.415   -12.732 43.369  1.00 42.69  ?  46  LEU C CD2 1 
ATOM   3616 N N   . LEU C 1 47  ? 1.673   -10.320 45.560  1.00 47.70  ?  47  LEU C N   1 
ATOM   3617 C CA  . LEU C 1 47  ? 0.347   -10.927 45.592  1.00 47.83  ?  47  LEU C CA  1 
ATOM   3618 C C   . LEU C 1 47  ? 0.042   -11.710 44.327  1.00 47.07  ?  47  LEU C C   1 
ATOM   3619 O O   . LEU C 1 47  ? -0.385  -12.865 44.402  1.00 48.44  ?  47  LEU C O   1 
ATOM   3620 C CB  . LEU C 1 47  ? -0.740  -9.860  45.776  1.00 46.16  ?  47  LEU C CB  1 
ATOM   3621 C CG  . LEU C 1 47  ? -0.834  -9.097  47.088  1.00 43.57  ?  47  LEU C CG  1 
ATOM   3622 C CD1 . LEU C 1 47  ? -1.840  -7.990  46.927  1.00 40.47  ?  47  LEU C CD1 1 
ATOM   3623 C CD2 . LEU C 1 47  ? -1.255  -10.053 48.183  1.00 43.03  ?  47  LEU C CD2 1 
ATOM   3624 N N   . ILE C 1 48  ? 0.241   -11.099 43.163  1.00 45.30  ?  48  ILE C N   1 
ATOM   3625 C CA  . ILE C 1 48  ? -0.222  -11.693 41.912  1.00 41.08  ?  48  ILE C CA  1 
ATOM   3626 C C   . ILE C 1 48  ? 0.845   -11.488 40.852  1.00 45.34  ?  48  ILE C C   1 
ATOM   3627 O O   . ILE C 1 48  ? 1.461   -10.422 40.787  1.00 50.30  ?  48  ILE C O   1 
ATOM   3628 C CB  . ILE C 1 48  ? -1.572  -11.081 41.470  1.00 41.35  ?  48  ILE C CB  1 
ATOM   3629 C CG1 . ILE C 1 48  ? -2.685  -11.510 42.428  1.00 41.74  ?  48  ILE C CG1 1 
ATOM   3630 C CG2 . ILE C 1 48  ? -1.923  -11.483 40.044  1.00 40.71  ?  48  ILE C CG2 1 
ATOM   3631 C CD1 . ILE C 1 48  ? -4.047  -11.085 41.998  1.00 42.12  ?  48  ILE C CD1 1 
ATOM   3632 N N   . TYR C 1 49  ? 1.074   -12.504 40.026  1.00 45.40  ?  49  TYR C N   1 
ATOM   3633 C CA  . TYR C 1 49  ? 2.034   -12.397 38.939  1.00 42.80  ?  49  TYR C CA  1 
ATOM   3634 C C   . TYR C 1 49  ? 1.409   -12.928 37.658  1.00 49.26  ?  49  TYR C C   1 
ATOM   3635 O O   . TYR C 1 49  ? 0.474   -13.737 37.683  1.00 45.92  ?  49  TYR C O   1 
ATOM   3636 C CB  . TYR C 1 49  ? 3.332   -13.147 39.257  1.00 38.88  ?  49  TYR C CB  1 
ATOM   3637 C CG  . TYR C 1 49  ? 3.158   -14.642 39.343  1.00 47.69  ?  49  TYR C CG  1 
ATOM   3638 C CD1 . TYR C 1 49  ? 2.738   -15.236 40.521  1.00 45.90  ?  49  TYR C CD1 1 
ATOM   3639 C CD2 . TYR C 1 49  ? 3.429   -15.461 38.252  1.00 44.23  ?  49  TYR C CD2 1 
ATOM   3640 C CE1 . TYR C 1 49  ? 2.573   -16.601 40.610  1.00 53.22  ?  49  TYR C CE1 1 
ATOM   3641 C CE2 . TYR C 1 49  ? 3.271   -16.830 38.333  1.00 49.11  ?  49  TYR C CE2 1 
ATOM   3642 C CZ  . TYR C 1 49  ? 2.843   -17.396 39.516  1.00 52.96  ?  49  TYR C CZ  1 
ATOM   3643 O OH  . TYR C 1 49  ? 2.678   -18.760 39.611  1.00 47.03  ?  49  TYR C OH  1 
ATOM   3644 N N   . ASP C 1 50  ? 1.948   -12.450 36.536  1.00 44.01  ?  50  ASP C N   1 
ATOM   3645 C CA  . ASP C 1 50  ? 1.435   -12.766 35.203  1.00 47.25  ?  50  ASP C CA  1 
ATOM   3646 C C   . ASP C 1 50  ? -0.058  -12.461 35.114  1.00 51.70  ?  50  ASP C C   1 
ATOM   3647 O O   . ASP C 1 50  ? -0.838  -13.225 34.540  1.00 50.67  ?  50  ASP C O   1 
ATOM   3648 C CB  . ASP C 1 50  ? 1.737   -14.210 34.805  1.00 55.78  ?  50  ASP C CB  1 
ATOM   3649 C CG  . ASP C 1 50  ? 1.916   -14.369 33.300  1.00 62.04  ?  50  ASP C CG  1 
ATOM   3650 O OD1 . ASP C 1 50  ? 1.265   -15.253 32.699  1.00 61.54  ?  50  ASP C OD1 1 
ATOM   3651 O OD2 . ASP C 1 50  ? 2.701   -13.590 32.713  1.00 64.17  ?  50  ASP C OD2 1 
ATOM   3652 N N   . ALA C 1 51  ? -0.450  -11.348 35.741  1.00 46.78  ?  51  ALA C N   1 
ATOM   3653 C CA  . ALA C 1 51  ? -1.792  -10.771 35.704  1.00 44.53  ?  51  ALA C CA  1 
ATOM   3654 C C   . ALA C 1 51  ? -2.735  -11.542 36.621  1.00 46.03  ?  51  ALA C C   1 
ATOM   3655 O O   . ALA C 1 51  ? -3.393  -10.936 37.470  1.00 49.12  ?  51  ALA C O   1 
ATOM   3656 C CB  . ALA C 1 51  ? -2.287  -10.645 34.259  1.00 48.60  ?  51  ALA C CB  1 
ATOM   3657 N N   . SER C 1 52  ? -2.821  -12.864 36.486  1.00 45.33  ?  52  SER C N   1 
ATOM   3658 C CA  . SER C 1 52  ? -3.840  -13.582 37.240  1.00 49.95  ?  52  SER C CA  1 
ATOM   3659 C C   . SER C 1 52  ? -3.406  -14.720 38.150  1.00 43.29  ?  52  SER C C   1 
ATOM   3660 O O   . SER C 1 52  ? -4.274  -15.342 38.765  1.00 42.35  ?  52  SER C O   1 
ATOM   3661 C CB  . SER C 1 52  ? -4.804  -14.132 36.177  1.00 44.07  ?  52  SER C CB  1 
ATOM   3662 O OG  . SER C 1 52  ? -4.100  -14.909 35.229  1.00 56.63  ?  52  SER C OG  1 
ATOM   3663 N N   . SER C 1 53  ? -2.118  -15.015 38.264  1.00 44.02  ?  53  SER C N   1 
ATOM   3664 C CA  . SER C 1 53  ? -1.661  -16.158 39.046  1.00 46.95  ?  53  SER C CA  1 
ATOM   3665 C C   . SER C 1 53  ? -1.340  -15.723 40.474  1.00 45.49  ?  53  SER C C   1 
ATOM   3666 O O   . SER C 1 53  ? -0.502  -14.839 40.689  1.00 48.11  ?  53  SER C O   1 
ATOM   3667 C CB  . SER C 1 53  ? -0.440  -16.808 38.396  1.00 47.23  ?  53  SER C CB  1 
ATOM   3668 O OG  . SER C 1 53  ? -0.704  -17.122 37.039  1.00 49.05  ?  53  SER C OG  1 
ATOM   3669 N N   . LEU C 1 54  ? -1.995  -16.356 41.442  1.00 48.00  ?  54  LEU C N   1 
ATOM   3670 C CA  . LEU C 1 54  ? -1.758  -16.055 42.847  1.00 48.68  ?  54  LEU C CA  1 
ATOM   3671 C C   . LEU C 1 54  ? -0.376  -16.525 43.279  1.00 50.24  ?  54  LEU C C   1 
ATOM   3672 O O   . LEU C 1 54  ? 0.067   -17.620 42.923  1.00 51.97  ?  54  LEU C O   1 
ATOM   3673 C CB  . LEU C 1 54  ? -2.814  -16.729 43.722  1.00 50.89  ?  54  LEU C CB  1 
ATOM   3674 C CG  . LEU C 1 54  ? -4.114  -15.986 44.003  1.00 49.56  ?  54  LEU C CG  1 
ATOM   3675 C CD1 . LEU C 1 54  ? -5.007  -16.803 44.925  1.00 55.71  ?  54  LEU C CD1 1 
ATOM   3676 C CD2 . LEU C 1 54  ? -3.805  -14.639 44.619  1.00 58.48  ?  54  LEU C CD2 1 
ATOM   3677 N N   . ALA C 1 55  ? 0.311   -15.684 44.045  1.00 55.10  ?  55  ALA C N   1 
ATOM   3678 C CA  . ALA C 1 55  ? 1.582   -16.076 44.625  1.00 50.27  ?  55  ALA C CA  1 
ATOM   3679 C C   . ALA C 1 55  ? 1.353   -16.974 45.836  1.00 55.46  ?  55  ALA C C   1 
ATOM   3680 O O   . ALA C 1 55  ? 0.254   -17.046 46.394  1.00 53.41  ?  55  ALA C O   1 
ATOM   3681 C CB  . ALA C 1 55  ? 2.401   -14.849 45.015  1.00 45.15  ?  55  ALA C CB  1 
ATOM   3682 N N   . SER C 1 56  ? 2.420   -17.657 46.241  1.00 53.44  ?  56  SER C N   1 
ATOM   3683 C CA  . SER C 1 56  ? 2.334   -18.628 47.322  1.00 53.67  ?  56  SER C CA  1 
ATOM   3684 C C   . SER C 1 56  ? 1.981   -17.945 48.639  1.00 56.62  ?  56  SER C C   1 
ATOM   3685 O O   . SER C 1 56  ? 2.630   -16.975 49.044  1.00 55.64  ?  56  SER C O   1 
ATOM   3686 C CB  . SER C 1 56  ? 3.660   -19.372 47.446  1.00 59.00  ?  56  SER C CB  1 
ATOM   3687 O OG  . SER C 1 56  ? 4.125   -19.775 46.168  1.00 67.45  ?  56  SER C OG  1 
ATOM   3688 N N   . GLY C 1 57  ? 0.954   -18.459 49.313  1.00 52.71  ?  57  GLY C N   1 
ATOM   3689 C CA  . GLY C 1 57  ? 0.574   -17.926 50.607  1.00 55.38  ?  57  GLY C CA  1 
ATOM   3690 C C   . GLY C 1 57  ? -0.306  -16.700 50.564  1.00 62.98  ?  57  GLY C C   1 
ATOM   3691 O O   . GLY C 1 57  ? -0.337  -15.938 51.536  1.00 67.58  ?  57  GLY C O   1 
ATOM   3692 N N   . VAL C 1 58  ? -1.014  -16.478 49.465  1.00 55.35  ?  58  VAL C N   1 
ATOM   3693 C CA  . VAL C 1 58  ? -1.898  -15.331 49.291  1.00 52.54  ?  58  VAL C CA  1 
ATOM   3694 C C   . VAL C 1 58  ? -3.335  -15.836 49.345  1.00 54.20  ?  58  VAL C C   1 
ATOM   3695 O O   . VAL C 1 58  ? -3.699  -16.721 48.560  1.00 55.64  ?  58  VAL C O   1 
ATOM   3696 C CB  . VAL C 1 58  ? -1.621  -14.604 47.967  1.00 55.91  ?  58  VAL C CB  1 
ATOM   3697 C CG1 . VAL C 1 58  ? -2.559  -13.424 47.812  1.00 54.38  ?  58  VAL C CG1 1 
ATOM   3698 C CG2 . VAL C 1 58  ? -0.168  -14.157 47.900  1.00 53.92  ?  58  VAL C CG2 1 
ATOM   3699 N N   . PRO C 1 59  ? -4.178  -15.310 50.236  1.00 54.11  ?  59  PRO C N   1 
ATOM   3700 C CA  . PRO C 1 59  ? -5.563  -15.792 50.323  1.00 55.02  ?  59  PRO C CA  1 
ATOM   3701 C C   . PRO C 1 59  ? -6.311  -15.674 48.999  1.00 58.87  ?  59  PRO C C   1 
ATOM   3702 O O   . PRO C 1 59  ? -5.996  -14.838 48.147  1.00 59.67  ?  59  PRO C O   1 
ATOM   3703 C CB  . PRO C 1 59  ? -6.185  -14.898 51.406  1.00 62.52  ?  59  PRO C CB  1 
ATOM   3704 C CG  . PRO C 1 59  ? -5.225  -13.747 51.588  1.00 52.55  ?  59  PRO C CG  1 
ATOM   3705 C CD  . PRO C 1 59  ? -3.877  -14.302 51.264  1.00 55.50  ?  59  PRO C CD  1 
ATOM   3706 N N   . SER C 1 60  ? -7.318  -16.536 48.838  1.00 57.04  ?  60  SER C N   1 
ATOM   3707 C CA  . SER C 1 60  ? -8.038  -16.672 47.576  1.00 54.50  ?  60  SER C CA  1 
ATOM   3708 C C   . SER C 1 60  ? -8.935  -15.483 47.250  1.00 51.20  ?  60  SER C C   1 
ATOM   3709 O O   . SER C 1 60  ? -9.453  -15.414 46.130  1.00 50.23  ?  60  SER C O   1 
ATOM   3710 C CB  . SER C 1 60  ? -8.880  -17.946 47.603  1.00 52.84  ?  60  SER C CB  1 
ATOM   3711 O OG  . SER C 1 60  ? -9.695  -17.974 48.762  1.00 55.41  ?  60  SER C OG  1 
ATOM   3712 N N   . ARG C 1 61  ? -9.128  -14.546 48.177  1.00 50.18  ?  61  ARG C N   1 
ATOM   3713 C CA  . ARG C 1 61  ? -9.951  -13.379 47.874  1.00 53.14  ?  61  ARG C CA  1 
ATOM   3714 C C   . ARG C 1 61  ? -9.250  -12.373 46.973  1.00 51.32  ?  61  ARG C C   1 
ATOM   3715 O O   . ARG C 1 61  ? -9.898  -11.436 46.496  1.00 52.51  ?  61  ARG C O   1 
ATOM   3716 C CB  . ARG C 1 61  ? -10.426 -12.731 49.172  1.00 54.72  ?  61  ARG C CB  1 
ATOM   3717 C CG  . ARG C 1 61  ? -9.349  -12.479 50.191  1.00 58.40  ?  61  ARG C CG  1 
ATOM   3718 C CD  . ARG C 1 61  ? -9.995  -11.992 51.470  1.00 62.91  ?  61  ARG C CD  1 
ATOM   3719 N NE  . ARG C 1 61  ? -9.084  -12.023 52.607  1.00 61.94  ?  61  ARG C NE  1 
ATOM   3720 C CZ  . ARG C 1 61  ? -8.202  -11.072 52.869  1.00 62.52  ?  61  ARG C CZ  1 
ATOM   3721 N NH1 . ARG C 1 61  ? -8.120  -10.027 52.062  1.00 69.21  ?  61  ARG C NH1 1 
ATOM   3722 N NH2 . ARG C 1 61  ? -7.408  -11.163 53.928  1.00 57.24  ?  61  ARG C NH2 1 
ATOM   3723 N N   . PHE C 1 62  ? -7.957  -12.538 46.728  1.00 48.47  ?  62  PHE C N   1 
ATOM   3724 C CA  . PHE C 1 62  ? -7.247  -11.709 45.771  1.00 48.14  ?  62  PHE C CA  1 
ATOM   3725 C C   . PHE C 1 62  ? -7.304  -12.372 44.403  1.00 46.03  ?  62  PHE C C   1 
ATOM   3726 O O   . PHE C 1 62  ? -7.077  -13.580 44.280  1.00 49.05  ?  62  PHE C O   1 
ATOM   3727 C CB  . PHE C 1 62  ? -5.797  -11.495 46.207  1.00 45.73  ?  62  PHE C CB  1 
ATOM   3728 C CG  . PHE C 1 62  ? -5.661  -10.697 47.469  1.00 44.82  ?  62  PHE C CG  1 
ATOM   3729 C CD1 . PHE C 1 62  ? -5.604  -9.318  47.429  1.00 43.36  ?  62  PHE C CD1 1 
ATOM   3730 C CD2 . PHE C 1 62  ? -5.618  -11.328 48.703  1.00 53.56  ?  62  PHE C CD2 1 
ATOM   3731 C CE1 . PHE C 1 62  ? -5.487  -8.582  48.596  1.00 47.69  ?  62  PHE C CE1 1 
ATOM   3732 C CE2 . PHE C 1 62  ? -5.503  -10.596 49.872  1.00 47.75  ?  62  PHE C CE2 1 
ATOM   3733 C CZ  . PHE C 1 62  ? -5.440  -9.223  49.816  1.00 45.31  ?  62  PHE C CZ  1 
ATOM   3734 N N   . SER C 1 63  ? -7.631  -11.584 43.384  1.00 41.88  ?  63  SER C N   1 
ATOM   3735 C CA  . SER C 1 63  ? -7.653  -12.088 42.020  1.00 37.83  ?  63  SER C CA  1 
ATOM   3736 C C   . SER C 1 63  ? -7.269  -10.962 41.072  1.00 40.09  ?  63  SER C C   1 
ATOM   3737 O O   . SER C 1 63  ? -7.347  -9.780  41.413  1.00 42.41  ?  63  SER C O   1 
ATOM   3738 C CB  . SER C 1 63  ? -9.023  -12.687 41.665  1.00 40.26  ?  63  SER C CB  1 
ATOM   3739 O OG  . SER C 1 63  ? -10.088 -11.819 42.025  1.00 47.12  ?  63  SER C OG  1 
ATOM   3740 N N   . GLY C 1 64  ? -6.821  -11.342 39.888  1.00 41.45  ?  64  GLY C N   1 
ATOM   3741 C CA  . GLY C 1 64  ? -6.375  -10.374 38.905  1.00 44.14  ?  64  GLY C CA  1 
ATOM   3742 C C   . GLY C 1 64  ? -6.860  -10.753 37.524  1.00 48.42  ?  64  GLY C C   1 
ATOM   3743 O O   . GLY C 1 64  ? -6.965  -11.932 37.178  1.00 50.18  ?  64  GLY C O   1 
ATOM   3744 N N   . SER C 1 65  ? -7.131  -9.731  36.721  1.00 49.88  ?  65  SER C N   1 
ATOM   3745 C CA  . SER C 1 65  ? -7.690  -9.945  35.396  1.00 47.54  ?  65  SER C CA  1 
ATOM   3746 C C   . SER C 1 65  ? -7.084  -8.957  34.413  1.00 48.65  ?  65  SER C C   1 
ATOM   3747 O O   . SER C 1 65  ? -6.651  -7.866  34.792  1.00 46.90  ?  65  SER C O   1 
ATOM   3748 C CB  . SER C 1 65  ? -9.213  -9.810  35.391  1.00 49.66  ?  65  SER C CB  1 
ATOM   3749 O OG  . SER C 1 65  ? -9.685  -9.667  34.062  1.00 58.84  ?  65  SER C OG  1 
ATOM   3750 N N   . ARG C 1 66  ? -7.055  -9.363  33.144  1.00 52.12  ?  66  ARG C N   1 
ATOM   3751 C CA  . ARG C 1 66  ? -6.517  -8.565  32.052  1.00 47.24  ?  66  ARG C CA  1 
ATOM   3752 C C   . ARG C 1 66  ? -7.580  -8.361  30.980  1.00 48.71  ?  66  ARG C C   1 
ATOM   3753 O O   . ARG C 1 66  ? -8.429  -9.225  30.743  1.00 50.08  ?  66  ARG C O   1 
ATOM   3754 C CB  . ARG C 1 66  ? -5.276  -9.232  31.434  1.00 38.17  ?  66  ARG C CB  1 
ATOM   3755 C CG  . ARG C 1 66  ? -4.666  -8.484  30.260  1.00 44.70  ?  66  ARG C CG  1 
ATOM   3756 C CD  . ARG C 1 66  ? -3.692  -9.349  29.465  1.00 45.67  ?  66  ARG C CD  1 
ATOM   3757 N NE  . ARG C 1 66  ? -3.300  -8.695  28.219  1.00 42.50  ?  66  ARG C NE  1 
ATOM   3758 C CZ  . ARG C 1 66  ? -2.562  -9.257  27.266  1.00 43.57  ?  66  ARG C CZ  1 
ATOM   3759 N NH1 . ARG C 1 66  ? -2.263  -8.571  26.174  1.00 49.08  ?  66  ARG C NH1 1 
ATOM   3760 N NH2 . ARG C 1 66  ? -2.116  -10.496 27.403  1.00 50.05  ?  66  ARG C NH2 1 
ATOM   3761 N N   . SER C 1 67  ? -7.508  -7.205  30.326  1.00 51.53  ?  67  SER C N   1 
ATOM   3762 C CA  . SER C 1 67  ? -8.345  -6.862  29.180  1.00 43.11  ?  67  SER C CA  1 
ATOM   3763 C C   . SER C 1 67  ? -7.527  -5.857  28.370  1.00 45.88  ?  67  SER C C   1 
ATOM   3764 O O   . SER C 1 67  ? -7.534  -4.657  28.653  1.00 56.56  ?  67  SER C O   1 
ATOM   3765 C CB  . SER C 1 67  ? -9.686  -6.290  29.617  1.00 47.81  ?  67  SER C CB  1 
ATOM   3766 O OG  . SER C 1 67  ? -10.496 -5.971  28.500  1.00 59.61  ?  67  SER C OG  1 
ATOM   3767 N N   . GLY C 1 68  ? -6.797  -6.373  27.384  1.00 45.26  ?  68  GLY C N   1 
ATOM   3768 C CA  . GLY C 1 68  ? -5.897  -5.555  26.596  1.00 51.91  ?  68  GLY C CA  1 
ATOM   3769 C C   . GLY C 1 68  ? -4.753  -4.982  27.411  1.00 54.89  ?  68  GLY C C   1 
ATOM   3770 O O   . GLY C 1 68  ? -3.853  -5.714  27.839  1.00 52.17  ?  68  GLY C O   1 
ATOM   3771 N N   . THR C 1 69  ? -4.783  -3.666  27.628  1.00 54.38  ?  69  THR C N   1 
ATOM   3772 C CA  . THR C 1 69  ? -3.813  -2.977  28.468  1.00 49.23  ?  69  THR C CA  1 
ATOM   3773 C C   . THR C 1 69  ? -4.402  -2.558  29.808  1.00 52.35  ?  69  THR C C   1 
ATOM   3774 O O   . THR C 1 69  ? -3.746  -1.824  30.557  1.00 52.85  ?  69  THR C O   1 
ATOM   3775 C CB  . THR C 1 69  ? -3.239  -1.752  27.746  1.00 49.38  ?  69  THR C CB  1 
ATOM   3776 O OG1 . THR C 1 69  ? -4.282  -0.797  27.497  1.00 53.60  ?  69  THR C OG1 1 
ATOM   3777 C CG2 . THR C 1 69  ? -2.579  -2.150  26.429  1.00 46.25  ?  69  THR C CG2 1 
ATOM   3778 N N   . LYS C 1 70  ? -5.622  -2.995  30.128  1.00 52.16  ?  70  LYS C N   1 
ATOM   3779 C CA  . LYS C 1 70  ? -6.246  -2.703  31.414  1.00 52.56  ?  70  LYS C CA  1 
ATOM   3780 C C   . LYS C 1 70  ? -6.154  -3.938  32.302  1.00 51.65  ?  70  LYS C C   1 
ATOM   3781 O O   . LYS C 1 70  ? -6.601  -5.020  31.916  1.00 49.51  ?  70  LYS C O   1 
ATOM   3782 C CB  . LYS C 1 70  ? -7.704  -2.268  31.253  1.00 49.40  ?  70  LYS C CB  1 
ATOM   3783 C CG  . LYS C 1 70  ? -7.902  -1.051  30.360  1.00 63.63  ?  70  LYS C CG  1 
ATOM   3784 C CD  . LYS C 1 70  ? -9.286  -0.440  30.552  1.00 72.99  ?  70  LYS C CD  1 
ATOM   3785 C CE  . LYS C 1 70  ? -9.437  0.165   31.947  1.00 69.90  ?  70  LYS C CE  1 
ATOM   3786 N NZ  . LYS C 1 70  ? -10.706 0.941   32.100  1.00 77.84  ?  70  LYS C NZ  1 
ATOM   3787 N N   . PHE C 1 71  ? -5.558  -3.780  33.477  1.00 49.83  ?  71  PHE C N   1 
ATOM   3788 C CA  . PHE C 1 71  ? -5.433  -4.847  34.451  1.00 41.26  ?  71  PHE C CA  1 
ATOM   3789 C C   . PHE C 1 71  ? -6.207  -4.449  35.694  1.00 43.62  ?  71  PHE C C   1 
ATOM   3790 O O   . PHE C 1 71  ? -6.300  -3.269  36.035  1.00 49.47  ?  71  PHE C O   1 
ATOM   3791 C CB  . PHE C 1 71  ? -3.965  -5.113  34.794  1.00 42.12  ?  71  PHE C CB  1 
ATOM   3792 C CG  . PHE C 1 71  ? -3.147  -5.562  33.619  1.00 45.62  ?  71  PHE C CG  1 
ATOM   3793 C CD1 . PHE C 1 71  ? -2.731  -4.657  32.660  1.00 43.68  ?  71  PHE C CD1 1 
ATOM   3794 C CD2 . PHE C 1 71  ? -2.803  -6.893  33.467  1.00 46.90  ?  71  PHE C CD2 1 
ATOM   3795 C CE1 . PHE C 1 71  ? -1.986  -5.071  31.574  1.00 44.42  ?  71  PHE C CE1 1 
ATOM   3796 C CE2 . PHE C 1 71  ? -2.056  -7.311  32.381  1.00 43.83  ?  71  PHE C CE2 1 
ATOM   3797 C CZ  . PHE C 1 71  ? -1.649  -6.399  31.435  1.00 40.22  ?  71  PHE C CZ  1 
ATOM   3798 N N   . THR C 1 72  ? -6.774  -5.436  36.368  1.00 43.88  ?  72  THR C N   1 
ATOM   3799 C CA  . THR C 1 72  ? -7.594  -5.145  37.530  1.00 43.65  ?  72  THR C CA  1 
ATOM   3800 C C   . THR C 1 72  ? -7.259  -6.124  38.642  1.00 46.75  ?  72  THR C C   1 
ATOM   3801 O O   . THR C 1 72  ? -7.215  -7.338  38.418  1.00 52.84  ?  72  THR C O   1 
ATOM   3802 C CB  . THR C 1 72  ? -9.087  -5.187  37.177  1.00 45.46  ?  72  THR C CB  1 
ATOM   3803 O OG1 . THR C 1 72  ? -9.867  -5.221  38.379  1.00 48.15  ?  72  THR C OG1 1 
ATOM   3804 C CG2 . THR C 1 72  ? -9.406  -6.394  36.311  1.00 48.57  ?  72  THR C CG2 1 
ATOM   3805 N N   . LEU C 1 73  ? -6.991  -5.578  39.823  1.00 44.27  ?  73  LEU C N   1 
ATOM   3806 C CA  . LEU C 1 73  ? -6.847  -6.344  41.050  1.00 42.27  ?  73  LEU C CA  1 
ATOM   3807 C C   . LEU C 1 73  ? -8.141  -6.242  41.836  1.00 45.72  ?  73  LEU C C   1 
ATOM   3808 O O   . LEU C 1 73  ? -8.673  -5.143  42.014  1.00 48.80  ?  73  LEU C O   1 
ATOM   3809 C CB  . LEU C 1 73  ? -5.691  -5.812  41.892  1.00 44.53  ?  73  LEU C CB  1 
ATOM   3810 C CG  . LEU C 1 73  ? -5.627  -6.357  43.319  1.00 44.69  ?  73  LEU C CG  1 
ATOM   3811 C CD1 . LEU C 1 73  ? -5.221  -7.824  43.312  1.00 46.05  ?  73  LEU C CD1 1 
ATOM   3812 C CD2 . LEU C 1 73  ? -4.685  -5.529  44.177  1.00 39.30  ?  73  LEU C CD2 1 
ATOM   3813 N N   . THR C 1 74  ? -8.642  -7.382  42.308  1.00 50.15  ?  74  THR C N   1 
ATOM   3814 C CA  . THR C 1 74  ? -9.924  -7.446  42.996  1.00 45.03  ?  74  THR C CA  1 
ATOM   3815 C C   . THR C 1 74  ? -9.749  -8.168  44.318  1.00 48.44  ?  74  THR C C   1 
ATOM   3816 O O   . THR C 1 74  ? -9.129  -9.239  44.375  1.00 50.17  ?  74  THR C O   1 
ATOM   3817 C CB  . THR C 1 74  ? -10.996 -8.169  42.169  1.00 45.50  ?  74  THR C CB  1 
ATOM   3818 O OG1 . THR C 1 74  ? -11.169 -7.512  40.908  1.00 51.72  ?  74  THR C OG1 1 
ATOM   3819 C CG2 . THR C 1 74  ? -12.330 -8.169  42.922  1.00 48.69  ?  74  THR C CG2 1 
ATOM   3820 N N   . ILE C 1 75  ? -10.271 -7.561  45.377  1.00 48.04  ?  75  ILE C N   1 
ATOM   3821 C CA  . ILE C 1 75  ? -10.414 -8.200  46.676  1.00 48.72  ?  75  ILE C CA  1 
ATOM   3822 C C   . ILE C 1 75  ? -11.902 -8.473  46.858  1.00 54.95  ?  75  ILE C C   1 
ATOM   3823 O O   . ILE C 1 75  ? -12.714 -7.539  46.846  1.00 56.68  ?  75  ILE C O   1 
ATOM   3824 C CB  . ILE C 1 75  ? -9.856  -7.321  47.801  1.00 49.16  ?  75  ILE C CB  1 
ATOM   3825 C CG1 . ILE C 1 75  ? -8.499  -6.759  47.387  1.00 48.10  ?  75  ILE C CG1 1 
ATOM   3826 C CG2 . ILE C 1 75  ? -9.715  -8.116  49.080  1.00 50.45  ?  75  ILE C CG2 1 
ATOM   3827 C CD1 . ILE C 1 75  ? -7.901  -5.832  48.401  1.00 44.71  ?  75  ILE C CD1 1 
ATOM   3828 N N   . SER C 1 76  ? -12.265 -9.751  46.998  1.00 57.98  ?  76  SER C N   1 
ATOM   3829 C CA  . SER C 1 76  ? -13.674 -10.133 46.980  1.00 57.39  ?  76  SER C CA  1 
ATOM   3830 C C   . SER C 1 76  ? -14.374 -9.836  48.304  1.00 61.06  ?  76  SER C C   1 
ATOM   3831 O O   . SER C 1 76  ? -15.510 -9.348  48.307  1.00 60.00  ?  76  SER C O   1 
ATOM   3832 C CB  . SER C 1 76  ? -13.811 -11.614 46.621  1.00 56.07  ?  76  SER C CB  1 
ATOM   3833 O OG  . SER C 1 76  ? -13.186 -12.446 47.582  1.00 57.21  ?  76  SER C OG  1 
ATOM   3834 N N   . SER C 1 77  ? -13.731 -10.133 49.434  1.00 61.32  ?  77  SER C N   1 
ATOM   3835 C CA  . SER C 1 77  ? -14.309 -9.879  50.755  1.00 62.50  ?  77  SER C CA  1 
ATOM   3836 C C   . SER C 1 77  ? -13.254 -9.184  51.616  1.00 61.76  ?  77  SER C C   1 
ATOM   3837 O O   . SER C 1 77  ? -12.387 -9.844  52.195  1.00 63.97  ?  77  SER C O   1 
ATOM   3838 C CB  . SER C 1 77  ? -14.797 -11.178 51.394  1.00 59.32  ?  77  SER C CB  1 
ATOM   3839 O OG  . SER C 1 77  ? -15.220 -10.969 52.728  1.00 63.70  ?  77  SER C OG  1 
ATOM   3840 N N   . LEU C 1 78  ? -13.353 -7.856  51.716  1.00 60.88  ?  78  LEU C N   1 
ATOM   3841 C CA  . LEU C 1 78  ? -12.337 -7.045  52.384  1.00 58.56  ?  78  LEU C CA  1 
ATOM   3842 C C   . LEU C 1 78  ? -12.267 -7.339  53.880  1.00 61.28  ?  78  LEU C C   1 
ATOM   3843 O O   . LEU C 1 78  ? -13.295 -7.411  54.561  1.00 57.24  ?  78  LEU C O   1 
ATOM   3844 C CB  . LEU C 1 78  ? -12.628 -5.562  52.157  1.00 60.99  ?  78  LEU C CB  1 
ATOM   3845 C CG  . LEU C 1 78  ? -11.614 -4.525  52.648  1.00 62.79  ?  78  LEU C CG  1 
ATOM   3846 C CD1 . LEU C 1 78  ? -10.306 -4.613  51.875  1.00 56.40  ?  78  LEU C CD1 1 
ATOM   3847 C CD2 . LEU C 1 78  ? -12.212 -3.130  52.540  1.00 57.95  ?  78  LEU C CD2 1 
ATOM   3848 N N   . GLN C 1 79  ? -11.044 -7.502  54.389  1.00 57.42  ?  79  GLN C N   1 
ATOM   3849 C CA  . GLN C 1 79  ? -10.762 -7.794  55.787  1.00 56.22  ?  79  GLN C CA  1 
ATOM   3850 C C   . GLN C 1 79  ? -9.999  -6.646  56.445  1.00 59.94  ?  79  GLN C C   1 
ATOM   3851 O O   . GLN C 1 79  ? -9.314  -5.871  55.768  1.00 53.68  ?  79  GLN C O   1 
ATOM   3852 C CB  . GLN C 1 79  ? -9.950  -9.089  55.910  1.00 59.34  ?  79  GLN C CB  1 
ATOM   3853 C CG  . GLN C 1 79  ? -10.610 -10.295 55.254  1.00 62.19  ?  79  GLN C CG  1 
ATOM   3854 C CD  . GLN C 1 79  ? -12.005 -10.554 55.783  1.00 60.55  ?  79  GLN C CD  1 
ATOM   3855 O OE1 . GLN C 1 79  ? -12.203 -10.750 56.985  1.00 59.06  ?  79  GLN C OE1 1 
ATOM   3856 N NE2 . GLN C 1 79  ? -12.986 -10.546 54.886  1.00 54.99  ?  79  GLN C NE2 1 
ATOM   3857 N N   . PRO C 1 80  ? -10.096 -6.507  57.773  1.00 60.12  ?  80  PRO C N   1 
ATOM   3858 C CA  . PRO C 1 80  ? -9.422  -5.380  58.441  1.00 53.50  ?  80  PRO C CA  1 
ATOM   3859 C C   . PRO C 1 80  ? -7.922  -5.386  58.259  1.00 59.21  ?  80  PRO C C   1 
ATOM   3860 O O   . PRO C 1 80  ? -7.308  -4.313  58.217  1.00 64.54  ?  80  PRO C O   1 
ATOM   3861 C CB  . PRO C 1 80  ? -9.803  -5.563  59.917  1.00 53.65  ?  80  PRO C CB  1 
ATOM   3862 C CG  . PRO C 1 80  ? -11.022 -6.402  59.897  1.00 57.18  ?  80  PRO C CG  1 
ATOM   3863 C CD  . PRO C 1 80  ? -10.866 -7.322  58.726  1.00 57.94  ?  80  PRO C CD  1 
ATOM   3864 N N   . GLU C 1 81  ? -7.309  -6.558  58.153  1.00 59.69  ?  81  GLU C N   1 
ATOM   3865 C CA  . GLU C 1 81  ? -5.872  -6.662  57.949  1.00 60.33  ?  81  GLU C CA  1 
ATOM   3866 C C   . GLU C 1 81  ? -5.451  -6.371  56.508  1.00 58.60  ?  81  GLU C C   1 
ATOM   3867 O O   . GLU C 1 81  ? -4.275  -6.551  56.174  1.00 59.27  ?  81  GLU C O   1 
ATOM   3868 C CB  . GLU C 1 81  ? -5.381  -8.049  58.376  1.00 59.34  ?  81  GLU C CB  1 
ATOM   3869 C CG  . GLU C 1 81  ? -5.905  -9.200  57.530  1.00 61.67  ?  81  GLU C CG  1 
ATOM   3870 C CD  . GLU C 1 81  ? -7.125  -9.875  58.142  1.00 71.97  ?  81  GLU C CD  1 
ATOM   3871 O OE1 . GLU C 1 81  ? -7.190  -11.126 58.099  1.00 69.33  ?  81  GLU C OE1 1 
ATOM   3872 O OE2 . GLU C 1 81  ? -8.008  -9.162  58.677  1.00 66.57  ?  81  GLU C OE2 1 
ATOM   3873 N N   . ASP C 1 82  ? -6.370  -5.937  55.649  1.00 56.07  ?  82  ASP C N   1 
ATOM   3874 C CA  . ASP C 1 82  ? -6.026  -5.594  54.278  1.00 52.86  ?  82  ASP C CA  1 
ATOM   3875 C C   . ASP C 1 82  ? -5.701  -4.122  54.101  1.00 56.03  ?  82  ASP C C   1 
ATOM   3876 O O   . ASP C 1 82  ? -5.375  -3.714  52.981  1.00 58.29  ?  82  ASP C O   1 
ATOM   3877 C CB  . ASP C 1 82  ? -7.162  -5.960  53.319  1.00 58.04  ?  82  ASP C CB  1 
ATOM   3878 C CG  . ASP C 1 82  ? -7.424  -7.447  53.258  1.00 59.49  ?  82  ASP C CG  1 
ATOM   3879 O OD1 . ASP C 1 82  ? -8.607  -7.830  53.143  1.00 58.85  ?  82  ASP C OD1 1 
ATOM   3880 O OD2 . ASP C 1 82  ? -6.458  -8.239  53.329  1.00 60.72  ?  82  ASP C OD2 1 
ATOM   3881 N N   . PHE C 1 83  ? -5.809  -3.312  55.155  1.00 54.34  ?  83  PHE C N   1 
ATOM   3882 C CA  . PHE C 1 83  ? -5.383  -1.922  55.066  1.00 51.51  ?  83  PHE C CA  1 
ATOM   3883 C C   . PHE C 1 83  ? -3.946  -1.857  54.596  1.00 50.10  ?  83  PHE C C   1 
ATOM   3884 O O   . PHE C 1 83  ? -3.044  -2.373  55.266  1.00 51.22  ?  83  PHE C O   1 
ATOM   3885 C CB  . PHE C 1 83  ? -5.515  -1.216  56.413  1.00 55.27  ?  83  PHE C CB  1 
ATOM   3886 C CG  . PHE C 1 83  ? -4.687  0.035   56.507  1.00 56.74  ?  83  PHE C CG  1 
ATOM   3887 C CD1 . PHE C 1 83  ? -3.474  0.036   57.182  1.00 58.37  ?  83  PHE C CD1 1 
ATOM   3888 C CD2 . PHE C 1 83  ? -5.109  1.206   55.897  1.00 53.95  ?  83  PHE C CD2 1 
ATOM   3889 C CE1 . PHE C 1 83  ? -2.708  1.179   57.253  1.00 58.37  ?  83  PHE C CE1 1 
ATOM   3890 C CE2 . PHE C 1 83  ? -4.346  2.354   55.967  1.00 57.91  ?  83  PHE C CE2 1 
ATOM   3891 C CZ  . PHE C 1 83  ? -3.146  2.342   56.646  1.00 59.95  ?  83  PHE C CZ  1 
ATOM   3892 N N   . ALA C 1 84  ? -3.732  -1.222  53.445  1.00 46.84  ?  84  ALA C N   1 
ATOM   3893 C CA  . ALA C 1 84  ? -2.388  -1.258  52.871  1.00 45.86  ?  84  ALA C CA  1 
ATOM   3894 C C   . ALA C 1 84  ? -2.375  -0.406  51.614  1.00 43.81  ?  84  ALA C C   1 
ATOM   3895 O O   . ALA C 1 84  ? -3.419  0.038   51.134  1.00 45.18  ?  84  ALA C O   1 
ATOM   3896 C CB  . ALA C 1 84  ? -1.944  -2.686  52.530  1.00 46.03  ?  84  ALA C CB  1 
ATOM   3897 N N   . THR C 1 85  ? -1.186  -0.229  51.050  1.00 39.70  ?  85  THR C N   1 
ATOM   3898 C CA  . THR C 1 85  ? -1.055  0.395   49.742  1.00 41.08  ?  85  THR C CA  1 
ATOM   3899 C C   . THR C 1 85  ? -0.728  -0.687  48.721  1.00 40.83  ?  85  THR C C   1 
ATOM   3900 O O   . THR C 1 85  ? 0.136   -1.533  48.964  1.00 43.01  ?  85  THR C O   1 
ATOM   3901 C CB  . THR C 1 85  ? 0.018   1.485   49.756  1.00 39.51  ?  85  THR C CB  1 
ATOM   3902 O OG1 . THR C 1 85  ? -0.221  2.358   50.865  1.00 36.21  ?  85  THR C OG1 1 
ATOM   3903 C CG2 . THR C 1 85  ? -0.031  2.299   48.467  1.00 33.69  ?  85  THR C CG2 1 
ATOM   3904 N N   . TYR C 1 86  ? -1.433  -0.679  47.597  1.00 42.69  ?  86  TYR C N   1 
ATOM   3905 C CA  . TYR C 1 86  ? -1.287  -1.710  46.580  1.00 39.34  ?  86  TYR C CA  1 
ATOM   3906 C C   . TYR C 1 86  ? -0.673  -1.112  45.324  1.00 42.65  ?  86  TYR C C   1 
ATOM   3907 O O   . TYR C 1 86  ? -1.078  -0.034  44.879  1.00 41.41  ?  86  TYR C O   1 
ATOM   3908 C CB  . TYR C 1 86  ? -2.635  -2.358  46.274  1.00 36.93  ?  86  TYR C CB  1 
ATOM   3909 C CG  . TYR C 1 86  ? -3.170  -3.123  47.458  1.00 44.53  ?  86  TYR C CG  1 
ATOM   3910 C CD1 . TYR C 1 86  ? -3.852  -2.470  48.477  1.00 40.94  ?  86  TYR C CD1 1 
ATOM   3911 C CD2 . TYR C 1 86  ? -2.982  -4.497  47.566  1.00 40.60  ?  86  TYR C CD2 1 
ATOM   3912 C CE1 . TYR C 1 86  ? -4.333  -3.164  49.570  1.00 44.82  ?  86  TYR C CE1 1 
ATOM   3913 C CE2 . TYR C 1 86  ? -3.463  -5.199  48.654  1.00 39.35  ?  86  TYR C CE2 1 
ATOM   3914 C CZ  . TYR C 1 86  ? -4.136  -4.526  49.653  1.00 43.95  ?  86  TYR C CZ  1 
ATOM   3915 O OH  . TYR C 1 86  ? -4.617  -5.212  50.743  1.00 51.39  ?  86  TYR C OH  1 
ATOM   3916 N N   . TYR C 1 87  ? 0.302   -1.815  44.759  1.00 39.04  ?  87  TYR C N   1 
ATOM   3917 C CA  . TYR C 1 87  ? 1.022   -1.341  43.588  1.00 41.31  ?  87  TYR C CA  1 
ATOM   3918 C C   . TYR C 1 87  ? 0.936   -2.363  42.466  1.00 39.92  ?  87  TYR C C   1 
ATOM   3919 O O   . TYR C 1 87  ? 0.902   -3.572  42.706  1.00 41.91  ?  87  TYR C O   1 
ATOM   3920 C CB  . TYR C 1 87  ? 2.499   -1.069  43.916  1.00 40.54  ?  87  TYR C CB  1 
ATOM   3921 C CG  . TYR C 1 87  ? 2.715   0.025   44.938  1.00 41.26  ?  87  TYR C CG  1 
ATOM   3922 C CD1 . TYR C 1 87  ? 2.921   1.341   44.547  1.00 39.80  ?  87  TYR C CD1 1 
ATOM   3923 C CD2 . TYR C 1 87  ? 2.722   -0.264  46.297  1.00 43.37  ?  87  TYR C CD2 1 
ATOM   3924 C CE1 . TYR C 1 87  ? 3.125   2.344   45.484  1.00 44.43  ?  87  TYR C CE1 1 
ATOM   3925 C CE2 . TYR C 1 87  ? 2.923   0.728   47.239  1.00 44.00  ?  87  TYR C CE2 1 
ATOM   3926 C CZ  . TYR C 1 87  ? 3.123   2.031   46.830  1.00 45.49  ?  87  TYR C CZ  1 
ATOM   3927 O OH  . TYR C 1 87  ? 3.323   3.015   47.776  1.00 41.60  ?  87  TYR C OH  1 
ATOM   3928 N N   . CYS C 1 88  ? 0.876   -1.871  41.234  1.00 41.26  ?  88  CYS C N   1 
ATOM   3929 C CA  . CYS C 1 88  ? 1.103   -2.717  40.074  1.00 38.21  ?  88  CYS C CA  1 
ATOM   3930 C C   . CYS C 1 88  ? 2.521   -2.510  39.554  1.00 41.10  ?  88  CYS C C   1 
ATOM   3931 O O   . CYS C 1 88  ? 3.142   -1.465  39.762  1.00 36.89  ?  88  CYS C O   1 
ATOM   3932 C CB  . CYS C 1 88  ? 0.082   -2.458  38.960  1.00 39.03  ?  88  CYS C CB  1 
ATOM   3933 S SG  . CYS C 1 88  ? -0.138  -0.740  38.460  1.00 56.00  ?  88  CYS C SG  1 
ATOM   3934 N N   . LEU C 1 89  ? 3.037   -3.546  38.907  1.00 39.01  ?  89  LEU C N   1 
ATOM   3935 C CA  . LEU C 1 89  ? 4.358   -3.532  38.305  1.00 32.70  ?  89  LEU C CA  1 
ATOM   3936 C C   . LEU C 1 89  ? 4.235   -4.114  36.909  1.00 37.02  ?  89  LEU C C   1 
ATOM   3937 O O   . LEU C 1 89  ? 3.841   -5.274  36.753  1.00 43.54  ?  89  LEU C O   1 
ATOM   3938 C CB  . LEU C 1 89  ? 5.348   -4.342  39.133  1.00 34.15  ?  89  LEU C CB  1 
ATOM   3939 C CG  . LEU C 1 89  ? 6.757   -4.430  38.552  1.00 36.06  ?  89  LEU C CG  1 
ATOM   3940 C CD1 . LEU C 1 89  ? 7.502   -3.108  38.724  1.00 30.50  ?  89  LEU C CD1 1 
ATOM   3941 C CD2 . LEU C 1 89  ? 7.500   -5.569  39.215  1.00 41.65  ?  89  LEU C CD2 1 
ATOM   3942 N N   . GLY C 1 90  ? 4.537   -3.304  35.901  1.00 32.44  ?  90  GLY C N   1 
ATOM   3943 C CA  . GLY C 1 90  ? 4.529   -3.740  34.521  1.00 31.97  ?  90  GLY C CA  1 
ATOM   3944 C C   . GLY C 1 90  ? 5.954   -3.842  34.008  1.00 34.00  ?  90  GLY C C   1 
ATOM   3945 O O   . GLY C 1 90  ? 6.771   -2.944  34.231  1.00 37.92  ?  90  GLY C O   1 
ATOM   3946 N N   . ILE C 1 91  ? 6.244   -4.950  33.336  1.00 35.04  ?  91  ILE C N   1 
ATOM   3947 C CA  . ILE C 1 91  ? 7.547   -5.180  32.729  1.00 40.03  ?  91  ILE C CA  1 
ATOM   3948 C C   . ILE C 1 91  ? 7.323   -5.402  31.240  1.00 40.70  ?  91  ILE C C   1 
ATOM   3949 O O   . ILE C 1 91  ? 6.690   -6.386  30.836  1.00 41.96  ?  91  ILE C O   1 
ATOM   3950 C CB  . ILE C 1 91  ? 8.289   -6.359  33.367  1.00 37.31  ?  91  ILE C CB  1 
ATOM   3951 C CG1 . ILE C 1 91  ? 8.497   -6.091  34.859  1.00 33.03  ?  91  ILE C CG1 1 
ATOM   3952 C CG2 . ILE C 1 91  ? 9.628   -6.563  32.674  1.00 36.69  ?  91  ILE C CG2 1 
ATOM   3953 C CD1 . ILE C 1 91  ? 9.249   -7.167  35.578  1.00 37.57  ?  91  ILE C CD1 1 
ATOM   3954 N N   . TYR C 1 92  ? 7.808   -4.471  30.430  1.00 36.87  ?  92  TYR C N   1 
ATOM   3955 C CA  . TYR C 1 92  ? 7.736   -4.591  28.981  1.00 41.27  ?  92  TYR C CA  1 
ATOM   3956 C C   . TYR C 1 92  ? 8.899   -5.444  28.487  1.00 40.41  ?  92  TYR C C   1 
ATOM   3957 O O   . TYR C 1 92  ? 10.065  -5.126  28.747  1.00 39.94  ?  92  TYR C O   1 
ATOM   3958 C CB  . TYR C 1 92  ? 7.773   -3.202  28.351  1.00 40.10  ?  92  TYR C CB  1 
ATOM   3959 C CG  . TYR C 1 92  ? 7.802   -3.174  26.843  1.00 39.10  ?  92  TYR C CG  1 
ATOM   3960 C CD1 . TYR C 1 92  ? 6.627   -3.277  26.106  1.00 37.90  ?  92  TYR C CD1 1 
ATOM   3961 C CD2 . TYR C 1 92  ? 9.003   -3.035  26.155  1.00 39.66  ?  92  TYR C CD2 1 
ATOM   3962 C CE1 . TYR C 1 92  ? 6.644   -3.236  24.727  1.00 40.99  ?  92  TYR C CE1 1 
ATOM   3963 C CE2 . TYR C 1 92  ? 9.033   -3.000  24.772  1.00 45.38  ?  92  TYR C CE2 1 
ATOM   3964 C CZ  . TYR C 1 92  ? 7.847   -3.102  24.063  1.00 48.07  ?  92  TYR C CZ  1 
ATOM   3965 O OH  . TYR C 1 92  ? 7.860   -3.065  22.689  1.00 50.25  ?  92  TYR C OH  1 
ATOM   3966 N N   . GLY C 1 93  ? 8.588   -6.511  27.760  1.00 41.62  ?  93  GLY C N   1 
ATOM   3967 C CA  . GLY C 1 93  ? 9.641   -7.397  27.286  1.00 42.89  ?  93  GLY C CA  1 
ATOM   3968 C C   . GLY C 1 93  ? 10.489  -7.910  28.434  1.00 41.15  ?  93  GLY C C   1 
ATOM   3969 O O   . GLY C 1 93  ? 9.978   -8.409  29.443  1.00 40.27  ?  93  GLY C O   1 
ATOM   3970 N N   . ASP C 1 94  ? 11.807  -7.761  28.292  1.00 40.15  ?  94  ASP C N   1 
ATOM   3971 C CA  . ASP C 1 94  ? 12.758  -8.180  29.313  1.00 41.39  ?  94  ASP C CA  1 
ATOM   3972 C C   . ASP C 1 94  ? 13.238  -7.010  30.174  1.00 42.31  ?  94  ASP C C   1 
ATOM   3973 O O   . ASP C 1 94  ? 14.340  -7.057  30.738  1.00 43.68  ?  94  ASP C O   1 
ATOM   3974 C CB  . ASP C 1 94  ? 13.942  -8.898  28.659  1.00 39.97  ?  94  ASP C CB  1 
ATOM   3975 C CG  . ASP C 1 94  ? 14.738  -9.733  29.646  1.00 44.10  ?  94  ASP C CG  1 
ATOM   3976 O OD1 . ASP C 1 94  ? 14.150  -10.128 30.676  1.00 43.16  ?  94  ASP C OD1 1 
ATOM   3977 O OD2 . ASP C 1 94  ? 15.944  -9.983  29.403  1.00 44.58  ?  94  ASP C OD2 1 
ATOM   3978 N N   . GLY C 1 95  ? 12.423  -5.962  30.293  1.00 40.52  ?  95  GLY C N   1 
ATOM   3979 C CA  . GLY C 1 95  ? 12.715  -4.837  31.169  1.00 38.58  ?  95  GLY C CA  1 
ATOM   3980 C C   . GLY C 1 95  ? 14.036  -4.131  30.932  1.00 38.89  ?  95  GLY C C   1 
ATOM   3981 O O   . GLY C 1 95  ? 14.879  -4.059  31.829  1.00 35.39  ?  95  GLY C O   1 
ATOM   3982 N N   . ALA C 1 96  ? 14.223  -3.576  29.738  1.00 40.77  ?  96  ALA C N   1 
ATOM   3983 C CA  . ALA C 1 96  ? 15.412  -2.781  29.462  1.00 40.64  ?  96  ALA C CA  1 
ATOM   3984 C C   . ALA C 1 96  ? 15.158  -1.356  29.936  1.00 39.70  ?  96  ALA C C   1 
ATOM   3985 O O   . ALA C 1 96  ? 14.241  -1.131  30.732  1.00 38.93  ?  96  ALA C O   1 
ATOM   3986 C CB  . ALA C 1 96  ? 15.736  -2.800  27.967  1.00 41.30  ?  96  ALA C CB  1 
ATOM   3987 N N   . ASP C 1 97  ? 15.969  -0.397  29.490  1.00 42.50  ?  97  ASP C N   1 
ATOM   3988 C CA  . ASP C 1 97  ? 15.846  0.980   29.961  1.00 42.83  ?  97  ASP C CA  1 
ATOM   3989 C C   . ASP C 1 97  ? 14.399  1.446   29.890  1.00 42.44  ?  97  ASP C C   1 
ATOM   3990 O O   . ASP C 1 97  ? 13.761  1.368   28.836  1.00 42.60  ?  97  ASP C O   1 
ATOM   3991 C CB  . ASP C 1 97  ? 16.748  1.909   29.144  1.00 41.94  ?  97  ASP C CB  1 
ATOM   3992 C CG  . ASP C 1 97  ? 18.203  1.833   29.571  1.00 47.06  ?  97  ASP C CG  1 
ATOM   3993 O OD1 . ASP C 1 97  ? 18.481  1.349   30.691  1.00 47.28  ?  97  ASP C OD1 1 
ATOM   3994 O OD2 . ASP C 1 97  ? 19.075  2.261   28.790  1.00 55.16  ?  97  ASP C OD2 1 
ATOM   3995 N N   . ASP C 1 98  ? 13.876  1.882   31.039  1.00 42.64  ?  98  ASP C N   1 
ATOM   3996 C CA  . ASP C 1 98  ? 12.474  2.275   31.198  1.00 38.78  ?  98  ASP C CA  1 
ATOM   3997 C C   . ASP C 1 98  ? 11.511  1.158   30.804  1.00 42.54  ?  98  ASP C C   1 
ATOM   3998 O O   . ASP C 1 98  ? 10.381  1.423   30.384  1.00 50.72  ?  98  ASP C O   1 
ATOM   3999 C CB  . ASP C 1 98  ? 12.168  3.555   30.420  1.00 40.77  ?  98  ASP C CB  1 
ATOM   4000 C CG  . ASP C 1 98  ? 13.051  4.710   30.850  1.00 44.89  ?  98  ASP C CG  1 
ATOM   4001 O OD1 . ASP C 1 98  ? 13.906  5.130   30.040  1.00 49.91  ?  98  ASP C OD1 1 
ATOM   4002 O OD2 . ASP C 1 98  ? 12.927  5.166   32.011  1.00 40.01  ?  98  ASP C OD2 1 
ATOM   4003 N N   . GLY C 1 99  ? 11.947  -0.096  30.944  1.00 43.22  ?  99  GLY C N   1 
ATOM   4004 C CA  . GLY C 1 99  ? 11.134  -1.263  30.678  1.00 41.11  ?  99  GLY C CA  1 
ATOM   4005 C C   . GLY C 1 99  ? 10.437  -1.840  31.890  1.00 43.17  ?  99  GLY C C   1 
ATOM   4006 O O   . GLY C 1 99  ? 9.731   -2.846  31.775  1.00 42.62  ?  99  GLY C O   1 
ATOM   4007 N N   . ILE C 1 100 ? 10.607  -1.224  33.057  1.00 40.47  ?  100 ILE C N   1 
ATOM   4008 C CA  . ILE C 1 100 ? 9.995   -1.670  34.301  1.00 39.25  ?  100 ILE C CA  1 
ATOM   4009 C C   . ILE C 1 100 ? 9.352   -0.455  34.952  1.00 39.60  ?  100 ILE C C   1 
ATOM   4010 O O   . ILE C 1 100 ? 10.015  0.569   35.143  1.00 42.23  ?  100 ILE C O   1 
ATOM   4011 C CB  . ILE C 1 100 ? 11.034  -2.298  35.246  1.00 37.86  ?  100 ILE C CB  1 
ATOM   4012 C CG1 . ILE C 1 100 ? 11.720  -3.489  34.574  1.00 42.57  ?  100 ILE C CG1 1 
ATOM   4013 C CG2 . ILE C 1 100 ? 10.381  -2.730  36.535  1.00 32.50  ?  100 ILE C CG2 1 
ATOM   4014 C CD1 . ILE C 1 100 ? 12.993  -3.957  35.292  1.00 39.14  ?  100 ILE C CD1 1 
ATOM   4015 N N   . ALA C 1 101 ? 8.073   -0.560  35.305  1.00 41.58  ?  101 ALA C N   1 
ATOM   4016 C CA  . ALA C 1 101 ? 7.365   0.603   35.826  1.00 41.21  ?  101 ALA C CA  1 
ATOM   4017 C C   . ALA C 1 101 ? 6.373   0.196   36.903  1.00 39.78  ?  101 ALA C C   1 
ATOM   4018 O O   . ALA C 1 101 ? 5.555   -0.705  36.690  1.00 39.03  ?  101 ALA C O   1 
ATOM   4019 C CB  . ALA C 1 101 ? 6.636   1.345   34.703  1.00 40.39  ?  101 ALA C CB  1 
ATOM   4020 N N   . PHE C 1 102 ? 6.451   0.865   38.051  1.00 36.96  ?  102 PHE C N   1 
ATOM   4021 C CA  . PHE C 1 102 ? 5.437   0.736   39.088  1.00 36.91  ?  102 PHE C CA  1 
ATOM   4022 C C   . PHE C 1 102 ? 4.270   1.675   38.822  1.00 38.27  ?  102 PHE C C   1 
ATOM   4023 O O   . PHE C 1 102 ? 4.430   2.755   38.247  1.00 44.01  ?  102 PHE C O   1 
ATOM   4024 C CB  . PHE C 1 102 ? 6.006   1.049   40.471  1.00 39.41  ?  102 PHE C CB  1 
ATOM   4025 C CG  . PHE C 1 102 ? 6.788   -0.063  41.076  1.00 34.29  ?  102 PHE C CG  1 
ATOM   4026 C CD1 . PHE C 1 102 ? 6.148   -1.060  41.798  1.00 36.96  ?  102 PHE C CD1 1 
ATOM   4027 C CD2 . PHE C 1 102 ? 8.166   -0.101  40.956  1.00 37.42  ?  102 PHE C CD2 1 
ATOM   4028 C CE1 . PHE C 1 102 ? 6.869   -2.092  42.372  1.00 39.04  ?  102 PHE C CE1 1 
ATOM   4029 C CE2 . PHE C 1 102 ? 8.899   -1.126  41.529  1.00 37.70  ?  102 PHE C CE2 1 
ATOM   4030 C CZ  . PHE C 1 102 ? 8.251   -2.127  42.238  1.00 38.16  ?  102 PHE C CZ  1 
ATOM   4031 N N   . GLY C 1 103 ? 3.084   1.244   39.232  1.00 45.85  ?  103 GLY C N   1 
ATOM   4032 C CA  . GLY C 1 103 ? 1.945   2.131   39.276  1.00 40.77  ?  103 GLY C CA  1 
ATOM   4033 C C   . GLY C 1 103 ? 2.026   3.081   40.454  1.00 42.38  ?  103 GLY C C   1 
ATOM   4034 O O   . GLY C 1 103 ? 2.852   2.926   41.356  1.00 39.01  ?  103 GLY C O   1 
ATOM   4035 N N   . GLY C 1 104 ? 1.137   4.079   40.440  1.00 40.50  ?  104 GLY C N   1 
ATOM   4036 C CA  . GLY C 1 104 ? 1.162   5.109   41.462  1.00 32.34  ?  104 GLY C CA  1 
ATOM   4037 C C   . GLY C 1 104 ? 0.806   4.618   42.847  1.00 35.12  ?  104 GLY C C   1 
ATOM   4038 O O   . GLY C 1 104 ? 1.154   5.271   43.834  1.00 42.28  ?  104 GLY C O   1 
ATOM   4039 N N   . GLY C 1 105 ? 0.134   3.485   42.946  1.00 38.72  ?  105 GLY C N   1 
ATOM   4040 C CA  . GLY C 1 105 ? -0.288  2.972   44.228  1.00 38.99  ?  105 GLY C CA  1 
ATOM   4041 C C   . GLY C 1 105 ? -1.739  3.312   44.523  1.00 40.73  ?  105 GLY C C   1 
ATOM   4042 O O   . GLY C 1 105 ? -2.315  4.257   43.981  1.00 42.95  ?  105 GLY C O   1 
ATOM   4043 N N   . THR C 1 106 ? -2.338  2.514   45.400  1.00 43.56  ?  106 THR C N   1 
ATOM   4044 C CA  . THR C 1 106 ? -3.711  2.731   45.837  1.00 43.18  ?  106 THR C CA  1 
ATOM   4045 C C   . THR C 1 106 ? -3.780  2.435   47.324  1.00 42.79  ?  106 THR C C   1 
ATOM   4046 O O   . THR C 1 106 ? -3.554  1.295   47.740  1.00 41.84  ?  106 THR C O   1 
ATOM   4047 C CB  . THR C 1 106 ? -4.704  1.844   45.075  1.00 40.24  ?  106 THR C CB  1 
ATOM   4048 O OG1 . THR C 1 106 ? -4.697  2.193   43.684  1.00 43.57  ?  106 THR C OG1 1 
ATOM   4049 C CG2 . THR C 1 106 ? -6.109  2.042   45.623  1.00 38.59  ?  106 THR C CG2 1 
ATOM   4050 N N   . LYS C 1 107 ? -4.071  3.460   48.118  1.00 40.99  ?  107 LYS C N   1 
ATOM   4051 C CA  . LYS C 1 107 ? -4.254  3.278   49.547  1.00 39.15  ?  107 LYS C CA  1 
ATOM   4052 C C   . LYS C 1 107 ? -5.643  2.709   49.799  1.00 44.19  ?  107 LYS C C   1 
ATOM   4053 O O   . LYS C 1 107 ? -6.642  3.239   49.303  1.00 47.86  ?  107 LYS C O   1 
ATOM   4054 C CB  . LYS C 1 107 ? -4.075  4.608   50.279  1.00 51.26  ?  107 LYS C CB  1 
ATOM   4055 C CG  . LYS C 1 107 ? -2.733  5.296   50.041  1.00 53.88  ?  107 LYS C CG  1 
ATOM   4056 C CD  . LYS C 1 107 ? -2.611  6.568   50.877  1.00 64.37  ?  107 LYS C CD  1 
ATOM   4057 C CE  . LYS C 1 107 ? -1.318  7.323   50.585  1.00 71.67  ?  107 LYS C CE  1 
ATOM   4058 N NZ  . LYS C 1 107 ? -1.441  8.235   49.411  1.00 71.32  ?  107 LYS C NZ  1 
ATOM   4059 N N   . VAL C 1 108 ? -5.707  1.630   50.565  1.00 42.67  ?  108 VAL C N   1 
ATOM   4060 C CA  . VAL C 1 108 ? -6.953  0.948   50.865  1.00 44.43  ?  108 VAL C CA  1 
ATOM   4061 C C   . VAL C 1 108 ? -7.140  1.007   52.372  1.00 47.93  ?  108 VAL C C   1 
ATOM   4062 O O   . VAL C 1 108 ? -6.345  0.427   53.135  1.00 53.03  ?  108 VAL C O   1 
ATOM   4063 C CB  . VAL C 1 108 ? -6.966  -0.496  50.348  1.00 40.33  ?  108 VAL C CB  1 
ATOM   4064 C CG1 . VAL C 1 108 ? -8.151  -1.250  50.921  1.00 45.65  ?  108 VAL C CG1 1 
ATOM   4065 C CG2 . VAL C 1 108 ? -7.024  -0.500  48.834  1.00 36.52  ?  108 VAL C CG2 1 
ATOM   4066 N N   . GLU C 1 109 ? -8.189  1.724   52.784  1.00 48.13  ?  109 GLU C N   1 
ATOM   4067 C CA  . GLU C 1 109 ? -8.589  1.931   54.166  1.00 51.02  ?  109 GLU C CA  1 
ATOM   4068 C C   . GLU C 1 109 ? -9.917  1.231   54.408  1.00 52.46  ?  109 GLU C C   1 
ATOM   4069 O O   . GLU C 1 109 ? -10.805 1.253   53.550  1.00 57.52  ?  109 GLU C O   1 
ATOM   4070 C CB  . GLU C 1 109 ? -8.736  3.426   54.475  1.00 50.03  ?  109 GLU C CB  1 
ATOM   4071 C CG  . GLU C 1 109 ? -9.409  3.730   55.805  1.00 54.61  ?  109 GLU C CG  1 
ATOM   4072 C CD  . GLU C 1 109 ? -10.154 5.050   55.805  1.00 60.26  ?  109 GLU C CD  1 
ATOM   4073 O OE1 . GLU C 1 109 ? -11.102 5.203   55.005  1.00 58.07  ?  109 GLU C OE1 1 
ATOM   4074 O OE2 . GLU C 1 109 ? -9.805  5.932   56.617  1.00 63.16  ?  109 GLU C OE2 1 
ATOM   4075 N N   . ILE C 1 110 ? -10.050 0.608   55.570  1.00 56.99  ?  110 ILE C N   1 
ATOM   4076 C CA  . ILE C 1 110 ? -11.267 -0.105  55.940  1.00 57.95  ?  110 ILE C CA  1 
ATOM   4077 C C   . ILE C 1 110 ? -12.246 0.890   56.547  1.00 60.00  ?  110 ILE C C   1 
ATOM   4078 O O   . ILE C 1 110 ? -11.889 1.659   57.448  1.00 57.33  ?  110 ILE C O   1 
ATOM   4079 C CB  . ILE C 1 110 ? -10.963 -1.246  56.926  1.00 53.69  ?  110 ILE C CB  1 
ATOM   4080 C CG1 . ILE C 1 110 ? -10.399 -2.458  56.186  1.00 57.70  ?  110 ILE C CG1 1 
ATOM   4081 C CG2 . ILE C 1 110 ? -12.206 -1.618  57.722  1.00 54.77  ?  110 ILE C CG2 1 
ATOM   4082 C CD1 . ILE C 1 110 ? -8.964  -2.304  55.754  1.00 53.88  ?  110 ILE C CD1 1 
ATOM   4083 N N   . LYS C 1 111 ? -13.477 0.891   56.046  1.00 57.49  ?  111 LYS C N   1 
ATOM   4084 C CA  . LYS C 1 111 ? -14.537 1.707   56.617  1.00 54.94  ?  111 LYS C CA  1 
ATOM   4085 C C   . LYS C 1 111 ? -15.248 0.903   57.697  1.00 55.69  ?  111 LYS C C   1 
ATOM   4086 O O   . LYS C 1 111 ? -15.861 -0.130  57.408  1.00 60.71  ?  111 LYS C O   1 
ATOM   4087 C CB  . LYS C 1 111 ? -15.516 2.168   55.540  1.00 56.00  ?  111 LYS C CB  1 
ATOM   4088 C CG  . LYS C 1 111 ? -16.562 3.139   56.050  1.00 59.70  ?  111 LYS C CG  1 
ATOM   4089 C CD  . LYS C 1 111 ? -17.517 3.562   54.945  1.00 63.88  ?  111 LYS C CD  1 
ATOM   4090 C CE  . LYS C 1 111 ? -16.787 4.361   53.877  1.00 65.25  ?  111 LYS C CE  1 
ATOM   4091 N NZ  . LYS C 1 111 ? -17.693 4.837   52.791  1.00 76.29  ?  111 LYS C NZ  1 
ATOM   4092 N N   . ARG C 1 112 ? -15.152 1.366   58.935  1.00 54.88  ?  112 ARG C N   1 
ATOM   4093 C CA  . ARG C 1 112 ? -15.811 0.742   60.071  1.00 53.32  ?  112 ARG C CA  1 
ATOM   4094 C C   . ARG C 1 112 ? -16.818 1.724   60.664  1.00 55.31  ?  112 ARG C C   1 
ATOM   4095 O O   . ARG C 1 112 ? -17.074 2.797   60.109  1.00 53.55  ?  112 ARG C O   1 
ATOM   4096 C CB  . ARG C 1 112 ? -14.789 0.300   61.119  1.00 52.60  ?  112 ARG C CB  1 
ATOM   4097 C CG  . ARG C 1 112 ? -13.972 1.443   61.697  1.00 53.19  ?  112 ARG C CG  1 
ATOM   4098 C CD  . ARG C 1 112 ? -13.499 1.116   63.098  1.00 55.21  ?  112 ARG C CD  1 
ATOM   4099 N NE  . ARG C 1 112 ? -14.542 1.377   64.084  1.00 57.54  ?  112 ARG C NE  1 
ATOM   4100 C CZ  . ARG C 1 112 ? -14.523 0.925   65.335  1.00 62.64  ?  112 ARG C CZ  1 
ATOM   4101 N NH1 . ARG C 1 112 ? -15.519 1.220   66.162  1.00 62.61  ?  112 ARG C NH1 1 
ATOM   4102 N NH2 . ARG C 1 112 ? -13.518 0.169   65.757  1.00 58.52  ?  112 ARG C NH2 1 
ATOM   4103 N N   . THR C 1 113 ? -17.388 1.353   61.804  1.00 57.56  ?  113 THR C N   1 
ATOM   4104 C CA  . THR C 1 113 ? -18.343 2.227   62.465  1.00 59.64  ?  113 THR C CA  1 
ATOM   4105 C C   . THR C 1 113 ? -17.628 3.426   63.069  1.00 61.40  ?  113 THR C C   1 
ATOM   4106 O O   . THR C 1 113 ? -16.442 3.367   63.407  1.00 64.74  ?  113 THR C O   1 
ATOM   4107 C CB  . THR C 1 113 ? -19.101 1.485   63.566  1.00 63.47  ?  113 THR C CB  1 
ATOM   4108 O OG1 . THR C 1 113 ? -18.196 1.143   64.625  1.00 58.32  ?  113 THR C OG1 1 
ATOM   4109 C CG2 . THR C 1 113 ? -19.754 0.219   63.012  1.00 59.15  ?  113 THR C CG2 1 
ATOM   4110 N N   . VAL C 1 114 ? -18.366 4.528   63.193  1.00 59.85  ?  114 VAL C N   1 
ATOM   4111 C CA  . VAL C 1 114 ? -17.807 5.733   63.785  1.00 56.64  ?  114 VAL C CA  1 
ATOM   4112 C C   . VAL C 1 114 ? -17.425 5.452   65.231  1.00 61.10  ?  114 VAL C C   1 
ATOM   4113 O O   . VAL C 1 114 ? -18.188 4.836   65.987  1.00 60.53  ?  114 VAL C O   1 
ATOM   4114 C CB  . VAL C 1 114 ? -18.811 6.891   63.679  1.00 56.74  ?  114 VAL C CB  1 
ATOM   4115 C CG1 . VAL C 1 114 ? -18.367 8.066   64.538  1.00 56.85  ?  114 VAL C CG1 1 
ATOM   4116 C CG2 . VAL C 1 114 ? -18.977 7.313   62.229  1.00 54.04  ?  114 VAL C CG2 1 
ATOM   4117 N N   . ALA C 1 115 ? -16.220 5.868   65.611  1.00 52.67  ?  115 ALA C N   1 
ATOM   4118 C CA  . ALA C 1 115 ? -15.745 5.732   66.979  1.00 54.12  ?  115 ALA C CA  1 
ATOM   4119 C C   . ALA C 1 115 ? -15.277 7.096   67.461  1.00 55.36  ?  115 ALA C C   1 
ATOM   4120 O O   . ALA C 1 115 ? -14.522 7.780   66.764  1.00 55.82  ?  115 ALA C O   1 
ATOM   4121 C CB  . ALA C 1 115 ? -14.615 4.707   67.084  1.00 55.42  ?  115 ALA C CB  1 
ATOM   4122 N N   . ALA C 1 116 ? -15.739 7.492   68.626  1.00 52.97  ?  116 ALA C N   1 
ATOM   4123 C CA  . ALA C 1 116 ? -15.313 8.764   69.183  1.00 54.99  ?  116 ALA C CA  1 
ATOM   4124 C C   . ALA C 1 116 ? -13.950 8.602   69.856  1.00 53.55  ?  116 ALA C C   1 
ATOM   4125 O O   . ALA C 1 116 ? -13.691 7.578   70.496  1.00 53.16  ?  116 ALA C O   1 
ATOM   4126 C CB  . ALA C 1 116 ? -16.348 9.286   70.181  1.00 43.97  ?  116 ALA C CB  1 
ATOM   4127 N N   . PRO C 1 117 ? -13.062 9.584   69.717  1.00 48.86  ?  117 PRO C N   1 
ATOM   4128 C CA  . PRO C 1 117 ? -11.711 9.449   70.278  1.00 56.10  ?  117 PRO C CA  1 
ATOM   4129 C C   . PRO C 1 117 ? -11.682 9.595   71.792  1.00 54.16  ?  117 PRO C C   1 
ATOM   4130 O O   . PRO C 1 117 ? -12.563 10.194  72.414  1.00 56.12  ?  117 PRO C O   1 
ATOM   4131 C CB  . PRO C 1 117 ? -10.935 10.589  69.607  1.00 52.54  ?  117 PRO C CB  1 
ATOM   4132 C CG  . PRO C 1 117 ? -11.977 11.612  69.294  1.00 49.30  ?  117 PRO C CG  1 
ATOM   4133 C CD  . PRO C 1 117 ? -13.218 10.826  68.938  1.00 50.16  ?  117 PRO C CD  1 
ATOM   4134 N N   . SER C 1 118 ? -10.648 9.003   72.386  1.00 50.97  ?  118 SER C N   1 
ATOM   4135 C CA  . SER C 1 118 ? -10.280 9.278   73.769  1.00 47.56  ?  118 SER C CA  1 
ATOM   4136 C C   . SER C 1 118 ? -9.250  10.399  73.760  1.00 48.23  ?  118 SER C C   1 
ATOM   4137 O O   . SER C 1 118 ? -8.187  10.258  73.152  1.00 49.14  ?  118 SER C O   1 
ATOM   4138 C CB  . SER C 1 118 ? -9.711  8.032   74.444  1.00 54.21  ?  118 SER C CB  1 
ATOM   4139 O OG  . SER C 1 118 ? -10.743 7.173   74.888  1.00 60.35  ?  118 SER C OG  1 
ATOM   4140 N N   . VAL C 1 119 ? -9.563  11.513  74.413  1.00 49.08  ?  119 VAL C N   1 
ATOM   4141 C CA  . VAL C 1 119 ? -8.758  12.725  74.315  1.00 46.05  ?  119 VAL C CA  1 
ATOM   4142 C C   . VAL C 1 119 ? -8.006  12.938  75.621  1.00 49.93  ?  119 VAL C C   1 
ATOM   4143 O O   . VAL C 1 119 ? -8.617  13.075  76.689  1.00 50.94  ?  119 VAL C O   1 
ATOM   4144 C CB  . VAL C 1 119 ? -9.618  13.947  73.970  1.00 42.20  ?  119 VAL C CB  1 
ATOM   4145 C CG1 . VAL C 1 119 ? -8.740  15.189  73.858  1.00 45.95  ?  119 VAL C CG1 1 
ATOM   4146 C CG2 . VAL C 1 119 ? -10.370 13.701  72.678  1.00 37.56  ?  119 VAL C CG2 1 
ATOM   4147 N N   . PHE C 1 120 ? -6.680  12.983  75.528  1.00 50.61  ?  120 PHE C N   1 
ATOM   4148 C CA  . PHE C 1 120 ? -5.810  13.293  76.654  1.00 52.30  ?  120 PHE C CA  1 
ATOM   4149 C C   . PHE C 1 120 ? -5.012  14.550  76.344  1.00 47.65  ?  120 PHE C C   1 
ATOM   4150 O O   . PHE C 1 120 ? -4.739  14.855  75.182  1.00 52.04  ?  120 PHE C O   1 
ATOM   4151 C CB  . PHE C 1 120 ? -4.838  12.147  76.958  1.00 49.26  ?  120 PHE C CB  1 
ATOM   4152 C CG  . PHE C 1 120 ? -5.499  10.815  77.145  1.00 49.39  ?  120 PHE C CG  1 
ATOM   4153 C CD1 . PHE C 1 120 ? -5.708  10.310  78.416  1.00 51.21  ?  120 PHE C CD1 1 
ATOM   4154 C CD2 . PHE C 1 120 ? -5.898  10.063  76.054  1.00 47.18  ?  120 PHE C CD2 1 
ATOM   4155 C CE1 . PHE C 1 120 ? -6.307  9.086   78.594  1.00 51.47  ?  120 PHE C CE1 1 
ATOM   4156 C CE2 . PHE C 1 120 ? -6.504  8.840   76.227  1.00 49.73  ?  120 PHE C CE2 1 
ATOM   4157 C CZ  . PHE C 1 120 ? -6.704  8.348   77.499  1.00 50.36  ?  120 PHE C CZ  1 
ATOM   4158 N N   . ILE C 1 121 ? -4.651  15.291  77.385  1.00 48.20  ?  121 ILE C N   1 
ATOM   4159 C CA  . ILE C 1 121 ? -3.817  16.474  77.227  1.00 52.74  ?  121 ILE C CA  1 
ATOM   4160 C C   . ILE C 1 121 ? -2.673  16.397  78.235  1.00 54.48  ?  121 ILE C C   1 
ATOM   4161 O O   . ILE C 1 121 ? -2.894  16.112  79.418  1.00 62.25  ?  121 ILE C O   1 
ATOM   4162 C CB  . ILE C 1 121 ? -4.626  17.786  77.365  1.00 51.83  ?  121 ILE C CB  1 
ATOM   4163 C CG1 . ILE C 1 121 ? -3.737  18.996  77.075  1.00 55.42  ?  121 ILE C CG1 1 
ATOM   4164 C CG2 . ILE C 1 121 ? -5.289  17.916  78.733  1.00 48.09  ?  121 ILE C CG2 1 
ATOM   4165 C CD1 . ILE C 1 121 ? -4.507  20.213  76.609  1.00 47.34  ?  121 ILE C CD1 1 
ATOM   4166 N N   . PHE C 1 122 ? -1.447  16.595  77.750  1.00 49.17  ?  122 PHE C N   1 
ATOM   4167 C CA  . PHE C 1 122 ? -0.233  16.553  78.548  1.00 48.13  ?  122 PHE C CA  1 
ATOM   4168 C C   . PHE C 1 122 ? 0.384   17.942  78.611  1.00 55.25  ?  122 PHE C C   1 
ATOM   4169 O O   . PHE C 1 122 ? 0.746   18.504  77.561  1.00 53.18  ?  122 PHE C O   1 
ATOM   4170 C CB  . PHE C 1 122 ? 0.774   15.567  77.959  1.00 44.21  ?  122 PHE C CB  1 
ATOM   4171 C CG  . PHE C 1 122 ? 0.346   14.136  78.020  1.00 48.02  ?  122 PHE C CG  1 
ATOM   4172 C CD1 . PHE C 1 122 ? 0.625   13.366  79.135  1.00 47.97  ?  122 PHE C CD1 1 
ATOM   4173 C CD2 . PHE C 1 122 ? -0.317  13.552  76.954  1.00 43.75  ?  122 PHE C CD2 1 
ATOM   4174 C CE1 . PHE C 1 122 ? 0.242   12.038  79.189  1.00 50.99  ?  122 PHE C CE1 1 
ATOM   4175 C CE2 . PHE C 1 122 ? -0.704  12.231  77.003  1.00 49.94  ?  122 PHE C CE2 1 
ATOM   4176 C CZ  . PHE C 1 122 ? -0.425  11.469  78.124  1.00 50.33  ?  122 PHE C CZ  1 
ATOM   4177 N N   . PRO C 1 123 ? 0.535   18.517  79.800  1.00 53.10  ?  123 PRO C N   1 
ATOM   4178 C CA  . PRO C 1 123 ? 1.297   19.759  79.936  1.00 51.76  ?  123 PRO C CA  1 
ATOM   4179 C C   . PRO C 1 123 ? 2.771   19.495  79.696  1.00 52.88  ?  123 PRO C C   1 
ATOM   4180 O O   . PRO C 1 123 ? 3.205   18.334  79.705  1.00 51.86  ?  123 PRO C O   1 
ATOM   4181 C CB  . PRO C 1 123 ? 1.038   20.177  81.395  1.00 52.63  ?  123 PRO C CB  1 
ATOM   4182 C CG  . PRO C 1 123 ? -0.122  19.337  81.855  1.00 57.07  ?  123 PRO C CG  1 
ATOM   4183 C CD  . PRO C 1 123 ? -0.017  18.062  81.086  1.00 49.78  ?  123 PRO C CD  1 
ATOM   4184 N N   . PRO C 1 124 ? 3.574   20.533  79.462  1.00 62.86  ?  124 PRO C N   1 
ATOM   4185 C CA  . PRO C 1 124 ? 5.012   20.308  79.289  1.00 53.67  ?  124 PRO C CA  1 
ATOM   4186 C C   . PRO C 1 124 ? 5.629   19.785  80.575  1.00 49.21  ?  124 PRO C C   1 
ATOM   4187 O O   . PRO C 1 124 ? 5.143   20.053  81.674  1.00 54.01  ?  124 PRO C O   1 
ATOM   4188 C CB  . PRO C 1 124 ? 5.551   21.698  78.931  1.00 52.73  ?  124 PRO C CB  1 
ATOM   4189 C CG  . PRO C 1 124 ? 4.551   22.646  79.486  1.00 51.92  ?  124 PRO C CG  1 
ATOM   4190 C CD  . PRO C 1 124 ? 3.224   21.961  79.350  1.00 54.02  ?  124 PRO C CD  1 
ATOM   4191 N N   . SER C 1 125 ? 6.693   19.002  80.428  1.00 55.21  ?  125 SER C N   1 
ATOM   4192 C CA  . SER C 1 125 ? 7.402   18.504  81.594  1.00 57.90  ?  125 SER C CA  1 
ATOM   4193 C C   . SER C 1 125 ? 8.259   19.612  82.198  1.00 58.55  ?  125 SER C C   1 
ATOM   4194 O O   . SER C 1 125 ? 8.568   20.617  81.551  1.00 60.37  ?  125 SER C O   1 
ATOM   4195 C CB  . SER C 1 125 ? 8.271   17.295  81.233  1.00 56.37  ?  125 SER C CB  1 
ATOM   4196 O OG  . SER C 1 125 ? 9.435   17.688  80.524  1.00 64.44  ?  125 SER C OG  1 
ATOM   4197 N N   . ASP C 1 126 ? 8.652   19.413  83.459  1.00 63.97  ?  126 ASP C N   1 
ATOM   4198 C CA  . ASP C 1 126 ? 9.470   20.415  84.134  1.00 69.36  ?  126 ASP C CA  1 
ATOM   4199 C C   . ASP C 1 126 ? 10.851  20.506  83.499  1.00 68.00  ?  126 ASP C C   1 
ATOM   4200 O O   . ASP C 1 126 ? 11.435  21.594  83.415  1.00 64.28  ?  126 ASP C O   1 
ATOM   4201 C CB  . ASP C 1 126 ? 9.589   20.080  85.622  1.00 73.98  ?  126 ASP C CB  1 
ATOM   4202 C CG  . ASP C 1 126 ? 8.382   20.533  86.422  1.00 88.57  ?  126 ASP C CG  1 
ATOM   4203 O OD1 . ASP C 1 126 ? 7.352   20.888  85.807  1.00 94.22  ?  126 ASP C OD1 1 
ATOM   4204 O OD2 . ASP C 1 126 ? 8.461   20.531  87.667  1.00 91.80  ?  126 ASP C OD2 1 
ATOM   4205 N N   . GLU C 1 127 ? 11.374  19.372  83.033  1.00 65.25  ?  127 GLU C N   1 
ATOM   4206 C CA  . GLU C 1 127 ? 12.669  19.347  82.362  1.00 66.38  ?  127 GLU C CA  1 
ATOM   4207 C C   . GLU C 1 127 ? 12.671  20.253  81.134  1.00 62.62  ?  127 GLU C C   1 
ATOM   4208 O O   . GLU C 1 127 ? 13.543  21.123  80.983  1.00 64.82  ?  127 GLU C O   1 
ATOM   4209 C CB  . GLU C 1 127 ? 12.997  17.902  81.989  1.00 67.01  ?  127 GLU C CB  1 
ATOM   4210 C CG  . GLU C 1 127 ? 12.264  16.907  82.896  1.00 72.55  ?  127 GLU C CG  1 
ATOM   4211 C CD  . GLU C 1 127 ? 12.586  15.451  82.606  1.00 74.65  ?  127 GLU C CD  1 
ATOM   4212 O OE1 . GLU C 1 127 ? 13.377  15.173  81.677  1.00 73.60  ?  127 GLU C OE1 1 
ATOM   4213 O OE2 . GLU C 1 127 ? 12.039  14.578  83.318  1.00 73.36  ?  127 GLU C OE2 1 
ATOM   4214 N N   . GLN C 1 128 ? 11.692  20.071  80.245  1.00 60.03  ?  128 GLN C N   1 
ATOM   4215 C CA  . GLN C 1 128 ? 11.647  20.892  79.042  1.00 59.78  ?  128 GLN C CA  1 
ATOM   4216 C C   . GLN C 1 128 ? 11.433  22.363  79.377  1.00 61.13  ?  128 GLN C C   1 
ATOM   4217 O O   . GLN C 1 128 ? 11.949  23.241  78.673  1.00 56.88  ?  128 GLN C O   1 
ATOM   4218 C CB  . GLN C 1 128 ? 10.559  20.391  78.093  1.00 52.65  ?  128 GLN C CB  1 
ATOM   4219 C CG  . GLN C 1 128 ? 10.720  20.932  76.689  1.00 52.54  ?  128 GLN C CG  1 
ATOM   4220 C CD  . GLN C 1 128 ? 9.445   20.878  75.879  1.00 54.70  ?  128 GLN C CD  1 
ATOM   4221 O OE1 . GLN C 1 128 ? 8.422   20.365  76.337  1.00 52.58  ?  128 GLN C OE1 1 
ATOM   4222 N NE2 . GLN C 1 128 ? 9.497   21.415  74.666  1.00 52.84  ?  128 GLN C NE2 1 
ATOM   4223 N N   . LEU C 1 129 ? 10.677  22.657  80.437  1.00 61.79  ?  129 LEU C N   1 
ATOM   4224 C CA  . LEU C 1 129 ? 10.507  24.050  80.837  1.00 63.47  ?  129 LEU C CA  1 
ATOM   4225 C C   . LEU C 1 129 ? 11.823  24.657  81.308  1.00 63.24  ?  129 LEU C C   1 
ATOM   4226 O O   . LEU C 1 129 ? 12.122  25.814  80.991  1.00 59.20  ?  129 LEU C O   1 
ATOM   4227 C CB  . LEU C 1 129 ? 9.447   24.170  81.926  1.00 58.58  ?  129 LEU C CB  1 
ATOM   4228 C CG  . LEU C 1 129 ? 8.050   24.482  81.407  1.00 58.66  ?  129 LEU C CG  1 
ATOM   4229 C CD1 . LEU C 1 129 ? 7.134   24.817  82.575  1.00 59.22  ?  129 LEU C CD1 1 
ATOM   4230 C CD2 . LEU C 1 129 ? 8.106   25.621  80.395  1.00 53.96  ?  129 LEU C CD2 1 
ATOM   4231 N N   . LYS C 1 130 ? 12.616  23.895  82.072  1.00 68.21  ?  130 LYS C N   1 
ATOM   4232 C CA  . LYS C 1 130 ? 13.967  24.338  82.412  1.00 67.78  ?  130 LYS C CA  1 
ATOM   4233 C C   . LYS C 1 130 ? 14.766  24.647  81.153  1.00 68.98  ?  130 LYS C C   1 
ATOM   4234 O O   . LYS C 1 130 ? 15.470  25.664  81.088  1.00 65.16  ?  130 LYS C O   1 
ATOM   4235 C CB  . LYS C 1 130 ? 14.694  23.273  83.239  1.00 67.81  ?  130 LYS C CB  1 
ATOM   4236 C CG  . LYS C 1 130 ? 14.065  22.943  84.586  1.00 70.35  ?  130 LYS C CG  1 
ATOM   4237 C CD  . LYS C 1 130 ? 14.754  21.744  85.240  1.00 63.50  ?  130 LYS C CD  1 
ATOM   4238 C CE  . LYS C 1 130 ? 14.235  21.509  86.652  1.00 64.82  ?  130 LYS C CE  1 
ATOM   4239 N NZ  . LYS C 1 130 ? 13.367  20.297  86.718  1.00 69.62  ?  130 LYS C NZ  1 
ATOM   4240 N N   . SER C 1 131 ? 14.665  23.775  80.140  1.00 63.88  ?  131 SER C N   1 
ATOM   4241 C CA  . SER C 1 131 ? 15.320  24.046  78.862  1.00 62.22  ?  131 SER C CA  1 
ATOM   4242 C C   . SER C 1 131 ? 14.900  25.389  78.270  1.00 63.70  ?  131 SER C C   1 
ATOM   4243 O O   . SER C 1 131 ? 15.670  26.005  77.524  1.00 63.86  ?  131 SER C O   1 
ATOM   4244 C CB  . SER C 1 131 ? 15.011  22.927  77.864  1.00 61.49  ?  131 SER C CB  1 
ATOM   4245 O OG  . SER C 1 131 ? 15.530  21.685  78.297  1.00 69.22  ?  131 SER C OG  1 
ATOM   4246 N N   . GLY C 1 132 ? 13.702  25.865  78.591  1.00 67.08  ?  132 GLY C N   1 
ATOM   4247 C CA  . GLY C 1 132 ? 13.203  27.100  78.030  1.00 63.46  ?  132 GLY C CA  1 
ATOM   4248 C C   . GLY C 1 132 ? 12.209  26.944  76.900  1.00 63.33  ?  132 GLY C C   1 
ATOM   4249 O O   . GLY C 1 132 ? 11.937  27.927  76.199  1.00 62.06  ?  132 GLY C O   1 
ATOM   4250 N N   . THR C 1 133 ? 11.671  25.742  76.690  1.00 64.16  ?  133 THR C N   1 
ATOM   4251 C CA  . THR C 1 133 ? 10.666  25.483  75.669  1.00 60.59  ?  133 THR C CA  1 
ATOM   4252 C C   . THR C 1 133 ? 9.502   24.755  76.321  1.00 59.53  ?  133 THR C C   1 
ATOM   4253 O O   . THR C 1 133 ? 9.681   24.040  77.310  1.00 64.07  ?  133 THR C O   1 
ATOM   4254 C CB  . THR C 1 133 ? 11.235  24.636  74.514  1.00 59.05  ?  133 THR C CB  1 
ATOM   4255 O OG1 . THR C 1 133 ? 12.492  25.179  74.095  1.00 64.69  ?  133 THR C OG1 1 
ATOM   4256 C CG2 . THR C 1 133 ? 10.285  24.623  73.327  1.00 56.33  ?  133 THR C CG2 1 
ATOM   4257 N N   . ALA C 1 134 ? 8.301   24.951  75.779  1.00 56.98  ?  134 ALA C N   1 
ATOM   4258 C CA  . ALA C 1 134 ? 7.094   24.346  76.331  1.00 56.99  ?  134 ALA C CA  1 
ATOM   4259 C C   . ALA C 1 134 ? 6.359   23.607  75.221  1.00 51.16  ?  134 ALA C C   1 
ATOM   4260 O O   . ALA C 1 134 ? 5.833   24.232  74.293  1.00 49.00  ?  134 ALA C O   1 
ATOM   4261 C CB  . ALA C 1 134 ? 6.198   25.406  76.968  1.00 58.09  ?  134 ALA C CB  1 
ATOM   4262 N N   . SER C 1 135 ? 6.300   22.285  75.326  1.00 51.87  ?  135 SER C N   1 
ATOM   4263 C CA  . SER C 1 135 ? 5.550   21.456  74.394  1.00 52.42  ?  135 SER C CA  1 
ATOM   4264 C C   . SER C 1 135 ? 4.369   20.854  75.137  1.00 47.81  ?  135 SER C C   1 
ATOM   4265 O O   . SER C 1 135 ? 4.556   20.086  76.087  1.00 50.79  ?  135 SER C O   1 
ATOM   4266 C CB  . SER C 1 135 ? 6.429   20.356  73.797  1.00 53.47  ?  135 SER C CB  1 
ATOM   4267 O OG  . SER C 1 135 ? 7.388   20.889  72.896  1.00 56.39  ?  135 SER C OG  1 
ATOM   4268 N N   . VAL C 1 136 ? 3.161   21.205  74.708  1.00 47.13  ?  136 VAL C N   1 
ATOM   4269 C CA  . VAL C 1 136 ? 1.930   20.639  75.243  1.00 47.46  ?  136 VAL C CA  1 
ATOM   4270 C C   . VAL C 1 136 ? 1.322   19.752  74.166  1.00 47.48  ?  136 VAL C C   1 
ATOM   4271 O O   . VAL C 1 136 ? 1.248   20.145  72.993  1.00 42.50  ?  136 VAL C O   1 
ATOM   4272 C CB  . VAL C 1 136 ? 0.962   21.740  75.723  1.00 49.37  ?  136 VAL C CB  1 
ATOM   4273 C CG1 . VAL C 1 136 ? 0.766   22.790  74.665  1.00 49.44  ?  136 VAL C CG1 1 
ATOM   4274 C CG2 . VAL C 1 136 ? -0.383  21.147  76.116  1.00 50.99  ?  136 VAL C CG2 1 
ATOM   4275 N N   . VAL C 1 137 ? 0.920   18.542  74.559  1.00 47.26  ?  137 VAL C N   1 
ATOM   4276 C CA  . VAL C 1 137 ? 0.572   17.479  73.618  1.00 44.82  ?  137 VAL C CA  1 
ATOM   4277 C C   . VAL C 1 137 ? -0.878  17.052  73.821  1.00 48.84  ?  137 VAL C C   1 
ATOM   4278 O O   . VAL C 1 137 ? -1.296  16.759  74.944  1.00 44.92  ?  137 VAL C O   1 
ATOM   4279 C CB  . VAL C 1 137 ? 1.519   16.273  73.761  1.00 47.21  ?  137 VAL C CB  1 
ATOM   4280 C CG1 . VAL C 1 137 ? 1.138   15.173  72.780  1.00 43.43  ?  137 VAL C CG1 1 
ATOM   4281 C CG2 . VAL C 1 137 ? 2.964   16.709  73.535  1.00 44.85  ?  137 VAL C CG2 1 
ATOM   4282 N N   . CYS C 1 138 ? -1.630  16.985  72.726  1.00 52.22  ?  138 CYS C N   1 
ATOM   4283 C CA  . CYS C 1 138 ? -3.017  16.538  72.705  1.00 49.14  ?  138 CYS C CA  1 
ATOM   4284 C C   . CYS C 1 138 ? -3.066  15.202  71.974  1.00 50.32  ?  138 CYS C C   1 
ATOM   4285 O O   . CYS C 1 138 ? -2.654  15.118  70.814  1.00 55.02  ?  138 CYS C O   1 
ATOM   4286 C CB  . CYS C 1 138 ? -3.892  17.574  72.001  1.00 50.70  ?  138 CYS C CB  1 
ATOM   4287 S SG  . CYS C 1 138 ? -5.677  17.284  71.979  1.00 69.99  ?  138 CYS C SG  1 
ATOM   4288 N N   . LEU C 1 139 ? -3.564  14.167  72.646  1.00 48.27  ?  139 LEU C N   1 
ATOM   4289 C CA  . LEU C 1 139 ? -3.626  12.818  72.092  1.00 49.74  ?  139 LEU C CA  1 
ATOM   4290 C C   . LEU C 1 139 ? -5.074  12.406  71.849  1.00 48.09  ?  139 LEU C C   1 
ATOM   4291 O O   . LEU C 1 139 ? -5.907  12.483  72.759  1.00 45.83  ?  139 LEU C O   1 
ATOM   4292 C CB  . LEU C 1 139 ? -2.946  11.813  73.027  1.00 48.11  ?  139 LEU C CB  1 
ATOM   4293 C CG  . LEU C 1 139 ? -3.201  10.313  72.801  1.00 50.36  ?  139 LEU C CG  1 
ATOM   4294 C CD1 . LEU C 1 139 ? -2.756  9.833   71.422  1.00 44.43  ?  139 LEU C CD1 1 
ATOM   4295 C CD2 . LEU C 1 139 ? -2.535  9.490   73.895  1.00 51.02  ?  139 LEU C CD2 1 
ATOM   4296 N N   . LEU C 1 140 ? -5.349  11.932  70.631  1.00 47.20  ?  140 LEU C N   1 
ATOM   4297 C CA  . LEU C 1 140 ? -6.647  11.418  70.206  1.00 46.11  ?  140 LEU C CA  1 
ATOM   4298 C C   . LEU C 1 140 ? -6.484  9.926   69.955  1.00 48.97  ?  140 LEU C C   1 
ATOM   4299 O O   . LEU C 1 140 ? -5.790  9.523   69.017  1.00 53.70  ?  140 LEU C O   1 
ATOM   4300 C CB  . LEU C 1 140 ? -7.119  12.116  68.934  1.00 46.56  ?  140 LEU C CB  1 
ATOM   4301 C CG  . LEU C 1 140 ? -7.710  13.521  68.983  1.00 48.76  ?  140 LEU C CG  1 
ATOM   4302 C CD1 . LEU C 1 140 ? -6.711  14.534  69.520  1.00 51.46  ?  140 LEU C CD1 1 
ATOM   4303 C CD2 . LEU C 1 140 ? -8.140  13.894  67.580  1.00 48.19  ?  140 LEU C CD2 1 
ATOM   4304 N N   . ASN C 1 141 ? -7.139  9.106   70.765  1.00 50.30  ?  141 ASN C N   1 
ATOM   4305 C CA  . ASN C 1 141 ? -6.904  7.673   70.762  1.00 52.11  ?  141 ASN C CA  1 
ATOM   4306 C C   . ASN C 1 141 ? -8.100  6.945   70.170  1.00 54.96  ?  141 ASN C C   1 
ATOM   4307 O O   . ASN C 1 141 ? -9.244  7.205   70.564  1.00 58.94  ?  141 ASN C O   1 
ATOM   4308 C CB  . ASN C 1 141 ? -6.635  7.165   72.180  1.00 50.68  ?  141 ASN C CB  1 
ATOM   4309 C CG  . ASN C 1 141 ? -5.581  6.085   72.215  1.00 55.68  ?  141 ASN C CG  1 
ATOM   4310 O OD1 . ASN C 1 141 ? -4.631  6.106   71.430  1.00 57.32  ?  141 ASN C OD1 1 
ATOM   4311 N ND2 . ASN C 1 141 ? -5.751  5.117   73.107  1.00 62.48  ?  141 ASN C ND2 1 
ATOM   4312 N N   . ASN C 1 142 ? -7.824  6.061   69.210  1.00 53.88  ?  142 ASN C N   1 
ATOM   4313 C CA  . ASN C 1 142 ? -8.737  5.008   68.756  1.00 56.51  ?  142 ASN C CA  1 
ATOM   4314 C C   . ASN C 1 142 ? -10.099 5.551   68.315  1.00 56.18  ?  142 ASN C C   1 
ATOM   4315 O O   . ASN C 1 142 ? -11.130 5.340   68.954  1.00 57.08  ?  142 ASN C O   1 
ATOM   4316 C CB  . ASN C 1 142 ? -8.900  3.956   69.853  1.00 55.20  ?  142 ASN C CB  1 
ATOM   4317 C CG  . ASN C 1 142 ? -7.576  3.348   70.260  1.00 60.52  ?  142 ASN C CG  1 
ATOM   4318 O OD1 . ASN C 1 142 ? -6.665  3.215   69.442  1.00 62.22  ?  142 ASN C OD1 1 
ATOM   4319 N ND2 . ASN C 1 142 ? -7.449  3.003   71.536  1.00 61.61  ?  142 ASN C ND2 1 
ATOM   4320 N N   . PHE C 1 143 ? -10.071 6.256   67.186  1.00 52.02  ?  143 PHE C N   1 
ATOM   4321 C CA  . PHE C 1 143 ? -11.267 6.877   66.638  1.00 52.32  ?  143 PHE C CA  1 
ATOM   4322 C C   . PHE C 1 143 ? -11.387 6.557   65.155  1.00 55.28  ?  143 PHE C C   1 
ATOM   4323 O O   . PHE C 1 143 ? -10.470 6.015   64.529  1.00 56.11  ?  143 PHE C O   1 
ATOM   4324 C CB  . PHE C 1 143 ? -11.254 8.400   66.847  1.00 49.14  ?  143 PHE C CB  1 
ATOM   4325 C CG  . PHE C 1 143 ? -10.103 9.096   66.179  1.00 47.61  ?  143 PHE C CG  1 
ATOM   4326 C CD1 . PHE C 1 143 ? -10.262 9.679   64.931  1.00 43.00  ?  143 PHE C CD1 1 
ATOM   4327 C CD2 . PHE C 1 143 ? -8.868  9.181   66.802  1.00 48.60  ?  143 PHE C CD2 1 
ATOM   4328 C CE1 . PHE C 1 143 ? -9.205  10.322  64.312  1.00 46.98  ?  143 PHE C CE1 1 
ATOM   4329 C CE2 . PHE C 1 143 ? -7.806  9.822   66.188  1.00 45.25  ?  143 PHE C CE2 1 
ATOM   4330 C CZ  . PHE C 1 143 ? -7.975  10.393  64.941  1.00 45.95  ?  143 PHE C CZ  1 
ATOM   4331 N N   . TYR C 1 144 ? -12.534 6.926   64.605  1.00 53.34  ?  144 TYR C N   1 
ATOM   4332 C CA  . TYR C 1 144 ? -12.856 6.780   63.195  1.00 54.64  ?  144 TYR C CA  1 
ATOM   4333 C C   . TYR C 1 144 ? -14.096 7.633   62.932  1.00 51.40  ?  144 TYR C C   1 
ATOM   4334 O O   . TYR C 1 144 ? -15.020 7.650   63.760  1.00 55.29  ?  144 TYR C O   1 
ATOM   4335 C CB  . TYR C 1 144 ? -13.085 5.306   62.818  1.00 51.75  ?  144 TYR C CB  1 
ATOM   4336 C CG  . TYR C 1 144 ? -13.136 5.108   61.324  1.00 53.16  ?  144 TYR C CG  1 
ATOM   4337 C CD1 . TYR C 1 144 ? -14.348 5.089   60.642  1.00 52.08  ?  144 TYR C CD1 1 
ATOM   4338 C CD2 . TYR C 1 144 ? -11.968 4.984   60.588  1.00 52.08  ?  144 TYR C CD2 1 
ATOM   4339 C CE1 . TYR C 1 144 ? -14.391 4.934   59.268  1.00 47.42  ?  144 TYR C CE1 1 
ATOM   4340 C CE2 . TYR C 1 144 ? -12.001 4.827   59.217  1.00 55.54  ?  144 TYR C CE2 1 
ATOM   4341 C CZ  . TYR C 1 144 ? -13.215 4.803   58.563  1.00 51.31  ?  144 TYR C CZ  1 
ATOM   4342 O OH  . TYR C 1 144 ? -13.250 4.649   57.197  1.00 52.83  ?  144 TYR C OH  1 
ATOM   4343 N N   . PRO C 1 145 ? -14.164 8.356   61.807  1.00 50.02  ?  145 PRO C N   1 
ATOM   4344 C CA  . PRO C 1 145 ? -13.216 8.331   60.695  1.00 52.31  ?  145 PRO C CA  1 
ATOM   4345 C C   . PRO C 1 145 ? -11.940 9.130   60.895  1.00 54.31  ?  145 PRO C C   1 
ATOM   4346 O O   . PRO C 1 145 ? -11.656 9.666   61.960  1.00 55.09  ?  145 PRO C O   1 
ATOM   4347 C CB  . PRO C 1 145 ? -14.019 8.934   59.548  1.00 47.23  ?  145 PRO C CB  1 
ATOM   4348 C CG  . PRO C 1 145 ? -14.918 9.894   60.227  1.00 46.37  ?  145 PRO C CG  1 
ATOM   4349 C CD  . PRO C 1 145 ? -15.301 9.241   61.531  1.00 52.69  ?  145 PRO C CD  1 
ATOM   4350 N N   . ARG C 1 146 ? -11.189 9.194   59.801  1.00 56.63  ?  146 ARG C N   1 
ATOM   4351 C CA  . ARG C 1 146 ? -9.834  9.729   59.834  1.00 59.90  ?  146 ARG C CA  1 
ATOM   4352 C C   . ARG C 1 146 ? -9.826  11.246  59.998  1.00 64.23  ?  146 ARG C C   1 
ATOM   4353 O O   . ARG C 1 146 ? -9.066  11.787  60.811  1.00 58.63  ?  146 ARG C O   1 
ATOM   4354 C CB  . ARG C 1 146 ? -9.119  9.307   58.560  1.00 66.14  ?  146 ARG C CB  1 
ATOM   4355 C CG  . ARG C 1 146 ? -7.643  9.533   58.525  1.00 64.10  ?  146 ARG C CG  1 
ATOM   4356 C CD  . ARG C 1 146 ? -7.118  8.778   57.333  1.00 67.98  ?  146 ARG C CD  1 
ATOM   4357 N NE  . ARG C 1 146 ? -5.737  9.110   57.039  1.00 69.76  ?  146 ARG C NE  1 
ATOM   4358 C CZ  . ARG C 1 146 ? -5.368  10.177  56.342  1.00 84.45  ?  146 ARG C CZ  1 
ATOM   4359 N NH1 . ARG C 1 146 ? -4.082  10.404  56.121  1.00 80.87  ?  146 ARG C NH1 1 
ATOM   4360 N NH2 . ARG C 1 146 ? -6.283  11.016  55.864  1.00 82.94  ?  146 ARG C NH2 1 
ATOM   4361 N N   . GLU C 1 147 ? -10.645 11.952  59.215  1.00 66.91  ?  147 GLU C N   1 
ATOM   4362 C CA  . GLU C 1 147 ? -10.641 13.411  59.252  1.00 71.42  ?  147 GLU C CA  1 
ATOM   4363 C C   . GLU C 1 147 ? -11.097 13.937  60.605  1.00 64.72  ?  147 GLU C C   1 
ATOM   4364 O O   . GLU C 1 147 ? -12.088 13.473  61.172  1.00 60.46  ?  147 GLU C O   1 
ATOM   4365 C CB  . GLU C 1 147 ? -11.523 13.986  58.140  1.00 76.23  ?  147 GLU C CB  1 
ATOM   4366 C CG  . GLU C 1 147 ? -10.898 13.975  56.750  1.00 88.53  ?  147 GLU C CG  1 
ATOM   4367 C CD  . GLU C 1 147 ? -9.563  14.719  56.700  1.00 96.22  ?  147 GLU C CD  1 
ATOM   4368 O OE1 . GLU C 1 147 ? -9.494  15.864  57.205  1.00 99.05  ?  147 GLU C OE1 1 
ATOM   4369 O OE2 . GLU C 1 147 ? -8.584  14.163  56.155  1.00 98.66  ?  147 GLU C OE2 1 
ATOM   4370 N N   . ALA C 1 148 ? -10.359 14.924  61.113  1.00 68.90  ?  148 ALA C N   1 
ATOM   4371 C CA  . ALA C 1 148 ? -10.662 15.542  62.397  1.00 58.04  ?  148 ALA C CA  1 
ATOM   4372 C C   . ALA C 1 148 ? -9.955  16.885  62.490  1.00 55.29  ?  148 ALA C C   1 
ATOM   4373 O O   . ALA C 1 148 ? -8.750  16.970  62.237  1.00 57.35  ?  148 ALA C O   1 
ATOM   4374 C CB  . ALA C 1 148 ? -10.236 14.640  63.557  1.00 49.77  ?  148 ALA C CB  1 
ATOM   4375 N N   . LYS C 1 149 ? -10.703 17.927  62.848  1.00 52.46  ?  149 LYS C N   1 
ATOM   4376 C CA  . LYS C 1 149 ? -10.134 19.251  63.060  1.00 49.40  ?  149 LYS C CA  1 
ATOM   4377 C C   . LYS C 1 149 ? -9.639  19.351  64.499  1.00 53.41  ?  149 LYS C C   1 
ATOM   4378 O O   . LYS C 1 149 ? -10.413 19.152  65.442  1.00 53.24  ?  149 LYS C O   1 
ATOM   4379 C CB  . LYS C 1 149 ? -11.172 20.334  62.771  1.00 54.19  ?  149 LYS C CB  1 
ATOM   4380 C CG  . LYS C 1 149 ? -10.713 21.741  63.137  1.00 65.84  ?  149 LYS C CG  1 
ATOM   4381 C CD  . LYS C 1 149 ? -11.701 22.825  62.687  1.00 75.03  ?  149 LYS C CD  1 
ATOM   4382 C CE  . LYS C 1 149 ? -13.060 22.692  63.385  1.00 75.58  ?  149 LYS C CE  1 
ATOM   4383 N NZ  . LYS C 1 149 ? -13.889 23.939  63.304  1.00 70.62  ?  149 LYS C NZ  1 
ATOM   4384 N N   . VAL C 1 150 ? -8.358  19.664  64.669  1.00 53.14  ?  150 VAL C N   1 
ATOM   4385 C CA  . VAL C 1 150 ? -7.756  19.854  65.984  1.00 50.78  ?  150 VAL C CA  1 
ATOM   4386 C C   . VAL C 1 150 ? -7.244  21.286  66.050  1.00 49.02  ?  150 VAL C C   1 
ATOM   4387 O O   . VAL C 1 150 ? -6.440  21.701  65.208  1.00 54.30  ?  150 VAL C O   1 
ATOM   4388 C CB  . VAL C 1 150 ? -6.624  18.851  66.247  1.00 56.52  ?  150 VAL C CB  1 
ATOM   4389 C CG1 . VAL C 1 150 ? -6.048  19.060  67.643  1.00 54.75  ?  150 VAL C CG1 1 
ATOM   4390 C CG2 . VAL C 1 150 ? -7.127  17.430  66.061  1.00 53.82  ?  150 VAL C CG2 1 
ATOM   4391 N N   . GLN C 1 151 ? -7.708  22.036  67.042  1.00 47.88  ?  151 GLN C N   1 
ATOM   4392 C CA  . GLN C 1 151 ? -7.355  23.437  67.197  1.00 49.41  ?  151 GLN C CA  1 
ATOM   4393 C C   . GLN C 1 151 ? -6.901  23.698  68.623  1.00 51.23  ?  151 GLN C C   1 
ATOM   4394 O O   . GLN C 1 151 ? -7.389  23.073  69.566  1.00 54.91  ?  151 GLN C O   1 
ATOM   4395 C CB  . GLN C 1 151 ? -8.545  24.341  66.874  1.00 51.96  ?  151 GLN C CB  1 
ATOM   4396 C CG  . GLN C 1 151 ? -9.128  24.159  65.484  1.00 57.74  ?  151 GLN C CG  1 
ATOM   4397 C CD  . GLN C 1 151 ? -10.047 25.304  65.097  1.00 69.48  ?  151 GLN C CD  1 
ATOM   4398 O OE1 . GLN C 1 151 ? -11.232 25.311  65.443  1.00 68.22  ?  151 GLN C OE1 1 
ATOM   4399 N NE2 . GLN C 1 151 ? -9.502  26.287  64.385  1.00 77.69  ?  151 GLN C NE2 1 
ATOM   4400 N N   . TRP C 1 152 ? -5.983  24.645  68.780  1.00 50.56  ?  152 TRP C N   1 
ATOM   4401 C CA  . TRP C 1 152 ? -5.469  25.024  70.088  1.00 47.91  ?  152 TRP C CA  1 
ATOM   4402 C C   . TRP C 1 152 ? -5.987  26.400  70.473  1.00 50.78  ?  152 TRP C C   1 
ATOM   4403 O O   . TRP C 1 152 ? -5.974  27.324  69.655  1.00 54.34  ?  152 TRP C O   1 
ATOM   4404 C CB  . TRP C 1 152 ? -3.940  25.023  70.097  1.00 49.89  ?  152 TRP C CB  1 
ATOM   4405 C CG  . TRP C 1 152 ? -3.368  23.659  70.083  1.00 46.19  ?  152 TRP C CG  1 
ATOM   4406 C CD1 . TRP C 1 152 ? -2.995  22.939  68.990  1.00 47.86  ?  152 TRP C CD1 1 
ATOM   4407 C CD2 . TRP C 1 152 ? -3.106  22.833  71.220  1.00 47.88  ?  152 TRP C CD2 1 
ATOM   4408 N NE1 . TRP C 1 152 ? -2.514  21.711  69.376  1.00 51.72  ?  152 TRP C NE1 1 
ATOM   4409 C CE2 . TRP C 1 152 ? -2.573  21.622  70.742  1.00 46.21  ?  152 TRP C CE2 1 
ATOM   4410 C CE3 . TRP C 1 152 ? -3.270  23.002  72.599  1.00 47.54  ?  152 TRP C CE3 1 
ATOM   4411 C CZ2 . TRP C 1 152 ? -2.201  20.585  71.589  1.00 49.07  ?  152 TRP C CZ2 1 
ATOM   4412 C CZ3 . TRP C 1 152 ? -2.901  21.971  73.440  1.00 52.01  ?  152 TRP C CZ3 1 
ATOM   4413 C CH2 . TRP C 1 152 ? -2.371  20.778  72.933  1.00 51.81  ?  152 TRP C CH2 1 
ATOM   4414 N N   . LYS C 1 153 ? -6.443  26.526  71.717  1.00 54.68  ?  153 LYS C N   1 
ATOM   4415 C CA  . LYS C 1 153 ? -6.827  27.803  72.304  1.00 57.64  ?  153 LYS C CA  1 
ATOM   4416 C C   . LYS C 1 153 ? -6.155  27.936  73.660  1.00 57.81  ?  153 LYS C C   1 
ATOM   4417 O O   . LYS C 1 153 ? -6.283  27.051  74.513  1.00 55.05  ?  153 LYS C O   1 
ATOM   4418 C CB  . LYS C 1 153 ? -8.349  27.958  72.447  1.00 54.51  ?  153 LYS C CB  1 
ATOM   4419 C CG  . LYS C 1 153 ? -9.131  27.780  71.157  1.00 56.77  ?  153 LYS C CG  1 
ATOM   4420 C CD  . LYS C 1 153 ? -10.632 27.842  71.414  1.00 69.29  ?  153 LYS C CD  1 
ATOM   4421 C CE  . LYS C 1 153 ? -11.421 27.122  70.327  1.00 79.76  ?  153 LYS C CE  1 
ATOM   4422 N NZ  . LYS C 1 153 ? -12.891 27.288  70.498  1.00 74.61  ?  153 LYS C NZ  1 
ATOM   4423 N N   . VAL C 1 154 ? -5.434  29.033  73.847  1.00 55.40  ?  154 VAL C N   1 
ATOM   4424 C CA  . VAL C 1 154 ? -4.789  29.353  75.112  1.00 60.47  ?  154 VAL C CA  1 
ATOM   4425 C C   . VAL C 1 154 ? -5.411  30.643  75.629  1.00 59.12  ?  154 VAL C C   1 
ATOM   4426 O O   . VAL C 1 154 ? -5.361  31.679  74.954  1.00 61.15  ?  154 VAL C O   1 
ATOM   4427 C CB  . VAL C 1 154 ? -3.258  29.453  74.966  1.00 60.67  ?  154 VAL C CB  1 
ATOM   4428 C CG1 . VAL C 1 154 ? -2.876  30.307  73.791  1.00 55.73  ?  154 VAL C CG1 1 
ATOM   4429 C CG2 . VAL C 1 154 ? -2.634  30.013  76.225  1.00 60.22  ?  154 VAL C CG2 1 
ATOM   4430 N N   . ASP C 1 155 ? -6.035  30.564  76.804  1.00 61.34  ?  155 ASP C N   1 
ATOM   4431 C CA  . ASP C 1 155 ? -6.846  31.653  77.350  1.00 67.25  ?  155 ASP C CA  1 
ATOM   4432 C C   . ASP C 1 155 ? -7.901  32.107  76.341  1.00 68.10  ?  155 ASP C C   1 
ATOM   4433 O O   . ASP C 1 155 ? -8.074  33.298  76.071  1.00 72.23  ?  155 ASP C O   1 
ATOM   4434 C CB  . ASP C 1 155 ? -5.966  32.819  77.801  1.00 58.73  ?  155 ASP C CB  1 
ATOM   4435 C CG  . ASP C 1 155 ? -5.147  32.480  79.030  1.00 64.99  ?  155 ASP C CG  1 
ATOM   4436 O OD1 . ASP C 1 155 ? -5.592  31.620  79.819  1.00 65.51  ?  155 ASP C OD1 1 
ATOM   4437 O OD2 . ASP C 1 155 ? -4.060  33.066  79.206  1.00 64.22  ?  155 ASP C OD2 1 
ATOM   4438 N N   . ASN C 1 156 ? -8.611  31.124  75.781  1.00 64.66  ?  156 ASN C N   1 
ATOM   4439 C CA  . ASN C 1 156 ? -9.720  31.321  74.846  1.00 65.89  ?  156 ASN C CA  1 
ATOM   4440 C C   . ASN C 1 156 ? -9.301  32.056  73.572  1.00 65.58  ?  156 ASN C C   1 
ATOM   4441 O O   . ASN C 1 156 ? -10.143 32.648  72.891  1.00 69.42  ?  156 ASN C O   1 
ATOM   4442 C CB  . ASN C 1 156 ? -10.879 32.065  75.526  1.00 66.99  ?  156 ASN C CB  1 
ATOM   4443 C CG  . ASN C 1 156 ? -11.478 31.285  76.690  1.00 70.96  ?  156 ASN C CG  1 
ATOM   4444 O OD1 . ASN C 1 156 ? -11.290 31.643  77.853  1.00 77.01  ?  156 ASN C OD1 1 
ATOM   4445 N ND2 . ASN C 1 156 ? -12.209 30.222  76.381  1.00 69.98  ?  156 ASN C ND2 1 
ATOM   4446 N N   . ALA C 1 157 ? -8.020  31.994  73.210  1.00 63.55  ?  157 ALA C N   1 
ATOM   4447 C CA  . ALA C 1 157 ? -7.491  32.625  72.004  1.00 60.57  ?  157 ALA C CA  1 
ATOM   4448 C C   . ALA C 1 157 ? -7.000  31.552  71.043  1.00 63.12  ?  157 ALA C C   1 
ATOM   4449 O O   . ALA C 1 157 ? -6.096  30.780  71.382  1.00 62.48  ?  157 ALA C O   1 
ATOM   4450 C CB  . ALA C 1 157 ? -6.359  33.598  72.344  1.00 60.47  ?  157 ALA C CB  1 
ATOM   4451 N N   . LEU C 1 158 ? -7.601  31.498  69.854  1.00 60.03  ?  158 LEU C N   1 
ATOM   4452 C CA  . LEU C 1 158 ? -7.214  30.512  68.850  1.00 58.32  ?  158 LEU C CA  1 
ATOM   4453 C C   . LEU C 1 158 ? -5.766  30.710  68.415  1.00 59.98  ?  158 LEU C C   1 
ATOM   4454 O O   . LEU C 1 158 ? -5.328  31.834  68.160  1.00 62.68  ?  158 LEU C O   1 
ATOM   4455 C CB  . LEU C 1 158 ? -8.141  30.608  67.639  1.00 57.90  ?  158 LEU C CB  1 
ATOM   4456 C CG  . LEU C 1 158 ? -7.720  29.827  66.391  1.00 65.86  ?  158 LEU C CG  1 
ATOM   4457 C CD1 . LEU C 1 158 ? -7.683  28.323  66.657  1.00 64.87  ?  158 LEU C CD1 1 
ATOM   4458 C CD2 . LEU C 1 158 ? -8.645  30.154  65.228  1.00 67.49  ?  158 LEU C CD2 1 
ATOM   4459 N N   . GLN C 1 159 ? -5.030  29.605  68.327  1.00 62.56  ?  159 GLN C N   1 
ATOM   4460 C CA  . GLN C 1 159 ? -3.617  29.602  67.968  1.00 60.83  ?  159 GLN C CA  1 
ATOM   4461 C C   . GLN C 1 159 ? -3.418  29.378  66.474  1.00 62.36  ?  159 GLN C C   1 
ATOM   4462 O O   . GLN C 1 159 ? -4.244  28.759  65.799  1.00 67.59  ?  159 GLN C O   1 
ATOM   4463 C CB  . GLN C 1 159 ? -2.870  28.525  68.753  1.00 58.00  ?  159 GLN C CB  1 
ATOM   4464 C CG  . GLN C 1 159 ? -2.754  28.827  70.228  1.00 55.22  ?  159 GLN C CG  1 
ATOM   4465 C CD  . GLN C 1 159 ? -2.058  30.143  70.474  1.00 62.03  ?  159 GLN C CD  1 
ATOM   4466 O OE1 . GLN C 1 159 ? -0.834  30.230  70.399  1.00 70.50  ?  159 GLN C OE1 1 
ATOM   4467 N NE2 . GLN C 1 159 ? -2.835  31.184  70.748  1.00 61.54  ?  159 GLN C NE2 1 
ATOM   4468 N N   . SER C 1 160 ? -2.304  29.895  65.963  1.00 66.77  ?  160 SER C N   1 
ATOM   4469 C CA  . SER C 1 160 ? -1.969  29.750  64.554  1.00 67.17  ?  160 SER C CA  1 
ATOM   4470 C C   . SER C 1 160 ? -0.460  29.650  64.402  1.00 61.67  ?  160 SER C C   1 
ATOM   4471 O O   . SER C 1 160 ? 0.275   30.494  64.921  1.00 64.13  ?  160 SER C O   1 
ATOM   4472 C CB  . SER C 1 160 ? -2.497  30.930  63.736  1.00 63.87  ?  160 SER C CB  1 
ATOM   4473 O OG  . SER C 1 160 ? -3.899  31.052  63.878  1.00 73.02  ?  160 SER C OG  1 
ATOM   4474 N N   . GLY C 1 161 ? -0.008  28.607  63.711  1.00 54.67  ?  161 GLY C N   1 
ATOM   4475 C CA  . GLY C 1 161 ? 1.375   28.487  63.312  1.00 54.04  ?  161 GLY C CA  1 
ATOM   4476 C C   . GLY C 1 161 ? 2.318   27.875  64.322  1.00 66.77  ?  161 GLY C C   1 
ATOM   4477 O O   . GLY C 1 161 ? 3.516   27.770  64.033  1.00 81.39  ?  161 GLY C O   1 
ATOM   4478 N N   . ASN C 1 162 ? 1.834   27.469  65.496  1.00 58.54  ?  162 ASN C N   1 
ATOM   4479 C CA  . ASN C 1 162 ? 2.708   26.895  66.513  1.00 54.83  ?  162 ASN C CA  1 
ATOM   4480 C C   . ASN C 1 162 ? 2.229   25.519  66.967  1.00 51.63  ?  162 ASN C C   1 
ATOM   4481 O O   . ASN C 1 162 ? 2.445   25.128  68.117  1.00 50.98  ?  162 ASN C O   1 
ATOM   4482 C CB  . ASN C 1 162 ? 2.852   27.843  67.703  1.00 57.80  ?  162 ASN C CB  1 
ATOM   4483 C CG  . ASN C 1 162 ? 1.521   28.374  68.190  1.00 63.30  ?  162 ASN C CG  1 
ATOM   4484 O OD1 . ASN C 1 162 ? 0.467   28.036  67.652  1.00 63.96  ?  162 ASN C OD1 1 
ATOM   4485 N ND2 . ASN C 1 162 ? 1.563   29.220  69.212  1.00 65.13  ?  162 ASN C ND2 1 
ATOM   4486 N N   . SER C 1 163 ? 1.582   24.768  66.079  1.00 51.49  ?  163 SER C N   1 
ATOM   4487 C CA  . SER C 1 163 ? 1.186   23.401  66.382  1.00 51.18  ?  163 SER C CA  1 
ATOM   4488 C C   . SER C 1 163 ? 1.383   22.531  65.150  1.00 51.36  ?  163 SER C C   1 
ATOM   4489 O O   . SER C 1 163 ? 1.340   23.011  64.014  1.00 53.10  ?  163 SER C O   1 
ATOM   4490 C CB  . SER C 1 163 ? -0.274  23.313  66.860  1.00 51.92  ?  163 SER C CB  1 
ATOM   4491 O OG  . SER C 1 163 ? -1.183  23.610  65.817  1.00 51.99  ?  163 SER C OG  1 
ATOM   4492 N N   . GLN C 1 164 ? 1.592   21.241  65.395  1.00 51.09  ?  164 GLN C N   1 
ATOM   4493 C CA  . GLN C 1 164 ? 1.787   20.265  64.331  1.00 52.06  ?  164 GLN C CA  1 
ATOM   4494 C C   . GLN C 1 164 ? 1.032   18.986  64.657  1.00 51.42  ?  164 GLN C C   1 
ATOM   4495 O O   . GLN C 1 164 ? 0.832   18.645  65.823  1.00 51.03  ?  164 GLN C O   1 
ATOM   4496 C CB  . GLN C 1 164 ? 3.268   19.942  64.121  1.00 55.05  ?  164 GLN C CB  1 
ATOM   4497 C CG  . GLN C 1 164 ? 4.075   21.086  63.537  1.00 61.31  ?  164 GLN C CG  1 
ATOM   4498 C CD  . GLN C 1 164 ? 5.448   20.645  63.080  1.00 66.25  ?  164 GLN C CD  1 
ATOM   4499 O OE1 . GLN C 1 164 ? 6.227   20.088  63.857  1.00 70.97  ?  164 GLN C OE1 1 
ATOM   4500 N NE2 . GLN C 1 164 ? 5.750   20.878  61.807  1.00 69.32  ?  164 GLN C NE2 1 
ATOM   4501 N N   . GLU C 1 165 ? 0.627   18.273  63.612  1.00 54.95  ?  165 GLU C N   1 
ATOM   4502 C CA  . GLU C 1 165 ? -0.148  17.051  63.763  1.00 55.00  ?  165 GLU C CA  1 
ATOM   4503 C C   . GLU C 1 165 ? 0.577   15.862  63.152  1.00 52.26  ?  165 GLU C C   1 
ATOM   4504 O O   . GLU C 1 165 ? 1.377   16.000  62.222  1.00 48.90  ?  165 GLU C O   1 
ATOM   4505 C CB  . GLU C 1 165 ? -1.534  17.151  63.111  1.00 55.05  ?  165 GLU C CB  1 
ATOM   4506 C CG  . GLU C 1 165 ? -2.456  18.162  63.715  1.00 61.27  ?  165 GLU C CG  1 
ATOM   4507 C CD  . GLU C 1 165 ? -3.762  18.252  62.962  1.00 75.39  ?  165 GLU C CD  1 
ATOM   4508 O OE1 . GLU C 1 165 ? -4.043  17.348  62.138  1.00 73.06  ?  165 GLU C OE1 1 
ATOM   4509 O OE2 . GLU C 1 165 ? -4.508  19.227  63.199  1.00 80.43  ?  165 GLU C OE2 1 
ATOM   4510 N N   . SER C 1 166 ? 0.273   14.689  63.698  1.00 55.28  ?  166 SER C N   1 
ATOM   4511 C CA  . SER C 1 166 ? 0.763   13.422  63.183  1.00 48.88  ?  166 SER C CA  1 
ATOM   4512 C C   . SER C 1 166 ? -0.324  12.387  63.436  1.00 48.74  ?  166 SER C C   1 
ATOM   4513 O O   . SER C 1 166 ? -0.936  12.381  64.506  1.00 45.45  ?  166 SER C O   1 
ATOM   4514 C CB  . SER C 1 166 ? 2.084   13.020  63.853  1.00 43.08  ?  166 SER C CB  1 
ATOM   4515 O OG  . SER C 1 166 ? 2.506   11.738  63.425  1.00 50.92  ?  166 SER C OG  1 
ATOM   4516 N N   . VAL C 1 167 ? -0.599  11.546  62.443  1.00 43.96  ?  167 VAL C N   1 
ATOM   4517 C CA  . VAL C 1 167 ? -1.634  10.527  62.561  1.00 44.91  ?  167 VAL C CA  1 
ATOM   4518 C C   . VAL C 1 167 ? -1.019  9.172   62.250  1.00 47.56  ?  167 VAL C C   1 
ATOM   4519 O O   . VAL C 1 167 ? -0.248  9.037   61.294  1.00 52.16  ?  167 VAL C O   1 
ATOM   4520 C CB  . VAL C 1 167 ? -2.841  10.816  61.641  1.00 51.25  ?  167 VAL C CB  1 
ATOM   4521 C CG1 . VAL C 1 167 ? -2.408  10.970  60.187  1.00 51.13  ?  167 VAL C CG1 1 
ATOM   4522 C CG2 . VAL C 1 167 ? -3.893  9.732   61.792  1.00 42.75  ?  167 VAL C CG2 1 
ATOM   4523 N N   . THR C 1 168 ? -1.350  8.174   63.069  1.00 47.36  ?  168 THR C N   1 
ATOM   4524 C CA  . THR C 1 168 ? -0.883  6.819   62.821  1.00 45.23  ?  168 THR C CA  1 
ATOM   4525 C C   . THR C 1 168 ? -1.576  6.243   61.592  1.00 55.33  ?  168 THR C C   1 
ATOM   4526 O O   . THR C 1 168 ? -2.570  6.777   61.086  1.00 54.92  ?  168 THR C O   1 
ATOM   4527 C CB  . THR C 1 168 ? -1.153  5.901   64.016  1.00 44.51  ?  168 THR C CB  1 
ATOM   4528 O OG1 . THR C 1 168 ? -2.552  5.621   64.093  1.00 55.67  ?  168 THR C OG1 1 
ATOM   4529 C CG2 . THR C 1 168 ? -0.724  6.547   65.312  1.00 51.15  ?  168 THR C CG2 1 
ATOM   4530 N N   . GLU C 1 169 ? -1.047  5.120   61.120  1.00 52.38  ?  169 GLU C N   1 
ATOM   4531 C CA  . GLU C 1 169 ? -1.753  4.363   60.106  1.00 56.57  ?  169 GLU C CA  1 
ATOM   4532 C C   . GLU C 1 169 ? -2.963  3.676   60.730  1.00 55.71  ?  169 GLU C C   1 
ATOM   4533 O O   . GLU C 1 169 ? -3.102  3.585   61.954  1.00 50.23  ?  169 GLU C O   1 
ATOM   4534 C CB  . GLU C 1 169 ? -0.829  3.331   59.460  1.00 59.93  ?  169 GLU C CB  1 
ATOM   4535 C CG  . GLU C 1 169 ? 0.420   3.910   58.791  1.00 69.80  ?  169 GLU C CG  1 
ATOM   4536 C CD  . GLU C 1 169 ? 0.164   4.424   57.377  1.00 71.51  ?  169 GLU C CD  1 
ATOM   4537 O OE1 . GLU C 1 169 ? -0.966  4.874   57.088  1.00 69.33  ?  169 GLU C OE1 1 
ATOM   4538 O OE2 . GLU C 1 169 ? 1.095   4.360   56.545  1.00 78.74  ?  169 GLU C OE2 1 
ATOM   4539 N N   . GLN C 1 170 ? -3.860  3.207   59.870  1.00 53.68  ?  170 GLN C N   1 
ATOM   4540 C CA  . GLN C 1 170 ? -5.062  2.559   60.367  1.00 60.50  ?  170 GLN C CA  1 
ATOM   4541 C C   . GLN C 1 170 ? -4.681  1.271   61.076  1.00 54.15  ?  170 GLN C C   1 
ATOM   4542 O O   . GLN C 1 170 ? -3.926  0.455   60.540  1.00 59.57  ?  170 GLN C O   1 
ATOM   4543 C CB  . GLN C 1 170 ? -6.032  2.265   59.231  1.00 57.64  ?  170 GLN C CB  1 
ATOM   4544 C CG  . GLN C 1 170 ? -7.376  1.813   59.732  1.00 51.93  ?  170 GLN C CG  1 
ATOM   4545 C CD  . GLN C 1 170 ? -8.430  1.860   58.660  1.00 59.39  ?  170 GLN C CD  1 
ATOM   4546 O OE1 . GLN C 1 170 ? -8.170  1.501   57.512  1.00 57.16  ?  170 GLN C OE1 1 
ATOM   4547 N NE2 . GLN C 1 170 ? -9.627  2.323   59.018  1.00 58.36  ?  170 GLN C NE2 1 
ATOM   4548 N N   . ASP C 1 171 ? -5.196  1.093   62.284  1.00 53.60  ?  171 ASP C N   1 
ATOM   4549 C CA  . ASP C 1 171 ? -4.896  -0.108  63.045  1.00 58.44  ?  171 ASP C CA  1 
ATOM   4550 C C   . ASP C 1 171 ? -5.400  -1.338  62.300  1.00 63.36  ?  171 ASP C C   1 
ATOM   4551 O O   . ASP C 1 171 ? -6.575  -1.422  61.930  1.00 65.42  ?  171 ASP C O   1 
ATOM   4552 C CB  . ASP C 1 171 ? -5.528  -0.011  64.432  1.00 59.90  ?  171 ASP C CB  1 
ATOM   4553 C CG  . ASP C 1 171 ? -4.996  -1.053  65.391  1.00 64.88  ?  171 ASP C CG  1 
ATOM   4554 O OD1 . ASP C 1 171 ? -5.271  -2.250  65.178  1.00 66.87  ?  171 ASP C OD1 1 
ATOM   4555 O OD2 . ASP C 1 171 ? -4.311  -0.673  66.364  1.00 76.13  ?  171 ASP C OD2 1 
ATOM   4556 N N   . SER C 1 172 ? -4.499  -2.291  62.069  1.00 60.45  ?  172 SER C N   1 
ATOM   4557 C CA  . SER C 1 172 ? -4.842  -3.475  61.291  1.00 63.89  ?  172 SER C CA  1 
ATOM   4558 C C   . SER C 1 172 ? -5.790  -4.420  62.022  1.00 63.66  ?  172 SER C C   1 
ATOM   4559 O O   . SER C 1 172 ? -6.303  -5.354  61.397  1.00 63.08  ?  172 SER C O   1 
ATOM   4560 C CB  . SER C 1 172 ? -3.566  -4.216  60.895  1.00 65.49  ?  172 SER C CB  1 
ATOM   4561 O OG  . SER C 1 172 ? -2.757  -4.468  62.030  1.00 72.20  ?  172 SER C OG  1 
ATOM   4562 N N   . LYS C 1 173 ? -6.038  -4.206  63.315  1.00 63.24  ?  173 LYS C N   1 
ATOM   4563 C CA  . LYS C 1 173 ? -6.957  -5.050  64.074  1.00 65.85  ?  173 LYS C CA  1 
ATOM   4564 C C   . LYS C 1 173 ? -8.367  -4.456  64.116  1.00 66.77  ?  173 LYS C C   1 
ATOM   4565 O O   . LYS C 1 173 ? -9.326  -5.082  63.653  1.00 60.39  ?  173 LYS C O   1 
ATOM   4566 C CB  . LYS C 1 173 ? -6.427  -5.267  65.500  1.00 71.56  ?  173 LYS C CB  1 
ATOM   4567 C CG  . LYS C 1 173 ? -5.252  -6.250  65.629  1.00 76.98  ?  173 LYS C CG  1 
ATOM   4568 C CD  . LYS C 1 173 ? -3.899  -5.600  65.320  1.00 77.25  ?  173 LYS C CD  1 
ATOM   4569 C CE  . LYS C 1 173 ? -3.506  -4.556  66.365  1.00 74.33  ?  173 LYS C CE  1 
ATOM   4570 N NZ  . LYS C 1 173 ? -2.299  -3.771  65.966  1.00 64.44  ?  173 LYS C NZ  1 
ATOM   4571 N N   . ASP C 1 174 ? -8.503  -3.239  64.646  1.00 63.97  ?  174 ASP C N   1 
ATOM   4572 C CA  . ASP C 1 174 ? -9.808  -2.640  64.890  1.00 58.31  ?  174 ASP C CA  1 
ATOM   4573 C C   . ASP C 1 174 ? -10.119 -1.459  63.979  1.00 62.70  ?  174 ASP C C   1 
ATOM   4574 O O   . ASP C 1 174 ? -11.161 -0.817  64.159  1.00 59.86  ?  174 ASP C O   1 
ATOM   4575 C CB  . ASP C 1 174 ? -9.924  -2.215  66.361  1.00 61.46  ?  174 ASP C CB  1 
ATOM   4576 C CG  . ASP C 1 174 ? -9.073  -1.000  66.697  1.00 70.30  ?  174 ASP C CG  1 
ATOM   4577 O OD1 . ASP C 1 174 ? -9.472  -0.223  67.590  1.00 75.55  ?  174 ASP C OD1 1 
ATOM   4578 O OD2 . ASP C 1 174 ? -8.023  -0.799  66.058  1.00 71.80  ?  174 ASP C OD2 1 
ATOM   4579 N N   . SER C 1 175 ? -9.243  -1.149  63.018  1.00 59.12  ?  175 SER C N   1 
ATOM   4580 C CA  . SER C 1 175 ? -9.499  -0.145  61.984  1.00 61.13  ?  175 SER C CA  1 
ATOM   4581 C C   . SER C 1 175 ? -9.622  1.273   62.546  1.00 57.14  ?  175 SER C C   1 
ATOM   4582 O O   . SER C 1 175 ? -10.244 2.137   61.922  1.00 51.28  ?  175 SER C O   1 
ATOM   4583 C CB  . SER C 1 175 ? -10.753 -0.493  61.174  1.00 57.31  ?  175 SER C CB  1 
ATOM   4584 O OG  . SER C 1 175 ? -10.639 -1.769  60.574  1.00 64.24  ?  175 SER C OG  1 
ATOM   4585 N N   . THR C 1 176 ? -9.019  1.548   63.699  1.00 58.07  ?  176 THR C N   1 
ATOM   4586 C CA  . THR C 1 176 ? -9.044  2.885   64.275  1.00 58.88  ?  176 THR C CA  1 
ATOM   4587 C C   . THR C 1 176 ? -7.735  3.623   64.012  1.00 53.15  ?  176 THR C C   1 
ATOM   4588 O O   . THR C 1 176 ? -6.715  3.029   63.654  1.00 51.48  ?  176 THR C O   1 
ATOM   4589 C CB  . THR C 1 176 ? -9.310  2.835   65.785  1.00 61.61  ?  176 THR C CB  1 
ATOM   4590 O OG1 . THR C 1 176 ? -8.335  2.002   66.428  1.00 60.11  ?  176 THR C OG1 1 
ATOM   4591 C CG2 . THR C 1 176 ? -10.708 2.307   66.066  1.00 63.34  ?  176 THR C CG2 1 
ATOM   4592 N N   . TYR C 1 177 ? -7.786  4.940   64.189  1.00 50.16  ?  177 TYR C N   1 
ATOM   4593 C CA  . TYR C 1 177 ? -6.637  5.821   64.071  1.00 44.40  ?  177 TYR C CA  1 
ATOM   4594 C C   . TYR C 1 177 ? -6.314  6.441   65.423  1.00 48.53  ?  177 TYR C C   1 
ATOM   4595 O O   . TYR C 1 177 ? -7.147  6.480   66.333  1.00 49.41  ?  177 TYR C O   1 
ATOM   4596 C CB  . TYR C 1 177 ? -6.893  6.947   63.066  1.00 40.91  ?  177 TYR C CB  1 
ATOM   4597 C CG  . TYR C 1 177 ? -6.951  6.531   61.621  1.00 52.56  ?  177 TYR C CG  1 
ATOM   4598 C CD1 . TYR C 1 177 ? -5.816  6.577   60.826  1.00 54.45  ?  177 TYR C CD1 1 
ATOM   4599 C CD2 . TYR C 1 177 ? -8.146  6.118   61.040  1.00 52.97  ?  177 TYR C CD2 1 
ATOM   4600 C CE1 . TYR C 1 177 ? -5.858  6.210   59.497  1.00 57.33  ?  177 TYR C CE1 1 
ATOM   4601 C CE2 . TYR C 1 177 ? -8.200  5.752   59.710  1.00 53.01  ?  177 TYR C CE2 1 
ATOM   4602 C CZ  . TYR C 1 177 ? -7.050  5.799   58.943  1.00 59.72  ?  177 TYR C CZ  1 
ATOM   4603 O OH  . TYR C 1 177 ? -7.082  5.439   57.615  1.00 61.61  ?  177 TYR C OH  1 
ATOM   4604 N N   . SER C 1 178 ? -5.084  6.932   65.542  1.00 42.70  ?  178 SER C N   1 
ATOM   4605 C CA  . SER C 1 178 ? -4.689  7.795   66.643  1.00 40.70  ?  178 SER C CA  1 
ATOM   4606 C C   . SER C 1 178 ? -3.974  9.006   66.071  1.00 42.80  ?  178 SER C C   1 
ATOM   4607 O O   . SER C 1 178 ? -3.348  8.936   65.012  1.00 46.29  ?  178 SER C O   1 
ATOM   4608 C CB  . SER C 1 178 ? -3.800  7.080   67.656  1.00 44.75  ?  178 SER C CB  1 
ATOM   4609 O OG  . SER C 1 178 ? -4.560  6.182   68.440  1.00 49.26  ?  178 SER C OG  1 
ATOM   4610 N N   . LEU C 1 179 ? -4.092  10.125  66.772  1.00 43.83  ?  179 LEU C N   1 
ATOM   4611 C CA  . LEU C 1 179 ? -3.537  11.387  66.320  1.00 45.57  ?  179 LEU C CA  1 
ATOM   4612 C C   . LEU C 1 179 ? -2.873  12.090  67.494  1.00 49.37  ?  179 LEU C C   1 
ATOM   4613 O O   . LEU C 1 179 ? -3.321  11.986  68.637  1.00 48.35  ?  179 LEU C O   1 
ATOM   4614 C CB  . LEU C 1 179 ? -4.635  12.267  65.696  1.00 45.79  ?  179 LEU C CB  1 
ATOM   4615 C CG  . LEU C 1 179 ? -4.311  13.708  65.304  1.00 49.72  ?  179 LEU C CG  1 
ATOM   4616 C CD1 . LEU C 1 179 ? -5.041  14.091  64.029  1.00 54.27  ?  179 LEU C CD1 1 
ATOM   4617 C CD2 . LEU C 1 179 ? -4.674  14.666  66.425  1.00 47.27  ?  179 LEU C CD2 1 
ATOM   4618 N N   . SER C 1 180 ? -1.795  12.804  67.207  1.00 48.37  ?  180 SER C N   1 
ATOM   4619 C CA  . SER C 1 180 ? -1.153  13.646  68.199  1.00 48.91  ?  180 SER C CA  1 
ATOM   4620 C C   . SER C 1 180 ? -1.001  15.039  67.618  1.00 48.94  ?  180 SER C C   1 
ATOM   4621 O O   . SER C 1 180 ? -0.656  15.198  66.442  1.00 52.91  ?  180 SER C O   1 
ATOM   4622 C CB  . SER C 1 180 ? 0.215   13.090  68.627  1.00 50.03  ?  180 SER C CB  1 
ATOM   4623 O OG  . SER C 1 180 ? 1.174   13.228  67.593  1.00 55.11  ?  180 SER C OG  1 
ATOM   4624 N N   . SER C 1 181 ? -1.282  16.040  68.445  1.00 49.11  ?  181 SER C N   1 
ATOM   4625 C CA  . SER C 1 181 ? -1.108  17.440  68.089  1.00 48.07  ?  181 SER C CA  1 
ATOM   4626 C C   . SER C 1 181 ? -0.211  18.081  69.137  1.00 49.37  ?  181 SER C C   1 
ATOM   4627 O O   . SER C 1 181 ? -0.420  17.899  70.338  1.00 51.13  ?  181 SER C O   1 
ATOM   4628 C CB  . SER C 1 181 ? -2.448  18.164  68.005  1.00 46.22  ?  181 SER C CB  1 
ATOM   4629 O OG  . SER C 1 181 ? -2.287  19.473  67.491  1.00 53.10  ?  181 SER C OG  1 
ATOM   4630 N N   . THR C 1 182 ? 0.797   18.811  68.690  1.00 44.49  ?  182 THR C N   1 
ATOM   4631 C CA  . THR C 1 182 ? 1.776   19.391  69.593  1.00 49.48  ?  182 THR C CA  1 
ATOM   4632 C C   . THR C 1 182 ? 1.808   20.895  69.406  1.00 45.44  ?  182 THR C C   1 
ATOM   4633 O O   . THR C 1 182 ? 1.989   21.378  68.285  1.00 46.72  ?  182 THR C O   1 
ATOM   4634 C CB  . THR C 1 182 ? 3.166   18.795  69.357  1.00 51.42  ?  182 THR C CB  1 
ATOM   4635 O OG1 . THR C 1 182 ? 3.103   17.371  69.525  1.00 48.30  ?  182 THR C OG1 1 
ATOM   4636 C CG2 . THR C 1 182 ? 4.177   19.381  70.338  1.00 43.99  ?  182 THR C CG2 1 
ATOM   4637 N N   . LEU C 1 183 ? 1.623   21.620  70.502  1.00 48.01  ?  183 LEU C N   1 
ATOM   4638 C CA  . LEU C 1 183 ? 1.723   23.072  70.524  1.00 51.33  ?  183 LEU C CA  1 
ATOM   4639 C C   . LEU C 1 183 ? 3.007   23.427  71.252  1.00 50.64  ?  183 LEU C C   1 
ATOM   4640 O O   . LEU C 1 183 ? 3.214   22.999  72.393  1.00 53.72  ?  183 LEU C O   1 
ATOM   4641 C CB  . LEU C 1 183 ? 0.520   23.702  71.227  1.00 50.88  ?  183 LEU C CB  1 
ATOM   4642 C CG  . LEU C 1 183 ? 0.554   25.215  71.446  1.00 47.70  ?  183 LEU C CG  1 
ATOM   4643 C CD1 . LEU C 1 183 ? 0.094   25.952  70.202  1.00 48.36  ?  183 LEU C CD1 1 
ATOM   4644 C CD2 . LEU C 1 183 ? -0.289  25.598  72.638  1.00 43.15  ?  183 LEU C CD2 1 
ATOM   4645 N N   . THR C 1 184 ? 3.865   24.204  70.596  1.00 54.15  ?  184 THR C N   1 
ATOM   4646 C CA  . THR C 1 184 ? 5.170   24.553  71.138  1.00 53.95  ?  184 THR C CA  1 
ATOM   4647 C C   . THR C 1 184 ? 5.255   26.064  71.304  1.00 53.94  ?  184 THR C C   1 
ATOM   4648 O O   . THR C 1 184 ? 4.954   26.817  70.371  1.00 56.37  ?  184 THR C O   1 
ATOM   4649 C CB  . THR C 1 184 ? 6.305   24.044  70.238  1.00 57.37  ?  184 THR C CB  1 
ATOM   4650 O OG1 . THR C 1 184 ? 6.117   22.649  69.963  1.00 56.46  ?  184 THR C OG1 1 
ATOM   4651 C CG2 . THR C 1 184 ? 7.655   24.232  70.922  1.00 54.71  ?  184 THR C CG2 1 
ATOM   4652 N N   . LEU C 1 185 ? 5.635   26.497  72.505  1.00 54.08  ?  185 LEU C N   1 
ATOM   4653 C CA  . LEU C 1 185 ? 5.847   27.901  72.825  1.00 57.16  ?  185 LEU C CA  1 
ATOM   4654 C C   . LEU C 1 185 ? 7.208   28.063  73.488  1.00 58.52  ?  185 LEU C C   1 
ATOM   4655 O O   . LEU C 1 185 ? 7.843   27.089  73.904  1.00 55.10  ?  185 LEU C O   1 
ATOM   4656 C CB  . LEU C 1 185 ? 4.753   28.432  73.759  1.00 55.03  ?  185 LEU C CB  1 
ATOM   4657 C CG  . LEU C 1 185 ? 3.322   28.072  73.372  1.00 56.93  ?  185 LEU C CG  1 
ATOM   4658 C CD1 . LEU C 1 185 ? 2.357   28.519  74.456  1.00 61.50  ?  185 LEU C CD1 1 
ATOM   4659 C CD2 . LEU C 1 185 ? 2.961   28.685  72.036  1.00 55.18  ?  185 LEU C CD2 1 
ATOM   4660 N N   . SER C 1 186 ? 7.652   29.312  73.601  1.00 55.64  ?  186 SER C N   1 
ATOM   4661 C CA  . SER C 1 186 ? 8.763   29.597  74.490  1.00 53.75  ?  186 SER C CA  1 
ATOM   4662 C C   . SER C 1 186 ? 8.282   29.519  75.934  1.00 57.82  ?  186 SER C C   1 
ATOM   4663 O O   . SER C 1 186 ? 7.087   29.629  76.221  1.00 64.54  ?  186 SER C O   1 
ATOM   4664 C CB  . SER C 1 186 ? 9.355   30.975  74.202  1.00 55.28  ?  186 SER C CB  1 
ATOM   4665 O OG  . SER C 1 186 ? 8.456   31.996  74.587  1.00 64.18  ?  186 SER C OG  1 
ATOM   4666 N N   . LYS C 1 187 ? 9.229   29.327  76.852  1.00 59.63  ?  187 LYS C N   1 
ATOM   4667 C CA  . LYS C 1 187 ? 8.874   29.283  78.267  1.00 61.88  ?  187 LYS C CA  1 
ATOM   4668 C C   . LYS C 1 187 ? 8.169   30.565  78.702  1.00 65.04  ?  187 LYS C C   1 
ATOM   4669 O O   . LYS C 1 187 ? 7.201   30.518  79.470  1.00 65.24  ?  187 LYS C O   1 
ATOM   4670 C CB  . LYS C 1 187 ? 10.121  29.035  79.119  1.00 66.06  ?  187 LYS C CB  1 
ATOM   4671 C CG  . LYS C 1 187 ? 9.857   29.050  80.623  1.00 67.47  ?  187 LYS C CG  1 
ATOM   4672 C CD  . LYS C 1 187 ? 11.148  29.035  81.425  1.00 65.48  ?  187 LYS C CD  1 
ATOM   4673 C CE  . LYS C 1 187 ? 10.864  29.083  82.919  1.00 70.12  ?  187 LYS C CE  1 
ATOM   4674 N NZ  . LYS C 1 187 ? 12.108  29.259  83.719  1.00 74.46  ?  187 LYS C NZ  1 
ATOM   4675 N N   . ALA C 1 188 ? 8.632   31.719  78.212  1.00 62.40  ?  188 ALA C N   1 
ATOM   4676 C CA  . ALA C 1 188 ? 8.018   32.988  78.597  1.00 61.69  ?  188 ALA C CA  1 
ATOM   4677 C C   . ALA C 1 188 ? 6.559   33.058  78.156  1.00 68.41  ?  188 ALA C C   1 
ATOM   4678 O O   . ALA C 1 188 ? 5.665   33.339  78.967  1.00 72.81  ?  188 ALA C O   1 
ATOM   4679 C CB  . ALA C 1 188 ? 8.813   34.152  78.005  1.00 57.51  ?  188 ALA C CB  1 
ATOM   4680 N N   . ASP C 1 189 ? 6.300   32.797  76.869  1.00 67.48  ?  189 ASP C N   1 
ATOM   4681 C CA  . ASP C 1 189 ? 4.928   32.792  76.364  1.00 68.66  ?  189 ASP C CA  1 
ATOM   4682 C C   . ASP C 1 189 ? 4.055   31.828  77.156  1.00 65.72  ?  189 ASP C C   1 
ATOM   4683 O O   . ASP C 1 189 ? 2.927   32.162  77.538  1.00 63.62  ?  189 ASP C O   1 
ATOM   4684 C CB  . ASP C 1 189 ? 4.910   32.430  74.879  1.00 64.95  ?  189 ASP C CB  1 
ATOM   4685 C CG  . ASP C 1 189 ? 5.571   33.480  74.015  1.00 70.50  ?  189 ASP C CG  1 
ATOM   4686 O OD1 . ASP C 1 189 ? 5.924   34.556  74.544  1.00 77.06  ?  189 ASP C OD1 1 
ATOM   4687 O OD2 . ASP C 1 189 ? 5.736   33.229  72.803  1.00 69.05  ?  189 ASP C OD2 1 
ATOM   4688 N N   . TYR C 1 190 ? 4.565   30.619  77.403  1.00 59.34  ?  190 TYR C N   1 
ATOM   4689 C CA  . TYR C 1 190 ? 3.791   29.622  78.131  1.00 62.32  ?  190 TYR C CA  1 
ATOM   4690 C C   . TYR C 1 190 ? 3.450   30.097  79.537  1.00 62.94  ?  190 TYR C C   1 
ATOM   4691 O O   . TYR C 1 190 ? 2.326   29.895  80.011  1.00 63.17  ?  190 TYR C O   1 
ATOM   4692 C CB  . TYR C 1 190 ? 4.559   28.301  78.185  1.00 59.95  ?  190 TYR C CB  1 
ATOM   4693 C CG  . TYR C 1 190 ? 3.876   27.226  79.004  1.00 59.63  ?  190 TYR C CG  1 
ATOM   4694 C CD1 . TYR C 1 190 ? 4.356   26.869  80.261  1.00 62.71  ?  190 TYR C CD1 1 
ATOM   4695 C CD2 . TYR C 1 190 ? 2.746   26.571  78.523  1.00 61.35  ?  190 TYR C CD2 1 
ATOM   4696 C CE1 . TYR C 1 190 ? 3.734   25.878  81.017  1.00 60.41  ?  190 TYR C CE1 1 
ATOM   4697 C CE2 . TYR C 1 190 ? 2.110   25.583  79.275  1.00 59.97  ?  190 TYR C CE2 1 
ATOM   4698 C CZ  . TYR C 1 190 ? 2.609   25.242  80.519  1.00 60.51  ?  190 TYR C CZ  1 
ATOM   4699 O OH  . TYR C 1 190 ? 1.982   24.268  81.265  1.00 58.72  ?  190 TYR C OH  1 
ATOM   4700 N N   . GLU C 1 191 ? 4.399   30.744  80.216  1.00 65.49  ?  191 GLU C N   1 
ATOM   4701 C CA  . GLU C 1 191 ? 4.154   31.208  81.576  1.00 67.34  ?  191 GLU C CA  1 
ATOM   4702 C C   . GLU C 1 191 ? 3.365   32.513  81.634  1.00 65.78  ?  191 GLU C C   1 
ATOM   4703 O O   . GLU C 1 191 ? 2.988   32.941  82.732  1.00 61.94  ?  191 GLU C O   1 
ATOM   4704 C CB  . GLU C 1 191 ? 5.480   31.348  82.336  1.00 63.19  ?  191 GLU C CB  1 
ATOM   4705 C CG  . GLU C 1 191 ? 6.265   30.039  82.451  1.00 69.41  ?  191 GLU C CG  1 
ATOM   4706 C CD  . GLU C 1 191 ? 7.484   30.144  83.363  1.00 79.39  ?  191 GLU C CD  1 
ATOM   4707 O OE1 . GLU C 1 191 ? 7.805   29.143  84.046  1.00 74.98  ?  191 GLU C OE1 1 
ATOM   4708 O OE2 . GLU C 1 191 ? 8.121   31.222  83.395  1.00 76.83  ?  191 GLU C OE2 1 
ATOM   4709 N N   . LYS C 1 192 ? 3.119   33.160  80.497  1.00 61.80  ?  192 LYS C N   1 
ATOM   4710 C CA  . LYS C 1 192 ? 2.266   34.344  80.480  1.00 63.02  ?  192 LYS C CA  1 
ATOM   4711 C C   . LYS C 1 192 ? 0.772   34.023  80.410  1.00 65.01  ?  192 LYS C C   1 
ATOM   4712 O O   . LYS C 1 192 ? -0.034  34.954  80.305  1.00 67.66  ?  192 LYS C O   1 
ATOM   4713 C CB  . LYS C 1 192 ? 2.642   35.256  79.307  1.00 67.32  ?  192 LYS C CB  1 
ATOM   4714 C CG  . LYS C 1 192 ? 3.984   35.954  79.454  1.00 65.23  ?  192 LYS C CG  1 
ATOM   4715 C CD  . LYS C 1 192 ? 4.126   37.078  78.448  1.00 72.91  ?  192 LYS C CD  1 
ATOM   4716 C CE  . LYS C 1 192 ? 3.797   36.605  77.041  1.00 78.79  ?  192 LYS C CE  1 
ATOM   4717 N NZ  . LYS C 1 192 ? 3.827   37.724  76.054  1.00 82.33  ?  192 LYS C NZ  1 
ATOM   4718 N N   . HIS C 1 193 ? 0.373   32.752  80.447  1.00 66.29  ?  193 HIS C N   1 
ATOM   4719 C CA  . HIS C 1 193 ? -1.017  32.380  80.203  1.00 63.01  ?  193 HIS C CA  1 
ATOM   4720 C C   . HIS C 1 193 ? -1.422  31.247  81.137  1.00 61.03  ?  193 HIS C C   1 
ATOM   4721 O O   . HIS C 1 193 ? -0.574  30.544  81.690  1.00 64.59  ?  193 HIS C O   1 
ATOM   4722 C CB  . HIS C 1 193 ? -1.216  31.978  78.741  1.00 57.77  ?  193 HIS C CB  1 
ATOM   4723 C CG  . HIS C 1 193 ? -0.837  33.053  77.772  1.00 60.92  ?  193 HIS C CG  1 
ATOM   4724 N ND1 . HIS C 1 193 ? 0.129   32.876  76.805  1.00 59.04  ?  193 HIS C ND1 1 
ATOM   4725 C CD2 . HIS C 1 193 ? -1.278  34.324  77.634  1.00 63.08  ?  193 HIS C CD2 1 
ATOM   4726 C CE1 . HIS C 1 193 ? 0.260   33.988  76.106  1.00 61.60  ?  193 HIS C CE1 1 
ATOM   4727 N NE2 . HIS C 1 193 ? -0.582  34.883  76.589  1.00 72.00  ?  193 HIS C NE2 1 
ATOM   4728 N N   . LYS C 1 194 ? -2.735  31.072  81.313  1.00 62.47  ?  194 LYS C N   1 
ATOM   4729 C CA  . LYS C 1 194 ? -3.260  30.144  82.313  1.00 65.65  ?  194 LYS C CA  1 
ATOM   4730 C C   . LYS C 1 194 ? -3.936  28.919  81.707  1.00 64.77  ?  194 LYS C C   1 
ATOM   4731 O O   . LYS C 1 194 ? -3.555  27.786  82.020  1.00 61.26  ?  194 LYS C O   1 
ATOM   4732 C CB  . LYS C 1 194 ? -4.246  30.858  83.254  1.00 65.86  ?  194 LYS C CB  1 
ATOM   4733 C CG  . LYS C 1 194 ? -4.594  30.018  84.491  1.00 80.89  ?  194 LYS C CG  1 
ATOM   4734 C CD  . LYS C 1 194 ? -5.531  30.724  85.474  1.00 84.96  ?  194 LYS C CD  1 
ATOM   4735 C CE  . LYS C 1 194 ? -6.995  30.364  85.213  1.00 78.88  ?  194 LYS C CE  1 
ATOM   4736 N NZ  . LYS C 1 194 ? -7.885  30.682  86.369  1.00 75.41  ?  194 LYS C NZ  1 
ATOM   4737 N N   . VAL C 1 195 ? -4.951  29.108  80.866  1.00 63.26  ?  195 VAL C N   1 
ATOM   4738 C CA  . VAL C 1 195 ? -5.810  28.023  80.400  1.00 63.16  ?  195 VAL C CA  1 
ATOM   4739 C C   . VAL C 1 195 ? -5.310  27.534  79.052  1.00 55.67  ?  195 VAL C C   1 
ATOM   4740 O O   . VAL C 1 195 ? -5.132  28.329  78.120  1.00 54.84  ?  195 VAL C O   1 
ATOM   4741 C CB  . VAL C 1 195 ? -7.278  28.474  80.300  1.00 66.85  ?  195 VAL C CB  1 
ATOM   4742 C CG1 . VAL C 1 195 ? -8.147  27.343  79.774  1.00 48.31  ?  195 VAL C CG1 1 
ATOM   4743 C CG2 . VAL C 1 195 ? -7.787  28.956  81.650  1.00 64.77  ?  195 VAL C CG2 1 
ATOM   4744 N N   . TYR C 1 196 ? -5.088  26.227  78.945  1.00 56.50  ?  196 TYR C N   1 
ATOM   4745 C CA  . TYR C 1 196 ? -4.645  25.599  77.709  1.00 56.76  ?  196 TYR C CA  1 
ATOM   4746 C C   . TYR C 1 196 ? -5.657  24.530  77.330  1.00 51.54  ?  196 TYR C C   1 
ATOM   4747 O O   . TYR C 1 196 ? -6.081  23.751  78.187  1.00 50.69  ?  196 TYR C O   1 
ATOM   4748 C CB  . TYR C 1 196 ? -3.236  25.010  77.877  1.00 55.31  ?  196 TYR C CB  1 
ATOM   4749 C CG  . TYR C 1 196 ? -2.174  26.082  78.002  1.00 57.31  ?  196 TYR C CG  1 
ATOM   4750 C CD1 . TYR C 1 196 ? -1.398  26.455  76.911  1.00 59.09  ?  196 TYR C CD1 1 
ATOM   4751 C CD2 . TYR C 1 196 ? -1.970  26.746  79.205  1.00 61.31  ?  196 TYR C CD2 1 
ATOM   4752 C CE1 . TYR C 1 196 ? -0.437  27.448  77.022  1.00 64.04  ?  196 TYR C CE1 1 
ATOM   4753 C CE2 . TYR C 1 196 ? -1.018  27.744  79.323  1.00 60.01  ?  196 TYR C CE2 1 
ATOM   4754 C CZ  . TYR C 1 196 ? -0.256  28.091  78.231  1.00 58.86  ?  196 TYR C CZ  1 
ATOM   4755 O OH  . TYR C 1 196 ? 0.692   29.078  78.353  1.00 56.25  ?  196 TYR C OH  1 
ATOM   4756 N N   . ALA C 1 197 ? -6.063  24.502  76.061  1.00 46.79  ?  197 ALA C N   1 
ATOM   4757 C CA  . ALA C 1 197 ? -7.104  23.575  75.640  1.00 46.46  ?  197 ALA C CA  1 
ATOM   4758 C C   . ALA C 1 197 ? -6.921  23.190  74.180  1.00 47.68  ?  197 ALA C C   1 
ATOM   4759 O O   . ALA C 1 197 ? -6.606  24.038  73.341  1.00 48.88  ?  197 ALA C O   1 
ATOM   4760 C CB  . ALA C 1 197 ? -8.497  24.183  75.842  1.00 47.77  ?  197 ALA C CB  1 
ATOM   4761 N N   . CYS C 1 198 ? -7.138  21.910  73.882  1.00 47.71  ?  198 CYS C N   1 
ATOM   4762 C CA  . CYS C 1 198 ? -7.250  21.444  72.506  1.00 50.03  ?  198 CYS C CA  1 
ATOM   4763 C C   . CYS C 1 198 ? -8.686  21.025  72.240  1.00 54.40  ?  198 CYS C C   1 
ATOM   4764 O O   . CYS C 1 198 ? -9.330  20.377  73.079  1.00 52.67  ?  198 CYS C O   1 
ATOM   4765 C CB  . CYS C 1 198 ? -6.294  20.285  72.173  1.00 51.02  ?  198 CYS C CB  1 
ATOM   4766 S SG  . CYS C 1 198 ? -6.470  18.772  73.131  1.00 65.44  ?  198 CYS C SG  1 
ATOM   4767 N N   . GLU C 1 199 ? -9.177  21.428  71.070  1.00 54.90  ?  199 GLU C N   1 
ATOM   4768 C CA  . GLU C 1 199 ? -10.549 21.213  70.643  1.00 51.23  ?  199 GLU C CA  1 
ATOM   4769 C C   . GLU C 1 199 ? -10.534 20.308  69.422  1.00 53.09  ?  199 GLU C C   1 
ATOM   4770 O O   . GLU C 1 199 ? -9.913  20.641  68.407  1.00 56.12  ?  199 GLU C O   1 
ATOM   4771 C CB  . GLU C 1 199 ? -11.218 22.551  70.327  1.00 53.46  ?  199 GLU C CB  1 
ATOM   4772 C CG  . GLU C 1 199 ? -12.381 22.489  69.355  1.00 60.03  ?  199 GLU C CG  1 
ATOM   4773 C CD  . GLU C 1 199 ? -13.019 23.850  69.143  1.00 70.87  ?  199 GLU C CD  1 
ATOM   4774 O OE1 . GLU C 1 199 ? -13.401 24.486  70.148  1.00 73.47  ?  199 GLU C OE1 1 
ATOM   4775 O OE2 . GLU C 1 199 ? -13.125 24.292  67.977  1.00 76.80  ?  199 GLU C OE2 1 
ATOM   4776 N N   . VAL C 1 200 ? -11.205 19.166  69.527  1.00 44.95  ?  200 VAL C N   1 
ATOM   4777 C CA  . VAL C 1 200 ? -11.326 18.194  68.452  1.00 43.64  ?  200 VAL C CA  1 
ATOM   4778 C C   . VAL C 1 200 ? -12.737 18.306  67.905  1.00 44.49  ?  200 VAL C C   1 
ATOM   4779 O O   . VAL C 1 200 ? -13.699 18.363  68.677  1.00 46.38  ?  200 VAL C O   1 
ATOM   4780 C CB  . VAL C 1 200 ? -11.039 16.765  68.949  1.00 46.57  ?  200 VAL C CB  1 
ATOM   4781 C CG1 . VAL C 1 200 ? -11.186 15.757  67.819  1.00 39.24  ?  200 VAL C CG1 1 
ATOM   4782 C CG2 . VAL C 1 200 ? -9.658  16.689  69.567  1.00 47.92  ?  200 VAL C CG2 1 
ATOM   4783 N N   . THR C 1 201 ? -12.865 18.368  66.586  1.00 47.64  ?  201 THR C N   1 
ATOM   4784 C CA  . THR C 1 201 ? -14.173 18.415  65.949  1.00 48.33  ?  201 THR C CA  1 
ATOM   4785 C C   . THR C 1 201 ? -14.245 17.295  64.929  1.00 53.64  ?  201 THR C C   1 
ATOM   4786 O O   . THR C 1 201 ? -13.345 17.148  64.097  1.00 51.94  ?  201 THR C O   1 
ATOM   4787 C CB  . THR C 1 201 ? -14.440 19.767  65.271  1.00 52.07  ?  201 THR C CB  1 
ATOM   4788 O OG1 . THR C 1 201 ? -14.329 20.823  66.233  1.00 54.99  ?  201 THR C OG1 1 
ATOM   4789 C CG2 . THR C 1 201 ? -15.832 19.793  64.655  1.00 49.21  ?  201 THR C CG2 1 
ATOM   4790 N N   . GLN C 1 202 ? -15.313 16.505  65.004  1.00 60.83  ?  202 GLN C N   1 
ATOM   4791 C CA  . GLN C 1 202 ? -15.611 15.530  63.966  1.00 62.17  ?  202 GLN C CA  1 
ATOM   4792 C C   . GLN C 1 202 ? -17.121 15.405  63.850  1.00 60.13  ?  202 GLN C C   1 
ATOM   4793 O O   . GLN C 1 202 ? -17.825 15.305  64.862  1.00 61.96  ?  202 GLN C O   1 
ATOM   4794 C CB  . GLN C 1 202 ? -14.955 14.169  64.255  1.00 52.25  ?  202 GLN C CB  1 
ATOM   4795 C CG  . GLN C 1 202 ? -15.451 13.441  65.498  1.00 62.25  ?  202 GLN C CG  1 
ATOM   4796 C CD  . GLN C 1 202 ? -14.980 11.990  65.549  1.00 73.58  ?  202 GLN C CD  1 
ATOM   4797 O OE1 . GLN C 1 202 ? -14.099 11.583  64.785  1.00 64.59  ?  202 GLN C OE1 1 
ATOM   4798 N NE2 . GLN C 1 202 ? -15.569 11.203  66.450  1.00 64.52  ?  202 GLN C NE2 1 
ATOM   4799 N N   . GLY C 1 203 ? -17.608 15.447  62.616  1.00 57.03  ?  203 GLY C N   1 
ATOM   4800 C CA  . GLY C 1 203 ? -19.041 15.399  62.392  1.00 63.48  ?  203 GLY C CA  1 
ATOM   4801 C C   . GLY C 1 203 ? -19.747 16.529  63.112  1.00 68.70  ?  203 GLY C C   1 
ATOM   4802 O O   . GLY C 1 203 ? -19.417 17.711  62.957  1.00 61.92  ?  203 GLY C O   1 
ATOM   4803 N N   . THR C 1 204 ? -20.730 16.158  63.924  1.00 76.16  ?  204 THR C N   1 
ATOM   4804 C CA  . THR C 1 204 ? -21.536 17.107  64.674  1.00 70.56  ?  204 THR C CA  1 
ATOM   4805 C C   . THR C 1 204 ? -20.994 17.367  66.074  1.00 63.31  ?  204 THR C C   1 
ATOM   4806 O O   . THR C 1 204 ? -21.614 18.119  66.834  1.00 60.62  ?  204 THR C O   1 
ATOM   4807 C CB  . THR C 1 204 ? -22.980 16.587  64.764  1.00 67.52  ?  204 THR C CB  1 
ATOM   4808 O OG1 . THR C 1 204 ? -22.983 15.259  65.305  1.00 59.33  ?  204 THR C OG1 1 
ATOM   4809 C CG2 . THR C 1 204 ? -23.607 16.538  63.379  1.00 71.99  ?  204 THR C CG2 1 
ATOM   4810 N N   . THR C 1 205 ? -19.843 16.793  66.419  1.00 63.09  ?  205 THR C N   1 
ATOM   4811 C CA  . THR C 1 205 ? -19.348 16.787  67.788  1.00 57.30  ?  205 THR C CA  1 
ATOM   4812 C C   . THR C 1 205 ? -18.050 17.574  67.906  1.00 55.37  ?  205 THR C C   1 
ATOM   4813 O O   . THR C 1 205 ? -17.188 17.516  67.021  1.00 56.92  ?  205 THR C O   1 
ATOM   4814 C CB  . THR C 1 205 ? -19.121 15.349  68.273  1.00 63.97  ?  205 THR C CB  1 
ATOM   4815 O OG1 . THR C 1 205 ? -20.318 14.585  68.086  1.00 65.10  ?  205 THR C OG1 1 
ATOM   4816 C CG2 . THR C 1 205 ? -18.728 15.324  69.747  1.00 59.38  ?  205 THR C CG2 1 
ATOM   4817 N N   . SER C 1 206 ? -17.924 18.315  69.004  1.00 52.56  ?  206 SER C N   1 
ATOM   4818 C CA  . SER C 1 206 ? -16.672 18.939  69.401  1.00 47.16  ?  206 SER C CA  1 
ATOM   4819 C C   . SER C 1 206 ? -16.392 18.585  70.853  1.00 48.28  ?  206 SER C C   1 
ATOM   4820 O O   . SER C 1 206 ? -17.258 18.747  71.715  1.00 53.43  ?  206 SER C O   1 
ATOM   4821 C CB  . SER C 1 206 ? -16.721 20.455  69.221  1.00 46.82  ?  206 SER C CB  1 
ATOM   4822 O OG  . SER C 1 206 ? -16.577 20.796  67.856  1.00 53.40  ?  206 SER C OG  1 
ATOM   4823 N N   . VAL C 1 207 ? -15.177 18.123  71.119  1.00 44.86  ?  207 VAL C N   1 
ATOM   4824 C CA  . VAL C 1 207 ? -14.719 17.785  72.460  1.00 43.80  ?  207 VAL C CA  1 
ATOM   4825 C C   . VAL C 1 207 ? -13.509 18.651  72.772  1.00 49.04  ?  207 VAL C C   1 
ATOM   4826 O O   . VAL C 1 207 ? -12.587 18.754  71.959  1.00 47.94  ?  207 VAL C O   1 
ATOM   4827 C CB  . VAL C 1 207 ? -14.364 16.292  72.582  1.00 50.31  ?  207 VAL C CB  1 
ATOM   4828 C CG1 . VAL C 1 207 ? -13.886 15.974  73.989  1.00 47.24  ?  207 VAL C CG1 1 
ATOM   4829 C CG2 . VAL C 1 207 ? -15.562 15.430  72.213  1.00 50.33  ?  207 VAL C CG2 1 
ATOM   4830 N N   . THR C 1 208 ? -13.515 19.286  73.937  1.00 50.18  ?  208 THR C N   1 
ATOM   4831 C CA  . THR C 1 208 ? -12.454 20.202  74.327  1.00 41.14  ?  208 THR C CA  1 
ATOM   4832 C C   . THR C 1 208 ? -11.847 19.747  75.647  1.00 45.30  ?  208 THR C C   1 
ATOM   4833 O O   . THR C 1 208 ? -12.543 19.686  76.668  1.00 43.59  ?  208 THR C O   1 
ATOM   4834 C CB  . THR C 1 208 ? -12.991 21.629  74.436  1.00 46.72  ?  208 THR C CB  1 
ATOM   4835 O OG1 . THR C 1 208 ? -13.335 22.100  73.130  1.00 53.55  ?  208 THR C OG1 1 
ATOM   4836 C CG2 . THR C 1 208 ? -11.950 22.552  75.051  1.00 47.41  ?  208 THR C CG2 1 
ATOM   4837 N N   . LYS C 1 209 ? -10.550 19.443  75.629  1.00 44.49  ?  209 LYS C N   1 
ATOM   4838 C CA  . LYS C 1 209 ? -9.821  19.072  76.835  1.00 42.94  ?  209 LYS C CA  1 
ATOM   4839 C C   . LYS C 1 209 ? -8.879  20.206  77.208  1.00 48.90  ?  209 LYS C C   1 
ATOM   4840 O O   . LYS C 1 209 ? -8.201  20.774  76.344  1.00 51.45  ?  209 LYS C O   1 
ATOM   4841 C CB  . LYS C 1 209 ? -9.029  17.777  76.641  1.00 44.89  ?  209 LYS C CB  1 
ATOM   4842 C CG  . LYS C 1 209 ? -9.644  16.560  77.274  1.00 49.22  ?  209 LYS C CG  1 
ATOM   4843 C CD  . LYS C 1 209 ? -9.167  16.446  78.699  1.00 52.58  ?  209 LYS C CD  1 
ATOM   4844 C CE  . LYS C 1 209 ? -10.157 15.701  79.550  1.00 53.29  ?  209 LYS C CE  1 
ATOM   4845 N NZ  . LYS C 1 209 ? -10.442 14.331  79.031  1.00 59.66  ?  209 LYS C NZ  1 
ATOM   4846 N N   . SER C 1 210 ? -8.837  20.536  78.496  1.00 45.48  ?  210 SER C N   1 
ATOM   4847 C CA  . SER C 1 210 ? -8.105  21.709  78.937  1.00 50.16  ?  210 SER C CA  1 
ATOM   4848 C C   . SER C 1 210 ? -7.403  21.422  80.253  1.00 51.49  ?  210 SER C C   1 
ATOM   4849 O O   . SER C 1 210 ? -7.632  20.401  80.905  1.00 55.46  ?  210 SER C O   1 
ATOM   4850 C CB  . SER C 1 210 ? -9.029  22.924  79.090  1.00 50.02  ?  210 SER C CB  1 
ATOM   4851 O OG  . SER C 1 210 ? -10.064 22.654  80.011  1.00 54.33  ?  210 SER C OG  1 
ATOM   4852 N N   . PHE C 1 211 ? -6.527  22.350  80.624  1.00 56.85  ?  211 PHE C N   1 
ATOM   4853 C CA  . PHE C 1 211 ? -5.908  22.374  81.938  1.00 59.55  ?  211 PHE C CA  1 
ATOM   4854 C C   . PHE C 1 211 ? -5.528  23.807  82.283  1.00 57.90  ?  211 PHE C C   1 
ATOM   4855 O O   . PHE C 1 211 ? -5.342  24.657  81.405  1.00 52.81  ?  211 PHE C O   1 
ATOM   4856 C CB  . PHE C 1 211 ? -4.687  21.446  82.023  1.00 58.72  ?  211 PHE C CB  1 
ATOM   4857 C CG  . PHE C 1 211 ? -3.498  21.906  81.219  1.00 64.51  ?  211 PHE C CG  1 
ATOM   4858 C CD1 . PHE C 1 211 ? -3.324  21.473  79.911  1.00 56.84  ?  211 PHE C CD1 1 
ATOM   4859 C CD2 . PHE C 1 211 ? -2.549  22.758  81.771  1.00 58.10  ?  211 PHE C CD2 1 
ATOM   4860 C CE1 . PHE C 1 211 ? -2.235  21.886  79.166  1.00 55.38  ?  211 PHE C CE1 1 
ATOM   4861 C CE2 . PHE C 1 211 ? -1.462  23.173  81.031  1.00 56.70  ?  211 PHE C CE2 1 
ATOM   4862 C CZ  . PHE C 1 211 ? -1.303  22.735  79.726  1.00 57.62  ?  211 PHE C CZ  1 
ATOM   4863 N N   . ASN C 1 212 ? -5.455  24.067  83.582  1.00 60.70  ?  212 ASN C N   1 
ATOM   4864 C CA  . ASN C 1 212 ? -5.060  25.356  84.128  1.00 68.82  ?  212 ASN C CA  1 
ATOM   4865 C C   . ASN C 1 212 ? -3.685  25.210  84.756  1.00 75.33  ?  212 ASN C C   1 
ATOM   4866 O O   . ASN C 1 212 ? -3.488  24.348  85.621  1.00 74.68  ?  212 ASN C O   1 
ATOM   4867 C CB  . ASN C 1 212 ? -6.062  25.846  85.170  1.00 76.03  ?  212 ASN C CB  1 
ATOM   4868 C CG  . ASN C 1 212 ? -7.406  26.170  84.575  1.00 80.43  ?  212 ASN C CG  1 
ATOM   4869 O OD1 . ASN C 1 212 ? -7.740  27.338  84.382  1.00 85.27  ?  212 ASN C OD1 1 
ATOM   4870 N ND2 . ASN C 1 212 ? -8.190  25.140  84.279  1.00 79.42  ?  212 ASN C ND2 1 
ATOM   4871 N N   . ARG C 1 213 ? -2.733  26.034  84.305  1.00 73.55  ?  213 ARG C N   1 
ATOM   4872 C CA  . ARG C 1 213 ? -1.398  26.004  84.893  1.00 69.55  ?  213 ARG C CA  1 
ATOM   4873 C C   . ARG C 1 213 ? -1.441  26.276  86.390  1.00 76.29  ?  213 ARG C C   1 
ATOM   4874 O O   . ARG C 1 213 ? -0.608  25.754  87.139  1.00 76.47  ?  213 ARG C O   1 
ATOM   4875 C CB  . ARG C 1 213 ? -0.491  27.018  84.201  1.00 67.07  ?  213 ARG C CB  1 
ATOM   4876 C CG  . ARG C 1 213 ? -0.048  26.621  82.809  1.00 64.72  ?  213 ARG C CG  1 
ATOM   4877 C CD  . ARG C 1 213 ? 1.026   27.560  82.247  1.00 66.22  ?  213 ARG C CD  1 
ATOM   4878 N NE  . ARG C 1 213 ? 1.072   28.879  82.874  1.00 70.36  ?  213 ARG C NE  1 
ATOM   4879 C CZ  . ARG C 1 213 ? 1.945   29.225  83.815  1.00 67.34  ?  213 ARG C CZ  1 
ATOM   4880 N NH1 . ARG C 1 213 ? 2.838   28.341  84.242  1.00 67.40  ?  213 ARG C NH1 1 
ATOM   4881 N NH2 . ARG C 1 213 ? 1.921   30.447  84.330  1.00 60.70  ?  213 ARG C NH2 1 
ATOM   4882 N N   . GLY C 1 214 ? -2.401  27.081  86.839  1.00 85.30  ?  214 GLY C N   1 
ATOM   4883 C CA  . GLY C 1 214 ? -2.531  27.415  88.242  1.00 89.67  ?  214 GLY C CA  1 
ATOM   4884 C C   . GLY C 1 214 ? -3.523  26.537  88.980  1.00 94.64  ?  214 GLY C C   1 
ATOM   4885 O O   . GLY C 1 214 ? -4.141  26.973  89.958  1.00 93.75  ?  214 GLY C O   1 
ATOM   4886 N N   . GLU C 1 215 ? -3.693  25.301  88.514  1.00 96.55  ?  215 GLU C N   1 
ATOM   4887 C CA  . GLU C 1 215 ? -4.572  24.328  89.152  1.00 95.55  ?  215 GLU C CA  1 
ATOM   4888 C C   . GLU C 1 215 ? -3.986  22.926  89.014  1.00 92.26  ?  215 GLU C C   1 
ATOM   4889 O O   . GLU C 1 215 ? -4.479  21.971  89.612  1.00 101.03 ?  215 GLU C O   1 
ATOM   4890 C CB  . GLU C 1 215 ? -5.988  24.372  88.555  1.00 95.30  ?  215 GLU C CB  1 
ATOM   4891 C CG  . GLU C 1 215 ? -6.743  25.681  88.793  1.00 96.40  ?  215 GLU C CG  1 
ATOM   4892 C CD  . GLU C 1 215 ? -8.108  25.701  88.129  1.00 101.87 ?  215 GLU C CD  1 
ATOM   4893 O OE1 . GLU C 1 215 ? -8.412  24.769  87.357  1.00 103.53 ?  215 GLU C OE1 1 
ATOM   4894 O OE2 . GLU C 1 215 ? -8.873  26.663  88.374  1.00 100.96 ?  215 GLU C OE2 1 
ATOM   4895 N N   . GLU D 2 1   ? 14.691  -18.953 53.490  1.00 68.73  ?  1   GLU D N   1 
ATOM   4896 C CA  . GLU D 2 1   ? 15.936  -18.810 54.237  1.00 73.67  ?  1   GLU D CA  1 
ATOM   4897 C C   . GLU D 2 1   ? 16.912  -17.894 53.495  1.00 66.74  ?  1   GLU D C   1 
ATOM   4898 O O   . GLU D 2 1   ? 17.955  -17.509 54.027  1.00 66.32  ?  1   GLU D O   1 
ATOM   4899 C CB  . GLU D 2 1   ? 16.565  -20.182 54.479  1.00 85.44  ?  1   GLU D CB  1 
ATOM   4900 C CG  . GLU D 2 1   ? 15.680  -21.124 55.283  1.00 98.46  ?  1   GLU D CG  1 
ATOM   4901 C CD  . GLU D 2 1   ? 16.360  -22.444 55.601  1.00 109.61 ?  1   GLU D CD  1 
ATOM   4902 O OE1 . GLU D 2 1   ? 15.705  -23.499 55.451  1.00 106.30 ?  1   GLU D OE1 1 
ATOM   4903 O OE2 . GLU D 2 1   ? 17.552  -22.427 55.982  1.00 107.10 ?  1   GLU D OE2 1 
ATOM   4904 N N   . VAL D 2 2   ? 16.563  -17.549 52.264  1.00 59.72  ?  2   VAL D N   1 
ATOM   4905 C CA  . VAL D 2 2   ? 17.308  -16.550 51.512  1.00 53.36  ?  2   VAL D CA  1 
ATOM   4906 C C   . VAL D 2 2   ? 16.970  -15.174 52.068  1.00 46.40  ?  2   VAL D C   1 
ATOM   4907 O O   . VAL D 2 2   ? 15.862  -14.939 52.557  1.00 47.65  ?  2   VAL D O   1 
ATOM   4908 C CB  . VAL D 2 2   ? 16.997  -16.644 50.005  1.00 45.19  ?  2   VAL D CB  1 
ATOM   4909 C CG1 . VAL D 2 2   ? 17.409  -17.997 49.467  1.00 44.65  ?  2   VAL D CG1 1 
ATOM   4910 C CG2 . VAL D 2 2   ? 15.522  -16.401 49.754  1.00 42.09  ?  2   VAL D CG2 1 
ATOM   4911 N N   . GLN D 2 3   ? 17.933  -14.257 52.023  1.00 52.05  ?  3   GLN D N   1 
ATOM   4912 C CA  . GLN D 2 3   ? 17.655  -12.900 52.473  1.00 49.36  ?  3   GLN D CA  1 
ATOM   4913 C C   . GLN D 2 3   ? 18.563  -11.920 51.748  1.00 45.06  ?  3   GLN D C   1 
ATOM   4914 O O   . GLN D 2 3   ? 19.619  -12.280 51.223  1.00 44.06  ?  3   GLN D O   1 
ATOM   4915 C CB  . GLN D 2 3   ? 17.804  -12.745 53.995  1.00 52.47  ?  3   GLN D CB  1 
ATOM   4916 C CG  . GLN D 2 3   ? 19.214  -12.904 54.541  1.00 55.58  ?  3   GLN D CG  1 
ATOM   4917 C CD  . GLN D 2 3   ? 19.291  -12.643 56.041  1.00 62.99  ?  3   GLN D CD  1 
ATOM   4918 O OE1 . GLN D 2 3   ? 18.299  -12.271 56.670  1.00 63.75  ?  3   GLN D OE1 1 
ATOM   4919 N NE2 . GLN D 2 3   ? 20.469  -12.853 56.622  1.00 62.57  ?  3   GLN D NE2 1 
ATOM   4920 N N   . LEU D 2 4   ? 18.098  -10.677 51.682  1.00 49.03  ?  4   LEU D N   1 
ATOM   4921 C CA  . LEU D 2 4   ? 18.845  -9.556  51.134  1.00 43.83  ?  4   LEU D CA  1 
ATOM   4922 C C   . LEU D 2 4   ? 19.020  -8.531  52.242  1.00 42.63  ?  4   LEU D C   1 
ATOM   4923 O O   . LEU D 2 4   ? 18.038  -8.126  52.871  1.00 46.34  ?  4   LEU D O   1 
ATOM   4924 C CB  . LEU D 2 4   ? 18.106  -8.940  49.944  1.00 35.96  ?  4   LEU D CB  1 
ATOM   4925 C CG  . LEU D 2 4   ? 18.002  -9.772  48.672  1.00 36.95  ?  4   LEU D CG  1 
ATOM   4926 C CD1 . LEU D 2 4   ? 16.935  -9.186  47.764  1.00 37.71  ?  4   LEU D CD1 1 
ATOM   4927 C CD2 . LEU D 2 4   ? 19.340  -9.839  47.961  1.00 38.15  ?  4   LEU D CD2 1 
ATOM   4928 N N   . VAL D 2 5   ? 20.256  -8.122  52.497  1.00 40.15  ?  5   VAL D N   1 
ATOM   4929 C CA  . VAL D 2 5   ? 20.547  -7.172  53.568  1.00 49.49  ?  5   VAL D CA  1 
ATOM   4930 C C   . VAL D 2 5   ? 21.237  -5.957  52.960  1.00 46.10  ?  5   VAL D C   1 
ATOM   4931 O O   . VAL D 2 5   ? 22.368  -6.061  52.475  1.00 44.74  ?  5   VAL D O   1 
ATOM   4932 C CB  . VAL D 2 5   ? 21.405  -7.798  54.675  1.00 47.26  ?  5   VAL D CB  1 
ATOM   4933 C CG1 . VAL D 2 5   ? 21.695  -6.775  55.756  1.00 48.54  ?  5   VAL D CG1 1 
ATOM   4934 C CG2 . VAL D 2 5   ? 20.687  -8.993  55.269  1.00 44.87  ?  5   VAL D CG2 1 
ATOM   4935 N N   . GLU D 2 6   ? 20.567  -4.808  52.986  1.00 42.97  ?  6   GLU D N   1 
ATOM   4936 C CA  . GLU D 2 6   ? 21.171  -3.581  52.491  1.00 40.08  ?  6   GLU D CA  1 
ATOM   4937 C C   . GLU D 2 6   ? 21.926  -2.883  53.607  1.00 43.06  ?  6   GLU D C   1 
ATOM   4938 O O   . GLU D 2 6   ? 21.609  -3.023  54.792  1.00 47.56  ?  6   GLU D O   1 
ATOM   4939 C CB  . GLU D 2 6   ? 20.131  -2.603  51.938  1.00 40.00  ?  6   GLU D CB  1 
ATOM   4940 C CG  . GLU D 2 6   ? 19.309  -3.106  50.788  1.00 42.35  ?  6   GLU D CG  1 
ATOM   4941 C CD  . GLU D 2 6   ? 17.994  -3.682  51.247  1.00 45.00  ?  6   GLU D CD  1 
ATOM   4942 O OE1 . GLU D 2 6   ? 17.928  -4.157  52.401  1.00 47.65  ?  6   GLU D OE1 1 
ATOM   4943 O OE2 . GLU D 2 6   ? 17.022  -3.643  50.464  1.00 42.98  ?  6   GLU D OE2 1 
ATOM   4944 N N   . SER D 2 7   ? 22.942  -2.131  53.210  1.00 37.92  ?  7   SER D N   1 
ATOM   4945 C CA  . SER D 2 7   ? 23.697  -1.298  54.130  1.00 39.74  ?  7   SER D CA  1 
ATOM   4946 C C   . SER D 2 7   ? 24.320  -0.177  53.316  1.00 40.22  ?  7   SER D C   1 
ATOM   4947 O O   . SER D 2 7   ? 24.190  -0.125  52.088  1.00 42.42  ?  7   SER D O   1 
ATOM   4948 C CB  . SER D 2 7   ? 24.747  -2.102  54.897  1.00 38.62  ?  7   SER D CB  1 
ATOM   4949 O OG  . SER D 2 7   ? 25.941  -2.181  54.154  1.00 44.25  ?  7   SER D OG  1 
ATOM   4950 N N   . GLY D 2 8   ? 25.041  0.691   54.004  1.00 39.48  ?  8   GLY D N   1 
ATOM   4951 C CA  . GLY D 2 8   ? 25.331  1.990   53.454  1.00 37.81  ?  8   GLY D CA  1 
ATOM   4952 C C   . GLY D 2 8   ? 24.155  2.895   53.754  1.00 50.45  ?  8   GLY D C   1 
ATOM   4953 O O   . GLY D 2 8   ? 23.270  2.570   54.550  1.00 59.94  ?  8   GLY D O   1 
ATOM   4954 N N   . GLY D 2 9   ? 24.136  4.045   53.104  1.00 46.60  ?  9   GLY D N   1 
ATOM   4955 C CA  . GLY D 2 9   ? 23.014  4.919   53.347  1.00 50.80  ?  9   GLY D CA  1 
ATOM   4956 C C   . GLY D 2 9   ? 23.114  5.621   54.683  1.00 55.04  ?  9   GLY D C   1 
ATOM   4957 O O   . GLY D 2 9   ? 23.697  5.109   55.643  1.00 51.80  ?  9   GLY D O   1 
ATOM   4958 N N   . GLY D 2 10  ? 22.548  6.806   54.739  1.00 48.35  ?  10  GLY D N   1 
ATOM   4959 C CA  . GLY D 2 10  ? 22.717  7.697   55.854  1.00 34.39  ?  10  GLY D CA  1 
ATOM   4960 C C   . GLY D 2 10  ? 22.656  9.117   55.345  1.00 44.25  ?  10  GLY D C   1 
ATOM   4961 O O   . GLY D 2 10  ? 22.155  9.367   54.253  1.00 47.73  ?  10  GLY D O   1 
ATOM   4962 N N   . LEU D 2 11  ? 23.198  10.025  56.150  1.00 42.33  ?  11  LEU D N   1 
ATOM   4963 C CA  . LEU D 2 11  ? 23.208  11.440  55.816  1.00 37.17  ?  11  LEU D CA  1 
ATOM   4964 C C   . LEU D 2 11  ? 24.329  11.730  54.829  1.00 40.82  ?  11  LEU D C   1 
ATOM   4965 O O   . LEU D 2 11  ? 25.477  11.337  55.049  1.00 39.43  ?  11  LEU D O   1 
ATOM   4966 C CB  . LEU D 2 11  ? 23.375  12.272  57.082  1.00 41.12  ?  11  LEU D CB  1 
ATOM   4967 C CG  . LEU D 2 11  ? 23.294  13.792  56.981  1.00 38.94  ?  11  LEU D CG  1 
ATOM   4968 C CD1 . LEU D 2 11  ? 22.103  14.227  56.140  1.00 43.38  ?  11  LEU D CD1 1 
ATOM   4969 C CD2 . LEU D 2 11  ? 23.181  14.356  58.386  1.00 38.08  ?  11  LEU D CD2 1 
ATOM   4970 N N   . VAL D 2 12  ? 23.987  12.387  53.725  1.00 42.35  ?  12  VAL D N   1 
ATOM   4971 C CA  . VAL D 2 12  ? 24.953  12.775  52.705  1.00 45.09  ?  12  VAL D CA  1 
ATOM   4972 C C   . VAL D 2 12  ? 24.706  14.225  52.313  1.00 48.02  ?  12  VAL D C   1 
ATOM   4973 O O   . VAL D 2 12  ? 23.555  14.665  52.202  1.00 44.42  ?  12  VAL D O   1 
ATOM   4974 C CB  . VAL D 2 12  ? 24.884  11.862  51.460  1.00 42.96  ?  12  VAL D CB  1 
ATOM   4975 C CG1 . VAL D 2 12  ? 25.977  12.227  50.477  1.00 41.53  ?  12  VAL D CG1 1 
ATOM   4976 C CG2 . VAL D 2 12  ? 25.022  10.417  51.862  1.00 50.96  ?  12  VAL D CG2 1 
ATOM   4977 N N   . GLN D 2 13  ? 25.793  14.966  52.110  1.00 51.14  ?  13  GLN D N   1 
ATOM   4978 C CA  . GLN D 2 13  ? 25.694  16.357  51.707  1.00 50.37  ?  13  GLN D CA  1 
ATOM   4979 C C   . GLN D 2 13  ? 25.251  16.432  50.245  1.00 47.57  ?  13  GLN D C   1 
ATOM   4980 O O   . GLN D 2 13  ? 25.613  15.571  49.438  1.00 46.46  ?  13  GLN D O   1 
ATOM   4981 C CB  . GLN D 2 13  ? 27.050  17.040  51.861  1.00 58.12  ?  13  GLN D CB  1 
ATOM   4982 C CG  . GLN D 2 13  ? 27.591  17.072  53.279  1.00 72.65  ?  13  GLN D CG  1 
ATOM   4983 C CD  . GLN D 2 13  ? 28.938  17.762  53.362  1.00 85.72  ?  13  GLN D CD  1 
ATOM   4984 O OE1 . GLN D 2 13  ? 29.447  18.273  52.362  1.00 81.63  ?  13  GLN D OE1 1 
ATOM   4985 N NE2 . GLN D 2 13  ? 29.536  17.754  54.548  1.00 88.66  ?  13  GLN D NE2 1 
ATOM   4986 N N   . PRO D 2 14  ? 24.457  17.445  49.880  1.00 47.02  ?  14  PRO D N   1 
ATOM   4987 C CA  . PRO D 2 14  ? 24.076  17.595  48.470  1.00 44.20  ?  14  PRO D CA  1 
ATOM   4988 C C   . PRO D 2 14  ? 25.309  17.664  47.591  1.00 45.92  ?  14  PRO D C   1 
ATOM   4989 O O   . PRO D 2 14  ? 26.314  18.280  47.943  1.00 46.48  ?  14  PRO D O   1 
ATOM   4990 C CB  . PRO D 2 14  ? 23.286  18.907  48.446  1.00 38.17  ?  14  PRO D CB  1 
ATOM   4991 C CG  . PRO D 2 14  ? 22.729  19.022  49.820  1.00 43.23  ?  14  PRO D CG  1 
ATOM   4992 C CD  . PRO D 2 14  ? 23.783  18.447  50.734  1.00 47.42  ?  14  PRO D CD  1 
ATOM   4993 N N   . GLY D 2 15  ? 25.233  16.999  46.438  1.00 45.77  ?  15  GLY D N   1 
ATOM   4994 C CA  . GLY D 2 15  ? 26.374  16.891  45.564  1.00 45.52  ?  15  GLY D CA  1 
ATOM   4995 C C   . GLY D 2 15  ? 27.338  15.777  45.903  1.00 47.50  ?  15  GLY D C   1 
ATOM   4996 O O   . GLY D 2 15  ? 28.196  15.449  45.070  1.00 51.16  ?  15  GLY D O   1 
ATOM   4997 N N   . GLY D 2 16  ? 27.250  15.198  47.096  1.00 46.48  ?  16  GLY D N   1 
ATOM   4998 C CA  . GLY D 2 16  ? 28.153  14.145  47.498  1.00 46.52  ?  16  GLY D CA  1 
ATOM   4999 C C   . GLY D 2 16  ? 27.848  12.812  46.833  1.00 47.69  ?  16  GLY D C   1 
ATOM   5000 O O   . GLY D 2 16  ? 26.935  12.662  46.021  1.00 50.30  ?  16  GLY D O   1 
ATOM   5001 N N   . SER D 2 17  ? 28.653  11.818  47.197  1.00 51.70  ?  17  SER D N   1 
ATOM   5002 C CA  . SER D 2 17  ? 28.542  10.468  46.666  1.00 49.57  ?  17  SER D CA  1 
ATOM   5003 C C   . SER D 2 17  ? 28.199  9.483   47.772  1.00 51.69  ?  17  SER D C   1 
ATOM   5004 O O   . SER D 2 17  ? 28.416  9.734   48.960  1.00 57.13  ?  17  SER D O   1 
ATOM   5005 C CB  . SER D 2 17  ? 29.838  10.011  45.983  1.00 47.71  ?  17  SER D CB  1 
ATOM   5006 O OG  . SER D 2 17  ? 29.822  10.306  44.601  1.00 58.62  ?  17  SER D OG  1 
ATOM   5007 N N   . LEU D 2 18  ? 27.665  8.342   47.353  1.00 48.32  ?  18  LEU D N   1 
ATOM   5008 C CA  . LEU D 2 18  ? 27.318  7.286   48.284  1.00 49.78  ?  18  LEU D CA  1 
ATOM   5009 C C   . LEU D 2 18  ? 27.371  5.957   47.548  1.00 49.27  ?  18  LEU D C   1 
ATOM   5010 O O   . LEU D 2 18  ? 27.115  5.892   46.344  1.00 50.27  ?  18  LEU D O   1 
ATOM   5011 C CB  . LEU D 2 18  ? 25.930  7.522   48.884  1.00 48.62  ?  18  LEU D CB  1 
ATOM   5012 C CG  . LEU D 2 18  ? 25.657  6.792   50.189  1.00 53.58  ?  18  LEU D CG  1 
ATOM   5013 C CD1 . LEU D 2 18  ? 26.741  7.141   51.192  1.00 56.93  ?  18  LEU D CD1 1 
ATOM   5014 C CD2 . LEU D 2 18  ? 24.281  7.158   50.711  1.00 48.15  ?  18  LEU D CD2 1 
ATOM   5015 N N   . ARG D 2 19  ? 27.715  4.895   48.271  1.00 44.86  ?  19  ARG D N   1 
ATOM   5016 C CA  . ARG D 2 19  ? 27.654  3.550   47.709  1.00 41.44  ?  19  ARG D CA  1 
ATOM   5017 C C   . ARG D 2 19  ? 26.813  2.683   48.630  1.00 39.63  ?  19  ARG D C   1 
ATOM   5018 O O   . ARG D 2 19  ? 27.181  2.461   49.787  1.00 40.58  ?  19  ARG D O   1 
ATOM   5019 C CB  . ARG D 2 19  ? 29.042  2.953   47.510  1.00 48.55  ?  19  ARG D CB  1 
ATOM   5020 C CG  . ARG D 2 19  ? 29.043  1.754   46.573  1.00 41.55  ?  19  ARG D CG  1 
ATOM   5021 C CD  . ARG D 2 19  ? 30.447  1.310   46.255  1.00 43.05  ?  19  ARG D CD  1 
ATOM   5022 N NE  . ARG D 2 19  ? 30.920  0.323   47.216  1.00 56.04  ?  19  ARG D NE  1 
ATOM   5023 C CZ  . ARG D 2 19  ? 31.933  0.523   48.052  1.00 69.25  ?  19  ARG D CZ  1 
ATOM   5024 N NH1 . ARG D 2 19  ? 32.583  1.681   48.038  1.00 78.31  ?  19  ARG D NH1 1 
ATOM   5025 N NH2 . ARG D 2 19  ? 32.299  -0.434  48.895  1.00 67.50  ?  19  ARG D NH2 1 
ATOM   5026 N N   . LEU D 2 20  ? 25.668  2.233   48.126  1.00 37.13  ?  20  LEU D N   1 
ATOM   5027 C CA  . LEU D 2 20  ? 24.827  1.265   48.808  1.00 36.49  ?  20  LEU D CA  1 
ATOM   5028 C C   . LEU D 2 20  ? 25.283  -0.150  48.477  1.00 42.33  ?  20  LEU D C   1 
ATOM   5029 O O   . LEU D 2 20  ? 25.667  -0.447  47.341  1.00 38.05  ?  20  LEU D O   1 
ATOM   5030 C CB  . LEU D 2 20  ? 23.369  1.446   48.395  1.00 34.85  ?  20  LEU D CB  1 
ATOM   5031 C CG  . LEU D 2 20  ? 22.729  2.794   48.708  1.00 40.16  ?  20  LEU D CG  1 
ATOM   5032 C CD1 . LEU D 2 20  ? 21.278  2.800   48.260  1.00 33.82  ?  20  LEU D CD1 1 
ATOM   5033 C CD2 . LEU D 2 20  ? 22.829  3.083   50.191  1.00 40.50  ?  20  LEU D CD2 1 
ATOM   5034 N N   . SER D 2 21  ? 25.224  -1.029  49.468  1.00 40.89  ?  21  SER D N   1 
ATOM   5035 C CA  . SER D 2 21  ? 25.574  -2.418  49.246  1.00 37.09  ?  21  SER D CA  1 
ATOM   5036 C C   . SER D 2 21  ? 24.421  -3.298  49.694  1.00 38.00  ?  21  SER D C   1 
ATOM   5037 O O   . SER D 2 21  ? 23.572  -2.897  50.491  1.00 44.75  ?  21  SER D O   1 
ATOM   5038 C CB  . SER D 2 21  ? 26.859  -2.806  49.983  1.00 36.49  ?  21  SER D CB  1 
ATOM   5039 O OG  . SER D 2 21  ? 26.733  -2.547  51.366  1.00 46.22  ?  21  SER D OG  1 
ATOM   5040 N N   . CYS D 2 22  ? 24.410  -4.510  49.161  1.00 38.98  ?  22  CYS D N   1 
ATOM   5041 C CA  . CYS D 2 22  ? 23.336  -5.459  49.416  1.00 44.15  ?  22  CYS D CA  1 
ATOM   5042 C C   . CYS D 2 22  ? 23.950  -6.851  49.426  1.00 41.51  ?  22  CYS D C   1 
ATOM   5043 O O   . CYS D 2 22  ? 24.408  -7.334  48.386  1.00 40.65  ?  22  CYS D O   1 
ATOM   5044 C CB  . CYS D 2 22  ? 22.245  -5.337  48.357  1.00 42.33  ?  22  CYS D CB  1 
ATOM   5045 S SG  . CYS D 2 22  ? 20.938  -6.558  48.497  1.00 60.49  ?  22  CYS D SG  1 
ATOM   5046 N N   . ALA D 2 23  ? 23.982  -7.479  50.597  1.00 39.29  ?  23  ALA D N   1 
ATOM   5047 C CA  . ALA D 2 23  ? 24.498  -8.833  50.743  1.00 36.83  ?  23  ALA D CA  1 
ATOM   5048 C C   . ALA D 2 23  ? 23.364  -9.817  50.504  1.00 38.59  ?  23  ALA D C   1 
ATOM   5049 O O   . ALA D 2 23  ? 22.324  -9.747  51.169  1.00 44.38  ?  23  ALA D O   1 
ATOM   5050 C CB  . ALA D 2 23  ? 25.105  -9.047  52.126  1.00 34.32  ?  23  ALA D CB  1 
ATOM   5051 N N   . ALA D 2 24  ? 23.556  -10.703 49.533  1.00 35.69  ?  24  ALA D N   1 
ATOM   5052 C CA  . ALA D 2 24  ? 22.631  -11.795 49.278  1.00 39.35  ?  24  ALA D CA  1 
ATOM   5053 C C   . ALA D 2 24  ? 23.081  -13.004 50.084  1.00 38.53  ?  24  ALA D C   1 
ATOM   5054 O O   . ALA D 2 24  ? 24.255  -13.379 50.041  1.00 40.55  ?  24  ALA D O   1 
ATOM   5055 C CB  . ALA D 2 24  ? 22.583  -12.132 47.786  1.00 40.34  ?  24  ALA D CB  1 
ATOM   5056 N N   . SER D 2 25  ? 22.155  -13.605 50.820  1.00 40.80  ?  25  SER D N   1 
ATOM   5057 C CA  . SER D 2 25  ? 22.454  -14.753 51.663  1.00 43.16  ?  25  SER D CA  1 
ATOM   5058 C C   . SER D 2 25  ? 21.550  -15.912 51.270  1.00 48.73  ?  25  SER D C   1 
ATOM   5059 O O   . SER D 2 25  ? 20.320  -15.776 51.280  1.00 49.56  ?  25  SER D O   1 
ATOM   5060 C CB  . SER D 2 25  ? 22.272  -14.407 53.140  1.00 42.05  ?  25  SER D CB  1 
ATOM   5061 O OG  . SER D 2 25  ? 22.365  -15.571 53.938  1.00 55.64  ?  25  SER D OG  1 
ATOM   5062 N N   . GLY D 2 26  ? 22.160  -17.041 50.909  1.00 40.60  ?  26  GLY D N   1 
ATOM   5063 C CA  . GLY D 2 26  ? 21.426  -18.263 50.665  1.00 36.01  ?  26  GLY D CA  1 
ATOM   5064 C C   . GLY D 2 26  ? 21.171  -18.593 49.214  1.00 37.48  ?  26  GLY D C   1 
ATOM   5065 O O   . GLY D 2 26  ? 20.557  -19.629 48.936  1.00 39.28  ?  26  GLY D O   1 
ATOM   5066 N N   . PHE D 2 27  ? 21.595  -17.746 48.284  1.00 39.18  ?  27  PHE D N   1 
ATOM   5067 C CA  . PHE D 2 27  ? 21.398  -18.022 46.870  1.00 39.60  ?  27  PHE D CA  1 
ATOM   5068 C C   . PHE D 2 27  ? 22.499  -17.326 46.082  1.00 41.28  ?  27  PHE D C   1 
ATOM   5069 O O   . PHE D 2 27  ? 23.247  -16.497 46.608  1.00 36.04  ?  27  PHE D O   1 
ATOM   5070 C CB  . PHE D 2 27  ? 20.003  -17.585 46.394  1.00 36.38  ?  27  PHE D CB  1 
ATOM   5071 C CG  . PHE D 2 27  ? 19.811  -16.096 46.349  1.00 39.48  ?  27  PHE D CG  1 
ATOM   5072 C CD1 . PHE D 2 27  ? 19.565  -15.377 47.509  1.00 37.57  ?  27  PHE D CD1 1 
ATOM   5073 C CD2 . PHE D 2 27  ? 19.860  -15.416 45.143  1.00 39.98  ?  27  PHE D CD2 1 
ATOM   5074 C CE1 . PHE D 2 27  ? 19.387  -14.006 47.464  1.00 40.58  ?  27  PHE D CE1 1 
ATOM   5075 C CE2 . PHE D 2 27  ? 19.686  -14.043 45.093  1.00 38.88  ?  27  PHE D CE2 1 
ATOM   5076 C CZ  . PHE D 2 27  ? 19.448  -13.339 46.255  1.00 39.78  ?  27  PHE D CZ  1 
ATOM   5077 N N   . SER D 2 28  ? 22.582  -17.673 44.801  1.00 44.00  ?  28  SER D N   1 
ATOM   5078 C CA  . SER D 2 28  ? 23.635  -17.183 43.923  1.00 42.03  ?  28  SER D CA  1 
ATOM   5079 C C   . SER D 2 28  ? 23.187  -15.874 43.284  1.00 35.36  ?  28  SER D C   1 
ATOM   5080 O O   . SER D 2 28  ? 22.376  -15.878 42.351  1.00 34.07  ?  28  SER D O   1 
ATOM   5081 C CB  . SER D 2 28  ? 23.975  -18.223 42.859  1.00 39.95  ?  28  SER D CB  1 
ATOM   5082 O OG  . SER D 2 28  ? 25.133  -17.838 42.143  1.00 46.80  ?  28  SER D OG  1 
ATOM   5083 N N   . LEU D 2 29  ? 23.744  -14.761 43.767  1.00 35.58  ?  29  LEU D N   1 
ATOM   5084 C CA  . LEU D 2 29  ? 23.296  -13.442 43.333  1.00 38.71  ?  29  LEU D CA  1 
ATOM   5085 C C   . LEU D 2 29  ? 23.394  -13.273 41.823  1.00 40.49  ?  29  LEU D C   1 
ATOM   5086 O O   . LEU D 2 29  ? 22.488  -12.710 41.195  1.00 43.31  ?  29  LEU D O   1 
ATOM   5087 C CB  . LEU D 2 29  ? 24.120  -12.366 44.026  1.00 38.83  ?  29  LEU D CB  1 
ATOM   5088 C CG  . LEU D 2 29  ? 23.766  -10.912 43.714  1.00 40.47  ?  29  LEU D CG  1 
ATOM   5089 C CD1 . LEU D 2 29  ? 22.477  -10.538 44.415  1.00 39.64  ?  29  LEU D CD1 1 
ATOM   5090 C CD2 . LEU D 2 29  ? 24.902  -9.996  44.135  1.00 37.77  ?  29  LEU D CD2 1 
ATOM   5091 N N   . SER D 2 30  ? 24.473  -13.766 41.218  1.00 35.87  ?  30  SER D N   1 
ATOM   5092 C CA  . SER D 2 30  ? 24.730  -13.483 39.810  1.00 36.53  ?  30  SER D CA  1 
ATOM   5093 C C   . SER D 2 30  ? 23.821  -14.244 38.851  1.00 40.31  ?  30  SER D C   1 
ATOM   5094 O O   . SER D 2 30  ? 23.924  -14.020 37.640  1.00 47.33  ?  30  SER D O   1 
ATOM   5095 C CB  . SER D 2 30  ? 26.198  -13.771 39.471  1.00 44.87  ?  30  SER D CB  1 
ATOM   5096 O OG  . SER D 2 30  ? 26.513  -15.148 39.586  1.00 45.47  ?  30  SER D OG  1 
ATOM   5097 N N   . SER D 2 31  ? 22.952  -15.136 39.322  1.00 37.73  ?  31  SER D N   1 
ATOM   5098 C CA  . SER D 2 31  ? 22.071  -15.873 38.425  1.00 41.07  ?  31  SER D CA  1 
ATOM   5099 C C   . SER D 2 31  ? 20.630  -15.389 38.507  1.00 42.26  ?  31  SER D C   1 
ATOM   5100 O O   . SER D 2 31  ? 19.713  -16.091 38.068  1.00 44.87  ?  31  SER D O   1 
ATOM   5101 C CB  . SER D 2 31  ? 22.139  -17.374 38.707  1.00 45.14  ?  31  SER D CB  1 
ATOM   5102 O OG  . SER D 2 31  ? 21.652  -17.661 40.001  1.00 48.83  ?  31  SER D OG  1 
ATOM   5103 N N   . TYR D 2 32  ? 20.413  -14.203 39.058  1.00 41.94  ?  32  TYR D N   1 
ATOM   5104 C CA  . TYR D 2 32  ? 19.108  -13.571 39.059  1.00 39.51  ?  32  TYR D CA  1 
ATOM   5105 C C   . TYR D 2 32  ? 19.259  -12.165 38.505  1.00 36.39  ?  32  TYR D C   1 
ATOM   5106 O O   . TYR D 2 32  ? 20.347  -11.582 38.532  1.00 43.64  ?  32  TYR D O   1 
ATOM   5107 C CB  . TYR D 2 32  ? 18.493  -13.515 40.463  1.00 39.25  ?  32  TYR D CB  1 
ATOM   5108 C CG  . TYR D 2 32  ? 18.040  -14.855 40.989  1.00 38.53  ?  32  TYR D CG  1 
ATOM   5109 C CD1 . TYR D 2 32  ? 16.716  -15.253 40.887  1.00 39.45  ?  32  TYR D CD1 1 
ATOM   5110 C CD2 . TYR D 2 32  ? 18.939  -15.723 41.587  1.00 43.09  ?  32  TYR D CD2 1 
ATOM   5111 C CE1 . TYR D 2 32  ? 16.304  -16.472 41.368  1.00 40.85  ?  32  TYR D CE1 1 
ATOM   5112 C CE2 . TYR D 2 32  ? 18.538  -16.949 42.066  1.00 41.30  ?  32  TYR D CE2 1 
ATOM   5113 C CZ  . TYR D 2 32  ? 17.224  -17.320 41.953  1.00 41.83  ?  32  TYR D CZ  1 
ATOM   5114 O OH  . TYR D 2 32  ? 16.833  -18.542 42.440  1.00 43.13  ?  32  TYR D OH  1 
ATOM   5115 N N   . TYR D 2 33  ? 18.156  -11.633 37.982  1.00 30.41  ?  33  TYR D N   1 
ATOM   5116 C CA  . TYR D 2 33  ? 18.069  -10.208 37.692  1.00 34.11  ?  33  TYR D CA  1 
ATOM   5117 C C   . TYR D 2 33  ? 17.926  -9.455  39.010  1.00 36.48  ?  33  TYR D C   1 
ATOM   5118 O O   . TYR D 2 33  ? 17.027  -9.751  39.804  1.00 39.72  ?  33  TYR D O   1 
ATOM   5119 C CB  . TYR D 2 33  ? 16.887  -9.926  36.769  1.00 35.22  ?  33  TYR D CB  1 
ATOM   5120 C CG  . TYR D 2 33  ? 17.128  -10.262 35.309  1.00 36.86  ?  33  TYR D CG  1 
ATOM   5121 C CD1 . TYR D 2 33  ? 16.592  -9.467  34.301  1.00 38.10  ?  33  TYR D CD1 1 
ATOM   5122 C CD2 . TYR D 2 33  ? 17.884  -11.375 34.936  1.00 33.05  ?  33  TYR D CD2 1 
ATOM   5123 C CE1 . TYR D 2 33  ? 16.802  -9.763  32.959  1.00 40.56  ?  33  TYR D CE1 1 
ATOM   5124 C CE2 . TYR D 2 33  ? 18.100  -11.681 33.595  1.00 34.51  ?  33  TYR D CE2 1 
ATOM   5125 C CZ  . TYR D 2 33  ? 17.555  -10.867 32.611  1.00 40.88  ?  33  TYR D CZ  1 
ATOM   5126 O OH  . TYR D 2 33  ? 17.758  -11.145 31.279  1.00 42.15  ?  33  TYR D OH  1 
ATOM   5127 N N   . MET D 2 34  ? 18.838  -8.531  39.283  1.00 30.65  ?  34  MET D N   1 
ATOM   5128 C CA  . MET D 2 34  ? 18.820  -7.815  40.550  1.00 35.10  ?  34  MET D CA  1 
ATOM   5129 C C   . MET D 2 34  ? 18.524  -6.339  40.320  1.00 37.94  ?  34  MET D C   1 
ATOM   5130 O O   . MET D 2 34  ? 19.035  -5.729  39.376  1.00 35.30  ?  34  MET D O   1 
ATOM   5131 C CB  . MET D 2 34  ? 20.146  -7.990  41.285  1.00 34.47  ?  34  MET D CB  1 
ATOM   5132 C CG  . MET D 2 34  ? 20.392  -9.425  41.690  1.00 38.24  ?  34  MET D CG  1 
ATOM   5133 S SD  . MET D 2 34  ? 19.181  -10.030 42.870  1.00 42.14  ?  34  MET D SD  1 
ATOM   5134 C CE  . MET D 2 34  ? 19.263  -8.773  44.145  1.00 37.02  ?  34  MET D CE  1 
ATOM   5135 N N   . THR D 2 35  ? 17.718  -5.753  41.199  1.00 34.56  ?  35  THR D N   1 
ATOM   5136 C CA  . THR D 2 35  ? 17.182  -4.428  40.954  1.00 33.62  ?  35  THR D CA  1 
ATOM   5137 C C   . THR D 2 35  ? 17.288  -3.589  42.212  1.00 34.40  ?  35  THR D C   1 
ATOM   5138 O O   . THR D 2 35  ? 17.323  -4.100  43.337  1.00 34.17  ?  35  THR D O   1 
ATOM   5139 C CB  . THR D 2 35  ? 15.694  -4.439  40.518  1.00 37.95  ?  35  THR D CB  1 
ATOM   5140 O OG1 . THR D 2 35  ? 14.861  -4.791  41.630  1.00 39.51  ?  35  THR D OG1 1 
ATOM   5141 C CG2 . THR D 2 35  ? 15.450  -5.407  39.385  1.00 41.97  ?  35  THR D CG2 1 
ATOM   5142 N N   . TRP D 2 36  ? 17.344  -2.288  41.989  1.00 34.81  ?  36  TRP D N   1 
ATOM   5143 C CA  . TRP D 2 36  ? 17.180  -1.293  43.030  1.00 34.71  ?  36  TRP D CA  1 
ATOM   5144 C C   . TRP D 2 36  ? 15.860  -0.578  42.782  1.00 34.40  ?  36  TRP D C   1 
ATOM   5145 O O   . TRP D 2 36  ? 15.585  -0.145  41.650  1.00 35.15  ?  36  TRP D O   1 
ATOM   5146 C CB  . TRP D 2 36  ? 18.337  -0.300  43.037  1.00 30.25  ?  36  TRP D CB  1 
ATOM   5147 C CG  . TRP D 2 36  ? 19.610  -0.873  43.553  1.00 34.48  ?  36  TRP D CG  1 
ATOM   5148 C CD1 . TRP D 2 36  ? 20.667  -1.318  42.812  1.00 33.26  ?  36  TRP D CD1 1 
ATOM   5149 C CD2 . TRP D 2 36  ? 19.978  -1.046  44.925  1.00 33.43  ?  36  TRP D CD2 1 
ATOM   5150 N NE1 . TRP D 2 36  ? 21.671  -1.754  43.639  1.00 35.52  ?  36  TRP D NE1 1 
ATOM   5151 C CE2 . TRP D 2 36  ? 21.271  -1.604  44.942  1.00 33.05  ?  36  TRP D CE2 1 
ATOM   5152 C CE3 . TRP D 2 36  ? 19.344  -0.778  46.140  1.00 33.83  ?  36  TRP D CE3 1 
ATOM   5153 C CZ2 . TRP D 2 36  ? 21.939  -1.903  46.126  1.00 31.72  ?  36  TRP D CZ2 1 
ATOM   5154 C CZ3 . TRP D 2 36  ? 20.008  -1.078  47.315  1.00 32.06  ?  36  TRP D CZ3 1 
ATOM   5155 C CH2 . TRP D 2 36  ? 21.291  -1.637  47.298  1.00 32.35  ?  36  TRP D CH2 1 
ATOM   5156 N N   . VAL D 2 37  ? 15.047  -0.497  43.836  1.00 30.64  ?  37  VAL D N   1 
ATOM   5157 C CA  . VAL D 2 37  ? 13.767  0.199   43.839  1.00 33.89  ?  37  VAL D CA  1 
ATOM   5158 C C   . VAL D 2 37  ? 13.789  1.188   44.995  1.00 36.07  ?  37  VAL D C   1 
ATOM   5159 O O   . VAL D 2 37  ? 14.191  0.833   46.104  1.00 36.28  ?  37  VAL D O   1 
ATOM   5160 C CB  . VAL D 2 37  ? 12.596  -0.795  44.008  1.00 35.99  ?  37  VAL D CB  1 
ATOM   5161 C CG1 . VAL D 2 37  ? 11.274  -0.055  44.186  1.00 37.50  ?  37  VAL D CG1 1 
ATOM   5162 C CG2 . VAL D 2 37  ? 12.544  -1.792  42.851  1.00 31.21  ?  37  VAL D CG2 1 
ATOM   5163 N N   . ARG D 2 38  ? 13.342  2.417   44.767  1.00 37.41  ?  38  ARG D N   1 
ATOM   5164 C CA  . ARG D 2 38  ? 13.382  3.390   45.849  1.00 36.00  ?  38  ARG D CA  1 
ATOM   5165 C C   . ARG D 2 38  ? 11.987  3.912   46.157  1.00 40.22  ?  38  ARG D C   1 
ATOM   5166 O O   . ARG D 2 38  ? 11.086  3.891   45.313  1.00 45.29  ?  38  ARG D O   1 
ATOM   5167 C CB  . ARG D 2 38  ? 14.323  4.557   45.528  1.00 37.15  ?  38  ARG D CB  1 
ATOM   5168 C CG  . ARG D 2 38  ? 13.737  5.650   44.654  1.00 39.75  ?  38  ARG D CG  1 
ATOM   5169 C CD  . ARG D 2 38  ? 14.739  6.783   44.512  1.00 40.11  ?  38  ARG D CD  1 
ATOM   5170 N NE  . ARG D 2 38  ? 14.229  7.900   43.724  1.00 49.38  ?  38  ARG D NE  1 
ATOM   5171 C CZ  . ARG D 2 38  ? 14.947  8.975   43.416  1.00 51.15  ?  38  ARG D CZ  1 
ATOM   5172 N NH1 . ARG D 2 38  ? 14.414  9.951   42.692  1.00 51.87  ?  38  ARG D NH1 1 
ATOM   5173 N NH2 . ARG D 2 38  ? 16.206  9.066   43.827  1.00 46.35  ?  38  ARG D NH2 1 
ATOM   5174 N N   . GLN D 2 39  ? 11.826  4.393   47.388  1.00 38.71  ?  39  GLN D N   1 
ATOM   5175 C CA  . GLN D 2 39  ? 10.553  4.938   47.853  1.00 46.25  ?  39  GLN D CA  1 
ATOM   5176 C C   . GLN D 2 39  ? 10.831  6.201   48.657  1.00 42.81  ?  39  GLN D C   1 
ATOM   5177 O O   . GLN D 2 39  ? 11.379  6.128   49.762  1.00 39.98  ?  39  GLN D O   1 
ATOM   5178 C CB  . GLN D 2 39  ? 9.781   3.917   48.688  1.00 41.57  ?  39  GLN D CB  1 
ATOM   5179 C CG  . GLN D 2 39  ? 8.330   4.296   48.938  1.00 44.20  ?  39  GLN D CG  1 
ATOM   5180 C CD  . GLN D 2 39  ? 7.540   3.172   49.578  1.00 44.43  ?  39  GLN D CD  1 
ATOM   5181 O OE1 . GLN D 2 39  ? 8.056   2.432   50.416  1.00 45.61  ?  39  GLN D OE1 1 
ATOM   5182 N NE2 . GLN D 2 39  ? 6.291   3.022   49.166  1.00 46.43  ?  39  GLN D NE2 1 
ATOM   5183 N N   . ALA D 2 40  ? 10.475  7.352   48.091  1.00 44.36  ?  40  ALA D N   1 
ATOM   5184 C CA  . ALA D 2 40  ? 10.595  8.620   48.789  1.00 47.93  ?  40  ALA D CA  1 
ATOM   5185 C C   . ALA D 2 40  ? 9.586   8.685   49.933  1.00 49.98  ?  40  ALA D C   1 
ATOM   5186 O O   . ALA D 2 40  ? 8.584   7.966   49.929  1.00 54.12  ?  40  ALA D O   1 
ATOM   5187 C CB  . ALA D 2 40  ? 10.371  9.777   47.820  1.00 43.79  ?  40  ALA D CB  1 
ATOM   5188 N N   . PRO D 2 41  ? 9.833   9.533   50.931  1.00 54.84  ?  41  PRO D N   1 
ATOM   5189 C CA  . PRO D 2 41  ? 8.910   9.612   52.074  1.00 55.89  ?  41  PRO D CA  1 
ATOM   5190 C C   . PRO D 2 41  ? 7.508   10.020  51.639  1.00 58.03  ?  41  PRO D C   1 
ATOM   5191 O O   . PRO D 2 41  ? 7.318   11.030  50.954  1.00 51.64  ?  41  PRO D O   1 
ATOM   5192 C CB  . PRO D 2 41  ? 9.554   10.670  52.977  1.00 59.45  ?  41  PRO D CB  1 
ATOM   5193 C CG  . PRO D 2 41  ? 10.999  10.660  52.596  1.00 60.03  ?  41  PRO D CG  1 
ATOM   5194 C CD  . PRO D 2 41  ? 11.024  10.379  51.124  1.00 50.84  ?  41  PRO D CD  1 
ATOM   5195 N N   . GLY D 2 42  ? 6.526   9.207   52.029  1.00 58.74  ?  42  GLY D N   1 
ATOM   5196 C CA  . GLY D 2 42  ? 5.141   9.470   51.680  1.00 54.16  ?  42  GLY D CA  1 
ATOM   5197 C C   . GLY D 2 42  ? 4.827   9.395   50.203  1.00 56.54  ?  42  GLY D C   1 
ATOM   5198 O O   . GLY D 2 42  ? 3.854   10.004  49.755  1.00 64.77  ?  42  GLY D O   1 
ATOM   5199 N N   . LYS D 2 43  ? 5.619   8.657   49.427  1.00 58.27  ?  43  LYS D N   1 
ATOM   5200 C CA  . LYS D 2 43  ? 5.406   8.505   47.993  1.00 54.29  ?  43  LYS D CA  1 
ATOM   5201 C C   . LYS D 2 43  ? 5.426   7.022   47.626  1.00 48.26  ?  43  LYS D C   1 
ATOM   5202 O O   . LYS D 2 43  ? 5.561   6.142   48.486  1.00 43.43  ?  43  LYS D O   1 
ATOM   5203 C CB  . LYS D 2 43  ? 6.454   9.306   47.209  1.00 56.44  ?  43  LYS D CB  1 
ATOM   5204 C CG  . LYS D 2 43  ? 6.241   10.812  47.314  1.00 53.50  ?  43  LYS D CG  1 
ATOM   5205 C CD  . LYS D 2 43  ? 7.451   11.608  46.850  1.00 66.48  ?  43  LYS D CD  1 
ATOM   5206 C CE  . LYS D 2 43  ? 7.850   11.286  45.418  1.00 73.06  ?  43  LYS D CE  1 
ATOM   5207 N NZ  . LYS D 2 43  ? 9.014   12.115  44.975  1.00 76.70  ?  43  LYS D NZ  1 
ATOM   5208 N N   . GLY D 2 44  ? 5.281   6.743   46.330  1.00 41.79  ?  44  GLY D N   1 
ATOM   5209 C CA  . GLY D 2 44  ? 5.169   5.381   45.857  1.00 45.06  ?  44  GLY D CA  1 
ATOM   5210 C C   . GLY D 2 44  ? 6.511   4.752   45.521  1.00 46.87  ?  44  GLY D C   1 
ATOM   5211 O O   . GLY D 2 44  ? 7.571   5.373   45.598  1.00 45.72  ?  44  GLY D O   1 
ATOM   5212 N N   . LEU D 2 45  ? 6.441   3.485   45.120  1.00 46.19  ?  45  LEU D N   1 
ATOM   5213 C CA  . LEU D 2 45  ? 7.628   2.749   44.712  1.00 43.18  ?  45  LEU D CA  1 
ATOM   5214 C C   . LEU D 2 45  ? 8.093   3.214   43.342  1.00 39.61  ?  45  LEU D C   1 
ATOM   5215 O O   . LEU D 2 45  ? 7.283   3.510   42.459  1.00 40.59  ?  45  LEU D O   1 
ATOM   5216 C CB  . LEU D 2 45  ? 7.330   1.255   44.676  1.00 42.62  ?  45  LEU D CB  1 
ATOM   5217 C CG  . LEU D 2 45  ? 6.824   0.701   46.003  1.00 43.15  ?  45  LEU D CG  1 
ATOM   5218 C CD1 . LEU D 2 45  ? 6.257   -0.696  45.804  1.00 44.72  ?  45  LEU D CD1 1 
ATOM   5219 C CD2 . LEU D 2 45  ? 7.951   0.697   47.017  1.00 39.70  ?  45  LEU D CD2 1 
ATOM   5220 N N   . GLU D 2 46  ? 9.408   3.273   43.164  1.00 38.53  ?  46  GLU D N   1 
ATOM   5221 C CA  . GLU D 2 46  ? 9.998   3.812   41.946  1.00 38.23  ?  46  GLU D CA  1 
ATOM   5222 C C   . GLU D 2 46  ? 11.167  2.930   41.535  1.00 40.00  ?  46  GLU D C   1 
ATOM   5223 O O   . GLU D 2 46  ? 12.127  2.778   42.296  1.00 41.08  ?  46  GLU D O   1 
ATOM   5224 C CB  . GLU D 2 46  ? 10.450  5.254   42.175  1.00 42.02  ?  46  GLU D CB  1 
ATOM   5225 C CG  . GLU D 2 46  ? 10.734  6.041   40.923  1.00 51.86  ?  46  GLU D CG  1 
ATOM   5226 C CD  . GLU D 2 46  ? 10.952  7.505   41.232  1.00 60.94  ?  46  GLU D CD  1 
ATOM   5227 O OE1 . GLU D 2 46  ? 10.709  8.343   40.336  1.00 68.68  ?  46  GLU D OE1 1 
ATOM   5228 O OE2 . GLU D 2 46  ? 11.349  7.817   42.380  1.00 59.68  ?  46  GLU D OE2 1 
ATOM   5229 N N   . TRP D 2 47  ? 11.089  2.341   40.346  1.00 37.40  ?  47  TRP D N   1 
ATOM   5230 C CA  . TRP D 2 47  ? 12.153  1.453   39.900  1.00 34.98  ?  47  TRP D CA  1 
ATOM   5231 C C   . TRP D 2 47  ? 13.383  2.259   39.490  1.00 41.31  ?  47  TRP D C   1 
ATOM   5232 O O   . TRP D 2 47  ? 13.284  3.217   38.716  1.00 45.32  ?  47  TRP D O   1 
ATOM   5233 C CB  . TRP D 2 47  ? 11.678  0.576   38.742  1.00 35.11  ?  47  TRP D CB  1 
ATOM   5234 C CG  . TRP D 2 47  ? 12.805  -0.187  38.122  1.00 43.27  ?  47  TRP D CG  1 
ATOM   5235 C CD1 . TRP D 2 47  ? 13.506  -1.227  38.678  1.00 37.69  ?  47  TRP D CD1 1 
ATOM   5236 C CD2 . TRP D 2 47  ? 13.390  0.050   36.840  1.00 37.46  ?  47  TRP D CD2 1 
ATOM   5237 N NE1 . TRP D 2 47  ? 14.483  -1.654  37.815  1.00 35.97  ?  47  TRP D NE1 1 
ATOM   5238 C CE2 . TRP D 2 47  ? 14.434  -0.888  36.678  1.00 41.63  ?  47  TRP D CE2 1 
ATOM   5239 C CE3 . TRP D 2 47  ? 13.133  0.958   35.812  1.00 31.96  ?  47  TRP D CE3 1 
ATOM   5240 C CZ2 . TRP D 2 47  ? 15.219  -0.941  35.526  1.00 40.70  ?  47  TRP D CZ2 1 
ATOM   5241 C CZ3 . TRP D 2 47  ? 13.904  0.902   34.670  1.00 39.81  ?  47  TRP D CZ3 1 
ATOM   5242 C CH2 . TRP D 2 47  ? 14.937  -0.040  34.533  1.00 38.32  ?  47  TRP D CH2 1 
ATOM   5243 N N   . VAL D 2 48  ? 14.548  1.869   40.010  1.00 42.63  ?  48  VAL D N   1 
ATOM   5244 C CA  . VAL D 2 48  ? 15.777  2.616   39.763  1.00 38.76  ?  48  VAL D CA  1 
ATOM   5245 C C   . VAL D 2 48  ? 16.619  1.904   38.714  1.00 38.46  ?  48  VAL D C   1 
ATOM   5246 O O   . VAL D 2 48  ? 16.974  2.505   37.692  1.00 34.84  ?  48  VAL D O   1 
ATOM   5247 C CB  . VAL D 2 48  ? 16.582  2.832   41.058  1.00 36.47  ?  48  VAL D CB  1 
ATOM   5248 C CG1 . VAL D 2 48  ? 17.886  3.570   40.759  1.00 33.20  ?  48  VAL D CG1 1 
ATOM   5249 C CG2 . VAL D 2 48  ? 15.745  3.578   42.089  1.00 36.60  ?  48  VAL D CG2 1 
ATOM   5250 N N   . SER D 2 49  ? 16.950  0.631   38.942  1.00 37.48  ?  49  SER D N   1 
ATOM   5251 C CA  . SER D 2 49  ? 17.847  -0.016  37.983  1.00 34.45  ?  49  SER D CA  1 
ATOM   5252 C C   . SER D 2 49  ? 17.839  -1.535  38.135  1.00 39.11  ?  49  SER D C   1 
ATOM   5253 O O   . SER D 2 49  ? 17.343  -2.083  39.120  1.00 39.49  ?  49  SER D O   1 
ATOM   5254 C CB  . SER D 2 49  ? 19.279  0.505   38.124  1.00 33.97  ?  49  SER D CB  1 
ATOM   5255 O OG  . SER D 2 49  ? 19.847  0.049   39.337  1.00 42.59  ?  49  SER D OG  1 
ATOM   5256 N N   . VAL D 2 50  ? 18.441  -2.204  37.146  1.00 33.51  ?  50  VAL D N   1 
ATOM   5257 C CA  . VAL D 2 50  ? 18.517  -3.658  37.096  1.00 33.57  ?  50  VAL D CA  1 
ATOM   5258 C C   . VAL D 2 50  ? 19.839  -4.067  36.465  1.00 35.31  ?  50  VAL D C   1 
ATOM   5259 O O   . VAL D 2 50  ? 20.357  -3.404  35.563  1.00 32.92  ?  50  VAL D O   1 
ATOM   5260 C CB  . VAL D 2 50  ? 17.341  -4.275  36.305  1.00 36.97  ?  50  VAL D CB  1 
ATOM   5261 C CG1 . VAL D 2 50  ? 17.439  -3.902  34.832  1.00 30.98  ?  50  VAL D CG1 1 
ATOM   5262 C CG2 . VAL D 2 50  ? 17.329  -5.783  36.468  1.00 29.08  ?  50  VAL D CG2 1 
ATOM   5263 N N   . ILE D 2 51  ? 20.370  -5.190  36.937  1.00 36.51  ?  51  ILE D N   1 
ATOM   5264 C CA  . ILE D 2 51  ? 21.520  -5.853  36.340  1.00 37.82  ?  51  ILE D CA  1 
ATOM   5265 C C   . ILE D 2 51  ? 21.142  -7.311  36.083  1.00 38.29  ?  51  ILE D C   1 
ATOM   5266 O O   . ILE D 2 51  ? 20.586  -7.985  36.964  1.00 35.54  ?  51  ILE D O   1 
ATOM   5267 C CB  . ILE D 2 51  ? 22.774  -5.740  37.232  1.00 36.52  ?  51  ILE D CB  1 
ATOM   5268 C CG1 . ILE D 2 51  ? 23.969  -6.433  36.570  1.00 37.53  ?  51  ILE D CG1 1 
ATOM   5269 C CG2 . ILE D 2 51  ? 22.507  -6.266  38.641  1.00 32.77  ?  51  ILE D CG2 1 
ATOM   5270 C CD1 . ILE D 2 51  ? 25.278  -6.168  37.269  1.00 36.89  ?  51  ILE D CD1 1 
ATOM   5271 N N   . ASN D 2 52  ? 21.418  -7.789  34.868  1.00 37.49  ?  52  ASN D N   1 
ATOM   5272 C CA  . ASN D 2 52  ? 21.010  -9.129  34.479  1.00 39.15  ?  52  ASN D CA  1 
ATOM   5273 C C   . ASN D 2 52  ? 22.154  -10.117 34.723  1.00 42.95  ?  52  ASN D C   1 
ATOM   5274 O O   . ASN D 2 52  ? 23.200  -9.774  35.284  1.00 41.35  ?  52  ASN D O   1 
ATOM   5275 C CB  . ASN D 2 52  ? 20.514  -9.150  33.028  1.00 30.35  ?  52  ASN D CB  1 
ATOM   5276 C CG  . ASN D 2 52  ? 21.595  -8.800  32.008  1.00 39.88  ?  52  ASN D CG  1 
ATOM   5277 O OD1 . ASN D 2 52  ? 22.779  -9.088  32.192  1.00 41.46  ?  52  ASN D OD1 1 
ATOM   5278 N ND2 . ASN D 2 52  ? 21.173  -8.200  30.900  1.00 35.48  ?  52  ASN D ND2 1 
ATOM   5279 N N   . VAL D 2 53  ? 21.950  -11.367 34.296  1.00 42.02  ?  53  VAL D N   1 
ATOM   5280 C CA  . VAL D 2 53  ? 22.872  -12.441 34.657  1.00 42.63  ?  53  VAL D CA  1 
ATOM   5281 C C   . VAL D 2 53  ? 24.214  -12.289 33.956  1.00 43.90  ?  53  VAL D C   1 
ATOM   5282 O O   . VAL D 2 53  ? 25.242  -12.721 34.489  1.00 47.04  ?  53  VAL D O   1 
ATOM   5283 C CB  . VAL D 2 53  ? 22.238  -13.811 34.362  1.00 43.31  ?  53  VAL D CB  1 
ATOM   5284 C CG1 . VAL D 2 53  ? 20.998  -13.990 35.210  1.00 45.07  ?  53  VAL D CG1 1 
ATOM   5285 C CG2 . VAL D 2 53  ? 21.898  -13.939 32.889  1.00 47.60  ?  53  VAL D CG2 1 
ATOM   5286 N N   . TYR D 2 54  ? 24.242  -11.673 32.770  1.00 45.60  ?  54  TYR D N   1 
ATOM   5287 C CA  . TYR D 2 54  ? 25.504  -11.443 32.078  1.00 45.22  ?  54  TYR D CA  1 
ATOM   5288 C C   . TYR D 2 54  ? 26.253  -10.227 32.597  1.00 49.64  ?  54  TYR D C   1 
ATOM   5289 O O   . TYR D 2 54  ? 27.406  -10.021 32.203  1.00 56.75  ?  54  TYR D O   1 
ATOM   5290 C CB  . TYR D 2 54  ? 25.284  -11.267 30.573  1.00 45.33  ?  54  TYR D CB  1 
ATOM   5291 C CG  . TYR D 2 54  ? 24.453  -12.347 29.928  1.00 55.77  ?  54  TYR D CG  1 
ATOM   5292 C CD1 . TYR D 2 54  ? 23.087  -12.169 29.743  1.00 59.57  ?  54  TYR D CD1 1 
ATOM   5293 C CD2 . TYR D 2 54  ? 25.028  -13.542 29.496  1.00 51.01  ?  54  TYR D CD2 1 
ATOM   5294 C CE1 . TYR D 2 54  ? 22.308  -13.145 29.151  1.00 63.97  ?  54  TYR D CE1 1 
ATOM   5295 C CE2 . TYR D 2 54  ? 24.255  -14.530 28.899  1.00 59.55  ?  54  TYR D CE2 1 
ATOM   5296 C CZ  . TYR D 2 54  ? 22.890  -14.322 28.732  1.00 67.76  ?  54  TYR D CZ  1 
ATOM   5297 O OH  . TYR D 2 54  ? 22.090  -15.280 28.147  1.00 75.78  ?  54  TYR D OH  1 
ATOM   5298 N N   . GLY D 2 55  ? 25.640  -9.427  33.464  1.00 45.83  ?  55  GLY D N   1 
ATOM   5299 C CA  . GLY D 2 55  ? 26.261  -8.216  33.950  1.00 45.62  ?  55  GLY D CA  1 
ATOM   5300 C C   . GLY D 2 55  ? 25.878  -6.953  33.213  1.00 44.35  ?  55  GLY D C   1 
ATOM   5301 O O   . GLY D 2 55  ? 26.496  -5.909  33.452  1.00 47.07  ?  55  GLY D O   1 
ATOM   5302 N N   . GLY D 2 56  ? 24.916  -7.022  32.295  1.00 38.49  ?  56  GLY D N   1 
ATOM   5303 C CA  . GLY D 2 56  ? 24.436  -5.827  31.628  1.00 39.04  ?  56  GLY D CA  1 
ATOM   5304 C C   . GLY D 2 56  ? 23.546  -5.012  32.555  1.00 39.95  ?  56  GLY D C   1 
ATOM   5305 O O   . GLY D 2 56  ? 22.768  -5.553  33.340  1.00 41.03  ?  56  GLY D O   1 
ATOM   5306 N N   . THR D 2 57  ? 23.668  -3.694  32.448  1.00 40.25  ?  57  THR D N   1 
ATOM   5307 C CA  . THR D 2 57  ? 22.979  -2.751  33.319  1.00 41.64  ?  57  THR D CA  1 
ATOM   5308 C C   . THR D 2 57  ? 21.916  -1.968  32.549  1.00 43.33  ?  57  THR D C   1 
ATOM   5309 O O   . THR D 2 57  ? 22.151  -1.536  31.412  1.00 41.02  ?  57  THR D O   1 
ATOM   5310 C CB  . THR D 2 57  ? 23.980  -1.776  33.934  1.00 42.90  ?  57  THR D CB  1 
ATOM   5311 O OG1 . THR D 2 57  ? 24.650  -1.071  32.877  1.00 42.30  ?  57  THR D OG1 1 
ATOM   5312 C CG2 . THR D 2 57  ? 25.006  -2.534  34.756  1.00 42.97  ?  57  THR D CG2 1 
ATOM   5313 N N   . TYR D 2 58  ? 20.754  -1.770  33.180  1.00 39.26  ?  58  TYR D N   1 
ATOM   5314 C CA  . TYR D 2 58  ? 19.663  -0.996  32.601  1.00 38.27  ?  58  TYR D CA  1 
ATOM   5315 C C   . TYR D 2 58  ? 19.017  -0.152  33.691  1.00 37.71  ?  58  TYR D C   1 
ATOM   5316 O O   . TYR D 2 58  ? 18.986  -0.538  34.861  1.00 39.15  ?  58  TYR D O   1 
ATOM   5317 C CB  . TYR D 2 58  ? 18.641  -1.901  31.908  1.00 35.33  ?  58  TYR D CB  1 
ATOM   5318 C CG  . TYR D 2 58  ? 19.267  -2.630  30.752  1.00 39.86  ?  58  TYR D CG  1 
ATOM   5319 C CD1 . TYR D 2 58  ? 19.299  -2.060  29.484  1.00 40.98  ?  58  TYR D CD1 1 
ATOM   5320 C CD2 . TYR D 2 58  ? 19.866  -3.867  30.932  1.00 38.47  ?  58  TYR D CD2 1 
ATOM   5321 C CE1 . TYR D 2 58  ? 19.893  -2.714  28.427  1.00 38.43  ?  58  TYR D CE1 1 
ATOM   5322 C CE2 . TYR D 2 58  ? 20.463  -4.524  29.884  1.00 39.39  ?  58  TYR D CE2 1 
ATOM   5323 C CZ  . TYR D 2 58  ? 20.470  -3.947  28.631  1.00 39.98  ?  58  TYR D CZ  1 
ATOM   5324 O OH  . TYR D 2 58  ? 21.065  -4.606  27.581  1.00 44.82  ?  58  TYR D OH  1 
ATOM   5325 N N   . TYR D 2 59  ? 18.530  1.026   33.306  1.00 39.45  ?  59  TYR D N   1 
ATOM   5326 C CA  . TYR D 2 59  ? 18.193  2.050   34.283  1.00 38.82  ?  59  TYR D CA  1 
ATOM   5327 C C   . TYR D 2 59  ? 16.854  2.695   33.964  1.00 38.75  ?  59  TYR D C   1 
ATOM   5328 O O   . TYR D 2 59  ? 16.347  2.620   32.841  1.00 41.80  ?  59  TYR D O   1 
ATOM   5329 C CB  . TYR D 2 59  ? 19.264  3.144   34.339  1.00 32.02  ?  59  TYR D CB  1 
ATOM   5330 C CG  . TYR D 2 59  ? 20.632  2.659   34.744  1.00 35.21  ?  59  TYR D CG  1 
ATOM   5331 C CD1 . TYR D 2 59  ? 21.066  2.774   36.060  1.00 32.57  ?  59  TYR D CD1 1 
ATOM   5332 C CD2 . TYR D 2 59  ? 21.500  2.100   33.812  1.00 32.78  ?  59  TYR D CD2 1 
ATOM   5333 C CE1 . TYR D 2 59  ? 22.323  2.331   36.439  1.00 30.07  ?  59  TYR D CE1 1 
ATOM   5334 C CE2 . TYR D 2 59  ? 22.751  1.653   34.182  1.00 32.18  ?  59  TYR D CE2 1 
ATOM   5335 C CZ  . TYR D 2 59  ? 23.162  1.772   35.500  1.00 32.50  ?  59  TYR D CZ  1 
ATOM   5336 O OH  . TYR D 2 59  ? 24.416  1.339   35.882  1.00 37.62  ?  59  TYR D OH  1 
ATOM   5337 N N   . ALA D 2 60  ? 16.275  3.317   34.987  1.00 34.25  ?  60  ALA D N   1 
ATOM   5338 C CA  . ALA D 2 60  ? 15.271  4.339   34.749  1.00 43.01  ?  60  ALA D CA  1 
ATOM   5339 C C   . ALA D 2 60  ? 15.953  5.587   34.197  1.00 44.02  ?  60  ALA D C   1 
ATOM   5340 O O   . ALA D 2 60  ? 17.089  5.910   34.559  1.00 38.22  ?  60  ALA D O   1 
ATOM   5341 C CB  . ALA D 2 60  ? 14.517  4.664   36.038  1.00 40.45  ?  60  ALA D CB  1 
ATOM   5342 N N   . SER D 2 61  ? 15.245  6.287   33.306  1.00 47.51  ?  61  SER D N   1 
ATOM   5343 C CA  . SER D 2 61  ? 15.819  7.436   32.607  1.00 49.95  ?  61  SER D CA  1 
ATOM   5344 C C   . SER D 2 61  ? 16.420  8.448   33.574  1.00 44.87  ?  61  SER D C   1 
ATOM   5345 O O   . SER D 2 61  ? 17.567  8.878   33.411  1.00 41.08  ?  61  SER D O   1 
ATOM   5346 C CB  . SER D 2 61  ? 14.751  8.107   31.744  1.00 48.83  ?  61  SER D CB  1 
ATOM   5347 O OG  . SER D 2 61  ? 14.499  7.347   30.579  1.00 56.51  ?  61  SER D OG  1 
ATOM   5348 N N   . TRP D 2 62  ? 15.654  8.833   34.596  1.00 46.11  ?  62  TRP D N   1 
ATOM   5349 C CA  . TRP D 2 62  ? 16.114  9.855   35.528  1.00 47.33  ?  62  TRP D CA  1 
ATOM   5350 C C   . TRP D 2 62  ? 17.354  9.432   36.297  1.00 47.93  ?  62  TRP D C   1 
ATOM   5351 O O   . TRP D 2 62  ? 18.061  10.294  36.825  1.00 57.10  ?  62  TRP D O   1 
ATOM   5352 C CB  . TRP D 2 62  ? 14.998  10.213  36.507  1.00 50.53  ?  62  TRP D CB  1 
ATOM   5353 C CG  . TRP D 2 62  ? 14.457  9.045   37.257  1.00 49.05  ?  62  TRP D CG  1 
ATOM   5354 C CD1 . TRP D 2 62  ? 13.345  8.320   36.949  1.00 50.33  ?  62  TRP D CD1 1 
ATOM   5355 C CD2 . TRP D 2 62  ? 15.001  8.462   38.447  1.00 52.35  ?  62  TRP D CD2 1 
ATOM   5356 N NE1 . TRP D 2 62  ? 13.159  7.321   37.873  1.00 52.64  ?  62  TRP D NE1 1 
ATOM   5357 C CE2 . TRP D 2 62  ? 14.163  7.386   38.804  1.00 53.30  ?  62  TRP D CE2 1 
ATOM   5358 C CE3 . TRP D 2 62  ? 16.113  8.745   39.246  1.00 49.99  ?  62  TRP D CE3 1 
ATOM   5359 C CZ2 . TRP D 2 62  ? 14.401  6.595   39.925  1.00 51.28  ?  62  TRP D CZ2 1 
ATOM   5360 C CZ3 . TRP D 2 62  ? 16.350  7.958   40.356  1.00 47.40  ?  62  TRP D CZ3 1 
ATOM   5361 C CH2 . TRP D 2 62  ? 15.498  6.896   40.686  1.00 48.19  ?  62  TRP D CH2 1 
ATOM   5362 N N   . ALA D 2 63  ? 17.627  8.132   36.385  1.00 49.92  ?  63  ALA D N   1 
ATOM   5363 C CA  . ALA D 2 63  ? 18.743  7.640   37.177  1.00 44.22  ?  63  ALA D CA  1 
ATOM   5364 C C   . ALA D 2 63  ? 20.011  7.417   36.370  1.00 42.28  ?  63  ALA D C   1 
ATOM   5365 O O   . ALA D 2 63  ? 21.088  7.301   36.961  1.00 43.60  ?  63  ALA D O   1 
ATOM   5366 C CB  . ALA D 2 63  ? 18.359  6.328   37.866  1.00 44.51  ?  63  ALA D CB  1 
ATOM   5367 N N   . LYS D 2 64  ? 19.915  7.384   35.040  1.00 44.67  ?  64  LYS D N   1 
ATOM   5368 C CA  . LYS D 2 64  ? 21.032  6.915   34.226  1.00 44.96  ?  64  LYS D CA  1 
ATOM   5369 C C   . LYS D 2 64  ? 22.263  7.806   34.350  1.00 54.74  ?  64  LYS D C   1 
ATOM   5370 O O   . LYS D 2 64  ? 23.392  7.312   34.265  1.00 60.14  ?  64  LYS D O   1 
ATOM   5371 C CB  . LYS D 2 64  ? 20.594  6.809   32.766  1.00 45.58  ?  64  LYS D CB  1 
ATOM   5372 C CG  . LYS D 2 64  ? 21.487  5.912   31.933  1.00 60.00  ?  64  LYS D CG  1 
ATOM   5373 C CD  . LYS D 2 64  ? 20.762  5.393   30.698  1.00 57.52  ?  64  LYS D CD  1 
ATOM   5374 C CE  . LYS D 2 64  ? 21.673  4.504   29.871  1.00 54.53  ?  64  LYS D CE  1 
ATOM   5375 N NZ  . LYS D 2 64  ? 21.025  4.109   28.594  1.00 61.46  ?  64  LYS D NZ  1 
ATOM   5376 N N   . GLY D 2 65  ? 22.077  9.109   34.568  1.00 58.19  ?  65  GLY D N   1 
ATOM   5377 C CA  . GLY D 2 65  ? 23.218  10.010  34.582  1.00 62.32  ?  65  GLY D CA  1 
ATOM   5378 C C   . GLY D 2 65  ? 24.112  9.869   35.802  1.00 60.03  ?  65  GLY D C   1 
ATOM   5379 O O   . GLY D 2 65  ? 25.334  10.011  35.697  1.00 57.71  ?  65  GLY D O   1 
ATOM   5380 N N   . ARG D 2 66  ? 23.530  9.567   36.963  1.00 56.66  ?  66  ARG D N   1 
ATOM   5381 C CA  . ARG D 2 66  ? 24.233  9.655   38.234  1.00 47.60  ?  66  ARG D CA  1 
ATOM   5382 C C   . ARG D 2 66  ? 24.322  8.340   38.995  1.00 50.83  ?  66  ARG D C   1 
ATOM   5383 O O   . ARG D 2 66  ? 25.093  8.254   39.958  1.00 49.71  ?  66  ARG D O   1 
ATOM   5384 C CB  . ARG D 2 66  ? 23.543  10.696  39.129  1.00 53.56  ?  66  ARG D CB  1 
ATOM   5385 C CG  . ARG D 2 66  ? 23.383  12.041  38.446  1.00 61.05  ?  66  ARG D CG  1 
ATOM   5386 C CD  . ARG D 2 66  ? 22.498  13.002  39.218  1.00 52.44  ?  66  ARG D CD  1 
ATOM   5387 N NE  . ARG D 2 66  ? 21.133  12.502  39.352  1.00 52.80  ?  66  ARG D NE  1 
ATOM   5388 C CZ  . ARG D 2 66  ? 20.545  12.257  40.517  1.00 52.39  ?  66  ARG D CZ  1 
ATOM   5389 N NH1 . ARG D 2 66  ? 21.198  12.497  41.646  1.00 50.52  ?  66  ARG D NH1 1 
ATOM   5390 N NH2 . ARG D 2 66  ? 19.297  11.802  40.557  1.00 51.00  ?  66  ARG D NH2 1 
ATOM   5391 N N   . PHE D 2 67  ? 23.565  7.326   38.605  1.00 50.44  ?  67  PHE D N   1 
ATOM   5392 C CA  . PHE D 2 67  ? 23.519  6.057   39.312  1.00 43.97  ?  67  PHE D CA  1 
ATOM   5393 C C   . PHE D 2 67  ? 24.194  4.970   38.486  1.00 41.93  ?  67  PHE D C   1 
ATOM   5394 O O   . PHE D 2 67  ? 24.096  4.956   37.255  1.00 40.42  ?  67  PHE D O   1 
ATOM   5395 C CB  . PHE D 2 67  ? 22.072  5.661   39.609  1.00 44.49  ?  67  PHE D CB  1 
ATOM   5396 C CG  . PHE D 2 67  ? 21.392  6.527   40.635  1.00 43.43  ?  67  PHE D CG  1 
ATOM   5397 C CD1 . PHE D 2 67  ? 21.066  6.019   41.883  1.00 46.34  ?  67  PHE D CD1 1 
ATOM   5398 C CD2 . PHE D 2 67  ? 21.035  7.830   40.339  1.00 53.93  ?  67  PHE D CD2 1 
ATOM   5399 C CE1 . PHE D 2 67  ? 20.418  6.803   42.827  1.00 45.91  ?  67  PHE D CE1 1 
ATOM   5400 C CE2 . PHE D 2 67  ? 20.393  8.623   41.283  1.00 55.57  ?  67  PHE D CE2 1 
ATOM   5401 C CZ  . PHE D 2 67  ? 20.084  8.106   42.527  1.00 48.07  ?  67  PHE D CZ  1 
ATOM   5402 N N   . THR D 2 68  ? 24.882  4.063   39.173  1.00 37.16  ?  68  THR D N   1 
ATOM   5403 C CA  . THR D 2 68  ? 25.489  2.900   38.535  1.00 35.41  ?  68  THR D CA  1 
ATOM   5404 C C   . THR D 2 68  ? 25.222  1.681   39.399  1.00 35.38  ?  68  THR D C   1 
ATOM   5405 O O   . THR D 2 68  ? 25.596  1.663   40.576  1.00 35.76  ?  68  THR D O   1 
ATOM   5406 C CB  . THR D 2 68  ? 26.997  3.076   38.336  1.00 44.05  ?  68  THR D CB  1 
ATOM   5407 O OG1 . THR D 2 68  ? 27.248  4.105   37.371  1.00 43.56  ?  68  THR D OG1 1 
ATOM   5408 C CG2 . THR D 2 68  ? 27.621  1.762   37.863  1.00 39.22  ?  68  THR D CG2 1 
ATOM   5409 N N   . ILE D 2 69  ? 24.581  0.672   38.822  1.00 33.03  ?  69  ILE D N   1 
ATOM   5410 C CA  . ILE D 2 69  ? 24.383  -0.606  39.497  1.00 36.19  ?  69  ILE D CA  1 
ATOM   5411 C C   . ILE D 2 69  ? 25.548  -1.525  39.148  1.00 39.57  ?  69  ILE D C   1 
ATOM   5412 O O   . ILE D 2 69  ? 26.105  -1.471  38.044  1.00 40.58  ?  69  ILE D O   1 
ATOM   5413 C CB  . ILE D 2 69  ? 23.026  -1.232  39.111  1.00 39.57  ?  69  ILE D CB  1 
ATOM   5414 C CG1 . ILE D 2 69  ? 22.689  -2.415  40.020  1.00 37.72  ?  69  ILE D CG1 1 
ATOM   5415 C CG2 . ILE D 2 69  ? 23.031  -1.673  37.655  1.00 37.05  ?  69  ILE D CG2 1 
ATOM   5416 C CD1 . ILE D 2 69  ? 21.292  -2.959  39.799  1.00 35.06  ?  69  ILE D CD1 1 
ATOM   5417 N N   . SER D 2 70  ? 25.946  -2.365  40.099  1.00 37.36  ?  70  SER D N   1 
ATOM   5418 C CA  . SER D 2 70  ? 27.026  -3.308  39.835  1.00 37.24  ?  70  SER D CA  1 
ATOM   5419 C C   . SER D 2 70  ? 26.939  -4.438  40.845  1.00 36.77  ?  70  SER D C   1 
ATOM   5420 O O   . SER D 2 70  ? 26.135  -4.399  41.774  1.00 36.91  ?  70  SER D O   1 
ATOM   5421 C CB  . SER D 2 70  ? 28.398  -2.625  39.890  1.00 35.75  ?  70  SER D CB  1 
ATOM   5422 O OG  . SER D 2 70  ? 28.773  -2.368  41.231  1.00 39.32  ?  70  SER D OG  1 
ATOM   5423 N N   . ARG D 2 71  ? 27.784  -5.451  40.660  1.00 38.52  ?  71  ARG D N   1 
ATOM   5424 C CA  . ARG D 2 71  ? 27.841  -6.537  41.628  1.00 41.06  ?  71  ARG D CA  1 
ATOM   5425 C C   . ARG D 2 71  ? 29.244  -7.127  41.653  1.00 40.04  ?  71  ARG D C   1 
ATOM   5426 O O   . ARG D 2 71  ? 29.937  -7.160  40.635  1.00 42.79  ?  71  ARG D O   1 
ATOM   5427 C CB  . ARG D 2 71  ? 26.807  -7.632  41.322  1.00 43.12  ?  71  ARG D CB  1 
ATOM   5428 C CG  . ARG D 2 71  ? 27.002  -8.330  39.991  1.00 39.23  ?  71  ARG D CG  1 
ATOM   5429 C CD  . ARG D 2 71  ? 26.259  -9.663  39.931  1.00 38.77  ?  71  ARG D CD  1 
ATOM   5430 N NE  . ARG D 2 71  ? 26.560  -10.376 38.690  1.00 44.47  ?  71  ARG D NE  1 
ATOM   5431 C CZ  . ARG D 2 71  ? 25.692  -10.565 37.701  1.00 47.27  ?  71  ARG D CZ  1 
ATOM   5432 N NH1 . ARG D 2 71  ? 24.451  -10.108 37.807  1.00 49.74  ?  71  ARG D NH1 1 
ATOM   5433 N NH2 . ARG D 2 71  ? 26.061  -11.220 36.607  1.00 47.51  ?  71  ARG D NH2 1 
ATOM   5434 N N   . ASP D 2 72  ? 29.659  -7.575  42.838  1.00 39.29  ?  72  ASP D N   1 
ATOM   5435 C CA  . ASP D 2 72  ? 30.881  -8.351  43.009  1.00 41.68  ?  72  ASP D CA  1 
ATOM   5436 C C   . ASP D 2 72  ? 30.485  -9.809  43.235  1.00 40.29  ?  72  ASP D C   1 
ATOM   5437 O O   . ASP D 2 72  ? 29.914  -10.156 44.282  1.00 43.33  ?  72  ASP D O   1 
ATOM   5438 C CB  . ASP D 2 72  ? 31.726  -7.825  44.166  1.00 42.31  ?  72  ASP D CB  1 
ATOM   5439 C CG  . ASP D 2 72  ? 33.167  -8.336  44.115  1.00 45.76  ?  72  ASP D CG  1 
ATOM   5440 O OD1 . ASP D 2 72  ? 34.083  -7.571  44.478  1.00 52.60  ?  72  ASP D OD1 1 
ATOM   5441 O OD2 . ASP D 2 72  ? 33.389  -9.490  43.682  1.00 47.00  ?  72  ASP D OD2 1 
ATOM   5442 N N   . ASN D 2 73  ? 30.789  -10.652 42.241  1.00 35.53  ?  73  ASN D N   1 
ATOM   5443 C CA  . ASN D 2 73  ? 30.483  -12.077 42.324  1.00 38.17  ?  73  ASN D CA  1 
ATOM   5444 C C   . ASN D 2 73  ? 31.355  -12.777 43.355  1.00 41.82  ?  73  ASN D C   1 
ATOM   5445 O O   . ASN D 2 73  ? 30.925  -13.764 43.961  1.00 38.54  ?  73  ASN D O   1 
ATOM   5446 C CB  . ASN D 2 73  ? 30.670  -12.732 40.959  1.00 35.94  ?  73  ASN D CB  1 
ATOM   5447 C CG  . ASN D 2 73  ? 29.782  -12.126 39.901  1.00 43.99  ?  73  ASN D CG  1 
ATOM   5448 O OD1 . ASN D 2 73  ? 28.655  -11.731 40.180  1.00 42.59  ?  73  ASN D OD1 1 
ATOM   5449 N ND2 . ASN D 2 73  ? 30.286  -12.048 38.674  1.00 53.51  ?  73  ASN D ND2 1 
ATOM   5450 N N   . SER D 2 74  ? 32.582  -12.298 43.556  1.00 41.84  ?  74  SER D N   1 
ATOM   5451 C CA  . SER D 2 74  ? 33.431  -12.871 44.585  1.00 36.58  ?  74  SER D CA  1 
ATOM   5452 C C   . SER D 2 74  ? 32.962  -12.516 45.988  1.00 36.23  ?  74  SER D C   1 
ATOM   5453 O O   . SER D 2 74  ? 33.469  -13.089 46.956  1.00 40.50  ?  74  SER D O   1 
ATOM   5454 C CB  . SER D 2 74  ? 34.872  -12.411 44.385  1.00 36.27  ?  74  SER D CB  1 
ATOM   5455 O OG  . SER D 2 74  ? 35.025  -11.055 44.743  1.00 37.26  ?  74  SER D OG  1 
ATOM   5456 N N   . LYS D 2 75  ? 32.018  -11.588 46.128  1.00 35.76  ?  75  LYS D N   1 
ATOM   5457 C CA  . LYS D 2 75  ? 31.452  -11.258 47.426  1.00 38.46  ?  75  LYS D CA  1 
ATOM   5458 C C   . LYS D 2 75  ? 29.959  -11.534 47.514  1.00 38.82  ?  75  LYS D C   1 
ATOM   5459 O O   . LYS D 2 75  ? 29.379  -11.374 48.594  1.00 35.55  ?  75  LYS D O   1 
ATOM   5460 C CB  . LYS D 2 75  ? 31.728  -9.787  47.766  1.00 39.37  ?  75  LYS D CB  1 
ATOM   5461 C CG  . LYS D 2 75  ? 33.205  -9.453  47.894  1.00 41.85  ?  75  LYS D CG  1 
ATOM   5462 C CD  . LYS D 2 75  ? 33.404  -8.098  48.550  1.00 51.20  ?  75  LYS D CD  1 
ATOM   5463 C CE  . LYS D 2 75  ? 34.867  -7.698  48.558  1.00 51.61  ?  75  LYS D CE  1 
ATOM   5464 N NZ  . LYS D 2 75  ? 35.371  -7.486  47.176  1.00 53.37  ?  75  LYS D NZ  1 
ATOM   5465 N N   . ASN D 2 76  ? 29.333  -11.970 46.417  1.00 37.74  ?  76  ASN D N   1 
ATOM   5466 C CA  . ASN D 2 76  ? 27.890  -12.189 46.352  1.00 35.71  ?  76  ASN D CA  1 
ATOM   5467 C C   . ASN D 2 76  ? 27.126  -10.917 46.725  1.00 37.79  ?  76  ASN D C   1 
ATOM   5468 O O   . ASN D 2 76  ? 26.097  -10.965 47.406  1.00 37.77  ?  76  ASN D O   1 
ATOM   5469 C CB  . ASN D 2 76  ? 27.479  -13.365 47.245  1.00 30.46  ?  76  ASN D CB  1 
ATOM   5470 C CG  . ASN D 2 76  ? 26.288  -14.136 46.695  1.00 34.57  ?  76  ASN D CG  1 
ATOM   5471 O OD1 . ASN D 2 76  ? 26.079  -14.206 45.486  1.00 32.90  ?  76  ASN D OD1 1 
ATOM   5472 N ND2 . ASN D 2 76  ? 25.512  -14.732 47.586  1.00 33.50  ?  76  ASN D ND2 1 
ATOM   5473 N N   . THR D 2 77  ? 27.616  -9.762  46.261  1.00 38.45  ?  77  THR D N   1 
ATOM   5474 C CA  . THR D 2 77  ? 27.105  -8.487  46.758  1.00 34.96  ?  77  THR D CA  1 
ATOM   5475 C C   . THR D 2 77  ? 26.707  -7.558  45.621  1.00 36.50  ?  77  THR D C   1 
ATOM   5476 O O   . THR D 2 77  ? 27.427  -7.429  44.630  1.00 37.25  ?  77  THR D O   1 
ATOM   5477 C CB  . THR D 2 77  ? 28.146  -7.794  47.655  1.00 40.69  ?  77  THR D CB  1 
ATOM   5478 O OG1 . THR D 2 77  ? 28.420  -8.621  48.797  1.00 38.39  ?  77  THR D OG1 1 
ATOM   5479 C CG2 . THR D 2 77  ? 27.647  -6.426  48.124  1.00 36.87  ?  77  THR D CG2 1 
ATOM   5480 N N   . LEU D 2 78  ? 25.560  -6.905  45.777  1.00 39.58  ?  78  LEU D N   1 
ATOM   5481 C CA  . LEU D 2 78  ? 25.092  -5.887  44.847  1.00 41.47  ?  78  LEU D CA  1 
ATOM   5482 C C   . LEU D 2 78  ? 25.450  -4.497  45.369  1.00 39.93  ?  78  LEU D C   1 
ATOM   5483 O O   . LEU D 2 78  ? 25.512  -4.268  46.576  1.00 36.50  ?  78  LEU D O   1 
ATOM   5484 C CB  . LEU D 2 78  ? 23.580  -5.996  44.647  1.00 37.33  ?  78  LEU D CB  1 
ATOM   5485 C CG  . LEU D 2 78  ? 22.988  -5.307  43.423  1.00 38.77  ?  78  LEU D CG  1 
ATOM   5486 C CD1 . LEU D 2 78  ? 23.271  -6.121  42.163  1.00 38.26  ?  78  LEU D CD1 1 
ATOM   5487 C CD2 . LEU D 2 78  ? 21.499  -5.102  43.621  1.00 35.27  ?  78  LEU D CD2 1 
ATOM   5488 N N   . TYR D 2 79  ? 25.676  -3.565  44.444  1.00 39.77  ?  79  TYR D N   1 
ATOM   5489 C CA  . TYR D 2 79  ? 26.087  -2.206  44.763  1.00 36.90  ?  79  TYR D CA  1 
ATOM   5490 C C   . TYR D 2 79  ? 25.276  -1.223  43.936  1.00 36.70  ?  79  TYR D C   1 
ATOM   5491 O O   . TYR D 2 79  ? 24.961  -1.482  42.766  1.00 36.57  ?  79  TYR D O   1 
ATOM   5492 C CB  . TYR D 2 79  ? 27.585  -1.968  44.487  1.00 39.63  ?  79  TYR D CB  1 
ATOM   5493 C CG  . TYR D 2 79  ? 28.530  -2.824  45.301  1.00 39.88  ?  79  TYR D CG  1 
ATOM   5494 C CD1 . TYR D 2 79  ? 28.832  -2.497  46.617  1.00 37.91  ?  79  TYR D CD1 1 
ATOM   5495 C CD2 . TYR D 2 79  ? 29.129  -3.957  44.751  1.00 44.31  ?  79  TYR D CD2 1 
ATOM   5496 C CE1 . TYR D 2 79  ? 29.695  -3.272  47.372  1.00 40.50  ?  79  TYR D CE1 1 
ATOM   5497 C CE2 . TYR D 2 79  ? 29.997  -4.751  45.502  1.00 43.18  ?  79  TYR D CE2 1 
ATOM   5498 C CZ  . TYR D 2 79  ? 30.273  -4.400  46.813  1.00 46.00  ?  79  TYR D CZ  1 
ATOM   5499 O OH  . TYR D 2 79  ? 31.125  -5.177  47.567  1.00 47.28  ?  79  TYR D OH  1 
ATOM   5500 N N   . LEU D 2 80  ? 24.950  -0.092  44.555  1.00 38.67  ?  80  LEU D N   1 
ATOM   5501 C CA  . LEU D 2 80  ? 24.376  1.062   43.868  1.00 36.60  ?  80  LEU D CA  1 
ATOM   5502 C C   . LEU D 2 80  ? 25.235  2.277   44.198  1.00 41.21  ?  80  LEU D C   1 
ATOM   5503 O O   . LEU D 2 80  ? 25.241  2.742   45.344  1.00 37.51  ?  80  LEU D O   1 
ATOM   5504 C CB  . LEU D 2 80  ? 22.921  1.280   44.278  1.00 33.03  ?  80  LEU D CB  1 
ATOM   5505 C CG  . LEU D 2 80  ? 22.144  2.396   43.580  1.00 37.59  ?  80  LEU D CG  1 
ATOM   5506 C CD1 . LEU D 2 80  ? 22.100  2.174   42.070  1.00 34.27  ?  80  LEU D CD1 1 
ATOM   5507 C CD2 . LEU D 2 80  ? 20.737  2.489   44.150  1.00 35.82  ?  80  LEU D CD2 1 
ATOM   5508 N N   . GLN D 2 81  ? 25.983  2.770   43.208  1.00 42.43  ?  81  GLN D N   1 
ATOM   5509 C CA  . GLN D 2 81  ? 26.774  3.985   43.354  1.00 39.04  ?  81  GLN D CA  1 
ATOM   5510 C C   . GLN D 2 81  ? 25.944  5.186   42.913  1.00 41.66  ?  81  GLN D C   1 
ATOM   5511 O O   . GLN D 2 81  ? 25.346  5.168   41.830  1.00 39.20  ?  81  GLN D O   1 
ATOM   5512 C CB  . GLN D 2 81  ? 28.063  3.896   42.536  1.00 36.20  ?  81  GLN D CB  1 
ATOM   5513 C CG  . GLN D 2 81  ? 28.940  5.142   42.593  1.00 42.63  ?  81  GLN D CG  1 
ATOM   5514 C CD  . GLN D 2 81  ? 29.697  5.269   43.907  1.00 46.49  ?  81  GLN D CD  1 
ATOM   5515 O OE1 . GLN D 2 81  ? 30.202  4.286   44.445  1.00 47.36  ?  81  GLN D OE1 1 
ATOM   5516 N NE2 . GLN D 2 81  ? 29.763  6.485   44.438  1.00 52.16  ?  81  GLN D NE2 1 
ATOM   5517 N N   . MET D 2 82  ? 25.898  6.212   43.765  1.00 47.36  ?  82  MET D N   1 
ATOM   5518 C CA  . MET D 2 82  ? 25.128  7.433   43.547  1.00 51.23  ?  82  MET D CA  1 
ATOM   5519 C C   . MET D 2 82  ? 26.071  8.631   43.600  1.00 46.84  ?  82  MET D C   1 
ATOM   5520 O O   . MET D 2 82  ? 26.689  8.883   44.642  1.00 47.25  ?  82  MET D O   1 
ATOM   5521 C CB  . MET D 2 82  ? 24.037  7.561   44.615  1.00 46.82  ?  82  MET D CB  1 
ATOM   5522 C CG  . MET D 2 82  ? 23.170  6.317   44.735  1.00 52.51  ?  82  MET D CG  1 
ATOM   5523 S SD  . MET D 2 82  ? 21.876  6.399   45.990  1.00 61.93  ?  82  MET D SD  1 
ATOM   5524 C CE  . MET D 2 82  ? 22.831  6.199   47.484  1.00 50.78  ?  82  MET D CE  1 
ATOM   5525 N N   . ASN D 2 83  ? 26.179  9.369   42.489  1.00 52.36  ?  83  ASN D N   1 
ATOM   5526 C CA  . ASN D 2 83  ? 27.017  10.565  42.416  1.00 51.20  ?  83  ASN D CA  1 
ATOM   5527 C C   . ASN D 2 83  ? 26.180  11.835  42.367  1.00 49.00  ?  83  ASN D C   1 
ATOM   5528 O O   . ASN D 2 83  ? 25.050  11.833  41.871  1.00 49.14  ?  83  ASN D O   1 
ATOM   5529 C CB  . ASN D 2 83  ? 27.928  10.558  41.188  1.00 39.92  ?  83  ASN D CB  1 
ATOM   5530 C CG  . ASN D 2 83  ? 28.873  9.395   41.179  1.00 50.03  ?  83  ASN D CG  1 
ATOM   5531 O OD1 . ASN D 2 83  ? 29.431  9.029   42.212  1.00 49.29  ?  83  ASN D OD1 1 
ATOM   5532 N ND2 . ASN D 2 83  ? 29.076  8.808   40.004  1.00 57.54  ?  83  ASN D ND2 1 
ATOM   5533 N N   . SER D 2 84  ? 26.774  12.921  42.863  1.00 48.96  ?  84  SER D N   1 
ATOM   5534 C CA  . SER D 2 84  ? 26.189  14.268  42.865  1.00 54.97  ?  84  SER D CA  1 
ATOM   5535 C C   . SER D 2 84  ? 24.707  14.225  43.249  1.00 57.47  ?  84  SER D C   1 
ATOM   5536 O O   . SER D 2 84  ? 23.815  14.609  42.492  1.00 55.02  ?  84  SER D O   1 
ATOM   5537 C CB  . SER D 2 84  ? 26.408  14.975  41.522  1.00 54.58  ?  84  SER D CB  1 
ATOM   5538 O OG  . SER D 2 84  ? 25.881  14.236  40.434  1.00 62.23  ?  84  SER D OG  1 
ATOM   5539 N N   . LEU D 2 85  ? 24.464  13.728  44.456  1.00 55.32  ?  85  LEU D N   1 
ATOM   5540 C CA  . LEU D 2 85  ? 23.103  13.503  44.911  1.00 53.31  ?  85  LEU D CA  1 
ATOM   5541 C C   . LEU D 2 85  ? 22.393  14.823  45.160  1.00 51.72  ?  85  LEU D C   1 
ATOM   5542 O O   . LEU D 2 85  ? 23.001  15.801  45.601  1.00 52.92  ?  85  LEU D O   1 
ATOM   5543 C CB  . LEU D 2 85  ? 23.116  12.670  46.189  1.00 54.60  ?  85  LEU D CB  1 
ATOM   5544 C CG  . LEU D 2 85  ? 23.401  11.185  45.999  1.00 48.49  ?  85  LEU D CG  1 
ATOM   5545 C CD1 . LEU D 2 85  ? 23.811  10.581  47.322  1.00 46.19  ?  85  LEU D CD1 1 
ATOM   5546 C CD2 . LEU D 2 85  ? 22.169  10.493  45.442  1.00 48.07  ?  85  LEU D CD2 1 
ATOM   5547 N N   . ARG D 2 86  ? 21.104  14.855  44.845  1.00 52.94  ?  86  ARG D N   1 
ATOM   5548 C CA  . ARG D 2 86  ? 20.265  16.006  45.134  1.00 53.96  ?  86  ARG D CA  1 
ATOM   5549 C C   . ARG D 2 86  ? 19.203  15.610  46.159  1.00 49.37  ?  86  ARG D C   1 
ATOM   5550 O O   . ARG D 2 86  ? 18.856  14.437  46.303  1.00 54.59  ?  86  ARG D O   1 
ATOM   5551 C CB  . ARG D 2 86  ? 19.674  16.584  43.841  1.00 55.70  ?  86  ARG D CB  1 
ATOM   5552 C CG  . ARG D 2 86  ? 20.808  16.987  42.879  1.00 61.49  ?  86  ARG D CG  1 
ATOM   5553 C CD  . ARG D 2 86  ? 20.390  17.616  41.548  1.00 75.98  ?  86  ARG D CD  1 
ATOM   5554 N NE  . ARG D 2 86  ? 19.896  18.988  41.711  1.00 75.97  ?  86  ARG D NE  1 
ATOM   5555 C CZ  . ARG D 2 86  ? 19.457  19.762  40.718  1.00 71.01  ?  86  ARG D CZ  1 
ATOM   5556 N NH1 . ARG D 2 86  ? 19.027  20.993  40.974  1.00 79.64  ?  86  ARG D NH1 1 
ATOM   5557 N NH2 . ARG D 2 86  ? 19.457  19.317  39.467  1.00 62.29  ?  86  ARG D NH2 1 
ATOM   5558 N N   . ALA D 2 87  ? 18.699  16.609  46.888  1.00 48.87  ?  87  ALA D N   1 
ATOM   5559 C CA  . ALA D 2 87  ? 17.760  16.364  47.982  1.00 48.54  ?  87  ALA D CA  1 
ATOM   5560 C C   . ALA D 2 87  ? 16.566  15.508  47.573  1.00 49.02  ?  87  ALA D C   1 
ATOM   5561 O O   . ALA D 2 87  ? 16.020  14.771  48.401  1.00 45.59  ?  87  ALA D O   1 
ATOM   5562 C CB  . ALA D 2 87  ? 17.272  17.698  48.553  1.00 48.36  ?  87  ALA D CB  1 
ATOM   5563 N N   . GLU D 2 88  ? 16.135  15.598  46.318  1.00 50.83  ?  88  GLU D N   1 
ATOM   5564 C CA  . GLU D 2 88  ? 15.054  14.743  45.844  1.00 49.88  ?  88  GLU D CA  1 
ATOM   5565 C C   . GLU D 2 88  ? 15.445  13.269  45.801  1.00 51.36  ?  88  GLU D C   1 
ATOM   5566 O O   . GLU D 2 88  ? 14.565  12.418  45.631  1.00 54.16  ?  88  GLU D O   1 
ATOM   5567 C CB  . GLU D 2 88  ? 14.587  15.211  44.463  1.00 45.45  ?  88  GLU D CB  1 
ATOM   5568 C CG  . GLU D 2 88  ? 13.918  16.585  44.467  1.00 64.87  ?  88  GLU D CG  1 
ATOM   5569 C CD  . GLU D 2 88  ? 14.883  17.737  44.714  1.00 59.14  ?  88  GLU D CD  1 
ATOM   5570 O OE1 . GLU D 2 88  ? 14.407  18.830  45.088  1.00 59.37  ?  88  GLU D OE1 1 
ATOM   5571 O OE2 . GLU D 2 88  ? 16.110  17.551  44.554  1.00 56.67  ?  88  GLU D OE2 1 
ATOM   5572 N N   . ASP D 2 89  ? 16.729  12.943  45.968  1.00 41.85  ?  89  ASP D N   1 
ATOM   5573 C CA  . ASP D 2 89  ? 17.129  11.545  46.039  1.00 45.86  ?  89  ASP D CA  1 
ATOM   5574 C C   . ASP D 2 89  ? 16.890  10.935  47.416  1.00 46.02  ?  89  ASP D C   1 
ATOM   5575 O O   . ASP D 2 89  ? 17.058  9.720   47.575  1.00 42.22  ?  89  ASP D O   1 
ATOM   5576 C CB  . ASP D 2 89  ? 18.602  11.391  45.653  1.00 42.23  ?  89  ASP D CB  1 
ATOM   5577 C CG  . ASP D 2 89  ? 18.889  11.850  44.232  1.00 48.38  ?  89  ASP D CG  1 
ATOM   5578 O OD1 . ASP D 2 89  ? 19.921  12.523  44.019  1.00 53.68  ?  89  ASP D OD1 1 
ATOM   5579 O OD2 . ASP D 2 89  ? 18.083  11.557  43.326  1.00 48.99  ?  89  ASP D OD2 1 
ATOM   5580 N N   . THR D 2 90  ? 16.504  11.743  48.405  1.00 41.33  ?  90  THR D N   1 
ATOM   5581 C CA  . THR D 2 90  ? 16.183  11.225  49.729  1.00 41.66  ?  90  THR D CA  1 
ATOM   5582 C C   . THR D 2 90  ? 15.074  10.189  49.638  1.00 40.23  ?  90  THR D C   1 
ATOM   5583 O O   . THR D 2 90  ? 13.965  10.494  49.187  1.00 42.95  ?  90  THR D O   1 
ATOM   5584 C CB  . THR D 2 90  ? 15.762  12.369  50.649  1.00 41.64  ?  90  THR D CB  1 
ATOM   5585 O OG1 . THR D 2 90  ? 16.879  13.245  50.858  1.00 44.33  ?  90  THR D OG1 1 
ATOM   5586 C CG2 . THR D 2 90  ? 15.253  11.831  51.988  1.00 33.53  ?  90  THR D CG2 1 
ATOM   5587 N N   . ALA D 2 91  ? 15.369  8.966   50.070  1.00 40.05  ?  91  ALA D N   1 
ATOM   5588 C CA  . ALA D 2 91  ? 14.417  7.874   49.900  1.00 39.06  ?  91  ALA D CA  1 
ATOM   5589 C C   . ALA D 2 91  ? 14.925  6.649   50.643  1.00 40.12  ?  91  ALA D C   1 
ATOM   5590 O O   . ALA D 2 91  ? 16.095  6.568   51.022  1.00 38.70  ?  91  ALA D O   1 
ATOM   5591 C CB  . ALA D 2 91  ? 14.201  7.539   48.419  1.00 34.24  ?  91  ALA D CB  1 
ATOM   5592 N N   . VAL D 2 92  ? 14.025  5.690   50.838  1.00 38.34  ?  92  VAL D N   1 
ATOM   5593 C CA  . VAL D 2 92  ? 14.426  4.345   51.222  1.00 39.15  ?  92  VAL D CA  1 
ATOM   5594 C C   . VAL D 2 92  ? 14.811  3.593   49.957  1.00 39.01  ?  92  VAL D C   1 
ATOM   5595 O O   . VAL D 2 92  ? 14.060  3.584   48.975  1.00 37.51  ?  92  VAL D O   1 
ATOM   5596 C CB  . VAL D 2 92  ? 13.289  3.632   51.966  1.00 35.67  ?  92  VAL D CB  1 
ATOM   5597 C CG1 . VAL D 2 92  ? 13.671  2.183   52.233  1.00 40.70  ?  92  VAL D CG1 1 
ATOM   5598 C CG2 . VAL D 2 92  ? 12.949  4.358   53.250  1.00 29.03  ?  92  VAL D CG2 1 
ATOM   5599 N N   . TYR D 2 93  ? 15.980  2.965   49.964  1.00 34.55  ?  93  TYR D N   1 
ATOM   5600 C CA  . TYR D 2 93  ? 16.440  2.196   48.818  1.00 36.82  ?  93  TYR D CA  1 
ATOM   5601 C C   . TYR D 2 93  ? 16.392  0.710   49.149  1.00 42.41  ?  93  TYR D C   1 
ATOM   5602 O O   . TYR D 2 93  ? 16.989  0.264   50.141  1.00 43.19  ?  93  TYR D O   1 
ATOM   5603 C CB  . TYR D 2 93  ? 17.836  2.635   48.393  1.00 37.80  ?  93  TYR D CB  1 
ATOM   5604 C CG  . TYR D 2 93  ? 17.817  3.983   47.718  1.00 40.11  ?  93  TYR D CG  1 
ATOM   5605 C CD1 . TYR D 2 93  ? 17.842  4.087   46.334  1.00 37.22  ?  93  TYR D CD1 1 
ATOM   5606 C CD2 . TYR D 2 93  ? 17.726  5.152   48.463  1.00 40.02  ?  93  TYR D CD2 1 
ATOM   5607 C CE1 . TYR D 2 93  ? 17.806  5.317   45.712  1.00 40.61  ?  93  TYR D CE1 1 
ATOM   5608 C CE2 . TYR D 2 93  ? 17.692  6.387   47.851  1.00 41.03  ?  93  TYR D CE2 1 
ATOM   5609 C CZ  . TYR D 2 93  ? 17.732  6.465   46.477  1.00 40.00  ?  93  TYR D CZ  1 
ATOM   5610 O OH  . TYR D 2 93  ? 17.694  7.695   45.868  1.00 40.94  ?  93  TYR D OH  1 
ATOM   5611 N N   . TYR D 2 94  ? 15.666  -0.039  48.321  1.00 38.29  ?  94  TYR D N   1 
ATOM   5612 C CA  . TYR D 2 94  ? 15.437  -1.463  48.477  1.00 35.22  ?  94  TYR D CA  1 
ATOM   5613 C C   . TYR D 2 94  ? 16.237  -2.218  47.432  1.00 37.17  ?  94  TYR D C   1 
ATOM   5614 O O   . TYR D 2 94  ? 16.187  -1.895  46.237  1.00 38.38  ?  94  TYR D O   1 
ATOM   5615 C CB  . TYR D 2 94  ? 13.960  -1.825  48.297  1.00 31.78  ?  94  TYR D CB  1 
ATOM   5616 C CG  . TYR D 2 94  ? 13.009  -1.314  49.347  1.00 37.56  ?  94  TYR D CG  1 
ATOM   5617 C CD1 . TYR D 2 94  ? 12.179  -0.232  49.081  1.00 38.79  ?  94  TYR D CD1 1 
ATOM   5618 C CD2 . TYR D 2 94  ? 12.900  -1.936  50.585  1.00 37.07  ?  94  TYR D CD2 1 
ATOM   5619 C CE1 . TYR D 2 94  ? 11.283  0.234   50.022  1.00 41.63  ?  94  TYR D CE1 1 
ATOM   5620 C CE2 . TYR D 2 94  ? 12.006  -1.471  51.543  1.00 38.41  ?  94  TYR D CE2 1 
ATOM   5621 C CZ  . TYR D 2 94  ? 11.197  -0.386  51.251  1.00 41.76  ?  94  TYR D CZ  1 
ATOM   5622 O OH  . TYR D 2 94  ? 10.300  0.095   52.181  1.00 43.62  ?  94  TYR D OH  1 
ATOM   5623 N N   . CYS D 2 95  ? 16.963  -3.218  47.903  1.00 43.26  ?  95  CYS D N   1 
ATOM   5624 C CA  . CYS D 2 95  ? 17.425  -4.323  47.083  1.00 42.69  ?  95  CYS D CA  1 
ATOM   5625 C C   . CYS D 2 95  ? 16.246  -5.242  46.758  1.00 43.63  ?  95  CYS D C   1 
ATOM   5626 O O   . CYS D 2 95  ? 15.415  -5.531  47.627  1.00 36.71  ?  95  CYS D O   1 
ATOM   5627 C CB  . CYS D 2 95  ? 18.493  -5.067  47.875  1.00 39.02  ?  95  CYS D CB  1 
ATOM   5628 S SG  . CYS D 2 95  ? 19.632  -6.071  47.009  1.00 60.22  ?  95  CYS D SG  1 
ATOM   5629 N N   . ALA D 2 96  ? 16.151  -5.697  45.506  1.00 42.10  ?  96  ALA D N   1 
ATOM   5630 C CA  . ALA D 2 96  ? 15.026  -6.557  45.149  1.00 40.33  ?  96  ALA D CA  1 
ATOM   5631 C C   . ALA D 2 96  ? 15.419  -7.540  44.053  1.00 41.56  ?  96  ALA D C   1 
ATOM   5632 O O   . ALA D 2 96  ? 16.061  -7.169  43.068  1.00 43.67  ?  96  ALA D O   1 
ATOM   5633 C CB  . ALA D 2 96  ? 13.814  -5.725  44.708  1.00 37.76  ?  96  ALA D CB  1 
ATOM   5634 N N   . ARG D 2 97  ? 14.998  -8.790  44.212  1.00 38.50  ?  97  ARG D N   1 
ATOM   5635 C CA  . ARG D 2 97  ? 15.321  -9.849  43.266  1.00 38.33  ?  97  ARG D CA  1 
ATOM   5636 C C   . ARG D 2 97  ? 14.147  -10.077 42.322  1.00 39.73  ?  97  ARG D C   1 
ATOM   5637 O O   . ARG D 2 97  ? 13.015  -10.295 42.767  1.00 38.22  ?  97  ARG D O   1 
ATOM   5638 C CB  . ARG D 2 97  ? 15.667  -11.143 44.003  1.00 44.44  ?  97  ARG D CB  1 
ATOM   5639 C CG  . ARG D 2 97  ? 16.110  -12.275 43.100  1.00 40.15  ?  97  ARG D CG  1 
ATOM   5640 C CD  . ARG D 2 97  ? 16.427  -13.501 43.913  1.00 39.58  ?  97  ARG D CD  1 
ATOM   5641 N NE  . ARG D 2 97  ? 15.230  -14.229 44.314  1.00 44.09  ?  97  ARG D NE  1 
ATOM   5642 C CZ  . ARG D 2 97  ? 15.251  -15.339 45.045  1.00 40.73  ?  97  ARG D CZ  1 
ATOM   5643 N NH1 . ARG D 2 97  ? 14.119  -15.954 45.364  1.00 31.77  ?  97  ARG D NH1 1 
ATOM   5644 N NH2 . ARG D 2 97  ? 16.409  -15.818 45.480  1.00 39.54  ?  97  ARG D NH2 1 
ATOM   5645 N N   . GLU D 2 98  ? 14.416  -10.020 41.023  1.00 42.65  ?  98  GLU D N   1 
ATOM   5646 C CA  . GLU D 2 98  ? 13.423  -10.290 39.998  1.00 41.38  ?  98  GLU D CA  1 
ATOM   5647 C C   . GLU D 2 98  ? 13.607  -11.705 39.476  1.00 45.53  ?  98  GLU D C   1 
ATOM   5648 O O   . GLU D 2 98  ? 14.708  -12.080 39.054  1.00 46.19  ?  98  GLU D O   1 
ATOM   5649 C CB  . GLU D 2 98  ? 13.544  -9.294  38.847  1.00 39.49  ?  98  GLU D CB  1 
ATOM   5650 C CG  . GLU D 2 98  ? 12.760  -9.693  37.618  1.00 44.30  ?  98  GLU D CG  1 
ATOM   5651 C CD  . GLU D 2 98  ? 13.091  -8.828  36.419  1.00 48.35  ?  98  GLU D CD  1 
ATOM   5652 O OE1 . GLU D 2 98  ? 13.877  -7.870  36.578  1.00 47.28  ?  98  GLU D OE1 1 
ATOM   5653 O OE2 . GLU D 2 98  ? 12.576  -9.111  35.318  1.00 50.41  ?  98  GLU D OE2 1 
ATOM   5654 N N   . ASP D 2 99  ? 12.536  -12.493 39.525  1.00 42.69  ?  99  ASP D N   1 
ATOM   5655 C CA  . ASP D 2 99  ? 12.543  -13.830 38.947  1.00 48.19  ?  99  ASP D CA  1 
ATOM   5656 C C   . ASP D 2 99  ? 12.051  -13.750 37.509  1.00 47.33  ?  99  ASP D C   1 
ATOM   5657 O O   . ASP D 2 99  ? 10.880  -13.445 37.262  1.00 49.32  ?  99  ASP D O   1 
ATOM   5658 C CB  . ASP D 2 99  ? 11.689  -14.795 39.760  1.00 56.08  ?  99  ASP D CB  1 
ATOM   5659 C CG  . ASP D 2 99  ? 11.601  -16.163 39.112  1.00 56.34  ?  99  ASP D CG  1 
ATOM   5660 O OD1 . ASP D 2 99  ? 12.646  -16.850 39.048  1.00 49.78  ?  99  ASP D OD1 1 
ATOM   5661 O OD2 . ASP D 2 99  ? 10.493  -16.547 38.671  1.00 54.89  ?  99  ASP D OD2 1 
ATOM   5662 N N   . VAL D 2 100 ? 12.949  -14.034 36.562  1.00 48.60  ?  100 VAL D N   1 
ATOM   5663 C CA  . VAL D 2 100 ? 12.586  -14.081 35.149  1.00 49.75  ?  100 VAL D CA  1 
ATOM   5664 C C   . VAL D 2 100 ? 12.194  -15.482 34.697  1.00 46.44  ?  100 VAL D C   1 
ATOM   5665 O O   . VAL D 2 100 ? 11.638  -15.636 33.598  1.00 46.17  ?  100 VAL D O   1 
ATOM   5666 C CB  . VAL D 2 100 ? 13.744  -13.567 34.266  1.00 49.04  ?  100 VAL D CB  1 
ATOM   5667 C CG1 . VAL D 2 100 ? 14.107  -12.147 34.644  1.00 49.71  ?  100 VAL D CG1 1 
ATOM   5668 C CG2 . VAL D 2 100 ? 14.962  -14.488 34.377  1.00 47.53  ?  100 VAL D CG2 1 
ATOM   5669 N N   . ALA D 2 101 ? 12.461  -16.509 35.508  1.00 46.93  ?  101 ALA D N   1 
ATOM   5670 C CA  . ALA D 2 101 ? 12.155  -17.874 35.098  1.00 49.88  ?  101 ALA D CA  1 
ATOM   5671 C C   . ALA D 2 101 ? 10.661  -18.054 34.861  1.00 49.26  ?  101 ALA D C   1 
ATOM   5672 O O   . ALA D 2 101 ? 10.245  -18.550 33.808  1.00 46.80  ?  101 ALA D O   1 
ATOM   5673 C CB  . ALA D 2 101 ? 12.658  -18.862 36.152  1.00 50.25  ?  101 ALA D CB  1 
ATOM   5674 N N   . VAL D 2 102 ? 9.837   -17.642 35.824  1.00 48.15  ?  102 VAL D N   1 
ATOM   5675 C CA  . VAL D 2 102 ? 8.394   -17.842 35.737  1.00 48.62  ?  102 VAL D CA  1 
ATOM   5676 C C   . VAL D 2 102 ? 7.653   -16.533 35.968  1.00 46.19  ?  102 VAL D C   1 
ATOM   5677 O O   . VAL D 2 102 ? 6.837   -16.116 35.138  1.00 48.93  ?  102 VAL D O   1 
ATOM   5678 C CB  . VAL D 2 102 ? 7.918   -18.909 36.738  1.00 52.32  ?  102 VAL D CB  1 
ATOM   5679 C CG1 . VAL D 2 102 ? 6.402   -19.054 36.673  1.00 42.07  ?  102 VAL D CG1 1 
ATOM   5680 C CG2 . VAL D 2 102 ? 8.602   -20.236 36.463  1.00 49.86  ?  102 VAL D CG2 1 
ATOM   5681 N N   . TYR D 2 103 ? 7.921   -15.887 37.106  1.00 44.59  ?  103 TYR D N   1 
ATOM   5682 C CA  . TYR D 2 103 ? 7.087   -14.773 37.551  1.00 46.13  ?  103 TYR D CA  1 
ATOM   5683 C C   . TYR D 2 103 ? 7.173   -13.579 36.607  1.00 44.88  ?  103 TYR D C   1 
ATOM   5684 O O   . TYR D 2 103 ? 6.150   -12.961 36.291  1.00 46.77  ?  103 TYR D O   1 
ATOM   5685 C CB  . TYR D 2 103 ? 7.491   -14.335 38.958  1.00 49.29  ?  103 TYR D CB  1 
ATOM   5686 C CG  . TYR D 2 103 ? 7.296   -15.367 40.045  1.00 59.57  ?  103 TYR D CG  1 
ATOM   5687 C CD1 . TYR D 2 103 ? 6.256   -16.288 39.990  1.00 58.13  ?  103 TYR D CD1 1 
ATOM   5688 C CD2 . TYR D 2 103 ? 8.162   -15.419 41.134  1.00 61.99  ?  103 TYR D CD2 1 
ATOM   5689 C CE1 . TYR D 2 103 ? 6.084   -17.230 40.992  1.00 60.92  ?  103 TYR D CE1 1 
ATOM   5690 C CE2 . TYR D 2 103 ? 7.999   -16.354 42.138  1.00 63.66  ?  103 TYR D CE2 1 
ATOM   5691 C CZ  . TYR D 2 103 ? 6.960   -17.257 42.064  1.00 69.98  ?  103 TYR D CZ  1 
ATOM   5692 O OH  . TYR D 2 103 ? 6.802   -18.187 43.067  1.00 84.73  ?  103 TYR D OH  1 
ATOM   5693 N N   . MET D 2 104 ? 8.380   -13.233 36.157  1.00 41.94  ?  104 MET D N   1 
ATOM   5694 C CA  . MET D 2 104 ? 8.645   -11.915 35.578  1.00 46.26  ?  104 MET D CA  1 
ATOM   5695 C C   . MET D 2 104 ? 8.165   -10.822 36.535  1.00 44.71  ?  104 MET D C   1 
ATOM   5696 O O   . MET D 2 104 ? 7.490   -9.865  36.153  1.00 39.42  ?  104 MET D O   1 
ATOM   5697 C CB  . MET D 2 104 ? 8.013   -11.767 34.190  1.00 44.92  ?  104 MET D CB  1 
ATOM   5698 C CG  . MET D 2 104 ? 8.694   -12.573 33.079  1.00 40.59  ?  104 MET D CG  1 
ATOM   5699 S SD  . MET D 2 104 ? 10.407  -12.080 32.742  1.00 48.94  ?  104 MET D SD  1 
ATOM   5700 C CE  . MET D 2 104 ? 10.170  -10.472 31.991  1.00 41.14  ?  104 MET D CE  1 
ATOM   5701 N N   . ALA D 2 105 ? 8.504   -11.002 37.809  1.00 41.92  ?  105 ALA D N   1 
ATOM   5702 C CA  . ALA D 2 105 ? 8.123   -10.082 38.867  1.00 40.83  ?  105 ALA D CA  1 
ATOM   5703 C C   . ALA D 2 105 ? 9.182   -10.151 39.963  1.00 44.16  ?  105 ALA D C   1 
ATOM   5704 O O   . ALA D 2 105 ? 10.129  -10.939 39.887  1.00 43.92  ?  105 ALA D O   1 
ATOM   5705 C CB  . ALA D 2 105 ? 6.726   -10.409 39.398  1.00 37.53  ?  105 ALA D CB  1 
ATOM   5706 N N   . ILE D 2 106 ? 9.018   -9.319  40.987  1.00 40.02  ?  106 ILE D N   1 
ATOM   5707 C CA  . ILE D 2 106 ? 9.945   -9.269  42.113  1.00 41.60  ?  106 ILE D CA  1 
ATOM   5708 C C   . ILE D 2 106 ? 9.420   -10.181 43.214  1.00 42.17  ?  106 ILE D C   1 
ATOM   5709 O O   . ILE D 2 106 ? 8.287   -10.012 43.680  1.00 43.13  ?  106 ILE D O   1 
ATOM   5710 C CB  . ILE D 2 106 ? 10.121  -7.833  42.627  1.00 38.91  ?  106 ILE D CB  1 
ATOM   5711 C CG1 . ILE D 2 106 ? 10.839  -6.982  41.580  1.00 38.34  ?  106 ILE D CG1 1 
ATOM   5712 C CG2 . ILE D 2 106 ? 10.884  -7.828  43.950  1.00 39.87  ?  106 ILE D CG2 1 
ATOM   5713 C CD1 . ILE D 2 106 ? 11.024  -5.537  41.989  1.00 45.28  ?  106 ILE D CD1 1 
ATOM   5714 N N   . ASP D 2 107 ? 10.242  -11.142 43.643  1.00 37.80  ?  107 ASP D N   1 
ATOM   5715 C CA  . ASP D 2 107 ? 9.796   -12.128 44.619  1.00 40.53  ?  107 ASP D CA  1 
ATOM   5716 C C   . ASP D 2 107 ? 10.533  -12.047 45.948  1.00 39.83  ?  107 ASP D C   1 
ATOM   5717 O O   . ASP D 2 107 ? 10.231  -12.833 46.851  1.00 40.83  ?  107 ASP D O   1 
ATOM   5718 C CB  . ASP D 2 107 ? 9.898   -13.553 44.044  1.00 36.14  ?  107 ASP D CB  1 
ATOM   5719 C CG  . ASP D 2 107 ? 11.313  -14.122 44.081  1.00 48.89  ?  107 ASP D CG  1 
ATOM   5720 O OD1 . ASP D 2 107 ? 12.294  -13.352 43.969  1.00 47.99  ?  107 ASP D OD1 1 
ATOM   5721 O OD2 . ASP D 2 107 ? 11.441  -15.362 44.211  1.00 50.74  ?  107 ASP D OD2 1 
ATOM   5722 N N   . LEU D 2 108 ? 11.470  -11.115 46.106  1.00 36.65  ?  108 LEU D N   1 
ATOM   5723 C CA  . LEU D 2 108 ? 12.247  -11.029 47.337  1.00 40.55  ?  108 LEU D CA  1 
ATOM   5724 C C   . LEU D 2 108 ? 12.775  -9.612  47.503  1.00 39.82  ?  108 LEU D C   1 
ATOM   5725 O O   . LEU D 2 108 ? 13.415  -9.085  46.590  1.00 42.48  ?  108 LEU D O   1 
ATOM   5726 C CB  . LEU D 2 108 ? 13.406  -12.032 47.309  1.00 40.82  ?  108 LEU D CB  1 
ATOM   5727 C CG  . LEU D 2 108 ? 14.392  -11.993 48.472  1.00 40.64  ?  108 LEU D CG  1 
ATOM   5728 C CD1 . LEU D 2 108 ? 13.719  -12.434 49.763  1.00 33.05  ?  108 LEU D CD1 1 
ATOM   5729 C CD2 . LEU D 2 108 ? 15.601  -12.861 48.151  1.00 39.40  ?  108 LEU D CD2 1 
ATOM   5730 N N   . TRP D 2 109 ? 12.513  -9.001  48.660  1.00 42.00  ?  109 TRP D N   1 
ATOM   5731 C CA  . TRP D 2 109 ? 12.958  -7.643  48.954  1.00 38.54  ?  109 TRP D CA  1 
ATOM   5732 C C   . TRP D 2 109 ? 13.936  -7.645  50.121  1.00 37.48  ?  109 TRP D C   1 
ATOM   5733 O O   . TRP D 2 109 ? 13.890  -8.522  50.990  1.00 41.20  ?  109 TRP D O   1 
ATOM   5734 C CB  . TRP D 2 109 ? 11.775  -6.716  49.296  1.00 35.82  ?  109 TRP D CB  1 
ATOM   5735 C CG  . TRP D 2 109 ? 10.794  -6.539  48.181  1.00 36.12  ?  109 TRP D CG  1 
ATOM   5736 C CD1 . TRP D 2 109 ? 9.915   -7.463  47.724  1.00 33.22  ?  109 TRP D CD1 1 
ATOM   5737 C CD2 . TRP D 2 109 ? 10.584  -5.360  47.390  1.00 42.36  ?  109 TRP D CD2 1 
ATOM   5738 N NE1 . TRP D 2 109 ? 9.171   -6.946  46.693  1.00 34.90  ?  109 TRP D NE1 1 
ATOM   5739 C CE2 . TRP D 2 109 ? 9.559   -5.655  46.467  1.00 38.00  ?  109 TRP D CE2 1 
ATOM   5740 C CE3 . TRP D 2 109 ? 11.162  -4.084  47.370  1.00 38.56  ?  109 TRP D CE3 1 
ATOM   5741 C CZ2 . TRP D 2 109 ? 9.101   -4.727  45.529  1.00 38.13  ?  109 TRP D CZ2 1 
ATOM   5742 C CZ3 . TRP D 2 109 ? 10.703  -3.157  46.438  1.00 36.22  ?  109 TRP D CZ3 1 
ATOM   5743 C CH2 . TRP D 2 109 ? 9.683   -3.486  45.531  1.00 39.57  ?  109 TRP D CH2 1 
ATOM   5744 N N   . GLY D 2 110 ? 14.821  -6.648  50.139  1.00 38.80  ?  110 GLY D N   1 
ATOM   5745 C CA  . GLY D 2 110 ? 15.600  -6.353  51.322  1.00 36.67  ?  110 GLY D CA  1 
ATOM   5746 C C   . GLY D 2 110 ? 14.777  -5.556  52.317  1.00 38.19  ?  110 GLY D C   1 
ATOM   5747 O O   . GLY D 2 110 ? 13.593  -5.287  52.116  1.00 40.06  ?  110 GLY D O   1 
ATOM   5748 N N   . GLN D 2 111 ? 15.414  -5.183  53.427  1.00 40.28  ?  111 GLN D N   1 
ATOM   5749 C CA  . GLN D 2 111 ? 14.711  -4.372  54.418  1.00 45.70  ?  111 GLN D CA  1 
ATOM   5750 C C   . GLN D 2 111 ? 14.733  -2.880  54.087  1.00 44.04  ?  111 GLN D C   1 
ATOM   5751 O O   . GLN D 2 111 ? 13.969  -2.117  54.687  1.00 44.05  ?  111 GLN D O   1 
ATOM   5752 C CB  . GLN D 2 111 ? 15.288  -4.620  55.821  1.00 43.63  ?  111 GLN D CB  1 
ATOM   5753 C CG  . GLN D 2 111 ? 16.427  -3.699  56.247  1.00 46.76  ?  111 GLN D CG  1 
ATOM   5754 C CD  . GLN D 2 111 ? 17.787  -4.216  55.808  1.00 52.02  ?  111 GLN D CD  1 
ATOM   5755 O OE1 . GLN D 2 111 ? 17.872  -5.184  55.055  1.00 54.59  ?  111 GLN D OE1 1 
ATOM   5756 N NE2 . GLN D 2 111 ? 18.857  -3.582  56.289  1.00 48.22  ?  111 GLN D NE2 1 
ATOM   5757 N N   . GLY D 2 112 ? 15.559  -2.455  53.134  1.00 41.46  ?  112 GLY D N   1 
ATOM   5758 C CA  . GLY D 2 112 ? 15.654  -1.059  52.768  1.00 39.68  ?  112 GLY D CA  1 
ATOM   5759 C C   . GLY D 2 112 ? 16.639  -0.312  53.637  1.00 44.48  ?  112 GLY D C   1 
ATOM   5760 O O   . GLY D 2 112 ? 16.783  -0.619  54.825  1.00 46.47  ?  112 GLY D O   1 
ATOM   5761 N N   . THR D 2 113 ? 17.350  0.650   53.058  1.00 40.01  ?  113 THR D N   1 
ATOM   5762 C CA  . THR D 2 113 ? 18.185  1.551   53.840  1.00 38.91  ?  113 THR D CA  1 
ATOM   5763 C C   . THR D 2 113 ? 17.834  2.984   53.465  1.00 38.67  ?  113 THR D C   1 
ATOM   5764 O O   . THR D 2 113 ? 17.634  3.293   52.287  1.00 40.49  ?  113 THR D O   1 
ATOM   5765 C CB  . THR D 2 113 ? 19.687  1.250   53.624  1.00 41.81  ?  113 THR D CB  1 
ATOM   5766 O OG1 . THR D 2 113 ? 20.482  2.193   54.349  1.00 49.50  ?  113 THR D OG1 1 
ATOM   5767 C CG2 . THR D 2 113 ? 20.061  1.293   52.153  1.00 39.06  ?  113 THR D CG2 1 
ATOM   5768 N N   . LEU D 2 114 ? 17.723  3.850   54.468  1.00 38.15  ?  114 LEU D N   1 
ATOM   5769 C CA  . LEU D 2 114 ? 17.346  5.237   54.220  1.00 38.31  ?  114 LEU D CA  1 
ATOM   5770 C C   . LEU D 2 114 ? 18.553  6.065   53.794  1.00 37.38  ?  114 LEU D C   1 
ATOM   5771 O O   . LEU D 2 114 ? 19.619  5.982   54.410  1.00 39.55  ?  114 LEU D O   1 
ATOM   5772 C CB  . LEU D 2 114 ? 16.695  5.848   55.461  1.00 35.53  ?  114 LEU D CB  1 
ATOM   5773 C CG  . LEU D 2 114 ? 16.348  7.338   55.330  1.00 44.82  ?  114 LEU D CG  1 
ATOM   5774 C CD1 . LEU D 2 114 ? 15.371  7.571   54.182  1.00 42.61  ?  114 LEU D CD1 1 
ATOM   5775 C CD2 . LEU D 2 114 ? 15.792  7.898   56.638  1.00 31.68  ?  114 LEU D CD2 1 
ATOM   5776 N N   . VAL D 2 115 ? 18.389  6.844   52.724  1.00 37.37  ?  115 VAL D N   1 
ATOM   5777 C CA  . VAL D 2 115 ? 19.378  7.818   52.274  1.00 39.19  ?  115 VAL D CA  1 
ATOM   5778 C C   . VAL D 2 115 ? 18.769  9.205   52.419  1.00 42.15  ?  115 VAL D C   1 
ATOM   5779 O O   . VAL D 2 115 ? 17.747  9.514   51.785  1.00 43.32  ?  115 VAL D O   1 
ATOM   5780 C CB  . VAL D 2 115 ? 19.808  7.573   50.822  1.00 36.46  ?  115 VAL D CB  1 
ATOM   5781 C CG1 . VAL D 2 115 ? 20.745  8.687   50.365  1.00 31.68  ?  115 VAL D CG1 1 
ATOM   5782 C CG2 . VAL D 2 115 ? 20.450  6.202   50.677  1.00 38.03  ?  115 VAL D CG2 1 
ATOM   5783 N N   . THR D 2 116 ? 19.389  10.035  53.255  1.00 39.93  ?  116 THR D N   1 
ATOM   5784 C CA  . THR D 2 116 ? 18.973  11.417  53.469  1.00 44.65  ?  116 THR D CA  1 
ATOM   5785 C C   . THR D 2 116 ? 20.002  12.351  52.841  1.00 45.07  ?  116 THR D C   1 
ATOM   5786 O O   . THR D 2 116 ? 21.167  12.365  53.258  1.00 40.48  ?  116 THR D O   1 
ATOM   5787 C CB  . THR D 2 116 ? 18.827  11.728  54.959  1.00 42.84  ?  116 THR D CB  1 
ATOM   5788 O OG1 . THR D 2 116 ? 17.987  10.746  55.576  1.00 48.67  ?  116 THR D OG1 1 
ATOM   5789 C CG2 . THR D 2 116 ? 18.210  13.097  55.144  1.00 36.86  ?  116 THR D CG2 1 
ATOM   5790 N N   . VAL D 2 117 ? 19.572  13.130  51.852  1.00 39.16  ?  117 VAL D N   1 
ATOM   5791 C CA  . VAL D 2 117 ? 20.436  14.078  51.159  1.00 39.86  ?  117 VAL D CA  1 
ATOM   5792 C C   . VAL D 2 117 ? 20.102  15.462  51.703  1.00 47.15  ?  117 VAL D C   1 
ATOM   5793 O O   . VAL D 2 117 ? 19.097  16.069  51.322  1.00 48.41  ?  117 VAL D O   1 
ATOM   5794 C CB  . VAL D 2 117 ? 20.263  13.999  49.641  1.00 48.04  ?  117 VAL D CB  1 
ATOM   5795 C CG1 . VAL D 2 117 ? 21.263  14.921  48.947  1.00 46.32  ?  117 VAL D CG1 1 
ATOM   5796 C CG2 . VAL D 2 117 ? 20.429  12.550  49.162  1.00 41.51  ?  117 VAL D CG2 1 
ATOM   5797 N N   . SER D 2 118 ? 20.941  15.961  52.608  1.00 45.14  ?  118 SER D N   1 
ATOM   5798 C CA  . SER D 2 118 ? 20.672  17.226  53.275  1.00 49.80  ?  118 SER D CA  1 
ATOM   5799 C C   . SER D 2 118 ? 21.986  17.879  53.679  1.00 50.71  ?  118 SER D C   1 
ATOM   5800 O O   . SER D 2 118 ? 23.027  17.225  53.777  1.00 52.80  ?  118 SER D O   1 
ATOM   5801 C CB  . SER D 2 118 ? 19.770  17.029  54.501  1.00 47.34  ?  118 SER D CB  1 
ATOM   5802 O OG  . SER D 2 118 ? 19.534  18.259  55.167  1.00 54.40  ?  118 SER D OG  1 
ATOM   5803 N N   . SER D 2 119 ? 21.932  19.188  53.907  1.00 51.81  ?  119 SER D N   1 
ATOM   5804 C CA  . SER D 2 119 ? 23.097  19.911  54.396  1.00 58.50  ?  119 SER D CA  1 
ATOM   5805 C C   . SER D 2 119 ? 23.096  20.099  55.910  1.00 56.89  ?  119 SER D C   1 
ATOM   5806 O O   . SER D 2 119 ? 24.095  20.575  56.455  1.00 56.13  ?  119 SER D O   1 
ATOM   5807 C CB  . SER D 2 119 ? 23.200  21.274  53.702  1.00 52.91  ?  119 SER D CB  1 
ATOM   5808 O OG  . SER D 2 119 ? 21.929  21.899  53.635  1.00 64.55  ?  119 SER D OG  1 
ATOM   5809 N N   . ALA D 2 120 ? 22.018  19.719  56.598  1.00 55.77  ?  120 ALA D N   1 
ATOM   5810 C CA  . ALA D 2 120 ? 21.945  19.804  58.052  1.00 52.15  ?  120 ALA D CA  1 
ATOM   5811 C C   . ALA D 2 120 ? 22.899  18.806  58.716  1.00 53.50  ?  120 ALA D C   1 
ATOM   5812 O O   . ALA D 2 120 ? 23.432  17.886  58.087  1.00 55.22  ?  120 ALA D O   1 
ATOM   5813 C CB  . ALA D 2 120 ? 20.514  19.560  58.531  1.00 55.69  ?  120 ALA D CB  1 
ATOM   5814 N N   . SER D 2 121 ? 23.115  19.004  60.013  1.00 51.50  ?  121 SER D N   1 
ATOM   5815 C CA  . SER D 2 121 ? 24.035  18.188  60.791  1.00 52.51  ?  121 SER D CA  1 
ATOM   5816 C C   . SER D 2 121 ? 23.288  17.172  61.648  1.00 54.31  ?  121 SER D C   1 
ATOM   5817 O O   . SER D 2 121 ? 22.159  17.402  62.088  1.00 52.92  ?  121 SER D O   1 
ATOM   5818 C CB  . SER D 2 121 ? 24.922  19.058  61.682  1.00 51.27  ?  121 SER D CB  1 
ATOM   5819 O OG  . SER D 2 121 ? 25.859  19.778  60.903  1.00 68.57  ?  121 SER D OG  1 
ATOM   5820 N N   . THR D 2 122 ? 23.944  16.037  61.872  1.00 50.45  ?  122 THR D N   1 
ATOM   5821 C CA  . THR D 2 122 ? 23.421  15.007  62.756  1.00 41.46  ?  122 THR D CA  1 
ATOM   5822 C C   . THR D 2 122 ? 23.259  15.538  64.173  1.00 51.85  ?  122 THR D C   1 
ATOM   5823 O O   . THR D 2 122 ? 24.162  16.181  64.716  1.00 58.44  ?  122 THR D O   1 
ATOM   5824 C CB  . THR D 2 122 ? 24.367  13.812  62.746  1.00 37.67  ?  122 THR D CB  1 
ATOM   5825 O OG1 . THR D 2 122 ? 24.356  13.220  61.443  1.00 46.06  ?  122 THR D OG1 1 
ATOM   5826 C CG2 . THR D 2 122 ? 23.950  12.780  63.771  1.00 44.23  ?  122 THR D CG2 1 
ATOM   5827 N N   . LYS D 2 123 ? 22.098  15.277  64.770  1.00 50.79  ?  123 LYS D N   1 
ATOM   5828 C CA  . LYS D 2 123 ? 21.844  15.645  66.156  1.00 51.26  ?  123 LYS D CA  1 
ATOM   5829 C C   . LYS D 2 123 ? 21.046  14.546  66.840  1.00 46.41  ?  123 LYS D C   1 
ATOM   5830 O O   . LYS D 2 123 ? 20.091  14.017  66.264  1.00 45.95  ?  123 LYS D O   1 
ATOM   5831 C CB  . LYS D 2 123 ? 21.103  16.982  66.255  1.00 49.60  ?  123 LYS D CB  1 
ATOM   5832 C CG  . LYS D 2 123 ? 20.931  17.471  67.684  1.00 58.43  ?  123 LYS D CG  1 
ATOM   5833 C CD  . LYS D 2 123 ? 20.297  18.848  67.743  1.00 59.18  ?  123 LYS D CD  1 
ATOM   5834 C CE  . LYS D 2 123 ? 20.019  19.251  69.179  1.00 61.38  ?  123 LYS D CE  1 
ATOM   5835 N NZ  . LYS D 2 123 ? 19.030  18.328  69.810  1.00 66.72  ?  123 LYS D NZ  1 
ATOM   5836 N N   . GLY D 2 124 ? 21.458  14.185  68.050  1.00 44.47  ?  124 GLY D N   1 
ATOM   5837 C CA  . GLY D 2 124 ? 20.739  13.213  68.834  1.00 43.93  ?  124 GLY D CA  1 
ATOM   5838 C C   . GLY D 2 124 ? 19.508  13.819  69.469  1.00 44.52  ?  124 GLY D C   1 
ATOM   5839 O O   . GLY D 2 124 ? 19.390  15.040  69.608  1.00 52.30  ?  124 GLY D O   1 
ATOM   5840 N N   . PRO D 2 125 ? 18.568  12.974  69.881  1.00 48.66  ?  125 PRO D N   1 
ATOM   5841 C CA  . PRO D 2 125 ? 17.270  13.465  70.354  1.00 46.18  ?  125 PRO D CA  1 
ATOM   5842 C C   . PRO D 2 125 ? 17.247  13.806  71.836  1.00 43.70  ?  125 PRO D C   1 
ATOM   5843 O O   . PRO D 2 125 ? 17.938  13.210  72.662  1.00 47.51  ?  125 PRO D O   1 
ATOM   5844 C CB  . PRO D 2 125 ? 16.347  12.273  70.073  1.00 44.15  ?  125 PRO D CB  1 
ATOM   5845 C CG  . PRO D 2 125 ? 17.237  11.092  70.315  1.00 39.03  ?  125 PRO D CG  1 
ATOM   5846 C CD  . PRO D 2 125 ? 18.618  11.502  69.840  1.00 45.10  ?  125 PRO D CD  1 
ATOM   5847 N N   . SER D 2 126 ? 16.420  14.790  72.169  1.00 48.79  ?  126 SER D N   1 
ATOM   5848 C CA  . SER D 2 126 ? 16.058  15.044  73.556  1.00 46.95  ?  126 SER D CA  1 
ATOM   5849 C C   . SER D 2 126 ? 14.782  14.274  73.864  1.00 46.26  ?  126 SER D C   1 
ATOM   5850 O O   . SER D 2 126 ? 13.849  14.256  73.058  1.00 46.54  ?  126 SER D O   1 
ATOM   5851 C CB  . SER D 2 126 ? 15.854  16.539  73.811  1.00 46.73  ?  126 SER D CB  1 
ATOM   5852 O OG  . SER D 2 126 ? 16.916  17.306  73.269  1.00 45.27  ?  126 SER D OG  1 
ATOM   5853 N N   . VAL D 2 127 ? 14.742  13.631  75.027  1.00 45.24  ?  127 VAL D N   1 
ATOM   5854 C CA  . VAL D 2 127 ? 13.624  12.771  75.399  1.00 46.07  ?  127 VAL D CA  1 
ATOM   5855 C C   . VAL D 2 127 ? 12.981  13.317  76.663  1.00 47.83  ?  127 VAL D C   1 
ATOM   5856 O O   . VAL D 2 127 ? 13.611  13.349  77.726  1.00 50.35  ?  127 VAL D O   1 
ATOM   5857 C CB  . VAL D 2 127 ? 14.065  11.314  75.593  1.00 42.10  ?  127 VAL D CB  1 
ATOM   5858 C CG1 . VAL D 2 127 ? 12.877  10.460  76.012  1.00 52.16  ?  127 VAL D CG1 1 
ATOM   5859 C CG2 . VAL D 2 127 ? 14.660  10.782  74.303  1.00 45.60  ?  127 VAL D CG2 1 
ATOM   5860 N N   . PHE D 2 128 ? 11.717  13.714  76.552  1.00 49.28  ?  128 PHE D N   1 
ATOM   5861 C CA  . PHE D 2 128 ? 10.971  14.233  77.679  1.00 49.97  ?  128 PHE D CA  1 
ATOM   5862 C C   . PHE D 2 128 ? 9.805   13.310  77.998  1.00 50.59  ?  128 PHE D C   1 
ATOM   5863 O O   . PHE D 2 128 ? 9.327   12.585  77.123  1.00 49.15  ?  128 PHE D O   1 
ATOM   5864 C CB  . PHE D 2 128 ? 10.444  15.641  77.384  1.00 47.95  ?  128 PHE D CB  1 
ATOM   5865 C CG  . PHE D 2 128 ? 11.512  16.613  76.993  1.00 53.40  ?  128 PHE D CG  1 
ATOM   5866 C CD1 . PHE D 2 128 ? 12.449  17.039  77.915  1.00 54.51  ?  128 PHE D CD1 1 
ATOM   5867 C CD2 . PHE D 2 128 ? 11.570  17.115  75.705  1.00 56.74  ?  128 PHE D CD2 1 
ATOM   5868 C CE1 . PHE D 2 128 ? 13.428  17.938  77.554  1.00 56.01  ?  128 PHE D CE1 1 
ATOM   5869 C CE2 . PHE D 2 128 ? 12.545  18.016  75.340  1.00 51.59  ?  128 PHE D CE2 1 
ATOM   5870 C CZ  . PHE D 2 128 ? 13.474  18.427  76.263  1.00 52.22  ?  128 PHE D CZ  1 
ATOM   5871 N N   . PRO D 2 129 ? 9.328   13.304  79.241  1.00 56.15  ?  129 PRO D N   1 
ATOM   5872 C CA  . PRO D 2 129 ? 8.203   12.428  79.582  1.00 50.89  ?  129 PRO D CA  1 
ATOM   5873 C C   . PRO D 2 129 ? 6.856   13.127  79.477  1.00 47.24  ?  129 PRO D C   1 
ATOM   5874 O O   . PRO D 2 129 ? 6.692   14.293  79.840  1.00 53.75  ?  129 PRO D O   1 
ATOM   5875 C CB  . PRO D 2 129 ? 8.515   12.035  81.033  1.00 52.92  ?  129 PRO D CB  1 
ATOM   5876 C CG  . PRO D 2 129 ? 9.404   13.163  81.570  1.00 49.20  ?  129 PRO D CG  1 
ATOM   5877 C CD  . PRO D 2 129 ? 9.826   14.036  80.418  1.00 49.59  ?  129 PRO D CD  1 
ATOM   5878 N N   . LEU D 2 130 ? 5.880   12.395  78.951  1.00 49.26  ?  130 LEU D N   1 
ATOM   5879 C CA  . LEU D 2 130 ? 4.473   12.774  79.002  1.00 48.39  ?  130 LEU D CA  1 
ATOM   5880 C C   . LEU D 2 130 ? 3.893   11.972  80.158  1.00 47.13  ?  130 LEU D C   1 
ATOM   5881 O O   . LEU D 2 130 ? 3.532   10.800  79.998  1.00 48.36  ?  130 LEU D O   1 
ATOM   5882 C CB  . LEU D 2 130 ? 3.766   12.463  77.688  1.00 45.01  ?  130 LEU D CB  1 
ATOM   5883 C CG  . LEU D 2 130 ? 4.383   13.040  76.415  1.00 44.63  ?  130 LEU D CG  1 
ATOM   5884 C CD1 . LEU D 2 130 ? 3.898   12.272  75.200  1.00 45.09  ?  130 LEU D CD1 1 
ATOM   5885 C CD2 . LEU D 2 130 ? 4.047   14.512  76.286  1.00 41.35  ?  130 LEU D CD2 1 
ATOM   5886 N N   . ALA D 2 131 ? 3.820   12.612  81.330  1.00 40.78  ?  131 ALA D N   1 
ATOM   5887 C CA  . ALA D 2 131 ? 3.540   11.949  82.595  1.00 48.35  ?  131 ALA D CA  1 
ATOM   5888 C C   . ALA D 2 131 ? 2.034   11.781  82.798  1.00 55.79  ?  131 ALA D C   1 
ATOM   5889 O O   . ALA D 2 131 ? 1.252   12.668  82.442  1.00 51.74  ?  131 ALA D O   1 
ATOM   5890 C CB  . ALA D 2 131 ? 4.138   12.742  83.760  1.00 45.82  ?  131 ALA D CB  1 
ATOM   5891 N N   . PRO D 2 132 ? 1.606   10.658  83.371  1.00 60.33  ?  132 PRO D N   1 
ATOM   5892 C CA  . PRO D 2 132 ? 0.176   10.468  83.638  1.00 63.69  ?  132 PRO D CA  1 
ATOM   5893 C C   . PRO D 2 132 ? -0.240  11.050  84.979  1.00 72.12  ?  132 PRO D C   1 
ATOM   5894 O O   . PRO D 2 132 ? 0.531   11.787  85.600  1.00 71.91  ?  132 PRO D O   1 
ATOM   5895 C CB  . PRO D 2 132 ? 0.029   8.943   83.625  1.00 66.16  ?  132 PRO D CB  1 
ATOM   5896 C CG  . PRO D 2 132 ? 1.348   8.460   84.150  1.00 61.14  ?  132 PRO D CG  1 
ATOM   5897 C CD  . PRO D 2 132 ? 2.388   9.442   83.659  1.00 57.53  ?  132 PRO D CD  1 
ATOM   5898 N N   . SER D 2 133 ? -1.465  10.740  85.415  1.00 87.87  ?  133 SER D N   1 
ATOM   5899 C CA  . SER D 2 133 ? -1.986  11.076  86.742  1.00 88.78  ?  133 SER D CA  1 
ATOM   5900 C C   . SER D 2 133 ? -2.278  12.571  86.883  1.00 94.34  ?  133 SER D C   1 
ATOM   5901 O O   . SER D 2 133 ? -2.261  13.111  87.994  1.00 102.64 ?  133 SER D O   1 
ATOM   5902 C CB  . SER D 2 133 ? -1.041  10.616  87.858  1.00 80.93  ?  133 SER D CB  1 
ATOM   5903 O OG  . SER D 2 133 ? -1.728  10.406  89.082  1.00 79.18  ?  133 SER D OG  1 
ATOM   5904 N N   . SER D 2 134 ? -2.558  13.272  85.774  1.00 92.30  ?  134 SER D N   1 
ATOM   5905 C CA  . SER D 2 134 ? -2.855  14.703  85.856  1.00 96.13  ?  134 SER D CA  1 
ATOM   5906 C C   . SER D 2 134 ? -4.099  15.058  85.048  1.00 95.15  ?  134 SER D C   1 
ATOM   5907 O O   . SER D 2 134 ? -5.208  15.122  85.591  1.00 94.62  ?  134 SER D O   1 
ATOM   5908 C CB  . SER D 2 134 ? -1.659  15.536  85.378  1.00 89.76  ?  134 SER D CB  1 
ATOM   5909 O OG  . SER D 2 134 ? -1.245  15.171  84.070  1.00 79.01  ?  134 SER D OG  1 
ATOM   5910 N N   . LYS D 2 135 ? -3.926  15.273  83.740  1.00 91.02  ?  135 LYS D N   1 
ATOM   5911 C CA  . LYS D 2 135 ? -5.045  15.430  82.816  1.00 84.27  ?  135 LYS D CA  1 
ATOM   5912 C C   . LYS D 2 135 ? -5.050  14.295  81.800  1.00 81.16  ?  135 LYS D C   1 
ATOM   5913 O O   . LYS D 2 135 ? -5.648  14.413  80.722  1.00 68.61  ?  135 LYS D O   1 
ATOM   5914 C CB  . LYS D 2 135 ? -4.959  16.775  82.090  1.00 80.71  ?  135 LYS D CB  1 
ATOM   5915 C CG  . LYS D 2 135 ? -4.683  17.990  82.964  1.00 80.24  ?  135 LYS D CG  1 
ATOM   5916 C CD  . LYS D 2 135 ? -5.792  18.349  83.934  1.00 75.64  ?  135 LYS D CD  1 
ATOM   5917 C CE  . LYS D 2 135 ? -5.251  19.363  84.942  1.00 86.67  ?  135 LYS D CE  1 
ATOM   5918 N NZ  . LYS D 2 135 ? -6.264  20.347  85.444  1.00 78.37  ?  135 LYS D NZ  1 
ATOM   5919 N N   . SER D 2 136 ? -4.381  13.193  82.142  1.00 89.05  ?  136 SER D N   1 
ATOM   5920 C CA  . SER D 2 136 ? -4.248  11.998  81.317  1.00 84.99  ?  136 SER D CA  1 
ATOM   5921 C C   . SER D 2 136 ? -4.891  10.788  81.985  1.00 84.80  ?  136 SER D C   1 
ATOM   5922 O O   . SER D 2 136 ? -4.444  9.657   81.791  1.00 81.70  ?  136 SER D O   1 
ATOM   5923 C CB  . SER D 2 136 ? -2.773  11.727  81.021  1.00 71.40  ?  136 SER D CB  1 
ATOM   5924 O OG  . SER D 2 136 ? -1.978  12.132  82.121  1.00 75.14  ?  136 SER D OG  1 
ATOM   5925 N N   . THR D 2 137 ? -5.925  11.019  82.797  1.00 86.05  ?  137 THR D N   1 
ATOM   5926 C CA  . THR D 2 137 ? -6.644  9.957   83.502  1.00 86.82  ?  137 THR D CA  1 
ATOM   5927 C C   . THR D 2 137 ? -8.140  10.170  83.299  1.00 92.08  ?  137 THR D C   1 
ATOM   5928 O O   . THR D 2 137 ? -8.705  11.154  83.789  1.00 96.37  ?  137 THR D O   1 
ATOM   5929 C CB  . THR D 2 137 ? -6.295  9.931   84.995  1.00 94.35  ?  137 THR D CB  1 
ATOM   5930 O OG1 . THR D 2 137 ? -6.556  11.215  85.586  1.00 98.20  ?  137 THR D OG1 1 
ATOM   5931 C CG2 . THR D 2 137 ? -4.830  9.547   85.210  1.00 87.20  ?  137 THR D CG2 1 
ATOM   5932 N N   . SER D 2 138 ? -8.778  9.236   82.594  1.00 85.31  ?  138 SER D N   1 
ATOM   5933 C CA  . SER D 2 138 ? -10.213 9.275   82.325  1.00 82.53  ?  138 SER D CA  1 
ATOM   5934 C C   . SER D 2 138 ? -10.761 7.899   82.670  1.00 80.41  ?  138 SER D C   1 
ATOM   5935 O O   . SER D 2 138 ? -10.501 6.926   81.954  1.00 78.11  ?  138 SER D O   1 
ATOM   5936 C CB  . SER D 2 138 ? -10.502 9.632   80.865  1.00 88.34  ?  138 SER D CB  1 
ATOM   5937 O OG  . SER D 2 138 ? -10.059 10.942  80.544  1.00 86.08  ?  138 SER D OG  1 
ATOM   5938 N N   . GLY D 2 139 ? -11.532 7.822   83.752  1.00 78.30  ?  139 GLY D N   1 
ATOM   5939 C CA  . GLY D 2 139 ? -11.991 6.529   84.222  1.00 62.74  ?  139 GLY D CA  1 
ATOM   5940 C C   . GLY D 2 139 ? -10.826 5.754   84.813  1.00 72.66  ?  139 GLY D C   1 
ATOM   5941 O O   . GLY D 2 139 ? -9.996  6.295   85.556  1.00 69.27  ?  139 GLY D O   1 
ATOM   5942 N N   . GLY D 2 140 ? -10.748 4.473   84.464  1.00 72.41  ?  140 GLY D N   1 
ATOM   5943 C CA  . GLY D 2 140 ? -9.666  3.616   84.891  1.00 71.32  ?  140 GLY D CA  1 
ATOM   5944 C C   . GLY D 2 140 ? -8.499  3.503   83.937  1.00 66.35  ?  140 GLY D C   1 
ATOM   5945 O O   . GLY D 2 140 ? -7.581  2.720   84.197  1.00 66.70  ?  140 GLY D O   1 
ATOM   5946 N N   . THR D 2 141 ? -8.495  4.256   82.840  1.00 64.34  ?  141 THR D N   1 
ATOM   5947 C CA  . THR D 2 141 ? -7.422  4.209   81.856  1.00 65.59  ?  141 THR D CA  1 
ATOM   5948 C C   . THR D 2 141 ? -6.627  5.507   81.854  1.00 63.87  ?  141 THR D C   1 
ATOM   5949 O O   . THR D 2 141 ? -7.194  6.591   81.683  1.00 62.36  ?  141 THR D O   1 
ATOM   5950 C CB  . THR D 2 141 ? -7.974  3.948   80.456  1.00 65.90  ?  141 THR D CB  1 
ATOM   5951 O OG1 . THR D 2 141 ? -8.445  2.599   80.377  1.00 72.27  ?  141 THR D OG1 1 
ATOM   5952 C CG2 . THR D 2 141 ? -6.892  4.180   79.405  1.00 57.80  ?  141 THR D CG2 1 
ATOM   5953 N N   . ALA D 2 142 ? -5.316  5.388   82.032  1.00 64.64  ?  142 ALA D N   1 
ATOM   5954 C CA  . ALA D 2 142 ? -4.402  6.513   81.932  1.00 66.88  ?  142 ALA D CA  1 
ATOM   5955 C C   . ALA D 2 142 ? -3.595  6.412   80.642  1.00 60.48  ?  142 ALA D C   1 
ATOM   5956 O O   . ALA D 2 142 ? -3.446  5.335   80.057  1.00 57.85  ?  142 ALA D O   1 
ATOM   5957 C CB  . ALA D 2 142 ? -3.463  6.567   83.143  1.00 64.36  ?  142 ALA D CB  1 
ATOM   5958 N N   . ALA D 2 143 ? -3.065  7.552   80.204  1.00 55.47  ?  143 ALA D N   1 
ATOM   5959 C CA  . ALA D 2 143 ? -2.175  7.613   79.054  1.00 55.36  ?  143 ALA D CA  1 
ATOM   5960 C C   . ALA D 2 143 ? -0.848  8.224   79.478  1.00 51.10  ?  143 ALA D C   1 
ATOM   5961 O O   . ALA D 2 143 ? -0.818  9.169   80.272  1.00 52.47  ?  143 ALA D O   1 
ATOM   5962 C CB  . ALA D 2 143 ? -2.784  8.432   77.912  1.00 49.27  ?  143 ALA D CB  1 
ATOM   5963 N N   . LEU D 2 144 ? 0.250   7.664   78.970  1.00 50.85  ?  144 LEU D N   1 
ATOM   5964 C CA  . LEU D 2 144 ? 1.580   8.200   79.240  1.00 52.76  ?  144 LEU D CA  1 
ATOM   5965 C C   . LEU D 2 144 ? 2.433   8.031   77.991  1.00 50.60  ?  144 LEU D C   1 
ATOM   5966 O O   . LEU D 2 144 ? 2.035   7.362   77.036  1.00 51.32  ?  144 LEU D O   1 
ATOM   5967 C CB  . LEU D 2 144 ? 2.225   7.520   80.453  1.00 49.00  ?  144 LEU D CB  1 
ATOM   5968 C CG  . LEU D 2 144 ? 2.345   5.998   80.393  1.00 47.29  ?  144 LEU D CG  1 
ATOM   5969 C CD1 . LEU D 2 144 ? 3.773   5.593   80.072  1.00 52.75  ?  144 LEU D CD1 1 
ATOM   5970 C CD2 . LEU D 2 144 ? 1.882   5.363   81.697  1.00 45.55  ?  144 LEU D CD2 1 
ATOM   5971 N N   . GLY D 2 145 ? 3.605   8.652   77.978  1.00 52.48  ?  145 GLY D N   1 
ATOM   5972 C CA  . GLY D 2 145 ? 4.451   8.494   76.809  1.00 48.98  ?  145 GLY D CA  1 
ATOM   5973 C C   . GLY D 2 145 ? 5.754   9.255   76.906  1.00 47.04  ?  145 GLY D C   1 
ATOM   5974 O O   . GLY D 2 145 ? 6.140   9.746   77.965  1.00 46.26  ?  145 GLY D O   1 
ATOM   5975 N N   . CYS D 2 146 ? 6.417   9.339   75.752  1.00 46.19  ?  146 CYS D N   1 
ATOM   5976 C CA  . CYS D 2 146 ? 7.709   9.988   75.567  1.00 48.39  ?  146 CYS D CA  1 
ATOM   5977 C C   . CYS D 2 146 ? 7.640   10.929  74.374  1.00 47.75  ?  146 CYS D C   1 
ATOM   5978 O O   . CYS D 2 146 ? 7.149   10.556  73.301  1.00 47.24  ?  146 CYS D O   1 
ATOM   5979 C CB  . CYS D 2 146 ? 8.829   8.957   75.345  1.00 43.47  ?  146 CYS D CB  1 
ATOM   5980 S SG  . CYS D 2 146 ? 9.472   8.270   76.874  1.00 70.78  ?  146 CYS D SG  1 
ATOM   5981 N N   . LEU D 2 147 ? 8.153   12.138  74.559  1.00 44.12  ?  147 LEU D N   1 
ATOM   5982 C CA  . LEU D 2 147 ? 8.311   13.106  73.486  1.00 47.25  ?  147 LEU D CA  1 
ATOM   5983 C C   . LEU D 2 147 ? 9.775   13.091  73.064  1.00 52.43  ?  147 LEU D C   1 
ATOM   5984 O O   . LEU D 2 147 ? 10.659  13.413  73.867  1.00 47.46  ?  147 LEU D O   1 
ATOM   5985 C CB  . LEU D 2 147 ? 7.888   14.498  73.950  1.00 47.31  ?  147 LEU D CB  1 
ATOM   5986 C CG  . LEU D 2 147 ? 7.999   15.655  72.960  1.00 55.35  ?  147 LEU D CG  1 
ATOM   5987 C CD1 . LEU D 2 147 ? 6.979   15.493  71.847  1.00 54.85  ?  147 LEU D CD1 1 
ATOM   5988 C CD2 . LEU D 2 147 ? 7.829   16.989  73.676  1.00 49.45  ?  147 LEU D CD2 1 
ATOM   5989 N N   . VAL D 2 148 ? 10.026  12.703  71.818  1.00 49.08  ?  148 VAL D N   1 
ATOM   5990 C CA  . VAL D 2 148 ? 11.364  12.587  71.261  1.00 42.56  ?  148 VAL D CA  1 
ATOM   5991 C C   . VAL D 2 148 ? 11.529  13.767  70.312  1.00 42.90  ?  148 VAL D C   1 
ATOM   5992 O O   . VAL D 2 148 ? 10.995  13.762  69.200  1.00 46.48  ?  148 VAL D O   1 
ATOM   5993 C CB  . VAL D 2 148 ? 11.557  11.247  70.542  1.00 47.43  ?  148 VAL D CB  1 
ATOM   5994 C CG1 . VAL D 2 148 ? 12.960  11.130  69.976  1.00 48.34  ?  148 VAL D CG1 1 
ATOM   5995 C CG2 . VAL D 2 148 ? 11.227  10.082  71.476  1.00 38.84  ?  148 VAL D CG2 1 
ATOM   5996 N N   . LYS D 2 149 ? 12.274  14.782  70.742  1.00 47.20  ?  149 LYS D N   1 
ATOM   5997 C CA  . LYS D 2 149 ? 12.272  16.089  70.102  1.00 49.83  ?  149 LYS D CA  1 
ATOM   5998 C C   . LYS D 2 149 ? 13.672  16.459  69.629  1.00 50.21  ?  149 LYS D C   1 
ATOM   5999 O O   . LYS D 2 149 ? 14.662  16.164  70.307  1.00 50.09  ?  149 LYS D O   1 
ATOM   6000 C CB  . LYS D 2 149 ? 11.749  17.151  71.083  1.00 49.96  ?  149 LYS D CB  1 
ATOM   6001 C CG  . LYS D 2 149 ? 11.577  18.537  70.506  1.00 54.03  ?  149 LYS D CG  1 
ATOM   6002 C CD  . LYS D 2 149 ? 11.082  19.494  71.576  1.00 62.47  ?  149 LYS D CD  1 
ATOM   6003 C CE  . LYS D 2 149 ? 11.146  20.937  71.111  1.00 63.83  ?  149 LYS D CE  1 
ATOM   6004 N NZ  . LYS D 2 149 ? 10.103  21.209  70.086  1.00 64.85  ?  149 LYS D NZ  1 
ATOM   6005 N N   . ASP D 2 150 ? 13.741  17.105  68.458  1.00 55.42  ?  150 ASP D N   1 
ATOM   6006 C CA  . ASP D 2 150 ? 14.945  17.775  67.974  1.00 52.01  ?  150 ASP D CA  1 
ATOM   6007 C C   . ASP D 2 150 ? 16.063  16.797  67.636  1.00 52.98  ?  150 ASP D C   1 
ATOM   6008 O O   . ASP D 2 150 ? 17.164  16.888  68.192  1.00 51.72  ?  150 ASP D O   1 
ATOM   6009 C CB  . ASP D 2 150 ? 15.428  18.813  68.990  1.00 53.32  ?  150 ASP D CB  1 
ATOM   6010 C CG  . ASP D 2 150 ? 14.498  20.005  69.087  1.00 55.11  ?  150 ASP D CG  1 
ATOM   6011 O OD1 . ASP D 2 150 ? 13.782  20.285  68.101  1.00 63.80  ?  150 ASP D OD1 1 
ATOM   6012 O OD2 . ASP D 2 150 ? 14.479  20.661  70.149  1.00 55.49  ?  150 ASP D OD2 1 
ATOM   6013 N N   . TYR D 2 151 ? 15.792  15.855  66.734  1.00 49.20  ?  151 TYR D N   1 
ATOM   6014 C CA  . TYR D 2 151 ? 16.821  14.952  66.246  1.00 49.15  ?  151 TYR D CA  1 
ATOM   6015 C C   . TYR D 2 151 ? 16.914  15.005  64.727  1.00 45.84  ?  151 TYR D C   1 
ATOM   6016 O O   . TYR D 2 151 ? 15.989  15.437  64.032  1.00 39.81  ?  151 TYR D O   1 
ATOM   6017 C CB  . TYR D 2 151 ? 16.560  13.510  66.682  1.00 47.13  ?  151 TYR D CB  1 
ATOM   6018 C CG  . TYR D 2 151 ? 15.365  12.869  66.028  1.00 47.82  ?  151 TYR D CG  1 
ATOM   6019 C CD1 . TYR D 2 151 ? 14.098  12.965  66.597  1.00 48.49  ?  151 TYR D CD1 1 
ATOM   6020 C CD2 . TYR D 2 151 ? 15.506  12.141  64.853  1.00 43.78  ?  151 TYR D CD2 1 
ATOM   6021 C CE1 . TYR D 2 151 ? 13.004  12.362  66.005  1.00 44.48  ?  151 TYR D CE1 1 
ATOM   6022 C CE2 . TYR D 2 151 ? 14.424  11.547  64.251  1.00 47.08  ?  151 TYR D CE2 1 
ATOM   6023 C CZ  . TYR D 2 151 ? 13.177  11.654  64.833  1.00 51.29  ?  151 TYR D CZ  1 
ATOM   6024 O OH  . TYR D 2 151 ? 12.105  11.046  64.228  1.00 48.07  ?  151 TYR D OH  1 
ATOM   6025 N N   . PHE D 2 152 ? 18.034  14.503  64.222  1.00 45.74  ?  152 PHE D N   1 
ATOM   6026 C CA  . PHE D 2 152 ? 18.308  14.482  62.795  1.00 42.20  ?  152 PHE D CA  1 
ATOM   6027 C C   . PHE D 2 152 ? 19.509  13.590  62.517  1.00 42.74  ?  152 PHE D C   1 
ATOM   6028 O O   . PHE D 2 152 ? 20.485  13.606  63.276  1.00 44.76  ?  152 PHE D O   1 
ATOM   6029 C CB  . PHE D 2 152 ? 18.556  15.896  62.276  1.00 41.93  ?  152 PHE D CB  1 
ATOM   6030 C CG  . PHE D 2 152 ? 18.650  15.984  60.786  1.00 42.32  ?  152 PHE D CG  1 
ATOM   6031 C CD1 . PHE D 2 152 ? 19.880  15.955  60.155  1.00 48.39  ?  152 PHE D CD1 1 
ATOM   6032 C CD2 . PHE D 2 152 ? 17.508  16.122  60.014  1.00 41.80  ?  152 PHE D CD2 1 
ATOM   6033 C CE1 . PHE D 2 152 ? 19.970  16.045  58.780  1.00 47.54  ?  152 PHE D CE1 1 
ATOM   6034 C CE2 . PHE D 2 152 ? 17.588  16.209  58.641  1.00 35.40  ?  152 PHE D CE2 1 
ATOM   6035 C CZ  . PHE D 2 152 ? 18.821  16.170  58.022  1.00 43.97  ?  152 PHE D CZ  1 
ATOM   6036 N N   . PRO D 2 153 ? 19.459  12.768  61.463  1.00 44.70  ?  153 PRO D N   1 
ATOM   6037 C CA  . PRO D 2 153 ? 18.265  12.634  60.632  1.00 46.50  ?  153 PRO D CA  1 
ATOM   6038 C C   . PRO D 2 153 ? 17.399  11.471  61.095  1.00 48.25  ?  153 PRO D C   1 
ATOM   6039 O O   . PRO D 2 153 ? 17.631  10.913  62.172  1.00 42.79  ?  153 PRO D O   1 
ATOM   6040 C CB  . PRO D 2 153 ? 18.848  12.353  59.254  1.00 42.54  ?  153 PRO D CB  1 
ATOM   6041 C CG  . PRO D 2 153 ? 20.028  11.494  59.576  1.00 37.77  ?  153 PRO D CG  1 
ATOM   6042 C CD  . PRO D 2 153 ? 20.581  11.994  60.908  1.00 41.72  ?  153 PRO D CD  1 
ATOM   6043 N N   . GLU D 2 154 ? 16.426  11.100  60.268  1.00 43.78  ?  154 GLU D N   1 
ATOM   6044 C CA  . GLU D 2 154 ? 15.673  9.883   60.493  1.00 42.96  ?  154 GLU D CA  1 
ATOM   6045 C C   . GLU D 2 154 ? 16.576  8.669   60.294  1.00 43.18  ?  154 GLU D C   1 
ATOM   6046 O O   . GLU D 2 154 ? 17.572  8.741   59.572  1.00 44.68  ?  154 GLU D O   1 
ATOM   6047 C CB  . GLU D 2 154 ? 14.483  9.822   59.543  1.00 43.59  ?  154 GLU D CB  1 
ATOM   6048 C CG  . GLU D 2 154 ? 13.408  10.835  59.853  1.00 45.07  ?  154 GLU D CG  1 
ATOM   6049 C CD  . GLU D 2 154 ? 12.320  10.234  60.706  1.00 55.73  ?  154 GLU D CD  1 
ATOM   6050 O OE1 . GLU D 2 154 ? 12.641  9.738   61.812  1.00 50.29  ?  154 GLU D OE1 1 
ATOM   6051 O OE2 . GLU D 2 154 ? 11.148  10.236  60.266  1.00 63.29  -1 154 GLU D OE2 1 
ATOM   6052 N N   . PRO D 2 155 ? 16.238  7.523   60.911  1.00 46.47  ?  155 PRO D N   1 
ATOM   6053 C CA  . PRO D 2 155 ? 15.065  7.241   61.742  1.00 46.29  ?  155 PRO D CA  1 
ATOM   6054 C C   . PRO D 2 155 ? 15.356  7.045   63.228  1.00 46.70  ?  155 PRO D C   1 
ATOM   6055 O O   . PRO D 2 155 ? 16.493  6.760   63.606  1.00 47.37  ?  155 PRO D O   1 
ATOM   6056 C CB  . PRO D 2 155 ? 14.573  5.928   61.159  1.00 41.53  ?  155 PRO D CB  1 
ATOM   6057 C CG  . PRO D 2 155 ? 15.872  5.204   60.868  1.00 34.44  ?  155 PRO D CG  1 
ATOM   6058 C CD  . PRO D 2 155 ? 16.904  6.268   60.521  1.00 43.27  ?  155 PRO D CD  1 
ATOM   6059 N N   . VAL D 2 156 ? 14.320  7.173   64.055  1.00 48.81  ?  156 VAL D N   1 
ATOM   6060 C CA  . VAL D 2 156 ? 14.369  6.756   65.450  1.00 47.25  ?  156 VAL D CA  1 
ATOM   6061 C C   . VAL D 2 156 ? 13.386  5.617   65.640  1.00 49.09  ?  156 VAL D C   1 
ATOM   6062 O O   . VAL D 2 156 ? 12.350  5.544   64.974  1.00 56.08  ?  156 VAL D O   1 
ATOM   6063 C CB  . VAL D 2 156 ? 14.045  7.890   66.444  1.00 45.65  ?  156 VAL D CB  1 
ATOM   6064 C CG1 . VAL D 2 156 ? 15.120  8.942   66.429  1.00 51.72  ?  156 VAL D CG1 1 
ATOM   6065 C CG2 . VAL D 2 156 ? 12.729  8.503   66.105  1.00 49.32  ?  156 VAL D CG2 1 
ATOM   6066 N N   . THR D 2 157 ? 13.717  4.725   66.561  1.00 47.64  ?  157 THR D N   1 
ATOM   6067 C CA  . THR D 2 157 ? 12.835  3.627   66.926  1.00 46.52  ?  157 THR D CA  1 
ATOM   6068 C C   . THR D 2 157 ? 12.486  3.774   68.396  1.00 48.59  ?  157 THR D C   1 
ATOM   6069 O O   . THR D 2 157 ? 13.331  4.175   69.206  1.00 42.44  ?  157 THR D O   1 
ATOM   6070 C CB  . THR D 2 157 ? 13.468  2.241   66.670  1.00 48.59  ?  157 THR D CB  1 
ATOM   6071 O OG1 . THR D 2 157 ? 14.649  2.073   67.470  1.00 50.03  ?  157 THR D OG1 1 
ATOM   6072 C CG2 . THR D 2 157 ? 13.818  2.081   65.204  1.00 44.32  ?  157 THR D CG2 1 
ATOM   6073 N N   . VAL D 2 158 ? 11.227  3.517   68.733  1.00 42.83  ?  158 VAL D N   1 
ATOM   6074 C CA  . VAL D 2 158 ? 10.778  3.570   70.115  1.00 40.10  ?  158 VAL D CA  1 
ATOM   6075 C C   . VAL D 2 158 ? 10.197  2.217   70.482  1.00 46.65  ?  158 VAL D C   1 
ATOM   6076 O O   . VAL D 2 158 ? 9.368   1.669   69.747  1.00 49.89  ?  158 VAL D O   1 
ATOM   6077 C CB  . VAL D 2 158 ? 9.749   4.686   70.355  1.00 46.07  ?  158 VAL D CB  1 
ATOM   6078 C CG1 . VAL D 2 158 ? 9.493   4.820   71.842  1.00 41.67  ?  158 VAL D CG1 1 
ATOM   6079 C CG2 . VAL D 2 158 ? 10.239  6.002   69.778  1.00 44.20  ?  158 VAL D CG2 1 
ATOM   6080 N N   . SER D 2 159 ? 10.659  1.668   71.596  1.00 45.73  ?  159 SER D N   1 
ATOM   6081 C CA  . SER D 2 159 ? 10.049  0.497   72.200  1.00 38.53  ?  159 SER D CA  1 
ATOM   6082 C C   . SER D 2 159 ? 9.709   0.833   73.644  1.00 42.23  ?  159 SER D C   1 
ATOM   6083 O O   . SER D 2 159 ? 10.151  1.845   74.188  1.00 43.50  ?  159 SER D O   1 
ATOM   6084 C CB  . SER D 2 159 ? 10.969  -0.724  72.132  1.00 47.28  ?  159 SER D CB  1 
ATOM   6085 O OG  . SER D 2 159 ? 12.045  -0.594  73.044  1.00 53.61  ?  159 SER D OG  1 
ATOM   6086 N N   . TRP D 2 160 ? 8.898   -0.012  74.266  1.00 50.04  ?  160 TRP D N   1 
ATOM   6087 C CA  . TRP D 2 160 ? 8.516   0.172   75.658  1.00 44.73  ?  160 TRP D CA  1 
ATOM   6088 C C   . TRP D 2 160 ? 8.886   -1.069  76.449  1.00 48.36  ?  160 TRP D C   1 
ATOM   6089 O O   . TRP D 2 160 ? 8.641   -2.194  75.999  1.00 50.56  ?  160 TRP D O   1 
ATOM   6090 C CB  . TRP D 2 160 ? 7.027   0.494   75.790  1.00 37.92  ?  160 TRP D CB  1 
ATOM   6091 C CG  . TRP D 2 160 ? 6.726   1.916   75.422  1.00 38.32  ?  160 TRP D CG  1 
ATOM   6092 C CD1 . TRP D 2 160 ? 6.498   2.410   74.171  1.00 37.61  ?  160 TRP D CD1 1 
ATOM   6093 C CD2 . TRP D 2 160 ? 6.642   3.033   76.316  1.00 37.52  ?  160 TRP D CD2 1 
ATOM   6094 N NE1 . TRP D 2 160 ? 6.268   3.764   74.231  1.00 38.69  ?  160 TRP D NE1 1 
ATOM   6095 C CE2 . TRP D 2 160 ? 6.350   4.172   75.537  1.00 40.08  ?  160 TRP D CE2 1 
ATOM   6096 C CE3 . TRP D 2 160 ? 6.782   3.180   77.700  1.00 39.26  ?  160 TRP D CE3 1 
ATOM   6097 C CZ2 . TRP D 2 160 ? 6.197   5.445   76.095  1.00 43.01  ?  160 TRP D CZ2 1 
ATOM   6098 C CZ3 . TRP D 2 160 ? 6.628   4.446   78.255  1.00 43.26  ?  160 TRP D CZ3 1 
ATOM   6099 C CH2 . TRP D 2 160 ? 6.338   5.561   77.452  1.00 40.82  ?  160 TRP D CH2 1 
ATOM   6100 N N   . ASN D 2 161 ? 9.501   -0.852  77.610  1.00 49.81  ?  161 ASN D N   1 
ATOM   6101 C CA  . ASN D 2 161 ? 9.995   -1.927  78.467  1.00 51.35  ?  161 ASN D CA  1 
ATOM   6102 C C   . ASN D 2 161 ? 10.770  -2.951  77.645  1.00 53.09  ?  161 ASN D C   1 
ATOM   6103 O O   . ASN D 2 161 ? 10.511  -4.155  77.691  1.00 55.91  ?  161 ASN D O   1 
ATOM   6104 C CB  . ASN D 2 161 ? 8.850   -2.579  79.240  1.00 52.06  ?  161 ASN D CB  1 
ATOM   6105 C CG  . ASN D 2 161 ? 8.170   -1.610  80.192  1.00 52.52  ?  161 ASN D CG  1 
ATOM   6106 O OD1 . ASN D 2 161 ? 8.419   -0.407  80.149  1.00 53.74  ?  161 ASN D OD1 1 
ATOM   6107 N ND2 . ASN D 2 161 ? 7.314   -2.130  81.058  1.00 53.90  ?  161 ASN D ND2 1 
ATOM   6108 N N   . SER D 2 162 ? 11.716  -2.439  76.856  1.00 56.14  ?  162 SER D N   1 
ATOM   6109 C CA  . SER D 2 162 ? 12.629  -3.257  76.061  1.00 56.46  ?  162 SER D CA  1 
ATOM   6110 C C   . SER D 2 162 ? 11.879  -4.192  75.114  1.00 60.24  ?  162 SER D C   1 
ATOM   6111 O O   . SER D 2 162 ? 12.390  -5.249  74.732  1.00 60.10  ?  162 SER D O   1 
ATOM   6112 C CB  . SER D 2 162 ? 13.579  -4.042  76.967  1.00 59.98  ?  162 SER D CB  1 
ATOM   6113 O OG  . SER D 2 162 ? 14.169  -3.181  77.926  1.00 58.72  ?  162 SER D OG  1 
ATOM   6114 N N   . GLY D 2 163 ? 10.659  -3.811  74.733  1.00 57.58  ?  163 GLY D N   1 
ATOM   6115 C CA  . GLY D 2 163 ? 9.839   -4.603  73.845  1.00 55.33  ?  163 GLY D CA  1 
ATOM   6116 C C   . GLY D 2 163 ? 8.794   -5.451  74.534  1.00 54.19  ?  163 GLY D C   1 
ATOM   6117 O O   . GLY D 2 163 ? 7.976   -6.071  73.847  1.00 58.92  ?  163 GLY D O   1 
ATOM   6118 N N   . ALA D 2 164 ? 8.792   -5.487  75.867  1.00 54.84  ?  164 ALA D N   1 
ATOM   6119 C CA  . ALA D 2 164 ? 7.833   -6.320  76.586  1.00 53.79  ?  164 ALA D CA  1 
ATOM   6120 C C   . ALA D 2 164 ? 6.418   -5.769  76.475  1.00 55.66  ?  164 ALA D C   1 
ATOM   6121 O O   . ALA D 2 164 ? 5.451   -6.538  76.416  1.00 60.65  ?  164 ALA D O   1 
ATOM   6122 C CB  . ALA D 2 164 ? 8.241   -6.443  78.053  1.00 55.23  ?  164 ALA D CB  1 
ATOM   6123 N N   . LEU D 2 165 ? 6.272   -4.446  76.459  1.00 55.03  ?  165 LEU D N   1 
ATOM   6124 C CA  . LEU D 2 165 ? 4.968   -3.790  76.401  1.00 51.61  ?  165 LEU D CA  1 
ATOM   6125 C C   . LEU D 2 165 ? 4.693   -3.357  74.964  1.00 56.07  ?  165 LEU D C   1 
ATOM   6126 O O   . LEU D 2 165 ? 5.388   -2.489  74.427  1.00 55.52  ?  165 LEU D O   1 
ATOM   6127 C CB  . LEU D 2 165 ? 4.924   -2.602  77.355  1.00 50.15  ?  165 LEU D CB  1 
ATOM   6128 C CG  . LEU D 2 165 ? 3.628   -1.790  77.384  1.00 50.54  ?  165 LEU D CG  1 
ATOM   6129 C CD1 . LEU D 2 165 ? 2.424   -2.688  77.613  1.00 50.68  ?  165 LEU D CD1 1 
ATOM   6130 C CD2 . LEU D 2 165 ? 3.709   -0.717  78.453  1.00 48.97  ?  165 LEU D CD2 1 
ATOM   6131 N N   . THR D 2 166 ? 3.670   -3.954  74.349  1.00 60.43  ?  166 THR D N   1 
ATOM   6132 C CA  . THR D 2 166 ? 3.334   -3.660  72.960  1.00 55.61  ?  166 THR D CA  1 
ATOM   6133 C C   . THR D 2 166 ? 1.873   -3.252  72.804  1.00 55.30  ?  166 THR D C   1 
ATOM   6134 O O   . THR D 2 166 ? 1.547   -2.420  71.951  1.00 54.65  ?  166 THR D O   1 
ATOM   6135 C CB  . THR D 2 166 ? 3.638   -4.863  72.060  1.00 53.49  ?  166 THR D CB  1 
ATOM   6136 O OG1 . THR D 2 166 ? 2.954   -6.020  72.555  1.00 62.65  ?  166 THR D OG1 1 
ATOM   6137 C CG2 . THR D 2 166 ? 5.131   -5.139  72.013  1.00 55.82  ?  166 THR D CG2 1 
ATOM   6138 N N   . SER D 2 167 ? 0.984   -3.824  73.610  1.00 58.07  ?  167 SER D N   1 
ATOM   6139 C CA  . SER D 2 167 ? -0.435  -3.534  73.461  1.00 56.98  ?  167 SER D CA  1 
ATOM   6140 C C   . SER D 2 167 ? -0.727  -2.125  73.951  1.00 51.19  ?  167 SER D C   1 
ATOM   6141 O O   . SER D 2 167 ? -0.304  -1.732  75.044  1.00 50.56  ?  167 SER D O   1 
ATOM   6142 C CB  . SER D 2 167 ? -1.282  -4.545  74.231  1.00 59.21  ?  167 SER D CB  1 
ATOM   6143 O OG  . SER D 2 167 ? -1.046  -4.447  75.623  1.00 67.10  ?  167 SER D OG  1 
ATOM   6144 N N   . GLY D 2 168 ? -1.453  -1.366  73.136  1.00 52.47  ?  168 GLY D N   1 
ATOM   6145 C CA  . GLY D 2 168 ? -1.777  0.004   73.461  1.00 48.08  ?  168 GLY D CA  1 
ATOM   6146 C C   . GLY D 2 168 ? -0.702  1.009   73.129  1.00 52.11  ?  168 GLY D C   1 
ATOM   6147 O O   . GLY D 2 168 ? -0.848  2.185   73.480  1.00 54.41  ?  168 GLY D O   1 
ATOM   6148 N N   . VAL D 2 169 ? 0.363   0.597   72.452  1.00 46.11  ?  169 VAL D N   1 
ATOM   6149 C CA  . VAL D 2 169 ? 1.458   1.498   72.119  1.00 50.82  ?  169 VAL D CA  1 
ATOM   6150 C C   . VAL D 2 169 ? 1.231   2.091   70.735  1.00 52.66  ?  169 VAL D C   1 
ATOM   6151 O O   . VAL D 2 169 ? 1.037   1.363   69.754  1.00 50.59  ?  169 VAL D O   1 
ATOM   6152 C CB  . VAL D 2 169 ? 2.810   0.772   72.194  1.00 46.19  ?  169 VAL D CB  1 
ATOM   6153 C CG1 . VAL D 2 169 ? 3.922   1.700   71.748  1.00 46.06  ?  169 VAL D CG1 1 
ATOM   6154 C CG2 . VAL D 2 169 ? 3.066   0.290   73.613  1.00 47.42  ?  169 VAL D CG2 1 
ATOM   6155 N N   . HIS D 2 170 ? 1.263   3.421   70.661  1.00 49.91  ?  170 HIS D N   1 
ATOM   6156 C CA  . HIS D 2 170 ? 1.203   4.168   69.412  1.00 48.95  ?  170 HIS D CA  1 
ATOM   6157 C C   . HIS D 2 170 ? 2.450   5.035   69.321  1.00 53.17  ?  170 HIS D C   1 
ATOM   6158 O O   . HIS D 2 170 ? 2.641   5.939   70.140  1.00 50.46  ?  170 HIS D O   1 
ATOM   6159 C CB  . HIS D 2 170 ? -0.053  5.042   69.339  1.00 51.48  ?  170 HIS D CB  1 
ATOM   6160 C CG  . HIS D 2 170 ? -1.333  4.268   69.365  1.00 55.07  ?  170 HIS D CG  1 
ATOM   6161 N ND1 . HIS D 2 170 ? -1.854  3.655   68.246  1.00 53.29  ?  170 HIS D ND1 1 
ATOM   6162 C CD2 . HIS D 2 170 ? -2.198  4.010   70.374  1.00 50.40  ?  170 HIS D CD2 1 
ATOM   6163 C CE1 . HIS D 2 170 ? -2.984  3.051   68.564  1.00 54.55  ?  170 HIS D CE1 1 
ATOM   6164 N NE2 . HIS D 2 170 ? -3.215  3.250   69.849  1.00 54.29  ?  170 HIS D NE2 1 
ATOM   6165 N N   . THR D 2 171 ? 3.290   4.766   68.333  1.00 48.76  ?  171 THR D N   1 
ATOM   6166 C CA  . THR D 2 171 ? 4.443   5.607   68.039  1.00 44.12  ?  171 THR D CA  1 
ATOM   6167 C C   . THR D 2 171 ? 4.112   6.405   66.786  1.00 49.08  ?  171 THR D C   1 
ATOM   6168 O O   . THR D 2 171 ? 3.986   5.835   65.698  1.00 50.53  ?  171 THR D O   1 
ATOM   6169 C CB  . THR D 2 171 ? 5.701   4.767   67.850  1.00 49.63  ?  171 THR D CB  1 
ATOM   6170 O OG1 . THR D 2 171 ? 5.962   4.025   69.049  1.00 53.49  ?  171 THR D OG1 1 
ATOM   6171 C CG2 . THR D 2 171 ? 6.890   5.658   67.546  1.00 49.59  ?  171 THR D CG2 1 
ATOM   6172 N N   . PHE D 2 172 ? 3.943   7.719   66.944  1.00 51.41  ?  172 PHE D N   1 
ATOM   6173 C CA  . PHE D 2 172 ? 3.484   8.521   65.823  1.00 48.99  ?  172 PHE D CA  1 
ATOM   6174 C C   . PHE D 2 172 ? 4.623   8.788   64.847  1.00 48.61  ?  172 PHE D C   1 
ATOM   6175 O O   . PHE D 2 172 ? 5.783   8.889   65.253  1.00 51.51  ?  172 PHE D O   1 
ATOM   6176 C CB  . PHE D 2 172 ? 2.903   9.840   66.310  1.00 40.45  ?  172 PHE D CB  1 
ATOM   6177 C CG  . PHE D 2 172 ? 1.689   9.677   67.163  1.00 46.62  ?  172 PHE D CG  1 
ATOM   6178 C CD1 . PHE D 2 172 ? 1.802   9.520   68.533  1.00 47.39  ?  172 PHE D CD1 1 
ATOM   6179 C CD2 . PHE D 2 172 ? 0.432   9.626   66.589  1.00 47.89  ?  172 PHE D CD2 1 
ATOM   6180 C CE1 . PHE D 2 172 ? 0.681   9.351   69.321  1.00 44.71  ?  172 PHE D CE1 1 
ATOM   6181 C CE2 . PHE D 2 172 ? -0.693  9.454   67.373  1.00 50.58  ?  172 PHE D CE2 1 
ATOM   6182 C CZ  . PHE D 2 172 ? -0.567  9.317   68.741  1.00 47.81  ?  172 PHE D CZ  1 
ATOM   6183 N N   . PRO D 2 173 ? 4.316   8.892   63.554  1.00 51.24  ?  173 PRO D N   1 
ATOM   6184 C CA  . PRO D 2 173 ? 5.352   9.256   62.579  1.00 46.81  ?  173 PRO D CA  1 
ATOM   6185 C C   . PRO D 2 173 ? 5.961   10.610  62.910  1.00 47.78  ?  173 PRO D C   1 
ATOM   6186 O O   . PRO D 2 173 ? 5.275   11.523  63.373  1.00 51.12  ?  173 PRO D O   1 
ATOM   6187 C CB  . PRO D 2 173 ? 4.594   9.289   61.246  1.00 47.97  ?  173 PRO D CB  1 
ATOM   6188 C CG  . PRO D 2 173 ? 3.362   8.456   61.480  1.00 51.35  ?  173 PRO D CG  1 
ATOM   6189 C CD  . PRO D 2 173 ? 3.009   8.646   62.919  1.00 51.17  ?  173 PRO D CD  1 
ATOM   6190 N N   . ALA D 2 174 ? 7.269   10.724  62.705  1.00 43.45  ?  174 ALA D N   1 
ATOM   6191 C CA  . ALA D 2 174 ? 7.941   11.983  62.975  1.00 45.68  ?  174 ALA D CA  1 
ATOM   6192 C C   . ALA D 2 174 ? 7.482   13.059  61.999  1.00 44.43  ?  174 ALA D C   1 
ATOM   6193 O O   . ALA D 2 174 ? 7.137   12.784  60.846  1.00 44.36  ?  174 ALA D O   1 
ATOM   6194 C CB  . ALA D 2 174 ? 9.455   11.817  62.885  1.00 48.49  ?  174 ALA D CB  1 
ATOM   6195 N N   . VAL D 2 175 ? 7.476   14.298  62.476  1.00 42.82  ?  175 VAL D N   1 
ATOM   6196 C CA  . VAL D 2 175 ? 7.184   15.458  61.646  1.00 46.75  ?  175 VAL D CA  1 
ATOM   6197 C C   . VAL D 2 175 ? 8.407   16.363  61.644  1.00 51.53  ?  175 VAL D C   1 
ATOM   6198 O O   . VAL D 2 175 ? 9.087   16.516  62.666  1.00 53.37  ?  175 VAL D O   1 
ATOM   6199 C CB  . VAL D 2 175 ? 5.930   16.221  62.125  1.00 48.99  ?  175 VAL D CB  1 
ATOM   6200 C CG1 . VAL D 2 175 ? 4.693   15.366  61.942  1.00 49.09  ?  175 VAL D CG1 1 
ATOM   6201 C CG2 . VAL D 2 175 ? 6.071   16.644  63.579  1.00 50.75  ?  175 VAL D CG2 1 
ATOM   6202 N N   . LEU D 2 176 ? 8.701   16.940  60.486  1.00 53.42  ?  176 LEU D N   1 
ATOM   6203 C CA  . LEU D 2 176 ? 9.800   17.887  60.372  1.00 52.12  ?  176 LEU D CA  1 
ATOM   6204 C C   . LEU D 2 176 ? 9.359   19.228  60.945  1.00 57.92  ?  176 LEU D C   1 
ATOM   6205 O O   . LEU D 2 176 ? 8.353   19.794  60.507  1.00 59.51  ?  176 LEU D O   1 
ATOM   6206 C CB  . LEU D 2 176 ? 10.227  18.029  58.914  1.00 48.36  ?  176 LEU D CB  1 
ATOM   6207 C CG  . LEU D 2 176 ? 11.517  18.806  58.664  1.00 53.49  ?  176 LEU D CG  1 
ATOM   6208 C CD1 . LEU D 2 176 ? 12.696  18.136  59.368  1.00 52.43  ?  176 LEU D CD1 1 
ATOM   6209 C CD2 . LEU D 2 176 ? 11.769  18.945  57.168  1.00 45.51  ?  176 LEU D CD2 1 
ATOM   6210 N N   . GLN D 2 177 ? 10.086  19.714  61.947  1.00 65.53  ?  177 GLN D N   1 
ATOM   6211 C CA  . GLN D 2 177 ? 9.787   20.998  62.561  1.00 64.22  ?  177 GLN D CA  1 
ATOM   6212 C C   . GLN D 2 177 ? 10.383  22.144  61.746  1.00 67.76  ?  177 GLN D C   1 
ATOM   6213 O O   . GLN D 2 177 ? 11.194  21.949  60.835  1.00 67.90  ?  177 GLN D O   1 
ATOM   6214 C CB  . GLN D 2 177 ? 10.304  21.050  63.996  1.00 60.93  ?  177 GLN D CB  1 
ATOM   6215 C CG  . GLN D 2 177 ? 9.645   20.067  64.931  1.00 60.95  ?  177 GLN D CG  1 
ATOM   6216 C CD  . GLN D 2 177 ? 10.323  20.024  66.285  1.00 70.83  ?  177 GLN D CD  1 
ATOM   6217 O OE1 . GLN D 2 177 ? 9.666   20.099  67.325  1.00 78.30  ?  177 GLN D OE1 1 
ATOM   6218 N NE2 . GLN D 2 177 ? 11.648  19.905  66.281  1.00 63.34  ?  177 GLN D NE2 1 
ATOM   6219 N N   . SER D 2 178 ? 9.970   23.365  62.097  1.00 68.17  ?  178 SER D N   1 
ATOM   6220 C CA  . SER D 2 178 ? 10.461  24.544  61.393  1.00 72.86  ?  178 SER D CA  1 
ATOM   6221 C C   . SER D 2 178 ? 11.973  24.676  61.505  1.00 70.88  ?  178 SER D C   1 
ATOM   6222 O O   . SER D 2 178 ? 12.619  25.207  60.594  1.00 72.95  ?  178 SER D O   1 
ATOM   6223 C CB  . SER D 2 178 ? 9.785   25.799  61.944  1.00 74.43  ?  178 SER D CB  1 
ATOM   6224 O OG  . SER D 2 178 ? 10.140  26.033  63.295  1.00 80.67  ?  178 SER D OG  1 
ATOM   6225 N N   . SER D 2 179 ? 12.557  24.172  62.592  1.00 62.85  ?  179 SER D N   1 
ATOM   6226 C CA  . SER D 2 179 ? 14.001  24.227  62.770  1.00 67.87  ?  179 SER D CA  1 
ATOM   6227 C C   . SER D 2 179 ? 14.758  23.326  61.799  1.00 66.52  ?  179 SER D C   1 
ATOM   6228 O O   . SER D 2 179 ? 15.989  23.404  61.744  1.00 62.47  ?  179 SER D O   1 
ATOM   6229 C CB  . SER D 2 179 ? 14.358  23.865  64.216  1.00 68.19  ?  179 SER D CB  1 
ATOM   6230 O OG  . SER D 2 179 ? 13.942  22.550  64.550  1.00 73.36  ?  179 SER D OG  1 
ATOM   6231 N N   . GLY D 2 180 ? 14.066  22.494  61.026  1.00 65.68  ?  180 GLY D N   1 
ATOM   6232 C CA  . GLY D 2 180 ? 14.731  21.497  60.215  1.00 63.26  ?  180 GLY D CA  1 
ATOM   6233 C C   . GLY D 2 180 ? 15.034  20.209  60.946  1.00 61.55  ?  180 GLY D C   1 
ATOM   6234 O O   . GLY D 2 180 ? 15.723  19.346  60.390  1.00 54.37  ?  180 GLY D O   1 
ATOM   6235 N N   . LEU D 2 181 ? 14.545  20.057  62.173  1.00 56.64  ?  181 LEU D N   1 
ATOM   6236 C CA  . LEU D 2 181 ? 14.748  18.872  62.986  1.00 53.96  ?  181 LEU D CA  1 
ATOM   6237 C C   . LEU D 2 181 ? 13.441  18.095  63.104  1.00 58.97  ?  181 LEU D C   1 
ATOM   6238 O O   . LEU D 2 181 ? 12.348  18.639  62.922  1.00 60.85  ?  181 LEU D O   1 
ATOM   6239 C CB  . LEU D 2 181 ? 15.263  19.251  64.379  1.00 55.54  ?  181 LEU D CB  1 
ATOM   6240 C CG  . LEU D 2 181 ? 16.609  19.973  64.446  1.00 56.81  ?  181 LEU D CG  1 
ATOM   6241 C CD1 . LEU D 2 181 ? 16.974  20.277  65.888  1.00 51.65  ?  181 LEU D CD1 1 
ATOM   6242 C CD2 . LEU D 2 181 ? 17.696  19.148  63.778  1.00 46.67  ?  181 LEU D CD2 1 
ATOM   6243 N N   . TYR D 2 182 ? 13.565  16.810  63.420  1.00 52.30  ?  182 TYR D N   1 
ATOM   6244 C CA  . TYR D 2 182 ? 12.411  15.933  63.540  1.00 51.00  ?  182 TYR D CA  1 
ATOM   6245 C C   . TYR D 2 182 ? 11.934  15.838  64.980  1.00 50.39  ?  182 TYR D C   1 
ATOM   6246 O O   . TYR D 2 182 ? 12.700  16.032  65.930  1.00 49.23  ?  182 TYR D O   1 
ATOM   6247 C CB  . TYR D 2 182 ? 12.732  14.528  63.022  1.00 46.90  ?  182 TYR D CB  1 
ATOM   6248 C CG  . TYR D 2 182 ? 12.776  14.416  61.520  1.00 47.34  ?  182 TYR D CG  1 
ATOM   6249 C CD1 . TYR D 2 182 ? 13.989  14.364  60.841  1.00 47.26  ?  182 TYR D CD1 1 
ATOM   6250 C CD2 . TYR D 2 182 ? 11.602  14.372  60.778  1.00 45.35  ?  182 TYR D CD2 1 
ATOM   6251 C CE1 . TYR D 2 182 ? 14.034  14.267  59.464  1.00 45.40  ?  182 TYR D CE1 1 
ATOM   6252 C CE2 . TYR D 2 182 ? 11.634  14.275  59.404  1.00 48.35  ?  182 TYR D CE2 1 
ATOM   6253 C CZ  . TYR D 2 182 ? 12.852  14.221  58.751  1.00 53.50  ?  182 TYR D CZ  1 
ATOM   6254 O OH  . TYR D 2 182 ? 12.886  14.125  57.378  1.00 56.07  ?  182 TYR D OH  1 
ATOM   6255 N N   . SER D 2 183 ? 10.650  15.532  65.132  1.00 50.24  ?  183 SER D N   1 
ATOM   6256 C CA  . SER D 2 183 ? 10.066  15.338  66.447  1.00 50.02  ?  183 SER D CA  1 
ATOM   6257 C C   . SER D 2 183 ? 8.928   14.335  66.329  1.00 45.53  ?  183 SER D C   1 
ATOM   6258 O O   . SER D 2 183 ? 8.188   14.341  65.339  1.00 47.12  ?  183 SER D O   1 
ATOM   6259 C CB  . SER D 2 183 ? 9.568   16.664  67.031  1.00 56.20  ?  183 SER D CB  1 
ATOM   6260 O OG  . SER D 2 183 ? 9.281   16.526  68.410  1.00 63.17  ?  183 SER D OG  1 
ATOM   6261 N N   . LEU D 2 184 ? 8.803   13.467  67.332  1.00 44.85  ?  184 LEU D N   1 
ATOM   6262 C CA  . LEU D 2 184 ? 7.717   12.498  67.372  1.00 45.06  ?  184 LEU D CA  1 
ATOM   6263 C C   . LEU D 2 184 ? 7.343   12.199  68.814  1.00 40.66  ?  184 LEU D C   1 
ATOM   6264 O O   . LEU D 2 184 ? 8.036   12.580  69.756  1.00 44.97  ?  184 LEU D O   1 
ATOM   6265 C CB  . LEU D 2 184 ? 8.074   11.207  66.624  1.00 44.84  ?  184 LEU D CB  1 
ATOM   6266 C CG  . LEU D 2 184 ? 9.170   10.220  67.047  1.00 47.89  ?  184 LEU D CG  1 
ATOM   6267 C CD1 . LEU D 2 184 ? 8.899   9.455   68.353  1.00 43.99  ?  184 LEU D CD1 1 
ATOM   6268 C CD2 . LEU D 2 184 ? 9.322   9.236   65.905  1.00 43.08  ?  184 LEU D CD2 1 
ATOM   6269 N N   . SER D 2 185 ? 6.234   11.498  68.974  1.00 42.90  ?  185 SER D N   1 
ATOM   6270 C CA  . SER D 2 185 ? 5.779   11.069  70.283  1.00 42.50  ?  185 SER D CA  1 
ATOM   6271 C C   . SER D 2 185 ? 5.432   9.590   70.250  1.00 45.17  ?  185 SER D C   1 
ATOM   6272 O O   . SER D 2 185 ? 5.002   9.052   69.225  1.00 44.67  ?  185 SER D O   1 
ATOM   6273 C CB  . SER D 2 185 ? 4.569   11.876  70.745  1.00 46.65  ?  185 SER D CB  1 
ATOM   6274 O OG  . SER D 2 185 ? 4.936   13.215  71.020  1.00 54.06  ?  185 SER D OG  1 
ATOM   6275 N N   . SER D 2 186 ? 5.648   8.934   71.384  1.00 42.99  ?  186 SER D N   1 
ATOM   6276 C CA  . SER D 2 186 ? 5.224   7.559   71.587  1.00 45.29  ?  186 SER D CA  1 
ATOM   6277 C C   . SER D 2 186 ? 4.375   7.525   72.845  1.00 47.45  ?  186 SER D C   1 
ATOM   6278 O O   . SER D 2 186 ? 4.769   8.076   73.872  1.00 48.28  ?  186 SER D O   1 
ATOM   6279 C CB  . SER D 2 186 ? 6.419   6.612   71.714  1.00 47.92  ?  186 SER D CB  1 
ATOM   6280 O OG  . SER D 2 186 ? 6.002   5.258   71.816  1.00 46.03  ?  186 SER D OG  1 
ATOM   6281 N N   . VAL D 2 187 ? 3.200   6.908   72.759  1.00 46.73  ?  187 VAL D N   1 
ATOM   6282 C CA  . VAL D 2 187 ? 2.257   6.880   73.865  1.00 46.68  ?  187 VAL D CA  1 
ATOM   6283 C C   . VAL D 2 187 ? 1.805   5.448   74.100  1.00 48.22  ?  187 VAL D C   1 
ATOM   6284 O O   . VAL D 2 187 ? 1.894   4.582   73.228  1.00 47.98  ?  187 VAL D O   1 
ATOM   6285 C CB  . VAL D 2 187 ? 1.032   7.788   73.623  1.00 48.47  ?  187 VAL D CB  1 
ATOM   6286 C CG1 . VAL D 2 187 ? 1.433   9.248   73.674  1.00 47.40  ?  187 VAL D CG1 1 
ATOM   6287 C CG2 . VAL D 2 187 ? 0.391   7.454   72.292  1.00 47.71  ?  187 VAL D CG2 1 
ATOM   6288 N N   . VAL D 2 188 ? 1.331   5.211   75.314  1.00 46.64  ?  188 VAL D N   1 
ATOM   6289 C CA  . VAL D 2 188 ? 0.735   3.939   75.687  1.00 49.89  ?  188 VAL D CA  1 
ATOM   6290 C C   . VAL D 2 188 ? -0.388  4.217   76.679  1.00 52.91  ?  188 VAL D C   1 
ATOM   6291 O O   . VAL D 2 188 ? -0.297  5.126   77.513  1.00 56.13  ?  188 VAL D O   1 
ATOM   6292 C CB  . VAL D 2 188 ? 1.797   2.969   76.249  1.00 51.93  ?  188 VAL D CB  1 
ATOM   6293 C CG1 . VAL D 2 188 ? 2.560   3.616   77.388  1.00 48.21  ?  188 VAL D CG1 1 
ATOM   6294 C CG2 . VAL D 2 188 ? 1.159   1.658   76.687  1.00 47.79  ?  188 VAL D CG2 1 
ATOM   6295 N N   . THR D 2 189 ? -1.475  3.467   76.536  1.00 54.64  ?  189 THR D N   1 
ATOM   6296 C CA  . THR D 2 189 ? -2.595  3.510   77.463  1.00 57.04  ?  189 THR D CA  1 
ATOM   6297 C C   . THR D 2 189 ? -2.475  2.330   78.418  1.00 53.56  ?  189 THR D C   1 
ATOM   6298 O O   . THR D 2 189 ? -2.284  1.191   77.979  1.00 54.45  ?  189 THR D O   1 
ATOM   6299 C CB  . THR D 2 189 ? -3.934  3.476   76.720  1.00 57.25  ?  189 THR D CB  1 
ATOM   6300 O OG1 . THR D 2 189 ? -3.847  2.586   75.599  1.00 61.55  ?  189 THR D OG1 1 
ATOM   6301 C CG2 . THR D 2 189 ? -4.305  4.866   76.228  1.00 52.43  ?  189 THR D CG2 1 
ATOM   6302 N N   . VAL D 2 190 ? -2.581  2.610   79.714  1.00 57.34  ?  190 VAL D N   1 
ATOM   6303 C CA  . VAL D 2 190 ? -2.365  1.613   80.761  1.00 58.93  ?  190 VAL D CA  1 
ATOM   6304 C C   . VAL D 2 190 ? -3.533  1.667   81.737  1.00 60.44  ?  190 VAL D C   1 
ATOM   6305 O O   . VAL D 2 190 ? -4.282  2.656   81.783  1.00 62.80  ?  190 VAL D O   1 
ATOM   6306 C CB  . VAL D 2 190 ? -1.028  1.847   81.501  1.00 57.41  ?  190 VAL D CB  1 
ATOM   6307 C CG1 . VAL D 2 190 ? 0.133   1.797   80.531  1.00 56.43  ?  190 VAL D CG1 1 
ATOM   6308 C CG2 . VAL D 2 190 ? -1.064  3.182   82.227  1.00 58.78  ?  190 VAL D CG2 1 
ATOM   6309 N N   . PRO D 2 191 ? -3.728  0.606   82.524  1.00 67.27  ?  191 PRO D N   1 
ATOM   6310 C CA  . PRO D 2 191 ? -4.690  0.687   83.627  1.00 64.38  ?  191 PRO D CA  1 
ATOM   6311 C C   . PRO D 2 191 ? -4.244  1.729   84.639  1.00 61.90  ?  191 PRO D C   1 
ATOM   6312 O O   . PRO D 2 191 ? -3.068  1.803   84.998  1.00 67.58  ?  191 PRO D O   1 
ATOM   6313 C CB  . PRO D 2 191 ? -4.667  -0.724  84.226  1.00 63.22  ?  191 PRO D CB  1 
ATOM   6314 C CG  . PRO D 2 191 ? -4.153  -1.595  83.138  1.00 56.70  ?  191 PRO D CG  1 
ATOM   6315 C CD  . PRO D 2 191 ? -3.184  -0.756  82.367  1.00 58.31  ?  191 PRO D CD  1 
ATOM   6316 N N   . SER D 2 192 ? -5.199  2.532   85.109  1.00 66.99  ?  192 SER D N   1 
ATOM   6317 C CA  . SER D 2 192 ? -4.864  3.568   86.082  1.00 67.70  ?  192 SER D CA  1 
ATOM   6318 C C   . SER D 2 192 ? -4.291  2.969   87.358  1.00 68.80  ?  192 SER D C   1 
ATOM   6319 O O   . SER D 2 192 ? -3.452  3.595   88.014  1.00 67.07  ?  192 SER D O   1 
ATOM   6320 C CB  . SER D 2 192 ? -6.099  4.417   86.394  1.00 70.00  ?  192 SER D CB  1 
ATOM   6321 O OG  . SER D 2 192 ? -5.780  5.490   87.260  1.00 78.62  ?  192 SER D OG  1 
ATOM   6322 N N   . SER D 2 193 ? -4.717  1.755   87.716  1.00 77.94  ?  193 SER D N   1 
ATOM   6323 C CA  . SER D 2 193 ? -4.208  1.079   88.903  1.00 76.82  ?  193 SER D CA  1 
ATOM   6324 C C   . SER D 2 193 ? -2.782  0.565   88.731  1.00 78.69  ?  193 SER D C   1 
ATOM   6325 O O   . SER D 2 193 ? -2.157  0.176   89.724  1.00 82.18  ?  193 SER D O   1 
ATOM   6326 C CB  . SER D 2 193 ? -5.139  -0.076  89.277  1.00 74.39  ?  193 SER D CB  1 
ATOM   6327 O OG  . SER D 2 193 ? -5.233  -1.027  88.230  1.00 73.04  ?  193 SER D OG  1 
ATOM   6328 N N   . SER D 2 194 ? -2.252  0.557   87.507  1.00 77.25  ?  194 SER D N   1 
ATOM   6329 C CA  . SER D 2 194 ? -0.888  0.097   87.287  1.00 75.69  ?  194 SER D CA  1 
ATOM   6330 C C   . SER D 2 194 ? 0.145   1.138   87.694  1.00 78.35  ?  194 SER D C   1 
ATOM   6331 O O   . SER D 2 194 ? 1.299   0.776   87.948  1.00 79.22  ?  194 SER D O   1 
ATOM   6332 C CB  . SER D 2 194 ? -0.679  -0.279  85.819  1.00 71.31  ?  194 SER D CB  1 
ATOM   6333 O OG  . SER D 2 194 ? -1.479  -1.387  85.453  1.00 81.77  ?  194 SER D OG  1 
ATOM   6334 N N   . LEU D 2 195 ? -0.238  2.412   87.758  1.00 74.18  ?  195 LEU D N   1 
ATOM   6335 C CA  . LEU D 2 195 ? 0.698   3.437   88.191  1.00 68.99  ?  195 LEU D CA  1 
ATOM   6336 C C   . LEU D 2 195 ? 1.146   3.135   89.613  1.00 76.45  ?  195 LEU D C   1 
ATOM   6337 O O   . LEU D 2 195 ? 0.361   2.670   90.446  1.00 78.83  ?  195 LEU D O   1 
ATOM   6338 C CB  . LEU D 2 195 ? 0.052   4.820   88.119  1.00 70.24  ?  195 LEU D CB  1 
ATOM   6339 C CG  . LEU D 2 195 ? -0.793  5.166   86.887  1.00 68.56  ?  195 LEU D CG  1 
ATOM   6340 C CD1 . LEU D 2 195 ? -1.312  6.594   86.984  1.00 64.90  ?  195 LEU D CD1 1 
ATOM   6341 C CD2 . LEU D 2 195 ? -0.015  4.956   85.596  1.00 62.64  ?  195 LEU D CD2 1 
ATOM   6342 N N   . GLY D 2 196 ? 2.413   3.404   89.895  1.00 77.20  ?  196 GLY D N   1 
ATOM   6343 C CA  . GLY D 2 196 ? 2.959   3.014   91.178  1.00 78.17  ?  196 GLY D CA  1 
ATOM   6344 C C   . GLY D 2 196 ? 3.407   1.565   91.220  1.00 80.31  ?  196 GLY D C   1 
ATOM   6345 O O   . GLY D 2 196 ? 4.560   1.282   91.559  1.00 83.34  ?  196 GLY D O   1 
ATOM   6346 N N   . THR D 2 197 ? 2.507   0.635   90.892  1.00 80.67  ?  197 THR D N   1 
ATOM   6347 C CA  . THR D 2 197 ? 2.810   -0.793  90.948  1.00 85.56  ?  197 THR D CA  1 
ATOM   6348 C C   . THR D 2 197 ? 3.528   -1.325  89.708  1.00 87.21  ?  197 THR D C   1 
ATOM   6349 O O   . THR D 2 197 ? 3.813   -2.528  89.653  1.00 88.48  ?  197 THR D O   1 
ATOM   6350 C CB  . THR D 2 197 ? 1.522   -1.601  91.176  1.00 84.37  ?  197 THR D CB  1 
ATOM   6351 O OG1 . THR D 2 197 ? 0.619   -1.409  90.078  1.00 85.84  ?  197 THR D OG1 1 
ATOM   6352 C CG2 . THR D 2 197 ? 0.843   -1.169  92.469  1.00 87.44  ?  197 THR D CG2 1 
ATOM   6353 N N   . GLN D 2 198 ? 3.828   -0.482  88.721  1.00 78.82  ?  198 GLN D N   1 
ATOM   6354 C CA  . GLN D 2 198 ? 4.499   -0.940  87.510  1.00 73.58  ?  198 GLN D CA  1 
ATOM   6355 C C   . GLN D 2 198 ? 5.350   0.190   86.952  1.00 74.54  ?  198 GLN D C   1 
ATOM   6356 O O   . GLN D 2 198 ? 4.902   1.339   86.890  1.00 75.83  ?  198 GLN D O   1 
ATOM   6357 C CB  . GLN D 2 198 ? 3.495   -1.418  86.453  1.00 76.34  ?  198 GLN D CB  1 
ATOM   6358 C CG  . GLN D 2 198 ? 4.138   -1.922  85.161  1.00 79.00  ?  198 GLN D CG  1 
ATOM   6359 C CD  . GLN D 2 198 ? 4.810   -3.279  85.325  1.00 84.10  ?  198 GLN D CD  1 
ATOM   6360 O OE1 . GLN D 2 198 ? 4.293   -4.162  86.014  1.00 87.44  ?  198 GLN D OE1 1 
ATOM   6361 N NE2 . GLN D 2 198 ? 5.966   -3.451  84.687  1.00 76.77  ?  198 GLN D NE2 1 
ATOM   6362 N N   . THR D 2 199 ? 6.570   -0.144  86.533  1.00 69.13  ?  199 THR D N   1 
ATOM   6363 C CA  . THR D 2 199 ? 7.480   0.843   85.965  1.00 69.04  ?  199 THR D CA  1 
ATOM   6364 C C   . THR D 2 199 ? 7.356   0.847   84.447  1.00 63.75  ?  199 THR D C   1 
ATOM   6365 O O   . THR D 2 199 ? 7.366   -0.212  83.812  1.00 59.26  ?  199 THR D O   1 
ATOM   6366 C CB  . THR D 2 199 ? 8.926   0.551   86.366  1.00 60.71  ?  199 THR D CB  1 
ATOM   6367 O OG1 . THR D 2 199 ? 9.272   -0.773  85.950  1.00 66.75  ?  199 THR D OG1 1 
ATOM   6368 C CG2 . THR D 2 199 ? 9.091   0.656   87.875  1.00 53.88  ?  199 THR D CG2 1 
ATOM   6369 N N   . TYR D 2 200 ? 7.251   2.041   83.872  1.00 61.02  ?  200 TYR D N   1 
ATOM   6370 C CA  . TYR D 2 200 ? 7.105   2.215   82.434  1.00 56.31  ?  200 TYR D CA  1 
ATOM   6371 C C   . TYR D 2 200 ? 8.320   2.966   81.912  1.00 55.78  ?  200 TYR D C   1 
ATOM   6372 O O   . TYR D 2 200 ? 8.590   4.092   82.342  1.00 55.71  ?  200 TYR D O   1 
ATOM   6373 C CB  . TYR D 2 200 ? 5.801   2.944   82.105  1.00 55.08  ?  200 TYR D CB  1 
ATOM   6374 C CG  . TYR D 2 200 ? 4.596   2.085   82.404  1.00 62.25  ?  200 TYR D CG  1 
ATOM   6375 C CD1 . TYR D 2 200 ? 4.217   1.071   81.532  1.00 65.51  ?  200 TYR D CD1 1 
ATOM   6376 C CD2 . TYR D 2 200 ? 3.860   2.257   83.569  1.00 59.42  ?  200 TYR D CD2 1 
ATOM   6377 C CE1 . TYR D 2 200 ? 3.128   0.265   81.801  1.00 59.87  ?  200 TYR D CE1 1 
ATOM   6378 C CE2 . TYR D 2 200 ? 2.766   1.457   83.844  1.00 61.63  ?  200 TYR D CE2 1 
ATOM   6379 C CZ  . TYR D 2 200 ? 2.406   0.462   82.954  1.00 61.82  ?  200 TYR D CZ  1 
ATOM   6380 O OH  . TYR D 2 200 ? 1.323   -0.344  83.213  1.00 64.16  ?  200 TYR D OH  1 
ATOM   6381 N N   . ILE D 2 201 ? 9.068   2.322   81.016  1.00 53.32  ?  201 ILE D N   1 
ATOM   6382 C CA  . ILE D 2 201 ? 10.323  2.847   80.498  1.00 50.79  ?  201 ILE D CA  1 
ATOM   6383 C C   . ILE D 2 201 ? 10.275  2.815   78.980  1.00 46.42  ?  201 ILE D C   1 
ATOM   6384 O O   . ILE D 2 201 ? 10.044  1.757   78.385  1.00 48.04  ?  201 ILE D O   1 
ATOM   6385 C CB  . ILE D 2 201 ? 11.528  2.037   81.003  1.00 49.61  ?  201 ILE D CB  1 
ATOM   6386 C CG1 . ILE D 2 201 ? 11.548  2.012   82.525  1.00 54.13  ?  201 ILE D CG1 1 
ATOM   6387 C CG2 . ILE D 2 201 ? 12.818  2.646   80.489  1.00 48.46  ?  201 ILE D CG2 1 
ATOM   6388 C CD1 . ILE D 2 201 ? 12.594  1.091   83.081  1.00 57.00  ?  201 ILE D CD1 1 
ATOM   6389 N N   . CYS D 2 202 ? 10.524  3.958   78.354  1.00 42.66  ?  202 CYS D N   1 
ATOM   6390 C CA  . CYS D 2 202 ? 10.595  4.033   76.903  1.00 46.85  ?  202 CYS D CA  1 
ATOM   6391 C C   . CYS D 2 202 ? 12.054  4.026   76.457  1.00 49.17  ?  202 CYS D C   1 
ATOM   6392 O O   . CYS D 2 202 ? 12.924  4.622   77.103  1.00 46.44  ?  202 CYS D O   1 
ATOM   6393 C CB  . CYS D 2 202 ? 9.865   5.276   76.379  1.00 43.70  ?  202 CYS D CB  1 
ATOM   6394 S SG  . CYS D 2 202 ? 10.808  6.815   76.351  1.00 63.54  ?  202 CYS D SG  1 
ATOM   6395 N N   . ASN D 2 203 ? 12.319  3.296   75.376  1.00 41.89  ?  203 ASN D N   1 
ATOM   6396 C CA  . ASN D 2 203 ? 13.653  3.105   74.828  1.00 42.13  ?  203 ASN D CA  1 
ATOM   6397 C C   . ASN D 2 203 ? 13.662  3.714   73.436  1.00 44.48  ?  203 ASN D C   1 
ATOM   6398 O O   . ASN D 2 203 ? 12.998  3.201   72.527  1.00 45.46  ?  203 ASN D O   1 
ATOM   6399 C CB  . ASN D 2 203 ? 14.022  1.626   74.782  1.00 45.14  ?  203 ASN D CB  1 
ATOM   6400 C CG  . ASN D 2 203 ? 13.437  0.840   75.939  1.00 47.70  ?  203 ASN D CG  1 
ATOM   6401 O OD1 . ASN D 2 203 ? 12.592  -0.032  75.743  1.00 49.34  ?  203 ASN D OD1 1 
ATOM   6402 N ND2 . ASN D 2 203 ? 13.877  1.151   77.153  1.00 47.96  ?  203 ASN D ND2 1 
ATOM   6403 N N   . VAL D 2 204 ? 14.387  4.820   73.287  1.00 39.76  ?  204 VAL D N   1 
ATOM   6404 C CA  . VAL D 2 204 ? 14.542  5.520   72.020  1.00 43.17  ?  204 VAL D CA  1 
ATOM   6405 C C   . VAL D 2 204 ? 15.916  5.182   71.470  1.00 47.97  ?  204 VAL D C   1 
ATOM   6406 O O   . VAL D 2 204 ? 16.917  5.258   72.191  1.00 47.63  ?  204 VAL D O   1 
ATOM   6407 C CB  . VAL D 2 204 ? 14.377  7.040   72.199  1.00 44.34  ?  204 VAL D CB  1 
ATOM   6408 C CG1 . VAL D 2 204 ? 14.335  7.739   70.852  1.00 42.85  ?  204 VAL D CG1 1 
ATOM   6409 C CG2 . VAL D 2 204 ? 13.123  7.345   72.995  1.00 38.55  ?  204 VAL D CG2 1 
ATOM   6410 N N   . ASN D 2 205 ? 15.969  4.795   70.201  1.00 49.73  ?  205 ASN D N   1 
ATOM   6411 C CA  . ASN D 2 205 ? 17.221  4.469   69.540  1.00 48.98  ?  205 ASN D CA  1 
ATOM   6412 C C   . ASN D 2 205 ? 17.361  5.322   68.289  1.00 44.58  ?  205 ASN D C   1 
ATOM   6413 O O   . ASN D 2 205 ? 16.454  5.362   67.450  1.00 50.25  ?  205 ASN D O   1 
ATOM   6414 C CB  . ASN D 2 205 ? 17.303  2.981   69.188  1.00 48.88  ?  205 ASN D CB  1 
ATOM   6415 C CG  . ASN D 2 205 ? 18.728  2.536   68.894  1.00 62.23  ?  205 ASN D CG  1 
ATOM   6416 O OD1 . ASN D 2 205 ? 19.091  2.293   67.743  1.00 66.27  ?  205 ASN D OD1 1 
ATOM   6417 N ND2 . ASN D 2 205 ? 19.547  2.438   69.938  1.00 61.19  ?  205 ASN D ND2 1 
ATOM   6418 N N   . HIS D 2 206 ? 18.487  6.021   68.187  1.00 44.40  ?  206 HIS D N   1 
ATOM   6419 C CA  . HIS D 2 206 ? 18.815  6.881   67.058  1.00 48.79  ?  206 HIS D CA  1 
ATOM   6420 C C   . HIS D 2 206 ? 20.180  6.404   66.569  1.00 48.71  ?  206 HIS D C   1 
ATOM   6421 O O   . HIS D 2 206 ? 21.221  6.899   67.014  1.00 45.04  ?  206 HIS D O   1 
ATOM   6422 C CB  . HIS D 2 206 ? 18.814  8.347   67.469  1.00 44.93  ?  206 HIS D CB  1 
ATOM   6423 C CG  . HIS D 2 206 ? 18.904  9.297   66.319  1.00 43.89  ?  206 HIS D CG  1 
ATOM   6424 N ND1 . HIS D 2 206 ? 19.827  10.318  66.272  1.00 41.46  ?  206 HIS D ND1 1 
ATOM   6425 C CD2 . HIS D 2 206 ? 18.192  9.376   65.171  1.00 41.87  ?  206 HIS D CD2 1 
ATOM   6426 C CE1 . HIS D 2 206 ? 19.677  10.989  65.144  1.00 46.17  ?  206 HIS D CE1 1 
ATOM   6427 N NE2 . HIS D 2 206 ? 18.687  10.442  64.461  1.00 47.48  ?  206 HIS D NE2 1 
ATOM   6428 N N   . LYS D 2 207 ? 20.158  5.399   65.694  1.00 51.95  ?  207 LYS D N   1 
ATOM   6429 C CA  . LYS D 2 207 ? 21.397  4.876   65.126  1.00 50.56  ?  207 LYS D CA  1 
ATOM   6430 C C   . LYS D 2 207 ? 22.237  5.923   64.408  1.00 44.29  ?  207 LYS D C   1 
ATOM   6431 O O   . LYS D 2 207 ? 23.467  5.901   64.584  1.00 49.31  ?  207 LYS D O   1 
ATOM   6432 C CB  . LYS D 2 207 ? 21.085  3.708   64.181  1.00 51.11  ?  207 LYS D CB  1 
ATOM   6433 C CG  . LYS D 2 207 ? 20.808  2.386   64.873  1.00 54.50  ?  207 LYS D CG  1 
ATOM   6434 C CD  . LYS D 2 207 ? 20.422  1.317   63.858  1.00 67.20  ?  207 LYS D CD  1 
ATOM   6435 C CE  . LYS D 2 207 ? 19.829  0.083   64.530  1.00 72.49  ?  207 LYS D CE  1 
ATOM   6436 N NZ  . LYS D 2 207 ? 20.723  -0.460  65.595  1.00 72.37  ?  207 LYS D NZ  1 
ATOM   6437 N N   . PRO D 2 208 ? 21.683  6.839   63.605  1.00 44.90  ?  208 PRO D N   1 
ATOM   6438 C CA  . PRO D 2 208 ? 22.553  7.817   62.924  1.00 50.64  ?  208 PRO D CA  1 
ATOM   6439 C C   . PRO D 2 208 ? 23.346  8.712   63.868  1.00 51.56  ?  208 PRO D C   1 
ATOM   6440 O O   . PRO D 2 208 ? 24.317  9.333   63.423  1.00 55.09  ?  208 PRO D O   1 
ATOM   6441 C CB  . PRO D 2 208 ? 21.573  8.630   62.062  1.00 47.54  ?  208 PRO D CB  1 
ATOM   6442 C CG  . PRO D 2 208 ? 20.216  8.313   62.583  1.00 44.83  ?  208 PRO D CG  1 
ATOM   6443 C CD  . PRO D 2 208 ? 20.291  6.939   63.132  1.00 44.75  ?  208 PRO D CD  1 
ATOM   6444 N N   . SER D 2 209 ? 22.967  8.803   65.144  1.00 54.26  ?  209 SER D N   1 
ATOM   6445 C CA  . SER D 2 209 ? 23.767  9.461   66.171  1.00 47.26  ?  209 SER D CA  1 
ATOM   6446 C C   . SER D 2 209 ? 24.520  8.487   67.059  1.00 50.41  ?  209 SER D C   1 
ATOM   6447 O O   . SER D 2 209 ? 25.280  8.931   67.923  1.00 53.02  ?  209 SER D O   1 
ATOM   6448 C CB  . SER D 2 209 ? 22.888  10.336  67.066  1.00 46.56  ?  209 SER D CB  1 
ATOM   6449 O OG  . SER D 2 209 ? 22.700  11.616  66.509  1.00 59.55  ?  209 SER D OG  1 
ATOM   6450 N N   . ASN D 2 210 ? 24.306  7.181   66.891  1.00 51.55  ?  210 ASN D N   1 
ATOM   6451 C CA  . ASN D 2 210 ? 24.772  6.186   67.857  1.00 51.75  ?  210 ASN D CA  1 
ATOM   6452 C C   . ASN D 2 210 ? 24.294  6.536   69.259  1.00 52.44  ?  210 ASN D C   1 
ATOM   6453 O O   . ASN D 2 210 ? 25.057  6.507   70.225  1.00 55.69  ?  210 ASN D O   1 
ATOM   6454 C CB  . ASN D 2 210 ? 26.293  6.035   67.829  1.00 60.45  ?  210 ASN D CB  1 
ATOM   6455 C CG  . ASN D 2 210 ? 26.799  5.447   66.530  1.00 62.04  ?  210 ASN D CG  1 
ATOM   6456 O OD1 . ASN D 2 210 ? 26.471  4.307   66.182  1.00 57.39  ?  210 ASN D OD1 1 
ATOM   6457 N ND2 . ASN D 2 210 ? 27.571  6.217   65.798  1.00 56.76  ?  210 ASN D ND2 1 
ATOM   6458 N N   . THR D 2 211 ? 23.025  6.907   69.370  1.00 53.27  ?  211 THR D N   1 
ATOM   6459 C CA  . THR D 2 211 ? 22.470  7.347   70.639  1.00 54.63  ?  211 THR D CA  1 
ATOM   6460 C C   . THR D 2 211 ? 21.324  6.429   71.033  1.00 51.38  ?  211 THR D C   1 
ATOM   6461 O O   . THR D 2 211 ? 20.506  6.051   70.193  1.00 51.12  ?  211 THR D O   1 
ATOM   6462 C CB  . THR D 2 211 ? 21.983  8.809   70.557  1.00 53.68  ?  211 THR D CB  1 
ATOM   6463 O OG1 . THR D 2 211 ? 23.045  9.650   70.093  1.00 53.80  ?  211 THR D OG1 1 
ATOM   6464 C CG2 . THR D 2 211 ? 21.511  9.298   71.917  1.00 46.15  ?  211 THR D CG2 1 
ATOM   6465 N N   . LYS D 2 212 ? 21.292  6.038   72.305  1.00 53.61  ?  212 LYS D N   1 
ATOM   6466 C CA  . LYS D 2 212 ? 20.145  5.345   72.877  1.00 49.87  ?  212 LYS D CA  1 
ATOM   6467 C C   . LYS D 2 212 ? 19.777  6.006   74.194  1.00 51.16  ?  212 LYS D C   1 
ATOM   6468 O O   . LYS D 2 212 ? 20.639  6.200   75.056  1.00 54.99  ?  212 LYS D O   1 
ATOM   6469 C CB  . LYS D 2 212 ? 20.409  3.854   73.111  1.00 49.75  ?  212 LYS D CB  1 
ATOM   6470 C CG  . LYS D 2 212 ? 19.234  3.201   73.834  1.00 60.73  ?  212 LYS D CG  1 
ATOM   6471 C CD  . LYS D 2 212 ? 19.253  1.680   73.865  1.00 67.18  ?  212 LYS D CD  1 
ATOM   6472 C CE  . LYS D 2 212 ? 17.900  1.158   74.385  1.00 64.64  ?  212 LYS D CE  1 
ATOM   6473 N NZ  . LYS D 2 212 ? 17.792  -0.330  74.459  1.00 72.24  ?  212 LYS D NZ  1 
ATOM   6474 N N   . VAL D 2 213 ? 18.497  6.315   74.363  1.00 48.59  ?  213 VAL D N   1 
ATOM   6475 C CA  . VAL D 2 213 ? 17.986  6.930   75.581  1.00 47.53  ?  213 VAL D CA  1 
ATOM   6476 C C   . VAL D 2 213 ? 16.953  5.998   76.198  1.00 50.95  ?  213 VAL D C   1 
ATOM   6477 O O   . VAL D 2 213 ? 16.096  5.449   75.498  1.00 48.59  ?  213 VAL D O   1 
ATOM   6478 C CB  . VAL D 2 213 ? 17.370  8.317   75.312  1.00 39.44  ?  213 VAL D CB  1 
ATOM   6479 C CG1 . VAL D 2 213 ? 16.954  8.960   76.611  1.00 44.65  ?  213 VAL D CG1 1 
ATOM   6480 C CG2 . VAL D 2 213 ? 18.354  9.197   74.580  1.00 48.48  ?  213 VAL D CG2 1 
ATOM   6481 N N   . ASP D 2 214 ? 17.034  5.823   77.511  1.00 48.70  ?  214 ASP D N   1 
ATOM   6482 C CA  . ASP D 2 214 ? 16.049  5.051   78.259  1.00 51.66  ?  214 ASP D CA  1 
ATOM   6483 C C   . ASP D 2 214 ? 15.459  5.973   79.316  1.00 52.75  ?  214 ASP D C   1 
ATOM   6484 O O   . ASP D 2 214 ? 16.158  6.381   80.250  1.00 57.40  ?  214 ASP D O   1 
ATOM   6485 C CB  . ASP D 2 214 ? 16.682  3.806   78.881  1.00 46.53  ?  214 ASP D CB  1 
ATOM   6486 C CG  . ASP D 2 214 ? 17.150  2.805   77.838  1.00 60.34  ?  214 ASP D CG  1 
ATOM   6487 O OD1 . ASP D 2 214 ? 18.314  2.899   77.392  1.00 68.96  ?  214 ASP D OD1 1 
ATOM   6488 O OD2 . ASP D 2 214 ? 16.354  1.920   77.459  1.00 61.87  ?  214 ASP D OD2 1 
ATOM   6489 N N   . LYS D 2 215 ? 14.180  6.309   79.168  1.00 49.02  ?  215 LYS D N   1 
ATOM   6490 C CA  . LYS D 2 215 ? 13.521  7.277   80.038  1.00 48.27  ?  215 LYS D CA  1 
ATOM   6491 C C   . LYS D 2 215 ? 12.389  6.591   80.785  1.00 51.80  ?  215 LYS D C   1 
ATOM   6492 O O   . LYS D 2 215 ? 11.484  6.021   80.165  1.00 52.87  ?  215 LYS D O   1 
ATOM   6493 C CB  . LYS D 2 215 ? 12.996  8.476   79.240  1.00 48.23  ?  215 LYS D CB  1 
ATOM   6494 C CG  . LYS D 2 215 ? 11.978  9.320   79.984  1.00 49.90  ?  215 LYS D CG  1 
ATOM   6495 C CD  . LYS D 2 215 ? 12.567  10.069  81.175  1.00 50.41  ?  215 LYS D CD  1 
ATOM   6496 C CE  . LYS D 2 215 ? 13.319  11.318  80.748  1.00 59.42  ?  215 LYS D CE  1 
ATOM   6497 N NZ  . LYS D 2 215 ? 13.695  12.170  81.921  1.00 59.40  ?  215 LYS D NZ  1 
ATOM   6498 N N   . LYS D 2 216 ? 12.456  6.630   82.113  1.00 51.51  ?  216 LYS D N   1 
ATOM   6499 C CA  . LYS D 2 216 ? 11.367  6.148   82.950  1.00 54.28  ?  216 LYS D CA  1 
ATOM   6500 C C   . LYS D 2 216 ? 10.316  7.241   83.088  1.00 54.03  ?  216 LYS D C   1 
ATOM   6501 O O   . LYS D 2 216 ? 10.630  8.370   83.475  1.00 57.12  ?  216 LYS D O   1 
ATOM   6502 C CB  . LYS D 2 216 ? 11.893  5.746   84.328  1.00 56.99  ?  216 LYS D CB  1 
ATOM   6503 C CG  . LYS D 2 216 ? 10.873  5.075   85.233  1.00 59.11  ?  216 LYS D CG  1 
ATOM   6504 C CD  . LYS D 2 216 ? 11.390  4.995   86.660  1.00 61.73  ?  216 LYS D CD  1 
ATOM   6505 C CE  . LYS D 2 216 ? 10.509  4.110   87.542  1.00 70.65  ?  216 LYS D CE  1 
ATOM   6506 N NZ  . LYS D 2 216 ? 9.117   4.607   87.697  1.00 68.89  ?  216 LYS D NZ  1 
ATOM   6507 N N   . VAL D 2 217 ? 9.074   6.913   82.754  1.00 54.46  ?  217 VAL D N   1 
ATOM   6508 C CA  . VAL D 2 217 ? 7.963   7.851   82.854  1.00 56.11  ?  217 VAL D CA  1 
ATOM   6509 C C   . VAL D 2 217 ? 7.276   7.617   84.191  1.00 53.65  ?  217 VAL D C   1 
ATOM   6510 O O   . VAL D 2 217 ? 6.761   6.524   84.452  1.00 62.04  ?  217 VAL D O   1 
ATOM   6511 C CB  . VAL D 2 217 ? 6.983   7.688   81.684  1.00 54.85  ?  217 VAL D CB  1 
ATOM   6512 C CG1 . VAL D 2 217 ? 5.956   8.806   81.701  1.00 51.35  ?  217 VAL D CG1 1 
ATOM   6513 C CG2 . VAL D 2 217 ? 7.749   7.674   80.365  1.00 51.94  ?  217 VAL D CG2 1 
ATOM   6514 N N   . GLU D 2 218 ? 7.268   8.639   85.035  1.00 59.30  ?  218 GLU D N   1 
ATOM   6515 C CA  . GLU D 2 218 ? 6.700   8.519   86.366  1.00 65.12  ?  218 GLU D CA  1 
ATOM   6516 C C   . GLU D 2 218 ? 5.449   9.378   86.498  1.00 65.35  ?  218 GLU D C   1 
ATOM   6517 O O   . GLU D 2 218 ? 5.422   10.511  86.003  1.00 67.12  ?  218 GLU D O   1 
ATOM   6518 C CB  . GLU D 2 218 ? 7.715   8.944   87.434  1.00 65.75  ?  218 GLU D CB  1 
ATOM   6519 C CG  . GLU D 2 218 ? 8.760   7.891   87.766  1.00 68.44  ?  218 GLU D CG  1 
ATOM   6520 C CD  . GLU D 2 218 ? 9.776   8.372   88.793  1.00 71.80  ?  218 GLU D CD  1 
ATOM   6521 O OE1 . GLU D 2 218 ? 10.039  9.595   88.860  1.00 71.77  ?  218 GLU D OE1 1 
ATOM   6522 O OE2 . GLU D 2 218 ? 10.306  7.521   89.539  1.00 67.93  ?  218 GLU D OE2 1 
ATOM   6523 N N   . PRO D 2 219 ? 4.406   8.871   87.159  1.00 67.52  ?  219 PRO D N   1 
ATOM   6524 C CA  . PRO D 2 219 ? 3.159   9.641   87.304  1.00 70.88  ?  219 PRO D CA  1 
ATOM   6525 C C   . PRO D 2 219 ? 3.358   10.812  88.254  1.00 73.04  ?  219 PRO D C   1 
ATOM   6526 O O   . PRO D 2 219 ? 3.714   10.625  89.419  1.00 75.14  ?  219 PRO D O   1 
ATOM   6527 C CB  . PRO D 2 219 ? 2.174   8.614   87.872  1.00 69.59  ?  219 PRO D CB  1 
ATOM   6528 C CG  . PRO D 2 219 ? 3.044   7.608   88.567  1.00 65.49  ?  219 PRO D CG  1 
ATOM   6529 C CD  . PRO D 2 219 ? 4.313   7.535   87.774  1.00 60.32  ?  219 PRO D CD  1 
ATOM   6530 N N   . LYS D 2 220 ? 3.141   12.023  87.750  1.00 75.37  ?  220 LYS D N   1 
ATOM   6531 C CA  . LYS D 2 220 ? 3.236   13.216  88.577  1.00 80.92  ?  220 LYS D CA  1 
ATOM   6532 C C   . LYS D 2 220 ? 1.859   13.649  89.063  1.00 85.70  ?  220 LYS D C   1 
ATOM   6533 O O   . LYS D 2 220 ? 0.876   13.598  88.318  1.00 86.64  ?  220 LYS D O   1 
ATOM   6534 C CB  . LYS D 2 220 ? 3.909   14.348  87.806  1.00 81.92  ?  220 LYS D CB  1 
ATOM   6535 C CG  . LYS D 2 220 ? 5.336   14.009  87.422  1.00 88.82  ?  220 LYS D CG  1 
ATOM   6536 C CD  . LYS D 2 220 ? 6.288   15.166  87.656  1.00 98.43  ?  220 LYS D CD  1 
ATOM   6537 C CE  . LYS D 2 220 ? 7.726   14.765  87.328  1.00 97.16  ?  220 LYS D CE  1 
ATOM   6538 N NZ  . LYS D 2 220 ? 8.718   15.821  87.672  1.00 91.76  ?  220 LYS D NZ  1 
ATOM   6539 N N   . SER D 2 221 ? 1.804   14.096  90.312  1.00 90.55  ?  221 SER D N   1 
ATOM   6540 C CA  . SER D 2 221 ? 0.548   14.511  90.912  1.00 90.57  ?  221 SER D CA  1 
ATOM   6541 C C   . SER D 2 221 ? 0.239   15.965  90.582  1.00 87.30  ?  221 SER D C   1 
ATOM   6542 O O   . SER D 2 221 ? -0.911  16.391  90.662  1.00 96.05  ?  221 SER D O   1 
ATOM   6543 C CB  . SER D 2 221 ? 0.583   14.303  92.428  1.00 90.10  ?  221 SER D CB  1 
ATOM   6544 O OG  . SER D 2 221 ? 0.149   12.995  92.760  1.00 85.94  ?  221 SER D OG  1 
ATOM   6545 N N   . GLU E 3 228 ? -11.817 58.664  57.199  1.00 91.54  ?  228 GLU E N   1 
ATOM   6546 C CA  . GLU E 3 228 ? -10.526 59.278  57.484  1.00 92.54  ?  228 GLU E CA  1 
ATOM   6547 C C   . GLU E 3 228 ? -10.060 58.895  58.896  1.00 90.91  ?  228 GLU E C   1 
ATOM   6548 O O   . GLU E 3 228 ? -9.804  59.755  59.739  1.00 90.14  ?  228 GLU E O   1 
ATOM   6549 C CB  . GLU E 3 228 ? -10.614 60.802  57.328  1.00 102.20 ?  228 GLU E CB  1 
ATOM   6550 C CG  . GLU E 3 228 ? -9.271  61.530  57.348  1.00 99.23  ?  228 GLU E CG  1 
ATOM   6551 C CD  . GLU E 3 228 ? -9.417  63.039  57.341  1.00 101.45 ?  228 GLU E CD  1 
ATOM   6552 O OE1 . GLU E 3 228 ? -10.501 63.531  56.952  1.00 100.38 ?  228 GLU E OE1 1 
ATOM   6553 O OE2 . GLU E 3 228 ? -8.451  63.728  57.736  1.00 95.09  ?  228 GLU E OE2 1 
ATOM   6554 N N   . LEU E 3 229 ? -9.979  57.589  59.151  1.00 90.00  ?  229 LEU E N   1 
ATOM   6555 C CA  . LEU E 3 229 ? -9.540  57.087  60.447  1.00 83.38  ?  229 LEU E CA  1 
ATOM   6556 C C   . LEU E 3 229 ? -8.042  57.296  60.648  1.00 85.83  ?  229 LEU E C   1 
ATOM   6557 O O   . LEU E 3 229 ? -7.293  57.517  59.692  1.00 87.37  ?  229 LEU E O   1 
ATOM   6558 C CB  . LEU E 3 229 ? -9.861  55.600  60.615  1.00 87.25  ?  229 LEU E CB  1 
ATOM   6559 C CG  . LEU E 3 229 ? -11.263 55.059  60.908  1.00 87.86  ?  229 LEU E CG  1 
ATOM   6560 C CD1 . LEU E 3 229 ? -12.301 55.773  60.100  1.00 89.54  ?  229 LEU E CD1 1 
ATOM   6561 C CD2 . LEU E 3 229 ? -11.328 53.552  60.662  1.00 85.90  ?  229 LEU E CD2 1 
ATOM   6562 N N   . PRO E 3 230 ? -7.589  57.256  61.903  1.00 85.88  ?  230 PRO E N   1 
ATOM   6563 C CA  . PRO E 3 230 ? -6.159  57.388  62.169  1.00 87.41  ?  230 PRO E CA  1 
ATOM   6564 C C   . PRO E 3 230 ? -5.401  56.151  61.714  1.00 85.01  ?  230 PRO E C   1 
ATOM   6565 O O   . PRO E 3 230 ? -5.957  55.039  61.686  1.00 79.62  ?  230 PRO E O   1 
ATOM   6566 C CB  . PRO E 3 230 ? -6.098  57.554  63.698  1.00 86.87  ?  230 PRO E CB  1 
ATOM   6567 C CG  . PRO E 3 230 ? -7.475  58.032  64.078  1.00 88.05  ?  230 PRO E CG  1 
ATOM   6568 C CD  . PRO E 3 230 ? -8.394  57.347  63.133  1.00 85.16  ?  230 PRO E CD  1 
ATOM   6569 N N   . PRO E 3 231 ? -4.125  56.293  61.368  1.00 81.49  ?  231 PRO E N   1 
ATOM   6570 C CA  . PRO E 3 231 ? -3.356  55.158  60.839  1.00 81.85  ?  231 PRO E CA  1 
ATOM   6571 C C   . PRO E 3 231 ? -2.846  54.254  61.946  1.00 76.54  ?  231 PRO E C   1 
ATOM   6572 O O   . PRO E 3 231 ? -2.582  54.718  63.065  1.00 75.82  ?  231 PRO E O   1 
ATOM   6573 C CB  . PRO E 3 231 ? -2.191  55.844  60.114  1.00 75.93  ?  231 PRO E CB  1 
ATOM   6574 C CG  . PRO E 3 231 ? -1.974  57.083  60.907  1.00 77.02  ?  231 PRO E CG  1 
ATOM   6575 C CD  . PRO E 3 231 ? -3.338  57.537  61.369  1.00 81.89  ?  231 PRO E CD  1 
ATOM   6576 N N   . PRO E 3 232 ? -2.702  52.954  61.671  1.00 78.22  ?  232 PRO E N   1 
ATOM   6577 C CA  . PRO E 3 232 ? -2.097  52.049  62.654  1.00 74.52  ?  232 PRO E CA  1 
ATOM   6578 C C   . PRO E 3 232 ? -0.643  52.415  62.905  1.00 74.45  ?  232 PRO E C   1 
ATOM   6579 O O   . PRO E 3 232 ? 0.005   53.094  62.105  1.00 77.25  ?  232 PRO E O   1 
ATOM   6580 C CB  . PRO E 3 232 ? -2.221  50.667  62.000  1.00 68.53  ?  232 PRO E CB  1 
ATOM   6581 C CG  . PRO E 3 232 ? -3.293  50.822  60.974  1.00 67.18  ?  232 PRO E CG  1 
ATOM   6582 C CD  . PRO E 3 232 ? -3.175  52.234  60.479  1.00 75.49  ?  232 PRO E CD  1 
ATOM   6583 N N   . GLU E 3 233 ? -0.122  51.942  64.032  1.00 75.64  ?  233 GLU E N   1 
ATOM   6584 C CA  . GLU E 3 233 ? 1.173   52.400  64.509  1.00 81.49  ?  233 GLU E CA  1 
ATOM   6585 C C   . GLU E 3 233 ? 1.963   51.253  65.137  1.00 77.56  ?  233 GLU E C   1 
ATOM   6586 O O   . GLU E 3 233 ? 1.415   50.199  65.472  1.00 74.92  ?  233 GLU E O   1 
ATOM   6587 C CB  . GLU E 3 233 ? 0.945   53.595  65.455  1.00 78.94  ?  233 GLU E CB  1 
ATOM   6588 C CG  . GLU E 3 233 ? -0.083  53.317  66.558  1.00 87.41  ?  233 GLU E CG  1 
ATOM   6589 C CD  . GLU E 3 233 ? -0.437  54.550  67.389  1.00 90.88  ?  233 GLU E CD  1 
ATOM   6590 O OE1 . GLU E 3 233 ? -1.365  54.452  68.226  1.00 88.55  ?  233 GLU E OE1 1 
ATOM   6591 O OE2 . GLU E 3 233 ? 0.187   55.617  67.192  1.00 85.93  ?  233 GLU E OE2 1 
ATOM   6592 N N   . ASN E 3 234 ? 3.275   51.482  65.279  1.00 75.47  ?  234 ASN E N   1 
ATOM   6593 C CA  . ASN E 3 234 ? 4.218   50.546  65.901  1.00 74.93  ?  234 ASN E CA  1 
ATOM   6594 C C   . ASN E 3 234 ? 4.252   49.209  65.156  1.00 74.77  ?  234 ASN E C   1 
ATOM   6595 O O   . ASN E 3 234 ? 4.002   48.139  65.716  1.00 74.18  ?  234 ASN E O   1 
ATOM   6596 C CB  . ASN E 3 234 ? 3.886   50.343  67.381  1.00 81.15  ?  234 ASN E CB  1 
ATOM   6597 C CG  . ASN E 3 234 ? 3.894   51.642  68.162  1.00 87.88  ?  234 ASN E CG  1 
ATOM   6598 O OD1 . ASN E 3 234 ? 4.544   52.614  67.771  1.00 83.96  ?  234 ASN E OD1 1 
ATOM   6599 N ND2 . ASN E 3 234 ? 3.165   51.666  69.271  1.00 91.24  ?  234 ASN E ND2 1 
ATOM   6600 N N   . ILE E 3 235 ? 4.594   49.291  63.875  1.00 74.54  ?  235 ILE E N   1 
ATOM   6601 C CA  . ILE E 3 235 ? 4.599   48.126  62.996  1.00 72.50  ?  235 ILE E CA  1 
ATOM   6602 C C   . ILE E 3 235 ? 5.894   47.348  63.194  1.00 73.03  ?  235 ILE E C   1 
ATOM   6603 O O   . ILE E 3 235 ? 6.989   47.917  63.102  1.00 71.29  ?  235 ILE E O   1 
ATOM   6604 C CB  . ILE E 3 235 ? 4.451   48.562  61.531  1.00 71.70  ?  235 ILE E CB  1 
ATOM   6605 C CG1 . ILE E 3 235 ? 3.248   49.491  61.365  1.00 72.74  ?  235 ILE E CG1 1 
ATOM   6606 C CG2 . ILE E 3 235 ? 4.232   47.351  60.657  1.00 70.52  ?  235 ILE E CG2 1 
ATOM   6607 C CD1 . ILE E 3 235 ? 1.924   48.804  61.485  1.00 71.21  ?  235 ILE E CD1 1 
ATOM   6608 N N   . GLU E 3 236 ? 5.779   46.042  63.456  1.00 69.35  ?  236 GLU E N   1 
ATOM   6609 C CA  . GLU E 3 236 ? 6.953   45.201  63.671  1.00 68.12  ?  236 GLU E CA  1 
ATOM   6610 C C   . GLU E 3 236 ? 6.759   43.821  63.058  1.00 71.17  ?  236 GLU E C   1 
ATOM   6611 O O   . GLU E 3 236 ? 5.655   43.273  63.082  1.00 74.78  ?  236 GLU E O   1 
ATOM   6612 C CB  . GLU E 3 236 ? 7.287   45.047  65.158  1.00 70.22  ?  236 GLU E CB  1 
ATOM   6613 C CG  . GLU E 3 236 ? 7.871   46.292  65.797  1.00 87.10  ?  236 GLU E CG  1 
ATOM   6614 C CD  . GLU E 3 236 ? 8.537   45.998  67.126  1.00 103.58 ?  236 GLU E CD  1 
ATOM   6615 O OE1 . GLU E 3 236 ? 8.098   45.048  67.811  1.00 106.59 ?  236 GLU E OE1 1 
ATOM   6616 O OE2 . GLU E 3 236 ? 9.498   46.714  67.486  1.00 103.93 ?  236 GLU E OE2 1 
ATOM   6617 N N   . VAL E 3 237 ? 7.833   43.271  62.486  1.00 65.37  ?  237 VAL E N   1 
ATOM   6618 C CA  . VAL E 3 237 ? 7.834   41.913  61.948  1.00 66.62  ?  237 VAL E CA  1 
ATOM   6619 C C   . VAL E 3 237 ? 8.689   41.034  62.844  1.00 64.58  ?  237 VAL E C   1 
ATOM   6620 O O   . VAL E 3 237 ? 9.711   41.478  63.377  1.00 64.14  ?  237 VAL E O   1 
ATOM   6621 C CB  . VAL E 3 237 ? 8.360   41.837  60.504  1.00 68.79  ?  237 VAL E CB  1 
ATOM   6622 C CG1 . VAL E 3 237 ? 7.843   40.573  59.826  1.00 66.35  ?  237 VAL E CG1 1 
ATOM   6623 C CG2 . VAL E 3 237 ? 7.968   43.049  59.739  1.00 68.96  ?  237 VAL E CG2 1 
ATOM   6624 N N   . SER E 3 238 ? 8.276   39.781  62.997  1.00 62.88  ?  238 SER E N   1 
ATOM   6625 C CA  . SER E 3 238 ? 9.053   38.796  63.729  1.00 67.01  ?  238 SER E CA  1 
ATOM   6626 C C   . SER E 3 238 ? 8.873   37.446  63.052  1.00 71.45  ?  238 SER E C   1 
ATOM   6627 O O   . SER E 3 238 ? 8.024   37.280  62.175  1.00 75.63  ?  238 SER E O   1 
ATOM   6628 C CB  . SER E 3 238 ? 8.633   38.736  65.200  1.00 69.01  ?  238 SER E CB  1 
ATOM   6629 O OG  . SER E 3 238 ? 7.277   38.342  65.318  1.00 78.34  ?  238 SER E OG  1 
ATOM   6630 N N   . VAL E 3 239 ? 9.684   36.473  63.455  1.00 68.55  ?  239 VAL E N   1 
ATOM   6631 C CA  . VAL E 3 239 ? 9.609   35.119  62.920  1.00 69.40  ?  239 VAL E CA  1 
ATOM   6632 C C   . VAL E 3 239 ? 9.168   34.186  64.038  1.00 72.17  ?  239 VAL E C   1 
ATOM   6633 O O   . VAL E 3 239 ? 9.683   34.267  65.159  1.00 74.68  ?  239 VAL E O   1 
ATOM   6634 C CB  . VAL E 3 239 ? 10.954  34.680  62.320  1.00 75.24  ?  239 VAL E CB  1 
ATOM   6635 C CG1 . VAL E 3 239 ? 10.885  33.237  61.829  1.00 73.52  ?  239 VAL E CG1 1 
ATOM   6636 C CG2 . VAL E 3 239 ? 11.363  35.621  61.187  1.00 71.22  ?  239 VAL E CG2 1 
ATOM   6637 N N   . GLN E 3 240 ? 8.218   33.300  63.734  1.00 76.34  ?  240 GLN E N   1 
ATOM   6638 C CA  . GLN E 3 240 ? 7.759   32.281  64.675  1.00 79.34  ?  240 GLN E CA  1 
ATOM   6639 C C   . GLN E 3 240 ? 7.534   30.991  63.898  1.00 75.85  ?  240 GLN E C   1 
ATOM   6640 O O   . GLN E 3 240 ? 6.603   30.901  63.088  1.00 77.01  ?  240 GLN E O   1 
ATOM   6641 C CB  . GLN E 3 240 ? 6.483   32.712  65.400  1.00 79.45  ?  240 GLN E CB  1 
ATOM   6642 C CG  . GLN E 3 240 ? 6.653   33.927  66.306  1.00 85.67  ?  240 GLN E CG  1 
ATOM   6643 C CD  . GLN E 3 240 ? 5.365   34.311  67.023  1.00 101.95 ?  240 GLN E CD  1 
ATOM   6644 O OE1 . GLN E 3 240 ? 4.308   33.715  66.791  1.00 103.88 ?  240 GLN E OE1 1 
ATOM   6645 N NE2 . GLN E 3 240 ? 5.442   35.329  67.877  1.00 100.23 ?  240 GLN E NE2 1 
ATOM   6646 N N   . ASN E 3 241 ? 8.387   30.003  64.153  1.00 74.28  ?  241 ASN E N   1 
ATOM   6647 C CA  . ASN E 3 241 ? 8.401   28.714  63.447  1.00 78.88  ?  241 ASN E CA  1 
ATOM   6648 C C   . ASN E 3 241 ? 8.531   28.994  61.952  1.00 75.83  ?  241 ASN E C   1 
ATOM   6649 O O   . ASN E 3 241 ? 9.436   29.745  61.552  1.00 78.55  ?  241 ASN E O   1 
ATOM   6650 C CB  . ASN E 3 241 ? 7.179   27.910  63.864  1.00 76.69  ?  241 ASN E CB  1 
ATOM   6651 C CG  . ASN E 3 241 ? 7.054   27.795  65.364  1.00 76.91  ?  241 ASN E CG  1 
ATOM   6652 O OD1 . ASN E 3 241 ? 6.225   28.467  65.979  1.00 77.85  ?  241 ASN E OD1 1 
ATOM   6653 N ND2 . ASN E 3 241 ? 7.907   26.974  65.969  1.00 71.31  ?  241 ASN E ND2 1 
ATOM   6654 N N   . GLN E 3 242 ? 7.656   28.454  61.104  1.00 72.07  ?  242 GLN E N   1 
ATOM   6655 C CA  . GLN E 3 242 ? 7.705   28.693  59.669  1.00 66.72  ?  242 GLN E CA  1 
ATOM   6656 C C   . GLN E 3 242 ? 6.818   29.849  59.254  1.00 66.71  ?  242 GLN E C   1 
ATOM   6657 O O   . GLN E 3 242 ? 6.344   29.883  58.111  1.00 64.75  ?  242 GLN E O   1 
ATOM   6658 C CB  . GLN E 3 242 ? 7.295   27.428  58.916  1.00 74.03  ?  242 GLN E CB  1 
ATOM   6659 C CG  . GLN E 3 242 ? 8.320   26.311  58.931  1.00 81.29  ?  242 GLN E CG  1 
ATOM   6660 C CD  . GLN E 3 242 ? 7.696   24.948  58.679  1.00 87.94  ?  242 GLN E CD  1 
ATOM   6661 O OE1 . GLN E 3 242 ? 6.492   24.759  58.874  1.00 81.50  ?  242 GLN E OE1 1 
ATOM   6662 N NE2 . GLN E 3 242 ? 8.512   23.991  58.240  1.00 89.59  ?  242 GLN E NE2 1 
ATOM   6663 N N   . ASN E 3 243 ? 6.577   30.798  60.155  1.00 66.57  ?  243 ASN E N   1 
ATOM   6664 C CA  . ASN E 3 243 ? 5.669   31.897  59.888  1.00 63.52  ?  243 ASN E CA  1 
ATOM   6665 C C   . ASN E 3 243 ? 6.327   33.234  60.189  1.00 68.51  ?  243 ASN E C   1 
ATOM   6666 O O   . ASN E 3 243 ? 7.231   33.333  61.022  1.00 67.19  ?  243 ASN E O   1 
ATOM   6667 C CB  . ASN E 3 243 ? 4.390   31.754  60.708  1.00 65.96  ?  243 ASN E CB  1 
ATOM   6668 C CG  . ASN E 3 243 ? 3.506   30.649  60.193  1.00 64.53  ?  243 ASN E CG  1 
ATOM   6669 O OD1 . ASN E 3 243 ? 2.737   30.845  59.258  1.00 66.04  ?  243 ASN E OD1 1 
ATOM   6670 N ND2 . ASN E 3 243 ? 3.621   29.471  60.792  1.00 69.97  ?  243 ASN E ND2 1 
ATOM   6671 N N   . TYR E 3 244 ? 5.864   34.258  59.480  1.00 68.35  ?  244 TYR E N   1 
ATOM   6672 C CA  . TYR E 3 244 ? 6.131   35.646  59.808  1.00 58.96  ?  244 TYR E CA  1 
ATOM   6673 C C   . TYR E 3 244 ? 4.945   36.166  60.605  1.00 66.82  ?  244 TYR E C   1 
ATOM   6674 O O   . TYR E 3 244 ? 3.790   35.815  60.324  1.00 69.74  ?  244 TYR E O   1 
ATOM   6675 C CB  . TYR E 3 244 ? 6.327   36.491  58.547  1.00 57.84  ?  244 TYR E CB  1 
ATOM   6676 C CG  . TYR E 3 244 ? 7.596   36.209  57.771  1.00 63.77  ?  244 TYR E CG  1 
ATOM   6677 C CD1 . TYR E 3 244 ? 7.570   36.096  56.384  1.00 63.92  ?  244 TYR E CD1 1 
ATOM   6678 C CD2 . TYR E 3 244 ? 8.818   36.064  58.415  1.00 65.97  ?  244 TYR E CD2 1 
ATOM   6679 C CE1 . TYR E 3 244 ? 8.722   35.838  55.660  1.00 60.89  ?  244 TYR E CE1 1 
ATOM   6680 C CE2 . TYR E 3 244 ? 9.979   35.806  57.696  1.00 63.57  ?  244 TYR E CE2 1 
ATOM   6681 C CZ  . TYR E 3 244 ? 9.922   35.697  56.321  1.00 60.53  ?  244 TYR E CZ  1 
ATOM   6682 O OH  . TYR E 3 244 ? 11.064  35.442  55.601  1.00 63.96  ?  244 TYR E OH  1 
ATOM   6683 N N   . VAL E 3 245 ? 5.234   36.991  61.605  1.00 65.77  ?  245 VAL E N   1 
ATOM   6684 C CA  . VAL E 3 245 ? 4.219   37.576  62.469  1.00 69.66  ?  245 VAL E CA  1 
ATOM   6685 C C   . VAL E 3 245 ? 4.360   39.089  62.405  1.00 67.17  ?  245 VAL E C   1 
ATOM   6686 O O   . VAL E 3 245 ? 5.386   39.644  62.818  1.00 73.48  ?  245 VAL E O   1 
ATOM   6687 C CB  . VAL E 3 245 ? 4.334   37.068  63.913  1.00 72.90  ?  245 VAL E CB  1 
ATOM   6688 C CG1 . VAL E 3 245 ? 3.400   37.849  64.819  1.00 75.57  ?  245 VAL E CG1 1 
ATOM   6689 C CG2 . VAL E 3 245 ? 4.021   35.578  63.971  1.00 67.91  ?  245 VAL E CG2 1 
ATOM   6690 N N   . LEU E 3 246 ? 3.335   39.747  61.886  1.00 61.33  ?  246 LEU E N   1 
ATOM   6691 C CA  . LEU E 3 246 ? 3.300   41.191  61.742  1.00 66.74  ?  246 LEU E CA  1 
ATOM   6692 C C   . LEU E 3 246 ? 2.372   41.750  62.810  1.00 71.46  ?  246 LEU E C   1 
ATOM   6693 O O   . LEU E 3 246 ? 1.179   41.423  62.835  1.00 73.60  ?  246 LEU E O   1 
ATOM   6694 C CB  . LEU E 3 246 ? 2.818   41.587  60.350  1.00 67.49  ?  246 LEU E CB  1 
ATOM   6695 C CG  . LEU E 3 246 ? 2.754   43.091  60.117  1.00 65.44  ?  246 LEU E CG  1 
ATOM   6696 C CD1 . LEU E 3 246 ? 4.153   43.685  60.170  1.00 64.91  ?  246 LEU E CD1 1 
ATOM   6697 C CD2 . LEU E 3 246 ? 2.074   43.386  58.799  1.00 62.90  ?  246 LEU E CD2 1 
ATOM   6698 N N   . LYS E 3 247 ? 2.926   42.561  63.704  1.00 69.26  ?  247 LYS E N   1 
ATOM   6699 C CA  . LYS E 3 247 ? 2.192   43.126  64.823  1.00 67.32  ?  247 LYS E CA  1 
ATOM   6700 C C   . LYS E 3 247 ? 2.111   44.638  64.678  1.00 72.97  ?  247 LYS E C   1 
ATOM   6701 O O   . LYS E 3 247 ? 3.051   45.283  64.196  1.00 74.85  ?  247 LYS E O   1 
ATOM   6702 C CB  . LYS E 3 247 ? 2.858   42.771  66.156  1.00 69.02  ?  247 LYS E CB  1 
ATOM   6703 C CG  . LYS E 3 247 ? 2.928   41.278  66.446  1.00 77.29  ?  247 LYS E CG  1 
ATOM   6704 C CD  . LYS E 3 247 ? 3.512   41.008  67.829  1.00 80.22  ?  247 LYS E CD  1 
ATOM   6705 C CE  . LYS E 3 247 ? 3.686   39.517  68.082  1.00 80.67  ?  247 LYS E CE  1 
ATOM   6706 N NZ  . LYS E 3 247 ? 4.102   39.219  69.482  1.00 83.06  ?  247 LYS E NZ  1 
ATOM   6707 N N   . TRP E 3 248 ? 0.977   45.196  65.094  1.00 72.85  ?  248 TRP E N   1 
ATOM   6708 C CA  . TRP E 3 248 ? 0.771   46.633  65.143  1.00 74.87  ?  248 TRP E CA  1 
ATOM   6709 C C   . TRP E 3 248 ? -0.058  46.951  66.378  1.00 77.90  ?  248 TRP E C   1 
ATOM   6710 O O   . TRP E 3 248 ? -0.507  46.054  67.101  1.00 74.48  ?  248 TRP E O   1 
ATOM   6711 C CB  . TRP E 3 248 ? 0.094   47.148  63.868  1.00 75.45  ?  248 TRP E CB  1 
ATOM   6712 C CG  . TRP E 3 248 ? -1.210  46.486  63.562  1.00 73.30  ?  248 TRP E CG  1 
ATOM   6713 C CD1 . TRP E 3 248 ? -2.456  46.921  63.915  1.00 71.89  ?  248 TRP E CD1 1 
ATOM   6714 C CD2 . TRP E 3 248 ? -1.403  45.272  62.825  1.00 73.69  ?  248 TRP E CD2 1 
ATOM   6715 N NE1 . TRP E 3 248 ? -3.411  46.046  63.453  1.00 70.45  ?  248 TRP E NE1 1 
ATOM   6716 C CE2 . TRP E 3 248 ? -2.791  45.027  62.778  1.00 71.52  ?  248 TRP E CE2 1 
ATOM   6717 C CE3 . TRP E 3 248 ? -0.537  44.367  62.202  1.00 73.29  ?  248 TRP E CE3 1 
ATOM   6718 C CZ2 . TRP E 3 248 ? -3.332  43.915  62.133  1.00 70.97  ?  248 TRP E CZ2 1 
ATOM   6719 C CZ3 . TRP E 3 248 ? -1.080  43.259  61.561  1.00 73.14  ?  248 TRP E CZ3 1 
ATOM   6720 C CH2 . TRP E 3 248 ? -2.462  43.046  61.533  1.00 67.96  ?  248 TRP E CH2 1 
ATOM   6721 N N   . ASP E 3 249 ? -0.255  48.241  66.629  1.00 81.05  ?  249 ASP E N   1 
ATOM   6722 C CA  . ASP E 3 249 ? -1.063  48.700  67.747  1.00 83.66  ?  249 ASP E CA  1 
ATOM   6723 C C   . ASP E 3 249 ? -2.151  49.623  67.225  1.00 81.60  ?  249 ASP E C   1 
ATOM   6724 O O   . ASP E 3 249 ? -1.871  50.523  66.422  1.00 74.21  ?  249 ASP E O   1 
ATOM   6725 C CB  . ASP E 3 249 ? -0.201  49.432  68.778  1.00 85.06  ?  249 ASP E CB  1 
ATOM   6726 C CG  . ASP E 3 249 ? 0.850   48.534  69.407  1.00 88.28  ?  249 ASP E CG  1 
ATOM   6727 O OD1 . ASP E 3 249 ? 0.587   47.323  69.584  1.00 88.68  ?  249 ASP E OD1 1 
ATOM   6728 O OD2 . ASP E 3 249 ? 1.948   49.042  69.719  1.00 88.31  ?  249 ASP E OD2 1 
ATOM   6729 N N   . TYR E 3 250 ? -3.383  49.406  67.684  1.00 88.48  ?  250 TYR E N   1 
ATOM   6730 C CA  . TYR E 3 250 ? -4.475  50.307  67.358  1.00 90.46  ?  250 TYR E CA  1 
ATOM   6731 C C   . TYR E 3 250 ? -5.288  50.563  68.619  1.00 96.65  ?  250 TYR E C   1 
ATOM   6732 O O   . TYR E 3 250 ? -5.607  49.632  69.369  1.00 90.25  ?  250 TYR E O   1 
ATOM   6733 C CB  . TYR E 3 250 ? -5.376  49.731  66.257  1.00 81.40  ?  250 TYR E CB  1 
ATOM   6734 C CG  . TYR E 3 250 ? -5.981  50.792  65.362  1.00 83.65  ?  250 TYR E CG  1 
ATOM   6735 C CD1 . TYR E 3 250 ? -7.355  50.915  65.219  1.00 84.86  ?  250 TYR E CD1 1 
ATOM   6736 C CD2 . TYR E 3 250 ? -5.171  51.694  64.684  1.00 79.68  ?  250 TYR E CD2 1 
ATOM   6737 C CE1 . TYR E 3 250 ? -7.903  51.893  64.409  1.00 82.63  ?  250 TYR E CE1 1 
ATOM   6738 C CE2 . TYR E 3 250 ? -5.709  52.672  63.874  1.00 78.78  ?  250 TYR E CE2 1 
ATOM   6739 C CZ  . TYR E 3 250 ? -7.075  52.769  63.740  1.00 78.92  ?  250 TYR E CZ  1 
ATOM   6740 O OH  . TYR E 3 250 ? -7.611  53.747  62.933  1.00 78.97  ?  250 TYR E OH  1 
ATOM   6741 N N   . THR E 3 251 ? -5.644  51.831  68.825  1.00 99.13  ?  251 THR E N   1 
ATOM   6742 C CA  . THR E 3 251 ? -6.332  52.261  70.035  1.00 102.24 ?  251 THR E CA  1 
ATOM   6743 C C   . THR E 3 251 ? -7.852  52.169  69.928  1.00 103.19 ?  251 THR E C   1 
ATOM   6744 O O   . THR E 3 251 ? -8.517  51.913  70.937  1.00 103.15 ?  251 THR E O   1 
ATOM   6745 C CB  . THR E 3 251 ? -5.901  53.692  70.393  1.00 99.93  ?  251 THR E CB  1 
ATOM   6746 O OG1 . THR E 3 251 ? -6.261  54.589  69.335  1.00 104.33 ?  251 THR E OG1 1 
ATOM   6747 C CG2 . THR E 3 251 ? -4.391  53.759  70.608  1.00 92.19  ?  251 THR E CG2 1 
ATOM   6748 N N   . TYR E 3 252 ? -8.425  52.332  68.736  1.00 98.75  ?  252 TYR E N   1 
ATOM   6749 C CA  . TYR E 3 252 ? -9.876  52.318  68.615  1.00 93.61  ?  252 TYR E CA  1 
ATOM   6750 C C   . TYR E 3 252 ? -10.332 50.866  68.546  1.00 92.64  ?  252 TYR E C   1 
ATOM   6751 O O   . TYR E 3 252 ? -9.827  50.084  67.732  1.00 98.29  ?  252 TYR E O   1 
ATOM   6752 C CB  . TYR E 3 252 ? -10.357 53.070  67.369  1.00 89.56  ?  252 TYR E CB  1 
ATOM   6753 C CG  . TYR E 3 252 ? -10.035 54.558  67.266  1.00 92.30  ?  252 TYR E CG  1 
ATOM   6754 C CD1 . TYR E 3 252 ? -9.025  55.145  68.020  1.00 93.69  ?  252 TYR E CD1 1 
ATOM   6755 C CD2 . TYR E 3 252 ? -10.756 55.375  66.395  1.00 89.50  ?  252 TYR E CD2 1 
ATOM   6756 C CE1 . TYR E 3 252 ? -8.738  56.506  67.908  1.00 100.93 ?  252 TYR E CE1 1 
ATOM   6757 C CE2 . TYR E 3 252 ? -10.482 56.733  66.276  1.00 91.32  ?  252 TYR E CE2 1 
ATOM   6758 C CZ  . TYR E 3 252 ? -9.472  57.293  67.032  1.00 98.81  ?  252 TYR E CZ  1 
ATOM   6759 O OH  . TYR E 3 252 ? -9.199  58.642  66.909  1.00 88.39  ?  252 TYR E OH  1 
ATOM   6760 N N   . ALA E 3 253 ? -11.290 50.505  69.391  1.00 87.90  ?  253 ALA E N   1 
ATOM   6761 C CA  . ALA E 3 253 ? -11.785 49.138  69.398  1.00 92.79  ?  253 ALA E CA  1 
ATOM   6762 C C   . ALA E 3 253 ? -12.735 48.892  68.229  1.00 91.92  ?  253 ALA E C   1 
ATOM   6763 O O   . ALA E 3 253 ? -13.122 49.808  67.503  1.00 94.98  ?  253 ALA E O   1 
ATOM   6764 C CB  . ALA E 3 253 ? -12.475 48.833  70.726  1.00 95.74  ?  253 ALA E CB  1 
ATOM   6765 N N   . ASN E 3 254 ? -13.107 47.623  68.063  1.00 91.07  ?  254 ASN E N   1 
ATOM   6766 C CA  . ASN E 3 254 ? -14.033 47.167  67.022  1.00 92.73  ?  254 ASN E CA  1 
ATOM   6767 C C   . ASN E 3 254 ? -13.577 47.621  65.632  1.00 90.08  ?  254 ASN E C   1 
ATOM   6768 O O   . ASN E 3 254 ? -14.285 48.332  64.915  1.00 95.63  ?  254 ASN E O   1 
ATOM   6769 C CB  . ASN E 3 254 ? -15.466 47.639  67.309  1.00 95.85  ?  254 ASN E CB  1 
ATOM   6770 C CG  . ASN E 3 254 ? -16.183 46.772  68.346  1.00 97.40  ?  254 ASN E CG  1 
ATOM   6771 O OD1 . ASN E 3 254 ? -15.572 45.920  68.992  1.00 97.21  ?  254 ASN E OD1 1 
ATOM   6772 N ND2 . ASN E 3 254 ? -17.482 46.992  68.508  1.00 94.90  ?  254 ASN E ND2 1 
ATOM   6773 N N   . MET E 3 255 ? -12.381 47.185  65.246  1.00 86.69  ?  255 MET E N   1 
ATOM   6774 C CA  . MET E 3 255 ? -11.839 47.522  63.940  1.00 84.48  ?  255 MET E CA  1 
ATOM   6775 C C   . MET E 3 255 ? -11.409 46.261  63.201  1.00 81.03  ?  255 MET E C   1 
ATOM   6776 O O   . MET E 3 255 ? -11.155 45.210  63.800  1.00 80.48  ?  255 MET E O   1 
ATOM   6777 C CB  . MET E 3 255 ? -10.651 48.486  64.065  1.00 81.83  ?  255 MET E CB  1 
ATOM   6778 C CG  . MET E 3 255 ? -11.032 49.889  64.517  1.00 86.56  ?  255 MET E CG  1 
ATOM   6779 S SD  . MET E 3 255 ? -11.724 50.902  63.192  1.00 94.13  ?  255 MET E SD  1 
ATOM   6780 C CE  . MET E 3 255 ? -12.163 52.399  64.077  1.00 90.65  ?  255 MET E CE  1 
ATOM   6781 N N   . THR E 3 256 ? -11.327 46.381  61.880  1.00 78.85  ?  256 THR E N   1 
ATOM   6782 C CA  . THR E 3 256 ? -10.740 45.353  61.038  1.00 78.81  ?  256 THR E CA  1 
ATOM   6783 C C   . THR E 3 256 ? -9.504  45.918  60.354  1.00 75.74  ?  256 THR E C   1 
ATOM   6784 O O   . THR E 3 256 ? -9.353  47.133  60.202  1.00 70.22  ?  256 THR E O   1 
ATOM   6785 C CB  . THR E 3 256 ? -11.737 44.839  59.999  1.00 78.01  ?  256 THR E CB  1 
ATOM   6786 O OG1 . THR E 3 256 ? -12.040 45.883  59.065  1.00 79.23  ?  256 THR E OG1 1 
ATOM   6787 C CG2 . THR E 3 256 ? -13.015 44.380  60.678  1.00 83.56  ?  256 THR E CG2 1 
ATOM   6788 N N   . PHE E 3 257 ? -8.613  45.023  59.944  1.00 77.22  ?  257 PHE E N   1 
ATOM   6789 C CA  . PHE E 3 257 ? -7.346  45.435  59.367  1.00 71.74  ?  257 PHE E CA  1 
ATOM   6790 C C   . PHE E 3 257 ? -7.076  44.675  58.077  1.00 66.65  ?  257 PHE E C   1 
ATOM   6791 O O   . PHE E 3 257 ? -7.514  43.536  57.895  1.00 70.00  ?  257 PHE E O   1 
ATOM   6792 C CB  . PHE E 3 257 ? -6.198  45.213  60.351  1.00 69.30  ?  257 PHE E CB  1 
ATOM   6793 C CG  . PHE E 3 257 ? -6.372  45.942  61.649  1.00 70.50  ?  257 PHE E CG  1 
ATOM   6794 C CD1 . PHE E 3 257 ? -6.001  47.268  61.771  1.00 74.01  ?  257 PHE E CD1 1 
ATOM   6795 C CD2 . PHE E 3 257 ? -6.912  45.300  62.750  1.00 72.72  ?  257 PHE E CD2 1 
ATOM   6796 C CE1 . PHE E 3 257 ? -6.160  47.939  62.969  1.00 76.23  ?  257 PHE E CE1 1 
ATOM   6797 C CE2 . PHE E 3 257 ? -7.071  45.964  63.948  1.00 70.14  ?  257 PHE E CE2 1 
ATOM   6798 C CZ  . PHE E 3 257 ? -6.696  47.285  64.057  1.00 70.77  ?  257 PHE E CZ  1 
ATOM   6799 N N   . GLN E 3 258 ? -6.344  45.334  57.184  1.00 62.37  ?  258 GLN E N   1 
ATOM   6800 C CA  . GLN E 3 258 ? -5.894  44.760  55.925  1.00 65.62  ?  258 GLN E CA  1 
ATOM   6801 C C   . GLN E 3 258 ? -4.387  44.948  55.821  1.00 62.66  ?  258 GLN E C   1 
ATOM   6802 O O   . GLN E 3 258 ? -3.886  46.063  55.998  1.00 63.47  ?  258 GLN E O   1 
ATOM   6803 C CB  . GLN E 3 258 ? -6.600  45.417  54.735  1.00 60.74  ?  258 GLN E CB  1 
ATOM   6804 C CG  . GLN E 3 258 ? -6.105  44.948  53.381  1.00 62.92  ?  258 GLN E CG  1 
ATOM   6805 C CD  . GLN E 3 258 ? -6.539  45.868  52.258  1.00 65.32  ?  258 GLN E CD  1 
ATOM   6806 O OE1 . GLN E 3 258 ? -6.694  47.073  52.454  1.00 67.15  ?  258 GLN E OE1 1 
ATOM   6807 N NE2 . GLN E 3 258 ? -6.738  45.304  51.072  1.00 67.12  ?  258 GLN E NE2 1 
ATOM   6808 N N   . VAL E 3 259 ? -3.670  43.865  55.532  1.00 60.23  ?  259 VAL E N   1 
ATOM   6809 C CA  . VAL E 3 259 ? -2.215  43.883  55.421  1.00 63.30  ?  259 VAL E CA  1 
ATOM   6810 C C   . VAL E 3 259 ? -1.827  43.753  53.956  1.00 57.50  ?  259 VAL E C   1 
ATOM   6811 O O   . VAL E 3 259 ? -2.302  42.851  53.254  1.00 58.21  ?  259 VAL E O   1 
ATOM   6812 C CB  . VAL E 3 259 ? -1.568  42.762  56.249  1.00 59.60  ?  259 VAL E CB  1 
ATOM   6813 C CG1 . VAL E 3 259 ? -0.067  42.820  56.102  1.00 55.26  ?  259 VAL E CG1 1 
ATOM   6814 C CG2 . VAL E 3 259 ? -1.961  42.886  57.707  1.00 63.84  ?  259 VAL E CG2 1 
ATOM   6815 N N   . GLN E 3 260 ? -0.948  44.638  53.503  1.00 53.26  ?  260 GLN E N   1 
ATOM   6816 C CA  . GLN E 3 260 ? -0.474  44.647  52.133  1.00 57.95  ?  260 GLN E CA  1 
ATOM   6817 C C   . GLN E 3 260 ? 1.046   44.566  52.103  1.00 58.56  ?  260 GLN E C   1 
ATOM   6818 O O   . GLN E 3 260 ? 1.730   44.947  53.058  1.00 60.09  ?  260 GLN E O   1 
ATOM   6819 C CB  . GLN E 3 260 ? -0.946  45.905  51.393  1.00 56.99  ?  260 GLN E CB  1 
ATOM   6820 C CG  . GLN E 3 260 ? -2.408  45.859  51.000  1.00 59.16  ?  260 GLN E CG  1 
ATOM   6821 C CD  . GLN E 3 260 ? -2.855  47.102  50.253  1.00 61.32  ?  260 GLN E CD  1 
ATOM   6822 O OE1 . GLN E 3 260 ? -2.067  48.025  50.024  1.00 55.27  ?  260 GLN E OE1 1 
ATOM   6823 N NE2 . GLN E 3 260 ? -4.131  47.138  49.877  1.00 56.33  ?  260 GLN E NE2 1 
ATOM   6824 N N   . TRP E 3 261 ? 1.563   44.096  50.967  1.00 55.91  ?  261 TRP E N   1 
ATOM   6825 C CA  . TRP E 3 261 ? 2.995   43.967  50.751  1.00 53.22  ?  261 TRP E CA  1 
ATOM   6826 C C   . TRP E 3 261 ? 3.343   44.485  49.363  1.00 49.56  ?  261 TRP E C   1 
ATOM   6827 O O   . TRP E 3 261 ? 2.475   44.661  48.503  1.00 51.33  ?  261 TRP E O   1 
ATOM   6828 C CB  . TRP E 3 261 ? 3.466   42.515  50.920  1.00 46.09  ?  261 TRP E CB  1 
ATOM   6829 C CG  . TRP E 3 261 ? 2.919   41.555  49.908  1.00 47.81  ?  261 TRP E CG  1 
ATOM   6830 C CD1 . TRP E 3 261 ? 1.725   40.900  49.965  1.00 52.72  ?  261 TRP E CD1 1 
ATOM   6831 C CD2 . TRP E 3 261 ? 3.562   41.110  48.711  1.00 47.34  ?  261 TRP E CD2 1 
ATOM   6832 N NE1 . TRP E 3 261 ? 1.573   40.091  48.867  1.00 48.33  ?  261 TRP E NE1 1 
ATOM   6833 C CE2 . TRP E 3 261 ? 2.690   40.200  48.082  1.00 50.67  ?  261 TRP E CE2 1 
ATOM   6834 C CE3 . TRP E 3 261 ? 4.786   41.397  48.106  1.00 47.20  ?  261 TRP E CE3 1 
ATOM   6835 C CZ2 . TRP E 3 261 ? 3.005   39.574  46.876  1.00 47.16  ?  261 TRP E CZ2 1 
ATOM   6836 C CZ3 . TRP E 3 261 ? 5.096   40.774  46.908  1.00 47.45  ?  261 TRP E CZ3 1 
ATOM   6837 C CH2 . TRP E 3 261 ? 4.210   39.873  46.307  1.00 44.93  ?  261 TRP E CH2 1 
ATOM   6838 N N   . LEU E 3 262 ? 4.633   44.740  49.164  1.00 47.94  ?  262 LEU E N   1 
ATOM   6839 C CA  . LEU E 3 262 ? 5.139   45.228  47.887  1.00 53.31  ?  262 LEU E CA  1 
ATOM   6840 C C   . LEU E 3 262 ? 6.593   44.808  47.726  1.00 49.14  ?  262 LEU E C   1 
ATOM   6841 O O   . LEU E 3 262 ? 7.319   44.669  48.709  1.00 52.14  ?  262 LEU E O   1 
ATOM   6842 C CB  . LEU E 3 262 ? 5.027   46.759  47.776  1.00 52.73  ?  262 LEU E CB  1 
ATOM   6843 C CG  . LEU E 3 262 ? 5.299   47.364  46.395  1.00 50.28  ?  262 LEU E CG  1 
ATOM   6844 C CD1 . LEU E 3 262 ? 4.123   47.094  45.469  1.00 51.95  ?  262 LEU E CD1 1 
ATOM   6845 C CD2 . LEU E 3 262 ? 5.584   48.845  46.472  1.00 49.53  ?  262 LEU E CD2 1 
ATOM   6846 N N   . HIS E 3 263 ? 7.008   44.586  46.481  1.00 52.09  ?  263 HIS E N   1 
ATOM   6847 C CA  . HIS E 3 263 ? 8.428   44.423  46.192  1.00 57.00  ?  263 HIS E CA  1 
ATOM   6848 C C   . HIS E 3 263 ? 9.151   45.741  46.434  1.00 51.03  ?  263 HIS E C   1 
ATOM   6849 O O   . HIS E 3 263 ? 8.714   46.789  45.956  1.00 53.14  ?  263 HIS E O   1 
ATOM   6850 C CB  . HIS E 3 263 ? 8.643   43.985  44.748  1.00 59.13  ?  263 HIS E CB  1 
ATOM   6851 C CG  . HIS E 3 263 ? 7.975   42.696  44.400  1.00 50.34  ?  263 HIS E CG  1 
ATOM   6852 N ND1 . HIS E 3 263 ? 6.639   42.618  44.071  1.00 53.51  ?  263 HIS E ND1 1 
ATOM   6853 C CD2 . HIS E 3 263 ? 8.457   41.434  44.326  1.00 46.33  ?  263 HIS E CD2 1 
ATOM   6854 C CE1 . HIS E 3 263 ? 6.327   41.361  43.808  1.00 51.05  ?  263 HIS E CE1 1 
ATOM   6855 N NE2 . HIS E 3 263 ? 7.413   40.623  43.954  1.00 45.97  ?  263 HIS E NE2 1 
ATOM   6856 N N   . ALA E 3 264 ? 10.260  45.693  47.172  1.00 50.85  ?  264 ALA E N   1 
ATOM   6857 C CA  . ALA E 3 264 ? 10.955  46.930  47.519  1.00 57.66  ?  264 ALA E CA  1 
ATOM   6858 C C   . ALA E 3 264 ? 11.440  47.671  46.278  1.00 55.06  ?  264 ALA E C   1 
ATOM   6859 O O   . ALA E 3 264 ? 11.332  48.898  46.201  1.00 59.17  ?  264 ALA E O   1 
ATOM   6860 C CB  . ALA E 3 264 ? 12.123  46.638  48.460  1.00 54.92  ?  264 ALA E CB  1 
ATOM   6861 N N   . PHE E 3 265 ? 11.963  46.945  45.288  1.00 56.05  ?  265 PHE E N   1 
ATOM   6862 C CA  . PHE E 3 265 ? 12.524  47.592  44.107  1.00 54.55  ?  265 PHE E CA  1 
ATOM   6863 C C   . PHE E 3 265 ? 11.489  48.343  43.279  1.00 58.88  ?  265 PHE E C   1 
ATOM   6864 O O   . PHE E 3 265 ? 11.873  49.070  42.358  1.00 64.41  ?  265 PHE E O   1 
ATOM   6865 C CB  . PHE E 3 265 ? 13.245  46.560  43.228  1.00 51.42  ?  265 PHE E CB  1 
ATOM   6866 C CG  . PHE E 3 265 ? 12.331  45.561  42.571  1.00 55.39  ?  265 PHE E CG  1 
ATOM   6867 C CD1 . PHE E 3 265 ? 11.803  45.803  41.313  1.00 53.06  ?  265 PHE E CD1 1 
ATOM   6868 C CD2 . PHE E 3 265 ? 12.023  44.364  43.202  1.00 59.13  ?  265 PHE E CD2 1 
ATOM   6869 C CE1 . PHE E 3 265 ? 10.967  44.882  40.707  1.00 51.03  ?  265 PHE E CE1 1 
ATOM   6870 C CE2 . PHE E 3 265 ? 11.195  43.436  42.598  1.00 53.72  ?  265 PHE E CE2 1 
ATOM   6871 C CZ  . PHE E 3 265 ? 10.664  43.696  41.350  1.00 53.54  ?  265 PHE E CZ  1 
ATOM   6872 N N   . LEU E 3 266 ? 10.199  48.185  43.566  1.00 59.99  ?  266 LEU E N   1 
ATOM   6873 C CA  . LEU E 3 266 ? 9.174   48.851  42.775  1.00 61.63  ?  266 LEU E CA  1 
ATOM   6874 C C   . LEU E 3 266 ? 9.050   50.339  43.088  1.00 69.56  ?  266 LEU E C   1 
ATOM   6875 O O   . LEU E 3 266 ? 8.433   51.069  42.304  1.00 71.21  ?  266 LEU E O   1 
ATOM   6876 C CB  . LEU E 3 266 ? 7.830   48.147  42.979  1.00 55.30  ?  266 LEU E CB  1 
ATOM   6877 C CG  . LEU E 3 266 ? 7.752   46.758  42.336  1.00 56.28  ?  266 LEU E CG  1 
ATOM   6878 C CD1 . LEU E 3 266 ? 6.410   46.082  42.585  1.00 49.37  ?  266 LEU E CD1 1 
ATOM   6879 C CD2 . LEU E 3 266 ? 8.035   46.844  40.851  1.00 54.19  ?  266 LEU E CD2 1 
ATOM   6880 N N   . LYS E 3 267 ? 9.640   50.811  44.190  1.00 69.37  ?  267 LYS E N   1 
ATOM   6881 C CA  . LYS E 3 267 ? 9.551   52.223  44.551  1.00 71.19  ?  267 LYS E CA  1 
ATOM   6882 C C   . LYS E 3 267 ? 10.499  53.112  43.754  1.00 80.34  ?  267 LYS E C   1 
ATOM   6883 O O   . LYS E 3 267 ? 10.293  54.331  43.715  1.00 85.46  ?  267 LYS E O   1 
ATOM   6884 C CB  . LYS E 3 267 ? 9.836   52.398  46.045  1.00 67.40  ?  267 LYS E CB  1 
ATOM   6885 C CG  . LYS E 3 267 ? 8.802   51.763  46.956  1.00 72.36  ?  267 LYS E CG  1 
ATOM   6886 C CD  . LYS E 3 267 ? 7.514   52.563  47.009  1.00 64.59  ?  267 LYS E CD  1 
ATOM   6887 C CE  . LYS E 3 267 ? 7.365   53.234  48.371  1.00 64.84  ?  267 LYS E CE  1 
ATOM   6888 N NZ  . LYS E 3 267 ? 6.001   53.792  48.596  1.00 65.43  ?  267 LYS E NZ  1 
ATOM   6889 N N   . ARG E 3 268 ? 11.523  52.541  43.117  1.00 86.33  ?  268 ARG E N   1 
ATOM   6890 C CA  . ARG E 3 268 ? 12.495  53.318  42.354  1.00 85.84  ?  268 ARG E CA  1 
ATOM   6891 C C   . ARG E 3 268 ? 12.556  52.924  40.886  1.00 85.78  ?  268 ARG E C   1 
ATOM   6892 O O   . ARG E 3 268 ? 12.550  53.805  40.019  1.00 93.03  ?  268 ARG E O   1 
ATOM   6893 C CB  . ARG E 3 268 ? 13.892  53.190  42.985  1.00 75.43  ?  268 ARG E CB  1 
ATOM   6894 C CG  . ARG E 3 268 ? 14.027  53.828  44.362  1.00 79.84  ?  268 ARG E CG  1 
ATOM   6895 C CD  . ARG E 3 268 ? 13.684  55.319  44.336  1.00 93.21  ?  268 ARG E CD  1 
ATOM   6896 N NE  . ARG E 3 268 ? 14.777  56.132  43.803  1.00 97.01  ?  268 ARG E NE  1 
ATOM   6897 C CZ  . ARG E 3 268 ? 14.609  57.297  43.183  1.00 91.23  ?  268 ARG E CZ  1 
ATOM   6898 N NH1 . ARG E 3 268 ? 13.388  57.791  43.014  1.00 90.14  ?  268 ARG E NH1 1 
ATOM   6899 N NH2 . ARG E 3 268 ? 15.660  57.965  42.724  1.00 71.89  ?  268 ARG E NH2 1 
ATOM   6900 N N   . ASN E 3 269 ? 12.622  51.614  40.575  1.00 86.55  ?  269 ASN E N   1 
ATOM   6901 C CA  . ASN E 3 269 ? 12.751  51.205  39.171  1.00 90.83  ?  269 ASN E CA  1 
ATOM   6902 C C   . ASN E 3 269 ? 11.532  51.589  38.340  1.00 96.70  ?  269 ASN E C   1 
ATOM   6903 O O   . ASN E 3 269 ? 11.689  52.338  37.357  1.00 98.92  ?  269 ASN E O   1 
ATOM   6904 C CB  . ASN E 3 269 ? 13.086  49.712  39.088  1.00 84.93  ?  269 ASN E CB  1 
ATOM   6905 C CG  . ASN E 3 269 ? 14.570  49.454  38.925  1.00 72.76  ?  269 ASN E CG  1 
ATOM   6906 O OD1 . ASN E 3 269 ? 15.293  50.260  38.339  1.00 73.41  ?  269 ASN E OD1 1 
ATOM   6907 N ND2 . ASN E 3 269 ? 15.033  48.319  39.444  1.00 64.81  ?  269 ASN E ND2 1 
ATOM   6908 N N   . PRO E 3 270 ? 10.295  51.129  38.650  1.00 93.22  ?  270 PRO E N   1 
ATOM   6909 C CA  . PRO E 3 270 ? 9.141   51.759  37.996  1.00 92.41  ?  270 PRO E CA  1 
ATOM   6910 C C   . PRO E 3 270 ? 8.888   53.132  38.581  1.00 95.41  ?  270 PRO E C   1 
ATOM   6911 O O   . PRO E 3 270 ? 8.739   54.116  37.848  1.00 92.94  ?  270 PRO E O   1 
ATOM   6912 C CB  . PRO E 3 270 ? 7.982   50.797  38.293  1.00 85.10  ?  270 PRO E CB  1 
ATOM   6913 C CG  . PRO E 3 270 ? 8.636   49.520  38.689  1.00 86.87  ?  270 PRO E CG  1 
ATOM   6914 C CD  . PRO E 3 270 ? 9.863   49.953  39.427  1.00 83.81  ?  270 PRO E CD  1 
ATOM   6915 N N   . GLY E 3 271 ? 8.871   53.197  39.912  1.00 94.89  ?  271 GLY E N   1 
ATOM   6916 C CA  . GLY E 3 271 ? 8.567   54.398  40.652  1.00 90.34  ?  271 GLY E CA  1 
ATOM   6917 C C   . GLY E 3 271 ? 7.282   55.004  40.135  1.00 96.94  ?  271 GLY E C   1 
ATOM   6918 O O   . GLY E 3 271 ? 6.408   54.311  39.609  1.00 96.80  ?  271 GLY E O   1 
ATOM   6919 N N   . ASN E 3 272 ? 7.163   56.324  40.294  1.00 103.87 ?  272 ASN E N   1 
ATOM   6920 C CA  . ASN E 3 272 ? 6.119   57.117  39.651  1.00 101.98 ?  272 ASN E CA  1 
ATOM   6921 C C   . ASN E 3 272 ? 4.741   56.460  39.714  1.00 100.38 ?  272 ASN E C   1 
ATOM   6922 O O   . ASN E 3 272 ? 3.917   56.647  38.812  1.00 98.59  ?  272 ASN E O   1 
ATOM   6923 C CB  . ASN E 3 272 ? 6.494   57.310  38.183  1.00 98.92  ?  272 ASN E CB  1 
ATOM   6924 C CG  . ASN E 3 272 ? 7.964   57.626  37.995  1.00 95.90  ?  272 ASN E CG  1 
ATOM   6925 O OD1 . ASN E 3 272 ? 8.662   56.950  37.240  1.00 95.58  ?  272 ASN E OD1 1 
ATOM   6926 N ND2 . ASN E 3 272 ? 8.448   58.629  38.704  1.00 95.09  ?  272 ASN E ND2 1 
ATOM   6927 N N   . HIS E 3 273 ? 4.483   55.704  40.782  1.00 97.92  ?  273 HIS E N   1 
ATOM   6928 C CA  . HIS E 3 273 ? 3.241   54.962  40.993  1.00 95.49  ?  273 HIS E CA  1 
ATOM   6929 C C   . HIS E 3 273 ? 2.934   53.975  39.861  1.00 94.20  ?  273 HIS E C   1 
ATOM   6930 O O   . HIS E 3 273 ? 1.766   53.621  39.653  1.00 93.07  ?  273 HIS E O   1 
ATOM   6931 C CB  . HIS E 3 273 ? 2.057   55.914  41.193  1.00 95.98  ?  273 HIS E CB  1 
ATOM   6932 C CG  . HIS E 3 273 ? 2.175   56.775  42.413  1.00 103.84 ?  273 HIS E CG  1 
ATOM   6933 N ND1 . HIS E 3 273 ? 1.276   57.777  42.708  1.00 106.77 ?  273 HIS E ND1 1 
ATOM   6934 C CD2 . HIS E 3 273 ? 3.095   56.793  43.406  1.00 101.54 ?  273 HIS E CD2 1 
ATOM   6935 C CE1 . HIS E 3 273 ? 1.632   58.371  43.833  1.00 103.14 ?  273 HIS E CE1 1 
ATOM   6936 N NE2 . HIS E 3 273 ? 2.733   57.792  44.278  1.00 102.54 ?  273 HIS E NE2 1 
ATOM   6937 N N   . LEU E 3 274 ? 3.946   53.495  39.133  1.00 92.83  ?  274 LEU E N   1 
ATOM   6938 C CA  . LEU E 3 274 ? 3.741   52.490  38.083  1.00 85.68  ?  274 LEU E CA  1 
ATOM   6939 C C   . LEU E 3 274 ? 3.782   51.074  38.654  1.00 78.15  ?  274 LEU E C   1 
ATOM   6940 O O   . LEU E 3 274 ? 4.473   50.192  38.145  1.00 77.35  ?  274 LEU E O   1 
ATOM   6941 C CB  . LEU E 3 274 ? 4.770   52.659  36.973  1.00 88.19  ?  274 LEU E CB  1 
ATOM   6942 C CG  . LEU E 3 274 ? 5.006   54.067  36.423  1.00 97.88  ?  274 LEU E CG  1 
ATOM   6943 C CD1 . LEU E 3 274 ? 6.214   54.094  35.492  1.00 96.29  ?  274 LEU E CD1 1 
ATOM   6944 C CD2 . LEU E 3 274 ? 3.765   54.582  35.717  1.00 89.43  ?  274 LEU E CD2 1 
ATOM   6945 N N   . TYR E 3 275 ? 3.030   50.854  39.727  1.00 72.00  ?  275 TYR E N   1 
ATOM   6946 C CA  . TYR E 3 275 ? 3.011   49.582  40.436  1.00 63.23  ?  275 TYR E CA  1 
ATOM   6947 C C   . TYR E 3 275 ? 1.708   49.516  41.223  1.00 58.33  ?  275 TYR E C   1 
ATOM   6948 O O   . TYR E 3 275 ? 0.936   50.477  41.264  1.00 63.51  ?  275 TYR E O   1 
ATOM   6949 C CB  . TYR E 3 275 ? 4.238   49.422  41.345  1.00 59.04  ?  275 TYR E CB  1 
ATOM   6950 C CG  . TYR E 3 275 ? 4.380   50.506  42.392  1.00 66.86  ?  275 TYR E CG  1 
ATOM   6951 C CD1 . TYR E 3 275 ? 3.670   50.443  43.585  1.00 68.99  ?  275 TYR E CD1 1 
ATOM   6952 C CD2 . TYR E 3 275 ? 5.223   51.592  42.191  1.00 73.88  ?  275 TYR E CD2 1 
ATOM   6953 C CE1 . TYR E 3 275 ? 3.790   51.434  44.545  1.00 73.50  ?  275 TYR E CE1 1 
ATOM   6954 C CE2 . TYR E 3 275 ? 5.352   52.589  43.150  1.00 74.05  ?  275 TYR E CE2 1 
ATOM   6955 C CZ  . TYR E 3 275 ? 4.631   52.503  44.326  1.00 72.60  ?  275 TYR E CZ  1 
ATOM   6956 O OH  . TYR E 3 275 ? 4.746   53.481  45.289  1.00 70.56  ?  275 TYR E OH  1 
ATOM   6957 N N   . LYS E 3 276 ? 1.473   48.374  41.856  1.00 55.69  ?  276 LYS E N   1 
ATOM   6958 C CA  . LYS E 3 276 ? 0.257   48.135  42.618  1.00 58.05  ?  276 LYS E CA  1 
ATOM   6959 C C   . LYS E 3 276 ? 0.608   47.308  43.845  1.00 58.40  ?  276 LYS E C   1 
ATOM   6960 O O   . LYS E 3 276 ? 1.373   46.344  43.749  1.00 63.45  ?  276 LYS E O   1 
ATOM   6961 C CB  . LYS E 3 276 ? -0.797  47.416  41.764  1.00 55.52  ?  276 LYS E CB  1 
ATOM   6962 C CG  . LYS E 3 276 ? -2.056  47.003  42.500  1.00 57.86  ?  276 LYS E CG  1 
ATOM   6963 C CD  . LYS E 3 276 ? -3.093  46.483  41.517  1.00 64.81  ?  276 LYS E CD  1 
ATOM   6964 C CE  . LYS E 3 276 ? -4.356  46.017  42.217  1.00 67.89  ?  276 LYS E CE  1 
ATOM   6965 N NZ  . LYS E 3 276 ? -5.358  45.523  41.233  1.00 73.58  ?  276 LYS E NZ  1 
ATOM   6966 N N   . TRP E 3 277 ? 0.071   47.697  44.998  1.00 60.41  ?  277 TRP E N   1 
ATOM   6967 C CA  . TRP E 3 277 ? 0.285   46.923  46.213  1.00 55.50  ?  277 TRP E CA  1 
ATOM   6968 C C   . TRP E 3 277 ? -0.517  45.623  46.162  1.00 54.40  ?  277 TRP E C   1 
ATOM   6969 O O   . TRP E 3 277 ? -1.587  45.549  45.551  1.00 52.05  ?  277 TRP E O   1 
ATOM   6970 C CB  . TRP E 3 277 ? -0.101  47.754  47.442  1.00 52.92  ?  277 TRP E CB  1 
ATOM   6971 C CG  . TRP E 3 277 ? 0.912   48.817  47.781  1.00 53.97  ?  277 TRP E CG  1 
ATOM   6972 C CD1 . TRP E 3 277 ? 1.066   50.028  47.166  1.00 54.72  ?  277 TRP E CD1 1 
ATOM   6973 C CD2 . TRP E 3 277 ? 1.899   48.770  48.823  1.00 54.46  ?  277 TRP E CD2 1 
ATOM   6974 N NE1 . TRP E 3 277 ? 2.095   50.730  47.751  1.00 54.63  ?  277 TRP E NE1 1 
ATOM   6975 C CE2 . TRP E 3 277 ? 2.620   49.982  48.771  1.00 52.57  ?  277 TRP E CE2 1 
ATOM   6976 C CE3 . TRP E 3 277 ? 2.245   47.821  49.791  1.00 54.58  ?  277 TRP E CE3 1 
ATOM   6977 C CZ2 . TRP E 3 277 ? 3.665   50.267  49.645  1.00 52.13  ?  277 TRP E CZ2 1 
ATOM   6978 C CZ3 . TRP E 3 277 ? 3.287   48.106  50.659  1.00 55.60  ?  277 TRP E CZ3 1 
ATOM   6979 C CH2 . TRP E 3 277 ? 3.982   49.319  50.580  1.00 57.08  ?  277 TRP E CH2 1 
ATOM   6980 N N   . LYS E 3 278 ? 0.021   44.588  46.803  1.00 50.06  ?  278 LYS E N   1 
ATOM   6981 C CA  . LYS E 3 278 ? -0.585  43.264  46.837  1.00 54.24  ?  278 LYS E CA  1 
ATOM   6982 C C   . LYS E 3 278 ? -1.076  42.962  48.248  1.00 55.59  ?  278 LYS E C   1 
ATOM   6983 O O   . LYS E 3 278 ? -0.665  43.608  49.213  1.00 59.10  ?  278 LYS E O   1 
ATOM   6984 C CB  . LYS E 3 278 ? 0.414   42.183  46.395  1.00 53.90  ?  278 LYS E CB  1 
ATOM   6985 C CG  . LYS E 3 278 ? 1.075   42.416  45.040  1.00 45.07  ?  278 LYS E CG  1 
ATOM   6986 C CD  . LYS E 3 278 ? 2.399   43.151  45.199  1.00 46.13  ?  278 LYS E CD  1 
ATOM   6987 C CE  . LYS E 3 278 ? 3.153   43.246  43.884  1.00 43.15  ?  278 LYS E CE  1 
ATOM   6988 N NZ  . LYS E 3 278 ? 2.337   43.829  42.782  1.00 48.81  ?  278 LYS E NZ  1 
ATOM   6989 N N   . GLN E 3 279 ? -1.971  41.982  48.365  1.00 48.47  ?  279 GLN E N   1 
ATOM   6990 C CA  . GLN E 3 279 ? -2.508  41.573  49.658  1.00 55.30  ?  279 GLN E CA  1 
ATOM   6991 C C   . GLN E 3 279 ? -1.838  40.303  50.176  1.00 57.22  ?  279 GLN E C   1 
ATOM   6992 O O   . GLN E 3 279 ? -1.611  39.349  49.427  1.00 56.99  ?  279 GLN E O   1 
ATOM   6993 C CB  . GLN E 3 279 ? -4.027  41.374  49.614  1.00 55.58  ?  279 GLN E CB  1 
ATOM   6994 C CG  . GLN E 3 279 ? -4.849  42.656  49.489  1.00 61.42  ?  279 GLN E CG  1 
ATOM   6995 C CD  . GLN E 3 279 ? -4.685  43.359  48.164  1.00 70.15  ?  279 GLN E CD  1 
ATOM   6996 O OE1 . GLN E 3 279 ? -4.109  42.809  47.226  1.00 84.43  ?  279 GLN E OE1 1 
ATOM   6997 N NE2 . GLN E 3 279 ? -5.193  44.586  48.075  1.00 64.14  ?  279 GLN E NE2 1 
ATOM   6998 N N   . ILE E 3 280 ? -1.535  40.300  51.469  1.00 53.41  ?  280 ILE E N   1 
ATOM   6999 C CA  . ILE E 3 280 ? -1.069  39.076  52.127  1.00 52.89  ?  280 ILE E CA  1 
ATOM   7000 C C   . ILE E 3 280 ? -2.187  38.039  52.079  1.00 57.53  ?  280 ILE E C   1 
ATOM   7001 O O   . ILE E 3 280 ? -3.327  38.342  52.479  1.00 60.13  ?  280 ILE E O   1 
ATOM   7002 C CB  . ILE E 3 280 ? -0.648  39.371  53.578  1.00 52.63  ?  280 ILE E CB  1 
ATOM   7003 C CG1 . ILE E 3 280 ? 0.565   40.308  53.598  1.00 56.04  ?  280 ILE E CG1 1 
ATOM   7004 C CG2 . ILE E 3 280 ? -0.349  38.076  54.327  1.00 55.31  ?  280 ILE E CG2 1 
ATOM   7005 C CD1 . ILE E 3 280 ? 1.912   39.617  53.425  1.00 53.64  ?  280 ILE E CD1 1 
ATOM   7006 N N   . PRO E 3 281 ? -1.924  36.812  51.580  1.00 60.96  ?  281 PRO E N   1 
ATOM   7007 C CA  . PRO E 3 281 ? -2.999  35.862  51.234  1.00 61.16  ?  281 PRO E CA  1 
ATOM   7008 C C   . PRO E 3 281 ? -4.167  35.727  52.202  1.00 68.93  ?  281 PRO E C   1 
ATOM   7009 O O   . PRO E 3 281 ? -5.323  35.782  51.764  1.00 72.75  ?  281 PRO E O   1 
ATOM   7010 C CB  . PRO E 3 281 ? -2.244  34.539  51.121  1.00 57.42  ?  281 PRO E CB  1 
ATOM   7011 C CG  . PRO E 3 281 ? -0.924  34.952  50.589  1.00 60.51  ?  281 PRO E CG  1 
ATOM   7012 C CD  . PRO E 3 281 ? -0.594  36.262  51.267  1.00 60.73  ?  281 PRO E CD  1 
ATOM   7013 N N   . ASP E 3 282 ? -3.912  35.563  53.502  1.00 61.79  ?  282 ASP E N   1 
ATOM   7014 C CA  . ASP E 3 282 ? -4.996  35.348  54.457  1.00 72.60  ?  282 ASP E CA  1 
ATOM   7015 C C   . ASP E 3 282 ? -5.058  36.436  55.521  1.00 71.00  ?  282 ASP E C   1 
ATOM   7016 O O   . ASP E 3 282 ? -5.496  36.187  56.646  1.00 75.18  ?  282 ASP E O   1 
ATOM   7017 C CB  . ASP E 3 282 ? -4.871  33.976  55.115  1.00 79.39  ?  282 ASP E CB  1 
ATOM   7018 C CG  . ASP E 3 282 ? -5.516  32.889  54.293  1.00 85.97  ?  282 ASP E CG  1 
ATOM   7019 O OD1 . ASP E 3 282 ? -6.169  33.253  53.298  1.00 83.98  ?  282 ASP E OD1 1 
ATOM   7020 O OD2 . ASP E 3 282 ? -5.378  31.690  54.623  1.00 87.48  ?  282 ASP E OD2 1 
ATOM   7021 N N   . CYS E 3 283 ? -4.665  37.655  55.170  1.00 67.52  ?  283 CYS E N   1 
ATOM   7022 C CA  . CYS E 3 283 ? -4.748  38.792  56.074  1.00 64.45  ?  283 CYS E CA  1 
ATOM   7023 C C   . CYS E 3 283 ? -5.466  39.947  55.398  1.00 65.71  ?  283 CYS E C   1 
ATOM   7024 O O   . CYS E 3 283 ? -5.102  41.117  55.558  1.00 62.32  ?  283 CYS E O   1 
ATOM   7025 C CB  . CYS E 3 283 ? -3.360  39.209  56.566  1.00 59.81  ?  283 CYS E CB  1 
ATOM   7026 S SG  . CYS E 3 283 ? -2.695  38.144  57.887  1.00 74.18  ?  283 CYS E SG  1 
ATOM   7027 N N   . GLU E 3 284 ? -6.518  39.626  54.642  1.00 62.32  ?  284 GLU E N   1 
ATOM   7028 C CA  . GLU E 3 284 ? -7.302  40.655  53.973  1.00 62.17  ?  284 GLU E CA  1 
ATOM   7029 C C   . GLU E 3 284 ? -8.275  41.330  54.926  1.00 69.57  ?  284 GLU E C   1 
ATOM   7030 O O   . GLU E 3 284 ? -8.581  42.517  54.757  1.00 69.79  ?  284 GLU E O   1 
ATOM   7031 C CB  . GLU E 3 284 ? -8.063  40.049  52.793  1.00 65.43  ?  284 GLU E CB  1 
ATOM   7032 C CG  . GLU E 3 284 ? -7.177  39.621  51.635  1.00 68.17  ?  284 GLU E CG  1 
ATOM   7033 C CD  . GLU E 3 284 ? -7.928  38.814  50.599  1.00 63.68  ?  284 GLU E CD  1 
ATOM   7034 O OE1 . GLU E 3 284 ? -8.596  39.424  49.740  1.00 63.38  ?  284 GLU E OE1 1 
ATOM   7035 O OE2 . GLU E 3 284 ? -7.845  37.569  50.641  1.00 65.79  ?  284 GLU E OE2 1 
ATOM   7036 N N   . ASN E 3 285 ? -8.773  40.598  55.927  1.00 68.12  ?  285 ASN E N   1 
ATOM   7037 C CA  . ASN E 3 285 ? -9.725  41.199  56.852  1.00 74.98  ?  285 ASN E CA  1 
ATOM   7038 C C   . ASN E 3 285 ? -9.528  40.538  58.223  1.00 78.40  ?  285 ASN E C   1 
ATOM   7039 O O   . ASN E 3 285 ? -10.303 39.676  58.647  1.00 77.99  ?  285 ASN E O   1 
ATOM   7040 C CB  . ASN E 3 285 ? -11.158 41.048  56.350  1.00 76.97  ?  285 ASN E CB  1 
ATOM   7041 C CG  . ASN E 3 285 ? -12.127 41.907  57.118  1.00 88.09  ?  285 ASN E CG  1 
ATOM   7042 O OD1 . ASN E 3 285 ? -11.799 43.031  57.498  1.00 89.36  ?  285 ASN E OD1 1 
ATOM   7043 N ND2 . ASN E 3 285 ? -13.322 41.386  57.365  1.00 98.62  ?  285 ASN E ND2 1 
ATOM   7044 N N   . VAL E 3 286 ? -8.467  40.956  58.920  1.00 74.78  ?  286 VAL E N   1 
ATOM   7045 C CA  . VAL E 3 286 ? -8.131  40.412  60.230  1.00 73.46  ?  286 VAL E CA  1 
ATOM   7046 C C   . VAL E 3 286 ? -8.904  41.172  61.301  1.00 77.59  ?  286 VAL E C   1 
ATOM   7047 O O   . VAL E 3 286 ? -9.276  42.336  61.129  1.00 81.28  ?  286 VAL E O   1 
ATOM   7048 C CB  . VAL E 3 286 ? -6.608  40.477  60.486  1.00 77.23  ?  286 VAL E CB  1 
ATOM   7049 C CG1 . VAL E 3 286 ? -6.220  39.714  61.755  1.00 80.32  ?  286 VAL E CG1 1 
ATOM   7050 C CG2 . VAL E 3 286 ? -5.855  39.942  59.290  1.00 78.53  ?  286 VAL E CG2 1 
ATOM   7051 N N   . LYS E 3 287 ? -9.125  40.510  62.441  1.00 77.45  ?  287 LYS E N   1 
ATOM   7052 C CA  . LYS E 3 287 ? -9.902  41.074  63.535  1.00 82.23  ?  287 LYS E CA  1 
ATOM   7053 C C   . LYS E 3 287 ? -9.062  41.523  64.720  1.00 81.56  ?  287 LYS E C   1 
ATOM   7054 O O   . LYS E 3 287 ? -9.558  42.295  65.547  1.00 82.32  ?  287 LYS E O   1 
ATOM   7055 C CB  . LYS E 3 287 ? -10.941 40.055  64.027  1.00 83.19  ?  287 LYS E CB  1 
ATOM   7056 C CG  . LYS E 3 287 ? -11.935 39.626  62.965  1.00 85.82  ?  287 LYS E CG  1 
ATOM   7057 C CD  . LYS E 3 287 ? -12.808 40.793  62.535  1.00 82.78  ?  287 LYS E CD  1 
ATOM   7058 C CE  . LYS E 3 287 ? -13.853 40.348  61.528  1.00 82.56  ?  287 LYS E CE  1 
ATOM   7059 N NZ  . LYS E 3 287 ? -14.704 41.484  61.085  1.00 95.15  ?  287 LYS E NZ  1 
ATOM   7060 N N   . THR E 3 288 ? -7.817  41.076  64.821  1.00 78.81  ?  288 THR E N   1 
ATOM   7061 C CA  . THR E 3 288 ? -6.916  41.491  65.883  1.00 78.14  ?  288 THR E CA  1 
ATOM   7062 C C   . THR E 3 288 ? -5.853  42.432  65.325  1.00 76.72  ?  288 THR E C   1 
ATOM   7063 O O   . THR E 3 288 ? -5.857  42.788  64.143  1.00 73.51  ?  288 THR E O   1 
ATOM   7064 C CB  . THR E 3 288 ? -6.265  40.276  66.547  1.00 81.81  ?  288 THR E CB  1 
ATOM   7065 O OG1 . THR E 3 288 ? -5.244  40.717  67.452  1.00 83.03  ?  288 THR E OG1 1 
ATOM   7066 C CG2 . THR E 3 288 ? -5.646  39.358  65.496  1.00 79.74  ?  288 THR E CG2 1 
ATOM   7067 N N   . THR E 3 289 ? -4.931  42.838  66.199  1.00 74.97  ?  289 THR E N   1 
ATOM   7068 C CA  . THR E 3 289 ? -3.795  43.662  65.815  1.00 72.99  ?  289 THR E CA  1 
ATOM   7069 C C   . THR E 3 289 ? -2.589  42.819  65.422  1.00 77.41  ?  289 THR E C   1 
ATOM   7070 O O   . THR E 3 289 ? -1.451  43.299  65.497  1.00 77.34  ?  289 THR E O   1 
ATOM   7071 C CB  . THR E 3 289 ? -3.420  44.626  66.945  1.00 73.29  ?  289 THR E CB  1 
ATOM   7072 O OG1 . THR E 3 289 ? -3.148  43.889  68.144  1.00 78.98  ?  289 THR E OG1 1 
ATOM   7073 C CG2 . THR E 3 289 ? -4.546  45.613  67.202  1.00 71.42  ?  289 THR E CG2 1 
ATOM   7074 N N   . GLN E 3 290 ? -2.817  41.575  65.006  1.00 75.06  ?  290 GLN E N   1 
ATOM   7075 C CA  . GLN E 3 290 ? -1.753  40.645  64.672  1.00 75.02  ?  290 GLN E CA  1 
ATOM   7076 C C   . GLN E 3 290 ? -2.105  39.931  63.377  1.00 77.16  ?  290 GLN E C   1 
ATOM   7077 O O   . GLN E 3 290 ? -3.281  39.697  63.082  1.00 77.28  ?  290 GLN E O   1 
ATOM   7078 C CB  . GLN E 3 290 ? -1.571  39.617  65.793  1.00 73.61  ?  290 GLN E CB  1 
ATOM   7079 C CG  . GLN E 3 290 ? -0.150  39.366  66.210  1.00 77.82  ?  290 GLN E CG  1 
ATOM   7080 C CD  . GLN E 3 290 ? -0.073  38.502  67.446  1.00 83.60  ?  290 GLN E CD  1 
ATOM   7081 O OE1 . GLN E 3 290 ? 0.590   38.850  68.420  1.00 91.08  ?  290 GLN E OE1 1 
ATOM   7082 N NE2 . GLN E 3 290 ? -0.761  37.367  67.416  1.00 80.60  ?  290 GLN E NE2 1 
ATOM   7083 N N   . CYS E 3 291 ? -1.078  39.574  62.609  1.00 73.43  ?  291 CYS E N   1 
ATOM   7084 C CA  . CYS E 3 291 ? -1.268  38.818  61.375  1.00 72.83  ?  291 CYS E CA  1 
ATOM   7085 C C   . CYS E 3 291 ? -0.140  37.804  61.253  1.00 71.04  ?  291 CYS E C   1 
ATOM   7086 O O   . CYS E 3 291 ? 1.035   38.178  61.258  1.00 71.11  ?  291 CYS E O   1 
ATOM   7087 C CB  . CYS E 3 291 ? -1.321  39.756  60.157  1.00 70.06  ?  291 CYS E CB  1 
ATOM   7088 S SG  . CYS E 3 291 ? -0.966  39.019  58.526  1.00 83.79  ?  291 CYS E SG  1 
ATOM   7089 N N   . VAL E 3 292 ? -0.484  36.524  61.157  1.00 71.47  ?  292 VAL E N   1 
ATOM   7090 C CA  . VAL E 3 292 ? 0.497   35.466  60.947  1.00 73.10  ?  292 VAL E CA  1 
ATOM   7091 C C   . VAL E 3 292 ? 0.331   34.947  59.526  1.00 71.20  ?  292 VAL E C   1 
ATOM   7092 O O   . VAL E 3 292 ? -0.797  34.784  59.042  1.00 71.24  ?  292 VAL E O   1 
ATOM   7093 C CB  . VAL E 3 292 ? 0.369   34.324  61.982  1.00 67.19  ?  292 VAL E CB  1 
ATOM   7094 C CG1 . VAL E 3 292 ? 0.433   34.873  63.402  1.00 62.04  ?  292 VAL E CG1 1 
ATOM   7095 C CG2 . VAL E 3 292 ? -0.908  33.521  61.774  1.00 71.31  ?  292 VAL E CG2 1 
ATOM   7096 N N   . PHE E 3 293 ? 1.452   34.736  58.839  1.00 66.49  ?  293 PHE E N   1 
ATOM   7097 C CA  . PHE E 3 293 ? 1.370   34.190  57.491  1.00 64.07  ?  293 PHE E CA  1 
ATOM   7098 C C   . PHE E 3 293 ? 2.607   33.352  57.209  1.00 63.75  ?  293 PHE E C   1 
ATOM   7099 O O   . PHE E 3 293 ? 3.679   33.633  57.756  1.00 61.03  ?  293 PHE E O   1 
ATOM   7100 C CB  . PHE E 3 293 ? 1.200   35.291  56.428  1.00 58.96  ?  293 PHE E CB  1 
ATOM   7101 C CG  . PHE E 3 293 ? 2.276   36.343  56.440  1.00 61.29  ?  293 PHE E CG  1 
ATOM   7102 C CD1 . PHE E 3 293 ? 2.141   37.483  57.217  1.00 63.19  ?  293 PHE E CD1 1 
ATOM   7103 C CD2 . PHE E 3 293 ? 3.405   36.211  55.643  1.00 58.39  ?  293 PHE E CD2 1 
ATOM   7104 C CE1 . PHE E 3 293 ? 3.122   38.463  57.217  1.00 60.69  ?  293 PHE E CE1 1 
ATOM   7105 C CE2 . PHE E 3 293 ? 4.389   37.186  55.638  1.00 61.06  ?  293 PHE E CE2 1 
ATOM   7106 C CZ  . PHE E 3 293 ? 4.247   38.315  56.425  1.00 59.49  ?  293 PHE E CZ  1 
ATOM   7107 N N   . PRO E 3 294 ? 2.489   32.311  56.382  1.00 54.67  ?  294 PRO E N   1 
ATOM   7108 C CA  . PRO E 3 294 ? 3.648   31.455  56.105  1.00 58.48  ?  294 PRO E CA  1 
ATOM   7109 C C   . PRO E 3 294 ? 4.779   32.227  55.443  1.00 56.96  ?  294 PRO E C   1 
ATOM   7110 O O   . PRO E 3 294 ? 4.562   33.229  54.759  1.00 52.13  ?  294 PRO E O   1 
ATOM   7111 C CB  . PRO E 3 294 ? 3.083   30.385  55.163  1.00 58.98  ?  294 PRO E CB  1 
ATOM   7112 C CG  . PRO E 3 294 ? 1.616   30.393  55.415  1.00 56.05  ?  294 PRO E CG  1 
ATOM   7113 C CD  . PRO E 3 294 ? 1.266   31.811  55.735  1.00 56.75  ?  294 PRO E CD  1 
ATOM   7114 N N   . GLN E 3 295 ? 6.004   31.736  55.655  1.00 58.42  ?  295 GLN E N   1 
ATOM   7115 C CA  . GLN E 3 295 ? 7.179   32.383  55.079  1.00 57.92  ?  295 GLN E CA  1 
ATOM   7116 C C   . GLN E 3 295 ? 7.272   32.165  53.574  1.00 55.09  ?  295 GLN E C   1 
ATOM   7117 O O   . GLN E 3 295 ? 7.848   33.000  52.866  1.00 51.06  ?  295 GLN E O   1 
ATOM   7118 C CB  . GLN E 3 295 ? 8.445   31.872  55.766  1.00 59.72  ?  295 GLN E CB  1 
ATOM   7119 C CG  . GLN E 3 295 ? 8.574   32.284  57.221  1.00 60.84  ?  295 GLN E CG  1 
ATOM   7120 C CD  . GLN E 3 295 ? 9.817   31.718  57.873  1.00 61.55  ?  295 GLN E CD  1 
ATOM   7121 O OE1 . GLN E 3 295 ? 10.795  31.407  57.199  1.00 65.12  ?  295 GLN E OE1 1 
ATOM   7122 N NE2 . GLN E 3 295 ? 9.787   31.587  59.193  1.00 65.21  ?  295 GLN E NE2 1 
ATOM   7123 N N   . ASN E 3 296 ? 6.697   31.068  53.061  1.00 54.32  ?  296 ASN E N   1 
ATOM   7124 C CA  . ASN E 3 296 ? 6.705   30.829  51.618  1.00 51.44  ?  296 ASN E CA  1 
ATOM   7125 C C   . ASN E 3 296 ? 5.720   31.717  50.872  1.00 50.73  ?  296 ASN E C   1 
ATOM   7126 O O   . ASN E 3 296 ? 5.501   31.543  49.664  1.00 51.38  ?  296 ASN E O   1 
ATOM   7127 C CB  . ASN E 3 296 ? 6.434   29.352  51.321  1.00 55.20  ?  296 ASN E CB  1 
ATOM   7128 C CG  . ASN E 3 296 ? 5.210   28.825  52.033  1.00 61.17  ?  296 ASN E CG  1 
ATOM   7129 O OD1 . ASN E 3 296 ? 5.268   28.478  53.211  1.00 70.52  ?  296 ASN E OD1 1 
ATOM   7130 N ND2 . ASN E 3 296 ? 4.097   28.738  51.315  1.00 63.83  ?  296 ASN E ND2 1 
ATOM   7131 N N   . VAL E 3 297 ? 5.106   32.661  51.585  1.00 51.38  ?  297 VAL E N   1 
ATOM   7132 C CA  . VAL E 3 297 ? 4.426   33.769  50.926  1.00 49.70  ?  297 VAL E CA  1 
ATOM   7133 C C   . VAL E 3 297 ? 5.431   34.615  50.152  1.00 52.28  ?  297 VAL E C   1 
ATOM   7134 O O   . VAL E 3 297 ? 5.110   35.171  49.093  1.00 46.93  ?  297 VAL E O   1 
ATOM   7135 C CB  . VAL E 3 297 ? 3.654   34.599  51.970  1.00 48.14  ?  297 VAL E CB  1 
ATOM   7136 C CG1 . VAL E 3 297 ? 3.257   35.953  51.411  1.00 54.52  ?  297 VAL E CG1 1 
ATOM   7137 C CG2 . VAL E 3 297 ? 2.432   33.839  52.434  1.00 51.07  ?  297 VAL E CG2 1 
ATOM   7138 N N   . PHE E 3 298 ? 6.661   34.705  50.648  1.00 48.58  ?  298 PHE E N   1 
ATOM   7139 C CA  . PHE E 3 298 ? 7.717   35.484  50.024  1.00 47.70  ?  298 PHE E CA  1 
ATOM   7140 C C   . PHE E 3 298 ? 8.805   34.570  49.475  1.00 47.41  ?  298 PHE E C   1 
ATOM   7141 O O   . PHE E 3 298 ? 8.919   33.401  49.852  1.00 47.03  ?  298 PHE E O   1 
ATOM   7142 C CB  . PHE E 3 298 ? 8.330   36.479  51.019  1.00 46.47  ?  298 PHE E CB  1 
ATOM   7143 C CG  . PHE E 3 298 ? 7.376   37.535  51.485  1.00 51.26  ?  298 PHE E CG  1 
ATOM   7144 C CD1 . PHE E 3 298 ? 6.602   38.236  50.576  1.00 50.15  ?  298 PHE E CD1 1 
ATOM   7145 C CD2 . PHE E 3 298 ? 7.238   37.813  52.836  1.00 52.92  ?  298 PHE E CD2 1 
ATOM   7146 C CE1 . PHE E 3 298 ? 5.714   39.203  51.006  1.00 49.46  ?  298 PHE E CE1 1 
ATOM   7147 C CE2 . PHE E 3 298 ? 6.348   38.775  53.270  1.00 50.59  ?  298 PHE E CE2 1 
ATOM   7148 C CZ  . PHE E 3 298 ? 5.588   39.473  52.354  1.00 51.24  ?  298 PHE E CZ  1 
ATOM   7149 N N   . GLN E 3 299 ? 9.579   35.120  48.542  1.00 47.81  ?  299 GLN E N   1 
ATOM   7150 C CA  . GLN E 3 299 ? 10.852  34.563  48.111  1.00 44.60  ?  299 GLN E CA  1 
ATOM   7151 C C   . GLN E 3 299 ? 11.967  35.219  48.922  1.00 49.96  ?  299 GLN E C   1 
ATOM   7152 O O   . GLN E 3 299 ? 11.712  35.971  49.866  1.00 51.33  ?  299 GLN E O   1 
ATOM   7153 C CB  . GLN E 3 299 ? 11.046  34.777  46.613  1.00 41.63  ?  299 GLN E CB  1 
ATOM   7154 C CG  . GLN E 3 299 ? 9.939   34.203  45.745  1.00 44.52  ?  299 GLN E CG  1 
ATOM   7155 C CD  . GLN E 3 299 ? 10.129  34.546  44.283  1.00 44.81  ?  299 GLN E CD  1 
ATOM   7156 O OE1 . GLN E 3 299 ? 11.082  35.234  43.918  1.00 46.85  ?  299 GLN E OE1 1 
ATOM   7157 N NE2 . GLN E 3 299 ? 9.232   34.057  43.434  1.00 39.95  ?  299 GLN E NE2 1 
ATOM   7158 N N   . LYS E 3 300 ? 13.219  34.926  48.587  1.00 53.30  ?  300 LYS E N   1 
ATOM   7159 C CA  . LYS E 3 300 ? 14.339  35.642  49.192  1.00 58.98  ?  300 LYS E CA  1 
ATOM   7160 C C   . LYS E 3 300 ? 14.485  36.994  48.500  1.00 54.63  ?  300 LYS E C   1 
ATOM   7161 O O   . LYS E 3 300 ? 14.925  37.068  47.349  1.00 59.98  ?  300 LYS E O   1 
ATOM   7162 C CB  . LYS E 3 300 ? 15.625  34.822  49.115  1.00 63.42  ?  300 LYS E CB  1 
ATOM   7163 C CG  . LYS E 3 300 ? 15.766  33.827  50.269  1.00 64.86  ?  300 LYS E CG  1 
ATOM   7164 C CD  . LYS E 3 300 ? 17.085  33.082  50.232  1.00 67.97  ?  300 LYS E CD  1 
ATOM   7165 C CE  . LYS E 3 300 ? 17.226  32.168  51.443  1.00 78.66  ?  300 LYS E CE  1 
ATOM   7166 N NZ  . LYS E 3 300 ? 18.635  31.727  51.674  1.00 70.46  ?  300 LYS E NZ  1 
ATOM   7167 N N   . GLY E 3 301 ? 14.092  38.057  49.193  1.00 53.22  ?  301 GLY E N   1 
ATOM   7168 C CA  . GLY E 3 301 ? 14.152  39.391  48.633  1.00 51.93  ?  301 GLY E CA  1 
ATOM   7169 C C   . GLY E 3 301 ? 13.882  40.439  49.689  1.00 51.33  ?  301 GLY E C   1 
ATOM   7170 O O   . GLY E 3 301 ? 13.906  40.164  50.890  1.00 50.41  ?  301 GLY E O   1 
ATOM   7171 N N   . ILE E 3 302 ? 13.626  41.658  49.222  1.00 54.40  ?  302 ILE E N   1 
ATOM   7172 C CA  . ILE E 3 302 ? 13.296  42.784  50.089  1.00 54.20  ?  302 ILE E CA  1 
ATOM   7173 C C   . ILE E 3 302 ? 11.855  43.180  49.825  1.00 46.85  ?  302 ILE E C   1 
ATOM   7174 O O   . ILE E 3 302 ? 11.489  43.501  48.687  1.00 48.79  ?  302 ILE E O   1 
ATOM   7175 C CB  . ILE E 3 302 ? 14.220  43.985  49.860  1.00 60.70  ?  302 ILE E CB  1 
ATOM   7176 C CG1 . ILE E 3 302 ? 15.679  43.569  49.791  1.00 57.66  ?  302 ILE E CG1 1 
ATOM   7177 C CG2 . ILE E 3 302 ? 14.056  44.991  50.978  1.00 59.75  ?  302 ILE E CG2 1 
ATOM   7178 C CD1 . ILE E 3 302 ? 16.553  44.750  49.488  1.00 69.01  ?  302 ILE E CD1 1 
ATOM   7179 N N   . TYR E 3 303 ? 11.042  43.182  50.873  1.00 45.58  ?  303 TYR E N   1 
ATOM   7180 C CA  . TYR E 3 303 ? 9.629   43.485  50.736  1.00 48.66  ?  303 TYR E CA  1 
ATOM   7181 C C   . TYR E 3 303 ? 9.228   44.581  51.715  1.00 52.97  ?  303 TYR E C   1 
ATOM   7182 O O   . TYR E 3 303 ? 9.859   44.787  52.754  1.00 52.14  ?  303 TYR E O   1 
ATOM   7183 C CB  . TYR E 3 303 ? 8.764   42.235  50.957  1.00 44.97  ?  303 TYR E CB  1 
ATOM   7184 C CG  . TYR E 3 303 ? 9.035   41.115  49.974  1.00 48.13  ?  303 TYR E CG  1 
ATOM   7185 C CD1 . TYR E 3 303 ? 8.362   41.048  48.763  1.00 47.73  ?  303 TYR E CD1 1 
ATOM   7186 C CD2 . TYR E 3 303 ? 9.968   40.121  50.261  1.00 47.28  ?  303 TYR E CD2 1 
ATOM   7187 C CE1 . TYR E 3 303 ? 8.608   40.025  47.864  1.00 43.86  ?  303 TYR E CE1 1 
ATOM   7188 C CE2 . TYR E 3 303 ? 10.221  39.099  49.371  1.00 44.07  ?  303 TYR E CE2 1 
ATOM   7189 C CZ  . TYR E 3 303 ? 9.536   39.053  48.175  1.00 44.50  ?  303 TYR E CZ  1 
ATOM   7190 O OH  . TYR E 3 303 ? 9.780   38.028  47.286  1.00 42.77  ?  303 TYR E OH  1 
ATOM   7191 N N   . LEU E 3 304 ? 8.155   45.278  51.360  1.00 51.38  ?  304 LEU E N   1 
ATOM   7192 C CA  . LEU E 3 304 ? 7.546   46.313  52.176  1.00 52.01  ?  304 LEU E CA  1 
ATOM   7193 C C   . LEU E 3 304 ? 6.201   45.807  52.670  1.00 59.64  ?  304 LEU E C   1 
ATOM   7194 O O   . LEU E 3 304 ? 5.472   45.145  51.926  1.00 59.79  ?  304 LEU E O   1 
ATOM   7195 C CB  . LEU E 3 304 ? 7.333   47.592  51.369  1.00 51.06  ?  304 LEU E CB  1 
ATOM   7196 C CG  . LEU E 3 304 ? 8.579   48.262  50.800  1.00 57.12  ?  304 LEU E CG  1 
ATOM   7197 C CD1 . LEU E 3 304 ? 8.190   49.420  49.895  1.00 50.90  ?  304 LEU E CD1 1 
ATOM   7198 C CD2 . LEU E 3 304 ? 9.466   48.730  51.922  1.00 58.37  ?  304 LEU E CD2 1 
ATOM   7199 N N   . LEU E 3 305 ? 5.900   46.091  53.930  1.00 58.97  ?  305 LEU E N   1 
ATOM   7200 C CA  . LEU E 3 305 ? 4.587   45.711  54.484  1.00 55.79  ?  305 LEU E CA  1 
ATOM   7201 C C   . LEU E 3 305 ? 3.884   46.969  55.004  1.00 60.08  ?  305 LEU E C   1 
ATOM   7202 O O   . LEU E 3 305 ? 4.576   47.874  55.453  1.00 59.88  ?  305 LEU E O   1 
ATOM   7203 C CB  . LEU E 3 305 ? 4.808   44.669  55.579  1.00 54.38  ?  305 LEU E CB  1 
ATOM   7204 C CG  . LEU E 3 305 ? 5.229   43.287  55.094  1.00 58.03  ?  305 LEU E CG  1 
ATOM   7205 C CD1 . LEU E 3 305 ? 5.648   42.413  56.263  1.00 62.14  ?  305 LEU E CD1 1 
ATOM   7206 C CD2 . LEU E 3 305 ? 4.107   42.627  54.316  1.00 54.68  ?  305 LEU E CD2 1 
ATOM   7207 N N   . ARG E 3 306 ? 2.557   47.023  54.902  1.00 58.10  ?  306 ARG E N   1 
ATOM   7208 C CA  . ARG E 3 306 ? 1.771   48.170  55.402  1.00 55.63  ?  306 ARG E CA  1 
ATOM   7209 C C   . ARG E 3 306 ? 0.413   47.659  55.854  1.00 61.22  ?  306 ARG E C   1 
ATOM   7210 O O   . ARG E 3 306 ? -0.030  46.647  55.320  1.00 60.97  ?  306 ARG E O   1 
ATOM   7211 C CB  . ARG E 3 306 ? 1.622   49.241  54.329  1.00 60.24  ?  306 ARG E CB  1 
ATOM   7212 C CG  . ARG E 3 306 ? 0.797   48.850  53.117  1.00 58.09  ?  306 ARG E CG  1 
ATOM   7213 C CD  . ARG E 3 306 ? 0.715   50.078  52.239  1.00 50.51  ?  306 ARG E CD  1 
ATOM   7214 N NE  . ARG E 3 306 ? -0.290  49.952  51.205  1.00 55.82  ?  306 ARG E NE  1 
ATOM   7215 C CZ  . ARG E 3 306 ? -0.557  50.893  50.319  1.00 56.00  ?  306 ARG E CZ  1 
ATOM   7216 N NH1 . ARG E 3 306 ? 0.109   52.032  50.349  1.00 52.82  ?  306 ARG E NH1 1 
ATOM   7217 N NH2 . ARG E 3 306 ? -1.488  50.694  49.406  1.00 59.68  ?  306 ARG E NH2 1 
ATOM   7218 N N   . VAL E 3 307 ? -0.200  48.338  56.822  1.00 61.40  ?  307 VAL E N   1 
ATOM   7219 C CA  . VAL E 3 307 ? -1.506  47.886  57.375  1.00 61.33  ?  307 VAL E CA  1 
ATOM   7220 C C   . VAL E 3 307 ? -2.504  49.040  57.313  1.00 62.93  ?  307 VAL E C   1 
ATOM   7221 O O   . VAL E 3 307 ? -2.067  50.187  57.308  1.00 67.25  ?  307 VAL E O   1 
ATOM   7222 C CB  . VAL E 3 307 ? -1.367  47.322  58.801  1.00 60.68  ?  307 VAL E CB  1 
ATOM   7223 C CG1 . VAL E 3 307 ? -2.573  46.492  59.200  1.00 62.61  ?  307 VAL E CG1 1 
ATOM   7224 C CG2 . VAL E 3 307 ? -0.091  46.518  58.972  1.00 62.74  ?  307 VAL E CG2 1 
ATOM   7225 N N   . GLN E 3 308 ? -3.793  48.725  57.219  1.00 64.27  ?  308 GLN E N   1 
ATOM   7226 C CA  . GLN E 3 308 ? -4.868  49.742  57.179  1.00 63.45  ?  308 GLN E CA  1 
ATOM   7227 C C   . GLN E 3 308 ? -6.017  49.246  58.036  1.00 65.48  ?  308 GLN E C   1 
ATOM   7228 O O   . GLN E 3 308 ? -6.090  48.047  58.288  1.00 65.84  ?  308 GLN E O   1 
ATOM   7229 C CB  . GLN E 3 308 ? -5.435  49.897  55.776  1.00 62.74  ?  308 GLN E CB  1 
ATOM   7230 C CG  . GLN E 3 308 ? -6.002  51.268  55.470  1.00 62.46  ?  308 GLN E CG  1 
ATOM   7231 C CD  . GLN E 3 308 ? -6.834  51.206  54.216  1.00 61.38  ?  308 GLN E CD  1 
ATOM   7232 O OE1 . GLN E 3 308 ? -7.544  50.237  53.972  1.00 64.33  ?  308 GLN E OE1 1 
ATOM   7233 N NE2 . GLN E 3 308 ? -6.740  52.238  53.399  1.00 61.46  ?  308 GLN E NE2 1 
ATOM   7234 N N   . ALA E 3 309 ? -6.904  50.153  58.414  1.00 67.79  ?  309 ALA E N   1 
ATOM   7235 C CA  . ALA E 3 309 ? -8.064  49.757  59.234  1.00 73.25  ?  309 ALA E CA  1 
ATOM   7236 C C   . ALA E 3 309 ? -9.352  50.358  58.688  1.00 72.06  ?  309 ALA E C   1 
ATOM   7237 O O   . ALA E 3 309 ? -9.293  51.384  58.013  1.00 71.27  ?  309 ALA E O   1 
ATOM   7238 C CB  . ALA E 3 309 ? -7.839  50.191  60.646  1.00 76.15  ?  309 ALA E CB  1 
ATOM   7239 N N   . SER E 3 310 ? -10.469 49.693  58.955  1.00 74.72  ?  310 SER E N   1 
ATOM   7240 C CA  . SER E 3 310 ? -11.775 50.271  58.560  1.00 85.39  ?  310 SER E CA  1 
ATOM   7241 C C   . SER E 3 310 ? -12.825 49.944  59.615  1.00 87.16  ?  310 SER E C   1 
ATOM   7242 O O   . SER E 3 310 ? -12.645 48.962  60.354  1.00 78.09  ?  310 SER E O   1 
ATOM   7243 C CB  . SER E 3 310 ? -12.237 49.822  57.213  1.00 86.03  ?  310 SER E CB  1 
ATOM   7244 O OG  . SER E 3 310 ? -13.473 50.439  56.895  1.00 86.22  ?  310 SER E OG  1 
ATOM   7245 N N   . ASP E 3 311 ? -13.878 50.755  59.654  1.00 88.52  ?  311 ASP E N   1 
ATOM   7246 C CA  . ASP E 3 311 ? -14.972 50.548  60.628  1.00 90.60  ?  311 ASP E CA  1 
ATOM   7247 C C   . ASP E 3 311 ? -16.096 49.849  59.896  1.00 88.53  ?  311 ASP E C   1 
ATOM   7248 O O   . ASP E 3 311 ? -17.102 49.529  60.531  1.00 92.78  ?  311 ASP E O   1 
ATOM   7249 C CB  . ASP E 3 311 ? -15.477 51.893  61.138  1.00 92.56  ?  311 ASP E CB  1 
ATOM   7250 C CG  . ASP E 3 311 ? -15.554 52.931  60.040  1.00 91.87  ?  311 ASP E CG  1 
ATOM   7251 O OD1 . ASP E 3 311 ? -15.601 52.525  58.871  1.00 93.80  ?  311 ASP E OD1 1 
ATOM   7252 O OD2 . ASP E 3 311 ? -15.562 54.128  60.367  1.00 90.79  ?  311 ASP E OD2 1 
ATOM   7253 N N   . GLY E 3 312 ? -15.911 49.635  58.602  1.00 89.56  ?  312 GLY E N   1 
ATOM   7254 C CA  . GLY E 3 312 ? -16.988 49.065  57.784  1.00 94.44  ?  312 GLY E CA  1 
ATOM   7255 C C   . GLY E 3 312 ? -17.352 50.065  56.712  1.00 95.00  ?  312 GLY E C   1 
ATOM   7256 O O   . GLY E 3 312 ? -17.763 49.647  55.624  1.00 101.07 ?  312 GLY E O   1 
ATOM   7257 N N   . ASN E 3 313 ? -17.170 51.345  57.008  1.00 91.30  ?  313 ASN E N   1 
ATOM   7258 C CA  . ASN E 3 313 ? -17.481 52.400  56.020  1.00 96.38  ?  313 ASN E CA  1 
ATOM   7259 C C   . ASN E 3 313 ? -16.238 53.241  55.795  1.00 94.07  ?  313 ASN E C   1 
ATOM   7260 O O   . ASN E 3 313 ? -15.789 53.337  54.643  1.00 93.77  ?  313 ASN E O   1 
ATOM   7261 C CB  . ASN E 3 313 ? -18.604 53.317  56.497  1.00 96.59  ?  313 ASN E CB  1 
ATOM   7262 C CG  . ASN E 3 313 ? -18.981 54.367  55.474  1.00 96.94  ?  313 ASN E CG  1 
ATOM   7263 O OD1 . ASN E 3 313 ? -18.925 55.561  55.751  1.00 99.27  ?  313 ASN E OD1 1 
ATOM   7264 N ND2 . ASN E 3 313 ? -19.369 53.929  54.289  1.00 93.53  ?  313 ASN E ND2 1 
ATOM   7265 N N   . ASN E 3 314 ? -15.727 53.830  56.866  1.00 90.59  ?  314 ASN E N   1 
ATOM   7266 C CA  . ASN E 3 314 ? -14.564 54.733  56.723  1.00 93.17  ?  314 ASN E CA  1 
ATOM   7267 C C   . ASN E 3 314 ? -13.280 53.903  56.733  1.00 90.41  ?  314 ASN E C   1 
ATOM   7268 O O   . ASN E 3 314 ? -13.236 52.878  57.430  1.00 85.64  ?  314 ASN E O   1 
ATOM   7269 C CB  . ASN E 3 314 ? -14.596 55.850  57.765  1.00 91.02  ?  314 ASN E CB  1 
ATOM   7270 C CG  . ASN E 3 314 ? -15.369 57.062  57.297  1.00 94.91  ?  314 ASN E CG  1 
ATOM   7271 O OD1 . ASN E 3 314 ? -16.465 57.328  57.782  1.00 98.24  ?  314 ASN E OD1 1 
ATOM   7272 N ND2 . ASN E 3 314 ? -14.805 57.799  56.356  1.00 93.38  ?  314 ASN E ND2 1 
ATOM   7273 N N   . THR E 3 315 ? -12.294 54.335  55.951  1.00 87.38  ?  315 THR E N   1 
ATOM   7274 C CA  . THR E 3 315 ? -10.998 53.631  55.891  1.00 81.35  ?  315 THR E CA  1 
ATOM   7275 C C   . THR E 3 315 ? -9.936  54.489  56.553  1.00 81.67  ?  315 THR E C   1 
ATOM   7276 O O   . THR E 3 315 ? -10.054 55.719  56.515  1.00 82.68  ?  315 THR E O   1 
ATOM   7277 C CB  . THR E 3 315 ? -10.540 53.387  54.454  1.00 79.74  ?  315 THR E CB  1 
ATOM   7278 O OG1 . THR E 3 315 ? -9.783  54.523  54.037  1.00 81.31  ?  315 THR E OG1 1 
ATOM   7279 C CG2 . THR E 3 315 ? -11.689 53.159  53.498  1.00 83.40  ?  315 THR E CG2 1 
ATOM   7280 N N   . SER E 3 316 ? -8.915  53.837  57.086  1.00 80.83  ?  316 SER E N   1 
ATOM   7281 C CA  . SER E 3 316 ? -7.832  54.563  57.773  1.00 79.24  ?  316 SER E CA  1 
ATOM   7282 C C   . SER E 3 316 ? -6.718  54.892  56.804  1.00 75.75  ?  316 SER E C   1 
ATOM   7283 O O   . SER E 3 316 ? -6.564  54.196  55.811  1.00 72.08  ?  316 SER E O   1 
ATOM   7284 C CB  . SER E 3 316 ? -7.281  53.729  58.883  1.00 79.73  ?  316 SER E CB  1 
ATOM   7285 O OG  . SER E 3 316 ? -6.171  52.965  58.443  1.00 77.26  ?  316 SER E OG  1 
ATOM   7286 N N   . PHE E 3 317 ? -5.979  55.938  57.109  1.00 77.60  ?  317 PHE E N   1 
ATOM   7287 C CA  . PHE E 3 317 ? -4.776  56.210  56.315  1.00 77.93  ?  317 PHE E CA  1 
ATOM   7288 C C   . PHE E 3 317 ? -3.912  54.961  56.437  1.00 75.86  ?  317 PHE E C   1 
ATOM   7289 O O   . PHE E 3 317 ? -4.107  54.175  57.375  1.00 70.98  ?  317 PHE E O   1 
ATOM   7290 C CB  . PHE E 3 317 ? -4.044  57.406  56.908  1.00 78.02  ?  317 PHE E CB  1 
ATOM   7291 C CG  . PHE E 3 317 ? -4.678  58.747  56.659  1.00 81.58  ?  317 PHE E CG  1 
ATOM   7292 C CD1 . PHE E 3 317 ? -4.357  59.481  55.531  1.00 84.59  ?  317 PHE E CD1 1 
ATOM   7293 C CD2 . PHE E 3 317 ? -5.576  59.282  57.564  1.00 87.57  ?  317 PHE E CD2 1 
ATOM   7294 C CE1 . PHE E 3 317 ? -4.935  60.719  55.304  1.00 88.55  ?  317 PHE E CE1 1 
ATOM   7295 C CE2 . PHE E 3 317 ? -6.152  60.520  57.336  1.00 87.83  ?  317 PHE E CE2 1 
ATOM   7296 C CZ  . PHE E 3 317 ? -5.833  61.236  56.207  1.00 83.27  ?  317 PHE E CZ  1 
ATOM   7297 N N   . TRP E 3 318 ? -2.943  54.813  55.548  1.00 71.30  ?  318 TRP E N   1 
ATOM   7298 C CA  . TRP E 3 318 ? -2.131  53.575  55.543  1.00 70.32  ?  318 TRP E CA  1 
ATOM   7299 C C   . TRP E 3 318 ? -1.017  53.678  56.576  1.00 68.98  ?  318 TRP E C   1 
ATOM   7300 O O   . TRP E 3 318 ? -0.504  54.776  56.792  1.00 69.88  ?  318 TRP E O   1 
ATOM   7301 C CB  . TRP E 3 318 ? -1.584  53.306  54.134  1.00 69.86  ?  318 TRP E CB  1 
ATOM   7302 C CG  . TRP E 3 318 ? -2.476  52.478  53.265  1.00 64.03  ?  318 TRP E CG  1 
ATOM   7303 C CD1 . TRP E 3 318 ? -3.200  52.903  52.191  1.00 61.12  ?  318 TRP E CD1 1 
ATOM   7304 C CD2 . TRP E 3 318 ? -2.735  51.071  53.390  1.00 58.87  ?  318 TRP E CD2 1 
ATOM   7305 N NE1 . TRP E 3 318 ? -3.894  51.860  51.646  1.00 61.41  ?  318 TRP E NE1 1 
ATOM   7306 C CE2 . TRP E 3 318 ? -3.629  50.725  52.359  1.00 55.20  ?  318 TRP E CE2 1 
ATOM   7307 C CE3 . TRP E 3 318 ? -2.305  50.077  54.270  1.00 60.26  ?  318 TRP E CE3 1 
ATOM   7308 C CZ2 . TRP E 3 318 ? -4.101  49.429  52.192  1.00 58.53  ?  318 TRP E CZ2 1 
ATOM   7309 C CZ3 . TRP E 3 318 ? -2.767  48.794  54.100  1.00 59.14  ?  318 TRP E CZ3 1 
ATOM   7310 C CH2 . TRP E 3 318 ? -3.655  48.478  53.077  1.00 60.58  ?  318 TRP E CH2 1 
ATOM   7311 N N   . SER E 3 319 ? -0.665  52.550  57.173  1.00 65.88  ?  319 SER E N   1 
ATOM   7312 C CA  . SER E 3 319 ? 0.403   52.522  58.191  1.00 67.10  ?  319 SER E CA  1 
ATOM   7313 C C   . SER E 3 319 ? 1.719   52.912  57.555  1.00 70.41  ?  319 SER E C   1 
ATOM   7314 O O   . SER E 3 319 ? 1.772   53.068  56.338  1.00 73.75  ?  319 SER E O   1 
ATOM   7315 C CB  . SER E 3 319 ? 0.521   51.164  58.771  1.00 65.35  ?  319 SER E CB  1 
ATOM   7316 O OG  . SER E 3 319 ? 1.472   50.396  58.057  1.00 69.80  ?  319 SER E OG  1 
ATOM   7317 N N   . GLU E 3 320 ? 2.738   53.085  58.374  1.00 67.54  ?  320 GLU E N   1 
ATOM   7318 C CA  . GLU E 3 320 ? 4.073   53.344  57.811  1.00 71.13  ?  320 GLU E CA  1 
ATOM   7319 C C   . GLU E 3 320 ? 4.536   52.060  57.133  1.00 72.20  ?  320 GLU E C   1 
ATOM   7320 O O   . GLU E 3 320 ? 4.342   50.995  57.716  1.00 69.21  ?  320 GLU E O   1 
ATOM   7321 C CB  . GLU E 3 320 ? 5.017   53.737  58.944  1.00 75.33  ?  320 GLU E CB  1 
ATOM   7322 C CG  . GLU E 3 320 ? 6.352   54.277  58.471  1.00 83.14  ?  320 GLU E CG  1 
ATOM   7323 C CD  . GLU E 3 320 ? 7.401   54.336  59.567  1.00 91.95  ?  320 GLU E CD  1 
ATOM   7324 O OE1 . GLU E 3 320 ? 7.066   53.991  60.710  1.00 97.63  ?  320 GLU E OE1 1 
ATOM   7325 O OE2 . GLU E 3 320 ? 8.547   54.726  59.274  1.00 91.25  ?  320 GLU E OE2 1 
ATOM   7326 N N   . GLU E 3 321 ? 5.116   52.172  55.946  1.00 71.62  ?  321 GLU E N   1 
ATOM   7327 C CA  . GLU E 3 321 ? 5.652   50.995  55.230  1.00 64.63  ?  321 GLU E CA  1 
ATOM   7328 C C   . GLU E 3 321 ? 6.947   50.534  55.904  1.00 61.53  ?  321 GLU E C   1 
ATOM   7329 O O   . GLU E 3 321 ? 7.819   51.369  56.126  1.00 69.77  ?  321 GLU E O   1 
ATOM   7330 C CB  . GLU E 3 321 ? 5.851   51.357  53.762  1.00 59.26  ?  321 GLU E CB  1 
ATOM   7331 C CG  . GLU E 3 321 ? 4.579   51.854  53.107  1.00 67.12  ?  321 GLU E CG  1 
ATOM   7332 C CD  . GLU E 3 321 ? 4.777   52.685  51.854  1.00 68.98  ?  321 GLU E CD  1 
ATOM   7333 O OE1 . GLU E 3 321 ? 5.924   52.774  51.385  1.00 63.61  ?  321 GLU E OE1 1 
ATOM   7334 O OE2 . GLU E 3 321 ? 3.780   53.241  51.352  1.00 62.71  ?  321 GLU E OE2 1 
ATOM   7335 N N   . ILE E 3 322 ? 7.041   49.250  56.228  1.00 59.32  ?  322 ILE E N   1 
ATOM   7336 C CA  . ILE E 3 322 ? 8.263   48.672  56.842  1.00 60.09  ?  322 ILE E CA  1 
ATOM   7337 C C   . ILE E 3 322 ? 8.997   47.858  55.783  1.00 61.58  ?  322 ILE E C   1 
ATOM   7338 O O   . ILE E 3 322 ? 8.322   47.187  55.004  1.00 55.88  ?  322 ILE E O   1 
ATOM   7339 C CB  . ILE E 3 322 ? 7.876   47.791  58.032  1.00 57.79  ?  322 ILE E CB  1 
ATOM   7340 C CG1 . ILE E 3 322 ? 6.575   47.039  57.763  1.00 61.51  ?  322 ILE E CG1 1 
ATOM   7341 C CG2 . ILE E 3 322 ? 7.794   48.619  59.301  1.00 66.84  ?  322 ILE E CG2 1 
ATOM   7342 C CD1 . ILE E 3 322 ? 6.489   45.721  58.471  1.00 64.52  ?  322 ILE E CD1 1 
ATOM   7343 N N   . LYS E 3 323 ? 10.326  47.934  55.768  1.00 60.09  ?  323 LYS E N   1 
ATOM   7344 C CA  . LYS E 3 323 ? 11.148  47.161  54.810  1.00 54.45  ?  323 LYS E CA  1 
ATOM   7345 C C   . LYS E 3 323 ? 11.650  45.907  55.505  1.00 60.28  ?  323 LYS E C   1 
ATOM   7346 O O   . LYS E 3 323 ? 11.916  45.975  56.699  1.00 65.45  ?  323 LYS E O   1 
ATOM   7347 C CB  . LYS E 3 323 ? 12.317  47.994  54.300  1.00 53.33  ?  323 LYS E CB  1 
ATOM   7348 C CG  . LYS E 3 323 ? 13.164  47.350  53.216  1.00 60.22  ?  323 LYS E CG  1 
ATOM   7349 C CD  . LYS E 3 323 ? 13.814  48.360  52.303  1.00 55.72  ?  323 LYS E CD  1 
ATOM   7350 C CE  . LYS E 3 323 ? 15.264  48.617  52.641  1.00 66.97  ?  323 LYS E CE  1 
ATOM   7351 N NZ  . LYS E 3 323 ? 15.976  49.267  51.517  1.00 71.42  ?  323 LYS E NZ  1 
ATOM   7352 N N   . PHE E 3 324 ? 11.784  44.816  54.760  1.00 58.38  ?  324 PHE E N   1 
ATOM   7353 C CA  . PHE E 3 324 ? 12.156  43.533  55.387  1.00 58.89  ?  324 PHE E CA  1 
ATOM   7354 C C   . PHE E 3 324 ? 12.973  42.678  54.420  1.00 62.94  ?  324 PHE E C   1 
ATOM   7355 O O   . PHE E 3 324 ? 12.633  42.642  53.238  1.00 57.26  ?  324 PHE E O   1 
ATOM   7356 C CB  . PHE E 3 324 ? 10.858  42.851  55.814  1.00 65.14  ?  324 PHE E CB  1 
ATOM   7357 C CG  . PHE E 3 324 ? 10.976  41.417  56.247  1.00 74.72  ?  324 PHE E CG  1 
ATOM   7358 C CD1 . PHE E 3 324 ? 11.987  41.013  57.099  1.00 80.82  ?  324 PHE E CD1 1 
ATOM   7359 C CD2 . PHE E 3 324 ? 10.060  40.478  55.813  1.00 67.26  ?  324 PHE E CD2 1 
ATOM   7360 C CE1 . PHE E 3 324 ? 12.086  39.693  57.501  1.00 83.58  ?  324 PHE E CE1 1 
ATOM   7361 C CE2 . PHE E 3 324 ? 10.158  39.159  56.218  1.00 74.26  ?  324 PHE E CE2 1 
ATOM   7362 C CZ  . PHE E 3 324 ? 11.172  38.770  57.058  1.00 80.92  ?  324 PHE E CZ  1 
ATOM   7363 N N   . ASP E 3 325 ? 14.028  42.029  54.920  1.00 67.29  ?  325 ASP E N   1 
ATOM   7364 C CA  . ASP E 3 325 ? 14.830  41.085  54.100  1.00 64.98  ?  325 ASP E CA  1 
ATOM   7365 C C   . ASP E 3 325 ? 14.445  39.675  54.522  1.00 68.28  ?  325 ASP E C   1 
ATOM   7366 O O   . ASP E 3 325 ? 14.604  39.347  55.694  1.00 68.73  ?  325 ASP E O   1 
ATOM   7367 C CB  . ASP E 3 325 ? 16.332  41.298  54.257  1.00 62.51  ?  325 ASP E CB  1 
ATOM   7368 C CG  . ASP E 3 325 ? 17.168  40.459  53.313  1.00 69.23  ?  325 ASP E CG  1 
ATOM   7369 O OD1 . ASP E 3 325 ? 17.323  40.869  52.153  1.00 70.98  ?  325 ASP E OD1 1 
ATOM   7370 O OD2 . ASP E 3 325 ? 17.661  39.408  53.750  1.00 79.26  ?  325 ASP E OD2 1 
ATOM   7371 N N   . THR E 3 326 ? 13.977  38.878  53.581  1.00 64.17  ?  326 THR E N   1 
ATOM   7372 C CA  . THR E 3 326 ? 13.491  37.533  53.923  1.00 65.94  ?  326 THR E CA  1 
ATOM   7373 C C   . THR E 3 326 ? 14.667  36.568  53.994  1.00 74.41  ?  326 THR E C   1 
ATOM   7374 O O   . THR E 3 326 ? 14.485  35.481  54.541  1.00 70.93  ?  326 THR E O   1 
ATOM   7375 C CB  . THR E 3 326 ? 12.458  37.089  52.893  1.00 62.55  ?  326 THR E CB  1 
ATOM   7376 O OG1 . THR E 3 326 ? 13.049  37.225  51.603  1.00 65.28  ?  326 THR E OG1 1 
ATOM   7377 C CG2 . THR E 3 326 ? 11.186  37.901  52.965  1.00 59.70  ?  326 THR E CG2 1 
ATOM   7378 N N   . GLU E 3 327 ? 15.829  36.953  53.482  1.00 76.15  ?  327 GLU E N   1 
ATOM   7379 C CA  . GLU E 3 327 ? 16.933  36.017  53.605  1.00 83.03  ?  327 GLU E CA  1 
ATOM   7380 C C   . GLU E 3 327 ? 17.508  36.061  55.008  1.00 90.74  ?  327 GLU E C   1 
ATOM   7381 O O   . GLU E 3 327 ? 17.765  35.005  55.595  1.00 96.05  ?  327 GLU E O   1 
ATOM   7382 C CB  . GLU E 3 327 ? 18.021  36.314  52.573  1.00 82.39  ?  327 GLU E CB  1 
ATOM   7383 C CG  . GLU E 3 327 ? 19.088  35.227  52.475  1.00 89.92  ?  327 GLU E CG  1 
ATOM   7384 C CD  . GLU E 3 327 ? 20.153  35.542  51.442  1.00 96.59  ?  327 GLU E CD  1 
ATOM   7385 O OE1 . GLU E 3 327 ? 19.789  35.980  50.333  1.00 97.62  ?  327 GLU E OE1 1 
ATOM   7386 O OE2 . GLU E 3 327 ? 21.354  35.359  51.744  1.00 96.46  ?  327 GLU E OE2 1 
ATOM   7387 N N   . ILE E 3 328 ? 17.776  37.268  55.491  1.00 89.41  ?  328 ILE E N   1 
ATOM   7388 C CA  . ILE E 3 328 ? 18.452  37.393  56.812  1.00 95.19  ?  328 ILE E CA  1 
ATOM   7389 C C   . ILE E 3 328 ? 19.968  37.211  56.917  1.00 104.21 ?  328 ILE E C   1 
ATOM   7390 O O   . ILE E 3 328 ? 20.452  36.986  58.039  1.00 103.40 ?  328 ILE E O   1 
ATOM   7391 C CB  . ILE E 3 328 ? 17.631  36.727  57.931  1.00 91.66  ?  328 ILE E CB  1 
ATOM   7392 C CG1 . ILE E 3 328 ? 16.306  37.459  58.161  1.00 84.87  ?  328 ILE E CG1 1 
ATOM   7393 C CG2 . ILE E 3 328 ? 18.450  36.623  59.207  1.00 91.21  ?  328 ILE E CG2 1 
ATOM   7394 C CD1 . ILE E 3 328 ? 15.336  36.725  59.050  1.00 75.26  ?  328 ILE E CD1 1 
ATOM   7395 N N   . GLN E 3 329 ? 20.662  37.216  55.769  1.00 106.01 ?  329 GLN E N   1 
ATOM   7396 C CA  . GLN E 3 329 ? 22.147  37.096  55.701  1.00 106.26 ?  329 GLN E CA  1 
ATOM   7397 C C   . GLN E 3 329 ? 22.234  35.884  54.767  1.00 106.04 ?  329 GLN E C   1 
ATOM   7398 O O   . GLN E 3 329 ? 23.022  35.966  53.811  1.00 100.30 ?  329 GLN E O   1 
ATOM   7399 C CB  . GLN E 3 329 ? 22.859  36.861  57.036  1.00 108.55 ?  329 GLN E CB  1 
ATOM   7400 C CG  . GLN E 3 329 ? 22.758  38.046  57.988  1.00 116.86 ?  329 GLN E CG  1 
ATOM   7401 C CD  . GLN E 3 329 ? 24.073  38.408  58.633  1.00 124.75 ?  329 GLN E CD  1 
ATOM   7402 O OE1 . GLN E 3 329 ? 24.613  37.662  59.447  1.00 126.25 ?  329 GLN E OE1 1 
ATOM   7403 N NE2 . GLN E 3 329 ? 24.595  39.570  58.279  1.00 116.03 ?  329 GLN E NE2 1 
ATOM   7404 N N   . GLU F 3 228 ? -2.133  -30.110 16.473  1.00 88.54  ?  228 GLU F N   1 
ATOM   7405 C CA  . GLU F 3 228 ? -2.670  -30.792 15.300  1.00 95.64  ?  228 GLU F CA  1 
ATOM   7406 C C   . GLU F 3 228 ? -2.191  -30.172 13.994  1.00 95.24  ?  228 GLU F C   1 
ATOM   7407 O O   . GLU F 3 228 ? -1.814  -30.882 13.058  1.00 94.66  ?  228 GLU F O   1 
ATOM   7408 C CB  . GLU F 3 228 ? -4.196  -30.780 15.327  1.00 100.23 ?  228 GLU F CB  1 
ATOM   7409 C CG  . GLU F 3 228 ? -4.821  -31.642 14.251  1.00 103.14 ?  228 GLU F CG  1 
ATOM   7410 C CD  . GLU F 3 228 ? -6.322  -31.488 14.195  1.00 111.00 ?  228 GLU F CD  1 
ATOM   7411 O OE1 . GLU F 3 228 ? -6.913  -31.812 13.144  1.00 114.26 ?  228 GLU F OE1 1 
ATOM   7412 O OE2 . GLU F 3 228 ? -6.909  -31.027 15.197  1.00 111.26 ?  228 GLU F OE2 1 
ATOM   7413 N N   . LEU F 3 229 ? -2.219  -28.844 13.935  1.00 87.23  ?  229 LEU F N   1 
ATOM   7414 C CA  . LEU F 3 229 ? -1.815  -28.136 12.737  1.00 83.70  ?  229 LEU F CA  1 
ATOM   7415 C C   . LEU F 3 229 ? -0.296  -28.231 12.572  1.00 83.84  ?  229 LEU F C   1 
ATOM   7416 O O   . LEU F 3 229 ? 0.429   -28.463 13.544  1.00 83.73  ?  229 LEU F O   1 
ATOM   7417 C CB  . LEU F 3 229 ? -2.271  -26.681 12.825  1.00 84.93  ?  229 LEU F CB  1 
ATOM   7418 C CG  . LEU F 3 229 ? -3.785  -26.441 12.742  1.00 89.78  ?  229 LEU F CG  1 
ATOM   7419 C CD1 . LEU F 3 229 ? -4.118  -24.955 12.647  1.00 85.44  ?  229 LEU F CD1 1 
ATOM   7420 C CD2 . LEU F 3 229 ? -4.404  -27.215 11.593  1.00 96.23  ?  229 LEU F CD2 1 
ATOM   7421 N N   . PRO F 3 230 ? 0.216   -28.057 11.349  1.00 84.89  ?  230 PRO F N   1 
ATOM   7422 C CA  . PRO F 3 230 ? 1.663   -28.150 11.151  1.00 82.20  ?  230 PRO F CA  1 
ATOM   7423 C C   . PRO F 3 230 ? 2.377   -26.953 11.762  1.00 83.86  ?  230 PRO F C   1 
ATOM   7424 O O   . PRO F 3 230 ? 1.809   -25.852 11.842  1.00 80.32  ?  230 PRO F O   1 
ATOM   7425 C CB  . PRO F 3 230 ? 1.810   -28.163 9.619   1.00 82.83  ?  230 PRO F CB  1 
ATOM   7426 C CG  . PRO F 3 230 ? 0.619   -27.409 9.137   1.00 88.51  ?  230 PRO F CG  1 
ATOM   7427 C CD  . PRO F 3 230 ? -0.496  -27.788 10.086  1.00 87.24  ?  230 PRO F CD  1 
ATOM   7428 N N   . PRO F 3 231 ? 3.624   -27.124 12.193  1.00 82.35  ?  231 PRO F N   1 
ATOM   7429 C CA  . PRO F 3 231 ? 4.358   -26.006 12.793  1.00 73.47  ?  231 PRO F CA  1 
ATOM   7430 C C   . PRO F 3 231 ? 4.949   -25.119 11.714  1.00 71.27  ?  231 PRO F C   1 
ATOM   7431 O O   . PRO F 3 231 ? 5.297   -25.608 10.630  1.00 71.76  ?  231 PRO F O   1 
ATOM   7432 C CB  . PRO F 3 231 ? 5.457   -26.706 13.600  1.00 74.00  ?  231 PRO F CB  1 
ATOM   7433 C CG  . PRO F 3 231 ? 5.730   -27.943 12.813  1.00 76.25  ?  231 PRO F CG  1 
ATOM   7434 C CD  . PRO F 3 231 ? 4.398   -28.377 12.239  1.00 77.56  ?  231 PRO F CD  1 
ATOM   7435 N N   . PRO F 3 232 ? 5.075   -23.815 11.968  1.00 76.63  ?  232 PRO F N   1 
ATOM   7436 C CA  . PRO F 3 232 ? 5.721   -22.927 10.990  1.00 79.60  ?  232 PRO F CA  1 
ATOM   7437 C C   . PRO F 3 232 ? 7.192   -23.278 10.794  1.00 79.33  ?  232 PRO F C   1 
ATOM   7438 O O   . PRO F 3 232 ? 7.809   -23.960 11.616  1.00 78.83  ?  232 PRO F O   1 
ATOM   7439 C CB  . PRO F 3 232 ? 5.556   -21.533 11.612  1.00 73.79  ?  232 PRO F CB  1 
ATOM   7440 C CG  . PRO F 3 232 ? 4.429   -21.684 12.603  1.00 69.15  ?  232 PRO F CG  1 
ATOM   7441 C CD  . PRO F 3 232 ? 4.539   -23.078 13.124  1.00 69.15  ?  232 PRO F CD  1 
ATOM   7442 N N   . GLU F 3 233 ? 7.765   -22.797 9.685   1.00 76.47  ?  233 GLU F N   1 
ATOM   7443 C CA  . GLU F 3 233 ? 9.117   -23.192 9.308   1.00 87.22  ?  233 GLU F CA  1 
ATOM   7444 C C   . GLU F 3 233 ? 9.899   -21.995 8.790   1.00 89.63  ?  233 GLU F C   1 
ATOM   7445 O O   . GLU F 3 233 ? 9.336   -20.956 8.433   1.00 83.79  ?  233 GLU F O   1 
ATOM   7446 C CB  . GLU F 3 233 ? 9.177   -24.246 8.193   1.00 96.95  ?  233 GLU F CB  1 
ATOM   7447 C CG  . GLU F 3 233 ? 8.532   -23.803 6.884   1.00 102.73 ?  233 GLU F CG  1 
ATOM   7448 C CD  . GLU F 3 233 ? 8.639   -24.852 5.790   1.00 113.42 ?  233 GLU F CD  1 
ATOM   7449 O OE1 . GLU F 3 233 ? 9.305   -25.885 6.020   1.00 114.73 ?  233 GLU F OE1 1 
ATOM   7450 O OE2 . GLU F 3 233 ? 8.087   -24.627 4.690   1.00 121.52 ?  233 GLU F OE2 1 
ATOM   7451 N N   . ASN F 3 234 ? 11.222  -22.181 8.735   1.00 89.83  ?  234 ASN F N   1 
ATOM   7452 C CA  . ASN F 3 234 ? 12.162  -21.215 8.171   1.00 87.12  ?  234 ASN F CA  1 
ATOM   7453 C C   . ASN F 3 234 ? 12.038  -19.862 8.871   1.00 82.50  ?  234 ASN F C   1 
ATOM   7454 O O   . ASN F 3 234 ? 11.801  -18.822 8.255   1.00 80.88  ?  234 ASN F O   1 
ATOM   7455 C CB  . ASN F 3 234 ? 11.969  -21.088 6.657   1.00 93.52  ?  234 ASN F CB  1 
ATOM   7456 C CG  . ASN F 3 234 ? 12.147  -22.412 5.939   1.00 100.43 ?  234 ASN F CG  1 
ATOM   7457 O OD1 . ASN F 3 234 ? 12.819  -23.316 6.438   1.00 98.33  ?  234 ASN F OD1 1 
ATOM   7458 N ND2 . ASN F 3 234 ? 11.545  -22.534 4.760   1.00 106.80 ?  234 ASN F ND2 1 
ATOM   7459 N N   . ILE F 3 235 ? 12.219  -19.903 10.183  1.00 82.25  ?  235 ILE F N   1 
ATOM   7460 C CA  . ILE F 3 235 ? 12.109  -18.711 11.012  1.00 85.13  ?  235 ILE F CA  1 
ATOM   7461 C C   . ILE F 3 235 ? 13.418  -17.938 10.923  1.00 83.92  ?  235 ILE F C   1 
ATOM   7462 O O   . ILE F 3 235 ? 14.498  -18.498 11.146  1.00 80.57  ?  235 ILE F O   1 
ATOM   7463 C CB  . ILE F 3 235 ? 11.767  -19.089 12.462  1.00 82.05  ?  235 ILE F CB  1 
ATOM   7464 C CG1 . ILE F 3 235 ? 10.464  -19.897 12.520  1.00 83.15  ?  235 ILE F CG1 1 
ATOM   7465 C CG2 . ILE F 3 235 ? 11.603  -17.860 13.291  1.00 80.40  ?  235 ILE F CG2 1 
ATOM   7466 C CD1 . ILE F 3 235 ? 10.640  -21.401 12.548  1.00 83.68  ?  235 ILE F CD1 1 
ATOM   7467 N N   . GLU F 3 236 ? 13.327  -16.647 10.596  1.00 82.37  ?  236 GLU F N   1 
ATOM   7468 C CA  . GLU F 3 236 ? 14.511  -15.821 10.408  1.00 80.71  ?  236 GLU F CA  1 
ATOM   7469 C C   . GLU F 3 236 ? 14.281  -14.439 11.001  1.00 79.02  ?  236 GLU F C   1 
ATOM   7470 O O   . GLU F 3 236 ? 13.206  -13.854 10.838  1.00 75.67  ?  236 GLU F O   1 
ATOM   7471 C CB  . GLU F 3 236 ? 14.863  -15.704 8.915   1.00 82.31  ?  236 GLU F CB  1 
ATOM   7472 C CG  . GLU F 3 236 ? 15.398  -16.997 8.295   1.00 93.33  ?  236 GLU F CG  1 
ATOM   7473 C CD  . GLU F 3 236 ? 16.061  -16.782 6.945   1.00 99.66  ?  236 GLU F CD  1 
ATOM   7474 O OE1 . GLU F 3 236 ? 15.663  -15.842 6.225   1.00 104.00 ?  236 GLU F OE1 1 
ATOM   7475 O OE2 . GLU F 3 236 ? 16.973  -17.564 6.596   1.00 96.11  ?  236 GLU F OE2 1 
ATOM   7476 N N   . VAL F 3 237 ? 15.305  -13.908 11.667  1.00 80.60  ?  237 VAL F N   1 
ATOM   7477 C CA  . VAL F 3 237 ? 15.261  -12.580 12.268  1.00 76.27  ?  237 VAL F CA  1 
ATOM   7478 C C   . VAL F 3 237 ? 16.161  -11.640 11.479  1.00 71.61  ?  237 VAL F C   1 
ATOM   7479 O O   . VAL F 3 237 ? 17.226  -12.040 10.997  1.00 75.11  ?  237 VAL F O   1 
ATOM   7480 C CB  . VAL F 3 237 ? 15.691  -12.618 13.746  1.00 76.64  ?  237 VAL F CB  1 
ATOM   7481 C CG1 . VAL F 3 237 ? 15.142  -11.414 14.486  1.00 79.55  ?  237 VAL F CG1 1 
ATOM   7482 C CG2 . VAL F 3 237 ? 15.239  -13.905 14.395  1.00 78.87  ?  237 VAL F CG2 1 
ATOM   7483 N N   . SER F 3 238 ? 15.733  -10.387 11.359  1.00 77.38  ?  238 SER F N   1 
ATOM   7484 C CA  . SER F 3 238 ? 16.531  -9.348  10.722  1.00 78.00  ?  238 SER F CA  1 
ATOM   7485 C C   . SER F 3 238 ? 16.287  -8.031  11.446  1.00 81.77  ?  238 SER F C   1 
ATOM   7486 O O   . SER F 3 238 ? 15.386  -7.918  12.281  1.00 83.65  ?  238 SER F O   1 
ATOM   7487 C CB  . SER F 3 238 ? 16.202  -9.212  9.229   1.00 82.01  ?  238 SER F CB  1 
ATOM   7488 O OG  . SER F 3 238 ? 14.855  -8.814  9.029   1.00 84.09  ?  238 SER F OG  1 
ATOM   7489 N N   . VAL F 3 239 ? 17.088  -7.018  11.111  1.00 86.48  ?  239 VAL F N   1 
ATOM   7490 C CA  . VAL F 3 239 ? 16.965  -5.687  11.697  1.00 78.97  ?  239 VAL F CA  1 
ATOM   7491 C C   . VAL F 3 239 ? 16.476  -4.727  10.624  1.00 81.89  ?  239 VAL F C   1 
ATOM   7492 O O   . VAL F 3 239 ? 16.903  -4.798  9.465   1.00 88.21  ?  239 VAL F O   1 
ATOM   7493 C CB  . VAL F 3 239 ? 18.285  -5.184  12.323  1.00 76.43  ?  239 VAL F CB  1 
ATOM   7494 C CG1 . VAL F 3 239 ? 18.771  -6.139  13.399  1.00 79.88  ?  239 VAL F CG1 1 
ATOM   7495 C CG2 . VAL F 3 239 ? 19.365  -4.968  11.264  1.00 76.23  ?  239 VAL F CG2 1 
ATOM   7496 N N   . GLN F 3 240 ? 15.542  -3.859  11.006  1.00 87.64  ?  240 GLN F N   1 
ATOM   7497 C CA  . GLN F 3 240 ? 15.020  -2.806  10.138  1.00 93.56  ?  240 GLN F CA  1 
ATOM   7498 C C   . GLN F 3 240 ? 14.866  -1.566  11.006  1.00 95.34  ?  240 GLN F C   1 
ATOM   7499 O O   . GLN F 3 240 ? 14.013  -1.538  11.901  1.00 92.67  ?  240 GLN F O   1 
ATOM   7500 C CB  . GLN F 3 240 ? 13.690  -3.205  9.497   1.00 95.93  ?  240 GLN F CB  1 
ATOM   7501 C CG  . GLN F 3 240 ? 13.793  -4.385  8.536   1.00 101.37 ?  240 GLN F CG  1 
ATOM   7502 C CD  . GLN F 3 240 ? 12.463  -4.749  7.896   1.00 107.58 ?  240 GLN F CD  1 
ATOM   7503 O OE1 . GLN F 3 240 ? 11.419  -4.181  8.230   1.00 107.50 ?  240 GLN F OE1 1 
ATOM   7504 N NE2 . GLN F 3 240 ? 12.495  -5.705  6.971   1.00 102.15 ?  240 GLN F NE2 1 
ATOM   7505 N N   . ASN F 3 241 ? 15.689  -0.552  10.742  1.00 99.78  ?  241 ASN F N   1 
ATOM   7506 C CA  . ASN F 3 241 ? 15.797  0.651   11.585  1.00 98.97  ?  241 ASN F CA  1 
ATOM   7507 C C   . ASN F 3 241 ? 16.117  0.146   12.992  1.00 95.29  ?  241 ASN F C   1 
ATOM   7508 O O   . ASN F 3 241 ? 17.061  -0.645  13.155  1.00 87.21  ?  241 ASN F O   1 
ATOM   7509 C CB  . ASN F 3 241 ? 14.544  1.529   11.475  1.00 100.24 ?  241 ASN F CB  1 
ATOM   7510 C CG  . ASN F 3 241 ? 14.210  1.916   10.047  1.00 103.40 ?  241 ASN F CG  1 
ATOM   7511 O OD1 . ASN F 3 241 ? 13.302  1.352   9.437   1.00 107.69 ?  241 ASN F OD1 1 
ATOM   7512 N ND2 . ASN F 3 241 ? 14.923  2.906   9.517   1.00 93.59  ?  241 ASN F ND2 1 
ATOM   7513 N N   . GLN F 3 242 ? 15.371  0.556   14.018  1.00 89.64  ?  242 GLN F N   1 
ATOM   7514 C CA  . GLN F 3 242 ? 15.560  0.100   15.388  1.00 81.79  ?  242 GLN F CA  1 
ATOM   7515 C C   . GLN F 3 242 ? 14.596  -1.016  15.769  1.00 82.07  ?  242 GLN F C   1 
ATOM   7516 O O   . GLN F 3 242 ? 14.218  -1.129  16.939  1.00 79.20  ?  242 GLN F O   1 
ATOM   7517 C CB  . GLN F 3 242 ? 15.421  1.279   16.345  1.00 81.91  ?  242 GLN F CB  1 
ATOM   7518 C CG  . GLN F 3 242 ? 16.595  2.228   16.295  1.00 78.38  ?  242 GLN F CG  1 
ATOM   7519 C CD  . GLN F 3 242 ? 16.207  3.610   16.745  1.00 74.29  ?  242 GLN F CD  1 
ATOM   7520 O OE1 . GLN F 3 242 ? 15.027  3.957   16.723  1.00 72.61  ?  242 GLN F OE1 1 
ATOM   7521 N NE2 . GLN F 3 242 ? 17.192  4.420   17.127  1.00 69.67  ?  242 GLN F NE2 1 
ATOM   7522 N N   . ASN F 3 243 ? 14.172  -1.832  14.806  1.00 83.31  ?  243 ASN F N   1 
ATOM   7523 C CA  . ASN F 3 243 ? 13.192  -2.879  15.053  1.00 76.71  ?  243 ASN F CA  1 
ATOM   7524 C C   . ASN F 3 243 ? 13.743  -4.229  14.616  1.00 80.29  ?  243 ASN F C   1 
ATOM   7525 O O   . ASN F 3 243 ? 14.581  -4.313  13.713  1.00 87.13  ?  243 ASN F O   1 
ATOM   7526 C CB  . ASN F 3 243 ? 11.872  -2.597  14.317  1.00 70.99  ?  243 ASN F CB  1 
ATOM   7527 C CG  . ASN F 3 243 ? 11.080  -1.479  14.954  1.00 67.09  ?  243 ASN F CG  1 
ATOM   7528 O OD1 . ASN F 3 243 ? 11.644  -0.580  15.571  1.00 75.34  ?  243 ASN F OD1 1 
ATOM   7529 N ND2 . ASN F 3 243 ? 9.761   -1.534  14.817  1.00 68.15  ?  243 ASN F ND2 1 
ATOM   7530 N N   . TYR F 3 244 ? 13.270  -5.286  15.276  1.00 74.65  ?  244 TYR F N   1 
ATOM   7531 C CA  . TYR F 3 244 ? 13.491  -6.656  14.842  1.00 75.73  ?  244 TYR F CA  1 
ATOM   7532 C C   . TYR F 3 244 ? 12.292  -7.122  14.029  1.00 74.74  ?  244 TYR F C   1 
ATOM   7533 O O   . TYR F 3 244 ? 11.141  -6.802  14.352  1.00 75.84  ?  244 TYR F O   1 
ATOM   7534 C CB  . TYR F 3 244 ? 13.700  -7.600  16.032  1.00 74.16  ?  244 TYR F CB  1 
ATOM   7535 C CG  . TYR F 3 244 ? 15.015  -7.456  16.783  1.00 72.91  ?  244 TYR F CG  1 
ATOM   7536 C CD1 . TYR F 3 244 ? 15.046  -7.494  18.173  1.00 67.12  ?  244 TYR F CD1 1 
ATOM   7537 C CD2 . TYR F 3 244 ? 16.223  -7.324  16.108  1.00 74.78  ?  244 TYR F CD2 1 
ATOM   7538 C CE1 . TYR F 3 244 ? 16.237  -7.379  18.870  1.00 67.37  ?  244 TYR F CE1 1 
ATOM   7539 C CE2 . TYR F 3 244 ? 17.423  -7.210  16.800  1.00 69.19  ?  244 TYR F CE2 1 
ATOM   7540 C CZ  . TYR F 3 244 ? 17.422  -7.238  18.180  1.00 70.59  ?  244 TYR F CZ  1 
ATOM   7541 O OH  . TYR F 3 244 ? 18.606  -7.127  18.877  1.00 70.07  ?  244 TYR F OH  1 
ATOM   7542 N N   . VAL F 3 245 ? 12.575  -7.875  12.970  1.00 75.81  ?  245 VAL F N   1 
ATOM   7543 C CA  . VAL F 3 245 ? 11.566  -8.428  12.077  1.00 76.91  ?  245 VAL F CA  1 
ATOM   7544 C C   . VAL F 3 245 ? 11.765  -9.933  12.038  1.00 77.38  ?  245 VAL F C   1 
ATOM   7545 O O   . VAL F 3 245 ? 12.819  -10.415 11.602  1.00 77.13  ?  245 VAL F O   1 
ATOM   7546 C CB  . VAL F 3 245 ? 11.656  -7.829  10.668  1.00 84.65  ?  245 VAL F CB  1 
ATOM   7547 C CG1 . VAL F 3 245 ? 10.733  -8.575  9.724   1.00 79.63  ?  245 VAL F CG1 1 
ATOM   7548 C CG2 . VAL F 3 245 ? 11.311  -6.351  10.706  1.00 88.68  ?  245 VAL F CG2 1 
ATOM   7549 N N   . LEU F 3 246 ? 10.766  -10.667 12.513  1.00 78.32  ?  246 LEU F N   1 
ATOM   7550 C CA  . LEU F 3 246 ? 10.775  -12.122 12.578  1.00 78.28  ?  246 LEU F CA  1 
ATOM   7551 C C   . LEU F 3 246 ? 9.837   -12.637 11.493  1.00 81.70  ?  246 LEU F C   1 
ATOM   7552 O O   . LEU F 3 246 ? 8.624   -12.415 11.564  1.00 77.88  ?  246 LEU F O   1 
ATOM   7553 C CB  . LEU F 3 246 ? 10.322  -12.581 13.961  1.00 72.93  ?  246 LEU F CB  1 
ATOM   7554 C CG  . LEU F 3 246 ? 10.294  -14.076 14.249  1.00 74.17  ?  246 LEU F CG  1 
ATOM   7555 C CD1 . LEU F 3 246 ? 11.706  -14.593 14.221  1.00 73.21  ?  246 LEU F CD1 1 
ATOM   7556 C CD2 . LEU F 3 246 ? 9.650   -14.345 15.589  1.00 69.56  ?  246 LEU F CD2 1 
ATOM   7557 N N   . LYS F 3 247 ? 10.390  -13.331 10.501  1.00 82.80  ?  247 LYS F N   1 
ATOM   7558 C CA  . LYS F 3 247 ? 9.625   -13.832 9.368   1.00 82.08  ?  247 LYS F CA  1 
ATOM   7559 C C   . LYS F 3 247 ? 9.639   -15.353 9.368   1.00 86.60  ?  247 LYS F C   1 
ATOM   7560 O O   . LYS F 3 247 ? 10.639  -15.977 9.738   1.00 87.00  ?  247 LYS F O   1 
ATOM   7561 C CB  . LYS F 3 247 ? 10.180  -13.304 8.035   1.00 86.23  ?  247 LYS F CB  1 
ATOM   7562 C CG  . LYS F 3 247 ? 10.115  -11.786 7.876   1.00 89.73  ?  247 LYS F CG  1 
ATOM   7563 C CD  . LYS F 3 247 ? 10.588  -11.335 6.490   1.00 93.36  ?  247 LYS F CD  1 
ATOM   7564 C CE  . LYS F 3 247 ? 10.612  -9.809  6.374   1.00 96.10  ?  247 LYS F CE  1 
ATOM   7565 N NZ  . LYS F 3 247 ? 10.920  -9.317  4.998   1.00 92.64  ?  247 LYS F NZ  1 
ATOM   7566 N N   . TRP F 3 248 ? 8.519   -15.947 8.960   1.00 87.12  ?  248 TRP F N   1 
ATOM   7567 C CA  . TRP F 3 248 ? 8.407   -17.390 8.818   1.00 80.12  ?  248 TRP F CA  1 
ATOM   7568 C C   . TRP F 3 248 ? 7.535   -17.688 7.607   1.00 82.80  ?  248 TRP F C   1 
ATOM   7569 O O   . TRP F 3 248 ? 7.010   -16.783 6.953   1.00 85.72  ?  248 TRP F O   1 
ATOM   7570 C CB  . TRP F 3 248 ? 7.835   -18.042 10.083  1.00 78.89  ?  248 TRP F CB  1 
ATOM   7571 C CG  . TRP F 3 248 ? 6.477   -17.534 10.480  1.00 84.27  ?  248 TRP F CG  1 
ATOM   7572 C CD1 . TRP F 3 248 ? 5.268   -18.082 10.155  1.00 82.97  ?  248 TRP F CD1 1 
ATOM   7573 C CD2 . TRP F 3 248 ? 6.190   -16.383 11.284  1.00 83.44  ?  248 TRP F CD2 1 
ATOM   7574 N NE1 . TRP F 3 248 ? 4.248   -17.342 10.703  1.00 76.32  ?  248 TRP F NE1 1 
ATOM   7575 C CE2 . TRP F 3 248 ? 4.786   -16.294 11.402  1.00 77.58  ?  248 TRP F CE2 1 
ATOM   7576 C CE3 . TRP F 3 248 ? 6.982   -15.418 11.915  1.00 81.42  ?  248 TRP F CE3 1 
ATOM   7577 C CZ2 . TRP F 3 248 ? 4.160   -15.281 12.123  1.00 74.69  ?  248 TRP F CZ2 1 
ATOM   7578 C CZ3 . TRP F 3 248 ? 6.355   -14.410 12.631  1.00 81.41  ?  248 TRP F CZ3 1 
ATOM   7579 C CH2 . TRP F 3 248 ? 4.959   -14.352 12.729  1.00 73.19  ?  248 TRP F CH2 1 
ATOM   7580 N N   . ASP F 3 249 ? 7.385   -18.972 7.306   1.00 86.69  ?  249 ASP F N   1 
ATOM   7581 C CA  . ASP F 3 249 ? 6.544   -19.432 6.214   1.00 86.36  ?  249 ASP F CA  1 
ATOM   7582 C C   . ASP F 3 249 ? 5.499   -20.392 6.752   1.00 87.07  ?  249 ASP F C   1 
ATOM   7583 O O   . ASP F 3 249 ? 5.789   -21.234 7.608   1.00 84.43  ?  249 ASP F O   1 
ATOM   7584 C CB  . ASP F 3 249 ? 7.353   -20.119 5.106   1.00 93.02  ?  249 ASP F CB  1 
ATOM   7585 C CG  . ASP F 3 249 ? 8.293   -19.170 4.394   1.00 99.94  ?  249 ASP F CG  1 
ATOM   7586 O OD1 . ASP F 3 249 ? 7.942   -17.976 4.256   1.00 103.93 ?  249 ASP F OD1 1 
ATOM   7587 O OD2 . ASP F 3 249 ? 9.375   -19.620 3.958   1.00 96.66  ?  249 ASP F OD2 1 
ATOM   7588 N N   . TYR F 3 250 ? 4.277   -20.233 6.262   1.00 87.16  ?  250 TYR F N   1 
ATOM   7589 C CA  . TYR F 3 250 ? 3.168   -21.116 6.580   1.00 79.97  ?  250 TYR F CA  1 
ATOM   7590 C C   . TYR F 3 250 ? 2.448   -21.454 5.286   1.00 88.68  ?  250 TYR F C   1 
ATOM   7591 O O   . TYR F 3 250 ? 2.358   -20.627 4.375   1.00 93.70  ?  250 TYR F O   1 
ATOM   7592 C CB  . TYR F 3 250 ? 2.201   -20.482 7.588   1.00 81.67  ?  250 TYR F CB  1 
ATOM   7593 C CG  . TYR F 3 250 ? 1.534   -21.482 8.505   1.00 75.13  ?  250 TYR F CG  1 
ATOM   7594 C CD1 . TYR F 3 250 ? 0.150   -21.558 8.600   1.00 76.49  ?  250 TYR F CD1 1 
ATOM   7595 C CD2 . TYR F 3 250 ? 2.291   -22.355 9.274   1.00 75.39  ?  250 TYR F CD2 1 
ATOM   7596 C CE1 . TYR F 3 250 ? -0.460  -22.477 9.441   1.00 81.30  ?  250 TYR F CE1 1 
ATOM   7597 C CE2 . TYR F 3 250 ? 1.693   -23.277 10.113  1.00 74.46  ?  250 TYR F CE2 1 
ATOM   7598 C CZ  . TYR F 3 250 ? 0.319   -23.336 10.192  1.00 75.82  ?  250 TYR F CZ  1 
ATOM   7599 O OH  . TYR F 3 250 ? -0.273  -24.253 11.031  1.00 74.55  ?  250 TYR F OH  1 
ATOM   7600 N N   . THR F 3 251 ? 1.954   -22.688 5.197   1.00 88.11  ?  251 THR F N   1 
ATOM   7601 C CA  . THR F 3 251 ? 1.352   -23.129 3.946   1.00 89.51  ?  251 THR F CA  1 
ATOM   7602 C C   . THR F 3 251 ? -0.102  -22.683 3.828   1.00 91.02  ?  251 THR F C   1 
ATOM   7603 O O   . THR F 3 251 ? -0.570  -22.408 2.718   1.00 95.48  ?  251 THR F O   1 
ATOM   7604 C CB  . THR F 3 251 ? 1.442   -24.653 3.830   1.00 90.52  ?  251 THR F CB  1 
ATOM   7605 O OG1 . THR F 3 251 ? 0.716   -25.267 4.904   1.00 95.03  ?  251 THR F OG1 1 
ATOM   7606 C CG2 . THR F 3 251 ? 2.897   -25.117 3.883   1.00 88.58  ?  251 THR F CG2 1 
ATOM   7607 N N   . TYR F 3 252 ? -0.818  -22.591 4.945   1.00 87.82  ?  252 TYR F N   1 
ATOM   7608 C CA  . TYR F 3 252 ? -2.231  -22.230 4.946   1.00 86.05  ?  252 TYR F CA  1 
ATOM   7609 C C   . TYR F 3 252 ? -2.418  -20.723 5.089   1.00 95.57  ?  252 TYR F C   1 
ATOM   7610 O O   . TYR F 3 252 ? -1.843  -20.106 5.990   1.00 98.67  ?  252 TYR F O   1 
ATOM   7611 C CB  . TYR F 3 252 ? -2.953  -22.958 6.079   1.00 85.03  ?  252 TYR F CB  1 
ATOM   7612 C CG  . TYR F 3 252 ? -2.846  -24.460 5.972   1.00 92.03  ?  252 TYR F CG  1 
ATOM   7613 C CD1 . TYR F 3 252 ? -2.010  -25.176 6.821   1.00 89.50  ?  252 TYR F CD1 1 
ATOM   7614 C CD2 . TYR F 3 252 ? -3.555  -25.161 5.005   1.00 94.63  ?  252 TYR F CD2 1 
ATOM   7615 C CE1 . TYR F 3 252 ? -1.897  -26.551 6.722   1.00 93.10  ?  252 TYR F CE1 1 
ATOM   7616 C CE2 . TYR F 3 252 ? -3.448  -26.538 4.896   1.00 94.15  ?  252 TYR F CE2 1 
ATOM   7617 C CZ  . TYR F 3 252 ? -2.617  -27.227 5.758   1.00 95.58  ?  252 TYR F CZ  1 
ATOM   7618 O OH  . TYR F 3 252 ? -2.500  -28.597 5.661   1.00 93.18  ?  252 TYR F OH  1 
ATOM   7619 N N   . ALA F 3 253 ? -3.218  -20.136 4.201   1.00 95.71  ?  253 ALA F N   1 
ATOM   7620 C CA  . ALA F 3 253 ? -3.570  -18.731 4.330   1.00 91.10  ?  253 ALA F CA  1 
ATOM   7621 C C   . ALA F 3 253 ? -4.663  -18.572 5.387   1.00 98.12  ?  253 ALA F C   1 
ATOM   7622 O O   . ALA F 3 253 ? -5.215  -19.551 5.899   1.00 101.11 ?  253 ALA F O   1 
ATOM   7623 C CB  . ALA F 3 253 ? -4.029  -18.158 2.990   1.00 90.46  ?  253 ALA F CB  1 
ATOM   7624 N N   . ASN F 3 254 ? -4.981  -17.319 5.713   1.00 94.45  ?  254 ASN F N   1 
ATOM   7625 C CA  . ASN F 3 254 ? -6.016  -16.992 6.697   1.00 96.13  ?  254 ASN F CA  1 
ATOM   7626 C C   . ASN F 3 254 ? -5.762  -17.703 8.031   1.00 99.18  ?  254 ASN F C   1 
ATOM   7627 O O   . ASN F 3 254 ? -6.561  -18.516 8.501   1.00 98.71  ?  254 ASN F O   1 
ATOM   7628 C CB  . ASN F 3 254 ? -7.413  -17.325 6.157   1.00 99.05  ?  254 ASN F CB  1 
ATOM   7629 C CG  . ASN F 3 254 ? -7.969  -16.241 5.244   1.00 105.92 ?  254 ASN F CG  1 
ATOM   7630 O OD1 . ASN F 3 254 ? -7.264  -15.306 4.866   1.00 103.76 ?  254 ASN F OD1 1 
ATOM   7631 N ND2 . ASN F 3 254 ? -9.246  -16.361 4.895   1.00 106.23 ?  254 ASN F ND2 1 
ATOM   7632 N N   . MET F 3 255 ? -4.611  -17.395 8.627   1.00 97.14  ?  255 MET F N   1 
ATOM   7633 C CA  . MET F 3 255 ? -4.221  -17.932 9.924   1.00 94.08  ?  255 MET F CA  1 
ATOM   7634 C C   . MET F 3 255 ? -3.836  -16.803 10.868  1.00 91.80  ?  255 MET F C   1 
ATOM   7635 O O   . MET F 3 255 ? -3.569  -15.676 10.441  1.00 92.43  ?  255 MET F O   1 
ATOM   7636 C CB  . MET F 3 255 ? -3.052  -18.922 9.807   1.00 90.81  ?  255 MET F CB  1 
ATOM   7637 C CG  . MET F 3 255 ? -3.418  -20.248 9.174   1.00 95.40  ?  255 MET F CG  1 
ATOM   7638 S SD  . MET F 3 255 ? -4.271  -21.313 10.355  1.00 96.54  ?  255 MET F SD  1 
ATOM   7639 C CE  . MET F 3 255 ? -4.667  -22.716 9.319   1.00 98.77  ?  255 MET F CE  1 
ATOM   7640 N N   . THR F 3 256 ? -3.833  -17.111 12.166  1.00 88.63  ?  256 THR F N   1 
ATOM   7641 C CA  . THR F 3 256 ? -3.271  -16.208 13.160  1.00 86.17  ?  256 THR F CA  1 
ATOM   7642 C C   . THR F 3 256 ? -2.061  -16.862 13.815  1.00 82.04  ?  256 THR F C   1 
ATOM   7643 O O   . THR F 3 256 ? -1.932  -18.087 13.849  1.00 78.64  ?  256 THR F O   1 
ATOM   7644 C CB  . THR F 3 256 ? -4.306  -15.817 14.226  1.00 78.43  ?  256 THR F CB  1 
ATOM   7645 O OG1 . THR F 3 256 ? -4.654  -16.964 15.012  1.00 85.16  ?  256 THR F OG1 1 
ATOM   7646 C CG2 . THR F 3 256 ? -5.553  -15.268 13.570  1.00 84.04  ?  256 THR F CG2 1 
ATOM   7647 N N   . PHE F 3 257 ? -1.161  -16.027 14.331  1.00 73.20  ?  257 PHE F N   1 
ATOM   7648 C CA  . PHE F 3 257 ? 0.089   -16.510 14.895  1.00 68.32  ?  257 PHE F CA  1 
ATOM   7649 C C   . PHE F 3 257 ? 0.372   -15.863 16.243  1.00 66.90  ?  257 PHE F C   1 
ATOM   7650 O O   . PHE F 3 257 ? -0.045  -14.734 16.518  1.00 68.30  ?  257 PHE F O   1 
ATOM   7651 C CB  . PHE F 3 257 ? 1.270   -16.250 13.954  1.00 73.41  ?  257 PHE F CB  1 
ATOM   7652 C CG  . PHE F 3 257 ? 1.132   -16.901 12.606  1.00 77.09  ?  257 PHE F CG  1 
ATOM   7653 C CD1 . PHE F 3 257 ? 1.492   -18.228 12.422  1.00 79.77  ?  257 PHE F CD1 1 
ATOM   7654 C CD2 . PHE F 3 257 ? 0.659   -16.184 11.519  1.00 76.79  ?  257 PHE F CD2 1 
ATOM   7655 C CE1 . PHE F 3 257 ? 1.372   -18.827 11.181  1.00 81.46  ?  257 PHE F CE1 1 
ATOM   7656 C CE2 . PHE F 3 257 ? 0.541   -16.775 10.274  1.00 77.12  ?  257 PHE F CE2 1 
ATOM   7657 C CZ  . PHE F 3 257 ? 0.897   -18.098 10.104  1.00 80.15  ?  257 PHE F CZ  1 
ATOM   7658 N N   . GLN F 3 258 ? 1.096   -16.603 17.078  1.00 66.25  ?  258 GLN F N   1 
ATOM   7659 C CA  . GLN F 3 258 ? 1.572   -16.130 18.371  1.00 63.61  ?  258 GLN F CA  1 
ATOM   7660 C C   . GLN F 3 258 ? 3.071   -16.365 18.462  1.00 61.10  ?  258 GLN F C   1 
ATOM   7661 O O   . GLN F 3 258 ? 3.546   -17.471 18.186  1.00 63.48  ?  258 GLN F O   1 
ATOM   7662 C CB  . GLN F 3 258 ? 0.861   -16.839 19.521  1.00 55.30  ?  258 GLN F CB  1 
ATOM   7663 C CG  . GLN F 3 258 ? 1.406   -16.473 20.880  1.00 60.46  ?  258 GLN F CG  1 
ATOM   7664 C CD  . GLN F 3 258 ? 0.958   -17.440 21.953  1.00 68.54  ?  258 GLN F CD  1 
ATOM   7665 O OE1 . GLN F 3 258 ? 0.740   -18.622 21.690  1.00 68.40  ?  258 GLN F OE1 1 
ATOM   7666 N NE2 . GLN F 3 258 ? 0.818   -16.944 23.172  1.00 72.51  ?  258 GLN F NE2 1 
ATOM   7667 N N   . VAL F 3 259 ? 3.813   -15.328 18.835  1.00 57.79  ?  259 VAL F N   1 
ATOM   7668 C CA  . VAL F 3 259 ? 5.264   -15.396 18.961  1.00 58.45  ?  259 VAL F CA  1 
ATOM   7669 C C   . VAL F 3 259 ? 5.644   -15.351 20.434  1.00 57.01  ?  259 VAL F C   1 
ATOM   7670 O O   . VAL F 3 259 ? 5.153   -14.501 21.187  1.00 56.96  ?  259 VAL F O   1 
ATOM   7671 C CB  . VAL F 3 259 ? 5.952   -14.263 18.187  1.00 58.01  ?  259 VAL F CB  1 
ATOM   7672 C CG1 . VAL F 3 259 ? 7.457   -14.370 18.349  1.00 59.94  ?  259 VAL F CG1 1 
ATOM   7673 C CG2 . VAL F 3 259 ? 5.563   -14.333 16.725  1.00 63.91  ?  259 VAL F CG2 1 
ATOM   7674 N N   . GLN F 3 260 ? 6.518   -16.262 20.841  1.00 55.25  ?  260 GLN F N   1 
ATOM   7675 C CA  . GLN F 3 260 ? 6.990   -16.343 22.211  1.00 55.80  ?  260 GLN F CA  1 
ATOM   7676 C C   . GLN F 3 260 ? 8.509   -16.254 22.246  1.00 54.71  ?  260 GLN F C   1 
ATOM   7677 O O   . GLN F 3 260 ? 9.196   -16.506 21.250  1.00 59.93  ?  260 GLN F O   1 
ATOM   7678 C CB  . GLN F 3 260 ? 6.524   -17.634 22.888  1.00 47.76  ?  260 GLN F CB  1 
ATOM   7679 C CG  . GLN F 3 260 ? 5.058   -17.615 23.257  1.00 54.28  ?  260 GLN F CG  1 
ATOM   7680 C CD  . GLN F 3 260 ? 4.624   -18.877 23.975  1.00 58.66  ?  260 GLN F CD  1 
ATOM   7681 O OE1 . GLN F 3 260 ? 5.430   -19.771 24.210  1.00 58.68  ?  260 GLN F OE1 1 
ATOM   7682 N NE2 . GLN F 3 260 ? 3.339   -18.966 24.304  1.00 59.19  ?  260 GLN F NE2 1 
ATOM   7683 N N   . TRP F 3 261 ? 9.030   -15.875 23.410  1.00 51.77  ?  261 TRP F N   1 
ATOM   7684 C CA  . TRP F 3 261 ? 10.466  -15.782 23.614  1.00 51.10  ?  261 TRP F CA  1 
ATOM   7685 C C   . TRP F 3 261 ? 10.819  -16.376 24.969  1.00 47.29  ?  261 TRP F C   1 
ATOM   7686 O O   . TRP F 3 261 ? 9.959   -16.590 25.829  1.00 42.84  ?  261 TRP F O   1 
ATOM   7687 C CB  . TRP F 3 261 ? 10.976  -14.330 23.510  1.00 50.38  ?  261 TRP F CB  1 
ATOM   7688 C CG  . TRP F 3 261 ? 10.463  -13.403 24.584  1.00 51.94  ?  261 TRP F CG  1 
ATOM   7689 C CD1 . TRP F 3 261 ? 9.293   -12.691 24.570  1.00 52.27  ?  261 TRP F CD1 1 
ATOM   7690 C CD2 . TRP F 3 261 ? 11.103  -13.096 25.827  1.00 49.30  ?  261 TRP F CD2 1 
ATOM   7691 N NE1 . TRP F 3 261 ? 9.168   -11.963 25.727  1.00 50.59  ?  261 TRP F NE1 1 
ATOM   7692 C CE2 . TRP F 3 261 ? 10.266  -12.190 26.516  1.00 51.83  ?  261 TRP F CE2 1 
ATOM   7693 C CE3 . TRP F 3 261 ? 12.300  -13.500 26.426  1.00 43.94  ?  261 TRP F CE3 1 
ATOM   7694 C CZ2 . TRP F 3 261 ? 10.589  -11.682 27.773  1.00 45.24  ?  261 TRP F CZ2 1 
ATOM   7695 C CZ3 . TRP F 3 261 ? 12.619  -12.996 27.673  1.00 45.69  ?  261 TRP F CZ3 1 
ATOM   7696 C CH2 . TRP F 3 261 ? 11.767  -12.095 28.334  1.00 47.53  ?  261 TRP F CH2 1 
ATOM   7697 N N   . LEU F 3 262 ? 12.107  -16.659 25.134  1.00 48.27  ?  262 LEU F N   1 
ATOM   7698 C CA  . LEU F 3 262 ? 12.621  -17.200 26.382  1.00 50.96  ?  262 LEU F CA  1 
ATOM   7699 C C   . LEU F 3 262 ? 14.084  -16.810 26.522  1.00 45.93  ?  262 LEU F C   1 
ATOM   7700 O O   . LEU F 3 262 ? 14.791  -16.657 25.526  1.00 48.63  ?  262 LEU F O   1 
ATOM   7701 C CB  . LEU F 3 262 ? 12.479  -18.726 26.442  1.00 52.40  ?  262 LEU F CB  1 
ATOM   7702 C CG  . LEU F 3 262 ? 12.777  -19.343 27.807  1.00 52.60  ?  262 LEU F CG  1 
ATOM   7703 C CD1 . LEU F 3 262 ? 11.616  -19.066 28.751  1.00 51.33  ?  262 LEU F CD1 1 
ATOM   7704 C CD2 . LEU F 3 262 ? 13.075  -20.833 27.700  1.00 52.29  ?  262 LEU F CD2 1 
ATOM   7705 N N   . HIS F 3 263 ? 14.533  -16.638 27.762  1.00 46.10  ?  263 HIS F N   1 
ATOM   7706 C CA  . HIS F 3 263 ? 15.962  -16.490 28.000  1.00 50.07  ?  263 HIS F CA  1 
ATOM   7707 C C   . HIS F 3 263 ? 16.662  -17.796 27.658  1.00 56.06  ?  263 HIS F C   1 
ATOM   7708 O O   . HIS F 3 263 ? 16.257  -18.864 28.129  1.00 57.34  ?  263 HIS F O   1 
ATOM   7709 C CB  . HIS F 3 263 ? 16.238  -16.129 29.454  1.00 50.84  ?  263 HIS F CB  1 
ATOM   7710 C CG  . HIS F 3 263 ? 15.602  -14.854 29.900  1.00 49.84  ?  263 HIS F CG  1 
ATOM   7711 N ND1 . HIS F 3 263 ? 14.279  -14.777 30.277  1.00 47.32  ?  263 HIS F ND1 1 
ATOM   7712 C CD2 . HIS F 3 263 ? 16.112  -13.610 30.052  1.00 45.56  ?  263 HIS F CD2 1 
ATOM   7713 C CE1 . HIS F 3 263 ? 13.999  -13.537 30.636  1.00 44.64  ?  263 HIS F CE1 1 
ATOM   7714 N NE2 . HIS F 3 263 ? 15.095  -12.809 30.508  1.00 47.47  ?  263 HIS F NE2 1 
ATOM   7715 N N   . ALA F 3 264 ? 17.722  -17.716 26.849  1.00 55.41  ?  264 ALA F N   1 
ATOM   7716 C CA  . ALA F 3 264 ? 18.389  -18.938 26.409  1.00 55.74  ?  264 ALA F CA  1 
ATOM   7717 C C   . ALA F 3 264 ? 18.950  -19.718 27.590  1.00 58.53  ?  264 ALA F C   1 
ATOM   7718 O O   . ALA F 3 264 ? 18.833  -20.948 27.641  1.00 63.66  ?  264 ALA F O   1 
ATOM   7719 C CB  . ALA F 3 264 ? 19.493  -18.616 25.407  1.00 53.20  ?  264 ALA F CB  1 
ATOM   7720 N N   . PHE F 3 265 ? 19.543  -19.023 28.562  1.00 55.63  ?  265 PHE F N   1 
ATOM   7721 C CA  . PHE F 3 265 ? 20.143  -19.728 29.687  1.00 58.82  ?  265 PHE F CA  1 
ATOM   7722 C C   . PHE F 3 265 ? 19.115  -20.471 30.534  1.00 56.75  ?  265 PHE F C   1 
ATOM   7723 O O   . PHE F 3 265 ? 19.507  -21.253 31.403  1.00 65.62  ?  265 PHE F O   1 
ATOM   7724 C CB  . PHE F 3 265 ? 20.951  -18.757 30.561  1.00 60.76  ?  265 PHE F CB  1 
ATOM   7725 C CG  . PHE F 3 265 ? 20.113  -17.758 31.310  1.00 59.38  ?  265 PHE F CG  1 
ATOM   7726 C CD1 . PHE F 3 265 ? 19.642  -18.044 32.582  1.00 55.62  ?  265 PHE F CD1 1 
ATOM   7727 C CD2 . PHE F 3 265 ? 19.814  -16.526 30.751  1.00 59.55  ?  265 PHE F CD2 1 
ATOM   7728 C CE1 . PHE F 3 265 ? 18.873  -17.133 33.271  1.00 51.10  ?  265 PHE F CE1 1 
ATOM   7729 C CE2 . PHE F 3 265 ? 19.050  -15.609 31.439  1.00 52.48  ?  265 PHE F CE2 1 
ATOM   7730 C CZ  . PHE F 3 265 ? 18.578  -15.914 32.700  1.00 54.11  ?  265 PHE F CZ  1 
ATOM   7731 N N   . LEU F 3 266 ? 17.819  -20.262 30.303  1.00 61.10  ?  266 LEU F N   1 
ATOM   7732 C CA  . LEU F 3 266 ? 16.810  -20.931 31.116  1.00 68.25  ?  266 LEU F CA  1 
ATOM   7733 C C   . LEU F 3 266 ? 16.665  -22.412 30.792  1.00 67.92  ?  266 LEU F C   1 
ATOM   7734 O O   . LEU F 3 266 ? 16.018  -23.134 31.559  1.00 69.01  ?  266 LEU F O   1 
ATOM   7735 C CB  . LEU F 3 266 ? 15.456  -20.233 30.970  1.00 63.30  ?  266 LEU F CB  1 
ATOM   7736 C CG  . LEU F 3 266 ? 15.339  -18.877 31.660  1.00 54.41  ?  266 LEU F CG  1 
ATOM   7737 C CD1 . LEU F 3 266 ? 13.961  -18.279 31.440  1.00 54.45  ?  266 LEU F CD1 1 
ATOM   7738 C CD2 . LEU F 3 266 ? 15.623  -19.033 33.142  1.00 50.96  ?  266 LEU F CD2 1 
ATOM   7739 N N   . LYS F 3 267 ? 17.235  -22.880 29.682  1.00 71.04  ?  267 LYS F N   1 
ATOM   7740 C CA  . LYS F 3 267 ? 17.154  -24.294 29.343  1.00 75.45  ?  267 LYS F CA  1 
ATOM   7741 C C   . LYS F 3 267 ? 18.143  -25.147 30.128  1.00 80.48  ?  267 LYS F C   1 
ATOM   7742 O O   . LYS F 3 267 ? 17.962  -26.369 30.202  1.00 86.47  ?  267 LYS F O   1 
ATOM   7743 C CB  . LYS F 3 267 ? 17.388  -24.490 27.845  1.00 73.02  ?  267 LYS F CB  1 
ATOM   7744 C CG  . LYS F 3 267 ? 16.303  -23.893 26.965  1.00 71.78  ?  267 LYS F CG  1 
ATOM   7745 C CD  . LYS F 3 267 ? 15.036  -24.727 27.042  1.00 68.65  ?  267 LYS F CD  1 
ATOM   7746 C CE  . LYS F 3 267 ? 14.254  -24.697 25.740  1.00 70.40  ?  267 LYS F CE  1 
ATOM   7747 N NZ  . LYS F 3 267 ? 15.004  -25.352 24.633  1.00 77.43  ?  267 LYS F NZ  1 
ATOM   7748 N N   . ARG F 3 268 ? 19.166  -24.539 30.731  1.00 83.96  ?  268 ARG F N   1 
ATOM   7749 C CA  . ARG F 3 268 ? 20.183  -25.284 31.466  1.00 86.43  ?  268 ARG F CA  1 
ATOM   7750 C C   . ARG F 3 268 ? 20.272  -24.908 32.938  1.00 88.82  ?  268 ARG F C   1 
ATOM   7751 O O   . ARG F 3 268 ? 20.302  -25.802 33.789  1.00 92.09  ?  268 ARG F O   1 
ATOM   7752 C CB  . ARG F 3 268 ? 21.557  -25.105 30.797  1.00 78.33  ?  268 ARG F CB  1 
ATOM   7753 C CG  . ARG F 3 268 ? 21.660  -25.764 29.430  1.00 83.22  ?  268 ARG F CG  1 
ATOM   7754 C CD  . ARG F 3 268 ? 21.376  -27.254 29.537  1.00 84.54  ?  268 ARG F CD  1 
ATOM   7755 N NE  . ARG F 3 268 ? 22.532  -27.992 30.040  1.00 84.19  ?  268 ARG F NE  1 
ATOM   7756 C CZ  . ARG F 3 268 ? 22.457  -29.122 30.739  1.00 87.96  ?  268 ARG F CZ  1 
ATOM   7757 N NH1 . ARG F 3 268 ? 21.274  -29.650 31.035  1.00 88.52  ?  268 ARG F NH1 1 
ATOM   7758 N NH2 . ARG F 3 268 ? 23.566  -29.719 31.162  1.00 74.44  ?  268 ARG F NH2 1 
ATOM   7759 N N   . ASN F 3 269 ? 20.298  -23.612 33.277  1.00 95.62  ?  269 ASN F N   1 
ATOM   7760 C CA  . ASN F 3 269 ? 20.435  -23.219 34.682  1.00 97.02  ?  269 ASN F CA  1 
ATOM   7761 C C   . ASN F 3 269 ? 19.270  -23.732 35.522  1.00 103.02 ?  269 ASN F C   1 
ATOM   7762 O O   . ASN F 3 269 ? 19.517  -24.436 36.521  1.00 104.18 ?  269 ASN F O   1 
ATOM   7763 C CB  . ASN F 3 269 ? 20.615  -21.697 34.785  1.00 79.04  ?  269 ASN F CB  1 
ATOM   7764 C CG  . ASN F 3 269 ? 22.066  -21.270 34.890  1.00 74.20  ?  269 ASN F CG  1 
ATOM   7765 O OD1 . ASN F 3 269 ? 22.904  -22.002 35.414  1.00 69.06  ?  269 ASN F OD1 1 
ATOM   7766 N ND2 . ASN F 3 269 ? 22.361  -20.054 34.423  1.00 74.70  ?  269 ASN F ND2 1 
ATOM   7767 N N   . PRO F 3 270 ? 17.965  -23.429 35.184  1.00 98.68  ?  270 PRO F N   1 
ATOM   7768 C CA  . PRO F 3 270 ? 16.857  -24.142 35.830  1.00 100.91 ?  270 PRO F CA  1 
ATOM   7769 C C   . PRO F 3 270 ? 16.709  -25.580 35.336  1.00 103.46 ?  270 PRO F C   1 
ATOM   7770 O O   . PRO F 3 270 ? 16.540  -26.508 36.130  1.00 105.80 ?  270 PRO F O   1 
ATOM   7771 C CB  . PRO F 3 270 ? 15.632  -23.301 35.446  1.00 94.23  ?  270 PRO F CB  1 
ATOM   7772 C CG  . PRO F 3 270 ? 16.174  -21.989 35.015  1.00 88.37  ?  270 PRO F CG  1 
ATOM   7773 C CD  . PRO F 3 270 ? 17.449  -22.341 34.332  1.00 87.77  ?  270 PRO F CD  1 
ATOM   7774 N N   . GLY F 3 271 ? 16.779  -25.770 34.019  1.00 98.34  ?  271 GLY F N   1 
ATOM   7775 C CA  . GLY F 3 271 ? 16.499  -27.062 33.412  1.00 100.11 ?  271 GLY F CA  1 
ATOM   7776 C C   . GLY F 3 271 ? 15.157  -27.624 33.833  1.00 104.03 ?  271 GLY F C   1 
ATOM   7777 O O   . GLY F 3 271 ? 14.288  -26.867 34.270  1.00 99.98  ?  271 GLY F O   1 
ATOM   7778 N N   . ASN F 3 272 ? 14.992  -28.947 33.706  1.00 102.80 ?  272 ASN F N   1 
ATOM   7779 C CA  . ASN F 3 272 ? 13.826  -29.706 34.166  1.00 102.39 ?  272 ASN F CA  1 
ATOM   7780 C C   . ASN F 3 272 ? 12.492  -28.988 33.961  1.00 105.67 ?  272 ASN F C   1 
ATOM   7781 O O   . ASN F 3 272 ? 11.585  -29.131 34.789  1.00 100.33 ?  272 ASN F O   1 
ATOM   7782 C CB  . ASN F 3 272 ? 13.984  -30.117 35.637  1.00 98.02  ?  272 ASN F CB  1 
ATOM   7783 C CG  . ASN F 3 272 ? 15.331  -30.751 35.927  1.00 102.21 ?  272 ASN F CG  1 
ATOM   7784 O OD1 . ASN F 3 272 ? 15.903  -31.457 35.090  1.00 103.51 ?  272 ASN F OD1 1 
ATOM   7785 N ND2 . ASN F 3 272 ? 15.828  -30.537 37.139  1.00 103.99 ?  272 ASN F ND2 1 
ATOM   7786 N N   . HIS F 3 273 ? 12.380  -28.189 32.893  1.00 105.06 ?  273 HIS F N   1 
ATOM   7787 C CA  . HIS F 3 273 ? 11.146  -27.471 32.550  1.00 99.18  ?  273 HIS F CA  1 
ATOM   7788 C C   . HIS F 3 273 ? 10.637  -26.576 33.688  1.00 92.97  ?  273 HIS F C   1 
ATOM   7789 O O   . HIS F 3 273 ? 9.434   -26.333 33.805  1.00 83.07  ?  273 HIS F O   1 
ATOM   7790 C CB  . HIS F 3 273 ? 10.052  -28.449 32.102  1.00 102.04 ?  273 HIS F CB  1 
ATOM   7791 C CG  . HIS F 3 273 ? 10.371  -29.190 30.838  1.00 98.50  ?  273 HIS F CG  1 
ATOM   7792 N ND1 . HIS F 3 273 ? 10.958  -30.438 30.834  1.00 103.92 ?  273 HIS F ND1 1 
ATOM   7793 C CD2 . HIS F 3 273 ? 10.159  -28.869 29.540  1.00 96.51  ?  273 HIS F CD2 1 
ATOM   7794 C CE1 . HIS F 3 273 ? 11.101  -30.848 29.586  1.00 103.71 ?  273 HIS F CE1 1 
ATOM   7795 N NE2 . HIS F 3 273 ? 10.623  -29.915 28.782  1.00 97.39  ?  273 HIS F NE2 1 
ATOM   7796 N N   . LEU F 3 274 ? 11.547  -26.082 34.533  1.00 93.97  ?  274 LEU F N   1 
ATOM   7797 C CA  . LEU F 3 274 ? 11.200  -25.212 35.652  1.00 90.54  ?  274 LEU F CA  1 
ATOM   7798 C C   . LEU F 3 274 ? 11.107  -23.745 35.244  1.00 77.76  ?  274 LEU F C   1 
ATOM   7799 O O   . LEU F 3 274 ? 11.639  -22.879 35.941  1.00 74.81  ?  274 LEU F O   1 
ATOM   7800 C CB  . LEU F 3 274 ? 12.245  -25.332 36.766  1.00 95.51  ?  274 LEU F CB  1 
ATOM   7801 C CG  . LEU F 3 274 ? 12.740  -26.707 37.204  1.00 101.93 ?  274 LEU F CG  1 
ATOM   7802 C CD1 . LEU F 3 274 ? 13.925  -26.550 38.142  1.00 99.59  ?  274 LEU F CD1 1 
ATOM   7803 C CD2 . LEU F 3 274 ? 11.630  -27.501 37.864  1.00 104.34 ?  274 LEU F CD2 1 
ATOM   7804 N N   . TYR F 3 275 ? 10.398  -23.443 34.164  1.00 72.20  ?  275 TYR F N   1 
ATOM   7805 C CA  . TYR F 3 275 ? 10.380  -22.091 33.620  1.00 61.42  ?  275 TYR F CA  1 
ATOM   7806 C C   . TYR F 3 275 ? 9.116   -21.921 32.784  1.00 61.50  ?  275 TYR F C   1 
ATOM   7807 O O   . TYR F 3 275 ? 8.340   -22.863 32.596  1.00 63.50  ?  275 TYR F O   1 
ATOM   7808 C CB  . TYR F 3 275 ? 11.645  -21.817 32.795  1.00 57.55  ?  275 TYR F CB  1 
ATOM   7809 C CG  . TYR F 3 275 ? 11.844  -22.781 31.642  1.00 64.47  ?  275 TYR F CG  1 
ATOM   7810 C CD1 . TYR F 3 275 ? 12.655  -23.903 31.780  1.00 71.43  ?  275 TYR F CD1 1 
ATOM   7811 C CD2 . TYR F 3 275 ? 11.207  -22.583 30.425  1.00 57.70  ?  275 TYR F CD2 1 
ATOM   7812 C CE1 . TYR F 3 275 ? 12.832  -24.792 30.732  1.00 70.56  ?  275 TYR F CE1 1 
ATOM   7813 C CE2 . TYR F 3 275 ? 11.380  -23.466 29.372  1.00 67.35  ?  275 TYR F CE2 1 
ATOM   7814 C CZ  . TYR F 3 275 ? 12.192  -24.569 29.530  1.00 69.11  ?  275 TYR F CZ  1 
ATOM   7815 O OH  . TYR F 3 275 ? 12.357  -25.448 28.479  1.00 66.58  ?  275 TYR F OH  1 
ATOM   7816 N N   . LYS F 3 276 ? 8.918   -20.707 32.271  1.00 56.96  ?  276 LYS F N   1 
ATOM   7817 C CA  . LYS F 3 276 ? 7.736   -20.380 31.485  1.00 54.01  ?  276 LYS F CA  1 
ATOM   7818 C C   . LYS F 3 276 ? 8.130   -19.461 30.336  1.00 49.05  ?  276 LYS F C   1 
ATOM   7819 O O   . LYS F 3 276 ? 8.908   -18.524 30.522  1.00 52.01  ?  276 LYS F O   1 
ATOM   7820 C CB  . LYS F 3 276 ? 6.650   -19.726 32.358  1.00 46.16  ?  276 LYS F CB  1 
ATOM   7821 C CG  . LYS F 3 276 ? 5.425   -19.241 31.593  1.00 56.08  ?  276 LYS F CG  1 
ATOM   7822 C CD  . LYS F 3 276 ? 4.285   -18.811 32.525  1.00 57.17  ?  276 LYS F CD  1 
ATOM   7823 C CE  . LYS F 3 276 ? 4.405   -17.354 32.941  1.00 61.37  ?  276 LYS F CE  1 
ATOM   7824 N NZ  . LYS F 3 276 ? 4.336   -16.424 31.772  1.00 61.47  ?  276 LYS F NZ  1 
ATOM   7825 N N   . TRP F 3 277 ? 7.611   -19.757 29.146  1.00 51.07  ?  277 TRP F N   1 
ATOM   7826 C CA  . TRP F 3 277 ? 7.841   -18.917 27.978  1.00 52.27  ?  277 TRP F CA  1 
ATOM   7827 C C   . TRP F 3 277 ? 7.073   -17.603 28.103  1.00 52.23  ?  277 TRP F C   1 
ATOM   7828 O O   . TRP F 3 277 ? 6.024   -17.529 28.747  1.00 56.58  ?  277 TRP F O   1 
ATOM   7829 C CB  . TRP F 3 277 ? 7.435   -19.651 26.694  1.00 49.69  ?  277 TRP F CB  1 
ATOM   7830 C CG  . TRP F 3 277 ? 8.431   -20.693 26.236  1.00 51.19  ?  277 TRP F CG  1 
ATOM   7831 C CD1 . TRP F 3 277 ? 8.587   -21.960 26.727  1.00 49.58  ?  277 TRP F CD1 1 
ATOM   7832 C CD2 . TRP F 3 277 ? 9.402   -20.547 25.192  1.00 51.46  ?  277 TRP F CD2 1 
ATOM   7833 N NE1 . TRP F 3 277 ? 9.602   -22.606 26.056  1.00 52.99  ?  277 TRP F NE1 1 
ATOM   7834 C CE2 . TRP F 3 277 ? 10.115  -21.761 25.108  1.00 52.24  ?  277 TRP F CE2 1 
ATOM   7835 C CE3 . TRP F 3 277 ? 9.736   -19.508 24.319  1.00 50.86  ?  277 TRP F CE3 1 
ATOM   7836 C CZ2 . TRP F 3 277 ? 11.143  -21.959 24.191  1.00 53.50  ?  277 TRP F CZ2 1 
ATOM   7837 C CZ3 . TRP F 3 277 ? 10.756  -19.708 23.407  1.00 56.32  ?  277 TRP F CZ3 1 
ATOM   7838 C CH2 . TRP F 3 277 ? 11.450  -20.923 23.351  1.00 55.99  ?  277 TRP F CH2 1 
ATOM   7839 N N   . LYS F 3 278 ? 7.611   -16.557 27.484  1.00 46.59  ?  278 LYS F N   1 
ATOM   7840 C CA  . LYS F 3 278 ? 7.026   -15.227 27.562  1.00 53.84  ?  278 LYS F CA  1 
ATOM   7841 C C   . LYS F 3 278 ? 6.409   -14.843 26.224  1.00 52.20  ?  278 LYS F C   1 
ATOM   7842 O O   . LYS F 3 278 ? 6.713   -15.429 25.186  1.00 54.35  ?  278 LYS F O   1 
ATOM   7843 C CB  . LYS F 3 278 ? 8.073   -14.185 27.974  1.00 50.52  ?  278 LYS F CB  1 
ATOM   7844 C CG  . LYS F 3 278 ? 8.814   -14.496 29.267  1.00 46.67  ?  278 LYS F CG  1 
ATOM   7845 C CD  . LYS F 3 278 ? 10.118  -15.246 29.011  1.00 46.94  ?  278 LYS F CD  1 
ATOM   7846 C CE  . LYS F 3 278 ? 10.925  -15.393 30.293  1.00 41.81  ?  278 LYS F CE  1 
ATOM   7847 N NZ  . LYS F 3 278 ? 10.121  -15.994 31.395  1.00 42.92  ?  278 LYS F NZ  1 
ATOM   7848 N N   . GLN F 3 279 ? 5.537   -13.840 26.260  1.00 53.32  ?  279 GLN F N   1 
ATOM   7849 C CA  . GLN F 3 279 ? 4.838   -13.370 25.073  1.00 51.55  ?  279 GLN F CA  1 
ATOM   7850 C C   . GLN F 3 279 ? 5.555   -12.136 24.539  1.00 56.12  ?  279 GLN F C   1 
ATOM   7851 O O   . GLN F 3 279 ? 5.838   -11.206 25.304  1.00 51.61  ?  279 GLN F O   1 
ATOM   7852 C CB  . GLN F 3 279 ? 3.398   -12.993 25.422  1.00 54.33  ?  279 GLN F CB  1 
ATOM   7853 C CG  . GLN F 3 279 ? 2.538   -14.096 25.976  1.00 46.06  ?  279 GLN F CG  1 
ATOM   7854 C CD  . GLN F 3 279 ? 2.440   -15.268 25.062  1.00 63.78  ?  279 GLN F CD  1 
ATOM   7855 O OE1 . GLN F 3 279 ? 2.276   -15.114 23.852  1.00 67.15  ?  279 GLN F OE1 1 
ATOM   7856 N NE2 . GLN F 3 279 ? 2.539   -16.464 25.628  1.00 67.34  ?  279 GLN F NE2 1 
ATOM   7857 N N   . ILE F 3 280 ? 5.803   -12.102 23.230  1.00 57.64  ?  280 ILE F N   1 
ATOM   7858 C CA  . ILE F 3 280 ? 6.308   -10.886 22.594  1.00 51.35  ?  280 ILE F CA  1 
ATOM   7859 C C   . ILE F 3 280 ? 5.213   -9.831  22.696  1.00 54.39  ?  280 ILE F C   1 
ATOM   7860 O O   . ILE F 3 280 ? 4.084   -10.073 22.247  1.00 56.46  ?  280 ILE F O   1 
ATOM   7861 C CB  . ILE F 3 280 ? 6.731   -11.128 21.139  1.00 50.81  ?  280 ILE F CB  1 
ATOM   7862 C CG1 . ILE F 3 280 ? 7.943   -12.055 21.081  1.00 51.66  ?  280 ILE F CG1 1 
ATOM   7863 C CG2 . ILE F 3 280 ? 7.044   -9.807  20.451  1.00 54.66  ?  280 ILE F CG2 1 
ATOM   7864 C CD1 . ILE F 3 280 ? 9.278   -11.342 21.269  1.00 51.42  ?  280 ILE F CD1 1 
ATOM   7865 N N   . PRO F 3 281 ? 5.510   -8.652  23.277  1.00 57.69  ?  281 PRO F N   1 
ATOM   7866 C CA  . PRO F 3 281 ? 4.459   -7.698  23.677  1.00 55.60  ?  281 PRO F CA  1 
ATOM   7867 C C   . PRO F 3 281 ? 3.328   -7.444  22.685  1.00 65.50  ?  281 PRO F C   1 
ATOM   7868 O O   . PRO F 3 281 ? 2.157   -7.510  23.075  1.00 72.19  ?  281 PRO F O   1 
ATOM   7869 C CB  . PRO F 3 281 ? 5.256   -6.419  23.938  1.00 48.22  ?  281 PRO F CB  1 
ATOM   7870 C CG  . PRO F 3 281 ? 6.559   -6.931  24.472  1.00 60.26  ?  281 PRO F CG  1 
ATOM   7871 C CD  . PRO F 3 281 ? 6.853   -8.186  23.670  1.00 58.46  ?  281 PRO F CD  1 
ATOM   7872 N N   . ASP F 3 282 ? 3.623   -7.168  21.417  1.00 56.84  ?  282 ASP F N   1 
ATOM   7873 C CA  . ASP F 3 282 ? 2.566   -6.845  20.463  1.00 65.58  ?  282 ASP F CA  1 
ATOM   7874 C C   . ASP F 3 282 ? 2.537   -7.822  19.293  1.00 68.37  ?  282 ASP F C   1 
ATOM   7875 O O   . ASP F 3 282 ? 2.186   -7.463  18.165  1.00 71.10  ?  282 ASP F O   1 
ATOM   7876 C CB  . ASP F 3 282 ? 2.725   -5.401  19.991  1.00 71.00  ?  282 ASP F CB  1 
ATOM   7877 C CG  . ASP F 3 282 ? 1.654   -4.486  20.552  1.00 72.95  ?  282 ASP F CG  1 
ATOM   7878 O OD1 . ASP F 3 282 ? 0.581   -5.011  20.923  1.00 78.88  ?  282 ASP F OD1 1 
ATOM   7879 O OD2 . ASP F 3 282 ? 1.906   -3.271  20.705  1.00 76.77  ?  282 ASP F OD2 1 
ATOM   7880 N N   . CYS F 3 283 ? 2.853   -9.071  19.596  1.00 68.20  ?  283 CYS F N   1 
ATOM   7881 C CA  . CYS F 3 283 ? 2.816   -10.128 18.574  1.00 62.36  ?  283 CYS F CA  1 
ATOM   7882 C C   . CYS F 3 283 ? 2.133   -11.334 19.219  1.00 63.22  ?  283 CYS F C   1 
ATOM   7883 O O   . CYS F 3 283 ? 2.592   -12.450 18.994  1.00 67.63  ?  283 CYS F O   1 
ATOM   7884 C CB  . CYS F 3 283 ? 4.233   -10.442 18.121  1.00 67.10  ?  283 CYS F CB  1 
ATOM   7885 S SG  . CYS F 3 283 ? 4.932   -9.242  16.958  1.00 79.60  ?  283 CYS F SG  1 
ATOM   7886 N N   . GLU F 3 284 ? 1.087   -11.100 20.016  1.00 64.56  ?  284 GLU F N   1 
ATOM   7887 C CA  . GLU F 3 284 ? 0.337   -12.191 20.630  1.00 57.27  ?  284 GLU F CA  1 
ATOM   7888 C C   . GLU F 3 284 ? -0.658  -12.816 19.662  1.00 63.98  ?  284 GLU F C   1 
ATOM   7889 O O   . GLU F 3 284 ? -0.947  -14.012 19.768  1.00 66.40  ?  284 GLU F O   1 
ATOM   7890 C CB  . GLU F 3 284 ? -0.391  -11.701 21.882  1.00 52.12  ?  284 GLU F CB  1 
ATOM   7891 C CG  . GLU F 3 284 ? 0.522   -11.356 23.049  1.00 62.07  ?  284 GLU F CG  1 
ATOM   7892 C CD  . GLU F 3 284 ? -0.217  -10.650 24.181  1.00 70.19  ?  284 GLU F CD  1 
ATOM   7893 O OE1 . GLU F 3 284 ? -0.216  -9.394  24.204  1.00 64.29  ?  284 GLU F OE1 1 
ATOM   7894 O OE2 . GLU F 3 284 ? -0.821  -11.352 25.027  1.00 61.66  ?  284 GLU F OE2 1 
ATOM   7895 N N   . ASN F 3 285 ? -1.185  -12.033 18.712  1.00 70.30  ?  285 ASN F N   1 
ATOM   7896 C CA  . ASN F 3 285 ? -2.188  -12.509 17.758  1.00 64.53  ?  285 ASN F CA  1 
ATOM   7897 C C   . ASN F 3 285 ? -1.971  -11.783 16.426  1.00 65.02  ?  285 ASN F C   1 
ATOM   7898 O O   . ASN F 3 285 ? -2.712  -10.878 16.041  1.00 73.29  ?  285 ASN F O   1 
ATOM   7899 C CB  . ASN F 3 285 ? -3.605  -12.289 18.287  1.00 60.82  ?  285 ASN F CB  1 
ATOM   7900 C CG  . ASN F 3 285 ? -4.655  -12.944 17.420  1.00 79.42  ?  285 ASN F CG  1 
ATOM   7901 O OD1 . ASN F 3 285 ? -4.438  -14.025 16.873  1.00 87.43  ?  285 ASN F OD1 1 
ATOM   7902 N ND2 . ASN F 3 285 ? -5.802  -12.284 17.276  1.00 82.56  ?  285 ASN F ND2 1 
ATOM   7903 N N   . VAL F 3 286 ? -0.946  -12.206 15.701  1.00 64.72  ?  286 VAL F N   1 
ATOM   7904 C CA  . VAL F 3 286 ? -0.608  -11.591 14.427  1.00 69.07  ?  286 VAL F CA  1 
ATOM   7905 C C   . VAL F 3 286 ? -1.431  -12.242 13.321  1.00 73.61  ?  286 VAL F C   1 
ATOM   7906 O O   . VAL F 3 286 ? -1.853  -13.395 13.422  1.00 80.62  ?  286 VAL F O   1 
ATOM   7907 C CB  . VAL F 3 286 ? 0.905   -11.704 14.146  1.00 73.72  ?  286 VAL F CB  1 
ATOM   7908 C CG1 . VAL F 3 286 ? 1.298   -10.886 12.930  1.00 75.75  ?  286 VAL F CG1 1 
ATOM   7909 C CG2 . VAL F 3 286 ? 1.696   -11.259 15.358  1.00 75.94  ?  286 VAL F CG2 1 
ATOM   7910 N N   . LYS F 3 287 ? -1.654  -11.495 12.237  1.00 73.73  ?  287 LYS F N   1 
ATOM   7911 C CA  . LYS F 3 287 ? -2.469  -11.967 11.128  1.00 76.15  ?  287 LYS F CA  1 
ATOM   7912 C C   . LYS F 3 287 ? -1.675  -12.327 9.880   1.00 78.91  ?  287 LYS F C   1 
ATOM   7913 O O   . LYS F 3 287 ? -2.212  -13.022 9.012   1.00 82.39  ?  287 LYS F O   1 
ATOM   7914 C CB  . LYS F 3 287 ? -3.517  -10.909 10.757  1.00 75.91  ?  287 LYS F CB  1 
ATOM   7915 C CG  . LYS F 3 287 ? -4.479  -10.574 11.881  1.00 79.97  ?  287 LYS F CG  1 
ATOM   7916 C CD  . LYS F 3 287 ? -5.364  -11.759 12.234  1.00 82.57  ?  287 LYS F CD  1 
ATOM   7917 C CE  . LYS F 3 287 ? -6.374  -11.366 13.299  1.00 91.76  ?  287 LYS F CE  1 
ATOM   7918 N NZ  . LYS F 3 287 ? -7.267  -12.489 13.683  1.00 89.44  ?  287 LYS F NZ  1 
ATOM   7919 N N   . THR F 3 288 ? -0.427  -11.878 9.765   1.00 75.27  ?  288 THR F N   1 
ATOM   7920 C CA  . THR F 3 288 ? 0.441   -12.210 8.644   1.00 76.64  ?  288 THR F CA  1 
ATOM   7921 C C   . THR F 3 288 ? 1.517   -13.186 9.110   1.00 80.79  ?  288 THR F C   1 
ATOM   7922 O O   . THR F 3 288 ? 1.535   -13.625 10.261  1.00 75.91  ?  288 THR F O   1 
ATOM   7923 C CB  . THR F 3 288 ? 1.071   -10.953 8.036   1.00 77.95  ?  288 THR F CB  1 
ATOM   7924 O OG1 . THR F 3 288 ? 2.249   -10.604 8.772   1.00 84.36  ?  288 THR F OG1 1 
ATOM   7925 C CG2 . THR F 3 288 ? 0.093   -9.787  8.078   1.00 79.71  ?  288 THR F CG2 1 
ATOM   7926 N N   . THR F 3 289 ? 2.436   -13.514 8.199   1.00 85.18  ?  289 THR F N   1 
ATOM   7927 C CA  . THR F 3 289 ? 3.545   -14.412 8.494   1.00 83.28  ?  289 THR F CA  1 
ATOM   7928 C C   . THR F 3 289 ? 4.786   -13.680 9.004   1.00 81.27  ?  289 THR F C   1 
ATOM   7929 O O   . THR F 3 289 ? 5.898   -14.212 8.898   1.00 80.02  ?  289 THR F O   1 
ATOM   7930 C CB  . THR F 3 289 ? 3.897   -15.238 7.252   1.00 86.41  ?  289 THR F CB  1 
ATOM   7931 O OG1 . THR F 3 289 ? 4.205   -14.361 6.161   1.00 86.57  ?  289 THR F OG1 1 
ATOM   7932 C CG2 . THR F 3 289 ? 2.728   -16.122 6.855   1.00 85.48  ?  289 THR F CG2 1 
ATOM   7933 N N   . GLN F 3 290 ? 4.576   -12.538 9.650   1.00 82.22  ?  290 GLN F N   1 
ATOM   7934 C CA  . GLN F 3 290 ? 5.723   -11.759 10.178  1.00 83.19  ?  290 GLN F CA  1 
ATOM   7935 C C   . GLN F 3 290 ? 5.393   -11.063 11.504  1.00 80.55  ?  290 GLN F C   1 
ATOM   7936 O O   . GLN F 3 290 ? 4.235   -10.686 11.686  1.00 74.70  ?  290 GLN F O   1 
ATOM   7937 C CB  . GLN F 3 290 ? 6.190   -10.747 9.130   1.00 78.14  ?  290 GLN F CB  1 
ATOM   7938 C CG  . GLN F 3 290 ? 5.391   -9.456  9.121   1.00 82.12  ?  290 GLN F CG  1 
ATOM   7939 C CD  . GLN F 3 290 ? 6.099   -8.384  8.332   1.00 90.12  ?  290 GLN F CD  1 
ATOM   7940 O OE1 . GLN F 3 290 ? 7.169   -8.606  7.773   1.00 90.67  ?  290 GLN F OE1 1 
ATOM   7941 N NE2 . GLN F 3 290 ? 5.501   -7.205  8.281   1.00 85.72  ?  290 GLN F NE2 1 
ATOM   7942 N N   . CYS F 3 291 ? 6.376   -10.943 12.401  1.00 83.93  ?  291 CYS F N   1 
ATOM   7943 C CA  . CYS F 3 291 ? 6.217   -10.167 13.664  1.00 83.44  ?  291 CYS F CA  1 
ATOM   7944 C C   . CYS F 3 291 ? 7.305   -9.097  13.705  1.00 79.54  ?  291 CYS F C   1 
ATOM   7945 O O   . CYS F 3 291 ? 8.482   -9.454  13.598  1.00 77.36  ?  291 CYS F O   1 
ATOM   7946 C CB  . CYS F 3 291 ? 6.380   -11.021 14.913  1.00 79.28  ?  291 CYS F CB  1 
ATOM   7947 S SG  . CYS F 3 291 ? 6.699   -10.074 16.422  1.00 87.59  ?  291 CYS F SG  1 
ATOM   7948 N N   . VAL F 3 292 ? 6.919   -7.830  13.820  1.00 78.35  ?  292 VAL F N   1 
ATOM   7949 C CA  . VAL F 3 292 ? 7.941   -6.756  13.973  1.00 78.03  ?  292 VAL F CA  1 
ATOM   7950 C C   . VAL F 3 292 ? 7.780   -6.142  15.359  1.00 69.21  ?  292 VAL F C   1 
ATOM   7951 O O   . VAL F 3 292 ? 6.656   -5.828  15.745  1.00 64.36  ?  292 VAL F O   1 
ATOM   7952 C CB  . VAL F 3 292 ? 7.879   -5.712  12.840  1.00 79.45  ?  292 VAL F CB  1 
ATOM   7953 C CG1 . VAL F 3 292 ? 6.451   -5.368  12.457  1.00 75.61  ?  292 VAL F CG1 1 
ATOM   7954 C CG2 . VAL F 3 292 ? 8.677   -4.461  13.169  1.00 70.96  ?  292 VAL F CG2 1 
ATOM   7955 N N   . PHE F 3 293 ? 8.883   -6.002  16.074  1.00 67.50  ?  293 PHE F N   1 
ATOM   7956 C CA  . PHE F 3 293 ? 8.835   -5.500  17.441  1.00 68.68  ?  293 PHE F CA  1 
ATOM   7957 C C   . PHE F 3 293 ? 10.098  -4.710  17.737  1.00 66.70  ?  293 PHE F C   1 
ATOM   7958 O O   . PHE F 3 293 ? 11.163  -5.025  17.195  1.00 66.25  ?  293 PHE F O   1 
ATOM   7959 C CB  . PHE F 3 293 ? 8.663   -6.632  18.470  1.00 61.97  ?  293 PHE F CB  1 
ATOM   7960 C CG  . PHE F 3 293 ? 9.718   -7.705  18.396  1.00 67.52  ?  293 PHE F CG  1 
ATOM   7961 C CD1 . PHE F 3 293 ? 9.502   -8.859  17.653  1.00 70.58  ?  293 PHE F CD1 1 
ATOM   7962 C CD2 . PHE F 3 293 ? 10.915  -7.578  19.088  1.00 64.17  ?  293 PHE F CD2 1 
ATOM   7963 C CE1 . PHE F 3 293 ? 10.464  -9.859  17.585  1.00 63.67  ?  293 PHE F CE1 1 
ATOM   7964 C CE2 . PHE F 3 293 ? 11.879  -8.575  19.024  1.00 68.09  ?  293 PHE F CE2 1 
ATOM   7965 C CZ  . PHE F 3 293 ? 11.651  -9.720  18.272  1.00 58.91  ?  293 PHE F CZ  1 
ATOM   7966 N N   . PRO F 3 294 ? 10.015  -3.689  18.593  1.00 63.56  ?  294 PRO F N   1 
ATOM   7967 C CA  . PRO F 3 294 ? 11.198  -2.877  18.898  1.00 61.26  ?  294 PRO F CA  1 
ATOM   7968 C C   . PRO F 3 294 ? 12.307  -3.699  19.542  1.00 58.50  ?  294 PRO F C   1 
ATOM   7969 O O   . PRO F 3 294 ? 12.061  -4.708  20.206  1.00 57.27  ?  294 PRO F O   1 
ATOM   7970 C CB  . PRO F 3 294 ? 10.659  -1.820  19.869  1.00 57.44  ?  294 PRO F CB  1 
ATOM   7971 C CG  . PRO F 3 294 ? 9.196   -1.778  19.615  1.00 56.50  ?  294 PRO F CG  1 
ATOM   7972 C CD  . PRO F 3 294 ? 8.805   -3.172  19.253  1.00 60.57  ?  294 PRO F CD  1 
ATOM   7973 N N   . GLN F 3 295 ? 13.545  -3.239  19.349  1.00 56.26  ?  295 GLN F N   1 
ATOM   7974 C CA  . GLN F 3 295 ? 14.700  -3.934  19.902  1.00 55.90  ?  295 GLN F CA  1 
ATOM   7975 C C   . GLN F 3 295 ? 14.805  -3.796  21.414  1.00 51.12  ?  295 GLN F C   1 
ATOM   7976 O O   . GLN F 3 295 ? 15.428  -4.651  22.054  1.00 54.12  ?  295 GLN F O   1 
ATOM   7977 C CB  . GLN F 3 295 ? 15.988  -3.433  19.248  1.00 60.95  ?  295 GLN F CB  1 
ATOM   7978 C CG  . GLN F 3 295 ? 16.106  -3.774  17.779  1.00 68.32  ?  295 GLN F CG  1 
ATOM   7979 C CD  . GLN F 3 295 ? 17.389  -3.258  17.170  1.00 74.57  ?  295 GLN F CD  1 
ATOM   7980 O OE1 . GLN F 3 295 ? 18.387  -3.068  17.865  1.00 77.19  ?  295 GLN F OE1 1 
ATOM   7981 N NE2 . GLN F 3 295 ? 17.370  -3.023  15.866  1.00 80.70  ?  295 GLN F NE2 1 
ATOM   7982 N N   . ASN F 3 296 ? 14.231  -2.746  22.003  1.00 50.19  ?  296 ASN F N   1 
ATOM   7983 C CA  . ASN F 3 296 ? 14.251  -2.593  23.451  1.00 50.40  ?  296 ASN F CA  1 
ATOM   7984 C C   . ASN F 3 296 ? 13.274  -3.532  24.150  1.00 50.56  ?  296 ASN F C   1 
ATOM   7985 O O   . ASN F 3 296 ? 13.095  -3.428  25.369  1.00 46.25  ?  296 ASN F O   1 
ATOM   7986 C CB  . ASN F 3 296 ? 13.979  -1.134  23.846  1.00 50.76  ?  296 ASN F CB  1 
ATOM   7987 C CG  . ASN F 3 296 ? 12.737  -0.564  23.190  1.00 54.67  ?  296 ASN F CG  1 
ATOM   7988 O OD1 . ASN F 3 296 ? 12.775  -0.134  22.039  1.00 64.05  ?  296 ASN F OD1 1 
ATOM   7989 N ND2 . ASN F 3 296 ? 11.634  -0.539  23.926  1.00 59.84  ?  296 ASN F ND2 1 
ATOM   7990 N N   . VAL F 3 297 ? 12.638  -4.441  23.406  1.00 48.82  ?  297 VAL F N   1 
ATOM   7991 C CA  . VAL F 3 297 ? 11.964  -5.572  24.035  1.00 46.71  ?  297 VAL F CA  1 
ATOM   7992 C C   . VAL F 3 297 ? 12.977  -6.451  24.752  1.00 45.69  ?  297 VAL F C   1 
ATOM   7993 O O   . VAL F 3 297 ? 12.680  -7.030  25.804  1.00 46.79  ?  297 VAL F O   1 
ATOM   7994 C CB  . VAL F 3 297 ? 11.161  -6.371  22.986  1.00 50.72  ?  297 VAL F CB  1 
ATOM   7995 C CG1 . VAL F 3 297 ? 10.788  -7.747  23.518  1.00 43.47  ?  297 VAL F CG1 1 
ATOM   7996 C CG2 . VAL F 3 297 ? 9.906   -5.615  22.579  1.00 49.99  ?  297 VAL F CG2 1 
ATOM   7997 N N   . PHE F 3 298 ? 14.192  -6.537  24.223  1.00 43.15  ?  298 PHE F N   1 
ATOM   7998 C CA  . PHE F 3 298 ? 15.240  -7.368  24.787  1.00 45.43  ?  298 PHE F CA  1 
ATOM   7999 C C   . PHE F 3 298 ? 16.349  -6.510  25.371  1.00 45.28  ?  298 PHE F C   1 
ATOM   8000 O O   . PHE F 3 298 ? 16.507  -5.336  25.032  1.00 49.37  ?  298 PHE F O   1 
ATOM   8001 C CB  . PHE F 3 298 ? 15.843  -8.301  23.730  1.00 48.38  ?  298 PHE F CB  1 
ATOM   8002 C CG  . PHE F 3 298 ? 14.884  -9.313  23.201  1.00 48.17  ?  298 PHE F CG  1 
ATOM   8003 C CD1 . PHE F 3 298 ? 13.922  -9.867  24.024  1.00 45.95  ?  298 PHE F CD1 1 
ATOM   8004 C CD2 . PHE F 3 298 ? 14.935  -9.704  21.873  1.00 51.97  ?  298 PHE F CD2 1 
ATOM   8005 C CE1 . PHE F 3 298 ? 13.031  -10.793 23.535  1.00 46.71  ?  298 PHE F CE1 1 
ATOM   8006 C CE2 . PHE F 3 298 ? 14.046  -10.634 21.377  1.00 43.88  ?  298 PHE F CE2 1 
ATOM   8007 C CZ  . PHE F 3 298 ? 13.091  -11.174 22.207  1.00 46.77  ?  298 PHE F CZ  1 
ATOM   8008 N N   . GLN F 3 299 ? 17.115  -7.122  26.265  1.00 49.54  ?  299 GLN F N   1 
ATOM   8009 C CA  . GLN F 3 299 ? 18.394  -6.587  26.686  1.00 46.68  ?  299 GLN F CA  1 
ATOM   8010 C C   . GLN F 3 299 ? 19.489  -7.197  25.814  1.00 54.39  ?  299 GLN F C   1 
ATOM   8011 O O   . GLN F 3 299 ? 19.218  -7.945  24.871  1.00 58.64  ?  299 GLN F O   1 
ATOM   8012 C CB  . GLN F 3 299 ? 18.619  -6.877  28.165  1.00 41.80  ?  299 GLN F CB  1 
ATOM   8013 C CG  . GLN F 3 299 ? 17.515  -6.349  29.054  1.00 43.72  ?  299 GLN F CG  1 
ATOM   8014 C CD  . GLN F 3 299 ? 17.714  -6.739  30.498  1.00 41.10  ?  299 GLN F CD  1 
ATOM   8015 O OE1 . GLN F 3 299 ? 18.684  -7.413  30.834  1.00 42.03  ?  299 GLN F OE1 1 
ATOM   8016 N NE2 . GLN F 3 299 ? 16.795  -6.322  31.362  1.00 39.97  ?  299 GLN F NE2 1 
ATOM   8017 N N   . LYS F 3 300 ? 20.744  -6.885  26.121  1.00 52.49  ?  300 LYS F N   1 
ATOM   8018 C CA  . LYS F 3 300 ? 21.859  -7.539  25.443  1.00 58.30  ?  300 LYS F CA  1 
ATOM   8019 C C   . LYS F 3 300 ? 22.039  -8.924  26.050  1.00 51.74  ?  300 LYS F C   1 
ATOM   8020 O O   . LYS F 3 300 ? 22.506  -9.055  27.185  1.00 55.36  ?  300 LYS F O   1 
ATOM   8021 C CB  . LYS F 3 300 ? 23.132  -6.704  25.549  1.00 68.28  ?  300 LYS F CB  1 
ATOM   8022 C CG  . LYS F 3 300 ? 23.223  -5.612  24.488  1.00 67.29  ?  300 LYS F CG  1 
ATOM   8023 C CD  . LYS F 3 300 ? 24.525  -4.842  24.569  1.00 72.92  ?  300 LYS F CD  1 
ATOM   8024 C CE  . LYS F 3 300 ? 24.608  -3.808  23.454  1.00 83.38  ?  300 LYS F CE  1 
ATOM   8025 N NZ  . LYS F 3 300 ? 25.995  -3.308  23.234  1.00 80.34  ?  300 LYS F NZ  1 
ATOM   8026 N N   . GLY F 3 301 ? 21.646  -9.949  25.308  1.00 56.90  ?  301 GLY F N   1 
ATOM   8027 C CA  . GLY F 3 301 ? 21.732  -11.307 25.804  1.00 60.43  ?  301 GLY F CA  1 
ATOM   8028 C C   . GLY F 3 301 ? 21.462  -12.319 24.713  1.00 58.50  ?  301 GLY F C   1 
ATOM   8029 O O   . GLY F 3 301 ? 21.484  -11.996 23.524  1.00 59.11  ?  301 GLY F O   1 
ATOM   8030 N N   . ILE F 3 302 ? 21.213  -13.558 25.135  1.00 60.87  ?  302 ILE F N   1 
ATOM   8031 C CA  . ILE F 3 302 ? 20.890  -14.660 24.231  1.00 59.78  ?  302 ILE F CA  1 
ATOM   8032 C C   . ILE F 3 302 ? 19.448  -15.061 24.482  1.00 52.76  ?  302 ILE F C   1 
ATOM   8033 O O   . ILE F 3 302 ? 19.089  -15.443 25.603  1.00 53.80  ?  302 ILE F O   1 
ATOM   8034 C CB  . ILE F 3 302 ? 21.805  -15.874 24.438  1.00 64.74  ?  302 ILE F CB  1 
ATOM   8035 C CG1 . ILE F 3 302 ? 23.264  -15.462 24.558  1.00 69.34  ?  302 ILE F CG1 1 
ATOM   8036 C CG2 . ILE F 3 302 ? 21.659  -16.841 23.273  1.00 54.86  ?  302 ILE F CG2 1 
ATOM   8037 C CD1 . ILE F 3 302 ? 24.126  -16.638 24.866  1.00 71.24  ?  302 ILE F CD1 1 
ATOM   8038 N N   . TYR F 3 303 ? 18.633  -15.011 23.438  1.00 52.52  ?  303 TYR F N   1 
ATOM   8039 C CA  . TYR F 3 303 ? 17.217  -15.302 23.562  1.00 53.28  ?  303 TYR F CA  1 
ATOM   8040 C C   . TYR F 3 303 ? 16.792  -16.340 22.532  1.00 55.96  ?  303 TYR F C   1 
ATOM   8041 O O   . TYR F 3 303 ? 17.405  -16.501 21.473  1.00 56.56  ?  303 TYR F O   1 
ATOM   8042 C CB  . TYR F 3 303 ? 16.370  -14.033 23.405  1.00 49.16  ?  303 TYR F CB  1 
ATOM   8043 C CG  . TYR F 3 303 ? 16.629  -12.964 24.447  1.00 51.16  ?  303 TYR F CG  1 
ATOM   8044 C CD1 . TYR F 3 303 ? 15.900  -12.929 25.627  1.00 50.45  ?  303 TYR F CD1 1 
ATOM   8045 C CD2 . TYR F 3 303 ? 17.590  -11.977 24.242  1.00 50.47  ?  303 TYR F CD2 1 
ATOM   8046 C CE1 . TYR F 3 303 ? 16.122  -11.946 26.578  1.00 50.73  ?  303 TYR F CE1 1 
ATOM   8047 C CE2 . TYR F 3 303 ? 17.820  -10.993 25.188  1.00 51.59  ?  303 TYR F CE2 1 
ATOM   8048 C CZ  . TYR F 3 303 ? 17.080  -10.981 26.353  1.00 50.38  ?  303 TYR F CZ  1 
ATOM   8049 O OH  . TYR F 3 303 ? 17.294  -10.005 27.299  1.00 44.39  ?  303 TYR F OH  1 
ATOM   8050 N N   . LEU F 3 304 ? 15.713  -17.039 22.863  1.00 53.69  ?  304 LEU F N   1 
ATOM   8051 C CA  . LEU F 3 304 ? 15.088  -18.023 21.999  1.00 58.56  ?  304 LEU F CA  1 
ATOM   8052 C C   . LEU F 3 304 ? 13.731  -17.499 21.563  1.00 57.28  ?  304 LEU F C   1 
ATOM   8053 O O   . LEU F 3 304 ? 12.992  -16.926 22.370  1.00 55.86  ?  304 LEU F O   1 
ATOM   8054 C CB  . LEU F 3 304 ? 14.905  -19.358 22.726  1.00 54.90  ?  304 LEU F CB  1 
ATOM   8055 C CG  . LEU F 3 304 ? 16.194  -20.020 23.196  1.00 55.69  ?  304 LEU F CG  1 
ATOM   8056 C CD1 . LEU F 3 304 ? 15.864  -21.244 24.026  1.00 58.77  ?  304 LEU F CD1 1 
ATOM   8057 C CD2 . LEU F 3 304 ? 17.062  -20.367 22.006  1.00 57.61  ?  304 LEU F CD2 1 
ATOM   8058 N N   . LEU F 3 305 ? 13.394  -17.735 20.300  1.00 60.83  ?  305 LEU F N   1 
ATOM   8059 C CA  . LEU F 3 305 ? 12.094  -17.371 19.758  1.00 54.12  ?  305 LEU F CA  1 
ATOM   8060 C C   . LEU F 3 305 ? 11.375  -18.616 19.249  1.00 59.40  ?  305 LEU F C   1 
ATOM   8061 O O   . LEU F 3 305 ? 12.002  -19.571 18.766  1.00 55.58  ?  305 LEU F O   1 
ATOM   8062 C CB  . LEU F 3 305 ? 12.217  -16.323 18.642  1.00 54.19  ?  305 LEU F CB  1 
ATOM   8063 C CG  . LEU F 3 305 ? 12.634  -14.912 19.081  1.00 60.20  ?  305 LEU F CG  1 
ATOM   8064 C CD1 . LEU F 3 305 ? 12.985  -14.043 17.884  1.00 57.56  ?  305 LEU F CD1 1 
ATOM   8065 C CD2 . LEU F 3 305 ? 11.546  -14.249 19.920  1.00 50.67  ?  305 LEU F CD2 1 
ATOM   8066 N N   . ARG F 3 306 ? 10.043  -18.578 19.367  1.00 57.74  ?  306 ARG F N   1 
ATOM   8067 C CA  . ARG F 3 306 ? 9.138   -19.660 19.007  1.00 53.58  ?  306 ARG F CA  1 
ATOM   8068 C C   . ARG F 3 306 ? 7.893   -19.064 18.363  1.00 56.15  ?  306 ARG F C   1 
ATOM   8069 O O   . ARG F 3 306 ? 7.476   -17.961 18.716  1.00 56.81  ?  306 ARG F O   1 
ATOM   8070 C CB  . ARG F 3 306 ? 8.729   -20.427 20.272  1.00 53.83  ?  306 ARG F CB  1 
ATOM   8071 C CG  . ARG F 3 306 ? 9.801   -21.168 21.009  1.00 54.01  ?  306 ARG F CG  1 
ATOM   8072 C CD  . ARG F 3 306 ? 9.180   -21.755 22.262  1.00 59.90  ?  306 ARG F CD  1 
ATOM   8073 N NE  . ARG F 3 306 ? 8.134   -22.763 22.074  1.00 60.52  ?  306 ARG F NE  1 
ATOM   8074 C CZ  . ARG F 3 306 ? 7.410   -23.293 23.053  1.00 54.22  ?  306 ARG F CZ  1 
ATOM   8075 N NH1 . ARG F 3 306 ? 7.600   -22.906 24.303  1.00 58.39  ?  306 ARG F NH1 1 
ATOM   8076 N NH2 . ARG F 3 306 ? 6.508   -24.225 22.786  1.00 47.17  ?  306 ARG F NH2 1 
ATOM   8077 N N   . VAL F 3 307 ? 7.285   -19.797 17.426  1.00 60.00  ?  307 VAL F N   1 
ATOM   8078 C CA  . VAL F 3 307 ? 6.070   -19.341 16.753  1.00 63.97  ?  307 VAL F CA  1 
ATOM   8079 C C   . VAL F 3 307 ? 5.036   -20.462 16.749  1.00 63.09  ?  307 VAL F C   1 
ATOM   8080 O O   . VAL F 3 307 ? 5.376   -21.632 16.550  1.00 65.54  ?  307 VAL F O   1 
ATOM   8081 C CB  . VAL F 3 307 ? 6.347   -18.859 15.312  1.00 63.81  ?  307 VAL F CB  1 
ATOM   8082 C CG1 . VAL F 3 307 ? 5.118   -18.171 14.748  1.00 65.90  ?  307 VAL F CG1 1 
ATOM   8083 C CG2 . VAL F 3 307 ? 7.534   -17.909 15.282  1.00 62.17  ?  307 VAL F CG2 1 
ATOM   8084 N N   . GLN F 3 308 ? 3.770   -20.098 16.959  1.00 65.28  ?  308 GLN F N   1 
ATOM   8085 C CA  . GLN F 3 308 ? 2.652   -21.031 16.904  1.00 66.96  ?  308 GLN F CA  1 
ATOM   8086 C C   . GLN F 3 308 ? 1.561   -20.463 16.006  1.00 67.70  ?  308 GLN F C   1 
ATOM   8087 O O   . GLN F 3 308 ? 1.377   -19.247 15.921  1.00 68.91  ?  308 GLN F O   1 
ATOM   8088 C CB  . GLN F 3 308 ? 2.089   -21.315 18.302  1.00 64.28  ?  308 GLN F CB  1 
ATOM   8089 C CG  . GLN F 3 308 ? 1.082   -22.446 18.370  1.00 64.55  ?  308 GLN F CG  1 
ATOM   8090 C CD  . GLN F 3 308 ? 0.609   -22.706 19.787  1.00 65.45  ?  308 GLN F CD  1 
ATOM   8091 O OE1 . GLN F 3 308 ? 0.087   -21.813 20.452  1.00 69.97  ?  308 GLN F OE1 1 
ATOM   8092 N NE2 . GLN F 3 308 ? 0.798   -23.933 20.260  1.00 68.36  ?  308 GLN F NE2 1 
ATOM   8093 N N   . ALA F 3 309 ? 0.831   -21.352 15.342  1.00 67.79  ?  309 ALA F N   1 
ATOM   8094 C CA  . ALA F 3 309 ? -0.256  -20.963 14.460  1.00 73.03  ?  309 ALA F CA  1 
ATOM   8095 C C   . ALA F 3 309 ? -1.586  -21.454 15.015  1.00 71.25  ?  309 ALA F C   1 
ATOM   8096 O O   . ALA F 3 309 ? -1.641  -22.422 15.779  1.00 69.06  ?  309 ALA F O   1 
ATOM   8097 C CB  . ALA F 3 309 ? -0.046  -21.510 13.048  1.00 74.18  ?  309 ALA F CB  1 
ATOM   8098 N N   . SER F 3 310 ? -2.659  -20.756 14.645  1.00 75.19  ?  310 SER F N   1 
ATOM   8099 C CA  . SER F 3 310 ? -3.999  -21.139 15.061  1.00 81.85  ?  310 SER F CA  1 
ATOM   8100 C C   . SER F 3 310 ? -5.012  -20.666 14.029  1.00 85.92  ?  310 SER F C   1 
ATOM   8101 O O   . SER F 3 310 ? -4.807  -19.654 13.346  1.00 86.35  ?  310 SER F O   1 
ATOM   8102 C CB  . SER F 3 310 ? -4.353  -20.562 16.436  1.00 81.90  ?  310 SER F CB  1 
ATOM   8103 O OG  . SER F 3 310 ? -5.614  -21.039 16.872  1.00 86.28  ?  310 SER F OG  1 
ATOM   8104 N N   . ASP F 3 311 ? -6.107  -21.424 13.926  1.00 89.40  ?  311 ASP F N   1 
ATOM   8105 C CA  . ASP F 3 311 ? -7.225  -21.107 13.046  1.00 94.29  ?  311 ASP F CA  1 
ATOM   8106 C C   . ASP F 3 311 ? -8.476  -20.701 13.816  1.00 90.95  ?  311 ASP F C   1 
ATOM   8107 O O   . ASP F 3 311 ? -9.526  -20.487 13.201  1.00 93.22  ?  311 ASP F O   1 
ATOM   8108 C CB  . ASP F 3 311 ? -7.545  -22.296 12.133  1.00 91.44  ?  311 ASP F CB  1 
ATOM   8109 C CG  . ASP F 3 311 ? -7.805  -23.583 12.904  1.00 95.80  ?  311 ASP F CG  1 
ATOM   8110 O OD1 . ASP F 3 311 ? -7.891  -23.544 14.151  1.00 97.37  ?  311 ASP F OD1 1 
ATOM   8111 O OD2 . ASP F 3 311 ? -7.932  -24.641 12.253  1.00 96.25  ?  311 ASP F OD2 1 
ATOM   8112 N N   . GLY F 3 312 ? -8.389  -20.582 15.142  1.00 89.93  ?  312 GLY F N   1 
ATOM   8113 C CA  . GLY F 3 312 ? -9.521  -20.274 15.981  1.00 90.74  ?  312 GLY F CA  1 
ATOM   8114 C C   . GLY F 3 312 ? -10.056 -21.449 16.780  1.00 91.33  ?  312 GLY F C   1 
ATOM   8115 O O   . GLY F 3 312 ? -10.637 -21.240 17.852  1.00 92.38  ?  312 GLY F O   1 
ATOM   8116 N N   . ASN F 3 313 ? -9.875  -22.675 16.291  1.00 93.98  ?  313 ASN F N   1 
ATOM   8117 C CA  . ASN F 3 313 ? -10.351 -23.869 16.980  1.00 99.30  ?  313 ASN F CA  1 
ATOM   8118 C C   . ASN F 3 313 ? -9.216  -24.762 17.461  1.00 99.10  ?  313 ASN F C   1 
ATOM   8119 O O   . ASN F 3 313 ? -9.180  -25.138 18.637  1.00 98.79  ?  313 ASN F O   1 
ATOM   8120 C CB  . ASN F 3 313 ? -11.293 -24.657 16.050  1.00 105.34 ?  313 ASN F CB  1 
ATOM   8121 C CG  . ASN F 3 313 ? -11.916 -25.874 16.723  1.00 107.44 ?  313 ASN F CG  1 
ATOM   8122 O OD1 . ASN F 3 313 ? -11.923 -25.991 17.951  1.00 104.56 ?  313 ASN F OD1 1 
ATOM   8123 N ND2 . ASN F 3 313 ? -12.454 -26.781 15.914  1.00 104.35 ?  313 ASN F ND2 1 
ATOM   8124 N N   . ASN F 3 314 ? -8.287  -25.121 16.579  1.00 98.96  ?  314 ASN F N   1 
ATOM   8125 C CA  . ASN F 3 314 ? -7.134  -25.936 16.930  1.00 100.75 ?  314 ASN F CA  1 
ATOM   8126 C C   . ASN F 3 314 ? -5.860  -25.099 16.951  1.00 93.24  ?  314 ASN F C   1 
ATOM   8127 O O   . ASN F 3 314 ? -5.764  -24.062 16.286  1.00 84.97  ?  314 ASN F O   1 
ATOM   8128 C CB  . ASN F 3 314 ? -6.969  -27.111 15.964  1.00 102.61 ?  314 ASN F CB  1 
ATOM   8129 C CG  . ASN F 3 314 ? -7.950  -28.230 16.242  1.00 107.73 ?  314 ASN F CG  1 
ATOM   8130 O OD1 . ASN F 3 314 ? -8.940  -28.400 15.529  1.00 110.14 ?  314 ASN F OD1 1 
ATOM   8131 N ND2 . ASN F 3 314 ? -7.682  -29.001 17.292  1.00 107.92 ?  314 ASN F ND2 1 
ATOM   8132 N N   . THR F 3 315 ? -4.885  -25.561 17.730  1.00 95.00  ?  315 THR F N   1 
ATOM   8133 C CA  . THR F 3 315 ? -3.576  -24.931 17.829  1.00 88.96  ?  315 THR F CA  1 
ATOM   8134 C C   . THR F 3 315 ? -2.526  -25.798 17.140  1.00 82.87  ?  315 THR F C   1 
ATOM   8135 O O   . THR F 3 315 ? -2.598  -27.030 17.167  1.00 87.14  ?  315 THR F O   1 
ATOM   8136 C CB  . THR F 3 315 ? -3.175  -24.704 19.292  1.00 85.13  ?  315 THR F CB  1 
ATOM   8137 O OG1 . THR F 3 315 ? -2.733  -25.940 19.871  1.00 83.44  ?  315 THR F OG1 1 
ATOM   8138 C CG2 . THR F 3 315 ? -4.358  -24.173 20.094  1.00 90.95  ?  315 THR F CG2 1 
ATOM   8139 N N   . SER F 3 316 ? -1.543  -25.141 16.527  1.00 81.19  ?  316 SER F N   1 
ATOM   8140 C CA  . SER F 3 316 ? -0.463  -25.856 15.865  1.00 77.72  ?  316 SER F CA  1 
ATOM   8141 C C   . SER F 3 316 ? 0.620   -26.246 16.862  1.00 74.58  ?  316 SER F C   1 
ATOM   8142 O O   . SER F 3 316 ? 0.693   -25.738 17.984  1.00 72.60  ?  316 SER F O   1 
ATOM   8143 C CB  . SER F 3 316 ? 0.160   -25.010 14.748  1.00 76.36  ?  316 SER F CB  1 
ATOM   8144 O OG  . SER F 3 316 ? 1.149   -24.122 15.248  1.00 73.34  ?  316 SER F OG  1 
ATOM   8145 N N   . PHE F 3 317 ? 1.466   -27.174 16.441  1.00 77.31  ?  317 PHE F N   1 
ATOM   8146 C CA  . PHE F 3 317 ? 2.665   -27.449 17.207  1.00 73.15  ?  317 PHE F CA  1 
ATOM   8147 C C   . PHE F 3 317 ? 3.599   -26.250 17.146  1.00 67.62  ?  317 PHE F C   1 
ATOM   8148 O O   . PHE F 3 317 ? 3.587   -25.470 16.189  1.00 69.23  ?  317 PHE F O   1 
ATOM   8149 C CB  . PHE F 3 317 ? 3.374   -28.695 16.680  1.00 76.55  ?  317 PHE F CB  1 
ATOM   8150 C CG  . PHE F 3 317 ? 2.723   -29.981 17.092  1.00 81.53  ?  317 PHE F CG  1 
ATOM   8151 C CD1 . PHE F 3 317 ? 3.014   -30.553 18.319  1.00 79.79  ?  317 PHE F CD1 1 
ATOM   8152 C CD2 . PHE F 3 317 ? 1.832   -30.626 16.250  1.00 86.86  ?  317 PHE F CD2 1 
ATOM   8153 C CE1 . PHE F 3 317 ? 2.422   -31.738 18.704  1.00 79.94  ?  317 PHE F CE1 1 
ATOM   8154 C CE2 . PHE F 3 317 ? 1.237   -31.812 16.629  1.00 83.59  ?  317 PHE F CE2 1 
ATOM   8155 C CZ  . PHE F 3 317 ? 1.533   -32.369 17.858  1.00 81.14  ?  317 PHE F CZ  1 
ATOM   8156 N N   . TRP F 3 318 ? 4.410   -26.106 18.184  1.00 60.87  ?  318 TRP F N   1 
ATOM   8157 C CA  . TRP F 3 318 ? 5.352   -25.003 18.238  1.00 61.58  ?  318 TRP F CA  1 
ATOM   8158 C C   . TRP F 3 318 ? 6.447   -25.197 17.199  1.00 65.78  ?  318 TRP F C   1 
ATOM   8159 O O   . TRP F 3 318 ? 6.890   -26.321 16.944  1.00 65.63  ?  318 TRP F O   1 
ATOM   8160 C CB  . TRP F 3 318 ? 5.944   -24.897 19.641  1.00 60.79  ?  318 TRP F CB  1 
ATOM   8161 C CG  . TRP F 3 318 ? 5.011   -24.212 20.576  1.00 63.60  ?  318 TRP F CG  1 
ATOM   8162 C CD1 . TRP F 3 318 ? 4.231   -24.789 21.539  1.00 56.23  ?  318 TRP F CD1 1 
ATOM   8163 C CD2 . TRP F 3 318 ? 4.746   -22.809 20.630  1.00 59.57  ?  318 TRP F CD2 1 
ATOM   8164 N NE1 . TRP F 3 318 ? 3.499   -23.825 22.190  1.00 53.22  ?  318 TRP F NE1 1 
ATOM   8165 C CE2 . TRP F 3 318 ? 3.800   -22.601 21.650  1.00 54.54  ?  318 TRP F CE2 1 
ATOM   8166 C CE3 . TRP F 3 318 ? 5.222   -21.705 19.914  1.00 59.38  ?  318 TRP F CE3 1 
ATOM   8167 C CZ2 . TRP F 3 318 ? 3.323   -21.335 21.972  1.00 58.07  ?  318 TRP F CZ2 1 
ATOM   8168 C CZ3 . TRP F 3 318 ? 4.753   -20.453 20.236  1.00 58.66  ?  318 TRP F CZ3 1 
ATOM   8169 C CH2 . TRP F 3 318 ? 3.806   -20.277 21.249  1.00 59.95  ?  318 TRP F CH2 1 
ATOM   8170 N N   . SER F 3 319 ? 6.862   -24.094 16.578  1.00 60.20  ?  319 SER F N   1 
ATOM   8171 C CA  . SER F 3 319 ? 7.926   -24.136 15.591  1.00 61.33  ?  319 SER F CA  1 
ATOM   8172 C C   . SER F 3 319 ? 9.261   -24.463 16.253  1.00 61.92  ?  319 SER F C   1 
ATOM   8173 O O   . SER F 3 319 ? 9.393   -24.498 17.480  1.00 59.61  ?  319 SER F O   1 
ATOM   8174 C CB  . SER F 3 319 ? 8.032   -22.804 14.852  1.00 71.70  ?  319 SER F CB  1 
ATOM   8175 O OG  . SER F 3 319 ? 8.638   -21.818 15.672  1.00 72.33  ?  319 SER F OG  1 
ATOM   8176 N N   . GLU F 3 320 ? 10.261  -24.711 15.414  1.00 69.17  ?  320 GLU F N   1 
ATOM   8177 C CA  . GLU F 3 320 ? 11.610  -24.945 15.906  1.00 77.49  ?  320 GLU F CA  1 
ATOM   8178 C C   . GLU F 3 320 ? 12.137  -23.696 16.609  1.00 73.65  ?  320 GLU F C   1 
ATOM   8179 O O   . GLU F 3 320 ? 12.062  -22.587 16.070  1.00 70.62  ?  320 GLU F O   1 
ATOM   8180 C CB  . GLU F 3 320 ? 12.516  -25.344 14.741  1.00 80.72  ?  320 GLU F CB  1 
ATOM   8181 C CG  . GLU F 3 320 ? 13.998  -25.229 15.024  1.00 97.64  ?  320 GLU F CG  1 
ATOM   8182 C CD  . GLU F 3 320 ? 14.845  -25.637 13.832  1.00 108.16 ?  320 GLU F CD  1 
ATOM   8183 O OE1 . GLU F 3 320 ? 14.344  -25.554 12.688  1.00 109.57 ?  320 GLU F OE1 1 
ATOM   8184 O OE2 . GLU F 3 320 ? 16.014  -26.029 14.037  1.00 112.35 ?  320 GLU F OE2 1 
ATOM   8185 N N   . GLU F 3 321 ? 12.661  -23.878 17.821  1.00 71.99  ?  321 GLU F N   1 
ATOM   8186 C CA  . GLU F 3 321 ? 13.152  -22.755 18.613  1.00 61.48  ?  321 GLU F CA  1 
ATOM   8187 C C   . GLU F 3 321 ? 14.431  -22.201 18.005  1.00 68.09  ?  321 GLU F C   1 
ATOM   8188 O O   . GLU F 3 321 ? 15.361  -22.953 17.699  1.00 75.98  ?  321 GLU F O   1 
ATOM   8189 C CB  . GLU F 3 321 ? 13.411  -23.196 20.053  1.00 55.07  ?  321 GLU F CB  1 
ATOM   8190 C CG  . GLU F 3 321 ? 12.208  -23.807 20.734  1.00 63.15  ?  321 GLU F CG  1 
ATOM   8191 C CD  . GLU F 3 321 ? 12.555  -24.520 22.031  1.00 67.74  ?  321 GLU F CD  1 
ATOM   8192 O OE1 . GLU F 3 321 ? 13.726  -24.437 22.457  1.00 66.25  ?  321 GLU F OE1 1 
ATOM   8193 O OE2 . GLU F 3 321 ? 11.652  -25.156 22.627  1.00 62.46  ?  321 GLU F OE2 1 
ATOM   8194 N N   . ILE F 3 322 ? 14.494  -20.884 17.838  1.00 68.57  ?  322 ILE F N   1 
ATOM   8195 C CA  . ILE F 3 322 ? 15.645  -20.249 17.207  1.00 69.34  ?  322 ILE F CA  1 
ATOM   8196 C C   . ILE F 3 322 ? 16.425  -19.463 18.253  1.00 70.06  ?  322 ILE F C   1 
ATOM   8197 O O   . ILE F 3 322 ? 15.837  -18.798 19.117  1.00 63.80  ?  322 ILE F O   1 
ATOM   8198 C CB  . ILE F 3 322 ? 15.237  -19.343 16.035  1.00 68.19  ?  322 ILE F CB  1 
ATOM   8199 C CG1 . ILE F 3 322 ? 14.329  -18.224 16.526  1.00 65.30  ?  322 ILE F CG1 1 
ATOM   8200 C CG2 . ILE F 3 322 ? 14.539  -20.169 14.964  1.00 74.27  ?  322 ILE F CG2 1 
ATOM   8201 C CD1 . ILE F 3 322 ? 14.191  -17.108 15.541  1.00 68.79  ?  322 ILE F CD1 1 
ATOM   8202 N N   . LYS F 3 323 ? 17.753  -19.548 18.169  1.00 69.16  ?  323 LYS F N   1 
ATOM   8203 C CA  . LYS F 3 323 ? 18.674  -18.915 19.101  1.00 62.93  ?  323 LYS F CA  1 
ATOM   8204 C C   . LYS F 3 323 ? 19.224  -17.633 18.492  1.00 65.72  ?  323 LYS F C   1 
ATOM   8205 O O   . LYS F 3 323 ? 19.558  -17.595 17.305  1.00 71.58  ?  323 LYS F O   1 
ATOM   8206 C CB  . LYS F 3 323 ? 19.824  -19.865 19.430  1.00 60.43  ?  323 LYS F CB  1 
ATOM   8207 C CG  . LYS F 3 323 ? 20.941  -19.277 20.271  1.00 61.00  ?  323 LYS F CG  1 
ATOM   8208 C CD  . LYS F 3 323 ? 21.976  -20.346 20.637  1.00 69.19  ?  323 LYS F CD  1 
ATOM   8209 C CE  . LYS F 3 323 ? 22.175  -20.465 22.138  1.00 63.20  ?  323 LYS F CE  1 
ATOM   8210 N NZ  . LYS F 3 323 ? 23.433  -21.187 22.477  1.00 68.00  ?  323 LYS F NZ  1 
ATOM   8211 N N   . PHE F 3 324 ? 19.328  -16.586 19.306  1.00 64.75  ?  324 PHE F N   1 
ATOM   8212 C CA  . PHE F 3 324 ? 19.702  -15.287 18.774  1.00 65.96  ?  324 PHE F CA  1 
ATOM   8213 C C   . PHE F 3 324 ? 20.469  -14.500 19.826  1.00 68.57  ?  324 PHE F C   1 
ATOM   8214 O O   . PHE F 3 324 ? 20.165  -14.575 21.018  1.00 67.97  ?  324 PHE F O   1 
ATOM   8215 C CB  . PHE F 3 324 ? 18.450  -14.528 18.323  1.00 72.51  ?  324 PHE F CB  1 
ATOM   8216 C CG  . PHE F 3 324 ? 18.735  -13.229 17.640  1.00 82.60  ?  324 PHE F CG  1 
ATOM   8217 C CD1 . PHE F 3 324 ? 18.257  -12.035 18.160  1.00 74.60  ?  324 PHE F CD1 1 
ATOM   8218 C CD2 . PHE F 3 324 ? 19.463  -13.205 16.456  1.00 85.05  ?  324 PHE F CD2 1 
ATOM   8219 C CE1 . PHE F 3 324 ? 18.511  -10.840 17.521  1.00 77.40  ?  324 PHE F CE1 1 
ATOM   8220 C CE2 . PHE F 3 324 ? 19.723  -12.012 15.808  1.00 82.06  ?  324 PHE F CE2 1 
ATOM   8221 C CZ  . PHE F 3 324 ? 19.249  -10.827 16.340  1.00 83.04  ?  324 PHE F CZ  1 
ATOM   8222 N N   . ASP F 3 325 ? 21.472  -13.760 19.369  1.00 75.77  ?  325 ASP F N   1 
ATOM   8223 C CA  . ASP F 3 325 ? 22.278  -12.876 20.200  1.00 75.22  ?  325 ASP F CA  1 
ATOM   8224 C C   . ASP F 3 325 ? 21.906  -11.445 19.846  1.00 74.13  ?  325 ASP F C   1 
ATOM   8225 O O   . ASP F 3 325 ? 21.842  -11.101 18.665  1.00 78.81  ?  325 ASP F O   1 
ATOM   8226 C CB  . ASP F 3 325 ? 23.772  -13.119 19.959  1.00 74.67  ?  325 ASP F CB  1 
ATOM   8227 C CG  . ASP F 3 325 ? 24.654  -12.463 21.003  1.00 82.83  ?  325 ASP F CG  1 
ATOM   8228 O OD1 . ASP F 3 325 ? 24.949  -13.121 22.025  1.00 86.01  ?  325 ASP F OD1 1 
ATOM   8229 O OD2 . ASP F 3 325 ? 25.065  -11.300 20.800  1.00 81.62  ?  325 ASP F OD2 1 
ATOM   8230 N N   . THR F 3 326 ? 21.604  -10.623 20.845  1.00 67.95  ?  326 THR F N   1 
ATOM   8231 C CA  . THR F 3 326 ? 21.194  -9.266  20.508  1.00 73.05  ?  326 THR F CA  1 
ATOM   8232 C C   . THR F 3 326 ? 22.367  -8.309  20.344  1.00 69.50  ?  326 THR F C   1 
ATOM   8233 O O   . THR F 3 326 ? 22.187  -7.233  19.765  1.00 71.23  ?  326 THR F O   1 
ATOM   8234 C CB  . THR F 3 326 ? 20.220  -8.716  21.554  1.00 66.94  ?  326 THR F CB  1 
ATOM   8235 O OG1 . THR F 3 326 ? 20.808  -8.806  22.855  1.00 63.00  ?  326 THR F OG1 1 
ATOM   8236 C CG2 . THR F 3 326 ? 18.903  -9.489  21.519  1.00 58.78  ?  326 THR F CG2 1 
ATOM   8237 N N   . GLU F 3 327 ? 23.544  -8.652  20.868  1.00 72.33  ?  327 GLU F N   1 
ATOM   8238 C CA  . GLU F 3 327 ? 24.762  -7.859  20.677  1.00 76.80  ?  327 GLU F CA  1 
ATOM   8239 C C   . GLU F 3 327 ? 25.521  -8.287  19.414  1.00 84.41  ?  327 GLU F C   1 
ATOM   8240 O O   . GLU F 3 327 ? 26.653  -8.769  19.480  1.00 91.16  ?  327 GLU F O   1 
ATOM   8241 C CB  . GLU F 3 327 ? 25.653  -7.967  21.909  1.00 73.11  ?  327 GLU F CB  1 
ATOM   8242 C CG  . GLU F 3 327 ? 26.787  -6.954  21.934  1.00 87.88  ?  327 GLU F CG  1 
ATOM   8243 C CD  . GLU F 3 327 ? 27.680  -7.117  23.146  1.00 91.24  ?  327 GLU F CD  1 
ATOM   8244 O OE1 . GLU F 3 327 ? 27.151  -7.323  24.255  1.00 89.23  ?  327 GLU F OE1 1 
ATOM   8245 O OE2 . GLU F 3 327 ? 28.919  -7.025  22.984  1.00 96.33  ?  327 GLU F OE2 1 
ATOM   8246 N N   . ILE F 3 328 ? 24.889  -8.129  18.243  1.00 90.84  ?  328 ILE F N   1 
ATOM   8247 C CA  . ILE F 3 328 ? 25.517  -8.563  16.987  1.00 92.92  ?  328 ILE F CA  1 
ATOM   8248 C C   . ILE F 3 328 ? 26.266  -7.429  16.269  1.00 99.85  ?  328 ILE F C   1 
ATOM   8249 O O   . ILE F 3 328 ? 26.898  -7.672  15.231  1.00 100.23 ?  328 ILE F O   1 
ATOM   8250 C CB  . ILE F 3 328 ? 24.463  -9.264  16.085  1.00 88.72  ?  328 ILE F CB  1 
ATOM   8251 C CG1 . ILE F 3 328 ? 24.048  -10.592 16.703  1.00 91.99  ?  328 ILE F CG1 1 
ATOM   8252 C CG2 . ILE F 3 328 ? 24.961  -9.611  14.692  1.00 98.11  ?  328 ILE F CG2 1 
ATOM   8253 C CD1 . ILE F 3 328 ? 23.029  -11.353 15.862  1.00 94.82  ?  328 ILE F CD1 1 
ATOM   8254 N N   . GLN F 3 329 ? 26.255  -6.212  16.817  1.00 103.84 ?  329 GLN F N   1 
ATOM   8255 C CA  . GLN F 3 329 ? 26.858  -4.996  16.209  1.00 102.03 ?  329 GLN F CA  1 
ATOM   8256 C C   . GLN F 3 329 ? 26.414  -4.794  14.763  1.00 102.28 ?  329 GLN F C   1 
ATOM   8257 O O   . GLN F 3 329 ? 25.214  -4.754  14.471  1.00 100.06 ?  329 GLN F O   1 
ATOM   8258 C CB  . GLN F 3 329 ? 28.409  -4.992  16.312  1.00 99.46  ?  329 GLN F CB  1 
ATOM   8259 C CG  . GLN F 3 329 ? 29.227  -6.047  15.541  1.00 95.68  ?  329 GLN F CG  1 
ATOM   8260 C CD  . GLN F 3 329 ? 29.576  -5.614  14.127  1.00 99.28  ?  329 GLN F CD  1 
ATOM   8261 O OE1 . GLN F 3 329 ? 29.505  -4.431  13.794  1.00 98.61  ?  329 GLN F OE1 1 
ATOM   8262 N NE2 . GLN F 3 329 ? 29.954  -6.574  13.287  1.00 90.39  ?  329 GLN F NE2 1 
HETATM 8263 O O   . HOH G 4 .   ? -9.193  37.853  22.086  1.00 59.11  ?  301 HOH A O   1 
HETATM 8264 O O   . HOH G 4 .   ? 2.505   26.770  49.233  1.00 63.43  ?  302 HOH A O   1 
HETATM 8265 O O   . HOH G 4 .   ? -2.977  8.043   -1.049  1.00 41.01  ?  303 HOH A O   1 
HETATM 8266 O O   . HOH G 4 .   ? -9.887  4.681   11.414  1.00 63.11  ?  304 HOH A O   1 
HETATM 8267 O O   . HOH G 4 .   ? -3.459  32.166  21.710  1.00 48.08  ?  305 HOH A O   1 
HETATM 8268 O O   . HOH G 4 .   ? -21.725 39.113  33.103  1.00 54.36  ?  306 HOH A O   1 
HETATM 8269 O O   . HOH G 4 .   ? -8.321  33.428  47.001  1.00 49.63  ?  307 HOH A O   1 
HETATM 8270 O O   . HOH G 4 .   ? -11.575 35.498  21.172  1.00 50.12  ?  308 HOH A O   1 
HETATM 8271 O O   . HOH G 4 .   ? -0.422  37.361  27.052  1.00 47.51  ?  309 HOH A O   1 
HETATM 8272 O O   . HOH G 4 .   ? 0.609   24.054  37.116  1.00 41.43  ?  310 HOH A O   1 
HETATM 8273 O O   . HOH G 4 .   ? -4.284  9.937   9.198   1.00 38.90  ?  311 HOH A O   1 
HETATM 8274 O O   . HOH G 4 .   ? -2.105  10.614  7.784   1.00 44.57  ?  312 HOH A O   1 
HETATM 8275 O O   . HOH G 4 .   ? -20.917 29.320  14.324  1.00 59.44  ?  313 HOH A O   1 
HETATM 8276 O O   . HOH G 4 .   ? -19.393 14.473  -0.588  1.00 60.80  ?  314 HOH A O   1 
HETATM 8277 O O   . HOH G 4 .   ? -6.560  24.499  21.897  1.00 47.96  ?  315 HOH A O   1 
HETATM 8278 O O   . HOH G 4 .   ? -7.492  20.625  28.952  1.00 47.96  ?  316 HOH A O   1 
HETATM 8279 O O   . HOH G 4 .   ? -0.740  22.209  36.512  1.00 40.16  ?  317 HOH A O   1 
HETATM 8280 O O   . HOH G 4 .   ? -24.361 27.936  12.377  1.00 48.35  ?  318 HOH A O   1 
HETATM 8281 O O   . HOH G 4 .   ? -22.453 29.072  11.447  1.00 51.30  ?  319 HOH A O   1 
HETATM 8282 O O   . HOH H 4 .   ? 23.311  32.006  25.073  1.00 47.31  ?  301 HOH B O   1 
HETATM 8283 O O   . HOH H 4 .   ? 6.627   43.689  36.531  1.00 49.64  ?  302 HOH B O   1 
HETATM 8284 O O   . HOH H 4 .   ? 0.072   6.413   7.732   1.00 54.28  ?  303 HOH B O   1 
HETATM 8285 O O   . HOH H 4 .   ? 1.493   19.479  30.226  1.00 44.00  ?  304 HOH B O   1 
HETATM 8286 O O   . HOH H 4 .   ? 5.477   35.952  41.861  1.00 48.37  ?  305 HOH B O   1 
HETATM 8287 O O   . HOH H 4 .   ? 8.304   14.253  18.216  1.00 47.01  ?  306 HOH B O   1 
HETATM 8288 O O   . HOH H 4 .   ? -0.385  21.486  -9.617  1.00 58.88  ?  307 HOH B O   1 
HETATM 8289 O O   . HOH H 4 .   ? 8.247   45.254  27.807  1.00 43.52  ?  308 HOH B O   1 
HETATM 8290 O O   . HOH H 4 .   ? 21.147  26.415  24.625  1.00 48.73  ?  309 HOH B O   1 
HETATM 8291 O O   . HOH H 4 .   ? 18.979  27.147  40.889  1.00 47.17  ?  310 HOH B O   1 
HETATM 8292 O O   . HOH H 4 .   ? 7.264   36.949  21.864  1.00 41.31  ?  311 HOH B O   1 
HETATM 8293 O O   . HOH H 4 .   ? 1.906   23.003  9.298   1.00 51.14  ?  312 HOH B O   1 
HETATM 8294 O O   . HOH H 4 .   ? 9.028   5.910   18.516  1.00 57.07  ?  313 HOH B O   1 
HETATM 8295 O O   . HOH H 4 .   ? -12.185 23.062  9.325   1.00 54.62  ?  314 HOH B O   1 
HETATM 8296 O O   . HOH H 4 .   ? 23.177  14.757  26.385  1.00 47.17  ?  315 HOH B O   1 
HETATM 8297 O O   . HOH H 4 .   ? 6.285   46.044  28.449  1.00 50.54  ?  316 HOH B O   1 
HETATM 8298 O O   . HOH I 4 .   ? -0.835  4.971   31.709  1.00 51.44  ?  301 HOH C O   1 
HETATM 8299 O O   . HOH I 4 .   ? -10.052 -8.491  39.125  1.00 46.16  ?  302 HOH C O   1 
HETATM 8300 O O   . HOH I 4 .   ? 3.952   -11.225 36.311  1.00 62.47  ?  303 HOH C O   1 
HETATM 8301 O O   . HOH I 4 .   ? 6.306   -7.372  27.681  1.00 40.78  ?  304 HOH C O   1 
HETATM 8302 O O   . HOH I 4 .   ? 5.580   -7.997  36.785  1.00 40.61  ?  305 HOH C O   1 
HETATM 8303 O O   . HOH I 4 .   ? -11.776 5.093   71.562  1.00 56.22  ?  306 HOH C O   1 
HETATM 8304 O O   . HOH I 4 .   ? -12.577 22.268  78.821  1.00 50.43  ?  307 HOH C O   1 
HETATM 8305 O O   . HOH I 4 .   ? 4.078   -5.728  53.368  1.00 45.32  ?  308 HOH C O   1 
HETATM 8306 O O   . HOH I 4 .   ? 10.474  0.634   26.707  1.00 48.10  ?  309 HOH C O   1 
HETATM 8307 O O   . HOH I 4 .   ? -13.688 -1.937  67.775  1.00 58.89  ?  310 HOH C O   1 
HETATM 8308 O O   . HOH I 4 .   ? 2.794   15.861  66.966  1.00 46.00  ?  311 HOH C O   1 
HETATM 8309 O O   . HOH I 4 .   ? -3.920  -8.139  36.540  1.00 42.36  ?  312 HOH C O   1 
HETATM 8310 O O   . HOH I 4 .   ? -0.443  2.308   53.852  1.00 53.96  ?  313 HOH C O   1 
HETATM 8311 O O   . HOH I 4 .   ? 8.518   3.043   38.518  1.00 42.54  ?  314 HOH C O   1 
HETATM 8312 O O   . HOH I 4 .   ? -6.555  -11.688 61.036  1.00 61.22  ?  315 HOH C O   1 
HETATM 8313 O O   . HOH I 4 .   ? 2.105   2.133   53.238  1.00 47.76  ?  316 HOH C O   1 
HETATM 8314 O O   . HOH J 4 .   ? 14.400  -16.390 37.710  1.00 52.78  ?  301 HOH D O   1 
HETATM 8315 O O   . HOH J 4 .   ? 12.944  -8.202  33.014  1.00 48.32  ?  302 HOH D O   1 
HETATM 8316 O O   . HOH J 4 .   ? 16.360  19.670  57.938  1.00 51.87  ?  303 HOH D O   1 
HETATM 8317 O O   . HOH J 4 .   ? 4.846   4.849   42.193  1.00 42.61  ?  304 HOH D O   1 
HETATM 8318 O O   . HOH J 4 .   ? 21.937  0.890   29.990  1.00 53.50  ?  305 HOH D O   1 
HETATM 8319 O O   . HOH J 4 .   ? 29.437  -7.601  51.225  1.00 50.40  ?  306 HOH D O   1 
HETATM 8320 O O   . HOH J 4 .   ? 16.069  -18.457 46.441  1.00 47.00  ?  307 HOH D O   1 
HETATM 8321 O O   . HOH J 4 .   ? 15.228  -10.716 52.490  1.00 40.98  ?  308 HOH D O   1 
HETATM 8322 O O   . HOH J 4 .   ? 14.031  -19.333 43.198  1.00 35.25  ?  309 HOH D O   1 
HETATM 8323 O O   . HOH J 4 .   ? 26.829  0.874   34.016  1.00 54.47  ?  310 HOH D O   1 
HETATM 8324 O O   . HOH J 4 .   ? 12.262  11.024  40.168  1.00 41.22  ?  311 HOH D O   1 
HETATM 8325 O O   . HOH J 4 .   ? 28.474  -1.784  35.923  1.00 55.15  ?  312 HOH D O   1 
HETATM 8326 O O   . HOH K 4 .   ? -6.493  64.090  58.770  1.00 62.52  ?  401 HOH E O   1 
HETATM 8327 O O   . HOH K 4 .   ? -2.114  56.563  53.967  1.00 62.96  ?  402 HOH E O   1 
HETATM 8328 O O   . HOH K 4 .   ? 14.837  46.271  37.779  1.00 57.33  ?  403 HOH E O   1 
HETATM 8329 O O   . HOH L 4 .   ? 12.173  -3.316  27.707  1.00 45.82  ?  401 HOH F O   1 
HETATM 8330 O O   . HOH L 4 .   ? 10.466  -26.071 25.308  1.00 53.85  ?  402 HOH F O   1 
# 
