data_8UWZ
# 
_entry.id   8UWZ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8UWZ         pdb_00008uwz 10.2210/pdb8uwz/pdb 
WWPDB D_1000278270 ?            ?                   
# 
_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       2024-11-13 
# 
_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                        8UWZ 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sachdev.sidhu@gmail.com 
_pdbx_contact_author.name_first         Sachdev 
_pdbx_contact_author.name_last          Sidhu 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7755-5918 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Singer, A.U.' 1 0000-0002-2247-0594 
'Bruce, H.'    2 ?                   
'Blazer, L.'   3 0000-0001-9594-4642 
'Sicheri, F.'  4 0000-0002-9824-2117 
'Adams, J.J.'  5 0000-0002-0182-922X 
'Sidhu, S.S.'  6 0000-0001-7755-5918 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'to be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Raamsizumab: A Potent Synthetic Human Anti-VEGF Neutralizing Fab for Treatment of Ocular Neovascularization Diseases' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Fellouse, F.A.'    1  ? 
primary 'Harit, R.K.'       2  ? 
primary 'Arun, S.'          3  ? 
primary 'Arora, R.'         4  ? 
primary 'Wagner, N.'        5  ? 
primary 'Antony, A.'        6  ? 
primary 'Wong, S.'          7  ? 
primary 'Yang, N.'          8  ? 
primary 'Rajakrishnan, S.'  9  ? 
primary 'Anthony, M.'       10 ? 
primary 'Gokul, S.'         11 ? 
primary 'Vinodh, S.'        12 ? 
primary 'Bhunia, S.'        13 ? 
primary 'Vinothini, T.M.'   14 ? 
primary 'Choubey, S.'       15 ? 
primary 'Rajendran, A.'     16 ? 
primary 'Srivastava, A.'    17 ? 
primary 'Seshagiri, S.'     18 ? 
primary 'Gross, M.L.'       19 ? 
primary 'Leung, D.W.'       20 ? 
primary 'Amarasinghe, G.K.' 21 ? 
primary 'Chaudhuri, A.'     22 ? 
primary 'Sidhu, S.S.'       23 ? 
primary 'Ramchand, C.N.'    24 ? 
# 
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 'Raamsizumab heavy chain' 24602.461 2 ? ?                                         ? ? 
2 polymer  man 'Raamsizumab light chain S1C variant' 23379.002 2 ? 'HAGLSSP replaced by QGTTS; Q165S, K167Y' ? ? 
3 polymer  syn 'Isoform VEGF121 of Vascular endothelial growth factor A, long form' 14078.085 2 ? ? ? ? 
4 branched man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   1 ? ? ? ? 
5 branched man 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542   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 
;EVQLVESGGGLVQPGGSLRLSCAASGFDLWYYSIHWVRQAPGKGLEWVAYIYPSYGYTYYADSVKGRFTISADTSKNTAY
LQMNSLRAEDTAVYYCARHAWYYGWGLDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVS
WNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
;
;EVQLVESGGGLVQPGGSLRLSCAASGFDLWYYSIHWVRQAPGKGLEWVAYIYPSYGYTYYADSVKGRFTISADTSKNTAY
LQMNSLRAEDTAVYYCARHAWYYGWGLDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVS
WNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
;
C,A ? 
2 'polypeptide(L)' no no 
;DIQMTQSPSSLSASVGDRVTITCRASQAAYGRVAWYQQKPGKAPKLLIYKASELYAGVPSRFSGSRSGTDFTLTISSLQP
EDFATYYCQQRGWYLFTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVSWYVDNALQSGNSQ
ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTQGTTSVTKSFNRGEC
;
;DIQMTQSPSSLSASVGDRVTITCRASQAAYGRVAWYQQKPGKAPKLLIYKASELYAGVPSRFSGSRSGTDFTLTISSLQP
EDFATYYCQQRGWYLFTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVSWYVDNALQSGNSQ
ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTQGTTSVTKSFNRGEC
;
D,B ? 
3 'polypeptide(L)' no no 
;APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQI
MRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQENCDKPRR
;
;APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQI
MRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQENCDKPRR
;
E,F ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   VAL n 
1 3   GLN n 
1 4   LEU n 
1 5   VAL n 
1 6   GLU n 
1 7   SER n 
1 8   GLY n 
1 9   GLY n 
1 10  GLY n 
1 11  LEU n 
1 12  VAL n 
1 13  GLN n 
1 14  PRO n 
1 15  GLY n 
1 16  GLY n 
1 17  SER n 
1 18  LEU n 
1 19  ARG n 
1 20  LEU n 
1 21  SER n 
1 22  CYS n 
1 23  ALA n 
1 24  ALA n 
1 25  SER n 
1 26  GLY n 
1 27  PHE n 
1 28  ASP n 
1 29  LEU n 
1 30  TRP n 
1 31  TYR n 
1 32  TYR n 
1 33  SER n 
1 34  ILE n 
1 35  HIS n 
1 36  TRP n 
1 37  VAL n 
1 38  ARG n 
1 39  GLN n 
1 40  ALA n 
1 41  PRO n 
1 42  GLY n 
1 43  LYS n 
1 44  GLY n 
1 45  LEU n 
1 46  GLU n 
1 47  TRP n 
1 48  VAL n 
1 49  ALA n 
1 50  TYR n 
1 51  ILE n 
1 52  TYR n 
1 53  PRO n 
1 54  SER n 
1 55  TYR n 
1 56  GLY n 
1 57  TYR n 
1 58  THR n 
1 59  TYR n 
1 60  TYR n 
1 61  ALA n 
1 62  ASP n 
1 63  SER n 
1 64  VAL n 
1 65  LYS n 
1 66  GLY n 
1 67  ARG n 
1 68  PHE n 
1 69  THR n 
1 70  ILE n 
1 71  SER n 
1 72  ALA n 
1 73  ASP n 
1 74  THR n 
1 75  SER n 
1 76  LYS n 
1 77  ASN n 
1 78  THR n 
1 79  ALA n 
1 80  TYR n 
1 81  LEU n 
1 82  GLN n 
1 83  MET n 
1 84  ASN n 
1 85  SER n 
1 86  LEU n 
1 87  ARG n 
1 88  ALA n 
1 89  GLU n 
1 90  ASP n 
1 91  THR n 
1 92  ALA n 
1 93  VAL n 
1 94  TYR n 
1 95  TYR n 
1 96  CYS n 
1 97  ALA n 
1 98  ARG n 
1 99  HIS n 
1 100 ALA n 
1 101 TRP n 
1 102 TYR n 
1 103 TYR n 
1 104 GLY n 
1 105 TRP n 
1 106 GLY n 
1 107 LEU n 
1 108 ASP n 
1 109 TYR n 
1 110 TRP n 
1 111 GLY n 
1 112 GLN n 
1 113 GLY n 
1 114 THR n 
1 115 LEU n 
1 116 VAL n 
1 117 THR n 
1 118 VAL n 
1 119 SER n 
1 120 SER n 
1 121 ALA n 
1 122 SER n 
1 123 THR n 
1 124 LYS n 
1 125 GLY n 
1 126 PRO n 
1 127 SER n 
1 128 VAL n 
1 129 PHE n 
1 130 PRO n 
1 131 LEU n 
1 132 ALA n 
1 133 PRO n 
1 134 SER n 
1 135 SER n 
1 136 LYS n 
1 137 SER n 
1 138 THR n 
1 139 SER n 
1 140 GLY n 
1 141 GLY n 
1 142 THR n 
1 143 ALA n 
1 144 ALA n 
1 145 LEU n 
1 146 GLY n 
1 147 CYS n 
1 148 LEU n 
1 149 VAL n 
1 150 LYS n 
1 151 ASP n 
1 152 TYR n 
1 153 PHE n 
1 154 PRO n 
1 155 GLU n 
1 156 PRO n 
1 157 VAL n 
1 158 THR n 
1 159 VAL n 
1 160 SER n 
1 161 TRP n 
1 162 ASN n 
1 163 SER n 
1 164 GLY n 
1 165 ALA n 
1 166 LEU n 
1 167 THR n 
1 168 SER n 
1 169 GLY n 
1 170 VAL n 
1 171 HIS n 
1 172 THR n 
1 173 PHE n 
1 174 PRO n 
1 175 ALA n 
1 176 VAL n 
1 177 LEU n 
1 178 GLN n 
1 179 SER n 
1 180 SER n 
1 181 GLY n 
1 182 LEU n 
1 183 TYR n 
1 184 SER n 
1 185 LEU n 
1 186 SER n 
1 187 SER n 
1 188 VAL n 
1 189 VAL n 
1 190 THR n 
1 191 VAL n 
1 192 PRO n 
1 193 SER n 
1 194 SER n 
1 195 SER n 
1 196 LEU n 
1 197 GLY n 
1 198 THR n 
1 199 GLN n 
1 200 THR n 
1 201 TYR n 
1 202 ILE n 
1 203 CYS n 
1 204 ASN n 
1 205 VAL n 
1 206 ASN n 
1 207 HIS n 
1 208 LYS n 
1 209 PRO n 
1 210 SER n 
1 211 ASN n 
1 212 THR n 
1 213 LYS n 
1 214 VAL n 
1 215 ASP n 
1 216 LYS n 
1 217 LYS n 
1 218 VAL n 
1 219 GLU n 
1 220 PRO n 
1 221 LYS n 
1 222 SER n 
1 223 CYS n 
1 224 ASP n 
1 225 LYS n 
1 226 THR n 
1 227 HIS n 
1 228 THR n 
2 1   ASP n 
2 2   ILE n 
2 3   GLN n 
2 4   MET n 
2 5   THR n 
2 6   GLN n 
2 7   SER n 
2 8   PRO n 
2 9   SER n 
2 10  SER n 
2 11  LEU n 
2 12  SER n 
2 13  ALA n 
2 14  SER n 
2 15  VAL n 
2 16  GLY n 
2 17  ASP n 
2 18  ARG n 
2 19  VAL n 
2 20  THR n 
2 21  ILE n 
2 22  THR n 
2 23  CYS n 
2 24  ARG n 
2 25  ALA n 
2 26  SER n 
2 27  GLN n 
2 28  ALA n 
2 29  ALA n 
2 30  TYR n 
2 31  GLY n 
2 32  ARG n 
2 33  VAL n 
2 34  ALA n 
2 35  TRP n 
2 36  TYR n 
2 37  GLN n 
2 38  GLN n 
2 39  LYS n 
2 40  PRO n 
2 41  GLY n 
2 42  LYS n 
2 43  ALA n 
2 44  PRO n 
2 45  LYS n 
2 46  LEU n 
2 47  LEU n 
2 48  ILE n 
2 49  TYR n 
2 50  LYS n 
2 51  ALA n 
2 52  SER n 
2 53  GLU n 
2 54  LEU n 
2 55  TYR n 
2 56  ALA n 
2 57  GLY n 
2 58  VAL n 
2 59  PRO n 
2 60  SER n 
2 61  ARG n 
2 62  PHE n 
2 63  SER n 
2 64  GLY n 
2 65  SER n 
2 66  ARG n 
2 67  SER n 
2 68  GLY n 
2 69  THR n 
2 70  ASP n 
2 71  PHE n 
2 72  THR n 
2 73  LEU n 
2 74  THR n 
2 75  ILE n 
2 76  SER n 
2 77  SER n 
2 78  LEU n 
2 79  GLN n 
2 80  PRO n 
2 81  GLU n 
2 82  ASP n 
2 83  PHE n 
2 84  ALA n 
2 85  THR n 
2 86  TYR n 
2 87  TYR n 
2 88  CYS n 
2 89  GLN n 
2 90  GLN n 
2 91  ARG n 
2 92  GLY n 
2 93  TRP n 
2 94  TYR n 
2 95  LEU n 
2 96  PHE n 
2 97  THR n 
2 98  PHE n 
2 99  GLY n 
2 100 GLN n 
2 101 GLY n 
2 102 THR n 
2 103 LYS n 
2 104 VAL n 
2 105 GLU n 
2 106 ILE n 
2 107 LYS n 
2 108 ARG n 
2 109 THR n 
2 110 VAL n 
2 111 ALA n 
2 112 ALA n 
2 113 PRO n 
2 114 SER n 
2 115 VAL n 
2 116 PHE n 
2 117 ILE n 
2 118 PHE n 
2 119 PRO n 
2 120 PRO n 
2 121 SER n 
2 122 ASP n 
2 123 GLU n 
2 124 GLN n 
2 125 LEU n 
2 126 LYS n 
2 127 SER n 
2 128 GLY n 
2 129 THR n 
2 130 ALA n 
2 131 SER n 
2 132 VAL n 
2 133 VAL n 
2 134 CYS n 
2 135 LEU n 
2 136 LEU n 
2 137 ASN n 
2 138 ASN n 
2 139 PHE n 
2 140 TYR n 
2 141 PRO n 
2 142 ARG n 
2 143 GLU n 
2 144 ALA n 
2 145 LYS n 
2 146 VAL n 
2 147 SER n 
2 148 TRP n 
2 149 TYR n 
2 150 VAL n 
2 151 ASP n 
2 152 ASN n 
2 153 ALA n 
2 154 LEU n 
2 155 GLN n 
2 156 SER n 
2 157 GLY n 
2 158 ASN n 
2 159 SER n 
2 160 GLN n 
2 161 GLU n 
2 162 SER n 
2 163 VAL n 
2 164 THR n 
2 165 GLU n 
2 166 GLN n 
2 167 ASP n 
2 168 SER n 
2 169 LYS n 
2 170 ASP n 
2 171 SER n 
2 172 THR n 
2 173 TYR n 
2 174 SER n 
2 175 LEU n 
2 176 SER n 
2 177 SER n 
2 178 THR n 
2 179 LEU n 
2 180 THR n 
2 181 LEU n 
2 182 SER n 
2 183 LYS n 
2 184 ALA n 
2 185 ASP n 
2 186 TYR n 
2 187 GLU n 
2 188 LYS n 
2 189 HIS n 
2 190 LYS n 
2 191 VAL n 
2 192 TYR n 
2 193 ALA n 
2 194 CYS n 
2 195 GLU n 
2 196 VAL n 
2 197 THR n 
2 198 GLN n 
2 199 GLY n 
2 200 THR n 
2 201 THR n 
2 202 SER n 
2 203 VAL n 
2 204 THR n 
2 205 LYS n 
2 206 SER n 
2 207 PHE n 
2 208 ASN n 
2 209 ARG n 
2 210 GLY n 
2 211 GLU n 
2 212 CYS n 
3 1   ALA n 
3 2   PRO n 
3 3   MET n 
3 4   ALA n 
3 5   GLU n 
3 6   GLY n 
3 7   GLY n 
3 8   GLY n 
3 9   GLN n 
3 10  ASN n 
3 11  HIS n 
3 12  HIS n 
3 13  GLU n 
3 14  VAL n 
3 15  VAL n 
3 16  LYS n 
3 17  PHE n 
3 18  MET n 
3 19  ASP n 
3 20  VAL n 
3 21  TYR n 
3 22  GLN n 
3 23  ARG n 
3 24  SER n 
3 25  TYR n 
3 26  CYS n 
3 27  HIS n 
3 28  PRO n 
3 29  ILE n 
3 30  GLU n 
3 31  THR n 
3 32  LEU n 
3 33  VAL n 
3 34  ASP n 
3 35  ILE n 
3 36  PHE n 
3 37  GLN n 
3 38  GLU n 
3 39  TYR n 
3 40  PRO n 
3 41  ASP n 
3 42  GLU n 
3 43  ILE n 
3 44  GLU n 
3 45  TYR n 
3 46  ILE n 
3 47  PHE n 
3 48  LYS n 
3 49  PRO n 
3 50  SER n 
3 51  CYS n 
3 52  VAL n 
3 53  PRO n 
3 54  LEU n 
3 55  MET n 
3 56  ARG n 
3 57  CYS n 
3 58  GLY n 
3 59  GLY n 
3 60  CYS n 
3 61  CYS n 
3 62  ASN n 
3 63  ASP n 
3 64  GLU n 
3 65  GLY n 
3 66  LEU n 
3 67  GLU n 
3 68  CYS n 
3 69  VAL n 
3 70  PRO n 
3 71  THR n 
3 72  GLU n 
3 73  GLU n 
3 74  SER n 
3 75  ASN n 
3 76  ILE n 
3 77  THR n 
3 78  MET n 
3 79  GLN n 
3 80  ILE n 
3 81  MET n 
3 82  ARG n 
3 83  ILE n 
3 84  LYS n 
3 85  PRO n 
3 86  HIS n 
3 87  GLN n 
3 88  GLY n 
3 89  GLN n 
3 90  HIS n 
3 91  ILE n 
3 92  GLY n 
3 93  GLU n 
3 94  MET n 
3 95  SER n 
3 96  PHE n 
3 97  LEU n 
3 98  GLN n 
3 99  HIS n 
3 100 ASN n 
3 101 LYS n 
3 102 CYS n 
3 103 GLU n 
3 104 CYS n 
3 105 ARG n 
3 106 PRO n 
3 107 LYS n 
3 108 LYS n 
3 109 ASP n 
3 110 ARG n 
3 111 ALA n 
3 112 ARG n 
3 113 GLN n 
3 114 GLU n 
3 115 ASN n 
3 116 CYS n 
3 117 ASP n 
3 118 LYS n 
3 119 PRO n 
3 120 ARG n 
3 121 ARG n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 228 human ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? ? ? ? 
? ? ? Expi293 ? ? ? ? ? plasmid ? ?      ? pSCSTa ? ? 
2 1 sample 'Biological sequence' 1 212 human ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? ? ? ? 
? ? ? Expi293 ? ? ? ? ? plasmid ? pSCSTa ? ?      ? ? 
# 
_pdbx_entity_src_syn.entity_id              3 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       121 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
4 oligosaccharide 
5 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 4 DGlcpNAcb1-4DGlcpNAcb1-ROH                                                   'Glycam Condensed Sequence' GMML       1.0   
2 4 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                        WURCS                       PDB2Glycan 1.1.0 
3 4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'                              LINUCS                      PDB-CARE   ?     
4 5 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                          'Glycam Condensed Sequence' GMML       1.0   
5 5 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1' WURCS                       PDB2Glycan 1.1.0 
6 5 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}'           LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 5 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
3 5 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
# 
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 
BMA 'D-saccharide, beta linking' . beta-D-mannopyranose                     'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      
180.156 
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 
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 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLU 1   1   1   GLU GLU C . n 
A 1 2   VAL 2   2   2   VAL VAL C . n 
A 1 3   GLN 3   3   3   GLN GLN C . n 
A 1 4   LEU 4   4   4   LEU LEU C . n 
A 1 5   VAL 5   5   5   VAL VAL C . n 
A 1 6   GLU 6   6   6   GLU GLU C . n 
A 1 7   SER 7   7   7   SER SER C . n 
A 1 8   GLY 8   8   8   GLY GLY C . n 
A 1 9   GLY 9   9   9   GLY GLY C . n 
A 1 10  GLY 10  11  11  GLY GLY C . n 
A 1 11  LEU 11  12  12  LEU LEU C . n 
A 1 12  VAL 12  13  13  VAL VAL C . n 
A 1 13  GLN 13  14  14  GLN GLN C . n 
A 1 14  PRO 14  15  15  PRO PRO C . n 
A 1 15  GLY 15  16  16  GLY GLY C . n 
A 1 16  GLY 16  17  17  GLY GLY C . n 
A 1 17  SER 17  18  18  SER SER C . n 
A 1 18  LEU 18  19  19  LEU LEU C . n 
A 1 19  ARG 19  20  20  ARG ARG C . n 
A 1 20  LEU 20  21  21  LEU LEU C . n 
A 1 21  SER 21  22  22  SER SER C . n 
A 1 22  CYS 22  23  23  CYS CYS C . n 
A 1 23  ALA 23  24  24  ALA ALA C . n 
A 1 24  ALA 24  25  25  ALA ALA C . n 
A 1 25  SER 25  26  26  SER SER C . n 
A 1 26  GLY 26  27  27  GLY GLY C . n 
A 1 27  PHE 27  28  28  PHE PHE C . n 
A 1 28  ASP 28  29  29  ASP ASP C . n 
A 1 29  LEU 29  30  30  LEU LEU C . n 
A 1 30  TRP 30  35  35  TRP TRP C . n 
A 1 31  TYR 31  36  36  TYR TYR C . n 
A 1 32  TYR 32  37  37  TYR TYR C . n 
A 1 33  SER 33  38  38  SER SER C . n 
A 1 34  ILE 34  39  39  ILE ILE C . n 
A 1 35  HIS 35  40  40  HIS HIS C . n 
A 1 36  TRP 36  41  41  TRP TRP C . n 
A 1 37  VAL 37  42  42  VAL VAL C . n 
A 1 38  ARG 38  43  43  ARG ARG C . n 
A 1 39  GLN 39  44  44  GLN GLN C . n 
A 1 40  ALA 40  45  45  ALA ALA C . n 
A 1 41  PRO 41  46  46  PRO PRO C . n 
A 1 42  GLY 42  47  47  GLY GLY C . n 
A 1 43  LYS 43  48  48  LYS LYS C . n 
A 1 44  GLY 44  49  49  GLY GLY C . n 
A 1 45  LEU 45  50  50  LEU LEU C . n 
A 1 46  GLU 46  51  51  GLU GLU C . n 
A 1 47  TRP 47  52  52  TRP TRP C . n 
A 1 48  VAL 48  53  53  VAL VAL C . n 
A 1 49  ALA 49  54  54  ALA ALA C . n 
A 1 50  TYR 50  55  55  TYR TYR C . n 
A 1 51  ILE 51  56  56  ILE ILE C . n 
A 1 52  TYR 52  57  57  TYR TYR C . n 
A 1 53  PRO 53  58  58  PRO PRO C . n 
A 1 54  SER 54  59  59  SER SER C . n 
A 1 55  TYR 55  62  62  TYR TYR C . n 
A 1 56  GLY 56  63  63  GLY GLY C . n 
A 1 57  TYR 57  64  64  TYR TYR C . n 
A 1 58  THR 58  65  65  THR THR C . n 
A 1 59  TYR 59  66  66  TYR TYR C . n 
A 1 60  TYR 60  67  67  TYR TYR C . n 
A 1 61  ALA 61  68  68  ALA ALA C . n 
A 1 62  ASP 62  69  69  ASP ASP C . n 
A 1 63  SER 63  70  70  SER SER C . n 
A 1 64  VAL 64  71  71  VAL VAL C . n 
A 1 65  LYS 65  72  72  LYS LYS C . n 
A 1 66  GLY 66  74  74  GLY GLY C . n 
A 1 67  ARG 67  75  75  ARG ARG C . n 
A 1 68  PHE 68  76  76  PHE PHE C . n 
A 1 69  THR 69  77  77  THR THR C . n 
A 1 70  ILE 70  78  78  ILE ILE C . n 
A 1 71  SER 71  79  79  SER SER C . n 
A 1 72  ALA 72  80  80  ALA ALA C . n 
A 1 73  ASP 73  81  81  ASP ASP C . n 
A 1 74  THR 74  82  82  THR THR C . n 
A 1 75  SER 75  83  83  SER SER C . n 
A 1 76  LYS 76  84  84  LYS LYS C . n 
A 1 77  ASN 77  85  85  ASN ASN C . n 
A 1 78  THR 78  86  86  THR THR C . n 
A 1 79  ALA 79  87  87  ALA ALA C . n 
A 1 80  TYR 80  88  88  TYR TYR C . n 
A 1 81  LEU 81  89  89  LEU LEU C . n 
A 1 82  GLN 82  90  90  GLN GLN C . n 
A 1 83  MET 83  91  91  MET MET C . n 
A 1 84  ASN 84  92  92  ASN ASN C . n 
A 1 85  SER 85  93  93  SER SER C . n 
A 1 86  LEU 86  94  94  LEU LEU C . n 
A 1 87  ARG 87  95  95  ARG ARG C . n 
A 1 88  ALA 88  96  96  ALA ALA C . n 
A 1 89  GLU 89  97  97  GLU GLU C . n 
A 1 90  ASP 90  98  98  ASP ASP C . n 
A 1 91  THR 91  99  99  THR THR C . n 
A 1 92  ALA 92  100 100 ALA ALA C . n 
A 1 93  VAL 93  101 101 VAL VAL C . n 
A 1 94  TYR 94  102 102 TYR TYR C . n 
A 1 95  TYR 95  103 103 TYR TYR C . n 
A 1 96  CYS 96  104 104 CYS CYS C . n 
A 1 97  ALA 97  105 105 ALA ALA C . n 
A 1 98  ARG 98  106 106 ARG ARG C . n 
A 1 99  HIS 99  107 107 HIS HIS C . n 
A 1 100 ALA 100 108 108 ALA ALA C . n 
A 1 101 TRP 101 109 109 TRP TRP C . n 
A 1 102 TYR 102 110 110 TYR TYR C . n 
A 1 103 TYR 103 111 111 TYR TYR C . n 
A 1 104 GLY 104 112 112 GLY GLY C . n 
A 1 105 TRP 105 113 113 TRP TRP C . n 
A 1 106 GLY 106 114 114 GLY GLY C . n 
A 1 107 LEU 107 115 115 LEU LEU C . n 
A 1 108 ASP 108 116 116 ASP ASP C . n 
A 1 109 TYR 109 117 117 TYR TYR C . n 
A 1 110 TRP 110 118 118 TRP TRP C . n 
A 1 111 GLY 111 119 119 GLY GLY C . n 
A 1 112 GLN 112 120 120 GLN GLN C . n 
A 1 113 GLY 113 121 121 GLY GLY C . n 
A 1 114 THR 114 122 122 THR THR C . n 
A 1 115 LEU 115 123 123 LEU LEU C . n 
A 1 116 VAL 116 124 124 VAL VAL C . n 
A 1 117 THR 117 125 125 THR THR C . n 
A 1 118 VAL 118 126 126 VAL VAL C . n 
A 1 119 SER 119 127 127 SER SER C . n 
A 1 120 SER 120 128 128 SER SER C . n 
A 1 121 ALA 121 129 129 ALA ALA C . n 
A 1 122 SER 122 130 130 SER SER C . n 
A 1 123 THR 123 131 131 THR THR C . n 
A 1 124 LYS 124 132 132 LYS LYS C . n 
A 1 125 GLY 125 133 133 GLY GLY C . n 
A 1 126 PRO 126 134 134 PRO PRO C . n 
A 1 127 SER 127 135 135 SER SER C . n 
A 1 128 VAL 128 136 136 VAL VAL C . n 
A 1 129 PHE 129 137 137 PHE PHE C . n 
A 1 130 PRO 130 138 138 PRO PRO C . n 
A 1 131 LEU 131 139 139 LEU LEU C . n 
A 1 132 ALA 132 140 140 ALA ALA C . n 
A 1 133 PRO 133 141 141 PRO PRO C . n 
A 1 134 SER 134 142 ?   ?   ?   C . n 
A 1 135 SER 135 143 143 SER SER C . n 
A 1 136 LYS 136 144 144 LYS LYS C . n 
A 1 137 SER 137 145 145 SER SER C . n 
A 1 138 THR 138 146 146 THR THR C . n 
A 1 139 SER 139 147 147 SER SER C . n 
A 1 140 GLY 140 148 ?   ?   ?   C . n 
A 1 141 GLY 141 149 ?   ?   ?   C . n 
A 1 142 THR 142 150 150 THR THR C . n 
A 1 143 ALA 143 151 151 ALA ALA C . n 
A 1 144 ALA 144 152 ?   ?   ?   C . n 
A 1 145 LEU 145 153 153 LEU LEU C . n 
A 1 146 GLY 146 154 154 GLY GLY C . n 
A 1 147 CYS 147 155 155 CYS CYS C . n 
A 1 148 LEU 148 156 156 LEU LEU C . n 
A 1 149 VAL 149 157 157 VAL VAL C . n 
A 1 150 LYS 150 158 158 LYS LYS C . n 
A 1 151 ASP 151 159 159 ASP ASP C . n 
A 1 152 TYR 152 160 160 TYR TYR C . n 
A 1 153 PHE 153 161 161 PHE PHE C . n 
A 1 154 PRO 154 162 162 PRO PRO C . n 
A 1 155 GLU 155 163 163 GLU GLU C . n 
A 1 156 PRO 156 164 164 PRO PRO C . n 
A 1 157 VAL 157 165 165 VAL VAL C . n 
A 1 158 THR 158 166 166 THR THR C . n 
A 1 159 VAL 159 167 167 VAL VAL C . n 
A 1 160 SER 160 168 168 SER SER C . n 
A 1 161 TRP 161 169 169 TRP TRP C . n 
A 1 162 ASN 162 170 170 ASN ASN C . n 
A 1 163 SER 163 171 171 SER SER C . n 
A 1 164 GLY 164 172 172 GLY GLY C . n 
A 1 165 ALA 165 173 173 ALA ALA C . n 
A 1 166 LEU 166 174 174 LEU LEU C . n 
A 1 167 THR 167 175 175 THR THR C . n 
A 1 168 SER 168 176 176 SER SER C . n 
A 1 169 GLY 169 177 177 GLY GLY C . n 
A 1 170 VAL 170 178 178 VAL VAL C . n 
A 1 171 HIS 171 179 179 HIS HIS C . n 
A 1 172 THR 172 180 180 THR THR C . n 
A 1 173 PHE 173 181 181 PHE PHE C . n 
A 1 174 PRO 174 182 182 PRO PRO C . n 
A 1 175 ALA 175 183 183 ALA ALA C . n 
A 1 176 VAL 176 184 184 VAL VAL C . n 
A 1 177 LEU 177 185 185 LEU LEU C . n 
A 1 178 GLN 178 186 186 GLN GLN C . n 
A 1 179 SER 179 187 187 SER SER C . n 
A 1 180 SER 180 188 188 SER SER C . n 
A 1 181 GLY 181 189 189 GLY GLY C . n 
A 1 182 LEU 182 190 190 LEU LEU C . n 
A 1 183 TYR 183 191 191 TYR TYR C . n 
A 1 184 SER 184 192 192 SER SER C . n 
A 1 185 LEU 185 193 193 LEU LEU C . n 
A 1 186 SER 186 194 194 SER SER C . n 
A 1 187 SER 187 195 195 SER SER C . n 
A 1 188 VAL 188 196 196 VAL VAL C . n 
A 1 189 VAL 189 197 197 VAL VAL C . n 
A 1 190 THR 190 198 198 THR THR C . n 
A 1 191 VAL 191 199 199 VAL VAL C . n 
A 1 192 PRO 192 200 200 PRO PRO C . n 
A 1 193 SER 193 201 201 SER SER C . n 
A 1 194 SER 194 202 202 SER SER C . n 
A 1 195 SER 195 203 203 SER SER C . n 
A 1 196 LEU 196 204 204 LEU LEU C . n 
A 1 197 GLY 197 205 205 GLY GLY C . n 
A 1 198 THR 198 206 206 THR THR C . n 
A 1 199 GLN 199 207 207 GLN GLN C . n 
A 1 200 THR 200 208 208 THR THR C . n 
A 1 201 TYR 201 209 209 TYR TYR C . n 
A 1 202 ILE 202 210 210 ILE ILE C . n 
A 1 203 CYS 203 211 211 CYS CYS C . n 
A 1 204 ASN 204 212 212 ASN ASN C . n 
A 1 205 VAL 205 213 213 VAL VAL C . n 
A 1 206 ASN 206 214 214 ASN ASN C . n 
A 1 207 HIS 207 215 215 HIS HIS C . n 
A 1 208 LYS 208 216 216 LYS LYS C . n 
A 1 209 PRO 209 217 217 PRO PRO C . n 
A 1 210 SER 210 218 218 SER SER C . n 
A 1 211 ASN 211 219 219 ASN ASN C . n 
A 1 212 THR 212 220 220 THR THR C . n 
A 1 213 LYS 213 221 221 LYS LYS C . n 
A 1 214 VAL 214 222 222 VAL VAL C . n 
A 1 215 ASP 215 223 223 ASP ASP C . n 
A 1 216 LYS 216 224 224 LYS LYS C . n 
A 1 217 LYS 217 225 225 LYS LYS C . n 
A 1 218 VAL 218 226 226 VAL VAL C . n 
A 1 219 GLU 219 227 227 GLU GLU C . n 
A 1 220 PRO 220 228 228 PRO PRO C . n 
A 1 221 LYS 221 229 ?   ?   ?   C . n 
A 1 222 SER 222 230 ?   ?   ?   C . n 
A 1 223 CYS 223 231 ?   ?   ?   C . n 
A 1 224 ASP 224 232 ?   ?   ?   C . n 
A 1 225 LYS 225 233 ?   ?   ?   C . n 
A 1 226 THR 226 234 ?   ?   ?   C . n 
A 1 227 HIS 227 235 ?   ?   ?   C . n 
A 1 228 THR 228 236 ?   ?   ?   C . n 
B 2 1   ASP 1   1   ?   ?   ?   D . n 
B 2 2   ILE 2   2   ?   ?   ?   D . n 
B 2 3   GLN 3   3   ?   ?   ?   D . n 
B 2 4   MET 4   4   ?   ?   ?   D . n 
B 2 5   THR 5   5   5   THR THR D . n 
B 2 6   GLN 6   6   6   GLN GLN D . n 
B 2 7   SER 7   7   7   SER SER D . n 
B 2 8   PRO 8   8   8   PRO PRO D . n 
B 2 9   SER 9   9   9   SER SER D . n 
B 2 10  SER 10  10  10  SER SER D . n 
B 2 11  LEU 11  11  11  LEU LEU D . n 
B 2 12  SER 12  12  12  SER SER D . n 
B 2 13  ALA 13  13  13  ALA ALA D . n 
B 2 14  SER 14  14  14  SER SER D . n 
B 2 15  VAL 15  15  15  VAL VAL D . n 
B 2 16  GLY 16  16  16  GLY GLY D . n 
B 2 17  ASP 17  17  17  ASP ASP D . n 
B 2 18  ARG 18  18  18  ARG ARG D . n 
B 2 19  VAL 19  19  19  VAL VAL D . n 
B 2 20  THR 20  20  20  THR THR D . n 
B 2 21  ILE 21  21  21  ILE ILE D . n 
B 2 22  THR 22  22  22  THR THR D . n 
B 2 23  CYS 23  23  23  CYS CYS D . n 
B 2 24  ARG 24  24  24  ARG ARG D . n 
B 2 25  ALA 25  25  25  ALA ALA D . n 
B 2 26  SER 26  26  26  SER SER D . n 
B 2 27  GLN 27  27  ?   ?   ?   D . n 
B 2 28  ALA 28  28  28  ALA ALA D . n 
B 2 29  ALA 29  29  29  ALA ALA D . n 
B 2 30  TYR 30  36  36  TYR TYR D . n 
B 2 31  GLY 31  37  37  GLY GLY D . n 
B 2 32  ARG 32  38  38  ARG ARG D . n 
B 2 33  VAL 33  39  39  VAL VAL D . n 
B 2 34  ALA 34  40  40  ALA ALA D . n 
B 2 35  TRP 35  41  41  TRP TRP D . n 
B 2 36  TYR 36  42  42  TYR TYR D . n 
B 2 37  GLN 37  43  43  GLN GLN D . n 
B 2 38  GLN 38  44  44  GLN GLN D . n 
B 2 39  LYS 39  45  45  LYS LYS D . n 
B 2 40  PRO 40  46  46  PRO PRO D . n 
B 2 41  GLY 41  47  47  GLY GLY D . n 
B 2 42  LYS 42  48  48  LYS LYS D . n 
B 2 43  ALA 43  49  49  ALA ALA D . n 
B 2 44  PRO 44  50  50  PRO PRO D . n 
B 2 45  LYS 45  51  51  LYS LYS D . n 
B 2 46  LEU 46  52  52  LEU LEU D . n 
B 2 47  LEU 47  53  53  LEU LEU D . n 
B 2 48  ILE 48  54  54  ILE ILE D . n 
B 2 49  TYR 49  55  55  TYR TYR D . n 
B 2 50  LYS 50  56  56  LYS LYS D . n 
B 2 51  ALA 51  57  57  ALA ALA D . n 
B 2 52  SER 52  65  65  SER SER D . n 
B 2 53  GLU 53  66  66  GLU GLU D . n 
B 2 54  LEU 54  67  67  LEU LEU D . n 
B 2 55  TYR 55  68  68  TYR TYR D . n 
B 2 56  ALA 56  69  69  ALA ALA D . n 
B 2 57  GLY 57  70  70  GLY GLY D . n 
B 2 58  VAL 58  71  71  VAL VAL D . n 
B 2 59  PRO 59  72  72  PRO PRO D . n 
B 2 60  SER 60  74  74  SER SER D . n 
B 2 61  ARG 61  75  75  ARG ARG D . n 
B 2 62  PHE 62  76  76  PHE PHE D . n 
B 2 63  SER 63  77  77  SER SER D . n 
B 2 64  GLY 64  78  78  GLY GLY D . n 
B 2 65  SER 65  79  79  SER SER D . n 
B 2 66  ARG 66  80  80  ARG ARG D . n 
B 2 67  SER 67  83  83  SER SER D . n 
B 2 68  GLY 68  84  84  GLY GLY D . n 
B 2 69  THR 69  85  85  THR THR D . n 
B 2 70  ASP 70  86  86  ASP ASP D . n 
B 2 71  PHE 71  87  87  PHE PHE D . n 
B 2 72  THR 72  88  88  THR THR D . n 
B 2 73  LEU 73  89  89  LEU LEU D . n 
B 2 74  THR 74  90  90  THR THR D . n 
B 2 75  ILE 75  91  91  ILE ILE D . n 
B 2 76  SER 76  92  92  SER SER D . n 
B 2 77  SER 77  93  93  SER SER D . n 
B 2 78  LEU 78  94  94  LEU LEU D . n 
B 2 79  GLN 79  95  95  GLN GLN D . n 
B 2 80  PRO 80  96  96  PRO PRO D . n 
B 2 81  GLU 81  97  97  GLU GLU D . n 
B 2 82  ASP 82  98  98  ASP ASP D . n 
B 2 83  PHE 83  99  99  PHE PHE D . n 
B 2 84  ALA 84  100 100 ALA ALA D . n 
B 2 85  THR 85  101 101 THR THR D . n 
B 2 86  TYR 86  102 102 TYR TYR D . n 
B 2 87  TYR 87  103 103 TYR TYR D . n 
B 2 88  CYS 88  104 104 CYS CYS D . n 
B 2 89  GLN 89  105 105 GLN GLN D . n 
B 2 90  GLN 90  106 106 GLN GLN D . n 
B 2 91  ARG 91  107 107 ARG ARG D . n 
B 2 92  GLY 92  108 108 GLY GLY D . n 
B 2 93  TRP 93  109 109 TRP TRP D . n 
B 2 94  TYR 94  114 114 TYR TYR D . n 
B 2 95  LEU 95  115 115 LEU LEU D . n 
B 2 96  PHE 96  116 116 PHE PHE D . n 
B 2 97  THR 97  117 117 THR THR D . n 
B 2 98  PHE 98  118 118 PHE PHE D . n 
B 2 99  GLY 99  119 119 GLY GLY D . n 
B 2 100 GLN 100 120 120 GLN GLN D . n 
B 2 101 GLY 101 121 121 GLY GLY D . n 
B 2 102 THR 102 122 122 THR THR D . n 
B 2 103 LYS 103 123 123 LYS LYS D . n 
B 2 104 VAL 104 124 124 VAL VAL D . n 
B 2 105 GLU 105 125 125 GLU GLU D . n 
B 2 106 ILE 106 126 126 ILE ILE D . n 
B 2 107 LYS 107 127 127 LYS LYS D . n 
B 2 108 ARG 108 128 128 ARG ARG D . n 
B 2 109 THR 109 129 129 THR THR D . n 
B 2 110 VAL 110 130 ?   ?   ?   D . n 
B 2 111 ALA 111 131 ?   ?   ?   D . n 
B 2 112 ALA 112 132 132 ALA ALA D . n 
B 2 113 PRO 113 133 133 PRO PRO D . n 
B 2 114 SER 114 134 134 SER SER D . n 
B 2 115 VAL 115 135 135 VAL VAL D . n 
B 2 116 PHE 116 136 136 PHE PHE D . n 
B 2 117 ILE 117 137 137 ILE ILE D . n 
B 2 118 PHE 118 138 138 PHE PHE D . n 
B 2 119 PRO 119 139 139 PRO PRO D . n 
B 2 120 PRO 120 140 140 PRO PRO D . n 
B 2 121 SER 121 141 141 SER SER D . n 
B 2 122 ASP 122 142 142 ASP ASP D . n 
B 2 123 GLU 123 143 143 GLU GLU D . n 
B 2 124 GLN 124 144 144 GLN GLN D . n 
B 2 125 LEU 125 145 145 LEU LEU D . n 
B 2 126 LYS 126 146 146 LYS LYS D . n 
B 2 127 SER 127 147 147 SER SER D . n 
B 2 128 GLY 128 148 148 GLY GLY D . n 
B 2 129 THR 129 149 149 THR THR D . n 
B 2 130 ALA 130 150 150 ALA ALA D . n 
B 2 131 SER 131 151 151 SER SER D . n 
B 2 132 VAL 132 152 152 VAL VAL D . n 
B 2 133 VAL 133 153 153 VAL VAL D . n 
B 2 134 CYS 134 154 154 CYS CYS D . n 
B 2 135 LEU 135 155 155 LEU LEU D . n 
B 2 136 LEU 136 156 156 LEU LEU D . n 
B 2 137 ASN 137 157 157 ASN ASN D . n 
B 2 138 ASN 138 158 158 ASN ASN D . n 
B 2 139 PHE 139 159 159 PHE PHE D . n 
B 2 140 TYR 140 160 160 TYR TYR D . n 
B 2 141 PRO 141 161 161 PRO PRO D . n 
B 2 142 ARG 142 162 162 ARG ARG D . n 
B 2 143 GLU 143 163 163 GLU GLU D . n 
B 2 144 ALA 144 164 164 ALA ALA D . n 
B 2 145 LYS 145 165 165 LYS LYS D . n 
B 2 146 VAL 146 166 166 VAL VAL D . n 
B 2 147 SER 147 167 167 SER SER D . n 
B 2 148 TRP 148 168 168 TRP TRP D . n 
B 2 149 TYR 149 169 169 TYR TYR D . n 
B 2 150 VAL 150 170 170 VAL VAL D . n 
B 2 151 ASP 151 171 171 ASP ASP D . n 
B 2 152 ASN 152 172 172 ASN ASN D . n 
B 2 153 ALA 153 173 173 ALA ALA D . n 
B 2 154 LEU 154 174 174 LEU LEU D . n 
B 2 155 GLN 155 175 175 GLN GLN D . n 
B 2 156 SER 156 176 176 SER SER D . n 
B 2 157 GLY 157 177 177 GLY GLY D . n 
B 2 158 ASN 158 178 178 ASN ASN D . n 
B 2 159 SER 159 179 179 SER SER D . n 
B 2 160 GLN 160 180 180 GLN GLN D . n 
B 2 161 GLU 161 181 181 GLU GLU D . n 
B 2 162 SER 162 182 182 SER SER D . n 
B 2 163 VAL 163 183 183 VAL VAL D . n 
B 2 164 THR 164 184 184 THR THR D . n 
B 2 165 GLU 165 185 185 GLU GLU D . n 
B 2 166 GLN 166 186 186 GLN GLN D . n 
B 2 167 ASP 167 187 187 ASP ASP D . n 
B 2 168 SER 168 188 188 SER SER D . n 
B 2 169 LYS 169 189 189 LYS LYS D . n 
B 2 170 ASP 170 190 190 ASP ASP D . n 
B 2 171 SER 171 191 191 SER SER D . n 
B 2 172 THR 172 192 192 THR THR D . n 
B 2 173 TYR 173 193 193 TYR TYR D . n 
B 2 174 SER 174 194 194 SER SER D . n 
B 2 175 LEU 175 195 195 LEU LEU D . n 
B 2 176 SER 176 196 196 SER SER D . n 
B 2 177 SER 177 197 197 SER SER D . n 
B 2 178 THR 178 198 198 THR THR D . n 
B 2 179 LEU 179 199 199 LEU LEU D . n 
B 2 180 THR 180 200 200 THR THR D . n 
B 2 181 LEU 181 201 201 LEU LEU D . n 
B 2 182 SER 182 202 202 SER SER D . n 
B 2 183 LYS 183 203 203 LYS LYS D . n 
B 2 184 ALA 184 204 204 ALA ALA D . n 
B 2 185 ASP 185 205 205 ASP ASP D . n 
B 2 186 TYR 186 206 206 TYR TYR D . n 
B 2 187 GLU 187 207 207 GLU GLU D . n 
B 2 188 LYS 188 208 208 LYS LYS D . n 
B 2 189 HIS 189 209 209 HIS HIS D . n 
B 2 190 LYS 190 210 210 LYS LYS D . n 
B 2 191 VAL 191 211 211 VAL VAL D . n 
B 2 192 TYR 192 212 212 TYR TYR D . n 
B 2 193 ALA 193 213 213 ALA ALA D . n 
B 2 194 CYS 194 214 214 CYS CYS D . n 
B 2 195 GLU 195 215 215 GLU GLU D . n 
B 2 196 VAL 196 216 216 VAL VAL D . n 
B 2 197 THR 197 217 217 THR THR D . n 
B 2 198 GLN 198 218 218 GLN GLN D . n 
B 2 199 GLY 199 219 219 GLY GLY D . n 
B 2 200 THR 200 220 220 THR THR D . n 
B 2 201 THR 201 221 221 THR THR D . n 
B 2 202 SER 202 222 222 SER SER D . n 
B 2 203 VAL 203 225 225 VAL VAL D . n 
B 2 204 THR 204 226 226 THR THR D . n 
B 2 205 LYS 205 227 227 LYS LYS D . n 
B 2 206 SER 206 228 228 SER SER D . n 
B 2 207 PHE 207 229 229 PHE PHE D . n 
B 2 208 ASN 208 230 230 ASN ASN D . n 
B 2 209 ARG 209 231 231 ARG ARG D . n 
B 2 210 GLY 210 232 232 GLY GLY D . n 
B 2 211 GLU 211 233 233 GLU GLU D . n 
B 2 212 CYS 212 234 234 CYS CYS D . n 
C 3 1   ALA 1   1   ?   ?   ?   E . n 
C 3 2   PRO 2   2   ?   ?   ?   E . n 
C 3 3   MET 3   3   ?   ?   ?   E . n 
C 3 4   ALA 4   4   ?   ?   ?   E . n 
C 3 5   GLU 5   5   ?   ?   ?   E . n 
C 3 6   GLY 6   6   ?   ?   ?   E . n 
C 3 7   GLY 7   7   ?   ?   ?   E . n 
C 3 8   GLY 8   8   ?   ?   ?   E . n 
C 3 9   GLN 9   9   ?   ?   ?   E . n 
C 3 10  ASN 10  10  ?   ?   ?   E . n 
C 3 11  HIS 11  11  11  HIS HIS E . n 
C 3 12  HIS 12  12  12  HIS HIS E . n 
C 3 13  GLU 13  13  13  GLU GLU E . n 
C 3 14  VAL 14  14  14  VAL VAL E . n 
C 3 15  VAL 15  15  15  VAL VAL E . n 
C 3 16  LYS 16  16  16  LYS LYS E . n 
C 3 17  PHE 17  17  17  PHE PHE E . n 
C 3 18  MET 18  18  18  MET MET E . n 
C 3 19  ASP 19  19  19  ASP ASP E . n 
C 3 20  VAL 20  20  20  VAL VAL E . n 
C 3 21  TYR 21  21  21  TYR TYR E . n 
C 3 22  GLN 22  22  22  GLN GLN E . n 
C 3 23  ARG 23  23  23  ARG ARG E . n 
C 3 24  SER 24  24  24  SER SER E . n 
C 3 25  TYR 25  25  25  TYR TYR E . n 
C 3 26  CYS 26  26  26  CYS CYS E . n 
C 3 27  HIS 27  27  27  HIS HIS E . n 
C 3 28  PRO 28  28  28  PRO PRO E . n 
C 3 29  ILE 29  29  29  ILE ILE E . n 
C 3 30  GLU 30  30  30  GLU GLU E . n 
C 3 31  THR 31  31  31  THR THR E . n 
C 3 32  LEU 32  32  32  LEU LEU E . n 
C 3 33  VAL 33  33  33  VAL VAL E . n 
C 3 34  ASP 34  34  34  ASP ASP E . n 
C 3 35  ILE 35  35  35  ILE ILE E . n 
C 3 36  PHE 36  36  36  PHE PHE E . n 
C 3 37  GLN 37  37  37  GLN GLN E . n 
C 3 38  GLU 38  38  38  GLU GLU E . n 
C 3 39  TYR 39  39  39  TYR TYR E . n 
C 3 40  PRO 40  40  40  PRO PRO E . n 
C 3 41  ASP 41  41  41  ASP ASP E . n 
C 3 42  GLU 42  42  42  GLU GLU E . n 
C 3 43  ILE 43  43  43  ILE ILE E . n 
C 3 44  GLU 44  44  44  GLU GLU E . n 
C 3 45  TYR 45  45  45  TYR TYR E . n 
C 3 46  ILE 46  46  46  ILE ILE E . n 
C 3 47  PHE 47  47  47  PHE PHE E . n 
C 3 48  LYS 48  48  48  LYS LYS E . n 
C 3 49  PRO 49  49  49  PRO PRO E . n 
C 3 50  SER 50  50  50  SER SER E . n 
C 3 51  CYS 51  51  51  CYS CYS E . n 
C 3 52  VAL 52  52  52  VAL VAL E . n 
C 3 53  PRO 53  53  53  PRO PRO E . n 
C 3 54  LEU 54  54  54  LEU LEU E . n 
C 3 55  MET 55  55  55  MET MET E . n 
C 3 56  ARG 56  56  56  ARG ARG E . n 
C 3 57  CYS 57  57  57  CYS CYS E . n 
C 3 58  GLY 58  58  58  GLY GLY E . n 
C 3 59  GLY 59  59  59  GLY GLY E . n 
C 3 60  CYS 60  60  60  CYS CYS E . n 
C 3 61  CYS 61  61  61  CYS CYS E . n 
C 3 62  ASN 62  62  62  ASN ASN E . n 
C 3 63  ASP 63  63  63  ASP ASP E . n 
C 3 64  GLU 64  64  64  GLU GLU E . n 
C 3 65  GLY 65  65  65  GLY GLY E . n 
C 3 66  LEU 66  66  66  LEU LEU E . n 
C 3 67  GLU 67  67  67  GLU GLU E . n 
C 3 68  CYS 68  68  68  CYS CYS E . n 
C 3 69  VAL 69  69  69  VAL VAL E . n 
C 3 70  PRO 70  70  70  PRO PRO E . n 
C 3 71  THR 71  71  71  THR THR E . n 
C 3 72  GLU 72  72  72  GLU GLU E . n 
C 3 73  GLU 73  73  73  GLU GLU E . n 
C 3 74  SER 74  74  74  SER SER E . n 
C 3 75  ASN 75  75  75  ASN ASN E . n 
C 3 76  ILE 76  76  76  ILE ILE E . n 
C 3 77  THR 77  77  77  THR THR E . n 
C 3 78  MET 78  78  78  MET MET E . n 
C 3 79  GLN 79  79  79  GLN GLN E . n 
C 3 80  ILE 80  80  80  ILE ILE E . n 
C 3 81  MET 81  81  81  MET MET E . n 
C 3 82  ARG 82  82  82  ARG ARG E . n 
C 3 83  ILE 83  83  83  ILE ILE E . n 
C 3 84  LYS 84  84  84  LYS LYS E . n 
C 3 85  PRO 85  85  85  PRO PRO E . n 
C 3 86  HIS 86  86  86  HIS HIS E . n 
C 3 87  GLN 87  87  87  GLN GLN E . n 
C 3 88  GLY 88  88  88  GLY GLY E . n 
C 3 89  GLN 89  89  89  GLN GLN E . n 
C 3 90  HIS 90  90  90  HIS HIS E . n 
C 3 91  ILE 91  91  91  ILE ILE E . n 
C 3 92  GLY 92  92  92  GLY GLY E . n 
C 3 93  GLU 93  93  93  GLU GLU E . n 
C 3 94  MET 94  94  94  MET MET E . n 
C 3 95  SER 95  95  95  SER SER E . n 
C 3 96  PHE 96  96  96  PHE PHE E . n 
C 3 97  LEU 97  97  97  LEU LEU E . n 
C 3 98  GLN 98  98  98  GLN GLN E . n 
C 3 99  HIS 99  99  99  HIS HIS E . n 
C 3 100 ASN 100 100 100 ASN ASN E . n 
C 3 101 LYS 101 101 101 LYS LYS E . n 
C 3 102 CYS 102 102 102 CYS CYS E . n 
C 3 103 GLU 103 103 103 GLU GLU E . n 
C 3 104 CYS 104 104 104 CYS CYS E . n 
C 3 105 ARG 105 105 105 ARG ARG E . n 
C 3 106 PRO 106 106 106 PRO PRO E . n 
C 3 107 LYS 107 107 107 LYS LYS E . n 
C 3 108 LYS 108 108 108 LYS LYS E . n 
C 3 109 ASP 109 109 ?   ?   ?   E . n 
C 3 110 ARG 110 110 ?   ?   ?   E . n 
C 3 111 ALA 111 111 ?   ?   ?   E . n 
C 3 112 ARG 112 112 ?   ?   ?   E . n 
C 3 113 GLN 113 113 ?   ?   ?   E . n 
C 3 114 GLU 114 114 ?   ?   ?   E . n 
C 3 115 ASN 115 115 ?   ?   ?   E . n 
C 3 116 CYS 116 116 ?   ?   ?   E . n 
C 3 117 ASP 117 117 ?   ?   ?   E . n 
C 3 118 LYS 118 118 ?   ?   ?   E . n 
C 3 119 PRO 119 119 ?   ?   ?   E . n 
C 3 120 ARG 120 120 ?   ?   ?   E . n 
C 3 121 ARG 121 121 ?   ?   ?   E . n 
D 3 1   ALA 1   1   ?   ?   ?   F . n 
D 3 2   PRO 2   2   ?   ?   ?   F . n 
D 3 3   MET 3   3   ?   ?   ?   F . n 
D 3 4   ALA 4   4   ?   ?   ?   F . n 
D 3 5   GLU 5   5   ?   ?   ?   F . n 
D 3 6   GLY 6   6   ?   ?   ?   F . n 
D 3 7   GLY 7   7   ?   ?   ?   F . n 
D 3 8   GLY 8   8   ?   ?   ?   F . n 
D 3 9   GLN 9   9   ?   ?   ?   F . n 
D 3 10  ASN 10  10  ?   ?   ?   F . n 
D 3 11  HIS 11  11  11  HIS HIS F . n 
D 3 12  HIS 12  12  12  HIS HIS F . n 
D 3 13  GLU 13  13  13  GLU GLU F . n 
D 3 14  VAL 14  14  14  VAL VAL F . n 
D 3 15  VAL 15  15  15  VAL VAL F . n 
D 3 16  LYS 16  16  16  LYS LYS F . n 
D 3 17  PHE 17  17  17  PHE PHE F . n 
D 3 18  MET 18  18  18  MET MET F . n 
D 3 19  ASP 19  19  19  ASP ASP F . n 
D 3 20  VAL 20  20  20  VAL VAL F . n 
D 3 21  TYR 21  21  21  TYR TYR F . n 
D 3 22  GLN 22  22  22  GLN GLN F . n 
D 3 23  ARG 23  23  23  ARG ARG F . n 
D 3 24  SER 24  24  24  SER SER F . n 
D 3 25  TYR 25  25  25  TYR TYR F . n 
D 3 26  CYS 26  26  26  CYS CYS F . n 
D 3 27  HIS 27  27  27  HIS HIS F . n 
D 3 28  PRO 28  28  28  PRO PRO F . n 
D 3 29  ILE 29  29  29  ILE ILE F . n 
D 3 30  GLU 30  30  30  GLU GLU F . n 
D 3 31  THR 31  31  31  THR THR F . n 
D 3 32  LEU 32  32  32  LEU LEU F . n 
D 3 33  VAL 33  33  33  VAL VAL F . n 
D 3 34  ASP 34  34  34  ASP ASP F . n 
D 3 35  ILE 35  35  35  ILE ILE F . n 
D 3 36  PHE 36  36  36  PHE PHE F . n 
D 3 37  GLN 37  37  37  GLN GLN F . n 
D 3 38  GLU 38  38  38  GLU GLU F . n 
D 3 39  TYR 39  39  39  TYR TYR F . n 
D 3 40  PRO 40  40  40  PRO PRO F . n 
D 3 41  ASP 41  41  41  ASP ASP F . n 
D 3 42  GLU 42  42  42  GLU GLU F . n 
D 3 43  ILE 43  43  43  ILE ILE F . n 
D 3 44  GLU 44  44  44  GLU GLU F . n 
D 3 45  TYR 45  45  45  TYR TYR F . n 
D 3 46  ILE 46  46  46  ILE ILE F . n 
D 3 47  PHE 47  47  47  PHE PHE F . n 
D 3 48  LYS 48  48  48  LYS LYS F . n 
D 3 49  PRO 49  49  49  PRO PRO F . n 
D 3 50  SER 50  50  50  SER SER F . n 
D 3 51  CYS 51  51  51  CYS CYS F . n 
D 3 52  VAL 52  52  52  VAL VAL F . n 
D 3 53  PRO 53  53  53  PRO PRO F . n 
D 3 54  LEU 54  54  54  LEU LEU F . n 
D 3 55  MET 55  55  55  MET MET F . n 
D 3 56  ARG 56  56  56  ARG ARG F . n 
D 3 57  CYS 57  57  57  CYS CYS F . n 
D 3 58  GLY 58  58  58  GLY GLY F . n 
D 3 59  GLY 59  59  59  GLY GLY F . n 
D 3 60  CYS 60  60  60  CYS CYS F . n 
D 3 61  CYS 61  61  61  CYS CYS F . n 
D 3 62  ASN 62  62  62  ASN ASN F . n 
D 3 63  ASP 63  63  63  ASP ASP F . n 
D 3 64  GLU 64  64  64  GLU GLU F . n 
D 3 65  GLY 65  65  65  GLY GLY F . n 
D 3 66  LEU 66  66  66  LEU LEU F . n 
D 3 67  GLU 67  67  67  GLU GLU F . n 
D 3 68  CYS 68  68  68  CYS CYS F . n 
D 3 69  VAL 69  69  69  VAL VAL F . n 
D 3 70  PRO 70  70  70  PRO PRO F . n 
D 3 71  THR 71  71  71  THR THR F . n 
D 3 72  GLU 72  72  72  GLU GLU F . n 
D 3 73  GLU 73  73  73  GLU GLU F . n 
D 3 74  SER 74  74  74  SER SER F . n 
D 3 75  ASN 75  75  75  ASN ASN F . n 
D 3 76  ILE 76  76  76  ILE ILE F . n 
D 3 77  THR 77  77  77  THR THR F . n 
D 3 78  MET 78  78  78  MET MET F . n 
D 3 79  GLN 79  79  79  GLN GLN F . n 
D 3 80  ILE 80  80  80  ILE ILE F . n 
D 3 81  MET 81  81  81  MET MET F . n 
D 3 82  ARG 82  82  82  ARG ARG F . n 
D 3 83  ILE 83  83  83  ILE ILE F . n 
D 3 84  LYS 84  84  84  LYS LYS F . n 
D 3 85  PRO 85  85  85  PRO PRO F . n 
D 3 86  HIS 86  86  86  HIS HIS F . n 
D 3 87  GLN 87  87  87  GLN GLN F . n 
D 3 88  GLY 88  88  88  GLY GLY F . n 
D 3 89  GLN 89  89  89  GLN GLN F . n 
D 3 90  HIS 90  90  90  HIS HIS F . n 
D 3 91  ILE 91  91  91  ILE ILE F . n 
D 3 92  GLY 92  92  92  GLY GLY F . n 
D 3 93  GLU 93  93  93  GLU GLU F . n 
D 3 94  MET 94  94  94  MET MET F . n 
D 3 95  SER 95  95  95  SER SER F . n 
D 3 96  PHE 96  96  96  PHE PHE F . n 
D 3 97  LEU 97  97  97  LEU LEU F . n 
D 3 98  GLN 98  98  98  GLN GLN F . n 
D 3 99  HIS 99  99  99  HIS HIS F . n 
D 3 100 ASN 100 100 100 ASN ASN F . n 
D 3 101 LYS 101 101 101 LYS LYS F . n 
D 3 102 CYS 102 102 102 CYS CYS F . n 
D 3 103 GLU 103 103 103 GLU GLU F . n 
D 3 104 CYS 104 104 104 CYS CYS F . n 
D 3 105 ARG 105 105 105 ARG ARG F . n 
D 3 106 PRO 106 106 106 PRO PRO F . n 
D 3 107 LYS 107 107 107 LYS LYS F . n 
D 3 108 LYS 108 108 108 LYS LYS F . n 
D 3 109 ASP 109 109 109 ASP ASP F . n 
D 3 110 ARG 110 110 ?   ?   ?   F . n 
D 3 111 ALA 111 111 ?   ?   ?   F . n 
D 3 112 ARG 112 112 ?   ?   ?   F . n 
D 3 113 GLN 113 113 ?   ?   ?   F . n 
D 3 114 GLU 114 114 ?   ?   ?   F . n 
D 3 115 ASN 115 115 ?   ?   ?   F . n 
D 3 116 CYS 116 116 ?   ?   ?   F . n 
D 3 117 ASP 117 117 ?   ?   ?   F . n 
D 3 118 LYS 118 118 ?   ?   ?   F . n 
D 3 119 PRO 119 119 ?   ?   ?   F . n 
D 3 120 ARG 120 120 ?   ?   ?   F . n 
D 3 121 ARG 121 121 ?   ?   ?   F . n 
E 1 1   GLU 1   1   1   GLU GLU A . n 
E 1 2   VAL 2   2   2   VAL VAL A . n 
E 1 3   GLN 3   3   3   GLN GLN A . n 
E 1 4   LEU 4   4   4   LEU LEU A . n 
E 1 5   VAL 5   5   5   VAL VAL A . n 
E 1 6   GLU 6   6   6   GLU GLU A . n 
E 1 7   SER 7   7   7   SER SER A . n 
E 1 8   GLY 8   8   8   GLY GLY A . n 
E 1 9   GLY 9   9   9   GLY GLY A . n 
E 1 10  GLY 10  11  11  GLY GLY A . n 
E 1 11  LEU 11  12  12  LEU LEU A . n 
E 1 12  VAL 12  13  13  VAL VAL A . n 
E 1 13  GLN 13  14  14  GLN GLN A . n 
E 1 14  PRO 14  15  15  PRO PRO A . n 
E 1 15  GLY 15  16  16  GLY GLY A . n 
E 1 16  GLY 16  17  17  GLY GLY A . n 
E 1 17  SER 17  18  18  SER SER A . n 
E 1 18  LEU 18  19  19  LEU LEU A . n 
E 1 19  ARG 19  20  20  ARG ARG A . n 
E 1 20  LEU 20  21  21  LEU LEU A . n 
E 1 21  SER 21  22  22  SER SER A . n 
E 1 22  CYS 22  23  23  CYS CYS A . n 
E 1 23  ALA 23  24  24  ALA ALA A . n 
E 1 24  ALA 24  25  25  ALA ALA A . n 
E 1 25  SER 25  26  26  SER SER A . n 
E 1 26  GLY 26  27  27  GLY GLY A . n 
E 1 27  PHE 27  28  28  PHE PHE A . n 
E 1 28  ASP 28  29  29  ASP ASP A . n 
E 1 29  LEU 29  30  30  LEU LEU A . n 
E 1 30  TRP 30  35  35  TRP TRP A . n 
E 1 31  TYR 31  36  36  TYR TYR A . n 
E 1 32  TYR 32  37  37  TYR TYR A . n 
E 1 33  SER 33  38  38  SER SER A . n 
E 1 34  ILE 34  39  39  ILE ILE A . n 
E 1 35  HIS 35  40  40  HIS HIS A . n 
E 1 36  TRP 36  41  41  TRP TRP A . n 
E 1 37  VAL 37  42  42  VAL VAL A . n 
E 1 38  ARG 38  43  43  ARG ARG A . n 
E 1 39  GLN 39  44  44  GLN GLN A . n 
E 1 40  ALA 40  45  45  ALA ALA A . n 
E 1 41  PRO 41  46  46  PRO PRO A . n 
E 1 42  GLY 42  47  47  GLY GLY A . n 
E 1 43  LYS 43  48  48  LYS LYS A . n 
E 1 44  GLY 44  49  49  GLY GLY A . n 
E 1 45  LEU 45  50  50  LEU LEU A . n 
E 1 46  GLU 46  51  51  GLU GLU A . n 
E 1 47  TRP 47  52  52  TRP TRP A . n 
E 1 48  VAL 48  53  53  VAL VAL A . n 
E 1 49  ALA 49  54  54  ALA ALA A . n 
E 1 50  TYR 50  55  55  TYR TYR A . n 
E 1 51  ILE 51  56  56  ILE ILE A . n 
E 1 52  TYR 52  57  57  TYR TYR A . n 
E 1 53  PRO 53  58  58  PRO PRO A . n 
E 1 54  SER 54  59  59  SER SER A . n 
E 1 55  TYR 55  62  62  TYR TYR A . n 
E 1 56  GLY 56  63  63  GLY GLY A . n 
E 1 57  TYR 57  64  64  TYR TYR A . n 
E 1 58  THR 58  65  65  THR THR A . n 
E 1 59  TYR 59  66  66  TYR TYR A . n 
E 1 60  TYR 60  67  67  TYR TYR A . n 
E 1 61  ALA 61  68  68  ALA ALA A . n 
E 1 62  ASP 62  69  69  ASP ASP A . n 
E 1 63  SER 63  70  70  SER SER A . n 
E 1 64  VAL 64  71  71  VAL VAL A . n 
E 1 65  LYS 65  72  72  LYS LYS A . n 
E 1 66  GLY 66  74  74  GLY GLY A . n 
E 1 67  ARG 67  75  75  ARG ARG A . n 
E 1 68  PHE 68  76  76  PHE PHE A . n 
E 1 69  THR 69  77  77  THR THR A . n 
E 1 70  ILE 70  78  78  ILE ILE A . n 
E 1 71  SER 71  79  79  SER SER A . n 
E 1 72  ALA 72  80  80  ALA ALA A . n 
E 1 73  ASP 73  81  81  ASP ASP A . n 
E 1 74  THR 74  82  82  THR THR A . n 
E 1 75  SER 75  83  83  SER SER A . n 
E 1 76  LYS 76  84  84  LYS LYS A . n 
E 1 77  ASN 77  85  85  ASN ASN A . n 
E 1 78  THR 78  86  86  THR THR A . n 
E 1 79  ALA 79  87  87  ALA ALA A . n 
E 1 80  TYR 80  88  88  TYR TYR A . n 
E 1 81  LEU 81  89  89  LEU LEU A . n 
E 1 82  GLN 82  90  90  GLN GLN A . n 
E 1 83  MET 83  91  91  MET MET A . n 
E 1 84  ASN 84  92  92  ASN ASN A . n 
E 1 85  SER 85  93  93  SER SER A . n 
E 1 86  LEU 86  94  94  LEU LEU A . n 
E 1 87  ARG 87  95  95  ARG ARG A . n 
E 1 88  ALA 88  96  96  ALA ALA A . n 
E 1 89  GLU 89  97  97  GLU GLU A . n 
E 1 90  ASP 90  98  98  ASP ASP A . n 
E 1 91  THR 91  99  99  THR THR A . n 
E 1 92  ALA 92  100 100 ALA ALA A . n 
E 1 93  VAL 93  101 101 VAL VAL A . n 
E 1 94  TYR 94  102 102 TYR TYR A . n 
E 1 95  TYR 95  103 103 TYR TYR A . n 
E 1 96  CYS 96  104 104 CYS CYS A . n 
E 1 97  ALA 97  105 105 ALA ALA A . n 
E 1 98  ARG 98  106 106 ARG ARG A . n 
E 1 99  HIS 99  107 107 HIS HIS A . n 
E 1 100 ALA 100 108 108 ALA ALA A . n 
E 1 101 TRP 101 109 109 TRP TRP A . n 
E 1 102 TYR 102 110 110 TYR TYR A . n 
E 1 103 TYR 103 111 111 TYR TYR A . n 
E 1 104 GLY 104 112 112 GLY GLY A . n 
E 1 105 TRP 105 113 113 TRP TRP A . n 
E 1 106 GLY 106 114 114 GLY GLY A . n 
E 1 107 LEU 107 115 115 LEU LEU A . n 
E 1 108 ASP 108 116 116 ASP ASP A . n 
E 1 109 TYR 109 117 117 TYR TYR A . n 
E 1 110 TRP 110 118 118 TRP TRP A . n 
E 1 111 GLY 111 119 119 GLY GLY A . n 
E 1 112 GLN 112 120 120 GLN GLN A . n 
E 1 113 GLY 113 121 121 GLY GLY A . n 
E 1 114 THR 114 122 122 THR THR A . n 
E 1 115 LEU 115 123 123 LEU LEU A . n 
E 1 116 VAL 116 124 124 VAL VAL A . n 
E 1 117 THR 117 125 125 THR THR A . n 
E 1 118 VAL 118 126 126 VAL VAL A . n 
E 1 119 SER 119 127 127 SER SER A . n 
E 1 120 SER 120 128 128 SER SER A . n 
E 1 121 ALA 121 129 129 ALA ALA A . n 
E 1 122 SER 122 130 130 SER SER A . n 
E 1 123 THR 123 131 131 THR THR A . n 
E 1 124 LYS 124 132 132 LYS LYS A . n 
E 1 125 GLY 125 133 133 GLY GLY A . n 
E 1 126 PRO 126 134 134 PRO PRO A . n 
E 1 127 SER 127 135 135 SER SER A . n 
E 1 128 VAL 128 136 136 VAL VAL A . n 
E 1 129 PHE 129 137 137 PHE PHE A . n 
E 1 130 PRO 130 138 138 PRO PRO A . n 
E 1 131 LEU 131 139 139 LEU LEU A . n 
E 1 132 ALA 132 140 140 ALA ALA A . n 
E 1 133 PRO 133 141 141 PRO PRO A . n 
E 1 134 SER 134 142 142 SER SER A . n 
E 1 135 SER 135 143 143 SER SER A . n 
E 1 136 LYS 136 144 144 LYS LYS A . n 
E 1 137 SER 137 145 145 SER SER A . n 
E 1 138 THR 138 146 146 THR THR A . n 
E 1 139 SER 139 147 147 SER SER A . n 
E 1 140 GLY 140 148 148 GLY GLY A . n 
E 1 141 GLY 141 149 149 GLY GLY A . n 
E 1 142 THR 142 150 150 THR THR A . n 
E 1 143 ALA 143 151 151 ALA ALA A . n 
E 1 144 ALA 144 152 152 ALA ALA A . n 
E 1 145 LEU 145 153 153 LEU LEU A . n 
E 1 146 GLY 146 154 154 GLY GLY A . n 
E 1 147 CYS 147 155 155 CYS CYS A . n 
E 1 148 LEU 148 156 156 LEU LEU A . n 
E 1 149 VAL 149 157 157 VAL VAL A . n 
E 1 150 LYS 150 158 158 LYS LYS A . n 
E 1 151 ASP 151 159 159 ASP ASP A . n 
E 1 152 TYR 152 160 160 TYR TYR A . n 
E 1 153 PHE 153 161 161 PHE PHE A . n 
E 1 154 PRO 154 162 162 PRO PRO A . n 
E 1 155 GLU 155 163 163 GLU GLU A . n 
E 1 156 PRO 156 164 164 PRO PRO A . n 
E 1 157 VAL 157 165 165 VAL VAL A . n 
E 1 158 THR 158 166 166 THR THR A . n 
E 1 159 VAL 159 167 167 VAL VAL A . n 
E 1 160 SER 160 168 168 SER SER A . n 
E 1 161 TRP 161 169 169 TRP TRP A . n 
E 1 162 ASN 162 170 170 ASN ASN A . n 
E 1 163 SER 163 171 171 SER SER A . n 
E 1 164 GLY 164 172 172 GLY GLY A . n 
E 1 165 ALA 165 173 173 ALA ALA A . n 
E 1 166 LEU 166 174 174 LEU LEU A . n 
E 1 167 THR 167 175 175 THR THR A . n 
E 1 168 SER 168 176 176 SER SER A . n 
E 1 169 GLY 169 177 177 GLY GLY A . n 
E 1 170 VAL 170 178 178 VAL VAL A . n 
E 1 171 HIS 171 179 179 HIS HIS A . n 
E 1 172 THR 172 180 180 THR THR A . n 
E 1 173 PHE 173 181 181 PHE PHE A . n 
E 1 174 PRO 174 182 182 PRO PRO A . n 
E 1 175 ALA 175 183 183 ALA ALA A . n 
E 1 176 VAL 176 184 184 VAL VAL A . n 
E 1 177 LEU 177 185 185 LEU LEU A . n 
E 1 178 GLN 178 186 186 GLN GLN A . n 
E 1 179 SER 179 187 187 SER SER A . n 
E 1 180 SER 180 188 188 SER SER A . n 
E 1 181 GLY 181 189 189 GLY GLY A . n 
E 1 182 LEU 182 190 190 LEU LEU A . n 
E 1 183 TYR 183 191 191 TYR TYR A . n 
E 1 184 SER 184 192 192 SER SER A . n 
E 1 185 LEU 185 193 193 LEU LEU A . n 
E 1 186 SER 186 194 194 SER SER A . n 
E 1 187 SER 187 195 195 SER SER A . n 
E 1 188 VAL 188 196 196 VAL VAL A . n 
E 1 189 VAL 189 197 197 VAL VAL A . n 
E 1 190 THR 190 198 198 THR THR A . n 
E 1 191 VAL 191 199 199 VAL VAL A . n 
E 1 192 PRO 192 200 200 PRO PRO A . n 
E 1 193 SER 193 201 201 SER SER A . n 
E 1 194 SER 194 202 202 SER SER A . n 
E 1 195 SER 195 203 203 SER SER A . n 
E 1 196 LEU 196 204 204 LEU LEU A . n 
E 1 197 GLY 197 205 205 GLY GLY A . n 
E 1 198 THR 198 206 206 THR THR A . n 
E 1 199 GLN 199 207 207 GLN GLN A . n 
E 1 200 THR 200 208 208 THR THR A . n 
E 1 201 TYR 201 209 209 TYR TYR A . n 
E 1 202 ILE 202 210 210 ILE ILE A . n 
E 1 203 CYS 203 211 211 CYS CYS A . n 
E 1 204 ASN 204 212 212 ASN ASN A . n 
E 1 205 VAL 205 213 213 VAL VAL A . n 
E 1 206 ASN 206 214 214 ASN ASN A . n 
E 1 207 HIS 207 215 215 HIS HIS A . n 
E 1 208 LYS 208 216 216 LYS LYS A . n 
E 1 209 PRO 209 217 217 PRO PRO A . n 
E 1 210 SER 210 218 218 SER SER A . n 
E 1 211 ASN 211 219 219 ASN ASN A . n 
E 1 212 THR 212 220 220 THR THR A . n 
E 1 213 LYS 213 221 221 LYS LYS A . n 
E 1 214 VAL 214 222 222 VAL VAL A . n 
E 1 215 ASP 215 223 223 ASP ASP A . n 
E 1 216 LYS 216 224 224 LYS LYS A . n 
E 1 217 LYS 217 225 225 LYS LYS A . n 
E 1 218 VAL 218 226 226 VAL VAL A . n 
E 1 219 GLU 219 227 227 GLU GLU A . n 
E 1 220 PRO 220 228 228 PRO PRO A . n 
E 1 221 LYS 221 229 229 LYS LYS A . n 
E 1 222 SER 222 230 ?   ?   ?   A . n 
E 1 223 CYS 223 231 ?   ?   ?   A . n 
E 1 224 ASP 224 232 ?   ?   ?   A . n 
E 1 225 LYS 225 233 ?   ?   ?   A . n 
E 1 226 THR 226 234 ?   ?   ?   A . n 
E 1 227 HIS 227 235 ?   ?   ?   A . n 
E 1 228 THR 228 236 ?   ?   ?   A . n 
F 2 1   ASP 1   1   ?   ?   ?   B . n 
F 2 2   ILE 2   2   ?   ?   ?   B . n 
F 2 3   GLN 3   3   ?   ?   ?   B . n 
F 2 4   MET 4   4   ?   ?   ?   B . n 
F 2 5   THR 5   5   5   THR THR B . n 
F 2 6   GLN 6   6   6   GLN GLN B . n 
F 2 7   SER 7   7   7   SER SER B . n 
F 2 8   PRO 8   8   8   PRO PRO B . n 
F 2 9   SER 9   9   9   SER SER B . n 
F 2 10  SER 10  10  10  SER SER B . n 
F 2 11  LEU 11  11  11  LEU LEU B . n 
F 2 12  SER 12  12  12  SER SER B . n 
F 2 13  ALA 13  13  13  ALA ALA B . n 
F 2 14  SER 14  14  14  SER SER B . n 
F 2 15  VAL 15  15  15  VAL VAL B . n 
F 2 16  GLY 16  16  16  GLY GLY B . n 
F 2 17  ASP 17  17  17  ASP ASP B . n 
F 2 18  ARG 18  18  18  ARG ARG B . n 
F 2 19  VAL 19  19  19  VAL VAL B . n 
F 2 20  THR 20  20  20  THR THR B . n 
F 2 21  ILE 21  21  21  ILE ILE B . n 
F 2 22  THR 22  22  22  THR THR B . n 
F 2 23  CYS 23  23  23  CYS CYS B . n 
F 2 24  ARG 24  24  24  ARG ARG B . n 
F 2 25  ALA 25  25  25  ALA ALA B . n 
F 2 26  SER 26  26  26  SER SER B . n 
F 2 27  GLN 27  27  27  GLN GLN B . n 
F 2 28  ALA 28  28  28  ALA ALA B . n 
F 2 29  ALA 29  29  29  ALA ALA B . n 
F 2 30  TYR 30  36  36  TYR TYR B . n 
F 2 31  GLY 31  37  37  GLY GLY B . n 
F 2 32  ARG 32  38  38  ARG ARG B . n 
F 2 33  VAL 33  39  39  VAL VAL B . n 
F 2 34  ALA 34  40  40  ALA ALA B . n 
F 2 35  TRP 35  41  41  TRP TRP B . n 
F 2 36  TYR 36  42  42  TYR TYR B . n 
F 2 37  GLN 37  43  43  GLN GLN B . n 
F 2 38  GLN 38  44  44  GLN GLN B . n 
F 2 39  LYS 39  45  45  LYS LYS B . n 
F 2 40  PRO 40  46  46  PRO PRO B . n 
F 2 41  GLY 41  47  47  GLY GLY B . n 
F 2 42  LYS 42  48  48  LYS LYS B . n 
F 2 43  ALA 43  49  49  ALA ALA B . n 
F 2 44  PRO 44  50  50  PRO PRO B . n 
F 2 45  LYS 45  51  51  LYS LYS B . n 
F 2 46  LEU 46  52  52  LEU LEU B . n 
F 2 47  LEU 47  53  53  LEU LEU B . n 
F 2 48  ILE 48  54  54  ILE ILE B . n 
F 2 49  TYR 49  55  55  TYR TYR B . n 
F 2 50  LYS 50  56  56  LYS LYS B . n 
F 2 51  ALA 51  57  57  ALA ALA B . n 
F 2 52  SER 52  65  65  SER SER B . n 
F 2 53  GLU 53  66  66  GLU GLU B . n 
F 2 54  LEU 54  67  67  LEU LEU B . n 
F 2 55  TYR 55  68  68  TYR TYR B . n 
F 2 56  ALA 56  69  69  ALA ALA B . n 
F 2 57  GLY 57  70  70  GLY GLY B . n 
F 2 58  VAL 58  71  71  VAL VAL B . n 
F 2 59  PRO 59  72  72  PRO PRO B . n 
F 2 60  SER 60  74  74  SER SER B . n 
F 2 61  ARG 61  75  75  ARG ARG B . n 
F 2 62  PHE 62  76  76  PHE PHE B . n 
F 2 63  SER 63  77  77  SER SER B . n 
F 2 64  GLY 64  78  78  GLY GLY B . n 
F 2 65  SER 65  79  79  SER SER B . n 
F 2 66  ARG 66  80  80  ARG ARG B . n 
F 2 67  SER 67  83  83  SER SER B . n 
F 2 68  GLY 68  84  84  GLY GLY B . n 
F 2 69  THR 69  85  85  THR THR B . n 
F 2 70  ASP 70  86  86  ASP ASP B . n 
F 2 71  PHE 71  87  87  PHE PHE B . n 
F 2 72  THR 72  88  88  THR THR B . n 
F 2 73  LEU 73  89  89  LEU LEU B . n 
F 2 74  THR 74  90  90  THR THR B . n 
F 2 75  ILE 75  91  91  ILE ILE B . n 
F 2 76  SER 76  92  92  SER SER B . n 
F 2 77  SER 77  93  93  SER SER B . n 
F 2 78  LEU 78  94  94  LEU LEU B . n 
F 2 79  GLN 79  95  95  GLN GLN B . n 
F 2 80  PRO 80  96  96  PRO PRO B . n 
F 2 81  GLU 81  97  97  GLU GLU B . n 
F 2 82  ASP 82  98  98  ASP ASP B . n 
F 2 83  PHE 83  99  99  PHE PHE B . n 
F 2 84  ALA 84  100 100 ALA ALA B . n 
F 2 85  THR 85  101 101 THR THR B . n 
F 2 86  TYR 86  102 102 TYR TYR B . n 
F 2 87  TYR 87  103 103 TYR TYR B . n 
F 2 88  CYS 88  104 104 CYS CYS B . n 
F 2 89  GLN 89  105 105 GLN GLN B . n 
F 2 90  GLN 90  106 106 GLN GLN B . n 
F 2 91  ARG 91  107 107 ARG ARG B . n 
F 2 92  GLY 92  108 108 GLY GLY B . n 
F 2 93  TRP 93  109 109 TRP TRP B . n 
F 2 94  TYR 94  114 114 TYR TYR B . n 
F 2 95  LEU 95  115 115 LEU LEU B . n 
F 2 96  PHE 96  116 116 PHE PHE B . n 
F 2 97  THR 97  117 117 THR THR B . n 
F 2 98  PHE 98  118 118 PHE PHE B . n 
F 2 99  GLY 99  119 119 GLY GLY B . n 
F 2 100 GLN 100 120 120 GLN GLN B . n 
F 2 101 GLY 101 121 121 GLY GLY B . n 
F 2 102 THR 102 122 122 THR THR B . n 
F 2 103 LYS 103 123 123 LYS LYS B . n 
F 2 104 VAL 104 124 124 VAL VAL B . n 
F 2 105 GLU 105 125 125 GLU GLU B . n 
F 2 106 ILE 106 126 126 ILE ILE B . n 
F 2 107 LYS 107 127 127 LYS LYS B . n 
F 2 108 ARG 108 128 128 ARG ARG B . n 
F 2 109 THR 109 129 129 THR THR B . n 
F 2 110 VAL 110 130 130 VAL VAL B . n 
F 2 111 ALA 111 131 131 ALA ALA B . n 
F 2 112 ALA 112 132 132 ALA ALA B . n 
F 2 113 PRO 113 133 133 PRO PRO B . n 
F 2 114 SER 114 134 134 SER SER B . n 
F 2 115 VAL 115 135 135 VAL VAL B . n 
F 2 116 PHE 116 136 136 PHE PHE B . n 
F 2 117 ILE 117 137 137 ILE ILE B . n 
F 2 118 PHE 118 138 138 PHE PHE B . n 
F 2 119 PRO 119 139 139 PRO PRO B . n 
F 2 120 PRO 120 140 140 PRO PRO B . n 
F 2 121 SER 121 141 141 SER SER B . n 
F 2 122 ASP 122 142 142 ASP ASP B . n 
F 2 123 GLU 123 143 143 GLU GLU B . n 
F 2 124 GLN 124 144 144 GLN GLN B . n 
F 2 125 LEU 125 145 145 LEU LEU B . n 
F 2 126 LYS 126 146 146 LYS LYS B . n 
F 2 127 SER 127 147 147 SER SER B . n 
F 2 128 GLY 128 148 148 GLY GLY B . n 
F 2 129 THR 129 149 149 THR THR B . n 
F 2 130 ALA 130 150 150 ALA ALA B . n 
F 2 131 SER 131 151 151 SER SER B . n 
F 2 132 VAL 132 152 152 VAL VAL B . n 
F 2 133 VAL 133 153 153 VAL VAL B . n 
F 2 134 CYS 134 154 154 CYS CYS B . n 
F 2 135 LEU 135 155 155 LEU LEU B . n 
F 2 136 LEU 136 156 156 LEU LEU B . n 
F 2 137 ASN 137 157 157 ASN ASN B . n 
F 2 138 ASN 138 158 158 ASN ASN B . n 
F 2 139 PHE 139 159 159 PHE PHE B . n 
F 2 140 TYR 140 160 160 TYR TYR B . n 
F 2 141 PRO 141 161 161 PRO PRO B . n 
F 2 142 ARG 142 162 162 ARG ARG B . n 
F 2 143 GLU 143 163 163 GLU GLU B . n 
F 2 144 ALA 144 164 164 ALA ALA B . n 
F 2 145 LYS 145 165 165 LYS LYS B . n 
F 2 146 VAL 146 166 166 VAL VAL B . n 
F 2 147 SER 147 167 167 SER SER B . n 
F 2 148 TRP 148 168 168 TRP TRP B . n 
F 2 149 TYR 149 169 169 TYR TYR B . n 
F 2 150 VAL 150 170 170 VAL VAL B . n 
F 2 151 ASP 151 171 171 ASP ASP B . n 
F 2 152 ASN 152 172 172 ASN ASN B . n 
F 2 153 ALA 153 173 173 ALA ALA B . n 
F 2 154 LEU 154 174 174 LEU LEU B . n 
F 2 155 GLN 155 175 175 GLN GLN B . n 
F 2 156 SER 156 176 176 SER SER B . n 
F 2 157 GLY 157 177 177 GLY GLY B . n 
F 2 158 ASN 158 178 178 ASN ASN B . n 
F 2 159 SER 159 179 179 SER SER B . n 
F 2 160 GLN 160 180 180 GLN GLN B . n 
F 2 161 GLU 161 181 181 GLU GLU B . n 
F 2 162 SER 162 182 182 SER SER B . n 
F 2 163 VAL 163 183 183 VAL VAL B . n 
F 2 164 THR 164 184 184 THR THR B . n 
F 2 165 GLU 165 185 185 GLU GLU B . n 
F 2 166 GLN 166 186 186 GLN GLN B . n 
F 2 167 ASP 167 187 187 ASP ASP B . n 
F 2 168 SER 168 188 188 SER SER B . n 
F 2 169 LYS 169 189 189 LYS LYS B . n 
F 2 170 ASP 170 190 190 ASP ASP B . n 
F 2 171 SER 171 191 191 SER SER B . n 
F 2 172 THR 172 192 192 THR THR B . n 
F 2 173 TYR 173 193 193 TYR TYR B . n 
F 2 174 SER 174 194 194 SER SER B . n 
F 2 175 LEU 175 195 195 LEU LEU B . n 
F 2 176 SER 176 196 196 SER SER B . n 
F 2 177 SER 177 197 197 SER SER B . n 
F 2 178 THR 178 198 198 THR THR B . n 
F 2 179 LEU 179 199 199 LEU LEU B . n 
F 2 180 THR 180 200 200 THR THR B . n 
F 2 181 LEU 181 201 201 LEU LEU B . n 
F 2 182 SER 182 202 202 SER SER B . n 
F 2 183 LYS 183 203 203 LYS LYS B . n 
F 2 184 ALA 184 204 204 ALA ALA B . n 
F 2 185 ASP 185 205 205 ASP ASP B . n 
F 2 186 TYR 186 206 206 TYR TYR B . n 
F 2 187 GLU 187 207 207 GLU GLU B . n 
F 2 188 LYS 188 208 208 LYS LYS B . n 
F 2 189 HIS 189 209 209 HIS HIS B . n 
F 2 190 LYS 190 210 210 LYS LYS B . n 
F 2 191 VAL 191 211 211 VAL VAL B . n 
F 2 192 TYR 192 212 212 TYR TYR B . n 
F 2 193 ALA 193 213 213 ALA ALA B . n 
F 2 194 CYS 194 214 214 CYS CYS B . n 
F 2 195 GLU 195 215 215 GLU GLU B . n 
F 2 196 VAL 196 216 216 VAL VAL B . n 
F 2 197 THR 197 217 217 THR THR B . n 
F 2 198 GLN 198 218 218 GLN GLN B . n 
F 2 199 GLY 199 219 219 GLY GLY B . n 
F 2 200 THR 200 220 220 THR THR B . n 
F 2 201 THR 201 221 221 THR THR B . n 
F 2 202 SER 202 222 222 SER SER B . n 
F 2 203 VAL 203 225 225 VAL VAL B . n 
F 2 204 THR 204 226 226 THR THR B . n 
F 2 205 LYS 205 227 227 LYS LYS B . n 
F 2 206 SER 206 228 228 SER SER B . n 
F 2 207 PHE 207 229 229 PHE PHE B . n 
F 2 208 ASN 208 230 230 ASN ASN B . n 
F 2 209 ARG 209 231 231 ARG ARG B . n 
F 2 210 GLY 210 232 232 GLY GLY B . n 
F 2 211 GLU 211 233 233 GLU GLU B . n 
F 2 212 CYS 212 234 234 CYS CYS B . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
G 4 NAG 1 G NAG 1 E NAG 109 n 
G 4 NAG 2 G NAG 2 E NAG 110 n 
H 5 NAG 1 H NAG 1 F NAG 110 n 
H 5 NAG 2 H NAG 2 F NAG 111 n 
H 5 BMA 3 H BMA 3 F BMA 112 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 BMA ? ? BMA ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NAG ? ? NAG ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 C GLU 1   ? CG  ? A GLU 1   CG  
2   1 Y 1 C GLU 1   ? CD  ? A GLU 1   CD  
3   1 Y 1 C GLU 1   ? OE1 ? A GLU 1   OE1 
4   1 Y 1 C GLU 1   ? OE2 ? A GLU 1   OE2 
5   1 Y 1 C GLN 3   ? CG  ? A GLN 3   CG  
6   1 Y 1 C GLN 3   ? CD  ? A GLN 3   CD  
7   1 Y 1 C GLN 3   ? OE1 ? A GLN 3   OE1 
8   1 Y 1 C GLN 3   ? NE2 ? A GLN 3   NE2 
9   1 Y 1 C GLN 14  ? CG  ? A GLN 13  CG  
10  1 Y 1 C GLN 14  ? CD  ? A GLN 13  CD  
11  1 Y 1 C GLN 14  ? OE1 ? A GLN 13  OE1 
12  1 Y 1 C GLN 14  ? NE2 ? A GLN 13  NE2 
13  1 Y 1 C LYS 48  ? CG  ? A LYS 43  CG  
14  1 Y 1 C LYS 48  ? CD  ? A LYS 43  CD  
15  1 Y 1 C LYS 48  ? CE  ? A LYS 43  CE  
16  1 Y 1 C LYS 48  ? NZ  ? A LYS 43  NZ  
17  1 Y 1 C LYS 72  ? CG  ? A LYS 65  CG  
18  1 Y 1 C LYS 72  ? CD  ? A LYS 65  CD  
19  1 Y 1 C LYS 72  ? CE  ? A LYS 65  CE  
20  1 Y 1 C LYS 72  ? NZ  ? A LYS 65  NZ  
21  1 Y 1 C LYS 84  ? CG  ? A LYS 76  CG  
22  1 Y 1 C LYS 84  ? CD  ? A LYS 76  CD  
23  1 Y 1 C LYS 84  ? CE  ? A LYS 76  CE  
24  1 Y 1 C LYS 84  ? NZ  ? A LYS 76  NZ  
25  1 Y 1 C ARG 95  ? NE  ? A ARG 87  NE  
26  1 Y 1 C ARG 95  ? CZ  ? A ARG 87  CZ  
27  1 Y 1 C ARG 95  ? NH1 ? A ARG 87  NH1 
28  1 Y 1 C ARG 95  ? NH2 ? A ARG 87  NH2 
29  1 Y 1 C LYS 132 ? CG  ? A LYS 124 CG  
30  1 Y 1 C LYS 132 ? CD  ? A LYS 124 CD  
31  1 Y 1 C LYS 132 ? CE  ? A LYS 124 CE  
32  1 Y 1 C LYS 132 ? NZ  ? A LYS 124 NZ  
33  1 Y 1 C LYS 144 ? CG  ? A LYS 136 CG  
34  1 Y 1 C LYS 144 ? CD  ? A LYS 136 CD  
35  1 Y 1 C LYS 144 ? CE  ? A LYS 136 CE  
36  1 Y 1 C LYS 144 ? NZ  ? A LYS 136 NZ  
37  1 Y 1 C LYS 158 ? CG  ? A LYS 150 CG  
38  1 Y 1 C LYS 158 ? CD  ? A LYS 150 CD  
39  1 Y 1 C LYS 158 ? CE  ? A LYS 150 CE  
40  1 Y 1 C LYS 158 ? NZ  ? A LYS 150 NZ  
41  1 Y 1 C PHE 181 ? CG  ? A PHE 173 CG  
42  1 Y 1 C PHE 181 ? CD1 ? A PHE 173 CD1 
43  1 Y 1 C PHE 181 ? CD2 ? A PHE 173 CD2 
44  1 Y 1 C PHE 181 ? CE1 ? A PHE 173 CE1 
45  1 Y 1 C PHE 181 ? CE2 ? A PHE 173 CE2 
46  1 Y 1 C PHE 181 ? CZ  ? A PHE 173 CZ  
47  1 Y 1 C LEU 185 ? CG  ? A LEU 177 CG  
48  1 Y 1 C LEU 185 ? CD1 ? A LEU 177 CD1 
49  1 Y 1 C LEU 185 ? CD2 ? A LEU 177 CD2 
50  1 Y 1 C GLN 186 ? CG  ? A GLN 178 CG  
51  1 Y 1 C GLN 186 ? CD  ? A GLN 178 CD  
52  1 Y 1 C GLN 186 ? OE1 ? A GLN 178 OE1 
53  1 Y 1 C GLN 186 ? NE2 ? A GLN 178 NE2 
54  1 Y 1 C LEU 190 ? CG  ? A LEU 182 CG  
55  1 Y 1 C LEU 190 ? CD1 ? A LEU 182 CD1 
56  1 Y 1 C LEU 190 ? CD2 ? A LEU 182 CD2 
57  1 Y 1 C TYR 191 ? CG  ? A TYR 183 CG  
58  1 Y 1 C TYR 191 ? CD1 ? A TYR 183 CD1 
59  1 Y 1 C TYR 191 ? CD2 ? A TYR 183 CD2 
60  1 Y 1 C TYR 191 ? CE1 ? A TYR 183 CE1 
61  1 Y 1 C TYR 191 ? CE2 ? A TYR 183 CE2 
62  1 Y 1 C TYR 191 ? CZ  ? A TYR 183 CZ  
63  1 Y 1 C TYR 191 ? OH  ? A TYR 183 OH  
64  1 Y 1 C LEU 204 ? CG  ? A LEU 196 CG  
65  1 Y 1 C LEU 204 ? CD1 ? A LEU 196 CD1 
66  1 Y 1 C LEU 204 ? CD2 ? A LEU 196 CD2 
67  1 Y 1 C LYS 216 ? CG  ? A LYS 208 CG  
68  1 Y 1 C LYS 216 ? CD  ? A LYS 208 CD  
69  1 Y 1 C LYS 216 ? CE  ? A LYS 208 CE  
70  1 Y 1 C LYS 216 ? NZ  ? A LYS 208 NZ  
71  1 Y 1 C LYS 221 ? CD  ? A LYS 213 CD  
72  1 Y 1 C LYS 221 ? CE  ? A LYS 213 CE  
73  1 Y 1 C LYS 221 ? NZ  ? A LYS 213 NZ  
74  1 Y 1 C LYS 224 ? CE  ? A LYS 216 CE  
75  1 Y 1 C LYS 224 ? NZ  ? A LYS 216 NZ  
76  1 Y 1 C LYS 225 ? CG  ? A LYS 217 CG  
77  1 Y 1 C LYS 225 ? CD  ? A LYS 217 CD  
78  1 Y 1 C LYS 225 ? CE  ? A LYS 217 CE  
79  1 Y 1 C LYS 225 ? NZ  ? A LYS 217 NZ  
80  1 Y 1 D GLN 6   ? CG  ? B GLN 6   CG  
81  1 Y 1 D GLN 6   ? CD  ? B GLN 6   CD  
82  1 Y 1 D GLN 6   ? OE1 ? B GLN 6   OE1 
83  1 Y 1 D GLN 6   ? NE2 ? B GLN 6   NE2 
84  1 Y 1 D LEU 11  ? CG  ? B LEU 11  CG  
85  1 Y 1 D LEU 11  ? CD1 ? B LEU 11  CD1 
86  1 Y 1 D LEU 11  ? CD2 ? B LEU 11  CD2 
87  1 Y 1 D ARG 38  ? CG  ? B ARG 32  CG  
88  1 Y 1 D ARG 38  ? CD  ? B ARG 32  CD  
89  1 Y 1 D ARG 38  ? NE  ? B ARG 32  NE  
90  1 Y 1 D ARG 38  ? CZ  ? B ARG 32  CZ  
91  1 Y 1 D ARG 38  ? NH1 ? B ARG 32  NH1 
92  1 Y 1 D ARG 38  ? NH2 ? B ARG 32  NH2 
93  1 Y 1 D LYS 45  ? CG  ? B LYS 39  CG  
94  1 Y 1 D LYS 45  ? CD  ? B LYS 39  CD  
95  1 Y 1 D LYS 45  ? CE  ? B LYS 39  CE  
96  1 Y 1 D LYS 45  ? NZ  ? B LYS 39  NZ  
97  1 Y 1 D LYS 51  ? CG  ? B LYS 45  CG  
98  1 Y 1 D LYS 51  ? CD  ? B LYS 45  CD  
99  1 Y 1 D LYS 51  ? CE  ? B LYS 45  CE  
100 1 Y 1 D LYS 51  ? NZ  ? B LYS 45  NZ  
101 1 Y 1 D GLN 106 ? CG  ? B GLN 90  CG  
102 1 Y 1 D GLN 106 ? CD  ? B GLN 90  CD  
103 1 Y 1 D GLN 106 ? OE1 ? B GLN 90  OE1 
104 1 Y 1 D GLN 106 ? NE2 ? B GLN 90  NE2 
105 1 Y 1 D ARG 107 ? CG  ? B ARG 91  CG  
106 1 Y 1 D ARG 107 ? CD  ? B ARG 91  CD  
107 1 Y 1 D ARG 107 ? NE  ? B ARG 91  NE  
108 1 Y 1 D ARG 107 ? CZ  ? B ARG 91  CZ  
109 1 Y 1 D ARG 107 ? NH1 ? B ARG 91  NH1 
110 1 Y 1 D ARG 107 ? NH2 ? B ARG 91  NH2 
111 1 Y 1 D GLN 120 ? CG  ? B GLN 100 CG  
112 1 Y 1 D GLN 120 ? CD  ? B GLN 100 CD  
113 1 Y 1 D GLN 120 ? OE1 ? B GLN 100 OE1 
114 1 Y 1 D GLN 120 ? NE2 ? B GLN 100 NE2 
115 1 Y 1 D LYS 123 ? CG  ? B LYS 103 CG  
116 1 Y 1 D LYS 123 ? CD  ? B LYS 103 CD  
117 1 Y 1 D LYS 123 ? CE  ? B LYS 103 CE  
118 1 Y 1 D LYS 123 ? NZ  ? B LYS 103 NZ  
119 1 Y 1 D ILE 126 ? CG1 ? B ILE 106 CG1 
120 1 Y 1 D ILE 126 ? CG2 ? B ILE 106 CG2 
121 1 Y 1 D ILE 126 ? CD1 ? B ILE 106 CD1 
122 1 Y 1 D LYS 127 ? CG  ? B LYS 107 CG  
123 1 Y 1 D LYS 127 ? CD  ? B LYS 107 CD  
124 1 Y 1 D LYS 127 ? CE  ? B LYS 107 CE  
125 1 Y 1 D LYS 127 ? NZ  ? B LYS 107 NZ  
126 1 Y 1 D ARG 128 ? CG  ? B ARG 108 CG  
127 1 Y 1 D ARG 128 ? CD  ? B ARG 108 CD  
128 1 Y 1 D ARG 128 ? NE  ? B ARG 108 NE  
129 1 Y 1 D ARG 128 ? CZ  ? B ARG 108 CZ  
130 1 Y 1 D ARG 128 ? NH1 ? B ARG 108 NH1 
131 1 Y 1 D ARG 128 ? NH2 ? B ARG 108 NH2 
132 1 Y 1 D ILE 137 ? CG1 ? B ILE 117 CG1 
133 1 Y 1 D ILE 137 ? CG2 ? B ILE 117 CG2 
134 1 Y 1 D ILE 137 ? CD1 ? B ILE 117 CD1 
135 1 Y 1 D LYS 146 ? CG  ? B LYS 126 CG  
136 1 Y 1 D LYS 146 ? CD  ? B LYS 126 CD  
137 1 Y 1 D LYS 146 ? CE  ? B LYS 126 CE  
138 1 Y 1 D LYS 146 ? NZ  ? B LYS 126 NZ  
139 1 Y 1 D LEU 156 ? CG  ? B LEU 136 CG  
140 1 Y 1 D LEU 156 ? CD1 ? B LEU 136 CD1 
141 1 Y 1 D LEU 156 ? CD2 ? B LEU 136 CD2 
142 1 Y 1 D PHE 159 ? CG  ? B PHE 139 CG  
143 1 Y 1 D PHE 159 ? CD1 ? B PHE 139 CD1 
144 1 Y 1 D PHE 159 ? CD2 ? B PHE 139 CD2 
145 1 Y 1 D PHE 159 ? CE1 ? B PHE 139 CE1 
146 1 Y 1 D PHE 159 ? CE2 ? B PHE 139 CE2 
147 1 Y 1 D PHE 159 ? CZ  ? B PHE 139 CZ  
148 1 Y 1 D TYR 160 ? CG  ? B TYR 140 CG  
149 1 Y 1 D TYR 160 ? CD1 ? B TYR 140 CD1 
150 1 Y 1 D TYR 160 ? CD2 ? B TYR 140 CD2 
151 1 Y 1 D TYR 160 ? CE1 ? B TYR 140 CE1 
152 1 Y 1 D TYR 160 ? CE2 ? B TYR 140 CE2 
153 1 Y 1 D TYR 160 ? CZ  ? B TYR 140 CZ  
154 1 Y 1 D TYR 160 ? OH  ? B TYR 140 OH  
155 1 Y 1 D ARG 162 ? CG  ? B ARG 142 CG  
156 1 Y 1 D ARG 162 ? CD  ? B ARG 142 CD  
157 1 Y 1 D ARG 162 ? NE  ? B ARG 142 NE  
158 1 Y 1 D ARG 162 ? CZ  ? B ARG 142 CZ  
159 1 Y 1 D ARG 162 ? NH1 ? B ARG 142 NH1 
160 1 Y 1 D ARG 162 ? NH2 ? B ARG 142 NH2 
161 1 Y 1 D GLU 163 ? CG  ? B GLU 143 CG  
162 1 Y 1 D GLU 163 ? CD  ? B GLU 143 CD  
163 1 Y 1 D GLU 163 ? OE1 ? B GLU 143 OE1 
164 1 Y 1 D GLU 163 ? OE2 ? B GLU 143 OE2 
165 1 Y 1 D LYS 165 ? CG  ? B LYS 145 CG  
166 1 Y 1 D LYS 165 ? CD  ? B LYS 145 CD  
167 1 Y 1 D LYS 165 ? CE  ? B LYS 145 CE  
168 1 Y 1 D LYS 165 ? NZ  ? B LYS 145 NZ  
169 1 Y 1 D GLN 180 ? CG  ? B GLN 160 CG  
170 1 Y 1 D GLN 180 ? CD  ? B GLN 160 CD  
171 1 Y 1 D GLN 180 ? OE1 ? B GLN 160 OE1 
172 1 Y 1 D GLN 180 ? NE2 ? B GLN 160 NE2 
173 1 Y 1 D GLU 181 ? CG  ? B GLU 161 CG  
174 1 Y 1 D GLU 181 ? CD  ? B GLU 161 CD  
175 1 Y 1 D GLU 181 ? OE1 ? B GLU 161 OE1 
176 1 Y 1 D GLU 181 ? OE2 ? B GLU 161 OE2 
177 1 Y 1 D GLU 185 ? CG  ? B GLU 165 CG  
178 1 Y 1 D GLU 185 ? CD  ? B GLU 165 CD  
179 1 Y 1 D GLU 185 ? OE1 ? B GLU 165 OE1 
180 1 Y 1 D GLU 185 ? OE2 ? B GLU 165 OE2 
181 1 Y 1 D LYS 189 ? CG  ? B LYS 169 CG  
182 1 Y 1 D LYS 189 ? CD  ? B LYS 169 CD  
183 1 Y 1 D LYS 189 ? CE  ? B LYS 169 CE  
184 1 Y 1 D LYS 189 ? NZ  ? B LYS 169 NZ  
185 1 Y 1 D LEU 195 ? CG  ? B LEU 175 CG  
186 1 Y 1 D LEU 195 ? CD1 ? B LEU 175 CD1 
187 1 Y 1 D LEU 195 ? CD2 ? B LEU 175 CD2 
188 1 Y 1 D LYS 203 ? CG  ? B LYS 183 CG  
189 1 Y 1 D LYS 203 ? CD  ? B LYS 183 CD  
190 1 Y 1 D LYS 203 ? CE  ? B LYS 183 CE  
191 1 Y 1 D LYS 203 ? NZ  ? B LYS 183 NZ  
192 1 Y 1 D LYS 208 ? CG  ? B LYS 188 CG  
193 1 Y 1 D LYS 208 ? CD  ? B LYS 188 CD  
194 1 Y 1 D LYS 208 ? CE  ? B LYS 188 CE  
195 1 Y 1 D LYS 208 ? NZ  ? B LYS 188 NZ  
196 1 Y 1 D LYS 210 ? CG  ? B LYS 190 CG  
197 1 Y 1 D LYS 210 ? CD  ? B LYS 190 CD  
198 1 Y 1 D LYS 210 ? CE  ? B LYS 190 CE  
199 1 Y 1 D LYS 210 ? NZ  ? B LYS 190 NZ  
200 1 Y 1 D LYS 227 ? CG  ? B LYS 205 CG  
201 1 Y 1 D LYS 227 ? CD  ? B LYS 205 CD  
202 1 Y 1 D LYS 227 ? CE  ? B LYS 205 CE  
203 1 Y 1 D LYS 227 ? NZ  ? B LYS 205 NZ  
204 1 Y 1 D PHE 229 ? CG  ? B PHE 207 CG  
205 1 Y 1 D PHE 229 ? CD1 ? B PHE 207 CD1 
206 1 Y 1 D PHE 229 ? CD2 ? B PHE 207 CD2 
207 1 Y 1 D PHE 229 ? CE1 ? B PHE 207 CE1 
208 1 Y 1 D PHE 229 ? CE2 ? B PHE 207 CE2 
209 1 Y 1 D PHE 229 ? CZ  ? B PHE 207 CZ  
210 1 Y 1 D GLU 233 ? CG  ? B GLU 211 CG  
211 1 Y 1 D GLU 233 ? CD  ? B GLU 211 CD  
212 1 Y 1 D GLU 233 ? OE1 ? B GLU 211 OE1 
213 1 Y 1 D GLU 233 ? OE2 ? B GLU 211 OE2 
214 1 Y 1 E GLU 13  ? CG  ? C GLU 13  CG  
215 1 Y 1 E GLU 13  ? CD  ? C GLU 13  CD  
216 1 Y 1 E GLU 13  ? OE1 ? C GLU 13  OE1 
217 1 Y 1 E GLU 13  ? OE2 ? C GLU 13  OE2 
218 1 Y 1 E LYS 16  ? CG  ? C LYS 16  CG  
219 1 Y 1 E LYS 16  ? CD  ? C LYS 16  CD  
220 1 Y 1 E LYS 16  ? CE  ? C LYS 16  CE  
221 1 Y 1 E LYS 16  ? NZ  ? C LYS 16  NZ  
222 1 Y 1 E ASP 41  ? CG  ? C ASP 41  CG  
223 1 Y 1 E ASP 41  ? OD1 ? C ASP 41  OD1 
224 1 Y 1 E ASP 41  ? OD2 ? C ASP 41  OD2 
225 1 Y 1 E GLU 42  ? CG  ? C GLU 42  CG  
226 1 Y 1 E GLU 42  ? CD  ? C GLU 42  CD  
227 1 Y 1 E GLU 42  ? OE1 ? C GLU 42  OE1 
228 1 Y 1 E GLU 42  ? OE2 ? C GLU 42  OE2 
229 1 Y 1 E ILE 43  ? CG1 ? C ILE 43  CG1 
230 1 Y 1 E ILE 43  ? CG2 ? C ILE 43  CG2 
231 1 Y 1 E ILE 43  ? CD1 ? C ILE 43  CD1 
232 1 Y 1 E GLU 44  ? CG  ? C GLU 44  CG  
233 1 Y 1 E GLU 44  ? CD  ? C GLU 44  CD  
234 1 Y 1 E GLU 44  ? OE1 ? C GLU 44  OE1 
235 1 Y 1 E GLU 44  ? OE2 ? C GLU 44  OE2 
236 1 Y 1 E LYS 48  ? CG  ? C LYS 48  CG  
237 1 Y 1 E LYS 48  ? CD  ? C LYS 48  CD  
238 1 Y 1 E LYS 48  ? CE  ? C LYS 48  CE  
239 1 Y 1 E LYS 48  ? NZ  ? C LYS 48  NZ  
240 1 Y 1 E ARG 56  ? CG  ? C ARG 56  CG  
241 1 Y 1 E ARG 56  ? CD  ? C ARG 56  CD  
242 1 Y 1 E ARG 56  ? NE  ? C ARG 56  NE  
243 1 Y 1 E ARG 56  ? CZ  ? C ARG 56  CZ  
244 1 Y 1 E ARG 56  ? NH1 ? C ARG 56  NH1 
245 1 Y 1 E ARG 56  ? NH2 ? C ARG 56  NH2 
246 1 Y 1 E GLU 64  ? CG  ? C GLU 64  CG  
247 1 Y 1 E GLU 64  ? CD  ? C GLU 64  CD  
248 1 Y 1 E GLU 64  ? OE1 ? C GLU 64  OE1 
249 1 Y 1 E GLU 64  ? OE2 ? C GLU 64  OE2 
250 1 Y 1 E GLU 72  ? CG  ? C GLU 72  CG  
251 1 Y 1 E GLU 72  ? CD  ? C GLU 72  CD  
252 1 Y 1 E GLU 72  ? OE1 ? C GLU 72  OE1 
253 1 Y 1 E GLU 72  ? OE2 ? C GLU 72  OE2 
254 1 Y 1 E GLU 73  ? CG  ? C GLU 73  CG  
255 1 Y 1 E GLU 73  ? CD  ? C GLU 73  CD  
256 1 Y 1 E GLU 73  ? OE1 ? C GLU 73  OE1 
257 1 Y 1 E GLU 73  ? OE2 ? C GLU 73  OE2 
258 1 Y 1 E LYS 84  ? CG  ? C LYS 84  CG  
259 1 Y 1 E LYS 84  ? CD  ? C LYS 84  CD  
260 1 Y 1 E LYS 84  ? CE  ? C LYS 84  CE  
261 1 Y 1 E LYS 84  ? NZ  ? C LYS 84  NZ  
262 1 Y 1 E GLN 87  ? CG  ? C GLN 87  CG  
263 1 Y 1 E GLN 87  ? CD  ? C GLN 87  CD  
264 1 Y 1 E GLN 87  ? OE1 ? C GLN 87  OE1 
265 1 Y 1 E GLN 87  ? NE2 ? C GLN 87  NE2 
266 1 Y 1 E GLU 93  ? CG  ? C GLU 93  CG  
267 1 Y 1 E GLU 93  ? CD  ? C GLU 93  CD  
268 1 Y 1 E GLU 93  ? OE1 ? C GLU 93  OE1 
269 1 Y 1 E GLU 93  ? OE2 ? C GLU 93  OE2 
270 1 Y 1 E LYS 108 ? CG  ? C LYS 108 CG  
271 1 Y 1 E LYS 108 ? CD  ? C LYS 108 CD  
272 1 Y 1 E LYS 108 ? CE  ? C LYS 108 CE  
273 1 Y 1 E LYS 108 ? NZ  ? C LYS 108 NZ  
274 1 Y 1 F HIS 11  ? CG  ? D HIS 11  CG  
275 1 Y 1 F HIS 11  ? ND1 ? D HIS 11  ND1 
276 1 Y 1 F HIS 11  ? CD2 ? D HIS 11  CD2 
277 1 Y 1 F HIS 11  ? CE1 ? D HIS 11  CE1 
278 1 Y 1 F HIS 11  ? NE2 ? D HIS 11  NE2 
279 1 Y 1 F GLU 13  ? CG  ? D GLU 13  CG  
280 1 Y 1 F GLU 13  ? CD  ? D GLU 13  CD  
281 1 Y 1 F GLU 13  ? OE1 ? D GLU 13  OE1 
282 1 Y 1 F GLU 13  ? OE2 ? D GLU 13  OE2 
283 1 Y 1 F LYS 16  ? CG  ? D LYS 16  CG  
284 1 Y 1 F LYS 16  ? CD  ? D LYS 16  CD  
285 1 Y 1 F LYS 16  ? CE  ? D LYS 16  CE  
286 1 Y 1 F LYS 16  ? NZ  ? D LYS 16  NZ  
287 1 Y 1 F PHE 36  ? CG  ? D PHE 36  CG  
288 1 Y 1 F PHE 36  ? CD1 ? D PHE 36  CD1 
289 1 Y 1 F PHE 36  ? CD2 ? D PHE 36  CD2 
290 1 Y 1 F PHE 36  ? CE1 ? D PHE 36  CE1 
291 1 Y 1 F PHE 36  ? CE2 ? D PHE 36  CE2 
292 1 Y 1 F PHE 36  ? CZ  ? D PHE 36  CZ  
293 1 Y 1 F GLN 37  ? CG  ? D GLN 37  CG  
294 1 Y 1 F GLN 37  ? CD  ? D GLN 37  CD  
295 1 Y 1 F GLN 37  ? OE1 ? D GLN 37  OE1 
296 1 Y 1 F GLN 37  ? NE2 ? D GLN 37  NE2 
297 1 Y 1 F ASP 41  ? CG  ? D ASP 41  CG  
298 1 Y 1 F ASP 41  ? OD1 ? D ASP 41  OD1 
299 1 Y 1 F ASP 41  ? OD2 ? D ASP 41  OD2 
300 1 Y 1 F GLU 42  ? CG  ? D GLU 42  CG  
301 1 Y 1 F GLU 42  ? CD  ? D GLU 42  CD  
302 1 Y 1 F GLU 42  ? OE1 ? D GLU 42  OE1 
303 1 Y 1 F GLU 42  ? OE2 ? D GLU 42  OE2 
304 1 Y 1 F ILE 43  ? CG1 ? D ILE 43  CG1 
305 1 Y 1 F ILE 43  ? CG2 ? D ILE 43  CG2 
306 1 Y 1 F ILE 43  ? CD1 ? D ILE 43  CD1 
307 1 Y 1 F GLU 44  ? CG  ? D GLU 44  CG  
308 1 Y 1 F GLU 44  ? CD  ? D GLU 44  CD  
309 1 Y 1 F GLU 44  ? OE1 ? D GLU 44  OE1 
310 1 Y 1 F GLU 44  ? OE2 ? D GLU 44  OE2 
311 1 Y 1 F LYS 48  ? CG  ? D LYS 48  CG  
312 1 Y 1 F LYS 48  ? CD  ? D LYS 48  CD  
313 1 Y 1 F LYS 48  ? CE  ? D LYS 48  CE  
314 1 Y 1 F LYS 48  ? NZ  ? D LYS 48  NZ  
315 1 Y 1 F GLU 72  ? CG  ? D GLU 72  CG  
316 1 Y 1 F GLU 72  ? CD  ? D GLU 72  CD  
317 1 Y 1 F GLU 72  ? OE1 ? D GLU 72  OE1 
318 1 Y 1 F GLU 72  ? OE2 ? D GLU 72  OE2 
319 1 Y 1 F HIS 90  ? CG  ? D HIS 90  CG  
320 1 Y 1 F HIS 90  ? ND1 ? D HIS 90  ND1 
321 1 Y 1 F HIS 90  ? CD2 ? D HIS 90  CD2 
322 1 Y 1 F HIS 90  ? CE1 ? D HIS 90  CE1 
323 1 Y 1 F HIS 90  ? NE2 ? D HIS 90  NE2 
324 1 Y 1 F GLU 93  ? CG  ? D GLU 93  CG  
325 1 Y 1 F GLU 93  ? CD  ? D GLU 93  CD  
326 1 Y 1 F GLU 93  ? OE1 ? D GLU 93  OE1 
327 1 Y 1 F GLU 93  ? OE2 ? D GLU 93  OE2 
328 1 Y 1 F LYS 101 ? CG  ? D LYS 101 CG  
329 1 Y 1 F LYS 101 ? CD  ? D LYS 101 CD  
330 1 Y 1 F LYS 101 ? CE  ? D LYS 101 CE  
331 1 Y 1 F LYS 101 ? NZ  ? D LYS 101 NZ  
332 1 Y 1 F LYS 107 ? CG  ? D LYS 107 CG  
333 1 Y 1 F LYS 107 ? CD  ? D LYS 107 CD  
334 1 Y 1 F LYS 107 ? CE  ? D LYS 107 CE  
335 1 Y 1 F LYS 107 ? NZ  ? D LYS 107 NZ  
336 1 Y 1 F LYS 108 ? CG  ? D LYS 108 CG  
337 1 Y 1 F LYS 108 ? CD  ? D LYS 108 CD  
338 1 Y 1 F LYS 108 ? CE  ? D LYS 108 CE  
339 1 Y 1 F LYS 108 ? NZ  ? D LYS 108 NZ  
340 1 Y 1 F ASP 109 ? CG  ? D ASP 109 CG  
341 1 Y 1 F ASP 109 ? OD1 ? D ASP 109 OD1 
342 1 Y 1 F ASP 109 ? OD2 ? D ASP 109 OD2 
343 1 Y 1 A GLU 1   ? CG  ? E GLU 1   CG  
344 1 Y 1 A GLU 1   ? CD  ? E GLU 1   CD  
345 1 Y 1 A GLU 1   ? OE1 ? E GLU 1   OE1 
346 1 Y 1 A GLU 1   ? OE2 ? E GLU 1   OE2 
347 1 Y 1 A LYS 72  ? CG  ? E LYS 65  CG  
348 1 Y 1 A LYS 72  ? CD  ? E LYS 65  CD  
349 1 Y 1 A LYS 72  ? CE  ? E LYS 65  CE  
350 1 Y 1 A LYS 72  ? NZ  ? E LYS 65  NZ  
351 1 Y 1 A LYS 84  ? CG  ? E LYS 76  CG  
352 1 Y 1 A LYS 84  ? CD  ? E LYS 76  CD  
353 1 Y 1 A LYS 84  ? CE  ? E LYS 76  CE  
354 1 Y 1 A LYS 84  ? NZ  ? E LYS 76  NZ  
355 1 Y 1 A LYS 132 ? CG  ? E LYS 124 CG  
356 1 Y 1 A LYS 132 ? CD  ? E LYS 124 CD  
357 1 Y 1 A LYS 132 ? CE  ? E LYS 124 CE  
358 1 Y 1 A LYS 132 ? NZ  ? E LYS 124 NZ  
359 1 Y 1 A LYS 144 ? CG  ? E LYS 136 CG  
360 1 Y 1 A LYS 144 ? CD  ? E LYS 136 CD  
361 1 Y 1 A LYS 144 ? CE  ? E LYS 136 CE  
362 1 Y 1 A LYS 144 ? NZ  ? E LYS 136 NZ  
363 1 Y 1 A LEU 204 ? CG  ? E LEU 196 CG  
364 1 Y 1 A LEU 204 ? CD1 ? E LEU 196 CD1 
365 1 Y 1 A LEU 204 ? CD2 ? E LEU 196 CD2 
366 1 Y 1 A GLN 207 ? CG  ? E GLN 199 CG  
367 1 Y 1 A GLN 207 ? CD  ? E GLN 199 CD  
368 1 Y 1 A GLN 207 ? OE1 ? E GLN 199 OE1 
369 1 Y 1 A GLN 207 ? NE2 ? E GLN 199 NE2 
370 1 Y 1 A LYS 216 ? CG  ? E LYS 208 CG  
371 1 Y 1 A LYS 216 ? CD  ? E LYS 208 CD  
372 1 Y 1 A LYS 216 ? CE  ? E LYS 208 CE  
373 1 Y 1 A LYS 216 ? NZ  ? E LYS 208 NZ  
374 1 Y 1 A LYS 224 ? CG  ? E LYS 216 CG  
375 1 Y 1 A LYS 224 ? CD  ? E LYS 216 CD  
376 1 Y 1 A LYS 224 ? CE  ? E LYS 216 CE  
377 1 Y 1 A LYS 224 ? NZ  ? E LYS 216 NZ  
378 1 Y 1 A LYS 225 ? CG  ? E LYS 217 CG  
379 1 Y 1 A LYS 225 ? CD  ? E LYS 217 CD  
380 1 Y 1 A LYS 225 ? CE  ? E LYS 217 CE  
381 1 Y 1 A LYS 225 ? NZ  ? E LYS 217 NZ  
382 1 Y 1 A LYS 229 ? CG  ? E LYS 221 CG  
383 1 Y 1 A LYS 229 ? CD  ? E LYS 221 CD  
384 1 Y 1 A LYS 229 ? CE  ? E LYS 221 CE  
385 1 Y 1 A LYS 229 ? NZ  ? E LYS 221 NZ  
386 1 Y 1 B ARG 18  ? CG  ? F ARG 18  CG  
387 1 Y 1 B ARG 18  ? CD  ? F ARG 18  CD  
388 1 Y 1 B ARG 18  ? NE  ? F ARG 18  NE  
389 1 Y 1 B ARG 18  ? CZ  ? F ARG 18  CZ  
390 1 Y 1 B ARG 18  ? NH1 ? F ARG 18  NH1 
391 1 Y 1 B ARG 18  ? NH2 ? F ARG 18  NH2 
392 1 Y 1 B LYS 45  ? CG  ? F LYS 39  CG  
393 1 Y 1 B LYS 45  ? CD  ? F LYS 39  CD  
394 1 Y 1 B LYS 45  ? CE  ? F LYS 39  CE  
395 1 Y 1 B LYS 45  ? NZ  ? F LYS 39  NZ  
396 1 Y 1 B LYS 48  ? CG  ? F LYS 42  CG  
397 1 Y 1 B LYS 48  ? CD  ? F LYS 42  CD  
398 1 Y 1 B LYS 48  ? CE  ? F LYS 42  CE  
399 1 Y 1 B LYS 48  ? NZ  ? F LYS 42  NZ  
400 1 Y 1 B LYS 51  ? CG  ? F LYS 45  CG  
401 1 Y 1 B LYS 51  ? CD  ? F LYS 45  CD  
402 1 Y 1 B LYS 51  ? CE  ? F LYS 45  CE  
403 1 Y 1 B LYS 51  ? NZ  ? F LYS 45  NZ  
404 1 Y 1 B LEU 52  ? CG  ? F LEU 46  CG  
405 1 Y 1 B LEU 52  ? CD1 ? F LEU 46  CD1 
406 1 Y 1 B LEU 52  ? CD2 ? F LEU 46  CD2 
407 1 Y 1 B LEU 53  ? CG  ? F LEU 47  CG  
408 1 Y 1 B LEU 53  ? CD1 ? F LEU 47  CD1 
409 1 Y 1 B LEU 53  ? CD2 ? F LEU 47  CD2 
410 1 Y 1 B GLN 106 ? CG  ? F GLN 90  CG  
411 1 Y 1 B GLN 106 ? CD  ? F GLN 90  CD  
412 1 Y 1 B GLN 106 ? OE1 ? F GLN 90  OE1 
413 1 Y 1 B GLN 106 ? NE2 ? F GLN 90  NE2 
414 1 Y 1 B LYS 123 ? CG  ? F LYS 103 CG  
415 1 Y 1 B LYS 123 ? CD  ? F LYS 103 CD  
416 1 Y 1 B LYS 123 ? CE  ? F LYS 103 CE  
417 1 Y 1 B LYS 123 ? NZ  ? F LYS 103 NZ  
418 1 Y 1 B GLU 125 ? CG  ? F GLU 105 CG  
419 1 Y 1 B GLU 125 ? CD  ? F GLU 105 CD  
420 1 Y 1 B GLU 125 ? OE1 ? F GLU 105 OE1 
421 1 Y 1 B GLU 125 ? OE2 ? F GLU 105 OE2 
422 1 Y 1 B LYS 127 ? CE  ? F LYS 107 CE  
423 1 Y 1 B LYS 127 ? NZ  ? F LYS 107 NZ  
424 1 Y 1 B ARG 128 ? CG  ? F ARG 108 CG  
425 1 Y 1 B ARG 128 ? CD  ? F ARG 108 CD  
426 1 Y 1 B ARG 128 ? NE  ? F ARG 108 NE  
427 1 Y 1 B ARG 128 ? CZ  ? F ARG 108 CZ  
428 1 Y 1 B ARG 128 ? NH1 ? F ARG 108 NH1 
429 1 Y 1 B ARG 128 ? NH2 ? F ARG 108 NH2 
430 1 Y 1 B LYS 146 ? CE  ? F LYS 126 CE  
431 1 Y 1 B LYS 146 ? NZ  ? F LYS 126 NZ  
432 1 Y 1 B TYR 160 ? CG  ? F TYR 140 CG  
433 1 Y 1 B TYR 160 ? CD1 ? F TYR 140 CD1 
434 1 Y 1 B TYR 160 ? CD2 ? F TYR 140 CD2 
435 1 Y 1 B TYR 160 ? CE1 ? F TYR 140 CE1 
436 1 Y 1 B TYR 160 ? CE2 ? F TYR 140 CE2 
437 1 Y 1 B TYR 160 ? CZ  ? F TYR 140 CZ  
438 1 Y 1 B TYR 160 ? OH  ? F TYR 140 OH  
439 1 Y 1 B ARG 162 ? CG  ? F ARG 142 CG  
440 1 Y 1 B ARG 162 ? CD  ? F ARG 142 CD  
441 1 Y 1 B ARG 162 ? NE  ? F ARG 142 NE  
442 1 Y 1 B ARG 162 ? CZ  ? F ARG 142 CZ  
443 1 Y 1 B ARG 162 ? NH1 ? F ARG 142 NH1 
444 1 Y 1 B ARG 162 ? NH2 ? F ARG 142 NH2 
445 1 Y 1 B LYS 165 ? CG  ? F LYS 145 CG  
446 1 Y 1 B LYS 165 ? CD  ? F LYS 145 CD  
447 1 Y 1 B LYS 165 ? CE  ? F LYS 145 CE  
448 1 Y 1 B LYS 165 ? NZ  ? F LYS 145 NZ  
449 1 Y 1 B LEU 174 ? CG  ? F LEU 154 CG  
450 1 Y 1 B LEU 174 ? CD1 ? F LEU 154 CD1 
451 1 Y 1 B LEU 174 ? CD2 ? F LEU 154 CD2 
452 1 Y 1 B GLN 180 ? CG  ? F GLN 160 CG  
453 1 Y 1 B GLN 180 ? CD  ? F GLN 160 CD  
454 1 Y 1 B GLN 180 ? OE1 ? F GLN 160 OE1 
455 1 Y 1 B GLN 180 ? NE2 ? F GLN 160 NE2 
456 1 Y 1 B GLU 185 ? CG  ? F GLU 165 CG  
457 1 Y 1 B GLU 185 ? CD  ? F GLU 165 CD  
458 1 Y 1 B GLU 185 ? OE1 ? F GLU 165 OE1 
459 1 Y 1 B GLU 185 ? OE2 ? F GLU 165 OE2 
460 1 Y 1 B LYS 189 ? CG  ? F LYS 169 CG  
461 1 Y 1 B LYS 189 ? CD  ? F LYS 169 CD  
462 1 Y 1 B LYS 189 ? CE  ? F LYS 169 CE  
463 1 Y 1 B LYS 189 ? NZ  ? F LYS 169 NZ  
464 1 Y 1 B LYS 203 ? CG  ? F LYS 183 CG  
465 1 Y 1 B LYS 203 ? CD  ? F LYS 183 CD  
466 1 Y 1 B LYS 203 ? CE  ? F LYS 183 CE  
467 1 Y 1 B LYS 203 ? NZ  ? F LYS 183 NZ  
468 1 Y 1 B LYS 208 ? CG  ? F LYS 188 CG  
469 1 Y 1 B LYS 208 ? CD  ? F LYS 188 CD  
470 1 Y 1 B LYS 208 ? CE  ? F LYS 188 CE  
471 1 Y 1 B LYS 208 ? NZ  ? F LYS 188 NZ  
472 1 Y 1 B LYS 210 ? CG  ? F LYS 190 CG  
473 1 Y 1 B LYS 210 ? CD  ? F LYS 190 CD  
474 1 Y 1 B LYS 210 ? CE  ? F LYS 190 CE  
475 1 Y 1 B LYS 210 ? NZ  ? F LYS 190 NZ  
476 1 Y 1 B GLU 233 ? CG  ? F GLU 211 CG  
477 1 Y 1 B GLU 233 ? CD  ? F GLU 211 CD  
478 1 Y 1 B GLU 233 ? OE1 ? F GLU 211 OE1 
479 1 Y 1 B GLU 233 ? OE2 ? F GLU 211 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM  ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8UWZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     167.747 
_cell.length_a_esd                 ? 
_cell.length_b                     167.747 
_cell.length_b_esd                 ? 
_cell.length_c                     42.501 
_cell.length_c_esd                 ? 
_cell.volume                       1035710.269 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         8UWZ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                144 
_symmetry.space_group_name_Hall            'P 31' 
_symmetry.space_group_name_H-M             'P 31' 
_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                   8UWZ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.98 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.77 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.1 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    'room temperature' 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M Sodium Phosphate mono basic, 30% PEG600' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      mirrors 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-02-07 
_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   0.97915 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 24-ID-E' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97915 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-E 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          133.58 
_reflns.entry_id                                       8UWZ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.40 
_reflns.d_resolution_low                               83.87 
_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                                     18391 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.130 
_reflns.pdbx_Rpim_I_all                                0.046 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.122 
_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                                    3.40 
_reflns_shell.d_res_low                                     3.67 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3833 
_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                               7.8 
_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                               1.297 
_reflns_shell.pdbx_Rpim_I_all                               0.458 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.769 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.212 
_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                               167.82 
_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                                 8UWZ 
_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                            3.50 
_refine.ls_d_res_low                             83.87 
_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                     16810 
_refine.ls_number_reflns_R_free                  1696 
_refine.ls_number_reflns_R_work                  15114 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.63 
_refine.ls_percent_reflns_R_free                 10.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2433 
_refine.ls_R_factor_R_free                       0.2981 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2370 
_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                          1.96 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 39.9167 
_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                            0.5771 
_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                       3.50 
_refine_hist.d_res_low                        83.87 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               7733 
_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        7666 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         67 
_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' ? 0.0048  ? 7933  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9477  ? 10872 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0552  ? 1247  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0184  ? 1394  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 17.4559 ? 2639  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.ncs_model_details 
1 'X-RAY DIFFRACTION' d_2 ens_1 0.984107314105 ? ? ? 'Torsion NCS' E A ? ? ? ? 
2 'X-RAY DIFFRACTION' d_2 ens_2 1.30684378744  ? ? ? 'Torsion NCS' F B ? ? ? ? 
3 'X-RAY DIFFRACTION' d_2 ens_3 1.39378384007  ? ? ? 'Torsion NCS' C E ? ? ? ? 
# 
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' 3.50 3.60  . . 138 1254 99.57  . . . . 0.4087 . . . . . . . . . . . 0.3935 
'X-RAY DIFFRACTION' 3.60 3.72  . . 137 1255 99.57  . . . . 0.3891 . . . . . . . . . . . 0.3902 
'X-RAY DIFFRACTION' 3.72 3.85  . . 148 1296 99.52  . . . . 0.3396 . . . . . . . . . . . 0.3353 
'X-RAY DIFFRACTION' 3.85 4.01  . . 139 1218 99.49  . . . . 0.3552 . . . . . . . . . . . 0.3520 
'X-RAY DIFFRACTION' 4.01 4.19  . . 142 1288 99.17  . . . . 0.3263 . . . . . . . . . . . 0.3721 
'X-RAY DIFFRACTION' 4.19 4.41  . . 138 1230 99.78  . . . . 0.2522 . . . . . . . . . . . 0.2808 
'X-RAY DIFFRACTION' 4.41 4.68  . . 148 1293 100.00 . . . . 0.2397 . . . . . . . . . . . 0.3001 
'X-RAY DIFFRACTION' 4.69 5.05  . . 140 1237 99.85  . . . . 0.2340 . . . . . . . . . . . 0.2686 
'X-RAY DIFFRACTION' 5.05 5.55  . . 142 1260 99.79  . . . . 0.2316 . . . . . . . . . . . 0.2970 
'X-RAY DIFFRACTION' 5.56 6.36  . . 142 1256 99.57  . . . . 0.2383 . . . . . . . . . . . 0.3131 
'X-RAY DIFFRACTION' 6.36 8.01  . . 146 1257 99.93  . . . . 0.2168 . . . . . . . . . . . 0.3087 
'X-RAY DIFFRACTION' 8.02 83.87 . . 136 1270 99.79  . . . . 0.1489 . . . . . . . . . . . 0.2462 
# 
loop_
_struct_ncs_oper.id 
_struct_ncs_oper.code 
_struct_ncs_oper.matrix[1][1] 
_struct_ncs_oper.matrix[1][2] 
_struct_ncs_oper.matrix[1][3] 
_struct_ncs_oper.matrix[2][1] 
_struct_ncs_oper.matrix[2][2] 
_struct_ncs_oper.matrix[2][3] 
_struct_ncs_oper.matrix[3][1] 
_struct_ncs_oper.matrix[3][2] 
_struct_ncs_oper.matrix[3][3] 
_struct_ncs_oper.vector[1] 
_struct_ncs_oper.vector[2] 
_struct_ncs_oper.vector[3] 
_struct_ncs_oper.details 
1 given -0.954351434718 0.298573908064 0.00818293805804 0.298450590061 0.954328804419 -0.0135564873175 -0.0118568268916  
-0.0104954504293 -0.999874622728 11.5547041973 -2.37546391928 -45.1042859781 ? 
2 given -0.960848978196 0.276761112001 0.0131349908302  0.276936042182 0.960783901768 0.0141676619053  -0.00869882987619 
0.0172505358398  -0.999813357268 12.7457837286 -2.18057876966 -46.5452627584 ? 
3 given -0.964034585558 0.265517542993 0.0117367887998  0.265579982151 0.964080118588 0.00409853925459 -0.0102269706652  
0.00706818975165 -0.999922721896 12.9833088055 -1.74865459687 -45.9210972023 ? 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
ens_1 d_1 
;(chain "A" and (resid 1 through 2 or (resid 3 and (name N or name CA or name C or name O or name CB )) or resid 4 through 13 or (resid 14 and (name N or name CA or name C or name O or name CB )) or resid 15 through 47 or (resid 48 and (name N or name CA or name C or name O or name CB )) or resid 49 through 94 or (resid 95 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 96 through 142 or resid 144 through 147 or resid 150 through 151 or resid 153 through 157 or (resid 158 and (name N or name CA or name C or name O or name CB )) or resid 159 through 180 or (resid 181 and (name N or name CA or name C or name O or name CB )) or resid 182 through 184 or (resid 185 through 186 and (name N or name CA or name C or name O or name CB )) or resid 187 through 189 or (resid 190 through 191 and (name N or name CA or name C or name O or name CB )) or resid 192 through 220 or (resid 221 and (name N or name CA or name C or name O or name CB or name CG )) or resid 222 through 228))
;
ens_1 d_2 
;(chain "C" and (resid 1 through 206 or (resid 207 and (name N or name CA or name C or name O or name CB )) or resid 208 through 223 or (resid 224 through 225 and (name N or name CA or name C or name O or name CB )) or resid 226 through 228))
;
ens_2 d_1 
;(chain "B" and (resid 5 or (resid 6 and (name N or name CA or name C or name O or name CB )) or resid 7 through 10 or (resid 11 and (name N or name CA or name C or name O or name CB )) or resid 12 through 26 or resid 28 through 37 or (resid 38 and (name N or name CA or name C or name O or name CB )) or resid 39 through 106 or (resid 107 and (name N or name CA or name C or name O or name CB )) or resid 108 through 119 or (resid 120 and (name N or name CA or name C or name O or name CB )) or resid 121 through 125 or (resid 126 through 128 and (name N or name CA or name C or name O or name CB )) or resid 129 or resid 132 through 136 or (resid 137 and (name N or name CA or name C or name O or name CB )) or resid 138 through 145 or (resid 146 and (name N or name CA or name C or name O or name CB )) or resid 147 through 155 or (resid 156 and (name N or name CA or name C or name O or name CB )) or resid 157 through 158 or (resid 159 through 160 and (name N or name CA or name C or name O or name CB )) or resid 161 through 162 or (resid 163 through 165 and (name N or name CA or name C or name O or name CB )) or resid 166 through 180 or (resid 181 and (name N or name CA or name C or name O or name CB )) or resid 182 through 194 or (resid 195 and (name N or name CA or name C or name O or name CB )) or resid 196 through 226 or (resid 227 and (name N or name CA or name C or name O or name CB )) or resid 228 or (resid 229 and (name N or name CA or name C or name O or name CB )) or resid 230 through 234))
;
ens_2 d_2 
;(chain "D" and (resid 5 through 17 or (resid 18 and (name N or name CA or name C or name O or name CB )) or resid 19 through 47 or (resid 48 through 49 and (name N or name CA or name C or name O or name CB )) or resid 50 through 51 or (resid 52 through 53 and (name N or name CA or name C or name O or name CB )) or resid 54 through 124 or (resid 125 through 128 and (name N or name CA or name C or name O or name CB )) or resid 129 through 173 or (resid 174 and (name N or name CA or name C or name O or name CB )) or resid 175 through 234))
;
ens_3 d_1 
;(chain "E" and ((resid 11 and (name N or name CA or name C or name O or name CB )) or resid 12 through 35 or (resid 36 through 37 and (name N or name CA or name C or name O or name CB )) or resid 38 through 89 or (resid 90 and (name N or name CA or name C or name O or name CB )) or resid 91 through 100 or (resid 101 and (name N or name CA or name C or name O or name CB )) or resid 102 through 106 or (resid 107 through 108 and (name N or name CA or name C or name O or name CB )) or resid 109))
;
ens_3 d_2 
;(chain "F" and (resid 11 through 55 or (resid 56 and (name N or name CA or name C or name O or name CB )) or resid 57 through 63 or (resid 64 and (name N or name CA or name C or name O or name CB )) or resid 65 through 72 or (resid 73 and (name N or name CA or name C or name O or name CB )) or resid 74 through 83 or (resid 84 and (name N or name CA or name C or name O or name CB )) or resid 85 through 86 or (resid 87 and (name N or name CA or name C or name O or name CB )) or resid 88 through 108 or resid 111))
;
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
ens_1 d_1 1 E GLU 1   . E SER 134 . A GLU 1   A SER 142 ? ? 
ens_1 d_1 2 E LYS 136 . E SER 139 . A LYS 144 A SER 147 ? ? 
ens_1 d_1 3 E THR 142 . E ALA 143 . A THR 150 A ALA 151 ? ? 
ens_1 d_1 4 E LEU 145 . E PRO 220 . A LEU 153 A PRO 228 ? ? 
ens_1 d_2 1 A GLU 1   . A PRO 220 . C GLU 1   C PRO 228 ? ? 
ens_2 d_1 1 F THR 5   . F SER 26  . B THR 5   B SER 26  ? ? 
ens_2 d_1 2 F ALA 28  . F THR 109 . B ALA 28  B THR 129 ? ? 
ens_2 d_1 3 F ALA 112 . F CYS 212 . B ALA 132 B CYS 234 ? ? 
ens_2 d_2 1 B THR 5   . B CYS 212 . D THR 5   D CYS 234 ? ? 
ens_3 d_1 1 C HIS 11  . C LYS 108 . E HIS 11  E LYS 108 ? ? 
ens_3 d_1 2 G NAG .   . G NAG .   . G NAG 1   G NAG 1   ? ? 
ens_3 d_2 1 D HIS 11  . D LYS 108 . F HIS 11  F LYS 108 ? ? 
ens_3 d_2 2 H NAG .   . H NAG .   . H NAG 2   H NAG 2   ? ? 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
ens_1 ? 
ens_2 ? 
ens_3 ? 
# 
loop_
_struct_ncs_ens_gen.ens_id 
_struct_ncs_ens_gen.dom_id_1 
_struct_ncs_ens_gen.dom_id_2 
_struct_ncs_ens_gen.oper_id 
ens_1 d_2 d_1 1 
ens_2 d_2 d_1 2 
ens_3 d_2 d_1 3 
# 
_struct.entry_id                     8UWZ 
_struct.title                        'The structure of Raamsizumab in complex with VEGF121' 
_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        8UWZ 
_struct_keywords.text            'SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 1 ? 
F N N 2 ? 
G N N 4 ? 
H N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 8UWZ        8UWZ   ?        1 ? 1  
2 PDB 8UWZ        8UWZ   ?        2 ? 1  
3 UNP VEGFA_HUMAN P15692 P15692-9 3 
;APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQI
MRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKCDKPRR
;
27 
# 
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 8UWZ C 1 ? 228 ? 8UWZ   1  ? 236 ? 1 236 
2 2 8UWZ D 1 ? 212 ? 8UWZ   1  ? 234 ? 1 234 
3 3 8UWZ E 1 ? 121 ? P15692 27 ? 147 ? 1 121 
4 3 8UWZ F 1 ? 121 ? P15692 27 ? 147 ? 1 121 
5 1 8UWZ A 1 ? 228 ? 8UWZ   1  ? 236 ? 1 236 
6 2 8UWZ B 1 ? 212 ? 8UWZ   1  ? 234 ? 1 234 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
3 8UWZ ASN E 115 ? UNP P15692 LYS 141 conflict 115 1 
4 8UWZ ASN F 115 ? UNP P15692 LYS 141 conflict 115 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 PRO A 53  ? GLY A 56  ? PRO C 58  GLY C 63  5 ? 4 
HELX_P HELX_P2  AA2 ARG A 87  ? THR A 91  ? ARG C 95  THR C 99  5 ? 5 
HELX_P HELX_P3  AA3 ALA A 100 ? GLY A 104 ? ALA C 108 GLY C 112 5 ? 5 
HELX_P HELX_P4  AA4 GLN B 79  ? PHE B 83  ? GLN D 95  PHE D 99  5 ? 5 
HELX_P HELX_P5  AA5 SER B 121 ? GLY B 128 ? SER D 141 GLY D 148 1 ? 8 
HELX_P HELX_P6  AA6 LYS C 16  ? SER C 24  ? LYS E 16  SER E 24  1 ? 9 
HELX_P HELX_P7  AA7 ILE C 35  ? TYR C 39  ? ILE E 35  TYR E 39  1 ? 5 
HELX_P HELX_P8  AA8 LYS D 16  ? SER D 24  ? LYS F 16  SER F 24  1 ? 9 
HELX_P HELX_P9  AA9 ILE D 35  ? TYR D 39  ? ILE F 35  TYR F 39  1 ? 5 
HELX_P HELX_P10 AB1 PRO E 53  ? GLY E 56  ? PRO A 58  GLY A 63  5 ? 4 
HELX_P HELX_P11 AB2 ARG E 87  ? THR E 91  ? ARG A 95  THR A 99  5 ? 5 
HELX_P HELX_P12 AB3 TRP E 101 ? GLY E 104 ? TRP A 109 GLY A 112 5 ? 4 
HELX_P HELX_P13 AB4 GLN F 79  ? PHE F 83  ? GLN B 95  PHE B 99  5 ? 5 
HELX_P HELX_P14 AB5 SER F 121 ? SER F 127 ? SER B 141 SER B 147 1 ? 7 
HELX_P HELX_P15 AB6 LYS F 183 ? LYS F 188 ? LYS B 203 LYS B 208 1 ? 6 
# 
_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 22  SG  ? ? ? 1_555 A CYS 96  SG ? ? C CYS 23  C CYS 104 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf2  disulf ?    ? A CYS 147 SG  ? ? ? 1_555 A CYS 203 SG ? ? C CYS 155 C CYS 211 1_555 ? ? ? ? ? ? ? 2.025 ? ?               
disulf3  disulf ?    ? B CYS 23  SG  ? ? ? 1_555 B CYS 88  SG ? ? D CYS 23  D CYS 104 1_555 ? ? ? ? ? ? ? 2.033 ? ?               
disulf4  disulf ?    ? B CYS 134 SG  ? ? ? 1_555 B CYS 194 SG ? ? D CYS 154 D CYS 214 1_555 ? ? ? ? ? ? ? 2.039 ? ?               
disulf5  disulf ?    ? C CYS 26  SG  ? ? ? 1_555 C CYS 68  SG ? ? E CYS 26  E CYS 68  1_555 ? ? ? ? ? ? ? 2.021 ? ?               
disulf6  disulf ?    ? C CYS 51  SG  ? ? ? 1_555 D CYS 60  SG ? ? E CYS 51  F CYS 60  1_555 ? ? ? ? ? ? ? 2.019 ? ?               
disulf7  disulf ?    ? C CYS 57  SG  ? ? ? 1_555 C CYS 102 SG ? ? E CYS 57  E CYS 102 1_555 ? ? ? ? ? ? ? 2.040 ? ?               
disulf8  disulf ?    ? C CYS 60  SG  ? ? ? 1_555 D CYS 51  SG ? ? E CYS 60  F CYS 51  1_555 ? ? ? ? ? ? ? 2.028 ? ?               
disulf9  disulf ?    ? C CYS 61  SG  ? ? ? 1_555 C CYS 104 SG ? ? E CYS 61  E CYS 104 1_555 ? ? ? ? ? ? ? 2.020 ? ?               
disulf10 disulf ?    ? D CYS 26  SG  ? ? ? 1_555 D CYS 68  SG ? ? F CYS 26  F CYS 68  1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf11 disulf ?    ? D CYS 57  SG  ? ? ? 1_555 D CYS 102 SG ? ? F CYS 57  F CYS 102 1_555 ? ? ? ? ? ? ? 2.036 ? ?               
disulf12 disulf ?    ? D CYS 61  SG  ? ? ? 1_555 D CYS 104 SG ? ? F CYS 61  F CYS 104 1_555 ? ? ? ? ? ? ? 2.025 ? ?               
disulf13 disulf ?    ? E CYS 22  SG  ? ? ? 1_555 E CYS 96  SG ? ? A CYS 23  A CYS 104 1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf14 disulf ?    ? E CYS 147 SG  ? ? ? 1_555 E CYS 203 SG ? ? A CYS 155 A CYS 211 1_555 ? ? ? ? ? ? ? 2.033 ? ?               
disulf15 disulf ?    ? F CYS 23  SG  ? ? ? 1_555 F CYS 88  SG ? ? B CYS 23  B CYS 104 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf16 disulf ?    ? F CYS 134 SG  ? ? ? 1_555 F CYS 194 SG ? ? B CYS 154 B CYS 214 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
covale1  covale one  ? C ASN 75  ND2 ? ? ? 1_555 G NAG .   C1 ? ? E ASN 75  G NAG 1   1_555 ? ? ? ? ? ? ? 1.453 ? N-Glycosylation 
covale2  covale one  ? D ASN 75  ND2 ? ? ? 1_555 H NAG .   C1 ? ? F ASN 75  H NAG 1   1_555 ? ? ? ? ? ? ? 1.438 ? N-Glycosylation 
covale3  covale both ? G NAG .   O4  ? ? ? 1_555 G NAG .   C1 ? ? G NAG 1   G NAG 2   1_555 ? ? ? ? ? ? ? 1.448 ? ?               
covale4  covale both ? H NAG .   O4  ? ? ? 1_555 H NAG .   C1 ? ? H NAG 1   H NAG 2   1_555 ? ? ? ? ? ? ? 1.460 ? ?               
covale5  covale both ? H NAG .   O4  ? ? ? 1_555 H BMA .   C1 ? ? H NAG 2   H BMA 3   1_555 ? ? ? ? ? ? ? 1.458 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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  NAG G .   ? ASN C 75  ? NAG G 1   ? 1_555 ASN E 75  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG H .   ? ASN D 75  ? NAG H 1   ? 1_555 ASN F 75  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  CYS A 22  ? CYS A 96  ? CYS C 23  ? 1_555 CYS C 104 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
4  CYS A 147 ? CYS A 203 ? CYS C 155 ? 1_555 CYS C 211 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
5  CYS B 23  ? CYS B 88  ? CYS D 23  ? 1_555 CYS D 104 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
6  CYS B 134 ? CYS B 194 ? CYS D 154 ? 1_555 CYS D 214 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7  CYS C 26  ? CYS C 68  ? CYS E 26  ? 1_555 CYS E 68  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8  CYS C 51  ? CYS D 60  ? CYS E 51  ? 1_555 CYS F 60  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9  CYS C 57  ? CYS C 102 ? CYS E 57  ? 1_555 CYS E 102 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
10 CYS C 60  ? CYS D 51  ? CYS E 60  ? 1_555 CYS F 51  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
11 CYS C 61  ? CYS C 104 ? CYS E 61  ? 1_555 CYS E 104 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
12 CYS D 26  ? CYS D 68  ? CYS F 26  ? 1_555 CYS F 68  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
13 CYS D 57  ? CYS D 102 ? CYS F 57  ? 1_555 CYS F 102 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
14 CYS D 61  ? CYS D 104 ? CYS F 61  ? 1_555 CYS F 104 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
15 CYS E 22  ? CYS E 96  ? CYS A 23  ? 1_555 CYS A 104 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
16 CYS E 147 ? CYS E 203 ? CYS A 155 ? 1_555 CYS A 211 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
17 CYS F 23  ? CYS F 88  ? CYS B 23  ? 1_555 CYS B 104 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
18 CYS F 134 ? CYS F 194 ? CYS B 154 ? 1_555 CYS B 214 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  PHE 153 A . ? PHE 161 C PRO 154 A ? PRO 162 C 1 -4.63 
2  GLU 155 A . ? GLU 163 C PRO 156 A ? PRO 164 C 1 2.60  
3  SER 7   B . ? SER 7   D PRO 8   B ? PRO 8   D 1 9.40  
4  TYR 140 B . ? TYR 160 D PRO 141 B ? PRO 161 D 1 -2.76 
5  LYS 48  C . ? LYS 48  E PRO 49  C ? PRO 49  E 1 0.01  
6  LYS 48  D . ? LYS 48  F PRO 49  D ? PRO 49  F 1 -3.36 
7  PHE 153 E . ? PHE 161 A PRO 154 E ? PRO 162 A 1 -6.20 
8  GLU 155 E . ? GLU 163 A PRO 156 E ? PRO 164 A 1 2.97  
9  SER 7   F . ? SER 7   B PRO 8   F ? PRO 8   B 1 6.76  
10 TYR 140 F . ? TYR 160 B PRO 141 F ? PRO 161 B 1 -0.76 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 3 ? 
AA6 ? 4 ? 
AA7 ? 6 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 3 ? 
AB2 ? 3 ? 
AB3 ? 2 ? 
AB4 ? 3 ? 
AB5 ? 3 ? 
AB6 ? 2 ? 
AB7 ? 4 ? 
AB8 ? 6 ? 
AB9 ? 4 ? 
AC1 ? 4 ? 
AC2 ? 4 ? 
AC3 ? 3 ? 
AC4 ? 4 ? 
AC5 ? 6 ? 
AC6 ? 4 ? 
AC7 ? 3 ? 
# 
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 ? anti-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 
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 ? anti-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 ? parallel      
AB1 2 3 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? parallel      
AB6 1 2 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? parallel      
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB8 4 5 ? anti-parallel 
AB8 5 6 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AC1 1 2 ? anti-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 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC5 1 2 ? parallel      
AC5 2 3 ? anti-parallel 
AC5 3 4 ? anti-parallel 
AC5 4 5 ? anti-parallel 
AC5 5 6 ? 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 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLN A 3   ? SER A 7   ? GLN C 3   SER C 7   
AA1 2 LEU A 18  ? SER A 25  ? LEU C 19  SER C 26  
AA1 3 THR A 78  ? MET A 83  ? THR C 86  MET C 91  
AA1 4 PHE A 68  ? ASP A 73  ? PHE C 76  ASP C 81  
AA2 1 GLY A 10  ? VAL A 12  ? GLY C 11  VAL C 13  
AA2 2 THR A 114 ? VAL A 118 ? THR C 122 VAL C 126 
AA2 3 ALA A 92  ? ARG A 98  ? ALA C 100 ARG C 106 
AA2 4 ILE A 34  ? GLN A 39  ? ILE C 39  GLN C 44  
AA2 5 LEU A 45  ? ILE A 51  ? LEU C 50  ILE C 56  
AA2 6 THR A 58  ? TYR A 60  ? THR C 65  TYR C 67  
AA3 1 SER A 127 ? LEU A 131 ? SER C 135 LEU C 139 
AA3 2 GLY A 146 ? TYR A 152 ? GLY C 154 TYR C 160 
AA3 3 TYR A 183 ? VAL A 191 ? TYR C 191 VAL C 199 
AA3 4 ALA A 143 ? ALA A 143 ? ALA C 151 ALA C 151 
AA4 1 SER A 127 ? LEU A 131 ? SER C 135 LEU C 139 
AA4 2 GLY A 146 ? TYR A 152 ? GLY C 154 TYR C 160 
AA4 3 TYR A 183 ? VAL A 191 ? TYR C 191 VAL C 199 
AA4 4 VAL A 176 ? LEU A 177 ? VAL C 184 LEU C 185 
AA5 1 THR A 158 ? TRP A 161 ? THR C 166 TRP C 169 
AA5 2 ILE A 202 ? HIS A 207 ? ILE C 210 HIS C 215 
AA5 3 THR A 212 ? LYS A 217 ? THR C 220 LYS C 225 
AA6 1 GLN B 6   ? SER B 7   ? GLN D 6   SER D 7   
AA6 2 VAL B 19  ? ARG B 24  ? VAL D 19  ARG D 24  
AA6 3 ASP B 70  ? ILE B 75  ? ASP D 86  ILE D 91  
AA6 4 PHE B 62  ? ARG B 66  ? PHE D 76  ARG D 80  
AA7 1 SER B 10  ? ALA B 13  ? SER D 10  ALA D 13  
AA7 2 THR B 102 ? ILE B 106 ? THR D 122 ILE D 126 
AA7 3 THR B 85  ? GLN B 89  ? THR D 101 GLN D 105 
AA7 4 ALA B 34  ? GLN B 38  ? ALA D 40  GLN D 44  
AA7 5 LYS B 45  ? TYR B 49  ? LYS D 51  TYR D 55  
AA7 6 GLU B 53  ? LEU B 54  ? GLU D 66  LEU D 67  
AA8 1 VAL B 115 ? PHE B 118 ? VAL D 135 PHE D 138 
AA8 2 THR B 129 ? PHE B 139 ? THR D 149 PHE D 159 
AA8 3 TYR B 173 ? SER B 182 ? TYR D 193 SER D 202 
AA8 4 SER B 159 ? VAL B 163 ? SER D 179 VAL D 183 
AA9 1 LEU B 154 ? GLN B 155 ? LEU D 174 GLN D 175 
AA9 2 VAL B 146 ? VAL B 150 ? VAL D 166 VAL D 170 
AA9 3 VAL B 191 ? VAL B 196 ? VAL D 211 VAL D 216 
AA9 4 THR B 204 ? ASN B 208 ? THR D 226 ASN D 230 
AB1 1 VAL C 14  ? VAL C 15  ? VAL E 14  VAL E 15  
AB1 2 LEU D 66  ? LYS D 84  ? LEU F 66  LYS F 84  
AB1 3 ILE D 46  ? LYS D 48  ? ILE F 46  LYS F 48  
AB2 1 VAL C 14  ? VAL C 15  ? VAL E 14  VAL E 15  
AB2 2 LEU D 66  ? LYS D 84  ? LEU F 66  LYS F 84  
AB2 3 GLY D 88  ? PRO D 106 ? GLY F 88  PRO F 106 
AB3 1 ILE C 29  ? ASP C 34  ? ILE E 29  ASP E 34  
AB3 2 CYS C 51  ? ARG C 56  ? CYS E 51  ARG E 56  
AB4 1 ILE C 46  ? LYS C 48  ? ILE E 46  LYS E 48  
AB4 2 LEU C 66  ? ILE C 83  ? LEU E 66  ILE E 83  
AB4 3 ILE C 91  ? PRO C 106 ? ILE E 91  PRO E 106 
AB5 1 ILE C 46  ? LYS C 48  ? ILE E 46  LYS E 48  
AB5 2 LEU C 66  ? ILE C 83  ? LEU E 66  ILE E 83  
AB5 3 VAL D 14  ? VAL D 15  ? VAL F 14  VAL F 15  
AB6 1 ILE D 29  ? ASP D 34  ? ILE F 29  ASP F 34  
AB6 2 CYS D 51  ? ARG D 56  ? CYS F 51  ARG F 56  
AB7 1 GLN E 3   ? SER E 7   ? GLN A 3   SER A 7   
AB7 2 LEU E 18  ? SER E 25  ? LEU A 19  SER A 26  
AB7 3 THR E 78  ? MET E 83  ? THR A 86  MET A 91  
AB7 4 PHE E 68  ? ASP E 73  ? PHE A 76  ASP A 81  
AB8 1 GLY E 10  ? VAL E 12  ? GLY A 11  VAL A 13  
AB8 2 THR E 114 ? VAL E 118 ? THR A 122 VAL A 126 
AB8 3 ALA E 92  ? HIS E 99  ? ALA A 100 HIS A 107 
AB8 4 ILE E 34  ? GLN E 39  ? ILE A 39  GLN A 44  
AB8 5 LEU E 45  ? ILE E 51  ? LEU A 50  ILE A 56  
AB8 6 THR E 58  ? TYR E 60  ? THR A 65  TYR A 67  
AB9 1 GLY E 10  ? VAL E 12  ? GLY A 11  VAL A 13  
AB9 2 THR E 114 ? VAL E 118 ? THR A 122 VAL A 126 
AB9 3 ALA E 92  ? HIS E 99  ? ALA A 100 HIS A 107 
AB9 4 LEU E 107 ? TRP E 110 ? LEU A 115 TRP A 118 
AC1 1 SER E 127 ? LEU E 131 ? SER A 135 LEU A 139 
AC1 2 THR E 142 ? TYR E 152 ? THR A 150 TYR A 160 
AC1 3 TYR E 183 ? PRO E 192 ? TYR A 191 PRO A 200 
AC1 4 VAL E 170 ? THR E 172 ? VAL A 178 THR A 180 
AC2 1 SER E 127 ? LEU E 131 ? SER A 135 LEU A 139 
AC2 2 THR E 142 ? TYR E 152 ? THR A 150 TYR A 160 
AC2 3 TYR E 183 ? PRO E 192 ? TYR A 191 PRO A 200 
AC2 4 VAL E 176 ? LEU E 177 ? VAL A 184 LEU A 185 
AC3 1 THR E 158 ? TRP E 161 ? THR A 166 TRP A 169 
AC3 2 ILE E 202 ? HIS E 207 ? ILE A 210 HIS A 215 
AC3 3 THR E 212 ? LYS E 217 ? THR A 220 LYS A 225 
AC4 1 GLN F 6   ? SER F 7   ? GLN B 6   SER B 7   
AC4 2 VAL F 19  ? ARG F 24  ? VAL B 19  ARG B 24  
AC4 3 ASP F 70  ? ILE F 75  ? ASP B 86  ILE B 91  
AC4 4 PHE F 62  ? ARG F 66  ? PHE B 76  ARG B 80  
AC5 1 SER F 10  ? ALA F 13  ? SER B 10  ALA B 13  
AC5 2 THR F 102 ? ILE F 106 ? THR B 122 ILE B 126 
AC5 3 ALA F 84  ? GLN F 89  ? ALA B 100 GLN B 105 
AC5 4 ALA F 34  ? GLN F 38  ? ALA B 40  GLN B 44  
AC5 5 LYS F 45  ? TYR F 49  ? LYS B 51  TYR B 55  
AC5 6 GLU F 53  ? LEU F 54  ? GLU B 66  LEU B 67  
AC6 1 SER F 114 ? PHE F 118 ? SER B 134 PHE B 138 
AC6 2 THR F 129 ? PHE F 139 ? THR B 149 PHE B 159 
AC6 3 TYR F 173 ? SER F 182 ? TYR B 193 SER B 202 
AC6 4 SER F 159 ? VAL F 163 ? SER B 179 VAL B 183 
AC7 1 LYS F 145 ? VAL F 150 ? LYS B 165 VAL B 170 
AC7 2 VAL F 191 ? GLN F 198 ? VAL B 211 GLN B 218 
AC7 3 THR F 201 ? ASN F 208 ? THR B 221 ASN B 230 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 5   ? N VAL C 5   O ALA A 23  ? O ALA C 24  
AA1 2 3 N LEU A 18  ? N LEU C 19  O MET A 83  ? O MET C 91  
AA1 3 4 O THR A 78  ? O THR C 86  N ASP A 73  ? N ASP C 81  
AA2 1 2 N GLY A 10  ? N GLY C 11  O THR A 117 ? O THR C 125 
AA2 2 3 O THR A 114 ? O THR C 122 N TYR A 94  ? N TYR C 102 
AA2 3 4 O VAL A 93  ? O VAL C 101 N GLN A 39  ? N GLN C 44  
AA2 4 5 N TRP A 36  ? N TRP C 41  O VAL A 48  ? O VAL C 53  
AA2 5 6 N TYR A 50  ? N TYR C 55  O TYR A 59  ? O TYR C 66  
AA3 1 2 N SER A 127 ? N SER C 135 O LYS A 150 ? O LYS C 158 
AA3 2 3 N TYR A 152 ? N TYR C 160 O TYR A 183 ? O TYR C 191 
AA3 3 4 O VAL A 191 ? O VAL C 199 N ALA A 143 ? N ALA C 151 
AA4 1 2 N SER A 127 ? N SER C 135 O LYS A 150 ? O LYS C 158 
AA4 2 3 N TYR A 152 ? N TYR C 160 O TYR A 183 ? O TYR C 191 
AA4 3 4 O SER A 184 ? O SER C 192 N VAL A 176 ? N VAL C 184 
AA5 1 2 N THR A 158 ? N THR C 166 O ASN A 206 ? O ASN C 214 
AA5 2 3 N VAL A 205 ? N VAL C 213 O VAL A 214 ? O VAL C 222 
AA6 1 2 N SER B 7   ? N SER D 7   O THR B 22  ? O THR D 22  
AA6 2 3 N CYS B 23  ? N CYS D 23  O PHE B 71  ? O PHE D 87  
AA6 3 4 O THR B 74  ? O THR D 90  N SER B 63  ? N SER D 77  
AA7 1 2 N LEU B 11  ? N LEU D 11  O GLU B 105 ? O GLU D 125 
AA7 2 3 O THR B 102 ? O THR D 122 N TYR B 86  ? N TYR D 102 
AA7 3 4 O TYR B 87  ? O TYR D 103 N TYR B 36  ? N TYR D 42  
AA7 4 5 N TRP B 35  ? N TRP D 41  O LEU B 47  ? O LEU D 53  
AA7 5 6 N TYR B 49  ? N TYR D 55  O GLU B 53  ? O GLU D 66  
AA8 1 2 N PHE B 118 ? N PHE D 138 O VAL B 133 ? O VAL D 153 
AA8 2 3 N LEU B 136 ? N LEU D 156 O LEU B 175 ? O LEU D 195 
AA8 3 4 O SER B 176 ? O SER D 196 N SER B 162 ? N SER D 182 
AA9 1 2 O GLN B 155 ? O GLN D 175 N TRP B 148 ? N TRP D 168 
AA9 2 3 N SER B 147 ? N SER D 167 O GLU B 195 ? O GLU D 215 
AA9 3 4 N CYS B 194 ? N CYS D 214 O LYS B 205 ? O LYS D 227 
AB1 1 2 N VAL C 15  ? N VAL E 15  O GLN D 79  ? O GLN F 79  
AB1 2 3 O MET D 81  ? O MET F 81  N LYS D 48  ? N LYS F 48  
AB2 1 2 N VAL C 15  ? N VAL E 15  O GLN D 79  ? O GLN F 79  
AB2 2 3 N SER D 74  ? N SER F 74  O GLN D 98  ? O GLN F 98  
AB3 1 2 N ILE C 29  ? N ILE E 29  O ARG C 56  ? O ARG E 56  
AB4 1 2 N ILE C 46  ? N ILE E 46  O ILE C 83  ? O ILE E 83  
AB4 2 3 N GLU C 67  ? N GLU E 67  O ARG C 105 ? O ARG E 105 
AB5 1 2 N ILE C 46  ? N ILE E 46  O ILE C 83  ? O ILE E 83  
AB5 2 3 N GLN C 79  ? N GLN E 79  O VAL D 15  ? O VAL F 15  
AB6 1 2 N ILE D 29  ? N ILE F 29  O ARG D 56  ? O ARG F 56  
AB7 1 2 N VAL E 5   ? N VAL A 5   O ALA E 23  ? O ALA A 24  
AB7 2 3 N LEU E 18  ? N LEU A 19  O MET E 83  ? O MET A 91  
AB7 3 4 O THR E 78  ? O THR A 86  N ASP E 73  ? N ASP A 81  
AB8 1 2 N VAL E 12  ? N VAL A 13  O THR E 117 ? O THR A 125 
AB8 2 3 O THR E 114 ? O THR A 122 N TYR E 94  ? N TYR A 102 
AB8 3 4 O TYR E 95  ? O TYR A 103 N VAL E 37  ? N VAL A 42  
AB8 4 5 N TRP E 36  ? N TRP A 41  O VAL E 48  ? O VAL A 53  
AB8 5 6 N TYR E 50  ? N TYR A 55  O TYR E 59  ? O TYR A 66  
AB9 1 2 N VAL E 12  ? N VAL A 13  O THR E 117 ? O THR A 125 
AB9 2 3 O THR E 114 ? O THR A 122 N TYR E 94  ? N TYR A 102 
AB9 3 4 N ARG E 98  ? N ARG A 106 O ASP E 108 ? O ASP A 116 
AC1 1 2 N SER E 127 ? N SER A 135 O LYS E 150 ? O LYS A 158 
AC1 2 3 N TYR E 152 ? N TYR A 160 O TYR E 183 ? O TYR A 191 
AC1 3 4 O VAL E 188 ? O VAL A 196 N HIS E 171 ? N HIS A 179 
AC2 1 2 N SER E 127 ? N SER A 135 O LYS E 150 ? O LYS A 158 
AC2 2 3 N TYR E 152 ? N TYR A 160 O TYR E 183 ? O TYR A 191 
AC2 3 4 O SER E 184 ? O SER A 192 N VAL E 176 ? N VAL A 184 
AC3 1 2 N THR E 158 ? N THR A 166 O ASN E 206 ? O ASN A 214 
AC3 2 3 N VAL E 205 ? N VAL A 213 O VAL E 214 ? O VAL A 222 
AC4 1 2 N SER F 7   ? N SER B 7   O THR F 22  ? O THR B 22  
AC4 2 3 N CYS F 23  ? N CYS B 23  O PHE F 71  ? O PHE B 87  
AC4 3 4 O THR F 74  ? O THR B 90  N SER F 63  ? N SER B 77  
AC5 1 2 N LEU F 11  ? N LEU B 11  O GLU F 105 ? O GLU B 125 
AC5 2 3 O VAL F 104 ? O VAL B 124 N ALA F 84  ? N ALA B 100 
AC5 3 4 O THR F 85  ? O THR B 101 N GLN F 38  ? N GLN B 44  
AC5 4 5 N TRP F 35  ? N TRP B 41  O LEU F 47  ? O LEU B 53  
AC5 5 6 N TYR F 49  ? N TYR B 55  O GLU F 53  ? O GLU B 66  
AC6 1 2 N PHE F 118 ? N PHE B 138 O VAL F 133 ? O VAL B 153 
AC6 2 3 N VAL F 132 ? N VAL B 152 O LEU F 179 ? O LEU B 199 
AC6 3 4 O THR F 178 ? O THR B 198 N GLN F 160 ? N GLN B 180 
AC7 1 2 N SER F 147 ? N SER B 167 O GLU F 195 ? O GLU B 215 
AC7 2 3 N VAL F 196 ? N VAL B 216 O VAL F 203 ? O VAL B 225 
# 
_pdbx_entry_details.entry_id                   8UWZ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_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 LEU C 19  ? ? -173.50 141.35  
2  1 ASP C 116 ? ? -78.97  -152.03 
3  1 TYR C 117 ? ? -27.25  120.86  
4  1 LEU C 204 ? ? 50.99   -107.28 
5  1 ALA D 29  ? ? -105.98 74.18   
6  1 ALA D 57  ? ? 69.51   -8.82   
7  1 SER D 83  ? ? -99.13  52.97   
8  1 ASP D 98  ? ? -85.83  34.35   
9  1 ALA D 100 ? ? -171.95 -172.52 
10 1 ARG D 107 ? ? 61.73   -160.29 
11 1 LEU D 115 ? ? -145.82 47.78   
12 1 GLU D 163 ? ? 57.85   70.64   
13 1 LYS D 189 ? ? -92.83  -62.25  
14 1 GLU D 207 ? ? 66.64   -9.90   
15 1 TYR E 39  ? ? -118.30 79.21   
16 1 PRO E 40  ? ? -78.10  35.22   
17 1 TYR E 45  ? ? -162.61 118.53  
18 1 MET E 55  ? ? -69.04  94.58   
19 1 SER F 24  ? ? -98.61  49.52   
20 1 TYR F 39  ? ? -114.28 78.80   
21 1 TYR F 45  ? ? -164.53 114.13  
22 1 LEU A 19  ? ? -173.88 142.76  
23 1 PHE A 28  ? ? -171.19 131.28  
24 1 TYR A 36  ? ? -85.21  41.90   
25 1 ASP A 116 ? ? -79.03  -155.03 
26 1 TYR A 117 ? ? -29.07  120.04  
27 1 LEU A 204 ? ? 44.13   -109.14 
28 1 ALA B 28  ? ? -67.93  85.30   
29 1 TYR B 36  ? ? 39.02   35.76   
30 1 ALA B 57  ? ? 67.78   -9.53   
31 1 SER B 83  ? ? -98.92  56.54   
32 1 ASP B 98  ? ? -85.50  42.33   
33 1 ALA B 100 ? ? -171.57 -174.34 
34 1 ARG B 107 ? ? 56.71   -169.39 
35 1 THR B 117 ? ? 56.92   71.04   
36 1 THR B 129 ? ? 50.37   76.54   
37 1 VAL B 130 ? ? -35.30  128.69  
38 1 PRO B 161 ? ? -79.48  -169.91 
39 1 LYS B 189 ? ? -91.37  -62.84  
40 1 SER B 222 ? ? -103.38 65.93   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG D 24 ? ? 0.254 'SIDE CHAIN' 
2 1 ARG F 56 ? ? 0.272 'SIDE CHAIN' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z         
2 -y,x-y,z+1/3  
3 -x+y,-x,z+2/3 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1  ? refined 28.752  46.129 -17.815 1.49708032611  0.900458568552  2.13426283423  -0.351652540319  
-0.0554253931774  0.095608919403    4.34913202988 7.95287862031 3.08387448746  0.907508934592   2.45862924494   4.74342025463   
0.426237173263   -1.19661155021   0.455917678396    -0.619095349727 1.83999783798    -1.41064454716   0.993579216723   
-0.307488093994  -0.250618764885  
'X-RAY DIFFRACTION' 2  ? refined 35.014  44.982 -12.140 1.49391653922  0.918312743712  2.10499450035  -0.326434878191  
-0.35627388794    0.211313935076    6.1592490701  2.17909301721 2.24562935215  2.14237017787    1.01179778147   -0.250991137054 
0.111986602544   -0.610514402199  0.422757524014    -0.497388168384 0.550590989169   -1.60571635965   1.28181038759    
-0.594122977083  0.44232613385    
'X-RAY DIFFRACTION' 3  ? refined 54.803  59.448 -19.456 1.53993635046  1.20544228088   2.77655611327  -0.242302403233  
-0.629090793982   0.236777820267    1.64235329477 7.67298076269 6.06150607415  -0.236557838829  0.293193399531  3.00110085075   
-0.0957785114885 -0.745270358487  0.861066812606    0.172772935317  -0.0225457906628 -1.02189539721   0.866214064063   
-0.109108666222  0.606884359686   
'X-RAY DIFFRACTION' 4  ? refined 47.987  25.707 -9.352  2.19045105775  1.10626802597   2.97283526343  -0.060337987803  
-0.479191750065   0.373536388023    3.01500378837 5.32020199738 5.37871576315  -2.41472709657   2.83409999963   0.506312752524  
-0.312627172035  -0.168742340241  0.850042271963    -1.11433224081  2.05734677182    -2.00349419992   -0.126908439622  
0.367041433233   0.548144247771   
'X-RAY DIFFRACTION' 5  ? refined 43.691  29.194 -19.968 1.56991561498  0.855438637968  3.39409542876  -0.0572359599296 
-0.561142703119   0.0682384858231   5.0792889943  3.15407982261 4.57199283329  0.444958378167   -1.76156932997  3.53619507501   
-0.90829473058   1.28677931108    0.19938880444     1.49537434063   -1.13479985619   -0.874467303468  1.4164657207     
0.867836693022   0.891902868723   
'X-RAY DIFFRACTION' 6  ? refined 44.321  26.995 -11.515 2.13082141612  1.29164202925   3.39912853462  -0.0831555996633 
-0.773272527377   0.487789379293    3.75471114939 4.45384741994 2.0733168671   1.55427180569    -1.34522662555  1.41261967406   
-0.111368532584  -0.456924435505  0.264961810674    -0.353928298209 -2.86770178846   -1.6166278262    1.44752536942    
0.728440182361   0.719777452911   
'X-RAY DIFFRACTION' 7  ? refined 64.655  56.358 -12.664 1.72514799581  2.25974319383   3.80374481238  0.0467414836804  
-0.767658814891   0.164475807275    8.18541922763 2.1507031214  0.530350462355 -3.96926826022   -2.82886587557  0.361350456649  
0.298524795881   -0.477219354858  0.511346346662    1.05030392695   1.6658777884     -2.45062436131   2.48992915735    
0.342642048139   1.28036224309    
'X-RAY DIFFRACTION' 8  ? refined 67.682  54.414 -6.736  1.71912810244  1.98228480007   3.74458649112  0.20092064746    
-0.9545476198     -0.0766732673466  1.57400935149 4.21624957728 8.95012304441  2.81476825321    1.05510029812   1.52868971177   
0.504375677557   -1.05090310554   0.106990666665    1.23862133409   1.06566054946    -1.88154246997   1.94329287679    
0.12529863148    3.01059341032    
'X-RAY DIFFRACTION' 9  ? refined 65.427  57.036 -6.272  1.87869442358  1.62358147148   3.39090499324  -0.360403556567  
-0.792409258189   0.381906994578    2.85125361246 2.39274213872 9.06880262171  2.51226065117    2.37799004078   1.56497615412   
-1.06472297751   0.271616057317   0.177221197739    0.419498035251  1.0079268911     -0.480886128033  1.24775195722    
-1.27262263872   1.75061648869    
'X-RAY DIFFRACTION' 10 ? refined 75.402  58.081 -7.276  1.14962101734  2.80583555911   5.7920933763   -0.988348969341  
-1.92079681769    1.21247316854     4.09926626802 6.22842740927 4.48676825561  -5.40005860576   -4.27924406041  3.78622986126   
2.81084789615    0.355818973004   -1.76887543156    -4.1035299033   -2.70383756794   -4.48873715703   1.33343462149    
-1.43779020779   0.404725737213   
'X-RAY DIFFRACTION' 11 ? refined 1.449   33.790 -5.924  2.05534021705  2.60171430464   0.813468655911 0.123060272243   
0.453498574793    0.151453704784    2.01136406253 3.36809145563 5.623185965    7.21246085357    9.38934173792   4.25296337784   
0.883384969894   -0.0873559988487 -0.321273342622   -2.72326338558  0.252462600302   -3.23540753243   -0.587609470367  
1.12564154522    -1.1060181639    
'X-RAY DIFFRACTION' 12 ? refined -4.441  31.594 -18.453 1.21643537556  0.944873899677  1.09400402321  -0.275463060861  
0.251584352849    -0.105297087881   5.86941168959 8.54294451441 8.07677361183  -1.81579780803   -0.702107011413 7.47402894979   
0.940991701221   -2.02001125023   1.24389673778     -1.30241820434  -0.395271780343  1.89666118558    -0.596054788827  
0.228798211921   -0.73186204779   
'X-RAY DIFFRACTION' 13 ? refined 9.802   20.703 -28.357 1.55934842045  0.881237588424  1.55092829365  -0.122878324624  
0.302063674778    -0.0259524929972  3.97042950462 2.81157994726 1.29088086183  -1.18304210423   -1.18545496715  0.683842080039  
1.42471478953    -1.15887837651   -0.485246983358   -0.295925002814 -3.2537880165    1.50496332881    0.669382991052   
-0.205083574492  -0.158374986491  
'X-RAY DIFFRACTION' 14 ? refined 24.131  9.981  -36.716 1.68710746967  1.4169014207    1.52280541804  0.378823340438   
-0.160958668473   0.189352543466    9.58901496479 2.07878914472 2.07969357892  -0.33926778755   5.46176821101   1.84658855424   
-0.14076142314   0.745527673785   -0.643941811872   1.09070404975   1.24468482662    -1.61601164366   -2.12763280185   
-1.91607605883   -1.78026808212   
'X-RAY DIFFRACTION' 15 ? refined 19.962  19.678 -29.759 0.862821625024 1.10840420009   1.24327183181  -0.0683581828184 
0.259272251422    -0.00863973684709 4.46551241449 7.4006097444  7.76416782579  1.47336993343    1.49794307389   1.461897743     
1.82804294666    -0.872965880977  -1.07579748636    -1.1091066852   -0.108463618162  -0.960335505263  -0.839199582256  
-0.0705085706953 -0.766904827591  
'X-RAY DIFFRACTION' 16 ? refined -5.450  21.150 -26.077 1.69141166989  1.42219707768   1.20843772401  -0.521108233417  
0.370615924649    0.0759184769128   8.24824382776 9.31993655533 2.14358712205  -8.70027341732   -9.12838093236  8.38591888759   
-1.88194469968   -0.659932308006  2.6281800855      -0.371614271771 -3.35830465249   1.59738445829    1.4851822791     
0.629901927086   -0.254100112535  
'X-RAY DIFFRACTION' 17 ? refined 13.507  21.743 -35.576 1.21299857442  0.85735831479   1.27045758206  -0.181378348238  
0.266204495179    -0.356132205839   1.97673592704 5.7884320401  4.28674372557  -0.470759888597  -1.54547427281  -4.3681777376   
0.349117546319   -0.607967951362  0.309078923263    1.2908751963    0.459781426938   -0.0567796364767 0.170350086676   
1.3029746836     -0.284793142412  
'X-RAY DIFFRACTION' 18 ? refined 36.718  13.333 -34.381 2.48194199371  1.93113552356   2.88244405832  -0.184794714313  
0.197975132975    -0.804289513348   2.05215781094 1.99364271979 1.99115212133  3.91305439697    -1.18101935153  7.62443096164   
2.95775036546    0.363738458547   -3.58124240273    0.856665785445  -1.92095321998   1.25385487467    -3.53441318182   
-4.15937270769   5.29265291519    
'X-RAY DIFFRACTION' 19 ? refined 18.030  21.687 -37.339 1.47450638511  1.00243327887   1.89875728081  0.285961806992   
0.461465567967    0.154325779519    3.29772196545 1.6833024273  5.13553069893  -0.8286106169    -0.41716741998  2.15640372691   
1.89798929893    -0.535911522993  -0.712988931631   0.678205945505  3.48839956307    1.50788665733    1.36283020156    
1.12654531502    0.857085809034   
'X-RAY DIFFRACTION' 20 ? refined -3.582  22.228 -34.668 0.975796216534 1.29879466607   1.68017910176  0.0149780195677  
0.46187181797     -0.432641624052   4.29737699837 1.59521741112 8.86976976171  -1.79180008452   0.997801619449  2.11086913252   
0.62675877754    -1.69943208889   0.412189061892    0.624486511186  0.359531410524   0.690813910204   -0.184869450635  
-0.275054788862  -1.44917523108   
'X-RAY DIFFRACTION' 21 ? refined 20.554  30.636 -39.742 2.2491549246   1.48156904393   1.8237589517   0.200836994735   
0.223813887294    0.374268636373    1.61551273511 4.57426970228 2.05753250464  -2.61854721703   5.41192363176   -9.52834817725  
1.54471294487    1.36312951882    -2.31395710918    1.49703892904   -0.351186630565  3.33581580788    -2.57580219124   
-0.776424986635  -3.45938364112   
'X-RAY DIFFRACTION' 22 ? refined 25.226  27.113 -27.273 1.21178152959  0.84891947798   1.39164211297  0.0774288386065  
0.346736155592    0.0832032360107   7.2979863762  7.38390590758 8.5619767501   -0.071751727423  1.77352070247   -7.57154913649  
-1.23243574854   -0.461344744021  1.70108163599     0.541253408124  0.827532796925   -0.335819373977  2.25233994088    
-0.441879486934  -0.746160013556  
'X-RAY DIFFRACTION' 23 ? refined 9.470   21.624 -17.787 2.05397953949  1.17571947349   0.813388143421 -0.468156188185  
-0.0468901597496  -0.0889498939051  8.6448118764  3.01617294815 1.75429981002  4.4573858101     -3.23513205764  -0.977551573601 
0.991213874514   -0.812025264472  -0.156664600424   -0.228847392307 -2.56761103116   -1.36310432612   1.16598102706    
0.328325777606   -0.808004497573  
'X-RAY DIFFRACTION' 24 ? refined -8.116  16.996 -12.080 1.23040647097  1.2252428781    1.80067612097  -0.299786155306  
-0.00500811345865 -0.156795815904   6.7172956106  9.53551032869 5.42606647088  -6.62133594248   2.40916305892   1.10768868887   
1.24376242592    -0.65360774162   -0.319152715264   -1.25724474144  -2.6884928318    2.7101758328     -0.308899927004  
1.38621163904    -0.548740408903  
'X-RAY DIFFRACTION' 25 ? refined 8.824   21.339 -13.388 1.86250143133  0.894030876149  1.10701085773  -0.28180164287   
-0.0133663339421  -0.0213224710108  4.84557197455 1.73407525855 4.75640393286  0.389309296044   0.924928438644  1.16630912875   
-0.21887404419   0.108005972822   0.245788032793    -0.147425528976 -0.910567804453  -0.0133095915196 1.17917024697    
-0.108912999863  0.0307750324293  
'X-RAY DIFFRACTION' 26 ? refined -7.037  22.358 -10.373 1.4129292337   1.10768524149   1.02643175057  -0.193882881797  
0.362315404935    -0.252266282445   4.9230236537  7.24735706376 2.38684001737  3.60287372895    -2.38608695387  -2.41935594022  
0.13472301363    -0.407024901096  0.193442724565    -1.57888742766  1.79294660523    1.517410143      0.347868523788   
-0.83912669511   0.607381739175   
'X-RAY DIFFRACTION' 27 ? refined 22.303  17.549 -10.717 1.73246503204  1.36477813716   1.43669913545  -0.494742306759  
-0.231377277472   0.281159252546    9.33554178349 8.28471639157 2.67212756979  -5.07934817373   1.17669077826   1.82620492283   
-1.58705373412   1.22154930731    0.555511382653    1.71271042815   -0.272510264166  0.559675554605   1.91912839342    
0.62005658693    -0.706795215319  
'X-RAY DIFFRACTION' 28 ? refined -4.661  57.263 -31.852 1.5811568933   0.917697430338  1.55444953964  -0.31212642951   
0.26521137219     -0.0101450908627  3.70365818071 7.70500546405 2.50337280772  -4.34395075262   3.47298851064   -7.45862376025  
-1.08485133783   -1.28474325649   2.75275781428     0.662827458402  0.315150605737   -2.38406270206   0.457609395473   
0.518459210939   -0.200536355228  
'X-RAY DIFFRACTION' 29 ? refined -0.464  45.651 -24.540 1.25056317846  0.982870523877  1.29076780531  -0.296537274401  
0.210657171753    0.0191150768295   2.43540892894 5.94225389797 3.58821269297  -8.07519648795   2.36702979402   -1.10122489319  
0.0688257716124  0.157620052002   -0.0718520275946  -0.446706092728 -0.0836202384813 -1.05158707739   -0.0512121997139 
0.357402678942   -0.11738537667   
'X-RAY DIFFRACTION' 30 ? refined -4.617  44.529 -37.624 1.10584147592  0.964054124237  1.11556133993  -0.0859916884867 
0.217048399256    -0.222354494147   10.6325879945 6.5077743422  4.21087221775  -0.792454891225  1.84260857921   -4.89732727059  
0.475992726447   -0.460191160775  -0.0158364920986  1.57409083606   -0.64160951882   0.378103444941   0.116301233109   
-0.0644678909478 0.066721881135   
'X-RAY DIFFRACTION' 31 ? refined 2.915   49.697 -30.394 1.34234182267  1.1436460838    1.85873342694  -0.231468816487  
0.158832118624    -0.181070722648   5.92961424219 2.53612407513 2.21689303819  -1.5194443933    0.352157199495  -4.51602378166  
0.882583759541   -0.62592118151   -0.0928481181562  0.115103104997  1.33393096512    -1.53713739021   1.1824957799     
-1.89687947736   2.56784289141    
'X-RAY DIFFRACTION' 32 ? refined -7.841  45.962 -34.195 1.2050360826   0.640690429617  1.30244987406  -0.0960556225564 
0.178763743794    -0.250754194934   4.7989909929  6.83565969124 5.35130260148  -2.09976283839   -0.934075180416 -5.0394856822   
-0.121285376882  0.540573531058   -0.432397106249   0.287086671497  -0.796374896675  0.549969150688   1.00265432282    
-0.523414088045  -0.31289732622   
'X-RAY DIFFRACTION' 33 ? refined -13.240 62.818 -32.734 1.5979921541   0.865491696154  1.88853058398  0.194077669998   
0.0764861174398   -0.230959402834   1.89463518161 1.50452989625 2.05595861299  -1.4177769021    2.47799932922   -0.768216934741 
-0.206910174811  0.297710981112   -0.241398667539   -0.370677992424 1.14136611619    0.989340870266   0.508831553869   
-1.65819728587   -0.0599064417961 
'X-RAY DIFFRACTION' 34 ? refined -32.223 75.457 -27.238 1.84840909061  1.08981524769   2.58577269342  0.0837261774265  
0.437636010497    -0.217705442302   4.98929064814 7.36432160265 6.2126237891   -3.95737227085   2.4373716237    0.643329283407  
-0.840529215564  0.399784023169   0.784457838148    0.220671443621  0.319527185615   0.579916171619   0.798676485202   
-1.15013460497   -1.39915712461   
'X-RAY DIFFRACTION' 35 ? refined -22.101 67.454 -24.465 2.10862611075  1.09872164741   1.86687441433  -0.139368947685  
0.472078389716    0.17106253234     3.09380981142 5.68948254369 4.38042155916  -3.85792353681   0.666274337582  0.592130656031  
0.696270165279   -0.0821593921505 -0.629716418059   -1.41356310272  -0.34486742955   0.104878521297   1.9603524286     
-2.52914733511   0.151763804376   
'X-RAY DIFFRACTION' 36 ? refined -25.088 69.772 -33.839 1.78479355332  1.10543839781   1.61745041435  0.142713986719   
0.507536871714    0.161955807339    3.151845301   2.71331423122 1.78846408655  -1.63393613946   -0.288481361596 -0.570056401043 
0.0907181662783  -0.198972007513  0.622039743799    1.76736799239   0.710123720215   -0.892820117101  -0.182044252917  
-0.304755005816  -1.17919141304   
'X-RAY DIFFRACTION' 37 ? refined -26.468 74.906 -18.627 3.31647396955  1.80153529194   1.45009129273  -0.0525541637015 
0.0808540770401   0.0736182492395   2.53856071597 2.82066365025 2.99378925934  -0.0305781804321 6.1073675324    0.637257967942  
-1.78778060337   0.0449353635791  1.594828455       -4.20406926951  -0.431034933234  0.347708046223   2.48744130359    
-2.29354038572   0.923204285561   
'X-RAY DIFFRACTION' 38 ? refined -18.524 76.842 -24.359 1.59421074756  1.68815242219   2.74012773994  -0.219265410497  
-0.066249834945   -0.484265032775   2.23925871717 2.46015284785 8.25244810796  -4.61267917281   -8.38089284721  1.6274973948    
-0.551351785607  1.32828344042    -0.545060758981   -2.73329704453  3.64089188726    -0.623313504221  -0.932765322892  
-2.33018267359   2.04173050178    
'X-RAY DIFFRACTION' 39 ? refined -33.623 41.850 -37.083 1.07704252549  1.4772195582    2.84461640281  -0.0171183764735 
0.0822928044719   -0.227498394133   6.89287234151 8.56964160351 6.87346425311  5.3948757874     -2.20917486884  -6.79460320346  
1.70918325569    -0.0384627443425 -1.25590026305    -1.10744537978  4.25632043594    2.83754776401    -0.0761365161019 
-1.61496961383   -0.173144879436  
'X-RAY DIFFRACTION' 40 ? refined -20.356 37.533 -35.024 1.15004141157  0.895136794898  2.33599736704  0.0103591830657  
0.379157032879    -0.0846606651552  5.54038753964 8.71090508308 5.10781583495  0.306276128912   3.84643702522   0.794626878445  
0.503093064334   -1.21686746658   0.778980964384    0.85881207893   -0.196290361465  1.79671222639    -0.846472485289  
-0.850911220257  0.107624219068   
'X-RAY DIFFRACTION' 41 ? refined -26.282 35.445 -28.543 1.50797642322  0.984076168959  2.77067485384  -0.266513328299  
0.500390468381    -0.0989898301085  5.37799541022 5.40816688659 3.21636337929  -5.00232283625   1.36791372827   2.55940031493   
0.0767800635695  -0.07534315792   -0.124906666919   0.269840419926  -1.13448293388   2.5269659028     1.21112588116    
0.341450779881   -0.688609015641  
'X-RAY DIFFRACTION' 42 ? refined -15.278 39.113 -37.977 1.13942465693  0.952655927455  1.88897409026  -0.0970644808383 
0.261145120367    -0.11895100366    7.6507990749  2.61322841482 2.93874097172  -2.65033300836   -3.87727112003  1.70014160166   
1.59640252822    -0.659085762446  -1.12641910154    0.577558762262  1.01484000752    -0.275478970273  -0.865390090566  
-0.567890568084  -0.523866166139  
'X-RAY DIFFRACTION' 43 ? refined -39.219 52.239 -33.162 0.989463744108 -0.229714253654 2.94144461634  1.87581589965    
1.18771787462     -0.270101934725   1.94334235995 1.61392435462 2.24795448597  -0.309348084625  -1.19471419317  0.815731336377  
2.8978603976     -1.79670268612   -0.957446883172   0.468669228777  1.61940290971    -0.369593262581  -2.05841032399   
-0.799241030023  -4.72755796855   
'X-RAY DIFFRACTION' 44 ? refined -31.450 81.071 -32.484 2.49900197707  1.17657305331   1.61025279118  0.128669181071   
0.446804612815    0.26825558719     2.68848088159 4.45554816498 3.69792570054  1.89368296366    -1.40488396391  2.52847617916   
2.1554427964     -1.0738192256    -0.720724630426   -1.09337655136  0.918000320359   1.59706076583    3.53847938307    
-1.382120863     0.365216464557   
'X-RAY DIFFRACTION' 45 ? refined -35.248 71.175 -33.827 2.11114627344  0.995643428322  2.06668193046  0.215480359286   
0.450981502991    0.342743637799    6.69437463713 5.59721233079 8.01921658815  3.47977858418    -3.7014011555   1.44231385054   
0.106809655046   -0.460901174271  0.244348761097    0.286751046526  1.33188250791    2.19876451323    0.702216635029   
-0.54906411538   -0.246300696154  
'X-RAY DIFFRACTION' 46 ? refined -40.249 67.858 -41.455 1.36270739687  1.66235453479   2.16798467411  0.101679384667   
0.389548004217    -0.0626133685952  7.02787310988 6.37005582505 5.29407225537  -4.39344972911   1.7742030175    2.90654385717   
0.390180103157   0.00599441558634 -0.789789551256   3.25303606599   -1.58109710755   3.17040902398    0.00133662343593 
-0.360708008642  -1.50528561279   
'X-RAY DIFFRACTION' 47 ? refined -35.400 66.186 -37.316 2.81167202637  1.07531833344   2.15945081159  0.398287338367   
0.380864819079    0.0849238109345   7.66480169419 8.6035642155  2.816684151    -2.6949038378    4.58184942008   -9.44180403818  
-1.79858170014   1.92224072123    -0.00774727696338 0.0704284071864 -1.99513194111   2.57978947342    4.54982284187    
-3.34713719933   -1.19937736798   
'X-RAY DIFFRACTION' 48 ? refined -32.661 77.047 -39.095 1.66053554859  1.24471638841   1.62406855801  -0.0347637444348 
0.0918712886954   0.318796604357    7.87245964682 4.99516730986 7.47786866789  -3.26102053013   -0.221614523342 5.26029834004   
0.00140042126434 0.36652399899    -0.0937087870238  1.05504893412   2.13888269884    2.11058671363    -0.266657725424  
-1.22365063411   0.412320749839   
'X-RAY DIFFRACTION' 49 ? refined -41.779 76.250 -40.688 1.72950301227  1.277356339     2.0845372621   0.0770200145839  
0.358627370546    0.423882017662    8.31023391288 3.73949252323 7.8305561387   -3.46050361784   0.240834450121  4.07201274584   
-0.403573588372  0.102446556276   0.64521383851     0.984919170253  0.802037559377   1.39908136421    1.31395277347    
-1.44083599685   -0.456144172033  
'X-RAY DIFFRACTION' 50 ? refined -43.990 77.044 -35.931 1.94595619034  1.46619590096   2.13503958285  0.370533198576   
0.229311521832    0.25965950581     8.43207230958 4.51100783674 8.52617211496  -4.17402763232   -0.820947407365 2.52651426327   
-1.36537915481   0.494307400332   0.769343460019    0.958894101041  1.73889837551    1.63589372513    0.807491431549   
-0.466914717429  0.32035713778    
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1  1  C 1   C 37  '( CHAIN C AND RESID 1:37 )'    ? ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  C 38  C 153 '( CHAIN C AND RESID 38:153 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  C 154 C 228 '( CHAIN C AND RESID 154:228 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  D 5   D 44  '( CHAIN D AND RESID 5:44 )'    ? ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  D 45  D 75  '( CHAIN D AND RESID 45:75 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  D 76  D 122 '( CHAIN D AND RESID 76:122 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  D 123 D 148 '( CHAIN D AND RESID 123:148 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  D 149 D 170 '( CHAIN D AND RESID 149:170 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  D 171 D 210 '( CHAIN D AND RESID 171:210 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 D 211 D 234 '( CHAIN D AND RESID 211:234 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 11 11 E 11  E 16  '( CHAIN E AND RESID 11:16 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 12 12 E 17  E 23  '( CHAIN E AND RESID 17:23 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 13 13 E 24  E 38  '( CHAIN E AND RESID 24:38 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 14 14 E 39  E 45  '( CHAIN E AND RESID 39:45 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 15 15 E 46  E 56  '( CHAIN E AND RESID 46:56 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 16 16 E 57  E 65  '( CHAIN E AND RESID 57:65 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 17 17 E 66  E 83  '( CHAIN E AND RESID 66:83 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 18 18 E 84  E 90  '( CHAIN E AND RESID 84:90 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 19 19 E 91  E 99  '( CHAIN E AND RESID 91:99 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 20 20 E 100 E 108 '( CHAIN E AND RESID 100:108 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 21 21 F 11  F 16  '( CHAIN F AND RESID 11:16 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 22 22 F 17  F 23  '( CHAIN F AND RESID 17:23 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 23 23 F 24  F 38  '( CHAIN F AND RESID 24:38 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 24 24 F 39  F 50  '( CHAIN F AND RESID 39:50 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 25 25 F 51  F 84  '( CHAIN F AND RESID 51:84 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 26 26 F 85  F 99  '( CHAIN F AND RESID 85:99 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 27 27 F 100 F 109 '( CHAIN F AND RESID 100:109 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 28 28 A 1   A 18  '( CHAIN A AND RESID 1:18 )'    ? ? ? ? ? 
'X-RAY DIFFRACTION' 29 29 A 19  A 38  '( CHAIN A AND RESID 19:38 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 30 30 A 39  A 75  '( CHAIN A AND RESID 39:75 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 31 31 A 76  A 91  '( CHAIN A AND RESID 76:91 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 32 32 A 92  A 114 '( CHAIN A AND RESID 92:114 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 33 33 A 115 A 139 '( CHAIN A AND RESID 115:139 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 34 34 A 140 A 160 '( CHAIN A AND RESID 140:160 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 35 35 A 161 A 180 '( CHAIN A AND RESID 161:180 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 36 36 A 181 A 200 '( CHAIN A AND RESID 181:200 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 37 37 A 201 A 215 '( CHAIN A AND RESID 201:215 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 38 38 A 216 A 229 '( CHAIN A AND RESID 216:229 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 39 39 B 5   B 18  '( CHAIN B AND RESID 5:18 )'    ? ? ? ? ? 
'X-RAY DIFFRACTION' 40 40 B 19  B 54  '( CHAIN B AND RESID 19:54 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 41 41 B 55  B 99  '( CHAIN B AND RESID 55:99 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 42 42 B 100 B 121 '( CHAIN B AND RESID 100:121 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 43 43 B 122 B 133 '( CHAIN B AND RESID 122:133 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 44 44 B 134 B 148 '( CHAIN B AND RESID 134:148 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 45 45 B 149 B 159 '( CHAIN B AND RESID 149:159 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 46 46 B 160 B 170 '( CHAIN B AND RESID 160:170 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 47 47 B 171 B 192 '( CHAIN B AND RESID 171:192 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 48 48 B 193 B 207 '( CHAIN B AND RESID 193:207 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 49 49 B 208 B 218 '( CHAIN B AND RESID 208:218 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 50 50 B 219 B 234 '( CHAIN B AND RESID 219:234 )' ? ? ? ? ? 
# 
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 C SER 142 ? A SER 134 
2  1 Y 1 C GLY 148 ? A GLY 140 
3  1 Y 1 C GLY 149 ? A GLY 141 
4  1 Y 1 C ALA 152 ? A ALA 144 
5  1 Y 1 C LYS 229 ? A LYS 221 
6  1 Y 1 C SER 230 ? A SER 222 
7  1 Y 1 C CYS 231 ? A CYS 223 
8  1 Y 1 C ASP 232 ? A ASP 224 
9  1 Y 1 C LYS 233 ? A LYS 225 
10 1 Y 1 C THR 234 ? A THR 226 
11 1 Y 1 C HIS 235 ? A HIS 227 
12 1 Y 1 C THR 236 ? A THR 228 
13 1 Y 1 D ASP 1   ? B ASP 1   
14 1 Y 1 D ILE 2   ? B ILE 2   
15 1 Y 1 D GLN 3   ? B GLN 3   
16 1 Y 1 D MET 4   ? B MET 4   
17 1 Y 1 D GLN 27  ? B GLN 27  
18 1 Y 1 D VAL 130 ? B VAL 110 
19 1 Y 1 D ALA 131 ? B ALA 111 
20 1 Y 1 E ALA 1   ? C ALA 1   
21 1 Y 1 E PRO 2   ? C PRO 2   
22 1 Y 1 E MET 3   ? C MET 3   
23 1 Y 1 E ALA 4   ? C ALA 4   
24 1 Y 1 E GLU 5   ? C GLU 5   
25 1 Y 1 E GLY 6   ? C GLY 6   
26 1 Y 1 E GLY 7   ? C GLY 7   
27 1 Y 1 E GLY 8   ? C GLY 8   
28 1 Y 1 E GLN 9   ? C GLN 9   
29 1 Y 1 E ASN 10  ? C ASN 10  
30 1 Y 1 E ASP 109 ? C ASP 109 
31 1 Y 1 E ARG 110 ? C ARG 110 
32 1 Y 1 E ALA 111 ? C ALA 111 
33 1 Y 1 E ARG 112 ? C ARG 112 
34 1 Y 1 E GLN 113 ? C GLN 113 
35 1 Y 1 E GLU 114 ? C GLU 114 
36 1 Y 1 E ASN 115 ? C ASN 115 
37 1 Y 1 E CYS 116 ? C CYS 116 
38 1 Y 1 E ASP 117 ? C ASP 117 
39 1 Y 1 E LYS 118 ? C LYS 118 
40 1 Y 1 E PRO 119 ? C PRO 119 
41 1 Y 1 E ARG 120 ? C ARG 120 
42 1 Y 1 E ARG 121 ? C ARG 121 
43 1 Y 1 F ALA 1   ? D ALA 1   
44 1 Y 1 F PRO 2   ? D PRO 2   
45 1 Y 1 F MET 3   ? D MET 3   
46 1 Y 1 F ALA 4   ? D ALA 4   
47 1 Y 1 F GLU 5   ? D GLU 5   
48 1 Y 1 F GLY 6   ? D GLY 6   
49 1 Y 1 F GLY 7   ? D GLY 7   
50 1 Y 1 F GLY 8   ? D GLY 8   
51 1 Y 1 F GLN 9   ? D GLN 9   
52 1 Y 1 F ASN 10  ? D ASN 10  
53 1 Y 1 F ARG 110 ? D ARG 110 
54 1 Y 1 F ALA 111 ? D ALA 111 
55 1 Y 1 F ARG 112 ? D ARG 112 
56 1 Y 1 F GLN 113 ? D GLN 113 
57 1 Y 1 F GLU 114 ? D GLU 114 
58 1 Y 1 F ASN 115 ? D ASN 115 
59 1 Y 1 F CYS 116 ? D CYS 116 
60 1 Y 1 F ASP 117 ? D ASP 117 
61 1 Y 1 F LYS 118 ? D LYS 118 
62 1 Y 1 F PRO 119 ? D PRO 119 
63 1 Y 1 F ARG 120 ? D ARG 120 
64 1 Y 1 F ARG 121 ? D ARG 121 
65 1 Y 1 A SER 230 ? E SER 222 
66 1 Y 1 A CYS 231 ? E CYS 223 
67 1 Y 1 A ASP 232 ? E ASP 224 
68 1 Y 1 A LYS 233 ? E LYS 225 
69 1 Y 1 A THR 234 ? E THR 226 
70 1 Y 1 A HIS 235 ? E HIS 227 
71 1 Y 1 A THR 236 ? E THR 228 
72 1 Y 1 B ASP 1   ? F ASP 1   
73 1 Y 1 B ILE 2   ? F ILE 2   
74 1 Y 1 B GLN 3   ? F GLN 3   
75 1 Y 1 B MET 4   ? F MET 4   
# 
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  
BMA C1   C N R 74  
BMA C2   C N S 75  
BMA C3   C N S 76  
BMA C4   C N S 77  
BMA C5   C N R 78  
BMA C6   C N N 79  
BMA O1   O N N 80  
BMA O2   O N N 81  
BMA O3   O N N 82  
BMA O4   O N N 83  
BMA O5   O N N 84  
BMA O6   O N N 85  
BMA H1   H N N 86  
BMA H2   H N N 87  
BMA H3   H N N 88  
BMA H4   H N N 89  
BMA H5   H N N 90  
BMA H61  H N N 91  
BMA H62  H N N 92  
BMA HO1  H N N 93  
BMA HO2  H N N 94  
BMA HO3  H N N 95  
BMA HO4  H N N 96  
BMA HO6  H N N 97  
CYS N    N N N 98  
CYS CA   C N R 99  
CYS C    C N N 100 
CYS O    O N N 101 
CYS CB   C N N 102 
CYS SG   S N N 103 
CYS OXT  O N N 104 
CYS H    H N N 105 
CYS H2   H N N 106 
CYS HA   H N N 107 
CYS HB2  H N N 108 
CYS HB3  H N N 109 
CYS HG   H N N 110 
CYS HXT  H N N 111 
GLN N    N N N 112 
GLN CA   C N S 113 
GLN C    C N N 114 
GLN O    O N N 115 
GLN CB   C N N 116 
GLN CG   C N N 117 
GLN CD   C N N 118 
GLN OE1  O N N 119 
GLN NE2  N N N 120 
GLN OXT  O N N 121 
GLN H    H N N 122 
GLN H2   H N N 123 
GLN HA   H N N 124 
GLN HB2  H N N 125 
GLN HB3  H N N 126 
GLN HG2  H N N 127 
GLN HG3  H N N 128 
GLN HE21 H N N 129 
GLN HE22 H N N 130 
GLN HXT  H N N 131 
GLU N    N N N 132 
GLU CA   C N S 133 
GLU C    C N N 134 
GLU O    O N N 135 
GLU CB   C N N 136 
GLU CG   C N N 137 
GLU CD   C N N 138 
GLU OE1  O N N 139 
GLU OE2  O N N 140 
GLU OXT  O N N 141 
GLU H    H N N 142 
GLU H2   H N N 143 
GLU HA   H N N 144 
GLU HB2  H N N 145 
GLU HB3  H N N 146 
GLU HG2  H N N 147 
GLU HG3  H N N 148 
GLU HE2  H N N 149 
GLU HXT  H N N 150 
GLY N    N N N 151 
GLY CA   C N N 152 
GLY C    C N N 153 
GLY O    O N N 154 
GLY OXT  O N N 155 
GLY H    H N N 156 
GLY H2   H N N 157 
GLY HA2  H N N 158 
GLY HA3  H N N 159 
GLY HXT  H N N 160 
HIS N    N N N 161 
HIS CA   C N S 162 
HIS C    C N N 163 
HIS O    O N N 164 
HIS CB   C N N 165 
HIS CG   C Y N 166 
HIS ND1  N Y N 167 
HIS CD2  C Y N 168 
HIS CE1  C Y N 169 
HIS NE2  N Y N 170 
HIS OXT  O N N 171 
HIS H    H N N 172 
HIS H2   H N N 173 
HIS HA   H N N 174 
HIS HB2  H N N 175 
HIS HB3  H N N 176 
HIS HD1  H N N 177 
HIS HD2  H N N 178 
HIS HE1  H N N 179 
HIS HE2  H N N 180 
HIS HXT  H N N 181 
ILE N    N N N 182 
ILE CA   C N S 183 
ILE C    C N N 184 
ILE O    O N N 185 
ILE CB   C N S 186 
ILE CG1  C N N 187 
ILE CG2  C N N 188 
ILE CD1  C N N 189 
ILE OXT  O N N 190 
ILE H    H N N 191 
ILE H2   H N N 192 
ILE HA   H N N 193 
ILE HB   H N N 194 
ILE HG12 H N N 195 
ILE HG13 H N N 196 
ILE HG21 H N N 197 
ILE HG22 H N N 198 
ILE HG23 H N N 199 
ILE HD11 H N N 200 
ILE HD12 H N N 201 
ILE HD13 H N N 202 
ILE HXT  H N N 203 
LEU N    N N N 204 
LEU CA   C N S 205 
LEU C    C N N 206 
LEU O    O N N 207 
LEU CB   C N N 208 
LEU CG   C N N 209 
LEU CD1  C N N 210 
LEU CD2  C N N 211 
LEU OXT  O N N 212 
LEU H    H N N 213 
LEU H2   H N N 214 
LEU HA   H N N 215 
LEU HB2  H N N 216 
LEU HB3  H N N 217 
LEU HG   H N N 218 
LEU HD11 H N N 219 
LEU HD12 H N N 220 
LEU HD13 H N N 221 
LEU HD21 H N N 222 
LEU HD22 H N N 223 
LEU HD23 H N N 224 
LEU HXT  H N N 225 
LYS N    N N N 226 
LYS CA   C N S 227 
LYS C    C N N 228 
LYS O    O N N 229 
LYS CB   C N N 230 
LYS CG   C N N 231 
LYS CD   C N N 232 
LYS CE   C N N 233 
LYS NZ   N N N 234 
LYS OXT  O N N 235 
LYS H    H N N 236 
LYS H2   H N N 237 
LYS HA   H N N 238 
LYS HB2  H N N 239 
LYS HB3  H N N 240 
LYS HG2  H N N 241 
LYS HG3  H N N 242 
LYS HD2  H N N 243 
LYS HD3  H N N 244 
LYS HE2  H N N 245 
LYS HE3  H N N 246 
LYS HZ1  H N N 247 
LYS HZ2  H N N 248 
LYS HZ3  H N N 249 
LYS HXT  H N N 250 
MET N    N N N 251 
MET CA   C N S 252 
MET C    C N N 253 
MET O    O N N 254 
MET CB   C N N 255 
MET CG   C N N 256 
MET SD   S N N 257 
MET CE   C N N 258 
MET OXT  O N N 259 
MET H    H N N 260 
MET H2   H N N 261 
MET HA   H N N 262 
MET HB2  H N N 263 
MET HB3  H N N 264 
MET HG2  H N N 265 
MET HG3  H N N 266 
MET HE1  H N N 267 
MET HE2  H N N 268 
MET HE3  H N N 269 
MET HXT  H N N 270 
NAG C1   C N R 271 
NAG C2   C N R 272 
NAG C3   C N R 273 
NAG C4   C N S 274 
NAG C5   C N R 275 
NAG C6   C N N 276 
NAG C7   C N N 277 
NAG C8   C N N 278 
NAG N2   N N N 279 
NAG O1   O N N 280 
NAG O3   O N N 281 
NAG O4   O N N 282 
NAG O5   O N N 283 
NAG O6   O N N 284 
NAG O7   O N N 285 
NAG H1   H N N 286 
NAG H2   H N N 287 
NAG H3   H N N 288 
NAG H4   H N N 289 
NAG H5   H N N 290 
NAG H61  H N N 291 
NAG H62  H N N 292 
NAG H81  H N N 293 
NAG H82  H N N 294 
NAG H83  H N N 295 
NAG HN2  H N N 296 
NAG HO1  H N N 297 
NAG HO3  H N N 298 
NAG HO4  H N N 299 
NAG HO6  H N N 300 
PHE N    N N N 301 
PHE CA   C N S 302 
PHE C    C N N 303 
PHE O    O N N 304 
PHE CB   C N N 305 
PHE CG   C Y N 306 
PHE CD1  C Y N 307 
PHE CD2  C Y N 308 
PHE CE1  C Y N 309 
PHE CE2  C Y N 310 
PHE CZ   C Y N 311 
PHE OXT  O N N 312 
PHE H    H N N 313 
PHE H2   H N N 314 
PHE HA   H N N 315 
PHE HB2  H N N 316 
PHE HB3  H N N 317 
PHE HD1  H N N 318 
PHE HD2  H N N 319 
PHE HE1  H N N 320 
PHE HE2  H N N 321 
PHE HZ   H N N 322 
PHE HXT  H N N 323 
PRO N    N N N 324 
PRO CA   C N S 325 
PRO C    C N N 326 
PRO O    O N N 327 
PRO CB   C N N 328 
PRO CG   C N N 329 
PRO CD   C N N 330 
PRO OXT  O N N 331 
PRO H    H N N 332 
PRO HA   H N N 333 
PRO HB2  H N N 334 
PRO HB3  H N N 335 
PRO HG2  H N N 336 
PRO HG3  H N N 337 
PRO HD2  H N N 338 
PRO HD3  H N N 339 
PRO HXT  H N N 340 
SER N    N N N 341 
SER CA   C N S 342 
SER C    C N N 343 
SER O    O N N 344 
SER CB   C N N 345 
SER OG   O N N 346 
SER OXT  O N N 347 
SER H    H N N 348 
SER H2   H N N 349 
SER HA   H N N 350 
SER HB2  H N N 351 
SER HB3  H N N 352 
SER HG   H N N 353 
SER HXT  H N N 354 
THR N    N N N 355 
THR CA   C N S 356 
THR C    C N N 357 
THR O    O N N 358 
THR CB   C N R 359 
THR OG1  O N N 360 
THR CG2  C N N 361 
THR OXT  O N N 362 
THR H    H N N 363 
THR H2   H N N 364 
THR HA   H N N 365 
THR HB   H N N 366 
THR HG1  H N N 367 
THR HG21 H N N 368 
THR HG22 H N N 369 
THR HG23 H N N 370 
THR HXT  H N N 371 
TRP N    N N N 372 
TRP CA   C N S 373 
TRP C    C N N 374 
TRP O    O N N 375 
TRP CB   C N N 376 
TRP CG   C Y N 377 
TRP CD1  C Y N 378 
TRP CD2  C Y N 379 
TRP NE1  N Y N 380 
TRP CE2  C Y N 381 
TRP CE3  C Y N 382 
TRP CZ2  C Y N 383 
TRP CZ3  C Y N 384 
TRP CH2  C Y N 385 
TRP OXT  O N N 386 
TRP H    H N N 387 
TRP H2   H N N 388 
TRP HA   H N N 389 
TRP HB2  H N N 390 
TRP HB3  H N N 391 
TRP HD1  H N N 392 
TRP HE1  H N N 393 
TRP HE3  H N N 394 
TRP HZ2  H N N 395 
TRP HZ3  H N N 396 
TRP HH2  H N N 397 
TRP HXT  H N N 398 
TYR N    N N N 399 
TYR CA   C N S 400 
TYR C    C N N 401 
TYR O    O N N 402 
TYR CB   C N N 403 
TYR CG   C Y N 404 
TYR CD1  C Y N 405 
TYR CD2  C Y N 406 
TYR CE1  C Y N 407 
TYR CE2  C Y N 408 
TYR CZ   C Y N 409 
TYR OH   O N N 410 
TYR OXT  O N N 411 
TYR H    H N N 412 
TYR H2   H N N 413 
TYR HA   H N N 414 
TYR HB2  H N N 415 
TYR HB3  H N N 416 
TYR HD1  H N N 417 
TYR HD2  H N N 418 
TYR HE1  H N N 419 
TYR HE2  H N N 420 
TYR HH   H N N 421 
TYR HXT  H N N 422 
VAL N    N N N 423 
VAL CA   C N S 424 
VAL C    C N N 425 
VAL O    O N N 426 
VAL CB   C N N 427 
VAL CG1  C N N 428 
VAL CG2  C N N 429 
VAL OXT  O N N 430 
VAL H    H N N 431 
VAL H2   H N N 432 
VAL HA   H N N 433 
VAL HB   H N N 434 
VAL HG11 H N N 435 
VAL HG12 H N N 436 
VAL HG13 H N N 437 
VAL HG21 H N N 438 
VAL HG22 H N N 439 
VAL HG23 H N N 440 
VAL HXT  H N N 441 
# 
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  
BMA C1  C2   sing N N 70  
BMA C1  O1   sing N N 71  
BMA C1  O5   sing N N 72  
BMA C1  H1   sing N N 73  
BMA C2  C3   sing N N 74  
BMA C2  O2   sing N N 75  
BMA C2  H2   sing N N 76  
BMA C3  C4   sing N N 77  
BMA C3  O3   sing N N 78  
BMA C3  H3   sing N N 79  
BMA C4  C5   sing N N 80  
BMA C4  O4   sing N N 81  
BMA C4  H4   sing N N 82  
BMA C5  C6   sing N N 83  
BMA C5  O5   sing N N 84  
BMA C5  H5   sing N N 85  
BMA C6  O6   sing N N 86  
BMA C6  H61  sing N N 87  
BMA C6  H62  sing N N 88  
BMA O1  HO1  sing N N 89  
BMA O2  HO2  sing N N 90  
BMA O3  HO3  sing N N 91  
BMA O4  HO4  sing N N 92  
BMA O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
GLN N   CA   sing N N 107 
GLN N   H    sing N N 108 
GLN N   H2   sing N N 109 
GLN CA  C    sing N N 110 
GLN CA  CB   sing N N 111 
GLN CA  HA   sing N N 112 
GLN C   O    doub N N 113 
GLN C   OXT  sing N N 114 
GLN CB  CG   sing N N 115 
GLN CB  HB2  sing N N 116 
GLN CB  HB3  sing N N 117 
GLN CG  CD   sing N N 118 
GLN CG  HG2  sing N N 119 
GLN CG  HG3  sing N N 120 
GLN CD  OE1  doub N N 121 
GLN CD  NE2  sing N N 122 
GLN NE2 HE21 sing N N 123 
GLN NE2 HE22 sing N N 124 
GLN OXT HXT  sing N N 125 
GLU N   CA   sing N N 126 
GLU N   H    sing N N 127 
GLU N   H2   sing N N 128 
GLU CA  C    sing N N 129 
GLU CA  CB   sing N N 130 
GLU CA  HA   sing N N 131 
GLU C   O    doub N N 132 
GLU C   OXT  sing N N 133 
GLU CB  CG   sing N N 134 
GLU CB  HB2  sing N N 135 
GLU CB  HB3  sing N N 136 
GLU CG  CD   sing N N 137 
GLU CG  HG2  sing N N 138 
GLU CG  HG3  sing N N 139 
GLU CD  OE1  doub N N 140 
GLU CD  OE2  sing N N 141 
GLU OE2 HE2  sing N N 142 
GLU OXT HXT  sing N N 143 
GLY N   CA   sing N N 144 
GLY N   H    sing N N 145 
GLY N   H2   sing N N 146 
GLY CA  C    sing N N 147 
GLY CA  HA2  sing N N 148 
GLY CA  HA3  sing N N 149 
GLY C   O    doub N N 150 
GLY C   OXT  sing N N 151 
GLY OXT HXT  sing N N 152 
HIS N   CA   sing N N 153 
HIS N   H    sing N N 154 
HIS N   H2   sing N N 155 
HIS CA  C    sing N N 156 
HIS CA  CB   sing N N 157 
HIS CA  HA   sing N N 158 
HIS C   O    doub N N 159 
HIS C   OXT  sing N N 160 
HIS CB  CG   sing N N 161 
HIS CB  HB2  sing N N 162 
HIS CB  HB3  sing N N 163 
HIS CG  ND1  sing Y N 164 
HIS CG  CD2  doub Y N 165 
HIS ND1 CE1  doub Y N 166 
HIS ND1 HD1  sing N N 167 
HIS CD2 NE2  sing Y N 168 
HIS CD2 HD2  sing N N 169 
HIS CE1 NE2  sing Y N 170 
HIS CE1 HE1  sing N N 171 
HIS NE2 HE2  sing N N 172 
HIS OXT HXT  sing N N 173 
ILE N   CA   sing N N 174 
ILE N   H    sing N N 175 
ILE N   H2   sing N N 176 
ILE CA  C    sing N N 177 
ILE CA  CB   sing N N 178 
ILE CA  HA   sing N N 179 
ILE C   O    doub N N 180 
ILE C   OXT  sing N N 181 
ILE CB  CG1  sing N N 182 
ILE CB  CG2  sing N N 183 
ILE CB  HB   sing N N 184 
ILE CG1 CD1  sing N N 185 
ILE CG1 HG12 sing N N 186 
ILE CG1 HG13 sing N N 187 
ILE CG2 HG21 sing N N 188 
ILE CG2 HG22 sing N N 189 
ILE CG2 HG23 sing N N 190 
ILE CD1 HD11 sing N N 191 
ILE CD1 HD12 sing N N 192 
ILE CD1 HD13 sing N N 193 
ILE OXT HXT  sing N N 194 
LEU N   CA   sing N N 195 
LEU N   H    sing N N 196 
LEU N   H2   sing N N 197 
LEU CA  C    sing N N 198 
LEU CA  CB   sing N N 199 
LEU CA  HA   sing N N 200 
LEU C   O    doub N N 201 
LEU C   OXT  sing N N 202 
LEU CB  CG   sing N N 203 
LEU CB  HB2  sing N N 204 
LEU CB  HB3  sing N N 205 
LEU CG  CD1  sing N N 206 
LEU CG  CD2  sing N N 207 
LEU CG  HG   sing N N 208 
LEU CD1 HD11 sing N N 209 
LEU CD1 HD12 sing N N 210 
LEU CD1 HD13 sing N N 211 
LEU CD2 HD21 sing N N 212 
LEU CD2 HD22 sing N N 213 
LEU CD2 HD23 sing N N 214 
LEU OXT HXT  sing N N 215 
LYS N   CA   sing N N 216 
LYS N   H    sing N N 217 
LYS N   H2   sing N N 218 
LYS CA  C    sing N N 219 
LYS CA  CB   sing N N 220 
LYS CA  HA   sing N N 221 
LYS C   O    doub N N 222 
LYS C   OXT  sing N N 223 
LYS CB  CG   sing N N 224 
LYS CB  HB2  sing N N 225 
LYS CB  HB3  sing N N 226 
LYS CG  CD   sing N N 227 
LYS CG  HG2  sing N N 228 
LYS CG  HG3  sing N N 229 
LYS CD  CE   sing N N 230 
LYS CD  HD2  sing N N 231 
LYS CD  HD3  sing N N 232 
LYS CE  NZ   sing N N 233 
LYS CE  HE2  sing N N 234 
LYS CE  HE3  sing N N 235 
LYS NZ  HZ1  sing N N 236 
LYS NZ  HZ2  sing N N 237 
LYS NZ  HZ3  sing N N 238 
LYS OXT HXT  sing N N 239 
MET N   CA   sing N N 240 
MET N   H    sing N N 241 
MET N   H2   sing N N 242 
MET CA  C    sing N N 243 
MET CA  CB   sing N N 244 
MET CA  HA   sing N N 245 
MET C   O    doub N N 246 
MET C   OXT  sing N N 247 
MET CB  CG   sing N N 248 
MET CB  HB2  sing N N 249 
MET CB  HB3  sing N N 250 
MET CG  SD   sing N N 251 
MET CG  HG2  sing N N 252 
MET CG  HG3  sing N N 253 
MET SD  CE   sing N N 254 
MET CE  HE1  sing N N 255 
MET CE  HE2  sing N N 256 
MET CE  HE3  sing N N 257 
MET OXT HXT  sing N N 258 
NAG C1  C2   sing N N 259 
NAG C1  O1   sing N N 260 
NAG C1  O5   sing N N 261 
NAG C1  H1   sing N N 262 
NAG C2  C3   sing N N 263 
NAG C2  N2   sing N N 264 
NAG C2  H2   sing N N 265 
NAG C3  C4   sing N N 266 
NAG C3  O3   sing N N 267 
NAG C3  H3   sing N N 268 
NAG C4  C5   sing N N 269 
NAG C4  O4   sing N N 270 
NAG C4  H4   sing N N 271 
NAG C5  C6   sing N N 272 
NAG C5  O5   sing N N 273 
NAG C5  H5   sing N N 274 
NAG C6  O6   sing N N 275 
NAG C6  H61  sing N N 276 
NAG C6  H62  sing N N 277 
NAG C7  C8   sing N N 278 
NAG C7  N2   sing N N 279 
NAG C7  O7   doub N N 280 
NAG C8  H81  sing N N 281 
NAG C8  H82  sing N N 282 
NAG C8  H83  sing N N 283 
NAG N2  HN2  sing N N 284 
NAG O1  HO1  sing N N 285 
NAG O3  HO3  sing N N 286 
NAG O4  HO4  sing N N 287 
NAG O6  HO6  sing N N 288 
PHE N   CA   sing N N 289 
PHE N   H    sing N N 290 
PHE N   H2   sing N N 291 
PHE CA  C    sing N N 292 
PHE CA  CB   sing N N 293 
PHE CA  HA   sing N N 294 
PHE C   O    doub N N 295 
PHE C   OXT  sing N N 296 
PHE CB  CG   sing N N 297 
PHE CB  HB2  sing N N 298 
PHE CB  HB3  sing N N 299 
PHE CG  CD1  doub Y N 300 
PHE CG  CD2  sing Y N 301 
PHE CD1 CE1  sing Y N 302 
PHE CD1 HD1  sing N N 303 
PHE CD2 CE2  doub Y N 304 
PHE CD2 HD2  sing N N 305 
PHE CE1 CZ   doub Y N 306 
PHE CE1 HE1  sing N N 307 
PHE CE2 CZ   sing Y N 308 
PHE CE2 HE2  sing N N 309 
PHE CZ  HZ   sing N N 310 
PHE OXT HXT  sing N N 311 
PRO N   CA   sing N N 312 
PRO N   CD   sing N N 313 
PRO N   H    sing N N 314 
PRO CA  C    sing N N 315 
PRO CA  CB   sing N N 316 
PRO CA  HA   sing N N 317 
PRO C   O    doub N N 318 
PRO C   OXT  sing N N 319 
PRO CB  CG   sing N N 320 
PRO CB  HB2  sing N N 321 
PRO CB  HB3  sing N N 322 
PRO CG  CD   sing N N 323 
PRO CG  HG2  sing N N 324 
PRO CG  HG3  sing N N 325 
PRO CD  HD2  sing N N 326 
PRO CD  HD3  sing N N 327 
PRO OXT HXT  sing N N 328 
SER N   CA   sing N N 329 
SER N   H    sing N N 330 
SER N   H2   sing N N 331 
SER CA  C    sing N N 332 
SER CA  CB   sing N N 333 
SER CA  HA   sing N N 334 
SER C   O    doub N N 335 
SER C   OXT  sing N N 336 
SER CB  OG   sing N N 337 
SER CB  HB2  sing N N 338 
SER CB  HB3  sing N N 339 
SER OG  HG   sing N N 340 
SER OXT HXT  sing N N 341 
THR N   CA   sing N N 342 
THR N   H    sing N N 343 
THR N   H2   sing N N 344 
THR CA  C    sing N N 345 
THR CA  CB   sing N N 346 
THR CA  HA   sing N N 347 
THR C   O    doub N N 348 
THR C   OXT  sing N N 349 
THR CB  OG1  sing N N 350 
THR CB  CG2  sing N N 351 
THR CB  HB   sing N N 352 
THR OG1 HG1  sing N N 353 
THR CG2 HG21 sing N N 354 
THR CG2 HG22 sing N N 355 
THR CG2 HG23 sing N N 356 
THR OXT HXT  sing N N 357 
TRP N   CA   sing N N 358 
TRP N   H    sing N N 359 
TRP N   H2   sing N N 360 
TRP CA  C    sing N N 361 
TRP CA  CB   sing N N 362 
TRP CA  HA   sing N N 363 
TRP C   O    doub N N 364 
TRP C   OXT  sing N N 365 
TRP CB  CG   sing N N 366 
TRP CB  HB2  sing N N 367 
TRP CB  HB3  sing N N 368 
TRP CG  CD1  doub Y N 369 
TRP CG  CD2  sing Y N 370 
TRP CD1 NE1  sing Y N 371 
TRP CD1 HD1  sing N N 372 
TRP CD2 CE2  doub Y N 373 
TRP CD2 CE3  sing Y N 374 
TRP NE1 CE2  sing Y N 375 
TRP NE1 HE1  sing N N 376 
TRP CE2 CZ2  sing Y N 377 
TRP CE3 CZ3  doub Y N 378 
TRP CE3 HE3  sing N N 379 
TRP CZ2 CH2  doub Y N 380 
TRP CZ2 HZ2  sing N N 381 
TRP CZ3 CH2  sing Y N 382 
TRP CZ3 HZ3  sing N N 383 
TRP CH2 HH2  sing N N 384 
TRP OXT HXT  sing N N 385 
TYR N   CA   sing N N 386 
TYR N   H    sing N N 387 
TYR N   H2   sing N N 388 
TYR CA  C    sing N N 389 
TYR CA  CB   sing N N 390 
TYR CA  HA   sing N N 391 
TYR C   O    doub N N 392 
TYR C   OXT  sing N N 393 
TYR CB  CG   sing N N 394 
TYR CB  HB2  sing N N 395 
TYR CB  HB3  sing N N 396 
TYR CG  CD1  doub Y N 397 
TYR CG  CD2  sing Y N 398 
TYR CD1 CE1  sing Y N 399 
TYR CD1 HD1  sing N N 400 
TYR CD2 CE2  doub Y N 401 
TYR CD2 HD2  sing N N 402 
TYR CE1 CZ   doub Y N 403 
TYR CE1 HE1  sing N N 404 
TYR CE2 CZ   sing Y N 405 
TYR CE2 HE2  sing N N 406 
TYR CZ  OH   sing N N 407 
TYR OH  HH   sing N N 408 
TYR OXT HXT  sing N N 409 
VAL N   CA   sing N N 410 
VAL N   H    sing N N 411 
VAL N   H2   sing N N 412 
VAL CA  C    sing N N 413 
VAL CA  CB   sing N N 414 
VAL CA  HA   sing N N 415 
VAL C   O    doub N N 416 
VAL C   OXT  sing N N 417 
VAL CB  CG1  sing N N 418 
VAL CB  CG2  sing N N 419 
VAL CB  HB   sing N N 420 
VAL CG1 HG11 sing N N 421 
VAL CG1 HG12 sing N N 422 
VAL CG1 HG13 sing N N 423 
VAL CG2 HG21 sing N N 424 
VAL CG2 HG22 sing N N 425 
VAL CG2 HG23 sing N N 426 
VAL OXT HXT  sing N N 427 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                India 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
4 NAG 1 n 
4 NAG 2 n 
5 NAG 1 n 
5 NAG 2 n 
5 BMA 3 n 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 1 'experimental model' PDB 8TV1 'heavy chain resi 1-136 and light chain resi 1-126'     
2 2 'experimental model' PDB 8TV1 'heavy chain resi 138-238 and light chain resi 128-232' 
3 3 'experimental model' PDB 6T9D 'chain C+D'                                             
# 
_space_group.name_H-M_alt     'P 31' 
_space_group.name_Hall        'P 31' 
_space_group.IT_number        144 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8UWZ 
_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]   0.005961 
_atom_sites.fract_transf_matrix[1][2]   0.003442 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006884 
_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]   0.023529 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 5.96793  ? ? ? 14.89577 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 6.96715  ? ? ? 11.43723 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 7.96527  ? ? ? 9.05267  ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 8.95260  ? ? ? 12.67477 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 15.91112 ? ? ? 10.84690 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU A 1 1   ? 36.13800  38.96500 -31.99300 1.000 145.89870 ?  1   GLU C N   1 
ATOM   2    C CA  . GLU A 1 1   ? 34.73800  38.56400 -31.90000 1.000 145.33234 ?  1   GLU C CA  1 
ATOM   3    C C   . GLU A 1 1   ? 34.10800  39.07800 -30.61000 1.000 143.67532 ?  1   GLU C C   1 
ATOM   4    O O   . GLU A 1 1   ? 33.77900  40.26000 -30.49600 1.000 143.66719 ?  1   GLU C O   1 
ATOM   5    C CB  . GLU A 1 1   ? 34.59700  37.03800 -31.97600 1.000 145.77858 ?  1   GLU C CB  1 
ATOM   6    N N   . VAL A 1 2   ? 33.95500  38.18000 -29.63600 1.000 137.04003 ?  2   VAL C N   1 
ATOM   7    C CA  . VAL A 1 2   ? 33.29500  38.52800 -28.38300 1.000 136.08664 ?  2   VAL C CA  1 
ATOM   8    C C   . VAL A 1 2   ? 34.15700  39.52800 -27.62500 1.000 135.65098 ?  2   VAL C C   1 
ATOM   9    O O   . VAL A 1 2   ? 35.36100  39.31500 -27.42800 1.000 135.65831 ?  2   VAL C O   1 
ATOM   10   C CB  . VAL A 1 2   ? 33.02400  37.27000 -27.54600 1.000 135.54006 ?  2   VAL C CB  1 
ATOM   11   C CG1 . VAL A 1 2   ? 32.16900  37.62000 -26.32600 1.000 135.49233 ?  2   VAL C CG1 1 
ATOM   12   C CG2 . VAL A 1 2   ? 32.37000  36.18700 -28.39800 1.000 136.30857 ?  2   VAL C CG2 1 
ATOM   13   N N   . GLN A 1 3   ? 33.55000  40.64000 -27.21700 1.000 131.82465 ?  3   GLN C N   1 
ATOM   14   C CA  . GLN A 1 3   ? 34.23300  41.66800 -26.44900 1.000 131.84201 ?  3   GLN C CA  1 
ATOM   15   C C   . GLN A 1 3   ? 33.35700  42.12000 -25.29000 1.000 132.55969 ?  3   GLN C C   1 
ATOM   16   O O   . GLN A 1 3   ? 32.13100  42.19000 -25.40400 1.000 133.51198 ?  3   GLN C O   1 
ATOM   17   C CB  . GLN A 1 3   ? 34.58500  42.88400 -27.32300 1.000 132.39348 ?  3   GLN C CB  1 
ATOM   18   N N   . LEU A 1 4   ? 34.00800  42.41000 -24.16400 1.000 134.48032 ?  4   LEU C N   1 
ATOM   19   C CA  . LEU A 1 4   ? 33.37800  43.05300 -23.01800 1.000 136.11202 ?  4   LEU C CA  1 
ATOM   20   C C   . LEU A 1 4   ? 34.01600  44.41600 -22.80700 1.000 136.72957 ?  4   LEU C C   1 
ATOM   21   O O   . LEU A 1 4   ? 35.24400  44.54400 -22.85500 1.000 136.12746 ?  4   LEU C O   1 
ATOM   22   C CB  . LEU A 1 4   ? 33.50900  42.19800 -21.75500 1.000 136.89358 ?  4   LEU C CB  1 
ATOM   23   C CG  . LEU A 1 4   ? 32.49800  41.05700 -21.69100 1.000 137.02380 ?  4   LEU C CG  1 
ATOM   24   C CD1 . LEU A 1 4   ? 32.45700  40.47700 -20.30200 1.000 138.68549 ?  4   LEU C CD1 1 
ATOM   25   C CD2 . LEU A 1 4   ? 31.12600  41.54600 -22.11300 1.000 138.24137 ?  4   LEU C CD2 1 
ATOM   26   N N   . VAL A 1 5   ? 33.18000  45.42900 -22.58900 1.000 133.86202 ?  5   VAL C N   1 
ATOM   27   C CA  . VAL A 1 5   ? 33.61900  46.81100 -22.43000 1.000 134.61629 ?  5   VAL C CA  1 
ATOM   28   C C   . VAL A 1 5   ? 33.03800  47.34400 -21.13000 1.000 137.15868 ?  5   VAL C C   1 
ATOM   29   O O   . VAL A 1 5   ? 31.83900  47.19900 -20.88000 1.000 138.90853 ?  5   VAL C O   1 
ATOM   30   C CB  . VAL A 1 5   ? 33.18900  47.68500 -23.62100 1.000 134.69903 ?  5   VAL C CB  1 
ATOM   31   C CG1 . VAL A 1 5   ? 33.62200  49.11700 -23.39600 1.000 135.72330 ?  5   VAL C CG1 1 
ATOM   32   C CG2 . VAL A 1 5   ? 33.76500  47.13200 -24.91100 1.000 132.90963 ?  5   VAL C CG2 1 
ATOM   33   N N   . GLU A 1 6   ? 33.87900  47.96300 -20.30800 1.000 139.45759 ?  6   GLU C N   1 
ATOM   34   C CA  . GLU A 1 6   ? 33.48000  48.43700 -18.99300 1.000 142.28004 ?  6   GLU C CA  1 
ATOM   35   C C   . GLU A 1 6   ? 33.49700  49.96100 -18.93700 1.000 143.26676 ?  6   GLU C C   1 
ATOM   36   O O   . GLU A 1 6   ? 34.22100  50.62000 -19.68900 1.000 143.18627 ?  6   GLU C O   1 
ATOM   37   C CB  . GLU A 1 6   ? 34.40400  47.86400 -17.91400 1.000 143.05620 ?  6   GLU C CB  1 
ATOM   38   C CG  . GLU A 1 6   ? 34.86100  46.43600 -18.20600 1.000 141.44517 ?  6   GLU C CG  1 
ATOM   39   C CD  . GLU A 1 6   ? 35.28000  45.68100 -16.96200 1.000 143.56377 ?  6   GLU C CD  1 
ATOM   40   O OE1 . GLU A 1 6   ? 35.96200  46.28400 -16.11200 1.000 145.46180 ?  6   GLU C OE1 1 
ATOM   41   O OE2 . GLU A 1 6   ? 34.94400  44.48400 -16.84200 1.000 143.54810 ?  6   GLU C OE2 1 
ATOM   42   N N   . SER A 1 7   ? 32.67900  50.51300 -18.04400 1.000 141.27224 ?  7   SER C N   1 
ATOM   43   C CA  . SER A 1 7   ? 32.66000  51.94800 -17.78900 1.000 142.97178 ?  7   SER C CA  1 
ATOM   44   C C   . SER A 1 7   ? 32.00900  52.19800 -16.43500 1.000 145.87572 ?  7   SER C C   1 
ATOM   45   O O   . SER A 1 7   ? 31.53900  51.27200 -15.76700 1.000 147.40785 ?  7   SER C O   1 
ATOM   46   C CB  . SER A 1 7   ? 31.91300  52.69100 -18.89800 1.000 142.72269 ?  7   SER C CB  1 
ATOM   47   O OG  . SER A 1 7   ? 30.53000  52.77200 -18.60100 1.000 145.16122 ?  7   SER C OG  1 
ATOM   48   N N   . GLY A 1 8   ? 31.95900  53.47400 -16.05300 1.000 142.67358 ?  8   GLY C N   1 
ATOM   49   C CA  . GLY A 1 8   ? 31.42100  53.90200 -14.78200 1.000 144.67040 ?  8   GLY C CA  1 
ATOM   50   C C   . GLY A 1 8   ? 32.46200  54.16500 -13.71600 1.000 148.33861 ?  8   GLY C C   1 
ATOM   51   O O   . GLY A 1 8   ? 32.11300  54.68400 -12.65100 1.000 150.91217 ?  8   GLY C O   1 
ATOM   52   N N   . GLY A 1 9   ? 33.72500  53.84100 -13.97800 1.000 150.26528 ?  9   GLY C N   1 
ATOM   53   C CA  . GLY A 1 9   ? 34.76100  54.01300 -12.98000 1.000 152.86515 ?  9   GLY C CA  1 
ATOM   54   C C   . GLY A 1 9   ? 35.04600  55.46500 -12.65100 1.000 157.57655 ?  9   GLY C C   1 
ATOM   55   O O   . GLY A 1 9   ? 34.78900  56.38400 -13.43300 1.000 158.45511 ?  9   GLY C O   1 
ATOM   56   N N   . GLY A 1 10  ? 35.56700  55.67200 -11.44700 1.000 161.05450 ?  11  GLY C N   1 
ATOM   57   C CA  . GLY A 1 10  ? 35.87000  57.02000 -11.00300 1.000 165.88391 ?  11  GLY C CA  1 
ATOM   58   C C   . GLY A 1 10  ? 36.06700  57.07000 -9.49700  1.000 169.18476 ?  11  GLY C C   1 
ATOM   59   O O   . GLY A 1 10  ? 36.40100  56.06700 -8.86000  1.000 168.69494 ?  11  GLY C O   1 
ATOM   60   N N   . LEU A 1 11  ? 35.83900  58.26500 -8.95900  1.000 172.94556 ?  12  LEU C N   1 
ATOM   61   C CA  . LEU A 1 11  ? 35.97000  58.54700 -7.53900  1.000 176.96954 ?  12  LEU C CA  1 
ATOM   62   C C   . LEU A 1 11  ? 34.58600  58.79300 -6.95600  1.000 176.73030 ?  12  LEU C C   1 
ATOM   63   O O   . LEU A 1 11  ? 33.72800  59.40300 -7.60400  1.000 175.59379 ?  12  LEU C O   1 
ATOM   64   C CB  . LEU A 1 11  ? 36.85500  59.77600 -7.30300  1.000 182.33542 ?  12  LEU C CB  1 
ATOM   65   C CG  . LEU A 1 11  ? 37.04500  60.27100 -5.86600  1.000 187.33478 ?  12  LEU C CG  1 
ATOM   66   C CD1 . LEU A 1 11  ? 37.77500  59.24500 -5.01800  1.000 188.29183 ?  12  LEU C CD1 1 
ATOM   67   C CD2 . LEU A 1 11  ? 37.76400  61.60900 -5.85200  1.000 192.35784 ?  12  LEU C CD2 1 
ATOM   68   N N   . VAL A 1 12  ? 34.37400  58.31200 -5.73500  1.000 178.36407 ?  13  VAL C N   1 
ATOM   69   C CA  . VAL A 1 12  ? 33.12100  58.51100 -5.01500  1.000 179.25977 ?  13  VAL C CA  1 
ATOM   70   C C   . VAL A 1 12  ? 33.46200  58.65500 -3.54100  1.000 184.45313 ?  13  VAL C C   1 
ATOM   71   O O   . VAL A 1 12  ? 34.22200  57.85100 -2.99700  1.000 185.33478 ?  13  VAL C O   1 
ATOM   72   C CB  . VAL A 1 12  ? 32.13200  57.34500 -5.23700  1.000 174.79169 ?  13  VAL C CB  1 
ATOM   73   C CG1 . VAL A 1 12  ? 31.11200  57.27700 -4.10500  1.000 177.24842 ?  13  VAL C CG1 1 
ATOM   74   C CG2 . VAL A 1 12  ? 31.44000  57.46400 -6.59000  1.000 170.54393 ?  13  VAL C CG2 1 
ATOM   75   N N   . GLN A 1 13  ? 32.90300  59.67400 -2.89100  1.000 188.32017 ?  14  GLN C N   1 
ATOM   76   C CA  . GLN A 1 13  ? 33.13300  59.85300 -1.46600  1.000 193.76058 ?  14  GLN C CA  1 
ATOM   77   C C   . GLN A 1 13  ? 32.43200  58.74300 -0.68300  1.000 193.49369 ?  14  GLN C C   1 
ATOM   78   O O   . GLN A 1 13  ? 31.40000  58.22600 -1.11900  1.000 189.96080 ?  14  GLN C O   1 
ATOM   79   C CB  . GLN A 1 13  ? 32.63400  61.22200 -1.00300  1.000 198.15540 ?  14  GLN C CB  1 
ATOM   80   N N   . PRO A 1 14  ? 33.00500  58.32700 0.44600   1.000 197.52327 ?  15  PRO C N   1 
ATOM   81   C CA  . PRO A 1 14  ? 32.34900  57.31600 1.28400   1.000 198.50823 ?  15  PRO C CA  1 
ATOM   82   C C   . PRO A 1 14  ? 30.88300  57.64200 1.52700   1.000 199.19401 ?  15  PRO C C   1 
ATOM   83   O O   . PRO A 1 14  ? 30.53600  58.73100 1.98500   1.000 203.08540 ?  15  PRO C O   1 
ATOM   84   C CB  . PRO A 1 14  ? 33.16400  57.36900 2.57900   1.000 204.93343 ?  15  PRO C CB  1 
ATOM   85   C CG  . PRO A 1 14  ? 34.55000  57.67300 2.09900   1.000 204.74871 ?  15  PRO C CG  1 
ATOM   86   C CD  . PRO A 1 14  ? 34.37700  58.61100 0.91100   1.000 201.35429 ?  15  PRO C CD  1 
ATOM   87   N N   . GLY A 1 15  ? 30.01700  56.68500 1.20600   1.000 195.67869 ?  16  GLY C N   1 
ATOM   88   C CA  . GLY A 1 15  ? 28.58700  56.86600 1.30500   1.000 196.07180 ?  16  GLY C CA  1 
ATOM   89   C C   . GLY A 1 15  ? 27.89600  57.13300 -0.01400  1.000 190.81663 ?  16  GLY C C   1 
ATOM   90   O O   . GLY A 1 15  ? 26.66800  56.99500 -0.08900  1.000 190.29828 ?  16  GLY C O   1 
ATOM   91   N N   . GLY A 1 16  ? 28.64700  57.46300 -1.06100  1.000 187.32869 ?  17  GLY C N   1 
ATOM   92   C CA  . GLY A 1 16  ? 28.06900  57.84100 -2.33100  1.000 183.19463 ?  17  GLY C CA  1 
ATOM   93   C C   . GLY A 1 16  ? 27.72500  56.64600 -3.19500  1.000 177.40829 ?  17  GLY C C   1 
ATOM   94   O O   . GLY A 1 16  ? 27.74600  55.49200 -2.76600  1.000 176.63638 ?  17  GLY C O   1 
ATOM   95   N N   . SER A 1 17  ? 27.39500  56.94300 -4.44900  1.000 173.65124 ?  18  SER C N   1 
ATOM   96   C CA  . SER A 1 17  ? 26.87000  55.94800 -5.37000  1.000 168.30964 ?  18  SER C CA  1 
ATOM   97   C C   . SER A 1 17  ? 27.59300  56.04500 -6.70500  1.000 164.50940 ?  18  SER C C   1 
ATOM   98   O O   . SER A 1 17  ? 28.26500  57.03600 -7.00400  1.000 166.24379 ?  18  SER C O   1 
ATOM   99   C CB  . SER A 1 17  ? 25.36400  56.13700 -5.57900  1.000 168.10045 ?  18  SER C CB  1 
ATOM   100  O OG  . SER A 1 17  ? 24.68800  56.22900 -4.33900  1.000 172.68966 ?  18  SER C OG  1 
ATOM   101  N N   . LEU A 1 18  ? 27.42900  55.00400 -7.52000  1.000 160.92085 ?  19  LEU C N   1 
ATOM   102  C CA  . LEU A 1 18  ? 28.04400  54.93000 -8.84000  1.000 156.86919 ?  19  LEU C CA  1 
ATOM   103  C C   . LEU A 1 18  ? 27.52800  53.69500 -9.56700  1.000 155.53217 ?  19  LEU C C   1 
ATOM   104  O O   . LEU A 1 18  ? 27.36200  52.64400 -8.95100  1.000 157.32356 ?  19  LEU C O   1 
ATOM   105  C CB  . LEU A 1 18  ? 29.56800  54.89100 -8.70600  1.000 157.27475 ?  19  LEU C CB  1 
ATOM   106  C CG  . LEU A 1 18  ? 30.43000  54.94300 -9.96200  1.000 155.04697 ?  19  LEU C CG  1 
ATOM   107  C CD1 . LEU A 1 18  ? 30.15500  56.22500 -10.73800 1.000 156.32793 ?  19  LEU C CD1 1 
ATOM   108  C CD2 . LEU A 1 18  ? 31.89800  54.85200 -9.57300  1.000 157.26660 ?  19  LEU C CD2 1 
ATOM   109  N N   . ARG A 1 19  ? 27.28000  53.78100 -10.86800 1.000 149.60311 ?  20  ARG C N   1 
ATOM   110  C CA  . ARG A 1 19  ? 26.83400  52.61700 -11.62300 1.000 148.94556 ?  20  ARG C CA  1 
ATOM   111  C C   . ARG A 1 19  ? 27.89700  52.23100 -12.63900 1.000 145.23154 ?  20  ARG C C   1 
ATOM   112  O O   . ARG A 1 19  ? 28.33900  53.06900 -13.43300 1.000 143.07922 ?  20  ARG C O   1 
ATOM   113  C CB  . ARG A 1 19  ? 25.48600  52.85900 -12.31000 1.000 149.77008 ?  20  ARG C CB  1 
ATOM   114  C CG  . ARG A 1 19  ? 25.47600  53.89400 -13.41300 1.000 147.99132 ?  20  ARG C CG  1 
ATOM   115  C CD  . ARG A 1 19  ? 24.07500  54.05900 -13.96200 1.000 149.51179 ?  20  ARG C CD  1 
ATOM   116  N NE  . ARG A 1 19  ? 23.53700  52.78300 -14.41800 1.000 149.58990 ?  20  ARG C NE  1 
ATOM   117  C CZ  . ARG A 1 19  ? 22.29600  52.60300 -14.85000 1.000 150.84429 ?  20  ARG C CZ  1 
ATOM   118  N NH1 . ARG A 1 19  ? 21.43300  53.60300 -14.91000 1.000 152.22312 ?  20  ARG C NH1 1 
ATOM   119  N NH2 . ARG A 1 19  ? 21.91400  51.39000 -15.24000 1.000 150.49744 ?  20  ARG C NH2 1 
ATOM   120  N N   . LEU A 1 20  ? 28.33000  50.97600 -12.59100 1.000 141.39038 ?  21  LEU C N   1 
ATOM   121  C CA  . LEU A 1 20  ? 29.19400  50.46100 -13.63800 1.000 137.66792 ?  21  LEU C CA  1 
ATOM   122  C C   . LEU A 1 20  ? 28.36700  49.90800 -14.78200 1.000 136.47787 ?  21  LEU C C   1 
ATOM   123  O O   . LEU A 1 20  ? 27.26100  49.39300 -14.58300 1.000 138.63926 ?  21  LEU C O   1 
ATOM   124  C CB  . LEU A 1 20  ? 30.11100  49.35500 -13.13700 1.000 137.13363 ?  21  LEU C CB  1 
ATOM   125  C CG  . LEU A 1 20  ? 31.00500  49.57900 -11.93600 1.000 139.57972 ?  21  LEU C CG  1 
ATOM   126  C CD1 . LEU A 1 20  ? 31.65900  48.25300 -11.63100 1.000 138.81968 ?  21  LEU C CD1 1 
ATOM   127  C CD2 . LEU A 1 20  ? 32.03200  50.65500 -12.21200 1.000 142.39848 ?  21  LEU C CD2 1 
ATOM   128  N N   . SER A 1 21  ? 28.97500  49.92500 -15.96300 1.000 136.47948 ?  22  SER C N   1 
ATOM   129  C CA  . SER A 1 21  ? 28.34500  49.50000 -17.20100 1.000 135.16178 ?  22  SER C CA  1 
ATOM   130  C C   . SER A 1 21  ? 29.26600  48.49400 -17.86900 1.000 131.54871 ?  22  SER C C   1 
ATOM   131  O O   . SER A 1 21  ? 30.47900  48.71300 -17.94700 1.000 129.40675 ?  22  SER C O   1 
ATOM   132  C CB  . SER A 1 21  ? 28.10300  50.68900 -18.13600 1.000 134.94604 ?  22  SER C CB  1 
ATOM   133  O OG  . SER A 1 21  ? 27.27900  51.65900 -17.51200 1.000 138.21567 ?  22  SER C OG  1 
ATOM   134  N N   . CYS A 1 22  ? 28.69500  47.38500 -18.32400 1.000 136.90078 ?  23  CYS C N   1 
ATOM   135  C CA  . CYS A 1 22  ? 29.43500  46.33200 -19.01300 1.000 133.46011 ?  23  CYS C CA  1 
ATOM   136  C C   . CYS A 1 22  ? 28.67900  45.98600 -20.29000 1.000 132.58243 ?  23  CYS C C   1 
ATOM   137  O O   . CYS A 1 22  ? 27.69800  45.23900 -20.25200 1.000 134.03770 ?  23  CYS C O   1 
ATOM   138  C CB  . CYS A 1 22  ? 29.61200  45.09800 -18.13200 1.000 133.75602 ?  23  CYS C CB  1 
ATOM   139  S SG  . CYS A 1 22  ? 30.40900  43.73400 -19.01900 1.000 129.68555 ?  23  CYS C SG  1 
ATOM   140  N N   . ALA A 1 23  ? 29.12600  46.52900 -21.41300 1.000 129.73018 ?  24  ALA C N   1 
ATOM   141  C CA  . ALA A 1 23  ? 28.49800  46.23400 -22.68600 1.000 129.37404 ?  24  ALA C CA  1 
ATOM   142  C C   . ALA A 1 23  ? 29.21200  45.08200 -23.37200 1.000 126.13207 ?  24  ALA C C   1 
ATOM   143  O O   . ALA A 1 23  ? 30.43200  44.92200 -23.27000 1.000 123.90813 ?  24  ALA C O   1 
ATOM   144  C CB  . ALA A 1 23  ? 28.49400  47.46000 -23.58900 1.000 129.86534 ?  24  ALA C CB  1 
ATOM   145  N N   . ALA A 1 24  ? 28.43500  44.30000 -24.11100 1.000 130.53742 ?  25  ALA C N   1 
ATOM   146  C CA  . ALA A 1 24  ? 28.87800  43.02800 -24.65400 1.000 128.06397 ?  25  ALA C CA  1 
ATOM   147  C C   . ALA A 1 24  ? 28.67600  43.01300 -26.16200 1.000 127.93660 ?  25  ALA C C   1 
ATOM   148  O O   . ALA A 1 24  ? 27.69400  43.56000 -26.67700 1.000 130.52372 ?  25  ALA C O   1 
ATOM   149  C CB  . ALA A 1 24  ? 28.12000  41.87100 -24.00600 1.000 128.90892 ?  25  ALA C CB  1 
ATOM   150  N N   . SER A 1 25  ? 29.60800  42.36200 -26.86400 1.000 131.12236 ?  26  SER C N   1 
ATOM   151  C CA  . SER A 1 25  ? 29.63800  42.35900 -28.32200 1.000 131.39621 ?  26  SER C CA  1 
ATOM   152  C C   . SER A 1 25  ? 29.68000  40.94000 -28.87100 1.000 130.66015 ?  26  SER C C   1 
ATOM   153  O O   . SER A 1 25  ? 30.28900  40.04800 -28.26900 1.000 128.99780 ?  26  SER C O   1 
ATOM   154  C CB  . SER A 1 25  ? 30.85000  43.14300 -28.82600 1.000 130.33684 ?  26  SER C CB  1 
ATOM   155  O OG  . SER A 1 25  ? 31.01700  44.33100 -28.07200 1.000 130.65931 ?  26  SER C OG  1 
ATOM   156  N N   . GLY A 1 26  ? 28.99200  40.72600 -29.99500 1.000 132.63025 ?  27  GLY C N   1 
ATOM   157  C CA  . GLY A 1 26  ? 29.02200  39.43100 -30.65300 1.000 132.54014 ?  27  GLY C CA  1 
ATOM   158  C C   . GLY A 1 26  ? 28.40700  38.34300 -29.81600 1.000 132.28919 ?  27  GLY C C   1 
ATOM   159  O O   . GLY A 1 26  ? 28.64000  37.15600 -30.07000 1.000 131.74840 ?  27  GLY C O   1 
ATOM   160  N N   . PHE A 1 27  ? 27.61100  38.72100 -28.82300 1.000 127.26298 ?  28  PHE C N   1 
ATOM   161  C CA  . PHE A 1 27  ? 27.21200  37.81400 -27.76100 1.000 126.86607 ?  28  PHE C CA  1 
ATOM   162  C C   . PHE A 1 27  ? 26.08900  38.42200 -26.92400 1.000 129.45333 ?  28  PHE C C   1 
ATOM   163  O O   . PHE A 1 27  ? 26.25600  39.49600 -26.33900 1.000 129.90204 ?  28  PHE C O   1 
ATOM   164  C CB  . PHE A 1 27  ? 28.49100  37.53700 -26.95700 1.000 124.09229 ?  28  PHE C CB  1 
ATOM   165  C CG  . PHE A 1 27  ? 28.30100  37.44000 -25.48700 1.000 124.23926 ?  28  PHE C CG  1 
ATOM   166  C CD1 . PHE A 1 27  ? 27.63000  36.38800 -24.90700 1.000 124.79424 ?  28  PHE C CD1 1 
ATOM   167  C CD2 . PHE A 1 27  ? 28.77900  38.44900 -24.68000 1.000 124.37550 ?  28  PHE C CD2 1 
ATOM   168  C CE1 . PHE A 1 27  ? 27.48500  36.35000 -23.54200 1.000 125.71890 ?  28  PHE C CE1 1 
ATOM   169  C CE2 . PHE A 1 27  ? 28.62300  38.41500 -23.32500 1.000 125.46324 ?  28  PHE C CE2 1 
ATOM   170  C CZ  . PHE A 1 27  ? 27.97900  37.36800 -22.74900 1.000 126.29434 ?  28  PHE C CZ  1 
ATOM   171  N N   . ASP A 1 28  ? 24.94300  37.75800 -26.85300 1.000 126.83534 ?  29  ASP C N   1 
ATOM   172  C CA  . ASP A 1 28  ? 23.81200  38.30500 -26.11400 1.000 130.17944 ?  29  ASP C CA  1 
ATOM   173  C C   . ASP A 1 28  ? 23.92400  37.99100 -24.62700 1.000 129.24926 ?  29  ASP C C   1 
ATOM   174  O O   . ASP A 1 28  ? 24.24900  36.86600 -24.23500 1.000 127.12647 ?  29  ASP C O   1 
ATOM   175  C CB  . ASP A 1 28  ? 22.49800  37.76400 -26.66900 1.000 133.59834 ?  29  ASP C CB  1 
ATOM   176  C CG  . ASP A 1 28  ? 22.34400  38.03300 -28.15200 1.000 135.77452 ?  29  ASP C CG  1 
ATOM   177  O OD1 . ASP A 1 28  ? 23.38600  38.18500 -28.82900 1.000 133.10899 ?  29  ASP C OD1 1 
ATOM   178  O OD2 . ASP A 1 28  ? 21.19100  38.11200 -28.63300 1.000 140.56201 ?  29  ASP C OD2 1 
ATOM   179  N N   . LEU A 1 29  ? 23.60500  38.98600 -23.79700 1.000 128.82924 ?  30  LEU C N   1 
ATOM   180  C CA  . LEU A 1 29  ? 23.60000  38.75300 -22.35700 1.000 128.92059 ?  30  LEU C CA  1 
ATOM   181  C C   . LEU A 1 29  ? 22.46000  37.84000 -21.95900 1.000 129.49544 ?  30  LEU C C   1 
ATOM   182  O O   . LEU A 1 29  ? 22.59600  37.05800 -21.01100 1.000 128.10782 ?  30  LEU C O   1 
ATOM   183  C CB  . LEU A 1 29  ? 23.46400  40.07000 -21.59700 1.000 131.51210 ?  30  LEU C CB  1 
ATOM   184  C CG  . LEU A 1 29  ? 24.69700  40.94400 -21.42600 1.000 130.58739 ?  30  LEU C CG  1 
ATOM   185  C CD1 . LEU A 1 29  ? 24.92000  41.69300 -22.70400 1.000 129.71561 ?  30  LEU C CD1 1 
ATOM   186  C CD2 . LEU A 1 29  ? 24.47400  41.92100 -20.27500 1.000 133.54951 ?  30  LEU C CD2 1 
ATOM   187  N N   . TRP A 1 30  ? 21.34300  37.92700 -22.68500 1.000 130.73603 ?  35  TRP C N   1 
ATOM   188  C CA  . TRP A 1 30  ? 20.11900  37.24400 -22.28900 1.000 131.68260 ?  35  TRP C CA  1 
ATOM   189  C C   . TRP A 1 30  ? 20.36700  35.76300 -22.02800 1.000 128.31658 ?  35  TRP C C   1 
ATOM   190  O O   . TRP A 1 30  ? 20.03900  35.24900 -20.95300 1.000 127.42112 ?  35  TRP C O   1 
ATOM   191  C CB  . TRP A 1 30  ? 19.05000  37.44000 -23.36300 1.000 135.52443 ?  35  TRP C CB  1 
ATOM   192  C CG  . TRP A 1 30  ? 17.79400  36.70500 -23.05000 1.000 136.22473 ?  35  TRP C CG  1 
ATOM   193  C CD1 . TRP A 1 30  ? 17.33000  35.57900 -23.66200 1.000 135.88706 ?  35  TRP C CD1 1 
ATOM   194  C CD2 . TRP A 1 30  ? 16.85300  37.01800 -22.01700 1.000 135.90840 ?  35  TRP C CD2 1 
ATOM   195  N NE1 . TRP A 1 30  ? 16.14800  35.17900 -23.08500 1.000 133.36130 ?  35  TRP C NE1 1 
ATOM   196  C CE2 . TRP A 1 30  ? 15.83500  36.04600 -22.07100 1.000 133.30294 ?  35  TRP C CE2 1 
ATOM   197  C CE3 . TRP A 1 30  ? 16.76800  38.02800 -21.05800 1.000 136.21760 ?  35  TRP C CE3 1 
ATOM   198  C CZ2 . TRP A 1 30  ? 14.74800  36.05700 -21.20400 1.000 130.08815 ?  35  TRP C CZ2 1 
ATOM   199  C CZ3 . TRP A 1 30  ? 15.68800  38.03300 -20.19800 1.000 134.40780 ?  35  TRP C CZ3 1 
ATOM   200  C CH2 . TRP A 1 30  ? 14.69300  37.05600 -20.27600 1.000 131.15645 ?  35  TRP C CH2 1 
ATOM   201  N N   . TYR A 1 31  ? 20.98500  35.06500 -22.98600 1.000 138.32870 ?  36  TYR C N   1 
ATOM   202  C CA  . TYR A 1 31  ? 21.24200  33.63500 -22.84500 1.000 135.43929 ?  36  TYR C CA  1 
ATOM   203  C C   . TYR A 1 31  ? 22.57200  33.33100 -22.15700 1.000 132.89705 ?  36  TYR C C   1 
ATOM   204  O O   . TYR A 1 31  ? 23.15600  32.27300 -22.42300 1.000 130.86817 ?  36  TYR C O   1 
ATOM   205  C CB  . TYR A 1 31  ? 21.24300  32.94000 -24.21000 1.000 135.31858 ?  36  TYR C CB  1 
ATOM   206  C CG  . TYR A 1 31  ? 20.18100  33.34600 -25.19700 1.000 139.09972 ?  36  TYR C CG  1 
ATOM   207  C CD1 . TYR A 1 31  ? 18.88900  32.86800 -25.08200 1.000 140.51893 ?  36  TYR C CD1 1 
ATOM   208  C CD2 . TYR A 1 31  ? 20.49400  34.14200 -26.29400 1.000 141.12625 ?  36  TYR C CD2 1 
ATOM   209  C CE1 . TYR A 1 31  ? 17.92100  33.21000 -25.99500 1.000 142.51582 ?  36  TYR C CE1 1 
ATOM   210  C CE2 . TYR A 1 31  ? 19.53400  34.48800 -27.21900 1.000 144.98467 ?  36  TYR C CE2 1 
ATOM   211  C CZ  . TYR A 1 31  ? 18.24800  34.02100 -27.06400 1.000 144.97101 ?  36  TYR C CZ  1 
ATOM   212  O OH  . TYR A 1 31  ? 17.28000  34.36200 -27.98000 1.000 144.89304 ?  36  TYR C OH  1 
ATOM   213  N N   . TYR A 1 32  ? 23.05900  34.18500 -21.26200 1.000 123.17082 ?  37  TYR C N   1 
ATOM   214  C CA  . TYR A 1 32  ? 24.41200  33.98800 -20.73400 1.000 121.81621 ?  37  TYR C CA  1 
ATOM   215  C C   . TYR A 1 32  ? 24.48900  34.55100 -19.31800 1.000 123.44646 ?  37  TYR C C   1 
ATOM   216  O O   . TYR A 1 32  ? 23.46400  34.78900 -18.67300 1.000 125.18126 ?  37  TYR C O   1 
ATOM   217  C CB  . TYR A 1 32  ? 25.45800  34.62400 -21.66100 1.000 121.34921 ?  37  TYR C CB  1 
ATOM   218  C CG  . TYR A 1 32  ? 25.83700  33.78500 -22.86800 1.000 119.67956 ?  37  TYR C CG  1 
ATOM   219  C CD1 . TYR A 1 32  ? 25.13500  33.89500 -24.06200 1.000 120.11748 ?  37  TYR C CD1 1 
ATOM   220  C CD2 . TYR A 1 32  ? 26.91500  32.91300 -22.82700 1.000 117.71568 ?  37  TYR C CD2 1 
ATOM   221  C CE1 . TYR A 1 32  ? 25.47800  33.14600 -25.17100 1.000 118.98049 ?  37  TYR C CE1 1 
ATOM   222  C CE2 . TYR A 1 32  ? 27.27000  32.15800 -23.94300 1.000 116.14742 ?  37  TYR C CE2 1 
ATOM   223  C CZ  . TYR A 1 32  ? 26.54100  32.28000 -25.11000 1.000 116.94606 ?  37  TYR C CZ  1 
ATOM   224  O OH  . TYR A 1 32  ? 26.86000  31.54500 -26.23000 1.000 116.54346 ?  37  TYR C OH  1 
ATOM   225  N N   . SER A 1 33  ? 25.71100  34.77200 -18.83900 1.000 123.30744 ?  38  SER C N   1 
ATOM   226  C CA  . SER A 1 33  ? 25.97000  35.12900 -17.45300 1.000 124.21171 ?  38  SER C CA  1 
ATOM   227  C C   . SER A 1 33  ? 26.96900  36.27000 -17.41400 1.000 124.43714 ?  38  SER C C   1 
ATOM   228  O O   . SER A 1 33  ? 28.02800  36.17700 -18.04200 1.000 123.53382 ?  38  SER C O   1 
ATOM   229  C CB  . SER A 1 33  ? 26.54900  33.93200 -16.70600 1.000 124.25922 ?  38  SER C CB  1 
ATOM   230  O OG  . SER A 1 33  ? 25.78700  32.76300 -16.94300 1.000 123.73841 ?  38  SER C OG  1 
ATOM   231  N N   . ILE A 1 34  ? 26.66300  37.33000 -16.67000 1.000 124.04035 ?  39  ILE C N   1 
ATOM   232  C CA  . ILE A 1 34  ? 27.63200  38.40300 -16.46400 1.000 124.51217 ?  39  ILE C CA  1 
ATOM   233  C C   . ILE A 1 34  ? 27.96400  38.49900 -14.98500 1.000 126.88153 ?  39  ILE C C   1 
ATOM   234  O O   . ILE A 1 34  ? 27.06400  38.59800 -14.14200 1.000 128.92520 ?  39  ILE C O   1 
ATOM   235  C CB  . ILE A 1 34  ? 27.15000  39.75700 -17.01600 1.000 124.78588 ?  39  ILE C CB  1 
ATOM   236  C CG1 . ILE A 1 34  ? 27.22000  39.76700 -18.54500 1.000 123.01372 ?  39  ILE C CG1 1 
ATOM   237  C CG2 . ILE A 1 34  ? 28.00800  40.88000 -16.46400 1.000 125.71903 ?  39  ILE C CG2 1 
ATOM   238  C CD1 . ILE A 1 34  ? 28.45500  39.09100 -19.12000 1.000 121.50084 ?  39  ILE C CD1 1 
ATOM   239  N N   . HIS A 1 35  ? 29.25600  38.45400 -14.67900 1.000 130.27155 ?  40  HIS C N   1 
ATOM   240  C CA  . HIS A 1 35  ? 29.71600  38.62900 -13.31400 1.000 133.39211 ?  40  HIS C CA  1 
ATOM   241  C C   . HIS A 1 35  ? 30.52100  39.90500 -13.17500 1.000 134.23442 ?  40  HIS C C   1 
ATOM   242  O O   . HIS A 1 35  ? 31.13700  40.39400 -14.12600 1.000 132.02419 ?  40  HIS C O   1 
ATOM   243  C CB  . HIS A 1 35  ? 30.59700  37.47100 -12.82900 1.000 134.11439 ?  40  HIS C CB  1 
ATOM   244  C CG  . HIS A 1 35  ? 30.07900  36.11700 -13.16800 1.000 132.59351 ?  40  HIS C CG  1 
ATOM   245  N ND1 . HIS A 1 35  ? 29.60900  35.25100 -12.20700 1.000 134.66757 ?  40  HIS C ND1 1 
ATOM   246  C CD2 . HIS A 1 35  ? 29.96300  35.47000 -14.35000 1.000 129.62472 ?  40  HIS C CD2 1 
ATOM   247  C CE1 . HIS A 1 35  ? 29.21600  34.13100 -12.78400 1.000 132.49373 ?  40  HIS C CE1 1 
ATOM   248  N NE2 . HIS A 1 35  ? 29.41900  34.23900 -14.08400 1.000 129.62671 ?  40  HIS C NE2 1 
ATOM   249  N N   . TRP A 1 36  ? 30.53800  40.39200 -11.94200 1.000 137.57505 ?  41  TRP C N   1 
ATOM   250  C CA  . TRP A 1 36  ? 31.42300  41.45700 -11.51500 1.000 139.11857 ?  41  TRP C CA  1 
ATOM   251  C C   . TRP A 1 36  ? 32.36000  40.81000 -10.51100 1.000 142.09416 ?  41  TRP C C   1 
ATOM   252  O O   . TRP A 1 36  ? 31.90200  40.19000 -9.54100  1.000 145.34321 ?  41  TRP C O   1 
ATOM   253  C CB  . TRP A 1 36  ? 30.65000  42.62200 -10.89200 1.000 141.53384 ?  41  TRP C CB  1 
ATOM   254  C CG  . TRP A 1 36  ? 29.93500  43.46100 -11.91400 1.000 139.12502 ?  41  TRP C CG  1 
ATOM   255  C CD1 . TRP A 1 36  ? 28.58800  43.53600 -12.10500 1.000 139.25858 ?  41  TRP C CD1 1 
ATOM   256  C CD2 . TRP A 1 36  ? 30.52500  44.33900 -12.88400 1.000 136.64834 ?  41  TRP C CD2 1 
ATOM   257  N NE1 . TRP A 1 36  ? 28.30100  44.39300 -13.13900 1.000 137.35288 ?  41  TRP C NE1 1 
ATOM   258  C CE2 . TRP A 1 36  ? 29.47200  44.90200 -13.63200 1.000 135.68291 ?  41  TRP C CE2 1 
ATOM   259  C CE3 . TRP A 1 36  ? 31.83800  44.70100 -13.19400 1.000 135.36370 ?  41  TRP C CE3 1 
ATOM   260  C CZ2 . TRP A 1 36  ? 29.69200  45.80400 -14.66800 1.000 133.63422 ?  41  TRP C CZ2 1 
ATOM   261  C CZ3 . TRP A 1 36  ? 32.05300  45.59800 -14.22400 1.000 133.02301 ?  41  TRP C CZ3 1 
ATOM   262  C CH2 . TRP A 1 36  ? 30.98500  46.13800 -14.94900 1.000 132.22409 ?  41  TRP C CH2 1 
ATOM   263  N N   . VAL A 1 37  ? 33.65400  40.92400 -10.78800 1.000 145.66767 ?  42  VAL C N   1 
ATOM   264  C CA  . VAL A 1 37  ? 34.73800  40.42900 -9.95600  1.000 148.70347 ?  42  VAL C CA  1 
ATOM   265  C C   . VAL A 1 37  ? 35.65000  41.60500 -9.66400  1.000 149.76610 ?  42  VAL C C   1 
ATOM   266  O O   . VAL A 1 37  ? 36.21000  42.20400 -10.58700 1.000 146.60811 ?  42  VAL C O   1 
ATOM   267  C CB  . VAL A 1 37  ? 35.52500  39.30800 -10.65100 1.000 146.60092 ?  42  VAL C CB  1 
ATOM   268  C CG1 . VAL A 1 37  ? 36.58300  38.77600 -9.72100  1.000 150.54662 ?  42  VAL C CG1 1 
ATOM   269  C CG2 . VAL A 1 37  ? 34.59500  38.19500 -11.11500 1.000 144.64628 ?  42  VAL C CG2 1 
ATOM   270  N N   . ARG A 1 38  ? 35.79400  41.94600 -8.39500  1.000 146.27969 ?  43  ARG C N   1 
ATOM   271  C CA  . ARG A 1 38  ? 36.64200  43.06200 -8.01600  1.000 147.30089 ?  43  ARG C CA  1 
ATOM   272  C C   . ARG A 1 38  ? 37.97500  42.54500 -7.49700  1.000 149.65128 ?  43  ARG C C   1 
ATOM   273  O O   . ARG A 1 38  ? 38.03400  41.54400 -6.77600  1.000 153.06632 ?  43  ARG C O   1 
ATOM   274  C CB  . ARG A 1 38  ? 35.94600  43.96300 -6.98800  1.000 150.50225 ?  43  ARG C CB  1 
ATOM   275  C CG  . ARG A 1 38  ? 35.98200  43.47600 -5.55900  1.000 155.85454 ?  43  ARG C CG  1 
ATOM   276  C CD  . ARG A 1 38  ? 34.82600  44.05000 -4.75200  1.000 158.35536 ?  43  ARG C CD  1 
ATOM   277  N NE  . ARG A 1 38  ? 35.10000  44.02200 -3.32000  1.000 163.23694 ?  43  ARG C NE  1 
ATOM   278  C CZ  . ARG A 1 38  ? 34.50700  44.79600 -2.42200  1.000 165.52736 ?  43  ARG C CZ  1 
ATOM   279  N NH1 . ARG A 1 38  ? 33.66600  45.75300 -2.77900  1.000 163.82025 ?  43  ARG C NH1 1 
ATOM   280  N NH2 . ARG A 1 38  ? 34.78800  44.62400 -1.13400  1.000 169.69878 ?  43  ARG C NH2 1 
ATOM   281  N N   . GLN A 1 39  ? 39.04000  43.22000 -7.90000  1.000 156.28674 ?  44  GLN C N   1 
ATOM   282  C CA  . GLN A 1 39  ? 40.40100  42.93500 -7.46500  1.000 158.35801 ?  44  GLN C CA  1 
ATOM   283  C C   . GLN A 1 39  ? 40.80000  44.13900 -6.62200  1.000 160.17632 ?  44  GLN C C   1 
ATOM   284  O O   . GLN A 1 39  ? 40.94700  45.25600 -7.14000  1.000 157.50490 ?  44  GLN C O   1 
ATOM   285  C CB  . GLN A 1 39  ? 41.34700  42.71200 -8.64900  1.000 154.81419 ?  44  GLN C CB  1 
ATOM   286  C CG  . GLN A 1 39  ? 42.81200  42.43800 -8.28600  1.000 156.92865 ?  44  GLN C CG  1 
ATOM   287  C CD  . GLN A 1 39  ? 43.42300  41.29600 -9.08600  1.000 155.85351 ?  44  GLN C CD  1 
ATOM   288  O OE1 . GLN A 1 39  ? 43.77600  40.25000 -8.53200  1.000 159.23140 ?  44  GLN C OE1 1 
ATOM   289  N NE2 . GLN A 1 39  ? 43.56100  41.49600 -10.38900 1.000 151.51835 ?  44  GLN C NE2 1 
ATOM   290  N N   . ALA A 1 40  ? 40.88100  43.91700 -5.31300  1.000 165.59426 ?  45  ALA C N   1 
ATOM   291  C CA  . ALA A 1 40  ? 41.27600  44.93700 -4.36500  1.000 167.68005 ?  45  ALA C CA  1 
ATOM   292  C C   . ALA A 1 40  ? 42.76000  45.26900 -4.52100  1.000 166.89409 ?  45  ALA C C   1 
ATOM   293  O O   . ALA A 1 40  ? 43.53000  44.47400 -5.06600  1.000 166.21310 ?  45  ALA C O   1 
ATOM   294  C CB  . ALA A 1 40  ? 40.96600  44.47500 -2.94400  1.000 172.71606 ?  45  ALA C CB  1 
ATOM   295  N N   . PRO A 1 41  ? 43.17400  46.47000 -4.07500  1.000 173.55621 ?  46  PRO C N   1 
ATOM   296  C CA  . PRO A 1 41  ? 44.57300  46.90200 -4.24000  1.000 172.62694 ?  46  PRO C CA  1 
ATOM   297  C C   . PRO A 1 41  ? 45.59900  45.88200 -3.77600  1.000 175.16623 ?  46  PRO C C   1 
ATOM   298  O O   . PRO A 1 41  ? 45.67900  45.55000 -2.59000  1.000 178.98746 ?  46  PRO C O   1 
ATOM   299  C CB  . PRO A 1 41  ? 44.65100  48.17200 -3.37600  1.000 175.60415 ?  46  PRO C CB  1 
ATOM   300  C CG  . PRO A 1 41  ? 43.29800  48.30900 -2.71100  1.000 176.03004 ?  46  PRO C CG  1 
ATOM   301  C CD  . PRO A 1 41  ? 42.33900  47.56800 -3.57200  1.000 174.00799 ?  46  PRO C CD  1 
ATOM   302  N N   . GLY A 1 42  ? 46.37000  45.36100 -4.72700  1.000 170.34803 ?  47  GLY C N   1 
ATOM   303  C CA  . GLY A 1 42  ? 47.43300  44.42200 -4.43600  1.000 172.97639 ?  47  GLY C CA  1 
ATOM   304  C C   . GLY A 1 42  ? 46.98300  43.08800 -3.89300  1.000 174.66082 ?  47  GLY C C   1 
ATOM   305  O O   . GLY A 1 42  ? 47.82900  42.27400 -3.51600  1.000 177.38186 ?  47  GLY C O   1 
ATOM   306  N N   . LYS A 1 43  ? 45.68100  42.82300 -3.88700  1.000 164.71556 ?  48  LYS C N   1 
ATOM   307  C CA  . LYS A 1 43  ? 45.09900  41.60500 -3.34500  1.000 167.76625 ?  48  LYS C CA  1 
ATOM   308  C C   . LYS A 1 43  ? 44.53000  40.75100 -4.47400  1.000 164.88426 ?  48  LYS C C   1 
ATOM   309  O O   . LYS A 1 43  ? 44.61400  41.09400 -5.65800  1.000 160.45885 ?  48  LYS C O   1 
ATOM   310  C CB  . LYS A 1 43  ? 44.01700  41.94100 -2.31500  1.000 170.21138 ?  48  LYS C CB  1 
ATOM   311  N N   . GLY A 1 44  ? 43.94000  39.62200 -4.09500  1.000 163.57181 ?  49  GLY C N   1 
ATOM   312  C CA  . GLY A 1 44  ? 43.39400  38.69500 -5.06000  1.000 161.20642 ?  49  GLY C CA  1 
ATOM   313  C C   . GLY A 1 44  ? 42.05300  39.14600 -5.60700  1.000 157.49557 ?  49  GLY C C   1 
ATOM   314  O O   . GLY A 1 44  ? 41.54200  40.22300 -5.30000  1.000 156.96349 ?  49  GLY C O   1 
ATOM   315  N N   . LEU A 1 45  ? 41.48100  38.29200 -6.44800  1.000 155.90266 ?  50  LEU C N   1 
ATOM   316  C CA  . LEU A 1 45  ? 40.18600  38.57600 -7.03500  1.000 152.58577 ?  50  LEU C CA  1 
ATOM   317  C C   . LEU A 1 45  ? 39.07600  38.26400 -6.04000  1.000 157.10161 ?  50  LEU C C   1 
ATOM   318  O O   . LEU A 1 45  ? 39.24200  37.49100 -5.09300  1.000 162.46675 ?  50  LEU C O   1 
ATOM   319  C CB  . LEU A 1 45  ? 39.98500  37.77500 -8.32000  1.000 147.51040 ?  50  LEU C CB  1 
ATOM   320  C CG  . LEU A 1 45  ? 40.77200  38.23500 -9.55200  1.000 143.43008 ?  50  LEU C CG  1 
ATOM   321  C CD1 . LEU A 1 45  ? 40.97900  37.08400 -10.52100 1.000 141.02688 ?  50  LEU C CD1 1 
ATOM   322  C CD2 . LEU A 1 45  ? 40.08400  39.40100 -10.24000 1.000 139.79499 ?  50  LEU C CD2 1 
ATOM   323  N N   . GLU A 1 46  ? 37.92800  38.88800 -6.27400  1.000 151.05275 ?  51  GLU C N   1 
ATOM   324  C CA  . GLU A 1 46  ? 36.77200  38.76800 -5.39500  1.000 155.14150 ?  51  GLU C CA  1 
ATOM   325  C C   . GLU A 1 46  ? 35.53600  38.81500 -6.27200  1.000 150.80623 ?  51  GLU C C   1 
ATOM   326  O O   . GLU A 1 46  ? 35.27100  39.84100 -6.90500  1.000 147.24608 ?  51  GLU C O   1 
ATOM   327  C CB  . GLU A 1 46  ? 36.73100  39.88900 -4.35900  1.000 158.68800 ?  51  GLU C CB  1 
ATOM   328  C CG  . GLU A 1 46  ? 35.50800  39.86900 -3.46600  1.000 162.75481 ?  51  GLU C CG  1 
ATOM   329  C CD  . GLU A 1 46  ? 35.37700  41.13400 -2.63600  1.000 164.50326 ?  51  GLU C CD  1 
ATOM   330  O OE1 . GLU A 1 46  ? 36.30400  41.97300 -2.67700  1.000 163.00110 ?  51  GLU C OE1 1 
ATOM   331  O OE2 . GLU A 1 46  ? 34.34900  41.29300 -1.94200  1.000 167.16166 ?  51  GLU C OE2 1 
ATOM   332  N N   . TRP A 1 47  ? 34.79200  37.71300 -6.31700  1.000 156.65442 ?  52  TRP C N   1 
ATOM   333  C CA  . TRP A 1 47  ? 33.52300  37.70800 -7.02800  1.000 152.84671 ?  52  TRP C CA  1 
ATOM   334  C C   . TRP A 1 47  ? 32.55900  38.65700 -6.33400  1.000 155.98530 ?  52  TRP C C   1 
ATOM   335  O O   . TRP A 1 47  ? 32.23800  38.47500 -5.15500  1.000 162.03524 ?  52  TRP C O   1 
ATOM   336  C CB  . TRP A 1 47  ? 32.95700  36.29300 -7.07800  1.000 152.57084 ?  52  TRP C CB  1 
ATOM   337  C CG  . TRP A 1 47  ? 31.55800  36.21400 -7.61400  1.000 149.46347 ?  52  TRP C CG  1 
ATOM   338  C CD1 . TRP A 1 47  ? 31.17700  36.13800 -8.92300  1.000 143.09443 ?  52  TRP C CD1 1 
ATOM   339  C CD2 . TRP A 1 47  ? 30.35000  36.19400 -6.84200  1.000 153.24165 ?  52  TRP C CD2 1 
ATOM   340  N NE1 . TRP A 1 47  ? 29.80400  36.08200 -9.01200  1.000 142.50254 ?  52  TRP C NE1 1 
ATOM   341  C CE2 . TRP A 1 47  ? 29.27600  36.11300 -7.74700  1.000 148.43275 ?  52  TRP C CE2 1 
ATOM   342  C CE3 . TRP A 1 47  ? 30.07400  36.24200 -5.47300  1.000 160.81833 ?  52  TRP C CE3 1 
ATOM   343  C CZ2 . TRP A 1 47  ? 27.95100  36.07900 -7.32500  1.000 150.45811 ?  52  TRP C CZ2 1 
ATOM   344  C CZ3 . TRP A 1 47  ? 28.76000  36.20400 -5.06100  1.000 163.07006 ?  52  TRP C CZ3 1 
ATOM   345  C CH2 . TRP A 1 47  ? 27.71500  36.12900 -5.98100  1.000 157.65775 ?  52  TRP C CH2 1 
ATOM   346  N N   . VAL A 1 48  ? 32.10100  39.67300 -7.06700  1.000 150.30065 ?  53  VAL C N   1 
ATOM   347  C CA  . VAL A 1 48  ? 31.19100  40.66400 -6.50600  1.000 152.67495 ?  53  VAL C CA  1 
ATOM   348  C C   . VAL A 1 48  ? 29.77900  40.13000 -6.64200  1.000 152.44802 ?  53  VAL C C   1 
ATOM   349  O O   . VAL A 1 48  ? 29.06700  39.95700 -5.64600  1.000 157.26971 ?  53  VAL C O   1 
ATOM   350  C CB  . VAL A 1 48  ? 31.31000  42.03200 -7.20200  1.000 149.17681 ?  53  VAL C CB  1 
ATOM   351  C CG1 . VAL A 1 48  ? 30.44000  43.06500 -6.49200  1.000 151.99078 ?  53  VAL C CG1 1 
ATOM   352  C CG2 . VAL A 1 48  ? 32.75200  42.47700 -7.28200  1.000 148.39957 ?  53  VAL C CG2 1 
ATOM   353  N N   . ALA A 1 49  ? 29.37200  39.85400 -7.87500  1.000 149.86443 ?  54  ALA C N   1 
ATOM   354  C CA  . ALA A 1 49  ? 27.99100  39.44500 -8.09100  1.000 149.10278 ?  54  ALA C CA  1 
ATOM   355  C C   . ALA A 1 49  ? 27.86000  38.80000 -9.45600  1.000 143.08166 ?  54  ALA C C   1 
ATOM   356  O O   . ALA A 1 49  ? 28.79800  38.79100 -10.25700 1.000 139.71283 ?  54  ALA C O   1 
ATOM   357  C CB  . ALA A 1 49  ? 27.03400  40.63700 -7.96900  1.000 149.99221 ?  54  ALA C CB  1 
ATOM   358  N N   . TYR A 1 50  ? 26.66100  38.28900 -9.72500  1.000 143.39676 ?  55  TYR C N   1 
ATOM   359  C CA  . TYR A 1 50  ? 26.36100  37.80100 -11.06200 1.000 138.20103 ?  55  TYR C CA  1 
ATOM   360  C C   . TYR A 1 50  ? 24.89900  38.05200 -11.37500 1.000 137.71688 ?  55  TYR C C   1 
ATOM   361  O O   . TYR A 1 50  ? 24.06400  38.22100 -10.48300 1.000 141.12594 ?  55  TYR C O   1 
ATOM   362  C CB  . TYR A 1 50  ? 26.70400  36.30700 -11.24200 1.000 136.54378 ?  55  TYR C CB  1 
ATOM   363  C CG  . TYR A 1 50  ? 25.81100  35.31000 -10.51000 1.000 138.57792 ?  55  TYR C CG  1 
ATOM   364  C CD1 . TYR A 1 50  ? 24.45100  35.19900 -10.78800 1.000 137.70607 ?  55  TYR C CD1 1 
ATOM   365  C CD2 . TYR A 1 50  ? 26.34700  34.45100 -9.56400  1.000 141.46770 ?  55  TYR C CD2 1 
ATOM   366  C CE1 . TYR A 1 50  ? 23.65100  34.29500 -10.12000 1.000 139.39232 ?  55  TYR C CE1 1 
ATOM   367  C CE2 . TYR A 1 50  ? 25.55600  33.54200 -8.89200  1.000 143.37680 ?  55  TYR C CE2 1 
ATOM   368  C CZ  . TYR A 1 50  ? 24.20900  33.46400 -9.17800  1.000 142.12533 ?  55  TYR C CZ  1 
ATOM   369  O OH  . TYR A 1 50  ? 23.41700  32.55800 -8.51100  1.000 143.73513 ?  55  TYR C OH  1 
ATOM   370  N N   . ILE A 1 51  ? 24.60700  38.07300 -12.66700 1.000 131.33486 ?  56  ILE C N   1 
ATOM   371  C CA  . ILE A 1 51  ? 23.23500  38.06700 -13.14500 1.000 130.57263 ?  56  ILE C CA  1 
ATOM   372  C C   . ILE A 1 51  ? 23.16300  37.09200 -14.30800 1.000 127.25423 ?  56  ILE C C   1 
ATOM   373  O O   . ILE A 1 51  ? 24.07500  37.02400 -15.14600 1.000 125.09381 ?  56  ILE C O   1 
ATOM   374  C CB  . ILE A 1 51  ? 22.72900  39.47300 -13.53900 1.000 130.78521 ?  56  ILE C CB  1 
ATOM   375  C CG1 . ILE A 1 51  ? 21.29500  39.37900 -14.05700 1.000 129.92607 ?  56  ILE C CG1 1 
ATOM   376  C CG2 . ILE A 1 51  ? 23.63300  40.12800 -14.58000 1.000 128.50098 ?  56  ILE C CG2 1 
ATOM   377  C CD1 . ILE A 1 51  ? 20.65400  40.72500 -14.32800 1.000 130.37235 ?  56  ILE C CD1 1 
ATOM   378  N N   . TYR A 1 52  ? 22.08600  36.30100 -14.32100 1.000 129.57674 ?  57  TYR C N   1 
ATOM   379  C CA  . TYR A 1 52  ? 21.83900  35.27500 -15.33400 1.000 127.04169 ?  57  TYR C CA  1 
ATOM   380  C C   . TYR A 1 52  ? 20.49700  35.59500 -15.97800 1.000 125.76308 ?  57  TYR C C   1 
ATOM   381  O O   . TYR A 1 52  ? 19.45300  35.08100 -15.54600 1.000 125.92105 ?  57  TYR C O   1 
ATOM   382  C CB  . TYR A 1 52  ? 21.83200  33.86600 -14.74000 1.000 127.22925 ?  57  TYR C CB  1 
ATOM   383  C CG  . TYR A 1 52  ? 23.20200  33.29900 -14.43100 1.000 127.10817 ?  57  TYR C CG  1 
ATOM   384  C CD1 . TYR A 1 52  ? 24.20200  34.10000 -13.90900 1.000 128.35803 ?  57  TYR C CD1 1 
ATOM   385  C CD2 . TYR A 1 52  ? 23.51300  31.97400 -14.70900 1.000 125.85908 ?  57  TYR C CD2 1 
ATOM   386  C CE1 . TYR A 1 52  ? 25.45200  33.59600 -13.62100 1.000 128.38903 ?  57  TYR C CE1 1 
ATOM   387  C CE2 . TYR A 1 52  ? 24.77300  31.46100 -14.43600 1.000 125.80170 ?  57  TYR C CE2 1 
ATOM   388  C CZ  . TYR A 1 52  ? 25.73700  32.28100 -13.89700 1.000 127.00061 ?  57  TYR C CZ  1 
ATOM   389  O OH  . TYR A 1 52  ? 26.99000  31.78800 -13.62700 1.000 127.06114 ?  57  TYR C OH  1 
ATOM   390  N N   . PRO A 1 53  ? 20.48200  36.45500 -17.00600 1.000 125.28442 ?  58  PRO C N   1 
ATOM   391  C CA  . PRO A 1 53  ? 19.22600  37.01400 -17.52900 1.000 124.77925 ?  58  PRO C CA  1 
ATOM   392  C C   . PRO A 1 53  ? 18.11500  36.00100 -17.78600 1.000 123.53719 ?  58  PRO C C   1 
ATOM   393  O O   . PRO A 1 53  ? 17.01700  36.13800 -17.24300 1.000 123.74417 ?  58  PRO C O   1 
ATOM   394  C CB  . PRO A 1 53  ? 19.68600  37.68200 -18.82900 1.000 123.76207 ?  58  PRO C CB  1 
ATOM   395  C CG  . PRO A 1 53  ? 21.04900  38.15200 -18.51800 1.000 124.36588 ?  58  PRO C CG  1 
ATOM   396  C CD  . PRO A 1 53  ? 21.65700  37.14600 -17.56800 1.000 124.87711 ?  58  PRO C CD  1 
ATOM   397  N N   . SER A 1 54  ? 18.38300  34.97000 -18.58800 1.000 127.95979 ?  59  SER C N   1 
ATOM   398  C CA  . SER A 1 54  ? 17.30700  34.05000 -18.94700 1.000 126.45535 ?  59  SER C CA  1 
ATOM   399  C C   . SER A 1 54  ? 16.86800  33.15400 -17.79700 1.000 126.69109 ?  59  SER C C   1 
ATOM   400  O O   . SER A 1 54  ? 15.97700  32.32200 -18.00500 1.000 124.69688 ?  59  SER C O   1 
ATOM   401  C CB  . SER A 1 54  ? 17.73300  33.17400 -20.12500 1.000 125.37256 ?  59  SER C CB  1 
ATOM   402  O OG  . SER A 1 54  ? 18.98500  32.55100 -19.88900 1.000 125.82676 ?  59  SER C OG  1 
ATOM   403  N N   . TYR A 1 55  ? 17.45400  33.30300 -16.60500 1.000 120.55948 ?  62  TYR C N   1 
ATOM   404  C CA  . TYR A 1 55  ? 17.12900  32.48800 -15.44100 1.000 121.61152 ?  62  TYR C CA  1 
ATOM   405  C C   . TYR A 1 55  ? 16.51000  33.28500 -14.30800 1.000 123.88368 ?  62  TYR C C   1 
ATOM   406  O O   . TYR A 1 55  ? 15.84600  32.69100 -13.45100 1.000 124.56041 ?  62  TYR C O   1 
ATOM   407  C CB  . TYR A 1 55  ? 18.38500  31.79200 -14.88300 1.000 122.84761 ?  62  TYR C CB  1 
ATOM   408  C CG  . TYR A 1 55  ? 19.09700  30.86800 -15.84600 1.000 121.00001 ?  62  TYR C CG  1 
ATOM   409  C CD1 . TYR A 1 55  ? 19.70500  31.36600 -16.98500 1.000 119.69056 ?  62  TYR C CD1 1 
ATOM   410  C CD2 . TYR A 1 55  ? 19.20200  29.51100 -15.59900 1.000 120.88487 ?  62  TYR C CD2 1 
ATOM   411  C CE1 . TYR A 1 55  ? 20.36300  30.54500 -17.87200 1.000 118.44100 ?  62  TYR C CE1 1 
ATOM   412  C CE2 . TYR A 1 55  ? 19.87100  28.68200 -16.48100 1.000 119.34440 ?  62  TYR C CE2 1 
ATOM   413  C CZ  . TYR A 1 55  ? 20.44800  29.20300 -17.62200 1.000 118.22353 ?  62  TYR C CZ  1 
ATOM   414  O OH  . TYR A 1 55  ? 21.11700  28.39200 -18.51800 1.000 117.33775 ?  62  TYR C OH  1 
ATOM   415  N N   . GLY A 1 56  ? 16.70100  34.59900 -14.27900 1.000 123.15982 ?  63  GLY C N   1 
ATOM   416  C CA  . GLY A 1 56  ? 16.26000  35.38400 -13.14800 1.000 125.91535 ?  63  GLY C CA  1 
ATOM   417  C C   . GLY A 1 56  ? 17.13000  35.19300 -11.92800 1.000 129.86292 ?  63  GLY C C   1 
ATOM   418  O O   . GLY A 1 56  ? 16.61000  35.09800 -10.80800 1.000 132.66077 ?  63  GLY C O   1 
ATOM   419  N N   . TYR A 1 57  ? 18.44700  35.13700 -12.10700 1.000 132.49010 ?  64  TYR C N   1 
ATOM   420  C CA  . TYR A 1 57  ? 19.37300  34.88900 -11.01200 1.000 135.77083 ?  64  TYR C CA  1 
ATOM   421  C C   . TYR A 1 57  ? 20.16000  36.16400 -10.76400 1.000 137.85358 ?  64  TYR C C   1 
ATOM   422  O O   . TYR A 1 57  ? 20.89000  36.63100 -11.64800 1.000 135.40902 ?  64  TYR C O   1 
ATOM   423  C CB  . TYR A 1 57  ? 20.33600  33.74400 -11.32700 1.000 133.76844 ?  64  TYR C CB  1 
ATOM   424  C CG  . TYR A 1 57  ? 19.70500  32.38400 -11.50700 1.000 131.90005 ?  64  TYR C CG  1 
ATOM   425  C CD1 . TYR A 1 57  ? 18.37500  32.15100 -11.18800 1.000 132.16200 ?  64  TYR C CD1 1 
ATOM   426  C CD2 . TYR A 1 57  ? 20.44300  31.33400 -12.02600 1.000 129.86509 ?  64  TYR C CD2 1 
ATOM   427  C CE1 . TYR A 1 57  ? 17.80800  30.90200 -11.36900 1.000 130.19811 ?  64  TYR C CE1 1 
ATOM   428  C CE2 . TYR A 1 57  ? 19.88100  30.09300 -12.21500 1.000 128.37647 ?  64  TYR C CE2 1 
ATOM   429  C CZ  . TYR A 1 57  ? 18.57100  29.87800 -11.88400 1.000 128.40948 ?  64  TYR C CZ  1 
ATOM   430  O OH  . TYR A 1 57  ? 18.03000  28.63000 -12.07600 1.000 126.72070 ?  64  TYR C OH  1 
ATOM   431  N N   . THR A 1 58  ? 20.03900  36.69100 -9.54600  1.000 135.97019 ?  65  THR C N   1 
ATOM   432  C CA  . THR A 1 58  ? 20.77300  37.86100 -9.07500  1.000 138.73182 ?  65  THR C CA  1 
ATOM   433  C C   . THR A 1 58  ? 21.25500  37.42700 -7.70000  1.000 144.29312 ?  65  THR C C   1 
ATOM   434  O O   . THR A 1 58  ? 20.54800  37.57800 -6.70000  1.000 148.44514 ?  65  THR C O   1 
ATOM   435  C CB  . THR A 1 58  ? 19.91000  39.13900 -8.98900  1.000 139.65579 ?  65  THR C CB  1 
ATOM   436  O OG1 . THR A 1 58  ? 18.75900  38.90300 -8.16800  1.000 141.62631 ?  65  THR C OG1 1 
ATOM   437  C CG2 . THR A 1 58  ? 19.44100  39.57700 -10.36400 1.000 134.78635 ?  65  THR C CG2 1 
ATOM   438  N N   . TYR A 1 59  ? 22.45100  36.86500 -7.65500  1.000 144.73580 ?  66  TYR C N   1 
ATOM   439  C CA  . TYR A 1 59  ? 23.10100  36.53800 -6.40300  1.000 150.61037 ?  66  TYR C CA  1 
ATOM   440  C C   . TYR A 1 59  ? 24.33500  37.41700 -6.30900  1.000 151.58880 ?  66  TYR C C   1 
ATOM   441  O O   . TYR A 1 59  ? 25.10100  37.53700 -7.27800  1.000 146.71464 ?  66  TYR C O   1 
ATOM   442  C CB  . TYR A 1 59  ? 23.44400  35.04500 -6.35600  1.000 149.35498 ?  66  TYR C CB  1 
ATOM   443  C CG  . TYR A 1 59  ? 24.19600  34.54100 -5.14500  1.000 155.23495 ?  66  TYR C CG  1 
ATOM   444  C CD1 . TYR A 1 59  ? 23.72000  34.76000 -3.85800  1.000 162.28182 ?  66  TYR C CD1 1 
ATOM   445  C CD2 . TYR A 1 59  ? 25.35600  33.79100 -5.29800  1.000 153.52396 ?  66  TYR C CD2 1 
ATOM   446  C CE1 . TYR A 1 59  ? 24.39900  34.27500 -2.76000  1.000 167.46000 ?  66  TYR C CE1 1 
ATOM   447  C CE2 . TYR A 1 59  ? 26.03700  33.30700 -4.21100  1.000 158.88370 ?  66  TYR C CE2 1 
ATOM   448  C CZ  . TYR A 1 59  ? 25.55500  33.54900 -2.94800  1.000 165.83935 ?  66  TYR C CZ  1 
ATOM   449  O OH  . TYR A 1 59  ? 26.24200  33.06000 -1.86800  1.000 170.43532 ?  66  TYR C OH  1 
ATOM   450  N N   . TYR A 1 60  ? 24.51800  38.02600 -5.14500  1.000 154.80486 ?  67  TYR C N   1 
ATOM   451  C CA  . TYR A 1 60  ? 25.63200  38.91100 -4.87200  1.000 155.80620 ?  67  TYR C CA  1 
ATOM   452  C C   . TYR A 1 60  ? 26.41600  38.31100 -3.72000  1.000 161.88585 ?  67  TYR C C   1 
ATOM   453  O O   . TYR A 1 60  ? 25.91000  37.46600 -2.97800  1.000 166.04438 ?  67  TYR C O   1 
ATOM   454  C CB  . TYR A 1 60  ? 25.19300  40.34300 -4.49500  1.000 156.39407 ?  67  TYR C CB  1 
ATOM   455  C CG  . TYR A 1 60  ? 23.90800  40.86200 -5.12400  1.000 153.20543 ?  67  TYR C CG  1 
ATOM   456  C CD1 . TYR A 1 60  ? 23.89000  41.33800 -6.43000  1.000 147.75785 ?  67  TYR C CD1 1 
ATOM   457  C CD2 . TYR A 1 60  ? 22.72600  40.92300 -4.39100  1.000 155.32786 ?  67  TYR C CD2 1 
ATOM   458  C CE1 . TYR A 1 60  ? 22.72700  41.83300 -6.99900  1.000 145.30335 ?  67  TYR C CE1 1 
ATOM   459  C CE2 . TYR A 1 60  ? 21.55700  41.41700 -4.95500  1.000 152.15089 ?  67  TYR C CE2 1 
ATOM   460  C CZ  . TYR A 1 60  ? 21.56600  41.87000 -6.26000  1.000 147.49737 ?  67  TYR C CZ  1 
ATOM   461  O OH  . TYR A 1 60  ? 20.41300  42.36000 -6.83200  1.000 144.64933 ?  67  TYR C OH  1 
ATOM   462  N N   . ALA A 1 61  ? 27.66400  38.73800 -3.58300  1.000 159.14995 ?  68  ALA C N   1 
ATOM   463  C CA  . ALA A 1 61  ? 28.41400  38.31500 -2.41900  1.000 164.91472 ?  68  ALA C CA  1 
ATOM   464  C C   . ALA A 1 61  ? 27.83500  38.99300 -1.18200  1.000 168.33162 ?  68  ALA C C   1 
ATOM   465  O O   . ALA A 1 61  ? 27.11300  39.98900 -1.26600  1.000 166.29899 ?  68  ALA C O   1 
ATOM   466  C CB  . ALA A 1 61  ? 29.89800  38.63900 -2.58400  1.000 163.72814 ?  68  ALA C CB  1 
ATOM   467  N N   . ASP A 1 62  ? 28.15100  38.43000 -0.02200  1.000 171.45761 ?  69  ASP C N   1 
ATOM   468  C CA  . ASP A 1 62  ? 27.57300  38.93700 1.21300   1.000 173.18636 ?  69  ASP C CA  1 
ATOM   469  C C   . ASP A 1 62  ? 28.10400  40.32000 1.58800   1.000 172.11309 ?  69  ASP C C   1 
ATOM   470  O O   . ASP A 1 62  ? 27.37800  41.10200 2.21300   1.000 171.67679 ?  69  ASP C O   1 
ATOM   471  C CB  . ASP A 1 62  ? 27.77400  37.91300 2.32900   1.000 176.62052 ?  69  ASP C CB  1 
ATOM   472  C CG  . ASP A 1 62  ? 29.13200  37.24800 2.28600   1.000 178.20483 ?  69  ASP C CG  1 
ATOM   473  O OD1 . ASP A 1 62  ? 29.99600  37.65600 1.47600   1.000 176.52029 ?  69  ASP C OD1 1 
ATOM   474  O OD2 . ASP A 1 62  ? 29.31700  36.28800 3.06500   1.000 180.50428 ?  69  ASP C OD2 1 
ATOM   475  N N   . SER A 1 63  ? 29.35400  40.64600 1.23900   1.000 170.27246 ?  70  SER C N   1 
ATOM   476  C CA  . SER A 1 63  ? 29.90400  41.94500 1.63300   1.000 169.39016 ?  70  SER C CA  1 
ATOM   477  C C   . SER A 1 63  ? 29.10900  43.10000 1.03000   1.000 166.26911 ?  70  SER C C   1 
ATOM   478  O O   . SER A 1 63  ? 28.92500  44.13900 1.67500   1.000 166.35996 ?  70  SER C O   1 
ATOM   479  C CB  . SER A 1 63  ? 31.37600  42.04800 1.23300   1.000 168.56477 ?  70  SER C CB  1 
ATOM   480  O OG  . SER A 1 63  ? 31.55700  41.89700 -0.16600  1.000 165.08457 ?  70  SER C OG  1 
ATOM   481  N N   . VAL A 1 64  ? 28.63800  42.94900 -0.20900  1.000 167.30721 ?  71  VAL C N   1 
ATOM   482  C CA  . VAL A 1 64  ? 27.91500  44.02400 -0.87500  1.000 164.05654 ?  71  VAL C CA  1 
ATOM   483  C C   . VAL A 1 64  ? 26.41900  43.78500 -0.90400  1.000 163.72229 ?  71  VAL C C   1 
ATOM   484  O O   . VAL A 1 64  ? 25.68600  44.58600 -1.50100  1.000 160.97976 ?  71  VAL C O   1 
ATOM   485  C CB  . VAL A 1 64  ? 28.43600  44.24700 -2.30500  1.000 159.66710 ?  71  VAL C CB  1 
ATOM   486  C CG1 . VAL A 1 64  ? 29.93400  44.45900 -2.28700  1.000 159.49505 ?  71  VAL C CG1 1 
ATOM   487  C CG2 . VAL A 1 64  ? 28.05800  43.07800 -3.19000  1.000 157.80266 ?  71  VAL C CG2 1 
ATOM   488  N N   . LYS A 1 65  ? 25.94200  42.69500 -0.30300  1.000 162.11065 ?  72  LYS C N   1 
ATOM   489  C CA  . LYS A 1 65  ? 24.52900  42.35700 -0.39500  1.000 161.34903 ?  72  LYS C CA  1 
ATOM   490  C C   . LYS A 1 65  ? 23.68800  43.48700 0.18200   1.000 161.48923 ?  72  LYS C C   1 
ATOM   491  O O   . LYS A 1 65  ? 23.93800  43.96300 1.29300   1.000 164.23626 ?  72  LYS C O   1 
ATOM   492  C CB  . LYS A 1 65  ? 24.24700  41.04900 0.34400   1.000 164.63702 ?  72  LYS C CB  1 
ATOM   493  N N   . GLY A 1 66  ? 22.67800  43.90000 -0.57000  1.000 170.01173 ?  74  GLY C N   1 
ATOM   494  C CA  . GLY A 1 66  ? 21.89300  45.07200 -0.19300  1.000 168.83157 ?  74  GLY C CA  1 
ATOM   495  C C   . GLY A 1 66  ? 22.49700  46.38800 -0.63900  1.000 167.76337 ?  74  GLY C C   1 
ATOM   496  O O   . GLY A 1 66  ? 21.78500  47.24700 -1.16800  1.000 165.51080 ?  74  GLY C O   1 
ATOM   497  N N   . ARG A 1 67  ? 23.80100  46.58100 -0.42100  1.000 162.83316 ?  75  ARG C N   1 
ATOM   498  C CA  . ARG A 1 67  ? 24.43600  47.80500 -0.90000  1.000 161.64132 ?  75  ARG C CA  1 
ATOM   499  C C   . ARG A 1 67  ? 24.44500  47.86300 -2.42100  1.000 158.03832 ?  75  ARG C C   1 
ATOM   500  O O   . ARG A 1 67  ? 24.13300  48.90400 -3.01000  1.000 156.25639 ?  75  ARG C O   1 
ATOM   501  C CB  . ARG A 1 67  ? 25.86400  47.91800 -0.37000  1.000 163.55583 ?  75  ARG C CB  1 
ATOM   502  C CG  . ARG A 1 67  ? 26.07000  47.44600 1.05100   1.000 166.99972 ?  75  ARG C CG  1 
ATOM   503  C CD  . ARG A 1 67  ? 27.30500  48.10800 1.65400   1.000 168.45302 ?  75  ARG C CD  1 
ATOM   504  N NE  . ARG A 1 67  ? 28.52900  47.34700 1.42600   1.000 168.85210 ?  75  ARG C NE  1 
ATOM   505  C CZ  . ARG A 1 67  ? 29.61000  47.82500 0.82500   1.000 167.32446 ?  75  ARG C CZ  1 
ATOM   506  N NH1 . ARG A 1 67  ? 29.65400  49.06400 0.36200   1.000 165.45802 ?  75  ARG C NH1 1 
ATOM   507  N NH2 . ARG A 1 67  ? 30.67600  47.04100 0.68700   1.000 167.60813 ?  75  ARG C NH2 1 
ATOM   508  N N   . PHE A 1 68  ? 24.77300  46.75600 -3.07500  1.000 162.44172 ?  76  PHE C N   1 
ATOM   509  C CA  . PHE A 1 68  ? 24.88500  46.73400 -4.52400  1.000 157.27211 ?  76  PHE C CA  1 
ATOM   510  C C   . PHE A 1 68  ? 23.69400  46.01900 -5.13200  1.000 155.50444 ?  76  PHE C C   1 
ATOM   511  O O   . PHE A 1 68  ? 22.99000  45.24900 -4.47400  1.000 157.67204 ?  76  PHE C O   1 
ATOM   512  C CB  . PHE A 1 68  ? 26.16900  46.04100 -5.00600  1.000 154.54873 ?  76  PHE C CB  1 
ATOM   513  C CG  . PHE A 1 68  ? 27.44000  46.75600 -4.64400  1.000 155.32288 ?  76  PHE C CG  1 
ATOM   514  C CD1 . PHE A 1 68  ? 27.43300  47.88400 -3.84100  1.000 158.60627 ?  76  PHE C CD1 1 
ATOM   515  C CD2 . PHE A 1 68  ? 28.65100  46.30900 -5.14800  1.000 152.48459 ?  76  PHE C CD2 1 
ATOM   516  C CE1 . PHE A 1 68  ? 28.60800  48.53400 -3.52300  1.000 159.22045 ?  76  PHE C CE1 1 
ATOM   517  C CE2 . PHE A 1 68  ? 29.82900  46.95700 -4.83600  1.000 153.10956 ?  76  PHE C CE2 1 
ATOM   518  C CZ  . PHE A 1 68  ? 29.80600  48.07100 -4.02000  1.000 156.52307 ?  76  PHE C CZ  1 
ATOM   519  N N   . THR A 1 69  ? 23.48600  46.28400 -6.41600  1.000 150.44499 ?  77  THR C N   1 
ATOM   520  C CA  . THR A 1 69  ? 22.47700  45.54500 -7.15800  1.000 148.11061 ?  77  THR C CA  1 
ATOM   521  C C   . THR A 1 69  ? 22.97100  45.39800 -8.58700  1.000 143.33747 ?  77  THR C C   1 
ATOM   522  O O   . THR A 1 69  ? 23.37800  46.38400 -9.21600  1.000 141.85176 ?  77  THR C O   1 
ATOM   523  C CB  . THR A 1 69  ? 21.10600  46.23000 -7.11400  1.000 149.04315 ?  77  THR C CB  1 
ATOM   524  O OG1 . THR A 1 69  ? 20.55400  46.09700 -5.79700  1.000 153.02845 ?  77  THR C OG1 1 
ATOM   525  C CG2 . THR A 1 69  ? 20.16000  45.57100 -8.10600  1.000 145.77994 ?  77  THR C CG2 1 
ATOM   526  N N   . ILE A 1 70  ? 22.97100  44.16000 -9.07300  1.000 141.44976 ?  78  ILE C N   1 
ATOM   527  C CA  . ILE A 1 70  ? 23.32600  43.86600 -10.45300 1.000 136.90796 ?  78  ILE C CA  1 
ATOM   528  C C   . ILE A 1 70  ? 22.04100  43.84200 -11.26100 1.000 135.59202 ?  78  ILE C C   1 
ATOM   529  O O   . ILE A 1 70  ? 20.95700  43.53400 -10.74900 1.000 137.13911 ?  78  ILE C O   1 
ATOM   530  C CB  . ILE A 1 70  ? 24.11000  42.53900 -10.57700 1.000 134.59271 ?  78  ILE C CB  1 
ATOM   531  C CG1 . ILE A 1 70  ? 24.87000  42.49600 -11.90200 1.000 130.19614 ?  78  ILE C CG1 1 
ATOM   532  C CG2 . ILE A 1 70  ? 23.19700  41.32500 -10.44300 1.000 134.40543 ?  78  ILE C CG2 1 
ATOM   533  C CD1 . ILE A 1 70  ? 25.87100  41.38100 -11.98200 1.000 127.85354 ?  78  ILE C CD1 1 
ATOM   534  N N   . SER A 1 71  ? 22.16200  44.18000 -12.53700 1.000 126.05168 ?  79  SER C N   1 
ATOM   535  C CA  . SER A 1 71  ? 20.99900  44.32800 -13.39900 1.000 124.96821 ?  79  SER C CA  1 
ATOM   536  C C   . SER A 1 71  ? 21.48200  44.28800 -14.83700 1.000 121.99343 ?  79  SER C C   1 
ATOM   537  O O   . SER A 1 71  ? 22.68200  44.29000 -15.10600 1.000 120.41292 ?  79  SER C O   1 
ATOM   538  C CB  . SER A 1 71  ? 20.24400  45.62800 -13.09900 1.000 127.35386 ?  79  SER C CB  1 
ATOM   539  O OG  . SER A 1 71  ? 21.01400  46.76000 -13.47000 1.000 127.48230 ?  79  SER C OG  1 
ATOM   540  N N   . ALA A 1 72  ? 20.53100  44.30400 -15.76100 1.000 127.29806 ?  80  ALA C N   1 
ATOM   541  C CA  . ALA A 1 72  ? 20.88100  44.25200 -17.16800 1.000 124.54193 ?  80  ALA C CA  1 
ATOM   542  C C   . ALA A 1 72  ? 19.78300  44.90600 -17.98500 1.000 124.10791 ?  80  ALA C C   1 
ATOM   543  O O   . ALA A 1 72  ? 18.59600  44.74500 -17.69100 1.000 124.22374 ?  80  ALA C O   1 
ATOM   544  C CB  . ALA A 1 72  ? 21.09200  42.80800 -17.63500 1.000 122.03850 ?  80  ALA C CB  1 
ATOM   545  N N   . ASP A 1 73  ? 20.18500  45.63500 -19.00900 1.000 120.67802 ?  81  ASP C N   1 
ATOM   546  C CA  . ASP A 1 73  ? 19.26500  46.21100 -19.97100 1.000 120.44386 ?  81  ASP C CA  1 
ATOM   547  C C   . ASP A 1 73  ? 19.51500  45.43000 -21.25500 1.000 118.48477 ?  81  ASP C C   1 
ATOM   548  O O   . ASP A 1 73  ? 20.60900  45.48900 -21.83400 1.000 117.70533 ?  81  ASP C O   1 
ATOM   549  C CB  . ASP A 1 73  ? 19.48000  47.71600 -20.13200 1.000 121.79097 ?  81  ASP C CB  1 
ATOM   550  C CG  . ASP A 1 73  ? 18.88900  48.26900 -21.41200 1.000 121.48276 ?  81  ASP C CG  1 
ATOM   551  O OD1 . ASP A 1 73  ? 17.83500  47.77500 -21.86500 1.000 121.07406 ?  81  ASP C OD1 1 
ATOM   552  O OD2 . ASP A 1 73  ? 19.48400  49.21600 -21.96300 1.000 121.58220 ?  81  ASP C OD2 1 
ATOM   553  N N   . THR A 1 74  ? 18.51300  44.63000 -21.62600 1.000 122.41248 ?  82  THR C N   1 
ATOM   554  C CA  . THR A 1 74  ? 18.60700  43.71500 -22.75800 1.000 120.81812 ?  82  THR C CA  1 
ATOM   555  C C   . THR A 1 74  ? 18.82800  44.46700 -24.06400 1.000 121.31809 ?  82  THR C C   1 
ATOM   556  O O   . THR A 1 74  ? 19.62000  44.04000 -24.91200 1.000 120.64215 ?  82  THR C O   1 
ATOM   557  C CB  . THR A 1 74  ? 17.33300  42.86000 -22.82500 1.000 118.89760 ?  82  THR C CB  1 
ATOM   558  O OG1 . THR A 1 74  ? 17.32900  42.07700 -24.02400 1.000 117.12955 ?  82  THR C OG1 1 
ATOM   559  C CG2 . THR A 1 74  ? 16.07400  43.72200 -22.78600 1.000 119.48022 ?  82  THR C CG2 1 
ATOM   560  N N   . SER A 1 75  ? 18.13700  45.59500 -24.23800 1.000 121.74215 ?  83  SER C N   1 
ATOM   561  C CA  . SER A 1 75  ? 18.18800  46.31600 -25.50400 1.000 122.10761 ?  83  SER C CA  1 
ATOM   562  C C   . SER A 1 75  ? 19.59100  46.82200 -25.79900 1.000 121.99504 ?  83  SER C C   1 
ATOM   563  O O   . SER A 1 75  ? 20.06500  46.72400 -26.93500 1.000 121.34226 ?  83  SER C O   1 
ATOM   564  C CB  . SER A 1 75  ? 17.19900  47.47600 -25.47300 1.000 123.71263 ?  83  SER C CB  1 
ATOM   565  O OG  . SER A 1 75  ? 17.80400  48.65500 -24.96200 1.000 124.92989 ?  83  SER C OG  1 
ATOM   566  N N   . LYS A 1 76  ? 20.27400  47.35200 -24.78700 1.000 125.72580 ?  84  LYS C N   1 
ATOM   567  C CA  . LYS A 1 76  ? 21.61600  47.89300 -24.94100 1.000 125.13220 ?  84  LYS C CA  1 
ATOM   568  C C   . LYS A 1 76  ? 22.69500  46.84200 -24.74000 1.000 123.67061 ?  84  LYS C C   1 
ATOM   569  O O   . LYS A 1 76  ? 23.88200  47.18300 -24.75900 1.000 123.01371 ?  84  LYS C O   1 
ATOM   570  C CB  . LYS A 1 76  ? 21.84200  49.04400 -23.95700 1.000 126.01996 ?  84  LYS C CB  1 
ATOM   571  N N   . ASN A 1 77  ? 22.31200  45.57900 -24.55000 1.000 131.26833 ?  85  ASN C N   1 
ATOM   572  C CA  . ASN A 1 77  ? 23.27300  44.49800 -24.34500 1.000 129.70277 ?  85  ASN C CA  1 
ATOM   573  C C   . ASN A 1 77  ? 24.21100  44.83500 -23.18900 1.000 129.35598 ?  85  ASN C C   1 
ATOM   574  O O   . ASN A 1 77  ? 25.43100  44.69300 -23.29100 1.000 128.31951 ?  85  ASN C O   1 
ATOM   575  C CB  . ASN A 1 77  ? 24.07500  44.21000 -25.61800 1.000 128.93486 ?  85  ASN C CB  1 
ATOM   576  C CG  . ASN A 1 77  ? 24.08200  42.74100 -25.99200 1.000 127.97726 ?  85  ASN C CG  1 
ATOM   577  O OD1 . ASN A 1 77  ? 23.20400  41.97500 -25.59100 1.000 127.86585 ?  85  ASN C OD1 1 
ATOM   578  N ND2 . ASN A 1 77  ? 25.09000  42.33700 -26.75900 1.000 127.35777 ?  85  ASN C ND2 1 
ATOM   579  N N   . THR A 1 78  ? 23.64800  45.31700 -22.08300 1.000 124.51009 ?  86  THR C N   1 
ATOM   580  C CA  . THR A 1 78  ? 24.53700  45.91600 -21.10100 1.000 124.75124 ?  86  THR C CA  1 
ATOM   581  C C   . THR A 1 78  ? 24.14000  45.52000 -19.69000 1.000 126.12949 ?  86  THR C C   1 
ATOM   582  O O   . THR A 1 78  ? 22.96600  45.54300 -19.32900 1.000 127.78543 ?  86  THR C O   1 
ATOM   583  C CB  . THR A 1 78  ? 24.55400  47.44100 -21.24200 1.000 125.79536 ?  86  THR C CB  1 
ATOM   584  O OG1 . THR A 1 78  ? 25.01200  47.77400 -22.55400 1.000 124.86000 ?  86  THR C OG1 1 
ATOM   585  C CG2 . THR A 1 78  ? 25.50900  48.05900 -20.24600 1.000 126.23657 ?  86  THR C CG2 1 
ATOM   586  N N   . ALA A 1 79  ? 25.13300  45.14700 -18.89800 1.000 123.64220 ?  87  ALA C N   1 
ATOM   587  C CA  . ALA A 1 79  ? 24.92000  44.88800 -17.48700 1.000 125.67580 ?  87  ALA C CA  1 
ATOM   588  C C   . ALA A 1 79  ? 25.31000  46.12900 -16.70500 1.000 127.64282 ?  87  ALA C C   1 
ATOM   589  O O   . ALA A 1 79  ? 26.13800  46.92400 -17.14700 1.000 126.68945 ?  87  ALA C O   1 
ATOM   590  C CB  . ALA A 1 79  ? 25.75100  43.69700 -17.01300 1.000 124.62546 ?  87  ALA C CB  1 
ATOM   591  N N   . TYR A 1 80  ? 24.69500  46.30400 -15.54900 1.000 125.26951 ?  88  TYR C N   1 
ATOM   592  C CA  . TYR A 1 80  ? 25.01500  47.42600 -14.68600 1.000 127.74046 ?  88  TYR C CA  1 
ATOM   593  C C   . TYR A 1 80  ? 25.14900  46.94100 -13.25900 1.000 130.50148 ?  88  TYR C C   1 
ATOM   594  O O   . TYR A 1 80  ? 24.35700  46.11900 -12.78800 1.000 131.75993 ?  88  TYR C O   1 
ATOM   595  C CB  . TYR A 1 80  ? 23.96600  48.53900 -14.75800 1.000 129.80911 ?  88  TYR C CB  1 
ATOM   596  C CG  . TYR A 1 80  ? 23.56100  48.92000 -16.15600 1.000 127.73266 ?  88  TYR C CG  1 
ATOM   597  C CD1 . TYR A 1 80  ? 24.28500  49.86400 -16.86500 1.000 126.32868 ?  88  TYR C CD1 1 
ATOM   598  C CD2 . TYR A 1 80  ? 22.44300  48.36700 -16.75400 1.000 127.41803 ?  88  TYR C CD2 1 
ATOM   599  C CE1 . TYR A 1 80  ? 23.91900  50.23100 -18.14100 1.000 124.90103 ?  88  TYR C CE1 1 
ATOM   600  C CE2 . TYR A 1 80  ? 22.07100  48.72800 -18.03100 1.000 125.90904 ?  88  TYR C CE2 1 
ATOM   601  C CZ  . TYR A 1 80  ? 22.81400  49.65900 -18.72100 1.000 124.82780 ?  88  TYR C CZ  1 
ATOM   602  O OH  . TYR A 1 80  ? 22.44700  50.02500 -19.99500 1.000 123.87036 ?  88  TYR C OH  1 
ATOM   603  N N   . LEU A 1 81  ? 26.16400  47.45000 -12.58900 1.000 134.14242 ?  89  LEU C N   1 
ATOM   604  C CA  . LEU A 1 81  ? 26.36200  47.19500 -11.16900 1.000 137.67797 ?  89  LEU C CA  1 
ATOM   605  C C   . LEU A 1 81  ? 26.16400  48.54000 -10.48800 1.000 140.92113 ?  89  LEU C C   1 
ATOM   606  O O   . LEU A 1 81  ? 27.05800  49.39100 -10.51100 1.000 140.79166 ?  89  LEU C O   1 
ATOM   607  C CB  . LEU A 1 81  ? 27.73600  46.59700 -10.87600 1.000 136.98428 ?  89  LEU C CB  1 
ATOM   608  C CG  . LEU A 1 81  ? 27.97700  46.29900 -9.39300  1.000 141.36078 ?  89  LEU C CG  1 
ATOM   609  C CD1 . LEU A 1 81  ? 26.75800  45.61400 -8.78300  1.000 143.71482 ?  89  LEU C CD1 1 
ATOM   610  C CD2 . LEU A 1 81  ? 29.21900  45.44700 -9.19100  1.000 140.78269 ?  89  LEU C CD2 1 
ATOM   611  N N   . GLN A 1 82  ? 24.96500  48.75600 -9.95100  1.000 147.30921 ?  90  GLN C N   1 
ATOM   612  C CA  . GLN A 1 82  ? 24.64700  49.99700 -9.25600  1.000 150.60425 ?  90  GLN C CA  1 
ATOM   613  C C   . GLN A 1 82  ? 25.07800  49.84500 -7.80100  1.000 154.63233 ?  90  GLN C C   1 
ATOM   614  O O   . GLN A 1 82  ? 24.51500  49.03000 -7.05500  1.000 156.88501 ?  90  GLN C O   1 
ATOM   615  C CB  . GLN A 1 82  ? 23.16500  50.34300 -9.39100  1.000 151.75750 ?  90  GLN C CB  1 
ATOM   616  C CG  . GLN A 1 82  ? 22.73700  51.55600 -8.57500  1.000 155.37724 ?  90  GLN C CG  1 
ATOM   617  C CD  . GLN A 1 82  ? 23.29900  52.86900 -9.11400  1.000 154.50248 ?  90  GLN C CD  1 
ATOM   618  O OE1 . GLN A 1 82  ? 22.96200  53.28800 -10.22100 1.000 152.26030 ?  90  GLN C OE1 1 
ATOM   619  N NE2 . GLN A 1 82  ? 24.14300  53.53100 -8.32000  1.000 156.51018 ?  90  GLN C NE2 1 
ATOM   620  N N   . MET A 1 83  ? 26.13800  50.56600 -7.43800  1.000 156.83305 ?  91  MET C N   1 
ATOM   621  C CA  . MET A 1 83  ? 26.64000  50.65800 -6.07900  1.000 161.14313 ?  91  MET C CA  1 
ATOM   622  C C   . MET A 1 83  ? 26.03100  51.88100 -5.40800  1.000 164.45739 ?  91  MET C C   1 
ATOM   623  O O   . MET A 1 83  ? 26.05500  52.97700 -5.98000  1.000 163.15227 ?  91  MET C O   1 
ATOM   624  C CB  . MET A 1 83  ? 28.15900  50.79900 -6.10100  1.000 160.23989 ?  91  MET C CB  1 
ATOM   625  C CG  . MET A 1 83  ? 28.83700  50.02800 -7.21300  1.000 155.53376 ?  91  MET C CG  1 
ATOM   626  S SD  . MET A 1 83  ? 30.55200  49.69300 -6.80400  1.000 155.98102 ?  91  MET C SD  1 
ATOM   627  C CE  . MET A 1 83  ? 31.22100  49.34200 -8.41600  1.000 149.76142 ?  91  MET C CE  1 
ATOM   628  N N   . ASN A 1 84  ? 25.50200  51.70700 -4.20200  1.000 164.77916 ?  92  ASN C N   1 
ATOM   629  C CA  . ASN A 1 84  ? 24.76400  52.77300 -3.54000  1.000 168.57644 ?  92  ASN C CA  1 
ATOM   630  C C   . ASN A 1 84  ? 25.37800  53.25400 -2.23700  1.000 174.08378 ?  92  ASN C C   1 
ATOM   631  O O   . ASN A 1 84  ? 25.15700  54.41000 -1.86900  1.000 176.44136 ?  92  ASN C O   1 
ATOM   632  C CB  . ASN A 1 84  ? 23.32000  52.33900 -3.25100  1.000 169.98247 ?  92  ASN C CB  1 
ATOM   633  C CG  . ASN A 1 84  ? 22.45900  52.31100 -4.49400  1.000 165.36218 ?  92  ASN C CG  1 
ATOM   634  O OD1 . ASN A 1 84  ? 22.04300  53.35800 -4.99400  1.000 164.55365 ?  92  ASN C OD1 1 
ATOM   635  N ND2 . ASN A 1 84  ? 22.16800  51.11100 -4.99200  1.000 162.55175 ?  92  ASN C ND2 1 
ATOM   636  N N   . SER A 1 85  ? 26.13400  52.41800 -1.53100  1.000 170.64548 ?  93  SER C N   1 
ATOM   637  C CA  . SER A 1 85  ? 26.70900  52.79000 -0.23900  1.000 176.26551 ?  93  SER C CA  1 
ATOM   638  C C   . SER A 1 85  ? 28.21100  52.50200 -0.22900  1.000 175.98578 ?  93  SER C C   1 
ATOM   639  O O   . SER A 1 85  ? 28.71200  51.76000 0.61400   1.000 179.38269 ?  93  SER C O   1 
ATOM   640  C CB  . SER A 1 85  ? 26.01200  52.06300 0.91000   1.000 180.89896 ?  93  SER C CB  1 
ATOM   641  O OG  . SER A 1 85  ? 26.56300  52.44900 2.15900   1.000 186.32536 ?  93  SER C OG  1 
ATOM   642  N N   . LEU A 1 86  ? 28.93800  53.11000 -1.16600  1.000 174.39554 ?  94  LEU C N   1 
ATOM   643  C CA  . LEU A 1 86  ? 30.34500  52.77700 -1.33600  1.000 173.35966 ?  94  LEU C CA  1 
ATOM   644  C C   . LEU A 1 86  ? 31.12200  53.11600 -0.07400  1.000 179.03715 ?  94  LEU C C   1 
ATOM   645  O O   . LEU A 1 86  ? 31.19900  54.27700 0.33900   1.000 181.25121 ?  94  LEU C O   1 
ATOM   646  C CB  . LEU A 1 86  ? 30.93000  53.51700 -2.53900  1.000 168.38920 ?  94  LEU C CB  1 
ATOM   647  C CG  . LEU A 1 86  ? 30.67500  52.90700 -3.92100  1.000 162.18509 ?  94  LEU C CG  1 
ATOM   648  C CD1 . LEU A 1 86  ? 30.64500  53.95600 -5.01100  1.000 159.25516 ?  94  LEU C CD1 1 
ATOM   649  C CD2 . LEU A 1 86  ? 31.74800  51.89100 -4.23000  1.000 160.23257 ?  94  LEU C CD2 1 
ATOM   650  N N   . ARG A 1 87  ? 31.68600  52.08300 0.53800   1.000 179.32955 ?  95  ARG C N   1 
ATOM   651  C CA  . ARG A 1 87  ? 32.57200  52.19500 1.68200   1.000 184.41467 ?  95  ARG C CA  1 
ATOM   652  C C   . ARG A 1 87  ? 34.01100  51.98800 1.22600   1.000 182.44478 ?  95  ARG C C   1 
ATOM   653  O O   . ARG A 1 87  ? 34.27600  51.62100 0.08100   1.000 177.34468 ?  95  ARG C O   1 
ATOM   654  C CB  . ARG A 1 87  ? 32.17700  51.18500 2.76500   1.000 189.10148 ?  95  ARG C CB  1 
ATOM   655  C CG  . ARG A 1 87  ? 30.82800  51.46600 3.43200   1.000 191.90789 ?  95  ARG C CG  1 
ATOM   656  C CD  . ARG A 1 87  ? 30.61400  52.95900 3.66700   1.000 193.05503 ?  95  ARG C CD  1 
ATOM   657  N N   . ALA A 1 88  ? 34.94600  52.24900 2.14200   1.000 182.36497 ?  96  ALA C N   1 
ATOM   658  C CA  . ALA A 1 88  ? 36.36800  52.22300 1.80600   1.000 181.01730 ?  96  ALA C CA  1 
ATOM   659  C C   . ALA A 1 88  ? 36.76300  50.92000 1.12400   1.000 178.16807 ?  96  ALA C C   1 
ATOM   660  O O   . ALA A 1 88  ? 37.38500  50.92700 0.05600   1.000 173.51144 ?  96  ALA C O   1 
ATOM   661  C CB  . ALA A 1 88  ? 37.20100  52.43200 3.06900   1.000 186.64138 ?  96  ALA C CB  1 
ATOM   662  N N   . GLU A 1 89  ? 36.40200  49.78800 1.73300   1.000 178.47868 ?  97  GLU C N   1 
ATOM   663  C CA  . GLU A 1 89  ? 36.75800  48.47300 1.21100   1.000 176.47088 ?  97  GLU C CA  1 
ATOM   664  C C   . GLU A 1 89  ? 36.29300  48.25400 -0.22400  1.000 169.77717 ?  97  GLU C C   1 
ATOM   665  O O   . GLU A 1 89  ? 36.87000  47.41800 -0.92900  1.000 166.90581 ?  97  GLU C O   1 
ATOM   666  C CB  . GLU A 1 89  ? 36.19800  47.39300 2.13900   1.000 180.77445 ?  97  GLU C CB  1 
ATOM   667  C CG  . GLU A 1 89  ? 36.26700  47.77600 3.61200   1.000 187.36167 ?  97  GLU C CG  1 
ATOM   668  C CD  . GLU A 1 89  ? 35.03900  48.52600 4.09300   1.000 188.96580 ?  97  GLU C CD  1 
ATOM   669  O OE1 . GLU A 1 89  ? 34.17700  48.85800 3.25400   1.000 184.93903 ?  97  GLU C OE1 1 
ATOM   670  O OE2 . GLU A 1 89  ? 34.94800  48.79700 5.30800   1.000 194.20760 ?  97  GLU C OE2 1 
ATOM   671  N N   . ASP A 1 90  ? 35.25500  48.96500 -0.66700  1.000 177.04411 ?  98  ASP C N   1 
ATOM   672  C CA  . ASP A 1 90  ? 34.77400  48.81100 -2.03700  1.000 170.61773 ?  98  ASP C CA  1 
ATOM   673  C C   . ASP A 1 90  ? 35.80300  49.24200 -3.07600  1.000 166.38146 ?  98  ASP C C   1 
ATOM   674  O O   . ASP A 1 90  ? 35.68100  48.85300 -4.24200  1.000 161.17846 ?  98  ASP C O   1 
ATOM   675  C CB  . ASP A 1 90  ? 33.48700  49.60700 -2.22300  1.000 169.50400 ?  98  ASP C CB  1 
ATOM   676  C CG  . ASP A 1 90  ? 32.44800  49.27600 -1.17300  1.000 174.05393 ?  98  ASP C CG  1 
ATOM   677  O OD1 . ASP A 1 90  ? 32.84400  48.88400 -0.05600  1.000 179.25536 ?  98  ASP C OD1 1 
ATOM   678  O OD2 . ASP A 1 90  ? 31.23900  49.40300 -1.45700  1.000 172.62668 ?  98  ASP C OD2 1 
ATOM   679  N N   . THR A 1 91  ? 36.79500  50.04200 -2.68900  1.000 170.25953 ?  99  THR C N   1 
ATOM   680  C CA  . THR A 1 91  ? 37.85800  50.43800 -3.60400  1.000 166.85390 ?  99  THR C CA  1 
ATOM   681  C C   . THR A 1 91  ? 38.45400  49.22100 -4.27900  1.000 164.43730 ?  99  THR C C   1 
ATOM   682  O O   . THR A 1 91  ? 38.97700  48.32700 -3.60800  1.000 167.70184 ?  99  THR C O   1 
ATOM   683  C CB  . THR A 1 91  ? 38.95700  51.17500 -2.84300  1.000 170.52884 ?  99  THR C CB  1 
ATOM   684  O OG1 . THR A 1 91  ? 39.15200  50.54400 -1.57200  1.000 176.06409 ?  99  THR C OG1 1 
ATOM   685  C CG2 . THR A 1 91  ? 38.58000  52.59600 -2.61600  1.000 171.24962 ?  99  THR C CG2 1 
ATOM   686  N N   . ALA A 1 92  ? 38.39800  49.19700 -5.60700  1.000 163.75236 ?  100 ALA C N   1 
ATOM   687  C CA  . ALA A 1 92  ? 38.90300  48.02700 -6.31800  1.000 161.14584 ?  100 ALA C CA  1 
ATOM   688  C C   . ALA A 1 92  ? 38.82600  48.29500 -7.81100  1.000 155.88788 ?  100 ALA C C   1 
ATOM   689  O O   . ALA A 1 92  ? 38.18100  49.24900 -8.26100  1.000 154.19815 ?  100 ALA C O   1 
ATOM   690  C CB  . ALA A 1 92  ? 38.12300  46.75300 -5.98600  1.000 161.59959 ?  100 ALA C CB  1 
ATOM   691  N N   . VAL A 1 93  ? 39.48400  47.43300 -8.57900  1.000 153.85874 ?  101 VAL C N   1 
ATOM   692  C CA  . VAL A 1 93  ? 39.19900  47.35500 -10.00200 1.000 149.95225 ?  101 VAL C CA  1 
ATOM   693  C C   . VAL A 1 93  ? 38.09000  46.33100 -10.19300 1.000 148.16637 ?  101 VAL C C   1 
ATOM   694  O O   . VAL A 1 93  ? 38.15300  45.21100 -9.67900  1.000 149.12873 ?  101 VAL C O   1 
ATOM   695  C CB  . VAL A 1 93  ? 40.45600  47.00700 -10.81900 1.000 149.27146 ?  101 VAL C CB  1 
ATOM   696  C CG1 . VAL A 1 93  ? 40.96700  45.62400 -10.49600 1.000 150.37613 ?  101 VAL C CG1 1 
ATOM   697  C CG2 . VAL A 1 93  ? 40.14800  47.11200 -12.30100 1.000 146.08718 ?  101 VAL C CG2 1 
ATOM   698  N N   . TYR A 1 94  ? 37.05800  46.72200 -10.91500 1.000 150.14422 ?  102 TYR C N   1 
ATOM   699  C CA  . TYR A 1 94  ? 35.88000  45.89700 -11.08300 1.000 148.43561 ?  102 TYR C CA  1 
ATOM   700  C C   . TYR A 1 94  ? 35.90500  45.40000 -12.51800 1.000 145.06926 ?  102 TYR C C   1 
ATOM   701  O O   . TYR A 1 94  ? 36.10600  46.19000 -13.45200 1.000 143.92278 ?  102 TYR C O   1 
ATOM   702  C CB  . TYR A 1 94  ? 34.60600  46.68500 -10.75700 1.000 148.69801 ?  102 TYR C CB  1 
ATOM   703  C CG  . TYR A 1 94  ? 34.35700  46.86400 -9.26300  1.000 153.18897 ?  102 TYR C CG  1 
ATOM   704  C CD1 . TYR A 1 94  ? 35.15700  47.71200 -8.50400  1.000 156.47933 ?  102 TYR C CD1 1 
ATOM   705  C CD2 . TYR A 1 94  ? 33.31400  46.20000 -8.61500  1.000 154.63396 ?  102 TYR C CD2 1 
ATOM   706  C CE1 . TYR A 1 94  ? 34.94000  47.88500 -7.14400  1.000 161.33008 ?  102 TYR C CE1 1 
ATOM   707  C CE2 . TYR A 1 94  ? 33.08700  46.37100 -7.24900  1.000 159.60952 ?  102 TYR C CE2 1 
ATOM   708  C CZ  . TYR A 1 94  ? 33.90400  47.21400 -6.52100  1.000 163.01698 ?  102 TYR C CZ  1 
ATOM   709  O OH  . TYR A 1 94  ? 33.68900  47.38900 -5.17100  1.000 168.50504 ?  102 TYR C OH  1 
ATOM   710  N N   . TYR A 1 95  ? 35.82200  44.08300 -12.66500 1.000 145.12941 ?  103 TYR C N   1 
ATOM   711  C CA  . TYR A 1 95  ? 35.81400  43.37300 -13.92600 1.000 143.06796 ?  103 TYR C CA  1 
ATOM   712  C C   . TYR A 1 95  ? 34.43400  42.79200 -14.16100 1.000 141.32019 ?  103 TYR C C   1 
ATOM   713  O O   . TYR A 1 95  ? 33.75400  42.38000 -13.22300 1.000 142.02712 ?  103 TYR C O   1 
ATOM   714  C CB  . TYR A 1 95  ? 36.81900  42.22000 -13.91600 1.000 144.16209 ?  103 TYR C CB  1 
ATOM   715  C CG  . TYR A 1 95  ? 38.24600  42.66200 -14.01100 1.000 146.08218 ?  103 TYR C CG  1 
ATOM   716  C CD1 . TYR A 1 95  ? 38.78700  43.05500 -15.22400 1.000 145.61812 ?  103 TYR C CD1 1 
ATOM   717  C CD2 . TYR A 1 95  ? 39.04900  42.71500 -12.87800 1.000 149.19318 ?  103 TYR C CD2 1 
ATOM   718  C CE1 . TYR A 1 95  ? 40.09000  43.46800 -15.31400 1.000 147.49302 ?  103 TYR C CE1 1 
ATOM   719  C CE2 . TYR A 1 95  ? 40.35300  43.13000 -12.95600 1.000 151.08441 ?  103 TYR C CE2 1 
ATOM   720  C CZ  . TYR A 1 95  ? 40.86800  43.50700 -14.17800 1.000 149.99984 ?  103 TYR C CZ  1 
ATOM   721  O OH  . TYR A 1 95  ? 42.17200  43.92600 -14.26800 1.000 151.96789 ?  103 TYR C OH  1 
ATOM   722  N N   . CYS A 1 96  ? 34.03300  42.74500 -15.41400 1.000 130.52104 ?  104 CYS C N   1 
ATOM   723  C CA  . CYS A 1 96  ? 32.83500  42.02900 -15.79600 1.000 128.74097 ?  104 CYS C CA  1 
ATOM   724  C C   . CYS A 1 96  ? 33.26200  40.92400 -16.74400 1.000 128.12293 ?  104 CYS C C   1 
ATOM   725  O O   . CYS A 1 96  ? 34.20100  41.09400 -17.52700 1.000 128.90766 ?  104 CYS C O   1 
ATOM   726  C CB  . CYS A 1 96  ? 31.80200  42.96300 -16.43700 1.000 127.56888 ?  104 CYS C CB  1 
ATOM   727  S SG  . CYS A 1 96  ? 32.21100  43.49600 -18.11700 1.000 126.88038 ?  104 CYS C SG  1 
ATOM   728  N N   . ALA A 1 97  ? 32.58100  39.78800 -16.66200 1.000 124.62931 ?  105 ALA C N   1 
ATOM   729  C CA  . ALA A 1 97  ? 33.03000  38.63800 -17.43700 1.000 124.75562 ?  105 ALA C CA  1 
ATOM   730  C C   . ALA A 1 97  ? 31.83900  37.79000 -17.83500 1.000 123.04081 ?  105 ALA C C   1 
ATOM   731  O O   . ALA A 1 97  ? 30.78600  37.82200 -17.18500 1.000 122.02378 ?  105 ALA C O   1 
ATOM   732  C CB  . ALA A 1 97  ? 34.03600  37.79000 -16.65500 1.000 126.58751 ?  105 ALA C CB  1 
ATOM   733  N N   . ARG A 1 98  ? 32.05300  36.96100 -18.86200 1.000 118.86388 ?  106 ARG C N   1 
ATOM   734  C CA  . ARG A 1 98  ? 31.01000  36.06100 -19.33600 1.000 117.50781 ?  106 ARG C CA  1 
ATOM   735  C C   . ARG A 1 98  ? 31.27100  34.66600 -18.79200 1.000 118.05306 ?  106 ARG C C   1 
ATOM   736  O O   . ARG A 1 98  ? 32.41900  34.22100 -18.72200 1.000 120.13351 ?  106 ARG C O   1 
ATOM   737  C CB  . ARG A 1 98  ? 30.93900  36.01700 -20.87000 1.000 118.09272 ?  106 ARG C CB  1 
ATOM   738  C CG  . ARG A 1 98  ? 30.32000  34.72700 -21.42100 1.000 117.97166 ?  106 ARG C CG  1 
ATOM   739  C CD  . ARG A 1 98  ? 30.29700  34.65600 -22.94400 1.000 119.82688 ?  106 ARG C CD  1 
ATOM   740  N NE  . ARG A 1 98  ? 31.33500  33.80200 -23.51200 1.000 123.25884 ?  106 ARG C NE  1 
ATOM   741  C CZ  . ARG A 1 98  ? 31.35200  33.38900 -24.77200 1.000 125.40335 ?  106 ARG C CZ  1 
ATOM   742  N NH1 . ARG A 1 98  ? 30.41700  33.75700 -25.63200 1.000 123.99924 ?  106 ARG C NH1 1 
ATOM   743  N NH2 . ARG A 1 98  ? 32.34400  32.60800 -25.18600 1.000 128.59684 ?  106 ARG C NH2 1 
ATOM   744  N N   . HIS A 1 99  ? 30.19900  33.99600 -18.37800 1.000 123.69715 ?  107 HIS C N   1 
ATOM   745  C CA  . HIS A 1 99  ? 30.24300  32.59600 -17.97500 1.000 123.94897 ?  107 HIS C CA  1 
ATOM   746  C C   . HIS A 1 99  ? 29.40200  31.82600 -18.97800 1.000 123.15017 ?  107 HIS C C   1 
ATOM   747  O O   . HIS A 1 99  ? 28.16800  31.87500 -18.92900 1.000 121.30614 ?  107 HIS C O   1 
ATOM   748  C CB  . HIS A 1 99  ? 29.72800  32.38000 -16.55000 1.000 123.30841 ?  107 HIS C CB  1 
ATOM   749  C CG  . HIS A 1 99  ? 29.30500  30.96700 -16.26200 1.000 122.96814 ?  107 HIS C CG  1 
ATOM   750  N ND1 . HIS A 1 99  ? 28.22600  30.65400 -15.46100 1.000 122.12615 ?  107 HIS C ND1 1 
ATOM   751  C CD2 . HIS A 1 99  ? 29.82200  29.78300 -16.66800 1.000 123.79768 ?  107 HIS C CD2 1 
ATOM   752  C CE1 . HIS A 1 99  ? 28.09600  29.34100 -15.38800 1.000 122.02728 ?  107 HIS C CE1 1 
ATOM   753  N NE2 . HIS A 1 99  ? 29.05000  28.78900 -16.11500 1.000 122.93999 ?  107 HIS C NE2 1 
ATOM   754  N N   . ALA A 1 100 ? 30.06700  31.11800 -19.87700 1.000 123.38205 ?  108 ALA C N   1 
ATOM   755  C CA  . ALA A 1 100 ? 29.39200  30.29600 -20.86300 1.000 123.41968 ?  108 ALA C CA  1 
ATOM   756  C C   . ALA A 1 100 ? 29.39700  28.85300 -20.38400 1.000 123.20501 ?  108 ALA C C   1 
ATOM   757  O O   . ALA A 1 100 ? 30.37100  28.39300 -19.78100 1.000 124.67082 ?  108 ALA C O   1 
ATOM   758  C CB  . ALA A 1 100 ? 30.07900  30.40200 -22.22200 1.000 126.68462 ?  108 ALA C CB  1 
ATOM   759  N N   . TRP A 1 101 ? 28.30400  28.13800 -20.65100 1.000 127.28935 ?  109 TRP C N   1 
ATOM   760  C CA  . TRP A 1 101 ? 28.21800  26.77000 -20.15900 1.000 126.86050 ?  109 TRP C CA  1 
ATOM   761  C C   . TRP A 1 101 ? 29.17800  25.85500 -20.89600 1.000 129.85442 ?  109 TRP C C   1 
ATOM   762  O O   . TRP A 1 101 ? 29.61800  24.84700 -20.33400 1.000 130.42004 ?  109 TRP C O   1 
ATOM   763  C CB  . TRP A 1 101 ? 26.79500  26.22700 -20.29200 1.000 124.29726 ?  109 TRP C CB  1 
ATOM   764  C CG  . TRP A 1 101 ? 25.79800  26.81900 -19.33600 1.000 122.01019 ?  109 TRP C CG  1 
ATOM   765  C CD1 . TRP A 1 101 ? 24.73200  27.62600 -19.64400 1.000 120.60572 ?  109 TRP C CD1 1 
ATOM   766  C CD2 . TRP A 1 101 ? 25.74600  26.61700 -17.92000 1.000 121.47263 ?  109 TRP C CD2 1 
ATOM   767  N NE1 . TRP A 1 101 ? 24.04200  27.95700 -18.50400 1.000 119.67923 ?  109 TRP C NE1 1 
ATOM   768  C CE2 . TRP A 1 101 ? 24.64000  27.34700 -17.43300 1.000 120.31860 ?  109 TRP C CE2 1 
ATOM   769  C CE3 . TRP A 1 101 ? 26.53400  25.90200 -17.01400 1.000 122.29308 ?  109 TRP C CE3 1 
ATOM   770  C CZ2 . TRP A 1 101 ? 24.30300  27.37500 -16.08300 1.000 120.53816 ?  109 TRP C CZ2 1 
ATOM   771  C CZ3 . TRP A 1 101 ? 26.19600  25.92900 -15.68200 1.000 121.99389 ?  109 TRP C CZ3 1 
ATOM   772  C CH2 . TRP A 1 101 ? 25.09200  26.65900 -15.22600 1.000 121.38045 ?  109 TRP C CH2 1 
ATOM   773  N N   . TYR A 1 102 ? 29.51500  26.18500 -22.14600 1.000 118.50666 ?  110 TYR C N   1 
ATOM   774  C CA  . TYR A 1 102 ? 30.45400  25.35400 -22.89100 1.000 121.95467 ?  110 TYR C CA  1 
ATOM   775  C C   . TYR A 1 102 ? 31.80100  25.25200 -22.19000 1.000 124.70570 ?  110 TYR C C   1 
ATOM   776  O O   . TYR A 1 102 ? 32.50100  24.24500 -22.33900 1.000 126.86957 ?  110 TYR C O   1 
ATOM   777  C CB  . TYR A 1 102 ? 30.65100  25.87600 -24.31500 1.000 124.25189 ?  110 TYR C CB  1 
ATOM   778  C CG  . TYR A 1 102 ? 31.69500  25.06500 -25.03400 1.000 127.57415 ?  110 TYR C CG  1 
ATOM   779  C CD1 . TYR A 1 102 ? 31.36100  23.86000 -25.62300 1.000 127.64295 ?  110 TYR C CD1 1 
ATOM   780  C CD2 . TYR A 1 102 ? 33.01700  25.48000 -25.09600 1.000 130.97506 ?  110 TYR C CD2 1 
ATOM   781  C CE1 . TYR A 1 102 ? 32.30600  23.08800 -26.25500 1.000 130.79984 ?  110 TYR C CE1 1 
ATOM   782  C CE2 . TYR A 1 102 ? 33.96900  24.71600 -25.72900 1.000 133.27115 ?  110 TYR C CE2 1 
ATOM   783  C CZ  . TYR A 1 102 ? 33.60700  23.52300 -26.30900 1.000 133.20511 ?  110 TYR C CZ  1 
ATOM   784  O OH  . TYR A 1 102 ? 34.55700  22.76200 -26.94300 1.000 134.54506 ?  110 TYR C OH  1 
ATOM   785  N N   . TYR A 1 103 ? 32.17700  26.26700 -21.42000 1.000 126.90076 ?  111 TYR C N   1 
ATOM   786  C CA  . TYR A 1 103 ? 33.39600  26.22800 -20.63000 1.000 129.26359 ?  111 TYR C CA  1 
ATOM   787  C C   . TYR A 1 103 ? 33.11200  25.86600 -19.18100 1.000 126.29289 ?  111 TYR C C   1 
ATOM   788  O O   . TYR A 1 103 ? 33.97700  26.04800 -18.32200 1.000 127.19073 ?  111 TYR C O   1 
ATOM   789  C CB  . TYR A 1 103 ? 34.11600  27.57100 -20.71900 1.000 131.04179 ?  111 TYR C CB  1 
ATOM   790  C CG  . TYR A 1 103 ? 34.47700  27.94500 -22.13500 1.000 134.32692 ?  111 TYR C CG  1 
ATOM   791  C CD1 . TYR A 1 103 ? 35.39800  27.20400 -22.85700 1.000 138.41254 ?  111 TYR C CD1 1 
ATOM   792  C CD2 . TYR A 1 103 ? 33.89400  29.04100 -22.75000 1.000 133.09680 ?  111 TYR C CD2 1 
ATOM   793  C CE1 . TYR A 1 103 ? 35.72700  27.54000 -24.15600 1.000 139.92542 ?  111 TYR C CE1 1 
ATOM   794  C CE2 . TYR A 1 103 ? 34.22000  29.38900 -24.04800 1.000 135.71454 ?  111 TYR C CE2 1 
ATOM   795  C CZ  . TYR A 1 103 ? 35.13700  28.63600 -24.74600 1.000 137.96827 ?  111 TYR C CZ  1 
ATOM   796  O OH  . TYR A 1 103 ? 35.47200  28.97300 -26.03800 1.000 136.43133 ?  111 TYR C OH  1 
ATOM   797  N N   . GLY A 1 104 ? 31.91900  25.34800 -18.89800 1.000 137.58803 ?  112 GLY C N   1 
ATOM   798  C CA  . GLY A 1 104 ? 31.57800  24.93900 -17.55400 1.000 135.22648 ?  112 GLY C CA  1 
ATOM   799  C C   . GLY A 1 104 ? 31.42100  26.15200 -16.65400 1.000 133.72693 ?  112 GLY C C   1 
ATOM   800  O O   . GLY A 1 104 ? 31.16100  27.26700 -17.10600 1.000 133.24635 ?  112 GLY C O   1 
ATOM   801  N N   . TRP A 1 105 ? 31.58000  25.91900 -15.35400 1.000 146.97037 ?  113 TRP C N   1 
ATOM   802  C CA  . TRP A 1 105 ? 31.58300  27.00400 -14.37900 1.000 146.78454 ?  113 TRP C CA  1 
ATOM   803  C C   . TRP A 1 105 ? 32.87400  27.80300 -14.45700 1.000 148.96800 ?  113 TRP C C   1 
ATOM   804  O O   . TRP A 1 105 ? 33.87100  27.45800 -13.81300 1.000 151.40260 ?  113 TRP C O   1 
ATOM   805  C CB  . TRP A 1 105 ? 31.36600  26.43600 -12.97900 1.000 147.45304 ?  113 TRP C CB  1 
ATOM   806  C CG  . TRP A 1 105 ? 29.94800  26.11200 -12.73900 1.000 145.54270 ?  113 TRP C CG  1 
ATOM   807  C CD1 . TRP A 1 105 ? 28.91200  26.25100 -13.62200 1.000 143.28676 ?  113 TRP C CD1 1 
ATOM   808  C CD2 . TRP A 1 105 ? 29.39900  25.52600 -11.56300 1.000 146.25752 ?  113 TRP C CD2 1 
ATOM   809  N NE1 . TRP A 1 105 ? 27.74400  25.82900 -13.04200 1.000 142.50466 ?  113 TRP C NE1 1 
ATOM   810  C CE2 . TRP A 1 105 ? 28.01600  25.37000 -11.78100 1.000 144.36849 ?  113 TRP C CE2 1 
ATOM   811  C CE3 . TRP A 1 105 ? 29.94000  25.12600 -10.33800 1.000 148.77318 ?  113 TRP C CE3 1 
ATOM   812  C CZ2 . TRP A 1 105 ? 27.16700  24.83000 -10.82000 1.000 144.98128 ?  113 TRP C CZ2 1 
ATOM   813  C CZ3 . TRP A 1 105 ? 29.09900  24.58400 -9.39100  1.000 149.48490 ?  113 TRP C CZ3 1 
ATOM   814  C CH2 . TRP A 1 105 ? 27.72700  24.44200 -9.63400  1.000 147.57473 ?  113 TRP C CH2 1 
ATOM   815  N N   . GLY A 1 106 ? 32.86200  28.88100 -15.22300 1.000 126.68737 ?  114 GLY C N   1 
ATOM   816  C CA  . GLY A 1 106 ? 34.09300  29.58000 -15.49700 1.000 128.85011 ?  114 GLY C CA  1 
ATOM   817  C C   . GLY A 1 106 ? 33.86500  30.85200 -16.26900 1.000 127.65511 ?  114 GLY C C   1 
ATOM   818  O O   . GLY A 1 106 ? 32.89500  30.98100 -17.02100 1.000 125.60612 ?  114 GLY C O   1 
ATOM   819  N N   . LEU A 1 107 ? 34.77100  31.80100 -16.09100 1.000 124.74673 ?  115 LEU C N   1 
ATOM   820  C CA  . LEU A 1 107 ? 34.63900  33.12800 -16.67300 1.000 123.79769 ?  115 LEU C CA  1 
ATOM   821  C C   . LEU A 1 107 ? 35.58300  33.20300 -17.86500 1.000 126.06899 ?  115 LEU C C   1 
ATOM   822  O O   . LEU A 1 107 ? 36.78600  33.43200 -17.71400 1.000 128.71092 ?  115 LEU C O   1 
ATOM   823  C CB  . LEU A 1 107 ? 34.91200  34.19000 -15.61200 1.000 124.15408 ?  115 LEU C CB  1 
ATOM   824  C CG  . LEU A 1 107 ? 33.70000  34.59700 -14.76200 1.000 122.43227 ?  115 LEU C CG  1 
ATOM   825  C CD1 . LEU A 1 107 ? 33.14700  33.46000 -13.94200 1.000 122.48749 ?  115 LEU C CD1 1 
ATOM   826  C CD2 . LEU A 1 107 ? 34.09600  35.72300 -13.82900 1.000 123.84832 ?  115 LEU C CD2 1 
ATOM   827  N N   . ASP A 1 108 ? 35.01700  33.00500 -19.05400 1.000 129.62114 ?  116 ASP C N   1 
ATOM   828  C CA  . ASP A 1 108 ? 35.67800  33.20600 -20.33700 1.000 133.27656 ?  116 ASP C CA  1 
ATOM   829  C C   . ASP A 1 108 ? 35.63000  34.70600 -20.53800 1.000 132.15746 ?  116 ASP C C   1 
ATOM   830  O O   . ASP A 1 108 ? 35.65400  35.42900 -19.53700 1.000 129.96173 ?  116 ASP C O   1 
ATOM   831  C CB  . ASP A 1 108 ? 35.01200  32.43900 -21.47400 1.000 134.54639 ?  116 ASP C CB  1 
ATOM   832  C CG  . ASP A 1 108 ? 33.56200  32.77500 -21.62200 1.000 130.78121 ?  116 ASP C CG  1 
ATOM   833  O OD1 . ASP A 1 108 ? 33.26500  33.77200 -22.31000 1.000 130.50322 ?  116 ASP C OD1 1 
ATOM   834  O OD2 . ASP A 1 108 ? 32.72300  32.06500 -21.03500 1.000 128.18279 ?  116 ASP C OD2 1 
ATOM   835  N N   . TYR A 1 109 ? 35.61800  35.18100 -21.78800 1.000 138.00178 ?  117 TYR C N   1 
ATOM   836  C CA  . TYR A 1 109 ? 35.97800  36.55100 -22.12500 1.000 138.06849 ?  117 TYR C CA  1 
ATOM   837  C C   . TYR A 1 109 ? 35.71300  37.49200 -20.96000 1.000 134.68944 ?  117 TYR C C   1 
ATOM   838  O O   . TYR A 1 109 ? 34.58300  37.58100 -20.44400 1.000 131.71005 ?  117 TYR C O   1 
ATOM   839  C CB  . TYR A 1 109 ? 35.13900  37.03900 -23.30800 1.000 137.88042 ?  117 TYR C CB  1 
ATOM   840  C CG  . TYR A 1 109 ? 35.33000  36.34400 -24.63100 1.000 140.69436 ?  117 TYR C CG  1 
ATOM   841  C CD1 . TYR A 1 109 ? 34.59800  35.20600 -24.94800 1.000 140.25112 ?  117 TYR C CD1 1 
ATOM   842  C CD2 . TYR A 1 109 ? 36.16900  36.87400 -25.59600 1.000 142.29539 ?  117 TYR C CD2 1 
ATOM   843  C CE1 . TYR A 1 109 ? 34.74300  34.58300 -26.16900 1.000 140.23652 ?  117 TYR C CE1 1 
ATOM   844  C CE2 . TYR A 1 109 ? 36.31900  36.26700 -26.81800 1.000 141.63183 ?  117 TYR C CE2 1 
ATOM   845  C CZ  . TYR A 1 109 ? 35.60500  35.12200 -27.10400 1.000 140.23628 ?  117 TYR C CZ  1 
ATOM   846  O OH  . TYR A 1 109 ? 35.76500  34.52800 -28.33300 1.000 138.24776 ?  117 TYR C OH  1 
ATOM   847  N N   . TRP A 1 110 ? 36.77600  38.14900 -20.51500 1.000 134.38468 ?  118 TRP C N   1 
ATOM   848  C CA  . TRP A 1 110 ? 36.76000  38.99600 -19.33900 1.000 132.16630 ?  118 TRP C CA  1 
ATOM   849  C C   . TRP A 1 110 ? 36.63200  40.44700 -19.76100 1.000 131.48811 ?  118 TRP C C   1 
ATOM   850  O O   . TRP A 1 110 ? 36.72000  40.79100 -20.94200 1.000 132.83128 ?  118 TRP C O   1 
ATOM   851  C CB  . TRP A 1 110 ? 38.03100  38.80500 -18.51200 1.000 133.74769 ?  118 TRP C CB  1 
ATOM   852  C CG  . TRP A 1 110 ? 37.89800  37.75500 -17.48700 1.000 133.30865 ?  118 TRP C CG  1 
ATOM   853  C CD1 . TRP A 1 110 ? 37.81500  36.41600 -17.70500 1.000 134.34496 ?  118 TRP C CD1 1 
ATOM   854  C CD2 . TRP A 1 110 ? 37.82200  37.93900 -16.07200 1.000 132.20979 ?  118 TRP C CD2 1 
ATOM   855  N NE1 . TRP A 1 110 ? 37.69500  35.74900 -16.51500 1.000 133.56056 ?  118 TRP C NE1 1 
ATOM   856  C CE2 . TRP A 1 110 ? 37.69800  36.66000 -15.49300 1.000 132.49449 ?  118 TRP C CE2 1 
ATOM   857  C CE3 . TRP A 1 110 ? 37.84500  39.06100 -15.23500 1.000 131.72556 ?  118 TRP C CE3 1 
ATOM   858  C CZ2 . TRP A 1 110 ? 37.60000  36.46500 -14.11600 1.000 132.98773 ?  118 TRP C CZ2 1 
ATOM   859  C CZ3 . TRP A 1 110 ? 37.75000  38.86700 -13.86400 1.000 132.78875 ?  118 TRP C CZ3 1 
ATOM   860  C CH2 . TRP A 1 110 ? 37.62900  37.57500 -13.31900 1.000 133.48803 ?  118 TRP C CH2 1 
ATOM   861  N N   . GLY A 1 111 ? 36.43200  41.30400 -18.77500 1.000 138.47289 ?  119 GLY C N   1 
ATOM   862  C CA  . GLY A 1 111 ? 36.37300  42.72300 -19.03100 1.000 137.99826 ?  119 GLY C CA  1 
ATOM   863  C C   . GLY A 1 111 ? 37.76200  43.28800 -19.23100 1.000 139.75550 ?  119 GLY C C   1 
ATOM   864  O O   . GLY A 1 111 ? 38.73400  42.57000 -19.48300 1.000 141.67143 ?  119 GLY C O   1 
ATOM   865  N N   . GLN A 1 112 ? 37.85100  44.60300 -19.11500 1.000 148.67805 ?  120 GLN C N   1 
ATOM   866  C CA  . GLN A 1 112 ? 39.12300  45.29400 -19.24900 1.000 149.95535 ?  120 GLN C CA  1 
ATOM   867  C C   . GLN A 1 112 ? 39.65300  45.79700 -17.92000 1.000 149.98685 ?  120 GLN C C   1 
ATOM   868  O O   . GLN A 1 112 ? 40.86700  45.77600 -17.69100 1.000 151.41434 ?  120 GLN C O   1 
ATOM   869  C CB  . GLN A 1 112 ? 38.98200  46.45000 -20.24500 1.000 149.73502 ?  120 GLN C CB  1 
ATOM   870  C CG  . GLN A 1 112 ? 38.05300  46.09500 -21.41700 1.000 149.47977 ?  120 GLN C CG  1 
ATOM   871  C CD  . GLN A 1 112 ? 38.49500  44.83300 -22.16600 1.000 151.13344 ?  120 GLN C CD  1 
ATOM   872  O OE1 . GLN A 1 112 ? 39.63900  44.72500 -22.60900 1.000 152.97512 ?  120 GLN C OE1 1 
ATOM   873  N NE2 . GLN A 1 112 ? 37.58200  43.86800 -22.29500 1.000 150.63550 ?  120 GLN C NE2 1 
ATOM   874  N N   . GLY A 1 113 ? 38.75800  46.24000 -17.04100 1.000 151.72469 ?  121 GLY C N   1 
ATOM   875  C CA  . GLY A 1 113 ? 39.11900  46.75000 -15.73700 1.000 152.80447 ?  121 GLY C CA  1 
ATOM   876  C C   . GLY A 1 113 ? 38.71200  48.19000 -15.55100 1.000 152.62986 ?  121 GLY C C   1 
ATOM   877  O O   . GLY A 1 113 ? 39.19800  49.06200 -16.27400 1.000 152.56041 ?  121 GLY C O   1 
ATOM   878  N N   . THR A 1 114 ? 37.81200  48.46500 -14.61200 1.000 154.53568 ?  122 THR C N   1 
ATOM   879  C CA  . THR A 1 114 ? 37.42900  49.84100 -14.31400 1.000 155.13837 ?  122 THR C CA  1 
ATOM   880  C C   . THR A 1 114 ? 37.68300  50.13400 -12.84000 1.000 157.73498 ?  122 THR C C   1 
ATOM   881  O O   . THR A 1 114 ? 37.27200  49.36200 -11.96900 1.000 158.75972 ?  122 THR C O   1 
ATOM   882  C CB  . THR A 1 114 ? 35.97000  50.10900 -14.69400 1.000 153.91446 ?  122 THR C CB  1 
ATOM   883  O OG1 . THR A 1 114 ? 35.62600  51.46600 -14.38800 1.000 155.03450 ?  122 THR C OG1 1 
ATOM   884  C CG2 . THR A 1 114 ? 35.03500  49.16800 -13.96600 1.000 154.07955 ?  122 THR C CG2 1 
ATOM   885  N N   . LEU A 1 115 ? 38.39400  51.22700 -12.56600 1.000 156.62746 ?  123 LEU C N   1 
ATOM   886  C CA  . LEU A 1 115 ? 38.87300  51.52100 -11.22100 1.000 159.63637 ?  123 LEU C CA  1 
ATOM   887  C C   . LEU A 1 115 ? 37.85000  52.35600 -10.46400 1.000 161.39506 ?  123 LEU C C   1 
ATOM   888  O O   . LEU A 1 115 ? 37.35100  53.36700 -10.98000 1.000 160.79051 ?  123 LEU C O   1 
ATOM   889  C CB  . LEU A 1 115 ? 40.21600  52.24900 -11.27100 1.000 160.58335 ?  123 LEU C CB  1 
ATOM   890  C CG  . LEU A 1 115 ? 41.02800  52.26600 -9.97300  1.000 163.78223 ?  123 LEU C CG  1 
ATOM   891  C CD1 . LEU A 1 115 ? 40.94800  50.92800 -9.27600  1.000 164.79154 ?  123 LEU C CD1 1 
ATOM   892  C CD2 . LEU A 1 115 ? 42.47400  52.61600 -10.26800 1.000 164.15655 ?  123 LEU C CD2 1 
ATOM   893  N N   . VAL A 1 116 ? 37.55400  51.94000 -9.23400  1.000 156.85258 ?  124 VAL C N   1 
ATOM   894  C CA  . VAL A 1 116 ? 36.63500  52.65400 -8.36300  1.000 159.52171 ?  124 VAL C CA  1 
ATOM   895  C C   . VAL A 1 116 ? 37.35700  52.97600 -7.06300  1.000 163.53230 ?  124 VAL C C   1 
ATOM   896  O O   . VAL A 1 116 ? 37.82700  52.06500 -6.35900  1.000 165.08302 ?  124 VAL C O   1 
ATOM   897  C CB  . VAL A 1 116 ? 35.36400  51.84000 -8.09800  1.000 159.64278 ?  124 VAL C CB  1 
ATOM   898  C CG1 . VAL A 1 116 ? 34.54500  52.49700 -7.00400  1.000 163.45853 ?  124 VAL C CG1 1 
ATOM   899  C CG2 . VAL A 1 116 ? 34.56400  51.69500 -9.37300  1.000 156.04556 ?  124 VAL C CG2 1 
ATOM   900  N N   . THR A 1 117 ? 37.43100  54.27000 -6.74800  1.000 160.74234 ?  125 THR C N   1 
ATOM   901  C CA  . THR A 1 117 ? 38.10200  54.77500 -5.55900  1.000 164.63704 ?  125 THR C CA  1 
ATOM   902  C C   . THR A 1 117 ? 37.07200  55.43800 -4.65800  1.000 168.02335 ?  125 THR C C   1 
ATOM   903  O O   . THR A 1 117 ? 36.38600  56.37200 -5.08200  1.000 167.59155 ?  125 THR C O   1 
ATOM   904  C CB  . THR A 1 117 ? 39.20100  55.77500 -5.91700  1.000 164.28901 ?  125 THR C CB  1 
ATOM   905  O OG1 . THR A 1 117 ? 40.18200  55.14200 -6.74900  1.000 161.52853 ?  125 THR C OG1 1 
ATOM   906  C CG2 . THR A 1 117 ? 39.86100  56.28900 -4.65100  1.000 168.79623 ?  125 THR C CG2 1 
ATOM   907  N N   . VAL A 1 118 ? 36.99400  54.98000 -3.41500  1.000 168.32559 ?  126 VAL C N   1 
ATOM   908  C CA  . VAL A 1 118 ? 36.06200  55.51200 -2.42500  1.000 172.20821 ?  126 VAL C CA  1 
ATOM   909  C C   . VAL A 1 118 ? 36.88300  56.41100 -1.50800  1.000 175.81756 ?  126 VAL C C   1 
ATOM   910  O O   . VAL A 1 118 ? 37.49300  55.96000 -0.53800  1.000 178.72867 ?  126 VAL C O   1 
ATOM   911  C CB  . VAL A 1 118 ? 35.35300  54.39900 -1.65400  1.000 174.19051 ?  126 VAL C CB  1 
ATOM   912  C CG1 . VAL A 1 118 ? 34.32900  54.98300 -0.69300  1.000 178.20293 ?  126 VAL C CG1 1 
ATOM   913  C CG2 . VAL A 1 118 ? 34.70500  53.41500 -2.61600  1.000 170.31253 ?  126 VAL C CG2 1 
ATOM   914  N N   . SER A 1 119 ? 36.90100  57.70600 -1.81700  1.000 178.96204 ?  127 SER C N   1 
ATOM   915  C CA  . SER A 1 119 ? 37.62900  58.65800 -0.99200  1.000 182.20893 ?  127 SER C CA  1 
ATOM   916  C C   . SER A 1 119 ? 36.91500  59.99900 -1.03500  1.000 183.25810 ?  127 SER C C   1 
ATOM   917  O O   . SER A 1 119 ? 36.38800  60.39800 -2.07600  1.000 180.15815 ?  127 SER C O   1 
ATOM   918  C CB  . SER A 1 119 ? 39.08400  58.80600 -1.46300  1.000 181.27192 ?  127 SER C CB  1 
ATOM   919  O OG  . SER A 1 119 ? 39.69900  59.95600 -0.90700  1.000 186.18798 ?  127 SER C OG  1 
ATOM   920  N N   . SER A 1 120 ? 36.92600  60.70000 0.09700   1.000 185.16770 ?  128 SER C N   1 
ATOM   921  C CA  . SER A 1 120 ? 36.28400  62.00300 0.18300   1.000 188.89933 ?  128 SER C CA  1 
ATOM   922  C C   . SER A 1 120 ? 37.18200  63.12700 -0.30300  1.000 192.21369 ?  128 SER C C   1 
ATOM   923  O O   . SER A 1 120 ? 36.73500  64.27700 -0.36600  1.000 195.56729 ?  128 SER C O   1 
ATOM   924  C CB  . SER A 1 120 ? 35.84600  62.27300 1.62200   1.000 194.24220 ?  128 SER C CB  1 
ATOM   925  O OG  . SER A 1 120 ? 36.93500  62.74900 2.38900   1.000 199.86284 ?  128 SER C OG  1 
ATOM   926  N N   . ALA A 1 121 ? 38.42800  62.81800 -0.64900  1.000 191.62553 ?  129 ALA C N   1 
ATOM   927  C CA  . ALA A 1 121 ? 39.32300  63.80200 -1.22300  1.000 194.40326 ?  129 ALA C CA  1 
ATOM   928  C C   . ALA A 1 121 ? 38.85000  64.17400 -2.62500  1.000 190.84990 ?  129 ALA C C   1 
ATOM   929  O O   . ALA A 1 121 ? 37.99600  63.51300 -3.22100  1.000 185.67414 ?  129 ALA C O   1 
ATOM   930  C CB  . ALA A 1 121 ? 40.75600  63.27200 -1.26300  1.000 194.50597 ?  129 ALA C CB  1 
ATOM   931  N N   . SER A 1 122 ? 39.41100  65.25200 -3.15200  1.000 193.97279 ?  130 SER C N   1 
ATOM   932  C CA  . SER A 1 122 ? 38.98100  65.78800 -4.43200  1.000 191.84616 ?  130 SER C CA  1 
ATOM   933  C C   . SER A 1 122 ? 39.98600  65.42700 -5.51800  1.000 189.06203 ?  130 SER C C   1 
ATOM   934  O O   . SER A 1 122 ? 41.18200  65.26800 -5.26000  1.000 190.89226 ?  130 SER C O   1 
ATOM   935  C CB  . SER A 1 122 ? 38.79200  67.30300 -4.36300  1.000 197.62976 ?  130 SER C CB  1 
ATOM   936  O OG  . SER A 1 122 ? 37.90300  67.73900 -5.37900  1.000 195.60029 ?  130 SER C OG  1 
ATOM   937  N N   . THR A 1 123 ? 39.47600  65.28800 -6.73900  1.000 184.84592 ?  131 THR C N   1 
ATOM   938  C CA  . THR A 1 123 ? 40.30400  64.94100 -7.88700  1.000 182.17829 ?  131 THR C CA  1 
ATOM   939  C C   . THR A 1 123 ? 41.38800  65.98800 -8.11300  1.000 187.13802 ?  131 THR C C   1 
ATOM   940  O O   . THR A 1 123 ? 41.12100  67.19300 -8.08800  1.000 191.32469 ?  131 THR C O   1 
ATOM   941  C CB  . THR A 1 123 ? 39.42600  64.81500 -9.13000  1.000 177.78773 ?  131 THR C CB  1 
ATOM   942  O OG1 . THR A 1 123 ? 38.16400  64.24600 -8.75900  1.000 174.72806 ?  131 THR C OG1 1 
ATOM   943  C CG2 . THR A 1 123 ? 40.08800  63.92700 -10.16900 1.000 173.62466 ?  131 THR C CG2 1 
ATOM   944  N N   . LYS A 1 124 ? 42.62100  65.52600 -8.31500  1.000 187.00517 ?  132 LYS C N   1 
ATOM   945  C CA  . LYS A 1 124 ? 43.75400  66.39300 -8.60600  1.000 191.43738 ?  132 LYS C CA  1 
ATOM   946  C C   . LYS A 1 124 ? 44.38500  66.00000 -9.93200  1.000 188.52686 ?  132 LYS C C   1 
ATOM   947  O O   . LYS A 1 124 ? 44.74900  64.83700 -10.13100 1.000 184.76923 ?  132 LYS C O   1 
ATOM   948  C CB  . LYS A 1 124 ? 44.80000  66.31200 -7.49100  1.000 195.32240 ?  132 LYS C CB  1 
ATOM   949  N N   . GLY A 1 125 ? 44.52800  66.97100 -10.82800 1.000 190.69331 ?  133 GLY C N   1 
ATOM   950  C CA  . GLY A 1 125 ? 45.20300  66.75900 -12.08700 1.000 189.06086 ?  133 GLY C CA  1 
ATOM   951  C C   . GLY A 1 125 ? 46.70100  66.58300 -11.94100 1.000 191.51726 ?  133 GLY C C   1 
ATOM   952  O O   . GLY A 1 125 ? 47.32000  67.08200 -10.99700 1.000 196.05432 ?  133 GLY C O   1 
ATOM   953  N N   . PRO A 1 126 ? 47.31200  65.88000 -12.88900 1.000 188.87008 ?  134 PRO C N   1 
ATOM   954  C CA  . PRO A 1 126 ? 48.74500  65.59000 -12.82700 1.000 190.98657 ?  134 PRO C CA  1 
ATOM   955  C C   . PRO A 1 126 ? 49.59300  66.69600 -13.44700 1.000 195.76484 ?  134 PRO C C   1 
ATOM   956  O O   . PRO A 1 126 ? 49.08800  67.65300 -14.03400 1.000 197.31483 ?  134 PRO C O   1 
ATOM   957  C CB  . PRO A 1 126 ? 48.85000  64.30600 -13.65400 1.000 185.91350 ?  134 PRO C CB  1 
ATOM   958  C CG  . PRO A 1 126 ? 47.84700  64.52900 -14.73600 1.000 183.10635 ?  134 PRO C CG  1 
ATOM   959  C CD  . PRO A 1 126 ? 46.69800  65.30300 -14.09500 1.000 184.02640 ?  134 PRO C CD  1 
ATOM   960  N N   . SER A 1 127 ? 50.90500  66.55800 -13.27400 1.000 198.45414 ?  135 SER C N   1 
ATOM   961  C CA  . SER A 1 127 ? 51.88100  67.36100 -13.99900 1.000 202.56630 ?  135 SER C CA  1 
ATOM   962  C C   . SER A 1 127 ? 52.94100  66.44700 -14.59600 1.000 201.31288 ?  135 SER C C   1 
ATOM   963  O O   . SER A 1 127 ? 53.30900  65.43500 -13.99600 1.000 199.62384 ?  135 SER C O   1 
ATOM   964  C CB  . SER A 1 127 ? 52.53700  68.42800 -13.11000 1.000 208.99908 ?  135 SER C CB  1 
ATOM   965  O OG  . SER A 1 127 ? 53.19000  67.84300 -12.00000 1.000 209.99356 ?  135 SER C OG  1 
ATOM   966  N N   . VAL A 1 128 ? 53.42100  66.80000 -15.78500 1.000 202.46612 ?  136 VAL C N   1 
ATOM   967  C CA  . VAL A 1 128 ? 54.38000  65.98700 -16.52200 1.000 201.60545 ?  136 VAL C CA  1 
ATOM   968  C C   . VAL A 1 128 ? 55.64200  66.80800 -16.74100 1.000 207.41381 ?  136 VAL C C   1 
ATOM   969  O O   . VAL A 1 128 ? 55.61000  67.84000 -17.42400 1.000 210.27207 ?  136 VAL C O   1 
ATOM   970  C CB  . VAL A 1 128 ? 53.81000  65.50600 -17.86200 1.000 197.61204 ?  136 VAL C CB  1 
ATOM   971  C CG1 . VAL A 1 128 ? 54.87000  64.73900 -18.64500 1.000 197.61351 ?  136 VAL C CG1 1 
ATOM   972  C CG2 . VAL A 1 128 ? 52.58700  64.65600 -17.61900 1.000 191.98336 ?  136 VAL C CG2 1 
ATOM   973  N N   . PHE A 1 129 ? 56.75000  66.34000 -16.18200 1.000 209.36147 ?  137 PHE C N   1 
ATOM   974  C CA  . PHE A 1 129 ? 58.01300  67.00000 -16.47500 1.000 214.75787 ?  137 PHE C CA  1 
ATOM   975  C C   . PHE A 1 129 ? 58.89500  66.12300 -17.35100 1.000 213.93314 ?  137 PHE C C   1 
ATOM   976  O O   . PHE A 1 129 ? 58.88800  64.88900 -17.20600 1.000 210.33245 ?  137 PHE C O   1 
ATOM   977  C CB  . PHE A 1 129 ? 58.80400  67.36000 -15.21200 1.000 219.23683 ?  137 PHE C CB  1 
ATOM   978  C CG  . PHE A 1 129 ? 57.96700  67.84300 -14.07600 1.000 219.62728 ?  137 PHE C CG  1 
ATOM   979  C CD1 . PHE A 1 129 ? 57.34300  69.07800 -14.12900 1.000 222.11212 ?  137 PHE C CD1 1 
ATOM   980  C CD2 . PHE A 1 129 ? 57.83100  67.07500 -12.93600 1.000 218.06154 ?  137 PHE C CD2 1 
ATOM   981  C CE1 . PHE A 1 129 ? 56.58100  69.52500 -13.07100 1.000 222.95544 ?  137 PHE C CE1 1 
ATOM   982  C CE2 . PHE A 1 129 ? 57.07200  67.51300 -11.87500 1.000 218.84885 ?  137 PHE C CE2 1 
ATOM   983  C CZ  . PHE A 1 129 ? 56.44500  68.74100 -11.94100 1.000 221.31551 ?  137 PHE C CZ  1 
ATOM   984  N N   . PRO A 1 130 ? 59.65100  66.73300 -18.26500 1.000 217.53113 ?  138 PRO C N   1 
ATOM   985  C CA  . PRO A 1 130 ? 60.55100  65.95100 -19.11100 1.000 217.51217 ?  138 PRO C CA  1 
ATOM   986  C C   . PRO A 1 130 ? 61.69000  65.39700 -18.27600 1.000 219.80949 ?  138 PRO C C   1 
ATOM   987  O O   . PRO A 1 130 ? 62.11200  65.99200 -17.28100 1.000 223.39557 ?  138 PRO C O   1 
ATOM   988  C CB  . PRO A 1 130 ? 61.06000  66.97500 -20.13400 1.000 221.88157 ?  138 PRO C CB  1 
ATOM   989  C CG  . PRO A 1 130 ? 60.99700  68.27600 -19.40500 1.000 226.03039 ?  138 PRO C CG  1 
ATOM   990  C CD  . PRO A 1 130 ? 59.80300  68.18300 -18.49100 1.000 222.52050 ?  138 PRO C CD  1 
ATOM   991  N N   . LEU A 1 131 ? 62.20200  64.25100 -18.70200 1.000 218.09224 ?  139 LEU C N   1 
ATOM   992  C CA  . LEU A 1 131 ? 63.41100  63.66000 -18.15200 1.000 220.76351 ?  139 LEU C CA  1 
ATOM   993  C C   . LEU A 1 131 ? 64.37800  63.59300 -19.32300 1.000 223.45769 ?  139 LEU C C   1 
ATOM   994  O O   . LEU A 1 131 ? 64.44000  62.58900 -20.04000 1.000 221.05152 ?  139 LEU C O   1 
ATOM   995  C CB  . LEU A 1 131 ? 63.12100  62.30900 -17.53600 1.000 216.73217 ?  139 LEU C CB  1 
ATOM   996  C CG  . LEU A 1 131 ? 61.90800  62.31400 -16.60400 1.000 213.27856 ?  139 LEU C CG  1 
ATOM   997  C CD1 . LEU A 1 131 ? 61.63500  60.92000 -16.07100 1.000 209.47420 ?  139 LEU C CD1 1 
ATOM   998  C CD2 . LEU A 1 131 ? 62.12200  63.29600 -15.46400 1.000 217.29111 ?  139 LEU C CD2 1 
ATOM   999  N N   . ALA A 1 132 ? 65.09400  64.69400 -19.51800 1.000 228.72270 ?  140 ALA C N   1 
ATOM   1000 C CA  . ALA A 1 132 ? 65.88200  64.89500 -20.72000 1.000 231.82198 ?  140 ALA C CA  1 
ATOM   1001 C C   . ALA A 1 132 ? 67.05000  63.91400 -20.76500 1.000 233.50182 ?  140 ALA C C   1 
ATOM   1002 O O   . ALA A 1 132 ? 67.72400  63.70200 -19.75300 1.000 235.55360 ?  140 ALA C O   1 
ATOM   1003 C CB  . ALA A 1 132 ? 66.39800  66.32900 -20.76000 1.000 237.54817 ?  140 ALA C CB  1 
ATOM   1004 N N   . PRO A 1 133 ? 67.34000  63.32300 -21.93400 1.000 233.18793 ?  141 PRO C N   1 
ATOM   1005 C CA  . PRO A 1 133 ? 68.50900  62.45200 -22.06700 1.000 235.60590 ?  141 PRO C CA  1 
ATOM   1006 C C   . PRO A 1 133 ? 69.78900  63.27200 -22.12300 1.000 242.38861 ?  141 PRO C C   1 
ATOM   1007 O O   . PRO A 1 133 ? 69.67900  64.48800 -22.28300 1.000 244.87198 ?  141 PRO C O   1 
ATOM   1008 C CB  . PRO A 1 133 ? 68.25600  61.72700 -23.38800 1.000 233.39903 ?  141 PRO C CB  1 
ATOM   1009 C CG  . PRO A 1 133 ? 67.45500  62.69100 -24.17900 1.000 232.77239 ?  141 PRO C CG  1 
ATOM   1010 C CD  . PRO A 1 133 ? 66.58900  63.43200 -23.19500 1.000 230.93734 ?  141 PRO C CD  1 
ATOM   1011 N N   . SER A 1 135 ? 74.46000  63.41800 -20.26700 1.000 261.34541 ?  143 SER C N   1 
ATOM   1012 C CA  . SER A 1 135 ? 75.77900  62.82000 -20.43300 1.000 265.69405 ?  143 SER C CA  1 
ATOM   1013 C C   . SER A 1 135 ? 75.81500  61.40700 -19.85400 1.000 263.10995 ?  143 SER C C   1 
ATOM   1014 O O   . SER A 1 135 ? 76.57100  60.55400 -20.32200 1.000 264.93576 ?  143 SER C O   1 
ATOM   1015 C CB  . SER A 1 135 ? 76.84700  63.69400 -19.77700 1.000 272.08654 ?  143 SER C CB  1 
ATOM   1016 O OG  . SER A 1 135 ? 76.57000  63.88800 -18.40200 1.000 271.45006 ?  143 SER C OG  1 
ATOM   1017 N N   . LYS A 1 136 ? 75.00200  61.16200 -18.82600 1.000 265.71152 ?  144 LYS C N   1 
ATOM   1018 C CA  . LYS A 1 136 ? 74.89800  59.81000 -18.29000 1.000 263.01106 ?  144 LYS C CA  1 
ATOM   1019 C C   . LYS A 1 136 ? 74.18800  58.88600 -19.27000 1.000 258.31658 ?  144 LYS C C   1 
ATOM   1020 O O   . LYS A 1 136 ? 74.59000  57.73000 -19.44600 1.000 258.34965 ?  144 LYS C O   1 
ATOM   1021 C CB  . LYS A 1 136 ? 74.17800  59.83100 -16.94400 1.000 260.40721 ?  144 LYS C CB  1 
ATOM   1022 N N   . SER A 1 137 ? 73.11700  59.37000 -19.90100 1.000 259.06295 ?  145 SER C N   1 
ATOM   1023 C CA  . SER A 1 137 ? 72.46700  58.59900 -20.95200 1.000 255.96345 ?  145 SER C CA  1 
ATOM   1024 C C   . SER A 1 137 ? 73.30100  58.54900 -22.22700 1.000 259.64643 ?  145 SER C C   1 
ATOM   1025 O O   . SER A 1 137 ? 73.02400  57.72500 -23.10400 1.000 258.25534 ?  145 SER C O   1 
ATOM   1026 C CB  . SER A 1 137 ? 71.07900  59.17300 -21.23000 1.000 251.05848 ?  145 SER C CB  1 
ATOM   1027 O OG  . SER A 1 137 ? 71.15900  60.35400 -22.00300 1.000 252.72883 ?  145 SER C OG  1 
ATOM   1028 N N   . THR A 1 138 ? 74.32200  59.40000 -22.34500 1.000 255.47009 ?  146 THR C N   1 
ATOM   1029 C CA  . THR A 1 138 ? 75.23900  59.36100 -23.47900 1.000 259.87318 ?  146 THR C CA  1 
ATOM   1030 C C   . THR A 1 138 ? 76.14600  58.13100 -23.43800 1.000 262.11506 ?  146 THR C C   1 
ATOM   1031 O O   . THR A 1 138 ? 77.00400  57.95900 -24.31000 1.000 266.29257 ?  146 THR C O   1 
ATOM   1032 C CB  . THR A 1 138 ? 76.05400  60.66200 -23.50300 1.000 265.62497 ?  146 THR C CB  1 
ATOM   1033 O OG1 . THR A 1 138 ? 75.15800  61.77100 -23.38200 1.000 263.63296 ?  146 THR C OG1 1 
ATOM   1034 C CG2 . THR A 1 138 ? 76.80700  60.83400 -24.81600 1.000 270.04953 ?  146 THR C CG2 1 
ATOM   1035 N N   . SER A 1 139 ? 75.94300  57.24700 -22.46700 1.000 262.30515 ?  147 SER C N   1 
ATOM   1036 C CA  . SER A 1 139 ? 76.68100  55.99500 -22.39800 1.000 264.20667 ?  147 SER C CA  1 
ATOM   1037 C C   . SER A 1 139 ? 75.92000  54.87700 -23.10600 1.000 259.86221 ?  147 SER C C   1 
ATOM   1038 O O   . SER A 1 139 ? 75.03900  54.24500 -22.52600 1.000 254.99946 ?  147 SER C O   1 
ATOM   1039 C CB  . SER A 1 139 ? 76.93700  55.61400 -20.94100 1.000 264.59781 ?  147 SER C CB  1 
ATOM   1040 O OG  . SER A 1 139 ? 75.76600  55.07600 -20.35400 1.000 258.60325 ?  147 SER C OG  1 
ATOM   1041 N N   . THR A 1 142 ? 73.30700  54.48200 -26.30300 1.000 246.57855 ?  150 THR C N   1 
ATOM   1042 C CA  . THR A 1 142 ? 71.89800  54.36500 -25.95000 1.000 239.90788 ?  150 THR C CA  1 
ATOM   1043 C C   . THR A 1 142 ? 71.55800  55.22800 -24.73800 1.000 238.50645 ?  150 THR C C   1 
ATOM   1044 O O   . THR A 1 142 ? 72.23400  55.17000 -23.71300 1.000 240.82603 ?  150 THR C O   1 
ATOM   1045 C CB  . THR A 1 142 ? 71.50800  52.90300 -25.67100 1.000 236.65892 ?  150 THR C CB  1 
ATOM   1046 O OG1 . THR A 1 142 ? 72.09500  52.05400 -26.66600 1.000 239.45188 ?  150 THR C OG1 1 
ATOM   1047 C CG2 . THR A 1 142 ? 69.99400  52.73800 -25.70100 1.000 229.93193 ?  150 THR C CG2 1 
ATOM   1048 N N   . ALA A 1 143 ? 70.50200  56.02800 -24.86700 1.000 234.82210 ?  151 ALA C N   1 
ATOM   1049 C CA  . ALA A 1 143 ? 70.10200  56.96100 -23.81700 1.000 233.84975 ?  151 ALA C CA  1 
ATOM   1050 C C   . ALA A 1 143 ? 68.87200  56.46600 -23.06000 1.000 227.80903 ?  151 ALA C C   1 
ATOM   1051 O O   . ALA A 1 143 ? 68.04400  55.73400 -23.60200 1.000 223.65454 ?  151 ALA C O   1 
ATOM   1052 C CB  . ALA A 1 143 ? 69.83700  58.34000 -24.41700 1.000 235.12970 ?  151 ALA C CB  1 
ATOM   1053 N N   . LEU A 1 145 ? 65.72700  58.81100 -21.93100 1.000 217.71800 ?  153 LEU C N   1 
ATOM   1054 C CA  . LEU A 1 145 ? 64.78200  59.87400 -21.59900 1.000 216.23243 ?  153 LEU C CA  1 
ATOM   1055 C C   . LEU A 1 145 ? 63.45800  59.33400 -21.08900 1.000 210.39762 ?  153 LEU C C   1 
ATOM   1056 O O   . LEU A 1 145 ? 63.08100  58.19800 -21.38500 1.000 206.89015 ?  153 LEU C O   1 
ATOM   1057 C CB  . LEU A 1 145 ? 64.53400  60.78300 -22.80500 1.000 217.36461 ?  153 LEU C CB  1 
ATOM   1058 C CG  . LEU A 1 145 ? 64.08800  60.25400 -24.17100 1.000 215.05053 ?  153 LEU C CG  1 
ATOM   1059 C CD1 . LEU A 1 145 ? 62.62400  59.82800 -24.19600 1.000 208.95559 ?  153 LEU C CD1 1 
ATOM   1060 C CD2 . LEU A 1 145 ? 64.34700  61.32200 -25.22200 1.000 218.73697 ?  153 LEU C CD2 1 
ATOM   1061 N N   . GLY A 1 146 ? 62.74700  60.16000 -20.33100 1.000 203.27835 ?  154 GLY C N   1 
ATOM   1062 C CA  . GLY A 1 146 ? 61.47800  59.72000 -19.79800 1.000 201.41063 ?  154 GLY C CA  1 
ATOM   1063 C C   . GLY A 1 146 ? 60.56500  60.87500 -19.44700 1.000 196.21833 ?  154 GLY C C   1 
ATOM   1064 O O   . GLY A 1 146 ? 60.82700  62.02900 -19.78500 1.000 194.44115 ?  154 GLY C O   1 
ATOM   1065 N N   . CYS A 1 147 ? 59.47000  60.53900 -18.78100 1.000 188.19793 ?  155 CYS C N   1 
ATOM   1066 C CA  . CYS A 1 147 ? 58.47400  61.48600 -18.32300 1.000 183.19989 ?  155 CYS C CA  1 
ATOM   1067 C C   . CYS A 1 147 ? 58.17800  61.21700 -16.86100 1.000 182.51864 ?  155 CYS C C   1 
ATOM   1068 O O   . CYS A 1 147 ? 58.23100  60.07000 -16.40500 1.000 185.56593 ?  155 CYS C O   1 
ATOM   1069 C CB  . CYS A 1 147 ? 57.19000  61.36400 -19.12300 1.000 180.97357 ?  155 CYS C CB  1 
ATOM   1070 S SG  . CYS A 1 147 ? 57.12000  62.44300 -20.53800 1.000 180.68663 ?  155 CYS C SG  1 
ATOM   1071 N N   . LEU A 1 148 ? 57.82900  62.27500 -16.14100 1.000 181.62283 ?  156 LEU C N   1 
ATOM   1072 C CA  . LEU A 1 148 ? 57.46000  62.15500 -14.73900 1.000 180.84970 ?  156 LEU C CA  1 
ATOM   1073 C C   . LEU A 1 148 ? 56.05500  62.70600 -14.56100 1.000 176.51936 ?  156 LEU C C   1 
ATOM   1074 O O   . LEU A 1 148 ? 55.81800  63.89000 -14.83000 1.000 174.12592 ?  156 LEU C O   1 
ATOM   1075 C CB  . LEU A 1 148 ? 58.45300  62.89400 -13.84300 1.000 181.68437 ?  156 LEU C CB  1 
ATOM   1076 C CG  . LEU A 1 148 ? 57.94600  63.25300 -12.44700 1.000 180.00211 ?  156 LEU C CG  1 
ATOM   1077 C CD1 . LEU A 1 148 ? 57.60900  62.01100 -11.62500 1.000 182.52632 ?  156 LEU C CD1 1 
ATOM   1078 C CD2 . LEU A 1 148 ? 58.99300  64.08200 -11.73800 1.000 181.27447 ?  156 LEU C CD2 1 
ATOM   1079 N N   . VAL A 1 149 ? 55.12600  61.84700 -14.14000 1.000 174.95940 ?  157 VAL C N   1 
ATOM   1080 C CA  . VAL A 1 149 ? 53.75200  62.25300 -13.86500 1.000 172.33838 ?  157 VAL C CA  1 
ATOM   1081 C C   . VAL A 1 149 ? 53.59300  62.33900 -12.35400 1.000 172.47213 ?  157 VAL C C   1 
ATOM   1082 O O   . VAL A 1 149 ? 53.54100  61.31800 -11.66000 1.000 174.40532 ?  157 VAL C O   1 
ATOM   1083 C CB  . VAL A 1 149 ? 52.73200  61.28700 -14.48100 1.000 172.51956 ?  157 VAL C CB  1 
ATOM   1084 C CG1 . VAL A 1 149 ? 51.32900  61.62600 -13.98800 1.000 171.11554 ?  157 VAL C CG1 1 
ATOM   1085 C CG2 . VAL A 1 149 ? 52.79900  61.35000 -15.99200 1.000 172.68099 ?  157 VAL C CG2 1 
ATOM   1086 N N   . LYS A 1 150 ? 53.50000  63.56500 -11.85600 1.000 174.35742 ?  158 LYS C N   1 
ATOM   1087 C CA  . LYS A 1 150 ? 53.55200  63.87800 -10.43900 1.000 174.72269 ?  158 LYS C CA  1 
ATOM   1088 C C   . LYS A 1 150 ? 52.25900  64.54800 -9.99500  1.000 173.52153 ?  158 LYS C C   1 
ATOM   1089 O O   . LYS A 1 150 ? 51.61500  65.26500 -10.76700 1.000 172.37905 ?  158 LYS C O   1 
ATOM   1090 C CB  . LYS A 1 150 ? 54.74400  64.78800 -10.12200 1.000 175.14039 ?  158 LYS C CB  1 
ATOM   1091 N N   . ASP A 1 151 ? 51.88700  64.29800 -8.73800  1.000 178.50335 ?  159 ASP C N   1 
ATOM   1092 C CA  . ASP A 1 151 ? 50.78400  64.99000 -8.07300  1.000 177.93247 ?  159 ASP C CA  1 
ATOM   1093 C C   . ASP A 1 151 ? 49.46300  64.81200 -8.82400  1.000 177.86300 ?  159 ASP C C   1 
ATOM   1094 O O   . ASP A 1 151 ? 48.88400  65.76200 -9.35100  1.000 176.85373 ?  159 ASP C O   1 
ATOM   1095 C CB  . ASP A 1 151 ? 51.11400  66.47500 -7.89200  1.000 176.07130 ?  159 ASP C CB  1 
ATOM   1096 C CG  . ASP A 1 151 ? 52.01300  66.72800 -6.70300  1.000 176.76667 ?  159 ASP C CG  1 
ATOM   1097 O OD1 . ASP A 1 151 ? 52.02500  65.89100 -5.77800  1.000 179.15312 ?  159 ASP C OD1 1 
ATOM   1098 O OD2 . ASP A 1 151 ? 52.70800  67.76500 -6.69100  1.000 175.55579 -1 159 ASP C OD2 1 
ATOM   1099 N N   . TYR A 1 152 ? 48.99900  63.56500 -8.87600  1.000 171.83676 ?  160 TYR C N   1 
ATOM   1100 C CA  . TYR A 1 152 ? 47.70300  63.23600 -9.45000  1.000 172.57118 ?  160 TYR C CA  1 
ATOM   1101 C C   . TYR A 1 152 ? 46.90700  62.35800 -8.49300  1.000 175.64405 ?  160 TYR C C   1 
ATOM   1102 O O   . TYR A 1 152 ? 47.47300  61.59400 -7.70600  1.000 177.31978 ?  160 TYR C O   1 
ATOM   1103 C CB  . TYR A 1 152 ? 47.86800  62.56500 -10.83100 1.000 172.04571 ?  160 TYR C CB  1 
ATOM   1104 C CG  . TYR A 1 152 ? 48.17000  61.08300 -10.82400 1.000 173.92571 ?  160 TYR C CG  1 
ATOM   1105 C CD1 . TYR A 1 152 ? 47.16400  60.13600 -10.67100 1.000 176.00565 ?  160 TYR C CD1 1 
ATOM   1106 C CD2 . TYR A 1 152 ? 49.47500  60.63200 -10.97100 1.000 174.24349 ?  160 TYR C CD2 1 
ATOM   1107 C CE1 . TYR A 1 152 ? 47.45300  58.78100 -10.66900 1.000 177.97214 ?  160 TYR C CE1 1 
ATOM   1108 C CE2 . TYR A 1 152 ? 49.77300  59.28700 -10.96800 1.000 176.56907 ?  160 TYR C CE2 1 
ATOM   1109 C CZ  . TYR A 1 152 ? 48.75900  58.36300 -10.81900 1.000 178.22081 ?  160 TYR C CZ  1 
ATOM   1110 O OH  . TYR A 1 152 ? 49.04900  57.01800 -10.81000 1.000 180.71269 ?  160 TYR C OH  1 
ATOM   1111 N N   . PHE A 1 153 ? 45.57700  62.48300 -8.57100  1.000 166.45649 ?  161 PHE C N   1 
ATOM   1112 C CA  . PHE A 1 153 ? 44.64400  61.71900 -7.75200  1.000 170.21170 ?  161 PHE C CA  1 
ATOM   1113 C C   . PHE A 1 153 ? 43.29500  61.75200 -8.44500  1.000 171.31332 ?  161 PHE C C   1 
ATOM   1114 O O   . PHE A 1 153 ? 42.92500  62.79800 -8.99200  1.000 169.77614 ?  161 PHE C O   1 
ATOM   1115 C CB  . PHE A 1 153 ? 44.53000  62.28400 -6.32800  1.000 172.17872 ?  161 PHE C CB  1 
ATOM   1116 C CG  . PHE A 1 153 ? 43.42700  61.65900 -5.50400  1.000 176.98147 ?  161 PHE C CG  1 
ATOM   1117 C CD1 . PHE A 1 153 ? 43.66000  60.50800 -4.76800  1.000 179.57586 ?  161 PHE C CD1 1 
ATOM   1118 C CD2 . PHE A 1 153 ? 42.16700  62.23600 -5.44600  1.000 179.42234 ?  161 PHE C CD2 1 
ATOM   1119 C CE1 . PHE A 1 153 ? 42.65400  59.93200 -4.00800  1.000 184.15006 ?  161 PHE C CE1 1 
ATOM   1120 C CE2 . PHE A 1 153 ? 41.15900  61.66500 -4.68800  1.000 184.73582 ?  161 PHE C CE2 1 
ATOM   1121 C CZ  . PHE A 1 153 ? 41.40400  60.51300 -3.96800  1.000 186.78090 ?  161 PHE C CZ  1 
ATOM   1122 N N   . PRO A 1 154 ? 42.55200  60.64700 -8.46800  1.000 171.21098 ?  162 PRO C N   1 
ATOM   1123 C CA  . PRO A 1 154 ? 42.92000  59.32100 -7.96800  1.000 173.48922 ?  162 PRO C CA  1 
ATOM   1124 C C   . PRO A 1 154 ? 43.55200  58.50800 -9.08500  1.000 171.36507 ?  162 PRO C C   1 
ATOM   1125 O O   . PRO A 1 154 ? 43.72200  59.01900 -10.18700 1.000 168.34976 ?  162 PRO C O   1 
ATOM   1126 C CB  . PRO A 1 154 ? 41.57300  58.75500 -7.51400  1.000 177.89538 ?  162 PRO C CB  1 
ATOM   1127 C CG  . PRO A 1 154 ? 40.61000  59.30500 -8.54300  1.000 175.78803 ?  162 PRO C CG  1 
ATOM   1128 C CD  . PRO A 1 154 ? 41.14400  60.68300 -8.90900  1.000 172.55797 ?  162 PRO C CD  1 
ATOM   1129 N N   . GLU A 1 155 ? 43.91700  57.25100 -8.84100  1.000 169.36308 ?  163 GLU C N   1 
ATOM   1130 C CA  . GLU A 1 155 ? 44.39000  56.41000 -9.92200  1.000 168.04268 ?  163 GLU C CA  1 
ATOM   1131 C C   . GLU A 1 155 ? 43.24300  56.18400 -10.90800 1.000 168.05728 ?  163 GLU C C   1 
ATOM   1132 O O   . GLU A 1 155 ? 42.07100  56.27500 -10.53700 1.000 169.95726 ?  163 GLU C O   1 
ATOM   1133 C CB  . GLU A 1 155 ? 44.89000  55.07600 -9.36600  1.000 170.87862 ?  163 GLU C CB  1 
ATOM   1134 C CG  . GLU A 1 155 ? 46.35100  55.05100 -8.92800  1.000 170.38195 ?  163 GLU C CG  1 
ATOM   1135 C CD  . GLU A 1 155 ? 47.24100  54.26700 -9.87900  1.000 169.93317 ?  163 GLU C CD  1 
ATOM   1136 O OE1 . GLU A 1 155 ? 47.06600  54.39000 -11.10600 1.000 167.96299 ?  163 GLU C OE1 1 
ATOM   1137 O OE2 . GLU A 1 155 ? 48.11200  53.51300 -9.39900  1.000 172.00663 -1 163 GLU C OE2 1 
ATOM   1138 N N   . PRO A 1 156 ? 43.54800  55.87300 -12.17500 1.000 171.68134 ?  164 PRO C N   1 
ATOM   1139 C CA  . PRO A 1 156 ? 44.85400  55.65400 -12.79900 1.000 170.29606 ?  164 PRO C CA  1 
ATOM   1140 C C   . PRO A 1 156 ? 45.34300  56.78200 -13.70000 1.000 167.35204 ?  164 PRO C C   1 
ATOM   1141 O O   . PRO A 1 156 ? 44.63700  57.74400 -13.99500 1.000 166.15994 ?  164 PRO C O   1 
ATOM   1142 C CB  . PRO A 1 156 ? 44.60000  54.38400 -13.61000 1.000 171.40163 ?  164 PRO C CB  1 
ATOM   1143 C CG  . PRO A 1 156 ? 43.18700  54.59400 -14.12800 1.000 170.96202 ?  164 PRO C CG  1 
ATOM   1144 C CD  . PRO A 1 156 ? 42.47000  55.44200 -13.08200 1.000 171.54263 ?  164 PRO C CD  1 
ATOM   1145 N N   . VAL A 1 157 ? 46.59700  56.67600 -14.13000 1.000 173.28932 ?  165 VAL C N   1 
ATOM   1146 C CA  . VAL A 1 157 ? 47.16600  57.54500 -15.15200 1.000 171.42616 ?  165 VAL C CA  1 
ATOM   1147 C C   . VAL A 1 157 ? 47.84100  56.66800 -16.19600 1.000 172.47315 ?  165 VAL C C   1 
ATOM   1148 O O   . VAL A 1 157 ? 48.57800  55.73900 -15.84700 1.000 174.18035 ?  165 VAL C O   1 
ATOM   1149 C CB  . VAL A 1 157 ? 48.16000  58.56200 -14.56000 1.000 170.18865 ?  165 VAL C CB  1 
ATOM   1150 C CG1 . VAL A 1 157 ? 49.20500  58.94600 -15.58700 1.000 169.65772 ?  165 VAL C CG1 1 
ATOM   1151 C CG2 . VAL A 1 157 ? 47.42200  59.80300 -14.10700 1.000 168.77643 ?  165 VAL C CG2 1 
ATOM   1152 N N   . THR A 1 158 ? 47.57200  56.94300 -17.47000 1.000 172.80984 ?  166 THR C N   1 
ATOM   1153 C CA  . THR A 1 158 ? 48.18600  56.21300 -18.57300 1.000 174.87401 ?  166 THR C CA  1 
ATOM   1154 C C   . THR A 1 158 ? 49.21500  57.10500 -19.25500 1.000 175.36024 ?  166 THR C C   1 
ATOM   1155 O O   . THR A 1 158 ? 48.92800  58.26500 -19.54500 1.000 174.51377 ?  166 THR C O   1 
ATOM   1156 C CB  . THR A 1 158 ? 47.13000  55.76500 -19.58400 1.000 176.09736 ?  166 THR C CB  1 
ATOM   1157 O OG1 . THR A 1 158 ? 46.81600  56.85300 -20.46200 1.000 176.39056 ?  166 THR C OG1 1 
ATOM   1158 C CG2 . THR A 1 158 ? 45.86200  55.33200 -18.86100 1.000 175.17561 ?  166 THR C CG2 1 
ATOM   1159 N N   . VAL A 1 159 ? 50.41600  56.58700 -19.49600 1.000 179.31320 ?  167 VAL C N   1 
ATOM   1160 C CA  . VAL A 1 159 ? 51.46500  57.36700 -20.15200 1.000 180.47313 ?  167 VAL C CA  1 
ATOM   1161 C C   . VAL A 1 159 ? 52.00200  56.53100 -21.30700 1.000 184.43665 ?  167 VAL C C   1 
ATOM   1162 O O   . VAL A 1 159 ? 52.89000  55.69300 -21.11900 1.000 186.58365 ?  167 VAL C O   1 
ATOM   1163 C CB  . VAL A 1 159 ? 52.59400  57.77800 -19.20100 1.000 179.69294 ?  167 VAL C CB  1 
ATOM   1164 C CG1 . VAL A 1 159 ? 53.54800  58.75100 -19.90800 1.000 180.73494 ?  167 VAL C CG1 1 
ATOM   1165 C CG2 . VAL A 1 159 ? 52.03900  58.38400 -17.92700 1.000 176.48312 ?  167 VAL C CG2 1 
ATOM   1166 N N   . SER A 1 160 ? 51.48900  56.78000 -22.50600 1.000 184.52378 ?  168 SER C N   1 
ATOM   1167 C CA  . SER A 1 160 ? 52.03600  56.21800 -23.72300 1.000 189.07478 ?  168 SER C CA  1 
ATOM   1168 C C   . SER A 1 160 ? 53.18800  57.09200 -24.19400 1.000 190.90524 ?  168 SER C C   1 
ATOM   1169 O O   . SER A 1 160 ? 53.45500  58.15800 -23.64200 1.000 188.39981 ?  168 SER C O   1 
ATOM   1170 C CB  . SER A 1 160 ? 50.97000  56.13800 -24.81400 1.000 191.16421 ?  168 SER C CB  1 
ATOM   1171 O OG  . SER A 1 160 ? 50.76100  57.40800 -25.41600 1.000 191.92303 ?  168 SER C OG  1 
ATOM   1172 N N   . TRP A 1 161 ? 53.88100  56.63700 -25.22800 1.000 188.08016 ?  169 TRP C N   1 
ATOM   1173 C CA  . TRP A 1 161 ? 54.97600  57.40500 -25.80100 1.000 190.55808 ?  169 TRP C CA  1 
ATOM   1174 C C   . TRP A 1 161 ? 54.75900  57.52800 -27.30100 1.000 195.28458 ?  169 TRP C C   1 
ATOM   1175 O O   . TRP A 1 161 ? 54.56300  56.52000 -27.98800 1.000 198.17434 ?  169 TRP C O   1 
ATOM   1176 C CB  . TRP A 1 161 ? 56.32400  56.76000 -25.47400 1.000 192.55221 ?  169 TRP C CB  1 
ATOM   1177 C CG  . TRP A 1 161 ? 56.85000  57.12000 -24.11500 1.000 189.16239 ?  169 TRP C CG  1 
ATOM   1178 C CD1 . TRP A 1 161 ? 56.65600  56.43600 -22.95000 1.000 187.43395 ?  169 TRP C CD1 1 
ATOM   1179 C CD2 . TRP A 1 161 ? 57.65900  58.25500 -23.78500 1.000 187.67846 ?  169 TRP C CD2 1 
ATOM   1180 N NE1 . TRP A 1 161 ? 57.29600  57.07500 -21.91500 1.000 185.36563 ?  169 TRP C NE1 1 
ATOM   1181 C CE2 . TRP A 1 161 ? 57.91900  58.19500 -22.40200 1.000 185.15501 ?  169 TRP C CE2 1 
ATOM   1182 C CE3 . TRP A 1 161 ? 58.19000  59.31500 -24.52600 1.000 188.78684 ?  169 TRP C CE3 1 
ATOM   1183 C CZ2 . TRP A 1 161 ? 58.68500  59.15600 -21.74400 1.000 183.36182 ?  169 TRP C CZ2 1 
ATOM   1184 C CZ3 . TRP A 1 161 ? 58.95200  60.26600 -23.87400 1.000 186.68823 ?  169 TRP C CZ3 1 
ATOM   1185 C CH2 . TRP A 1 161 ? 59.19300  60.18000 -22.49700 1.000 183.80437 ?  169 TRP C CH2 1 
ATOM   1186 N N   . ASN A 1 162 ? 54.77100  58.76900 -27.79300 1.000 193.10488 ?  170 ASN C N   1 
ATOM   1187 C CA  . ASN A 1 162 ? 54.65200  59.07800 -29.21800 1.000 198.67764 ?  170 ASN C CA  1 
ATOM   1188 C C   . ASN A 1 162 ? 53.36200  58.51700 -29.82200 1.000 199.37058 ?  170 ASN C C   1 
ATOM   1189 O O   . ASN A 1 162 ? 53.36700  57.89100 -30.88500 1.000 202.26997 ?  170 ASN C O   1 
ATOM   1190 C CB  . ASN A 1 162 ? 55.88600  58.58400 -29.97500 1.000 203.61985 ?  170 ASN C CB  1 
ATOM   1191 C CG  . ASN A 1 162 ? 57.12100  59.41400 -29.67400 1.000 203.66854 ?  170 ASN C CG  1 
ATOM   1192 O OD1 . ASN A 1 162 ? 57.04200  60.44900 -29.01000 1.000 199.89795 ?  170 ASN C OD1 1 
ATOM   1193 N ND2 . ASN A 1 162 ? 58.27400  58.95500 -30.14800 1.000 207.63088 ?  170 ASN C ND2 1 
ATOM   1194 N N   . SER A 1 163 ? 52.24600  58.75600 -29.12700 1.000 198.24818 ?  171 SER C N   1 
ATOM   1195 C CA  . SER A 1 163 ? 50.91100  58.35200 -29.58000 1.000 198.46957 ?  171 SER C CA  1 
ATOM   1196 C C   . SER A 1 163 ? 50.85200  56.86200 -29.90700 1.000 199.09120 ?  171 SER C C   1 
ATOM   1197 O O   . SER A 1 163 ? 50.40700  56.44800 -30.98000 1.000 200.90943 ?  171 SER C O   1 
ATOM   1198 C CB  . SER A 1 163 ? 50.46600  59.19300 -30.77700 1.000 200.94598 ?  171 SER C CB  1 
ATOM   1199 O OG  . SER A 1 163 ? 50.11700  60.50400 -30.37600 1.000 199.87470 ?  171 SER C OG  1 
ATOM   1200 N N   . GLY A 1 164 ? 51.32300  56.04800 -28.96700 1.000 196.21108 ?  172 GLY C N   1 
ATOM   1201 C CA  . GLY A 1 164 ? 51.27700  54.61600 -29.10900 1.000 197.09634 ?  172 GLY C CA  1 
ATOM   1202 C C   . GLY A 1 164 ? 52.45300  54.02900 -29.85700 1.000 199.59942 ?  172 GLY C C   1 
ATOM   1203 O O   . GLY A 1 164 ? 52.76000  52.84700 -29.67100 1.000 199.89202 ?  172 GLY C O   1 
ATOM   1204 N N   . ALA A 1 165 ? 53.11000  54.82200 -30.70700 1.000 196.90944 ?  173 ALA C N   1 
ATOM   1205 C CA  . ALA A 1 165 ? 54.17500  54.29500 -31.55200 1.000 200.39920 ?  173 ALA C CA  1 
ATOM   1206 C C   . ALA A 1 165 ? 55.38000  53.87000 -30.72100 1.000 200.42404 ?  173 ALA C C   1 
ATOM   1207 O O   . ALA A 1 165 ? 55.89200  52.75400 -30.87400 1.000 201.28191 ?  173 ALA C O   1 
ATOM   1208 C CB  . ALA A 1 165 ? 54.58100  55.33600 -32.59500 1.000 204.75171 ?  173 ALA C CB  1 
ATOM   1209 N N   . LEU A 1 166 ? 55.85100  54.74800 -29.83800 1.000 200.25083 ?  174 LEU C N   1 
ATOM   1210 C CA  . LEU A 1 166 ? 57.02900  54.45300 -29.02700 1.000 200.04785 ?  174 LEU C CA  1 
ATOM   1211 C C   . LEU A 1 166 ? 56.63400  53.46800 -27.93400 1.000 197.39400 ?  174 LEU C C   1 
ATOM   1212 O O   . LEU A 1 166 ? 56.07900  53.85100 -26.90100 1.000 194.39208 ?  174 LEU C O   1 
ATOM   1213 C CB  . LEU A 1 166 ? 57.59700  55.74100 -28.44300 1.000 198.56518 ?  174 LEU C CB  1 
ATOM   1214 C CG  . LEU A 1 166 ? 58.96000  55.70200 -27.74800 1.000 198.21017 ?  174 LEU C CG  1 
ATOM   1215 C CD1 . LEU A 1 166 ? 59.96500  54.93900 -28.59000 1.000 202.46814 ?  174 LEU C CD1 1 
ATOM   1216 C CD2 . LEU A 1 166 ? 59.45600  57.11200 -27.45100 1.000 196.64167 ?  174 LEU C CD2 1 
ATOM   1217 N N   . THR A 1 167 ? 56.92700  52.19300 -28.15500 1.000 194.73424 ?  175 THR C N   1 
ATOM   1218 C CA  . THR A 1 167 ? 56.59400  51.13800 -27.20500 1.000 193.55337 ?  175 THR C CA  1 
ATOM   1219 C C   . THR A 1 167 ? 57.76400  50.22700 -26.87900 1.000 194.65097 ?  175 THR C C   1 
ATOM   1220 O O   . THR A 1 167 ? 57.87300  49.76900 -25.73900 1.000 193.92584 ?  175 THR C O   1 
ATOM   1221 C CB  . THR A 1 167 ? 55.42800  50.30800 -27.75300 1.000 193.30550 ?  175 THR C CB  1 
ATOM   1222 O OG1 . THR A 1 167 ? 55.58800  50.13200 -29.16700 1.000 194.69368 ?  175 THR C OG1 1 
ATOM   1223 C CG2 . THR A 1 167 ? 54.11700  51.00700 -27.47100 1.000 191.68890 ?  175 THR C CG2 1 
ATOM   1224 N N   . SER A 1 168 ? 58.62900  49.93300 -27.85100 1.000 193.70694 ?  176 SER C N   1 
ATOM   1225 C CA  . SER A 1 168 ? 59.76100  49.05300 -27.59900 1.000 194.75241 ?  176 SER C CA  1 
ATOM   1226 C C   . SER A 1 168 ? 60.66500  49.66500 -26.54000 1.000 194.01365 ?  176 SER C C   1 
ATOM   1227 O O   . SER A 1 168 ? 61.11400  50.80600 -26.67500 1.000 194.07824 ?  176 SER C O   1 
ATOM   1228 C CB  . SER A 1 168 ? 60.54500  48.80300 -28.89000 1.000 197.66385 ?  176 SER C CB  1 
ATOM   1229 O OG  . SER A 1 168 ? 59.69600  48.30300 -29.90800 1.000 198.07115 ?  176 SER C OG  1 
ATOM   1230 N N   . GLY A 1 169 ? 60.93500  48.90400 -25.48500 1.000 199.61008 ?  177 GLY C N   1 
ATOM   1231 C CA  . GLY A 1 169 ? 61.80700  49.40800 -24.44500 1.000 199.07359 ?  177 GLY C CA  1 
ATOM   1232 C C   . GLY A 1 169 ? 61.16500  50.42900 -23.53300 1.000 197.18782 ?  177 GLY C C   1 
ATOM   1233 O O   . GLY A 1 169 ? 61.86700  51.28500 -22.98700 1.000 196.49545 ?  177 GLY C O   1 
ATOM   1234 N N   . VAL A 1 170 ? 59.84500  50.38400 -23.36900 1.000 197.74659 ?  178 VAL C N   1 
ATOM   1235 C CA  . VAL A 1 170 ? 59.14500  51.27500 -22.45100 1.000 196.16718 ?  178 VAL C CA  1 
ATOM   1236 C C   . VAL A 1 170 ? 59.00600  50.57100 -21.10600 1.000 195.21597 ?  178 VAL C C   1 
ATOM   1237 O O   . VAL A 1 170 ? 58.57500  49.41400 -21.03900 1.000 194.96288 ?  178 VAL C O   1 
ATOM   1238 C CB  . VAL A 1 170 ? 57.77300  51.67900 -23.01700 1.000 194.81906 ?  178 VAL C CB  1 
ATOM   1239 C CG1 . VAL A 1 170 ? 56.84000  52.14000 -21.89900 1.000 189.52805 ?  178 VAL C CG1 1 
ATOM   1240 C CG2 . VAL A 1 170 ? 57.92500  52.76200 -24.07600 1.000 194.99392 ?  178 VAL C CG2 1 
ATOM   1241 N N   . HIS A 1 171 ? 59.37000  51.27600 -20.03400 1.000 198.86368 ?  179 HIS C N   1 
ATOM   1242 C CA  . HIS A 1 171 ? 59.36600  50.75800 -18.66300 1.000 197.52618 ?  179 HIS C CA  1 
ATOM   1243 C C   . HIS A 1 171 ? 58.60200  51.73100 -17.76400 1.000 193.32251 ?  179 HIS C C   1 
ATOM   1244 O O   . HIS A 1 171 ? 59.15400  52.32300 -16.83900 1.000 193.31560 ?  179 HIS C O   1 
ATOM   1245 C CB  . HIS A 1 171 ? 60.77500  50.52200 -18.11900 1.000 200.10077 ?  179 HIS C CB  1 
ATOM   1246 C CG  . HIS A 1 171 ? 61.61100  49.61200 -18.96100 1.000 202.17677 ?  179 HIS C CG  1 
ATOM   1247 N ND1 . HIS A 1 171 ? 62.42900  50.07000 -19.97000 1.000 202.87812 ?  179 HIS C ND1 1 
ATOM   1248 C CD2 . HIS A 1 171 ? 61.77300  48.26900 -18.92800 1.000 203.13382 ?  179 HIS C CD2 1 
ATOM   1249 C CE1 . HIS A 1 171 ? 63.04500  49.04600 -20.53400 1.000 204.23764 ?  179 HIS C CE1 1 
ATOM   1250 N NE2 . HIS A 1 171 ? 62.66600  47.94200 -19.91800 1.000 204.58577 ?  179 HIS C NE2 1 
ATOM   1251 N N   . THR A 1 172 ? 57.30700  51.88600 -18.03900 1.000 192.50867 ?  180 THR C N   1 
ATOM   1252 C CA  . THR A 1 172 ? 56.44000  52.71400 -17.20700 1.000 187.58484 ?  180 THR C CA  1 
ATOM   1253 C C   . THR A 1 172 ? 56.37300  52.20300 -15.77300 1.000 186.88359 ?  180 THR C C   1 
ATOM   1254 O O   . THR A 1 172 ? 55.78100  51.15300 -15.50400 1.000 186.78877 ?  180 THR C O   1 
ATOM   1255 C CB  . THR A 1 172 ? 55.02500  52.76400 -17.79000 1.000 184.30528 ?  180 THR C CB  1 
ATOM   1256 O OG1 . THR A 1 172 ? 55.08600  52.98700 -19.20400 1.000 185.88747 ?  180 THR C OG1 1 
ATOM   1257 C CG2 . THR A 1 172 ? 54.21600  53.87600 -17.13100 1.000 179.80452 ?  180 THR C CG2 1 
ATOM   1258 N N   . PHE A 1 173 ? 56.96600  52.95400 -14.84800 1.000 191.68143 ?  181 PHE C N   1 
ATOM   1259 C CA  . PHE A 1 173 ? 57.02900  52.52500 -13.46200 1.000 191.76122 ?  181 PHE C CA  1 
ATOM   1260 C C   . PHE A 1 173 ? 55.65000  52.61000 -12.80800 1.000 187.88359 ?  181 PHE C C   1 
ATOM   1261 O O   . PHE A 1 173 ? 54.80500  53.41100 -13.21800 1.000 184.76176 ?  181 PHE C O   1 
ATOM   1262 C CB  . PHE A 1 173 ? 58.02300  53.38200 -12.68200 1.000 193.03360 ?  181 PHE C CB  1 
ATOM   1263 N N   . PRO A 1 174 ? 55.39800  51.78700 -11.79200 1.000 192.64451 ?  182 PRO C N   1 
ATOM   1264 C CA  . PRO A 1 174 ? 54.14600  51.90000 -11.03300 1.000 190.10316 ?  182 PRO C CA  1 
ATOM   1265 C C   . PRO A 1 174 ? 54.04500  53.23800 -10.31700 1.000 187.98296 ?  182 PRO C C   1 
ATOM   1266 O O   . PRO A 1 174 ? 54.98900  54.02900 -10.26500 1.000 188.43491 ?  182 PRO C O   1 
ATOM   1267 C CB  . PRO A 1 174 ? 54.22300  50.73400 -10.04100 1.000 192.16227 ?  182 PRO C CB  1 
ATOM   1268 C CG  . PRO A 1 174 ? 55.20500  49.77900 -10.65400 1.000 195.19301 ?  182 PRO C CG  1 
ATOM   1269 C CD  . PRO A 1 174 ? 56.21100  50.64600 -11.34100 1.000 196.03379 ?  182 PRO C CD  1 
ATOM   1270 N N   . ALA A 1 175 ? 52.87100  53.48700 -9.74800  1.000 186.49272 ?  183 ALA C N   1 
ATOM   1271 C CA  . ALA A 1 175 ? 52.65800  54.74000 -9.04800  1.000 184.70499 ?  183 ALA C CA  1 
ATOM   1272 C C   . ALA A 1 175 ? 53.21900  54.65800 -7.63200  1.000 186.39494 ?  183 ALA C C   1 
ATOM   1273 O O   . ALA A 1 175 ? 53.41000  53.57600 -7.06800  1.000 188.55366 ?  183 ALA C O   1 
ATOM   1274 C CB  . ALA A 1 175 ? 51.17000  55.09600 -9.00300  1.000 182.95595 ?  183 ALA C CB  1 
ATOM   1275 N N   . VAL A 1 176 ? 53.48700  55.82700 -7.05700  1.000 190.61749 ?  184 VAL C N   1 
ATOM   1276 C CA  . VAL A 1 176 ? 53.93700  55.94900 -5.67700  1.000 192.14452 ?  184 VAL C CA  1 
ATOM   1277 C C   . VAL A 1 176 ? 52.95800  56.84200 -4.93200  1.000 190.66102 ?  184 VAL C C   1 
ATOM   1278 O O   . VAL A 1 176 ? 52.46500  57.83500 -5.47900  1.000 188.36703 ?  184 VAL C O   1 
ATOM   1279 C CB  . VAL A 1 176 ? 55.37800  56.50200 -5.57000  1.000 193.56556 ?  184 VAL C CB  1 
ATOM   1280 C CG1 . VAL A 1 176 ? 56.30900  55.76300 -6.50100  1.000 195.67089 ?  184 VAL C CG1 1 
ATOM   1281 C CG2 . VAL A 1 176 ? 55.42700  57.99900 -5.85400  1.000 191.26578 ?  184 VAL C CG2 1 
ATOM   1282 N N   . LEU A 1 177 ? 52.63600  56.45600 -3.70200  1.000 195.82731 ?  185 LEU C N   1 
ATOM   1283 C CA  . LEU A 1 177 ? 51.81900  57.29800 -2.83300  1.000 195.44839 ?  185 LEU C CA  1 
ATOM   1284 C C   . LEU A 1 177 ? 52.73500  58.34300 -2.21100  1.000 195.44551 ?  185 LEU C C   1 
ATOM   1285 O O   . LEU A 1 177 ? 53.38400  58.10400 -1.19000  1.000 197.46664 ?  185 LEU C O   1 
ATOM   1286 C CB  . LEU A 1 177 ? 51.11600  56.46400 -1.76900  1.000 197.50566 ?  185 LEU C CB  1 
ATOM   1287 N N   . GLN A 1 178 ? 52.80600  59.51200 -2.84900  1.000 189.07584 ?  186 GLN C N   1 
ATOM   1288 C CA  . GLN A 1 178 ? 53.62400  60.59500 -2.32400  1.000 189.28180 ?  186 GLN C CA  1 
ATOM   1289 C C   . GLN A 1 178 ? 53.14200  60.98400 -0.93400  1.000 190.62894 ?  186 GLN C C   1 
ATOM   1290 O O   . GLN A 1 178 ? 51.94000  60.97100 -0.65300  1.000 190.35679 ?  186 GLN C O   1 
ATOM   1291 C CB  . GLN A 1 178 ? 53.57900  61.80500 -3.26000  1.000 186.12455 ?  186 GLN C CB  1 
ATOM   1292 N N   . SER A 1 179 ? 54.09800  61.30600 -0.05600  1.000 194.04128 ?  187 SER C N   1 
ATOM   1293 C CA  . SER A 1 179 ? 53.77700  61.66900 1.32300   1.000 196.63261 ?  187 SER C CA  1 
ATOM   1294 C C   . SER A 1 179 ? 52.68100  62.72400 1.40300   1.000 195.07673 ?  187 SER C C   1 
ATOM   1295 O O   . SER A 1 179 ? 51.93600  62.77300 2.38800   1.000 197.36869 ?  187 SER C O   1 
ATOM   1296 C CB  . SER A 1 179 ? 55.03300  62.17600 2.03400   1.000 198.97573 ?  187 SER C CB  1 
ATOM   1297 O OG  . SER A 1 179 ? 55.62100  63.24300 1.31200   1.000 196.64713 ?  187 SER C OG  1 
ATOM   1298 N N   . SER A 1 180 ? 52.57600  63.58300 0.38700   1.000 198.53342 ?  188 SER C N   1 
ATOM   1299 C CA  . SER A 1 180 ? 51.46100  64.52200 0.30600   1.000 197.17184 ?  188 SER C CA  1 
ATOM   1300 C C   . SER A 1 180 ? 50.11800  63.80900 0.24600   1.000 198.10493 ?  188 SER C C   1 
ATOM   1301 O O   . SER A 1 180 ? 49.11600  64.32400 0.75500   1.000 199.52352 ?  188 SER C O   1 
ATOM   1302 C CB  . SER A 1 180 ? 51.62400  65.42200 -0.91600  1.000 193.53935 ?  188 SER C CB  1 
ATOM   1303 O OG  . SER A 1 180 ? 51.65000  64.65900 -2.11100  1.000 192.32951 ?  188 SER C OG  1 
ATOM   1304 N N   . GLY A 1 181 ? 50.07200  62.63700 -0.37800  1.000 189.31476 ?  189 GLY C N   1 
ATOM   1305 C CA  . GLY A 1 181 ? 48.82300  61.94200 -0.61600  1.000 190.09826 ?  189 GLY C CA  1 
ATOM   1306 C C   . GLY A 1 181 ? 48.40100  61.88400 -2.06800  1.000 187.83796 ?  189 GLY C C   1 
ATOM   1307 O O   . GLY A 1 181 ? 47.29600  61.40400 -2.35900  1.000 188.78257 ?  189 GLY C O   1 
ATOM   1308 N N   . LEU A 1 182 ? 49.24600  62.35300 -2.98300  1.000 189.26647 ?  190 LEU C N   1 
ATOM   1309 C CA  . LEU A 1 182 ? 49.00600  62.28800 -4.41500  1.000 187.21322 ?  190 LEU C CA  1 
ATOM   1310 C C   . LEU A 1 182 ? 49.87200  61.19100 -5.01600  1.000 187.07197 ?  190 LEU C C   1 
ATOM   1311 O O   . LEU A 1 182 ? 50.92500  60.84400 -4.47500  1.000 188.05806 ?  190 LEU C O   1 
ATOM   1312 C CB  . LEU A 1 182 ? 49.32800  63.62300 -5.09300  1.000 184.53038 ?  190 LEU C CB  1 
ATOM   1313 N N   . TYR A 1 183 ? 49.41700  60.63600 -6.13200  1.000 183.64520 ?  191 TYR C N   1 
ATOM   1314 C CA  . TYR A 1 183 ? 50.14600  59.57300 -6.80000  1.000 183.91924 ?  191 TYR C CA  1 
ATOM   1315 C C   . TYR A 1 183 ? 51.20400  60.14800 -7.73400  1.000 182.21772 ?  191 TYR C C   1 
ATOM   1316 O O   . TYR A 1 183 ? 51.09600  61.28100 -8.21200  1.000 180.18620 ?  191 TYR C O   1 
ATOM   1317 C CB  . TYR A 1 183 ? 49.18700  58.66600 -7.57200  1.000 184.30519 ?  191 TYR C CB  1 
ATOM   1318 N N   . SER A 1 184 ? 52.24000  59.35200 -7.98700  1.000 181.51363 ?  192 SER C N   1 
ATOM   1319 C CA  . SER A 1 184 ? 53.31400  59.76900 -8.87400  1.000 181.06211 ?  192 SER C CA  1 
ATOM   1320 C C   . SER A 1 184 ? 53.93000  58.54200 -9.52000  1.000 183.27668 ?  192 SER C C   1 
ATOM   1321 O O   . SER A 1 184 ? 54.11300  57.51200 -8.86700  1.000 185.59660 ?  192 SER C O   1 
ATOM   1322 C CB  . SER A 1 184 ? 54.39200  60.56100 -8.12800  1.000 181.73017 ?  192 SER C CB  1 
ATOM   1323 O OG  . SER A 1 184 ? 53.90500  61.82400 -7.71800  1.000 179.57495 ?  192 SER C OG  1 
ATOM   1324 N N   . LEU A 1 185 ? 54.26200  58.66900 -10.80000 1.000 174.20375 ?  193 LEU C N   1 
ATOM   1325 C CA  . LEU A 1 185 ? 54.86600  57.58600 -11.55400 1.000 176.83099 ?  193 LEU C CA  1 
ATOM   1326 C C   . LEU A 1 185 ? 55.85500  58.18500 -12.54200 1.000 177.63989 ?  193 LEU C C   1 
ATOM   1327 O O   . LEU A 1 185 ? 55.95800  59.40800 -12.69500 1.000 175.51403 ?  193 LEU C O   1 
ATOM   1328 C CB  . LEU A 1 185 ? 53.80700  56.75700 -12.28500 1.000 176.26489 ?  193 LEU C CB  1 
ATOM   1329 C CG  . LEU A 1 185 ? 53.10400  57.49900 -13.42300 1.000 173.90611 ?  193 LEU C CG  1 
ATOM   1330 C CD1 . LEU A 1 185 ? 53.63800  57.07600 -14.79500 1.000 175.66204 ?  193 LEU C CD1 1 
ATOM   1331 C CD2 . LEU A 1 185 ? 51.60400  57.31400 -13.34300 1.000 172.47718 ?  193 LEU C CD2 1 
ATOM   1332 N N   . SER A 1 186 ? 56.52500  57.30200 -13.27200 1.000 172.47733 ?  194 SER C N   1 
ATOM   1333 C CA  . SER A 1 186 ? 57.58100  57.69700 -14.19300 1.000 174.62233 ?  194 SER C CA  1 
ATOM   1334 C C   . SER A 1 186 ? 57.56000  56.72800 -15.36200 1.000 176.92988 ?  194 SER C C   1 
ATOM   1335 O O   . SER A 1 186 ? 57.75300  55.52300 -15.17300 1.000 179.91561 ?  194 SER C O   1 
ATOM   1336 C CB  . SER A 1 186 ? 58.95100  57.67800 -13.50500 1.000 179.41310 ?  194 SER C CB  1 
ATOM   1337 O OG  . SER A 1 186 ? 59.18100  56.46100 -12.80500 1.000 182.86869 ?  194 SER C OG  1 
ATOM   1338 N N   . SER A 1 187 ? 57.34900  57.24700 -16.56600 1.000 176.76513 ?  195 SER C N   1 
ATOM   1339 C CA  . SER A 1 187 ? 57.35600  56.41900 -17.76200 1.000 178.87323 ?  195 SER C CA  1 
ATOM   1340 C C   . SER A 1 187 ? 58.66400  56.69400 -18.47600 1.000 182.67847 ?  195 SER C C   1 
ATOM   1341 O O   . SER A 1 187 ? 58.94700  57.83500 -18.83400 1.000 180.82714 ?  195 SER C O   1 
ATOM   1342 C CB  . SER A 1 187 ? 56.17400  56.74300 -18.67700 1.000 175.49716 ?  195 SER C CB  1 
ATOM   1343 O OG  . SER A 1 187 ? 55.95400  55.72700 -19.64500 1.000 177.58399 ?  195 SER C OG  1 
ATOM   1344 N N   . VAL A 1 188 ? 59.44000  55.65200 -18.73900 1.000 184.92146 ?  196 VAL C N   1 
ATOM   1345 C CA  . VAL A 1 188 ? 60.73800  55.85500 -19.35900 1.000 187.82128 ?  196 VAL C CA  1 
ATOM   1346 C C   . VAL A 1 188 ? 60.84100  54.96100 -20.58200 1.000 190.42299 ?  196 VAL C C   1 
ATOM   1347 O O   . VAL A 1 188 ? 60.12000  53.97100 -20.72800 1.000 192.51818 ?  196 VAL C O   1 
ATOM   1348 C CB  . VAL A 1 188 ? 61.90100  55.59500 -18.37200 1.000 190.05591 ?  196 VAL C CB  1 
ATOM   1349 C CG1 . VAL A 1 188 ? 61.78400  56.49500 -17.15000 1.000 188.04599 ?  196 VAL C CG1 1 
ATOM   1350 C CG2 . VAL A 1 188 ? 61.89900  54.14700 -17.92000 1.000 193.46690 ?  196 VAL C CG2 1 
ATOM   1351 N N   . VAL A 1 189 ? 61.75800  55.32700 -21.46600 1.000 199.51698 ?  197 VAL C N   1 
ATOM   1352 C CA  . VAL A 1 189 ? 62.00900  54.54400 -22.66600 1.000 201.63427 ?  197 VAL C CA  1 
ATOM   1353 C C   . VAL A 1 189 ? 63.47600  54.71000 -23.02700 1.000 202.35194 ?  197 VAL C C   1 
ATOM   1354 O O   . VAL A 1 189 ? 63.97600  55.83000 -23.18200 1.000 201.50830 ?  197 VAL C O   1 
ATOM   1355 C CB  . VAL A 1 189 ? 61.06600  54.94100 -23.82100 1.000 201.23037 ?  197 VAL C CB  1 
ATOM   1356 C CG1 . VAL A 1 189 ? 61.08400  56.43800 -24.06300 1.000 199.33546 ?  197 VAL C CG1 1 
ATOM   1357 C CG2 . VAL A 1 189 ? 61.44400  54.19900 -25.10100 1.000 203.11264 ?  197 VAL C CG2 1 
ATOM   1358 N N   . THR A 1 190 ? 64.17900  53.58800 -23.10500 1.000 210.41569 ?  198 THR C N   1 
ATOM   1359 C CA  . THR A 1 190 ? 65.59100  53.57600 -23.45900 1.000 211.59259 ?  198 THR C CA  1 
ATOM   1360 C C   . THR A 1 190 ? 65.73600  53.83800 -24.95100 1.000 212.81130 ?  198 THR C C   1 
ATOM   1361 O O   . THR A 1 190 ? 65.28700  53.03300 -25.77300 1.000 213.78117 ?  198 THR C O   1 
ATOM   1362 C CB  . THR A 1 190 ? 66.19400  52.23000 -23.08100 1.000 213.07336 ?  198 THR C CB  1 
ATOM   1363 O OG1 . THR A 1 190 ? 65.93600  51.29000 -24.13000 1.000 214.17735 ?  198 THR C OG1 1 
ATOM   1364 C CG2 . THR A 1 190 ? 65.55000  51.71800 -21.80400 1.000 212.78245 ?  198 THR C CG2 1 
ATOM   1365 N N   . VAL A 1 191 ? 66.34100  54.96900 -25.30600 1.000 218.73645 ?  199 VAL C N   1 
ATOM   1366 C CA  . VAL A 1 191 ? 66.47600  55.34600 -26.71100 1.000 221.35726 ?  199 VAL C CA  1 
ATOM   1367 C C   . VAL A 1 191 ? 67.95700  55.48600 -27.05600 1.000 223.97665 ?  199 VAL C C   1 
ATOM   1368 O O   . VAL A 1 191 ? 68.72200  56.03500 -26.25900 1.000 223.22152 ?  199 VAL C O   1 
ATOM   1369 C CB  . VAL A 1 191 ? 65.69900  56.64000 -26.99700 1.000 220.97653 ?  199 VAL C CB  1 
ATOM   1370 C CG1 . VAL A 1 191 ? 66.09500  57.73600 -26.00900 1.000 218.85526 ?  199 VAL C CG1 1 
ATOM   1371 C CG2 . VAL A 1 191 ? 65.88700  57.08000 -28.43700 1.000 225.38382 ?  199 VAL C CG2 1 
ATOM   1372 N N   . PRO A 1 192 ? 68.39900  55.02600 -28.22500 1.000 225.48630 ?  200 PRO C N   1 
ATOM   1373 C CA  . PRO A 1 192 ? 69.82400  55.13500 -28.58300 1.000 228.45451 ?  200 PRO C CA  1 
ATOM   1374 C C   . PRO A 1 192 ? 70.33300  56.56800 -28.74100 1.000 230.19960 ?  200 PRO C C   1 
ATOM   1375 O O   . PRO A 1 192 ? 69.63400  57.44800 -29.24400 1.000 231.19784 ?  200 PRO C O   1 
ATOM   1376 C CB  . PRO A 1 192 ? 69.91500  54.34600 -29.89400 1.000 232.01457 ?  200 PRO C CB  1 
ATOM   1377 C CG  . PRO A 1 192 ? 68.78900  53.35600 -29.79200 1.000 229.72059 ?  200 PRO C CG  1 
ATOM   1378 C CD  . PRO A 1 192 ? 67.68000  54.09100 -29.10400 1.000 226.63045 ?  200 PRO C CD  1 
ATOM   1379 N N   . SER A 1 193 ? 71.57700  56.78700 -28.29300 1.000 235.11575 ?  201 SER C N   1 
ATOM   1380 C CA  . SER A 1 193 ? 72.21900  58.09300 -28.44300 1.000 237.15198 ?  201 SER C CA  1 
ATOM   1381 C C   . SER A 1 193 ? 72.45700  58.45200 -29.90700 1.000 242.56618 ?  201 SER C C   1 
ATOM   1382 O O   . SER A 1 193 ? 72.28200  59.61200 -30.30200 1.000 244.58272 ?  201 SER C O   1 
ATOM   1383 C CB  . SER A 1 193 ? 73.54300  58.11800 -27.67900 1.000 237.25375 ?  201 SER C CB  1 
ATOM   1384 O OG  . SER A 1 193 ? 73.36800  57.75100 -26.32400 1.000 233.33901 ?  201 SER C OG  1 
ATOM   1385 N N   . SER A 1 194 ? 72.87400  57.47800 -30.72500 1.000 233.41816 ?  202 SER C N   1 
ATOM   1386 C CA  . SER A 1 194 ? 73.05600  57.72400 -32.15600 1.000 239.24776 ?  202 SER C CA  1 
ATOM   1387 C C   . SER A 1 194 ? 71.79200  58.27500 -32.80500 1.000 240.52089 ?  202 SER C C   1 
ATOM   1388 O O   . SER A 1 194 ? 71.87200  59.06500 -33.75300 1.000 245.39368 ?  202 SER C O   1 
ATOM   1389 C CB  . SER A 1 194 ? 73.50800  56.44200 -32.86200 1.000 241.64578 ?  202 SER C CB  1 
ATOM   1390 O OG  . SER A 1 194 ? 72.49100  55.45700 -32.85800 1.000 239.24635 ?  202 SER C OG  1 
ATOM   1391 N N   . SER A 1 195 ? 70.62500  57.85000 -32.32500 1.000 234.11278 ?  203 SER C N   1 
ATOM   1392 C CA  . SER A 1 195 ? 69.35300  58.31000 -32.87400 1.000 235.38674 ?  203 SER C CA  1 
ATOM   1393 C C   . SER A 1 195 ? 69.16800  59.82400 -32.76600 1.000 236.22059 ?  203 SER C C   1 
ATOM   1394 O O   . SER A 1 195 ? 68.54700  60.42800 -33.64400 1.000 240.44949 ?  203 SER C O   1 
ATOM   1395 C CB  . SER A 1 195 ? 68.21100  57.58500 -32.17600 1.000 230.48360 ?  203 SER C CB  1 
ATOM   1396 O OG  . SER A 1 195 ? 67.87900  58.23400 -30.96300 1.000 225.76833 ?  203 SER C OG  1 
ATOM   1397 N N   . LEU A 1 196 ? 69.68100  60.45100 -31.70700 1.000 231.90091 ?  204 LEU C N   1 
ATOM   1398 C CA  . LEU A 1 196 ? 69.61100  61.90400 -31.53500 1.000 232.32743 ?  204 LEU C CA  1 
ATOM   1399 C C   . LEU A 1 196 ? 68.20400  62.48100 -31.70500 1.000 231.54275 ?  204 LEU C C   1 
ATOM   1400 O O   . LEU A 1 196 ? 67.35600  62.32200 -30.82100 1.000 226.25528 ?  204 LEU C O   1 
ATOM   1401 C CB  . LEU A 1 196 ? 70.56700  62.60000 -32.51100 1.000 238.77323 ?  204 LEU C CB  1 
ATOM   1402 N N   . GLY A 1 197 ? 67.95600  63.17400 -32.81400 1.000 228.78967 ?  205 GLY C N   1 
ATOM   1403 C CA  . GLY A 1 197 ? 66.65500  63.74600 -33.12100 1.000 229.40488 ?  205 GLY C CA  1 
ATOM   1404 C C   . GLY A 1 197 ? 65.95600  63.09400 -34.29500 1.000 234.84522 ?  205 GLY C C   1 
ATOM   1405 O O   . GLY A 1 197 ? 65.00700  63.65100 -34.85100 1.000 237.66980 ?  205 GLY C O   1 
ATOM   1406 N N   . THR A 1 198 ? 66.42300  61.91200 -34.68300 1.000 229.72745 ?  206 THR C N   1 
ATOM   1407 C CA  . THR A 1 198 ? 65.89100  61.26900 -35.87600 1.000 235.77123 ?  206 THR C CA  1 
ATOM   1408 C C   . THR A 1 198 ? 64.41300  60.92400 -35.72700 1.000 233.99941 ?  206 THR C C   1 
ATOM   1409 O O   . THR A 1 198 ? 63.62700  61.12800 -36.66100 1.000 239.51073 ?  206 THR C O   1 
ATOM   1410 C CB  . THR A 1 198 ? 66.72800  60.03400 -36.17300 1.000 236.71772 ?  206 THR C CB  1 
ATOM   1411 O OG1 . THR A 1 198 ? 66.82300  59.22100 -34.99700 1.000 229.26918 ?  206 THR C OG1 1 
ATOM   1412 C CG2 . THR A 1 198 ? 68.12000  60.47500 -36.60200 1.000 240.60342 ?  206 THR C CG2 1 
ATOM   1413 N N   . GLN A 1 199 ? 64.01600  60.37400 -34.58500 1.000 231.57132 ?  207 GLN C N   1 
ATOM   1414 C CA  . GLN A 1 199 ? 62.59800  60.27800 -34.26400 1.000 228.92640 ?  207 GLN C CA  1 
ATOM   1415 C C   . GLN A 1 199 ? 62.21400  61.50700 -33.44000 1.000 224.77919 ?  207 GLN C C   1 
ATOM   1416 O O   . GLN A 1 199 ? 62.93200  62.50900 -33.41900 1.000 226.05916 ?  207 GLN C O   1 
ATOM   1417 C CB  . GLN A 1 199 ? 62.25500  58.98000 -33.51800 1.000 223.41925 ?  207 GLN C CB  1 
ATOM   1418 C CG  . GLN A 1 199 ? 63.21500  58.56400 -32.43200 1.000 218.32557 ?  207 GLN C CG  1 
ATOM   1419 C CD  . GLN A 1 199 ? 64.43900  57.86100 -32.95200 1.000 220.91565 ?  207 GLN C CD  1 
ATOM   1420 O OE1 . GLN A 1 199 ? 64.73600  57.89300 -34.14600 1.000 226.96228 ?  207 GLN C OE1 1 
ATOM   1421 N NE2 . GLN A 1 199 ? 65.15800  57.20700 -32.05200 1.000 216.76354 ?  207 GLN C NE2 1 
ATOM   1422 N N   . THR A 1 200 ? 61.06000  61.45200 -32.78700 1.000 226.04780 ?  208 THR C N   1 
ATOM   1423 C CA  . THR A 1 200 ? 60.58800  62.46500 -31.85700 1.000 221.07740 ?  208 THR C CA  1 
ATOM   1424 C C   . THR A 1 200 ? 60.43600  61.83800 -30.47500 1.000 213.59414 ?  208 THR C C   1 
ATOM   1425 O O   . THR A 1 200 ? 60.39400  60.61300 -30.33100 1.000 212.45636 ?  208 THR C O   1 
ATOM   1426 C CB  . THR A 1 200 ? 59.26300  63.07600 -32.31800 1.000 222.61733 ?  208 THR C CB  1 
ATOM   1427 O OG1 . THR A 1 200 ? 58.86900  64.10700 -31.40400 1.000 217.85456 ?  208 THR C OG1 1 
ATOM   1428 C CG2 . THR A 1 200 ? 58.18400  62.01000 -32.38900 1.000 221.40332 ?  208 THR C CG2 1 
ATOM   1429 N N   . TYR A 1 201 ? 60.38000  62.68000 -29.44300 1.000 218.08777 ?  209 TYR C N   1 
ATOM   1430 C CA  . TYR A 1 201 ? 60.27300  62.19400 -28.06700 1.000 211.61953 ?  209 TYR C CA  1 
ATOM   1431 C C   . TYR A 1 201 ? 59.18600  62.98200 -27.35200 1.000 207.63792 ?  209 TYR C C   1 
ATOM   1432 O O   . TYR A 1 201 ? 59.42800  64.08200 -26.84900 1.000 205.84251 ?  209 TYR C O   1 
ATOM   1433 C CB  . TYR A 1 201 ? 61.60400  62.32500 -27.34800 1.000 209.94341 ?  209 TYR C CB  1 
ATOM   1434 C CG  . TYR A 1 201 ? 62.73600  61.82000 -28.18800 1.000 214.56241 ?  209 TYR C CG  1 
ATOM   1435 C CD1 . TYR A 1 201 ? 62.97800  60.45900 -28.29800 1.000 215.17364 ?  209 TYR C CD1 1 
ATOM   1436 C CD2 . TYR A 1 201 ? 63.53700  62.69700 -28.90500 1.000 218.60145 ?  209 TYR C CD2 1 
ATOM   1437 C CE1 . TYR A 1 201 ? 64.00200  59.98300 -29.07600 1.000 219.29564 ?  209 TYR C CE1 1 
ATOM   1438 C CE2 . TYR A 1 201 ? 64.56100  62.23100 -29.68900 1.000 223.09903 ?  209 TYR C CE2 1 
ATOM   1439 C CZ  . TYR A 1 201 ? 64.79200  60.87000 -29.77100 1.000 223.30264 ?  209 TYR C CZ  1 
ATOM   1440 O OH  . TYR A 1 201 ? 65.81800  60.39100 -30.55100 1.000 227.63182 ?  209 TYR C OH  1 
ATOM   1441 N N   . ILE A 1 202 ? 57.99500  62.39300 -27.30800 1.000 197.04444 ?  210 ILE C N   1 
ATOM   1442 C CA  . ILE A 1 202 ? 56.83100  62.97300 -26.65300 1.000 193.43232 ?  210 ILE C CA  1 
ATOM   1443 C C   . ILE A 1 202 ? 56.10200  61.84900 -25.93300 1.000 189.91908 ?  210 ILE C C   1 
ATOM   1444 O O   . ILE A 1 202 ? 55.80300  60.81500 -26.54000 1.000 191.87662 ?  210 ILE C O   1 
ATOM   1445 C CB  . ILE A 1 202 ? 55.88500  63.66100 -27.65800 1.000 196.84609 ?  210 ILE C CB  1 
ATOM   1446 C CG1 . ILE A 1 202 ? 56.45100  65.00800 -28.10000 1.000 199.56612 ?  210 ILE C CG1 1 
ATOM   1447 C CG2 . ILE A 1 202 ? 54.52100  63.87100 -27.02300 1.000 193.13016 ?  210 ILE C CG2 1 
ATOM   1448 C CD1 . ILE A 1 202 ? 55.96600  65.48000 -29.44700 1.000 205.28291 ?  210 ILE C CD1 1 
ATOM   1449 N N   . CYS A 1 203 ? 55.83500  62.03100 -24.64800 1.000 190.85257 ?  211 CYS C N   1 
ATOM   1450 C CA  . CYS A 1 203 ? 54.99200  61.10500 -23.90800 1.000 187.92743 ?  211 CYS C CA  1 
ATOM   1451 C C   . CYS A 1 203 ? 53.57200  61.65500 -23.84100 1.000 186.88949 ?  211 CYS C C   1 
ATOM   1452 O O   . CYS A 1 203 ? 53.36700  62.83500 -23.52900 1.000 185.38402 ?  211 CYS C O   1 
ATOM   1453 C CB  . CYS A 1 203 ? 55.54500  60.83300 -22.50700 1.000 183.91060 ?  211 CYS C CB  1 
ATOM   1454 S SG  . CYS A 1 203 ? 55.26500  62.11200 -21.28100 1.000 179.03072 ?  211 CYS C SG  1 
ATOM   1455 N N   . ASN A 1 204 ? 52.60200  60.80000 -24.16900 1.000 187.20353 ?  212 ASN C N   1 
ATOM   1456 C CA  . ASN A 1 204 ? 51.18500  61.13700 -24.14900 1.000 186.69602 ?  212 ASN C CA  1 
ATOM   1457 C C   . ASN A 1 204 ? 50.60700  60.57100 -22.85800 1.000 182.71229 ?  212 ASN C C   1 
ATOM   1458 O O   . ASN A 1 204 ? 50.38000  59.36600 -22.75100 1.000 182.38916 ?  212 ASN C O   1 
ATOM   1459 C CB  . ASN A 1 204 ? 50.44800  60.54800 -25.35200 1.000 190.22837 ?  212 ASN C CB  1 
ATOM   1460 C CG  . ASN A 1 204 ? 51.17500  60.77100 -26.65900 1.000 195.03060 ?  212 ASN C CG  1 
ATOM   1461 O OD1 . ASN A 1 204 ? 52.08300  60.01700 -27.00800 1.000 196.43270 ?  212 ASN C OD1 1 
ATOM   1462 N ND2 . ASN A 1 204 ? 50.75600  61.78100 -27.41000 1.000 198.10915 ?  212 ASN C ND2 1 
ATOM   1463 N N   . VAL A 1 205 ? 50.33500  61.43400 -21.90900 1.000 181.83791 ?  213 VAL C N   1 
ATOM   1464 C CA  . VAL A 1 205 ? 49.71500  61.07700 -20.64600 1.000 178.50046 ?  213 VAL C CA  1 
ATOM   1465 C C   . VAL A 1 205 ? 48.23100  61.37600 -20.74300 1.000 179.09021 ?  213 VAL C C   1 
ATOM   1466 O O   . VAL A 1 205 ? 47.82400  62.35400 -21.37200 1.000 180.98158 ?  213 VAL C O   1 
ATOM   1467 C CB  . VAL A 1 205 ? 50.35900  61.85500 -19.48400 1.000 175.37177 ?  213 VAL C CB  1 
ATOM   1468 C CG1 . VAL A 1 205 ? 49.95300  61.25500 -18.16200 1.000 172.90759 ?  213 VAL C CG1 1 
ATOM   1469 C CG2 . VAL A 1 205 ? 51.87100  61.87400 -19.63500 1.000 175.34810 ?  213 VAL C CG2 1 
ATOM   1470 N N   . ASN A 1 206 ? 47.42000  60.51100 -20.14900 1.000 175.14547 ?  214 ASN C N   1 
ATOM   1471 C CA  . ASN A 1 206 ? 45.98500  60.71500 -20.07700 1.000 175.41026 ?  214 ASN C CA  1 
ATOM   1472 C C   . ASN A 1 206 ? 45.52800  60.35100 -18.67100 1.000 173.26757 ?  214 ASN C C   1 
ATOM   1473 O O   . ASN A 1 206 ? 45.92100  59.31200 -18.12800 1.000 172.46569 ?  214 ASN C O   1 
ATOM   1474 C CB  . ASN A 1 206 ? 45.25300  59.88900 -21.14100 1.000 177.33256 ?  214 ASN C CB  1 
ATOM   1475 C CG  . ASN A 1 206 ? 43.75400  60.04500 -21.06400 1.000 177.19607 ?  214 ASN C CG  1 
ATOM   1476 O OD1 . ASN A 1 206 ? 43.18700  60.96000 -21.66400 1.000 178.48538 ?  214 ASN C OD1 1 
ATOM   1477 N ND2 . ASN A 1 206 ? 43.10000  59.15800 -20.32400 1.000 175.85260 ?  214 ASN C ND2 1 
ATOM   1478 N N   . HIS A 1 207 ? 44.71600  61.23700 -18.09600 1.000 170.20463 ?  215 HIS C N   1 
ATOM   1479 C CA  . HIS A 1 207 ? 44.14400  61.14400 -16.75700 1.000 169.23279 ?  215 HIS C CA  1 
ATOM   1480 C C   . HIS A 1 207 ? 42.63600  61.38500 -16.86600 1.000 170.27053 ?  215 HIS C C   1 
ATOM   1481 O O   . HIS A 1 207 ? 42.13200  62.43500 -16.46500 1.000 170.48667 ?  215 HIS C O   1 
ATOM   1482 C CB  . HIS A 1 207 ? 44.80200  62.13200 -15.80800 1.000 167.95137 ?  215 HIS C CB  1 
ATOM   1483 C CG  . HIS A 1 207 ? 44.46400  61.90600 -14.36700 1.000 167.61209 ?  215 HIS C CG  1 
ATOM   1484 N ND1 . HIS A 1 207 ? 44.92200  62.73100 -13.36300 1.000 166.58780 ?  215 HIS C ND1 1 
ATOM   1485 C CD2 . HIS A 1 207 ? 43.71800  60.95400 -13.76000 1.000 168.64889 ?  215 HIS C CD2 1 
ATOM   1486 C CE1 . HIS A 1 207 ? 44.47100  62.29900 -12.19900 1.000 167.39606 ?  215 HIS C CE1 1 
ATOM   1487 N NE2 . HIS A 1 207 ? 43.73800  61.22100 -12.41200 1.000 168.85409 ?  215 HIS C NE2 1 
ATOM   1488 N N   . LYS A 1 208 ? 41.94700  60.46300 -17.52000 1.000 166.80050 ?  216 LYS C N   1 
ATOM   1489 C CA  . LYS A 1 208 ? 40.49900  60.52000 -17.68900 1.000 167.21190 ?  216 LYS C CA  1 
ATOM   1490 C C   . LYS A 1 208 ? 39.73500  60.72000 -16.37600 1.000 167.19649 ?  216 LYS C C   1 
ATOM   1491 O O   . LYS A 1 208 ? 38.67200  61.35600 -16.39300 1.000 167.84611 ?  216 LYS C O   1 
ATOM   1492 C CB  . LYS A 1 208 ? 40.01000  59.24800 -18.39000 1.000 167.16688 ?  216 LYS C CB  1 
ATOM   1493 N N   . PRO A 1 209 ? 40.19600  60.18200 -15.23400 1.000 161.89440 ?  217 PRO C N   1 
ATOM   1494 C CA  . PRO A 1 209 ? 39.54700  60.55900 -13.96300 1.000 163.26518 ?  217 PRO C CA  1 
ATOM   1495 C C   . PRO A 1 209 ? 39.55600  62.05200 -13.72400 1.000 163.57664 ?  217 PRO C C   1 
ATOM   1496 O O   . PRO A 1 209 ? 38.59700  62.59300 -13.16500 1.000 164.98413 ?  217 PRO C O   1 
ATOM   1497 C CB  . PRO A 1 209 ? 40.37100  59.81000 -12.91400 1.000 163.74086 ?  217 PRO C CB  1 
ATOM   1498 C CG  . PRO A 1 209 ? 40.82500  58.59300 -13.62600 1.000 162.87672 ?  217 PRO C CG  1 
ATOM   1499 C CD  . PRO A 1 209 ? 41.01900  58.96800 -15.07300 1.000 161.53207 ?  217 PRO C CD  1 
ATOM   1500 N N   . SER A 1 210 ? 40.62200  62.73600 -14.13300 1.000 165.47497 ?  218 SER C N   1 
ATOM   1501 C CA  . SER A 1 210 ? 40.68700  64.18700 -14.08700 1.000 165.39379 ?  218 SER C CA  1 
ATOM   1502 C C   . SER A 1 210 ? 40.53600  64.81100 -15.46700 1.000 165.07062 ?  218 SER C C   1 
ATOM   1503 O O   . SER A 1 210 ? 40.61500  66.03700 -15.59200 1.000 165.32365 ?  218 SER C O   1 
ATOM   1504 C CB  . SER A 1 210 ? 41.99900  64.63400 -13.44200 1.000 164.10397 ?  218 SER C CB  1 
ATOM   1505 O OG  . SER A 1 210 ? 43.06000  64.50600 -14.36100 1.000 162.36640 ?  218 SER C OG  1 
ATOM   1506 N N   . ASN A 1 211 ? 40.33200  63.98700 -16.50200 1.000 170.27756 ?  219 ASN C N   1 
ATOM   1507 C CA  . ASN A 1 211 ? 40.10500  64.43700 -17.87900 1.000 171.18993 ?  219 ASN C CA  1 
ATOM   1508 C C   . ASN A 1 211 ? 41.26100  65.29200 -18.40500 1.000 171.75832 ?  219 ASN C C   1 
ATOM   1509 O O   . ASN A 1 211 ? 41.05300  66.29600 -19.08600 1.000 173.10382 ?  219 ASN C O   1 
ATOM   1510 C CB  . ASN A 1 211 ? 38.76400  65.16900 -17.98500 1.000 171.85879 ?  219 ASN C CB  1 
ATOM   1511 C CG  . ASN A 1 211 ? 38.21800  65.19600 -19.39900 1.000 172.75560 ?  219 ASN C CG  1 
ATOM   1512 O OD1 . ASN A 1 211 ? 38.95200  65.03300 -20.37300 1.000 173.68308 ?  219 ASN C OD1 1 
ATOM   1513 N ND2 . ASN A 1 211 ? 36.90300  65.35700 -19.51100 1.000 172.65596 ?  219 ASN C ND2 1 
ATOM   1514 N N   . THR A 1 212 ? 42.49100  64.90400 -18.06700 1.000 175.00134 ?  220 THR C N   1 
ATOM   1515 C CA  . THR A 1 212 ? 43.69100  65.60900 -18.50900 1.000 175.30871 ?  220 THR C CA  1 
ATOM   1516 C C   . THR A 1 212 ? 44.41900  64.81500 -19.58800 1.000 176.25602 ?  220 THR C C   1 
ATOM   1517 O O   . THR A 1 212 ? 44.46500  63.58800 -19.53600 1.000 175.52207 ?  220 THR C O   1 
ATOM   1518 C CB  . THR A 1 212 ? 44.64000  65.86700 -17.33300 1.000 173.17408 ?  220 THR C CB  1 
ATOM   1519 O OG1 . THR A 1 212 ? 43.88600  66.30700 -16.19700 1.000 172.67453 ?  220 THR C OG1 1 
ATOM   1520 C CG2 . THR A 1 212 ? 45.67700  66.91900 -17.68800 1.000 173.42940 ?  220 THR C CG2 1 
ATOM   1521 N N   . LYS A 1 213 ? 44.93600  65.50400 -20.60300 1.000 178.15286 ?  221 LYS C N   1 
ATOM   1522 C CA  . LYS A 1 213 ? 45.70500  64.83800 -21.65100 1.000 179.89645 ?  221 LYS C CA  1 
ATOM   1523 C C   . LYS A 1 213 ? 46.91900  65.70100 -21.96000 1.000 180.66714 ?  221 LYS C C   1 
ATOM   1524 O O   . LYS A 1 213 ? 46.76800  66.84000 -22.41200 1.000 182.41127 ?  221 LYS C O   1 
ATOM   1525 C CB  . LYS A 1 213 ? 44.86500  64.59200 -22.90700 1.000 182.87640 ?  221 LYS C CB  1 
ATOM   1526 C CG  . LYS A 1 213 ? 45.25900  63.32400 -23.65800 1.000 184.08018 ?  221 LYS C CG  1 
ATOM   1527 N N   . VAL A 1 214 ? 48.11600  65.16300 -21.74500 1.000 182.73022 ?  222 VAL C N   1 
ATOM   1528 C CA  . VAL A 1 214 ? 49.35300  65.92700 -21.87400 1.000 182.52492 ?  222 VAL C CA  1 
ATOM   1529 C C   . VAL A 1 214 ? 50.31100  65.17100 -22.77900 1.000 184.74369 ?  222 VAL C C   1 
ATOM   1530 O O   . VAL A 1 214 ? 50.77600  64.08700 -22.42500 1.000 183.54622 ?  222 VAL C O   1 
ATOM   1531 C CB  . VAL A 1 214 ? 50.01600  66.16900 -20.51000 1.000 178.20473 ?  222 VAL C CB  1 
ATOM   1532 C CG1 . VAL A 1 214 ? 51.36400  66.84500 -20.69900 1.000 177.50961 ?  222 VAL C CG1 1 
ATOM   1533 C CG2 . VAL A 1 214 ? 49.11100  66.98000 -19.60300 1.000 176.60514 ?  222 VAL C CG2 1 
ATOM   1534 N N   . ASP A 1 215 ? 50.66000  65.76500 -23.90600 1.000 181.44503 ?  223 ASP C N   1 
ATOM   1535 C CA  . ASP A 1 215 ? 51.60500  65.15500 -24.83100 1.000 184.42560 ?  223 ASP C CA  1 
ATOM   1536 C C   . ASP A 1 215 ? 52.84300  66.04300 -24.76500 1.000 183.92659 ?  223 ASP C C   1 
ATOM   1537 O O   . ASP A 1 215 ? 52.99300  66.98400 -25.54500 1.000 186.82379 ?  223 ASP C O   1 
ATOM   1538 C CB  . ASP A 1 215 ? 51.02600  65.07400 -26.23900 1.000 189.69541 ?  223 ASP C CB  1 
ATOM   1539 C CG  . ASP A 1 215 ? 49.71800  64.31400 -26.28600 1.000 189.87387 ?  223 ASP C CG  1 
ATOM   1540 O OD1 . ASP A 1 215 ? 49.01300  64.26600 -25.25700 1.000 186.31488 ?  223 ASP C OD1 1 
ATOM   1541 O OD2 . ASP A 1 215 ? 49.39000  63.76700 -27.35600 1.000 193.60129 -1 223 ASP C OD2 1 
ATOM   1542 N N   . LYS A 1 216 ? 53.73700  65.72700 -23.82900 1.000 190.46466 ?  224 LYS C N   1 
ATOM   1543 C CA  . LYS A 1 216 ? 54.90300  66.55900 -23.56000 1.000 189.30175 ?  224 LYS C CA  1 
ATOM   1544 C C   . LYS A 1 216 ? 56.13100  66.01300 -24.26800 1.000 192.76966 ?  224 LYS C C   1 
ATOM   1545 O O   . LYS A 1 216 ? 56.38800  64.80800 -24.24300 1.000 193.38283 ?  224 LYS C O   1 
ATOM   1546 C CB  . LYS A 1 216 ? 55.18300  66.65400 -22.05800 1.000 183.75457 ?  224 LYS C CB  1 
ATOM   1547 C CG  . LYS A 1 216 ? 56.67500  66.80400 -21.73200 1.000 183.09684 ?  224 LYS C CG  1 
ATOM   1548 C CD  . LYS A 1 216 ? 56.93100  67.51900 -20.42100 1.000 178.59056 ?  224 LYS C CD  1 
ATOM   1549 N N   . LYS A 1 217 ? 56.91900  66.91100 -24.85300 1.000 191.10147 ?  225 LYS C N   1 
ATOM   1550 C CA  . LYS A 1 217 ? 58.13400  66.51100 -25.54200 1.000 195.31049 ?  225 LYS C CA  1 
ATOM   1551 C C   . LYS A 1 217 ? 59.29300  66.52200 -24.56000 1.000 192.58953 ?  225 LYS C C   1 
ATOM   1552 O O   . LYS A 1 217 ? 59.45600  67.47400 -23.79000 1.000 190.39324 ?  225 LYS C O   1 
ATOM   1553 C CB  . LYS A 1 217 ? 58.44000  67.42700 -26.72700 1.000 200.75352 ?  225 LYS C CB  1 
ATOM   1554 N N   . VAL A 1 218 ? 60.08400  65.45600 -24.58000 1.000 204.72010 ?  226 VAL C N   1 
ATOM   1555 C CA  . VAL A 1 218 ? 61.25800  65.33600 -23.73100 1.000 203.15107 ?  226 VAL C CA  1 
ATOM   1556 C C   . VAL A 1 218 ? 62.49000  65.54200 -24.60200 1.000 208.07925 ?  226 VAL C C   1 
ATOM   1557 O O   . VAL A 1 218 ? 62.75400  64.75200 -25.51800 1.000 211.99152 ?  226 VAL C O   1 
ATOM   1558 C CB  . VAL A 1 218 ? 61.29900  63.97600 -23.02000 1.000 201.61243 ?  226 VAL C CB  1 
ATOM   1559 C CG1 . VAL A 1 218 ? 62.37900  63.96600 -21.97600 1.000 200.33369 ?  226 VAL C CG1 1 
ATOM   1560 C CG2 . VAL A 1 218 ? 59.94800  63.67500 -22.38900 1.000 197.65056 ?  226 VAL C CG2 1 
ATOM   1561 N N   . GLU A 1 219 ? 63.23600  66.60500 -24.32200 1.000 201.00828 ?  227 GLU C N   1 
ATOM   1562 C CA  . GLU A 1 219 ? 64.44700  66.92800 -25.05400 1.000 205.57590 ?  227 GLU C CA  1 
ATOM   1563 C C   . GLU A 1 219 ? 65.46800  67.48300 -24.07400 1.000 203.73804 ?  227 GLU C C   1 
ATOM   1564 O O   . GLU A 1 219 ? 65.09300  68.06500 -23.04800 1.000 199.61636 ?  227 GLU C O   1 
ATOM   1565 C CB  . GLU A 1 219 ? 64.17500  67.93700 -26.18400 1.000 209.56511 ?  227 GLU C CB  1 
ATOM   1566 C CG  . GLU A 1 219 ? 64.22000  69.39300 -25.76900 1.000 207.87461 ?  227 GLU C CG  1 
ATOM   1567 C CD  . GLU A 1 219 ? 63.47200  70.28700 -26.73700 1.000 210.84056 ?  227 GLU C CD  1 
ATOM   1568 O OE1 . GLU A 1 219 ? 63.22900  69.85600 -27.88300 1.000 215.76648 ?  227 GLU C OE1 1 
ATOM   1569 O OE2 . GLU A 1 219 ? 63.12800  71.42200 -26.35000 1.000 208.49325 -1 227 GLU C OE2 1 
ATOM   1570 N N   . PRO A 1 220 ? 66.76700  67.30600 -24.35400 1.000 203.49192 ?  228 PRO C N   1 
ATOM   1571 C CA  . PRO A 1 220 ? 67.86000  67.73100 -23.47100 1.000 203.36185 ?  228 PRO C CA  1 
ATOM   1572 C C   . PRO A 1 220 ? 67.83300  69.22000 -23.12400 1.000 202.66107 ?  228 PRO C C   1 
ATOM   1573 O O   . PRO A 1 220 ? 67.56600  70.04900 -23.99400 1.000 204.63465 ?  228 PRO C O   1 
ATOM   1574 C CB  . PRO A 1 220 ? 69.10700  67.38500 -24.27800 1.000 208.56036 ?  228 PRO C CB  1 
ATOM   1575 C CG  . PRO A 1 220 ? 68.70000  66.20000 -25.09000 1.000 209.58247 ?  228 PRO C CG  1 
ATOM   1576 C CD  . PRO A 1 220 ? 67.22000  66.32600 -25.35700 1.000 207.75442 ?  228 PRO C CD  1 
ATOM   1577 N N   . THR B 2 5   ? 42.84300  26.90000 -0.91400  1.000 191.14116 ?  5   THR D N   1 
ATOM   1578 C CA  . THR B 2 5   ? 44.21600  27.39100 -0.84900  1.000 192.92499 ?  5   THR D CA  1 
ATOM   1579 C C   . THR B 2 5   ? 44.98100  27.01100 -2.11500  1.000 193.68806 ?  5   THR D C   1 
ATOM   1580 O O   . THR B 2 5   ? 44.57500  26.10100 -2.84100  1.000 193.38057 ?  5   THR D O   1 
ATOM   1581 C CB  . THR B 2 5   ? 44.96000  26.83400 0.37700   1.000 194.57657 ?  5   THR D CB  1 
ATOM   1582 O OG1 . THR B 2 5   ? 45.46800  25.53000 0.07500   1.000 196.03796 ?  5   THR D OG1 1 
ATOM   1583 C CG2 . THR B 2 5   ? 44.02400  26.73200 1.57300   1.000 195.12131 ?  5   THR D CG2 1 
ATOM   1584 N N   . GLN B 2 6   ? 46.07800  27.71900 -2.37900  1.000 192.91576 ?  6   GLN D N   1 
ATOM   1585 C CA  . GLN B 2 6   ? 46.98300  27.41800 -3.47800  1.000 199.24572 ?  6   GLN D CA  1 
ATOM   1586 C C   . GLN B 2 6   ? 48.38900  27.14000 -2.95800  1.000 206.49129 ?  6   GLN D C   1 
ATOM   1587 O O   . GLN B 2 6   ? 48.77200  27.57000 -1.86700  1.000 205.90241 ?  6   GLN D O   1 
ATOM   1588 C CB  . GLN B 2 6   ? 47.03000  28.56400 -4.49700  1.000 198.61463 ?  6   GLN D CB  1 
ATOM   1589 N N   . SER B 2 7   ? 49.15700  26.40100 -3.75900  1.000 195.28717 ?  7   SER D N   1 
ATOM   1590 C CA  . SER B 2 7   ? 50.54400  26.05800 -3.46300  1.000 202.92110 ?  7   SER D CA  1 
ATOM   1591 C C   . SER B 2 7   ? 51.25600  25.71600 -4.76800  1.000 208.03550 ?  7   SER D C   1 
ATOM   1592 O O   . SER B 2 7   ? 50.71800  24.94900 -5.57500  1.000 205.87598 ?  7   SER D O   1 
ATOM   1593 C CB  . SER B 2 7   ? 50.61500  24.89700 -2.47100  1.000 204.32332 ?  7   SER D CB  1 
ATOM   1594 O OG  . SER B 2 7   ? 49.84500  23.79500 -2.91800  1.000 202.14918 ?  7   SER D OG  1 
ATOM   1595 N N   . PRO B 2 8   ? 52.47200  26.23300 -5.01600  1.000 205.20737 ?  8   PRO D N   1 
ATOM   1596 C CA  . PRO B 2 8   ? 53.36800  26.97900 -4.11900  1.000 207.83767 ?  8   PRO D CA  1 
ATOM   1597 C C   . PRO B 2 8   ? 53.04100  28.45600 -3.96900  1.000 202.49293 ?  8   PRO D C   1 
ATOM   1598 O O   . PRO B 2 8   ? 52.33400  29.03700 -4.78800  1.000 199.34354 ?  8   PRO D O   1 
ATOM   1599 C CB  . PRO B 2 8   ? 54.72900  26.79300 -4.79500  1.000 215.89854 ?  8   PRO D CB  1 
ATOM   1600 C CG  . PRO B 2 8   ? 54.39100  26.80800 -6.26100  1.000 213.27314 ?  8   PRO D CG  1 
ATOM   1601 C CD  . PRO B 2 8   ? 53.05500  26.10000 -6.36400  1.000 207.62144 ?  8   PRO D CD  1 
ATOM   1602 N N   . SER B 2 9   ? 53.54200  29.09200 -2.90900  1.000 213.83563 ?  9   SER D N   1 
ATOM   1603 C CA  . SER B 2 9   ? 53.37200  30.53400 -2.77700  1.000 208.50947 ?  9   SER D CA  1 
ATOM   1604 C C   . SER B 2 9   ? 54.13300  31.26700 -3.87100  1.000 212.65900 ?  9   SER D C   1 
ATOM   1605 O O   . SER B 2 9   ? 53.62500  32.23000 -4.45700  1.000 209.95943 ?  9   SER D O   1 
ATOM   1606 C CB  . SER B 2 9   ? 53.84800  30.99000 -1.40000  1.000 204.11926 ?  9   SER D CB  1 
ATOM   1607 O OG  . SER B 2 9   ? 55.26200  30.92100 -1.31300  1.000 208.89328 ?  9   SER D OG  1 
ATOM   1608 N N   . SER B 2 10  ? 55.34900  30.81600 -4.15700  1.000 209.52684 ?  10  SER D N   1 
ATOM   1609 C CA  . SER B 2 10  ? 56.19100  31.38100 -5.19800  1.000 213.63648 ?  10  SER D CA  1 
ATOM   1610 C C   . SER B 2 10  ? 57.25600  30.34900 -5.51600  1.000 219.44557 ?  10  SER D C   1 
ATOM   1611 O O   . SER B 2 10  ? 57.63500  29.54600 -4.65900  1.000 220.00283 ?  10  SER D O   1 
ATOM   1612 C CB  . SER B 2 10  ? 56.83500  32.70700 -4.77800  1.000 212.47767 ?  10  SER D CB  1 
ATOM   1613 O OG  . SER B 2 10  ? 57.51200  32.58200 -3.54100  1.000 216.19821 ?  10  SER D OG  1 
ATOM   1614 N N   . LEU B 2 11  ? 57.74100  30.37700 -6.74900  1.000 213.23995 ?  11  LEU D N   1 
ATOM   1615 C CA  . LEU B 2 11  ? 58.69700  29.37500 -7.18400  1.000 216.18319 ?  11  LEU D CA  1 
ATOM   1616 C C   . LEU B 2 11  ? 59.55100  29.98100 -8.27800  1.000 218.60258 ?  11  LEU D C   1 
ATOM   1617 O O   . LEU B 2 11  ? 59.05900  30.75900 -9.09800  1.000 217.87935 ?  11  LEU D O   1 
ATOM   1618 C CB  . LEU B 2 11  ? 57.99700  28.10900 -7.69200  1.000 214.64787 ?  11  LEU D CB  1 
ATOM   1619 N N   . SER B 2 12  ? 60.82600  29.60700 -8.29800  1.000 219.22010 ?  12  SER D N   1 
ATOM   1620 C CA  . SER B 2 12  ? 61.73900  30.05100 -9.34300  1.000 223.79641 ?  12  SER D CA  1 
ATOM   1621 C C   . SER B 2 12  ? 62.41500  28.82000 -9.92000  1.000 223.80252 ?  12  SER D C   1 
ATOM   1622 O O   . SER B 2 12  ? 63.29900  28.22800 -9.28900  1.000 226.86084 ?  12  SER D O   1 
ATOM   1623 C CB  . SER B 2 12  ? 62.77100  31.04500 -8.80300  1.000 231.79866 ?  12  SER D CB  1 
ATOM   1624 O OG  . SER B 2 12  ? 63.54200  30.47000 -7.76500  1.000 234.44095 ?  12  SER D OG  1 
ATOM   1625 N N   . ALA B 2 13  ? 61.98700  28.44700 -11.11500 1.000 221.82072 ?  13  ALA D N   1 
ATOM   1626 C CA  . ALA B 2 13  ? 62.63600  27.47700 -11.97100 1.000 222.53622 ?  13  ALA D CA  1 
ATOM   1627 C C   . ALA B 2 13  ? 63.17400  28.22200 -13.18600 1.000 226.42989 ?  13  ALA D C   1 
ATOM   1628 O O   . ALA B 2 13  ? 63.16000  29.45700 -13.23700 1.000 229.57605 ?  13  ALA D O   1 
ATOM   1629 C CB  . ALA B 2 13  ? 61.66400  26.35900 -12.35200 1.000 218.56597 ?  13  ALA D CB  1 
ATOM   1630 N N   . SER B 2 14  ? 63.65200  27.47800 -14.16900 1.000 227.49122 ?  14  SER D N   1 
ATOM   1631 C CA  . SER B 2 14  ? 64.16500  28.06100 -15.39900 1.000 232.40247 ?  14  SER D CA  1 
ATOM   1632 C C   . SER B 2 14  ? 63.35400  27.55900 -16.58700 1.000 227.58942 ?  14  SER D C   1 
ATOM   1633 O O   . SER B 2 14  ? 62.35200  26.85600 -16.43600 1.000 220.51050 ?  14  SER D O   1 
ATOM   1634 C CB  . SER B 2 14  ? 65.65100  27.74900 -15.56600 1.000 240.05986 ?  14  SER D CB  1 
ATOM   1635 O OG  . SER B 2 14  ? 66.29200  27.74900 -14.30200 1.000 242.90308 ?  14  SER D OG  1 
ATOM   1636 N N   . VAL B 2 15  ? 63.78400  27.95700 -17.78200 1.000 231.96030 ?  15  VAL D N   1 
ATOM   1637 C CA  . VAL B 2 15  ? 63.07000  27.58800 -18.99500 1.000 228.35782 ?  15  VAL D CA  1 
ATOM   1638 C C   . VAL B 2 15  ? 63.15100  26.08200 -19.18700 1.000 225.43844 ?  15  VAL D C   1 
ATOM   1639 O O   . VAL B 2 15  ? 64.22600  25.47700 -19.07400 1.000 229.84761 ?  15  VAL D O   1 
ATOM   1640 C CB  . VAL B 2 15  ? 63.64600  28.33000 -20.20600 1.000 234.85401 ?  15  VAL D CB  1 
ATOM   1641 C CG1 . VAL B 2 15  ? 62.67900  28.26200 -21.37400 1.000 230.85060 ?  15  VAL D CG1 1 
ATOM   1642 C CG2 . VAL B 2 15  ? 63.93900  29.76700 -19.83800 1.000 239.93168 ?  15  VAL D CG2 1 
ATOM   1643 N N   . GLY B 2 16  ? 62.00900  25.46500 -19.46700 1.000 218.32478 ?  16  GLY D N   1 
ATOM   1644 C CA  . GLY B 2 16  ? 61.93500  24.04100 -19.64200 1.000 215.21442 ?  16  GLY D CA  1 
ATOM   1645 C C   . GLY B 2 16  ? 61.63700  23.27400 -18.37200 1.000 211.72921 ?  16  GLY D C   1 
ATOM   1646 O O   . GLY B 2 16  ? 61.05000  22.18900 -18.44000 1.000 208.95682 ?  16  GLY D O   1 
ATOM   1647 N N   . ASP B 2 17  ? 62.02800  23.80900 -17.21700 1.000 215.34050 ?  17  ASP D N   1 
ATOM   1648 C CA  . ASP B 2 17  ? 61.77500  23.12600 -15.95700 1.000 214.42860 ?  17  ASP D CA  1 
ATOM   1649 C C   . ASP B 2 17  ? 60.27900  22.92600 -15.79200 1.000 210.33334 ?  17  ASP D C   1 
ATOM   1650 O O   . ASP B 2 17  ? 59.51000  23.89300 -15.80900 1.000 209.20886 ?  17  ASP D O   1 
ATOM   1651 C CB  . ASP B 2 17  ? 62.31900  23.93700 -14.78800 1.000 217.30758 ?  17  ASP D CB  1 
ATOM   1652 C CG  . ASP B 2 17  ? 63.80700  24.16000 -14.86800 1.000 221.99229 ?  17  ASP D CG  1 
ATOM   1653 O OD1 . ASP B 2 17  ? 64.37100  24.07900 -15.97900 1.000 224.82562 ?  17  ASP D OD1 1 
ATOM   1654 O OD2 . ASP B 2 17  ? 64.40600  24.41600 -13.80400 1.000 224.57427 ?  17  ASP D OD2 1 
ATOM   1655 N N   . ARG B 2 18  ? 59.86300  21.67300 -15.64600 1.000 212.47734 ?  18  ARG D N   1 
ATOM   1656 C CA  . ARG B 2 18  ? 58.45900  21.40100 -15.38700 1.000 208.42255 ?  18  ARG D CA  1 
ATOM   1657 C C   . ARG B 2 18  ? 58.07800  22.00200 -14.04000 1.000 208.94298 ?  18  ARG D C   1 
ATOM   1658 O O   . ARG B 2 18  ? 58.79900  21.84700 -13.05100 1.000 212.25355 ?  18  ARG D O   1 
ATOM   1659 C CB  . ARG B 2 18  ? 58.21100  19.89000 -15.42200 1.000 206.96146 ?  18  ARG D CB  1 
ATOM   1660 C CG  . ARG B 2 18  ? 56.78900  19.44800 -15.13000 1.000 204.18941 ?  18  ARG D CG  1 
ATOM   1661 C CD  . ARG B 2 18  ? 56.41200  18.27700 -16.03200 1.000 202.16539 ?  18  ARG D CD  1 
ATOM   1662 N NE  . ARG B 2 18  ? 55.29100  17.49800 -15.52000 1.000 200.33451 ?  18  ARG D NE  1 
ATOM   1663 C CZ  . ARG B 2 18  ? 54.36600  16.93200 -16.28400 1.000 197.90560 ?  18  ARG D CZ  1 
ATOM   1664 N NH1 . ARG B 2 18  ? 54.38100  17.06000 -17.60200 1.000 196.94915 ?  18  ARG D NH1 1 
ATOM   1665 N NH2 . ARG B 2 18  ? 53.39900  16.22400 -15.71100 1.000 196.55510 ?  18  ARG D NH2 1 
ATOM   1666 N N   . VAL B 2 19  ? 56.93800  22.68100 -14.00300 1.000 203.05104 ?  19  VAL D N   1 
ATOM   1667 C CA  . VAL B 2 19  ? 56.51300  23.42900 -12.82800 1.000 203.13899 ?  19  VAL D CA  1 
ATOM   1668 C C   . VAL B 2 19  ? 55.03600  23.14900 -12.59500 1.000 195.94761 ?  19  VAL D C   1 
ATOM   1669 O O   . VAL B 2 19  ? 54.23200  23.20800 -13.53000 1.000 191.52752 ?  19  VAL D O   1 
ATOM   1670 C CB  . VAL B 2 19  ? 56.77900  24.93600 -13.01300 1.000 207.27636 ?  19  VAL D CB  1 
ATOM   1671 C CG1 . VAL B 2 19  ? 58.25400  25.23400 -12.84000 1.000 215.51551 ?  19  VAL D CG1 1 
ATOM   1672 C CG2 . VAL B 2 19  ? 56.35200  25.36700 -14.39500 1.000 204.96605 ?  19  VAL D CG2 1 
ATOM   1673 N N   . THR B 2 20  ? 54.66400  22.87900 -11.34700 1.000 198.78292 ?  20  THR D N   1 
ATOM   1674 C CA  . THR B 2 20  ? 53.29300  22.47500 -11.05900 1.000 192.80521 ?  20  THR D CA  1 
ATOM   1675 C C   . THR B 2 20  ? 52.78200  23.19900 -9.82400  1.000 193.90473 ?  20  THR D C   1 
ATOM   1676 O O   . THR B 2 20  ? 53.38900  23.12700 -8.75200  1.000 197.73925 ?  20  THR D O   1 
ATOM   1677 C CB  . THR B 2 20  ? 53.19200  20.95500 -10.88000 1.000 190.23155 ?  20  THR D CB  1 
ATOM   1678 O OG1 . THR B 2 20  ? 53.31800  20.31600 -12.15800 1.000 188.20258 ?  20  THR D OG1 1 
ATOM   1679 C CG2 . THR B 2 20  ? 51.85100  20.57400 -10.25800 1.000 185.63678 ?  20  THR D CG2 1 
ATOM   1680 N N   . ILE B 2 21  ? 51.66600  23.88700 -9.99100  1.000 194.32122 ?  21  ILE D N   1 
ATOM   1681 C CA  . ILE B 2 21  ? 50.93200  24.54300 -8.92200  1.000 194.93049 ?  21  ILE D CA  1 
ATOM   1682 C C   . ILE B 2 21  ? 49.83900  23.59800 -8.45300  1.000 190.70886 ?  21  ILE D C   1 
ATOM   1683 O O   . ILE B 2 21  ? 49.29700  22.81900 -9.23900  1.000 186.08989 ?  21  ILE D O   1 
ATOM   1684 C CB  . ILE B 2 21  ? 50.34900  25.87500 -9.43300  1.000 194.39519 ?  21  ILE D CB  1 
ATOM   1685 C CG1 . ILE B 2 21  ? 51.38400  26.57600 -10.32100 1.000 197.71462 ?  21  ILE D CG1 1 
ATOM   1686 C CG2 . ILE B 2 21  ? 49.90900  26.73600 -8.27300  1.000 197.13199 ?  21  ILE D CG2 1 
ATOM   1687 C CD1 . ILE B 2 21  ? 50.94300  27.90600 -10.84800 1.000 197.64062 ?  21  ILE D CD1 1 
ATOM   1688 N N   . THR B 2 22  ? 49.51400  23.65300 -7.16200  1.000 194.82622 ?  22  THR D N   1 
ATOM   1689 C CA  . THR B 2 22  ? 48.47100  22.81100 -6.59300  1.000 191.98548 ?  22  THR D CA  1 
ATOM   1690 C C   . THR B 2 22  ? 47.47400  23.66700 -5.82200  1.000 192.86532 ?  22  THR D C   1 
ATOM   1691 O O   . THR B 2 22  ? 47.84900  24.64000 -5.16100  1.000 197.01469 ?  22  THR D O   1 
ATOM   1692 C CB  . THR B 2 22  ? 49.06700  21.71800 -5.68500  1.000 193.93778 ?  22  THR D CB  1 
ATOM   1693 O OG1 . THR B 2 22  ? 50.06900  20.99400 -6.41000  1.000 193.86514 ?  22  THR D OG1 1 
ATOM   1694 C CG2 . THR B 2 22  ? 47.98600  20.73700 -5.24100  1.000 191.10450 ?  22  THR D CG2 1 
ATOM   1695 N N   . CYS B 2 23  ? 46.20300  23.29600 -5.92600  1.000 192.10688 ?  23  CYS D N   1 
ATOM   1696 C CA  . CYS B 2 23  ? 45.06900  23.99800 -5.35300  1.000 192.81240 ?  23  CYS D CA  1 
ATOM   1697 C C   . CYS B 2 23  ? 44.27900  23.02600 -4.48800  1.000 192.68754 ?  23  CYS D C   1 
ATOM   1698 O O   . CYS B 2 23  ? 44.02300  21.88500 -4.89600  1.000 189.34570 ?  23  CYS D O   1 
ATOM   1699 C CB  . CYS B 2 23  ? 44.17900  24.55300 -6.46600  1.000 188.71094 ?  23  CYS D CB  1 
ATOM   1700 S SG  . CYS B 2 23  ? 43.08700  25.90000 -6.02500  1.000 190.59496 ?  23  CYS D SG  1 
ATOM   1701 N N   . ARG B 2 24  ? 43.91000  23.51100 -3.30400  1.000 191.05354 ?  24  ARG D N   1 
ATOM   1702 C CA  . ARG B 2 24  ? 43.13800  22.66800 -2.36500  1.000 191.95317 ?  24  ARG D CA  1 
ATOM   1703 C C   . ARG B 2 24  ? 41.64900  22.94700 -2.53900  1.000 190.89794 ?  24  ARG D C   1 
ATOM   1704 O O   . ARG B 2 24  ? 41.30300  24.06600 -2.95500  1.000 191.21293 ?  24  ARG D O   1 
ATOM   1705 C CB  . ARG B 2 24  ? 43.54400  22.97000 -0.92200  1.000 196.72434 ?  24  ARG D CB  1 
ATOM   1706 C CG  . ARG B 2 24  ? 43.46200  21.76700 0.00500   1.000 197.97927 ?  24  ARG D CG  1 
ATOM   1707 C CD  . ARG B 2 24  ? 42.27300  21.85800 0.94000   1.000 198.82497 ?  24  ARG D CD  1 
ATOM   1708 N NE  . ARG B 2 24  ? 42.53900  22.75500 2.05300   1.000 202.47236 ?  24  ARG D NE  1 
ATOM   1709 C CZ  . ARG B 2 24  ? 43.51100  22.57800 2.93900   1.000 205.12907 ?  24  ARG D CZ  1 
ATOM   1710 N NH1 . ARG B 2 24  ? 43.53500  21.48700 3.68400   1.000 205.91672 ?  24  ARG D NH1 1 
ATOM   1711 N NH2 . ARG B 2 24  ? 44.45800  23.48900 3.07400   1.000 207.25793 ?  24  ARG D NH2 1 
ATOM   1712 N N   . ALA B 2 25  ? 40.81700  21.96400 -2.22800  1.000 198.08276 ?  25  ALA D N   1 
ATOM   1713 C CA  . ALA B 2 25  ? 39.35700  22.09400 -2.29900  1.000 197.71203 ?  25  ALA D CA  1 
ATOM   1714 C C   . ALA B 2 25  ? 38.71800  21.44100 -1.07400  1.000 201.37209 ?  25  ALA D C   1 
ATOM   1715 O O   . ALA B 2 25  ? 38.26200  20.29700 -1.14100  1.000 199.79804 ?  25  ALA D O   1 
ATOM   1716 C CB  . ALA B 2 25  ? 38.83100  21.49700 -3.58500  1.000 191.89036 ?  25  ALA D CB  1 
ATOM   1717 N N   . SER B 2 26  ? 38.69300  22.17100 0.03900   1.000 190.05614 ?  26  SER D N   1 
ATOM   1718 C CA  . SER B 2 26  ? 38.12400  21.68400 1.29700   1.000 207.36906 ?  26  SER D CA  1 
ATOM   1719 C C   . SER B 2 26  ? 36.73700  21.06400 1.12300   1.000 217.75996 ?  26  SER D C   1 
ATOM   1720 O O   . SER B 2 26  ? 36.50000  19.92800 1.53600   1.000 220.44417 ?  26  SER D O   1 
ATOM   1721 C CB  . SER B 2 26  ? 38.04600  22.82500 2.31200   1.000 219.50531 ?  26  SER D CB  1 
ATOM   1722 O OG  . SER B 2 26  ? 36.93500  23.66300 2.04300   1.000 226.64390 ?  26  SER D OG  1 
ATOM   1723 N N   . ALA B 2 28  ? 34.06000  18.76100 -1.63200  1.000 190.29842 ?  28  ALA D N   1 
ATOM   1724 C CA  . ALA B 2 28  ? 34.39900  19.65900 -2.76000  1.000 178.63099 ?  28  ALA D CA  1 
ATOM   1725 C C   . ALA B 2 28  ? 33.15300  19.89300 -3.62000  1.000 182.80711 ?  28  ALA D C   1 
ATOM   1726 O O   . ALA B 2 28  ? 32.10300  19.29600 -3.31700  1.000 194.67537 ?  28  ALA D O   1 
ATOM   1727 C CB  . ALA B 2 28  ? 35.52500  19.06600 -3.57000  1.000 156.98926 ?  28  ALA D CB  1 
ATOM   1728 N N   . ALA B 2 29  ? 33.27000  20.73400 -4.65100  1.000 177.73346 ?  29  ALA D N   1 
ATOM   1729 C CA  . ALA B 2 29  ? 32.13400  20.97600 -5.53400  1.000 179.93248 ?  29  ALA D CA  1 
ATOM   1730 C C   . ALA B 2 29  ? 32.32500  20.27700 -6.88200  1.000 159.95174 ?  29  ALA D C   1 
ATOM   1731 O O   . ALA B 2 29  ? 32.62500  20.89400 -7.90800  1.000 148.70056 ?  29  ALA D O   1 
ATOM   1732 C CB  . ALA B 2 29  ? 31.92300  22.47300 -5.71300  1.000 182.64456 ?  29  ALA D CB  1 
ATOM   1733 N N   . TYR B 2 30  ? 32.15800  18.95900 -6.84900  1.000 154.85374 ?  36  TYR D N   1 
ATOM   1734 C CA  . TYR B 2 30  ? 31.95900  18.10500 -8.03400  1.000 148.62584 ?  36  TYR D CA  1 
ATOM   1735 C C   . TYR B 2 30  ? 32.95400  18.39100 -9.16100  1.000 145.96943 ?  36  TYR D C   1 
ATOM   1736 O O   . TYR B 2 30  ? 32.61800  18.31700 -10.34400 1.000 144.25149 ?  36  TYR D O   1 
ATOM   1737 C CB  . TYR B 2 30  ? 30.53100  18.25300 -8.56100  1.000 157.71499 ?  36  TYR D CB  1 
ATOM   1738 C CG  . TYR B 2 30  ? 29.46900  17.76800 -7.59900  1.000 175.21668 ?  36  TYR D CG  1 
ATOM   1739 C CD1 . TYR B 2 30  ? 29.64100  16.58900 -6.88200  1.000 172.28443 ?  36  TYR D CD1 1 
ATOM   1740 C CD2 . TYR B 2 30  ? 28.29900  18.48800 -7.40900  1.000 193.04611 ?  36  TYR D CD2 1 
ATOM   1741 C CE1 . TYR B 2 30  ? 28.67400  16.14300 -6.00200  1.000 185.32432 ?  36  TYR D CE1 1 
ATOM   1742 C CE2 . TYR B 2 30  ? 27.32500  18.04800 -6.53000  1.000 205.95328 ?  36  TYR D CE2 1 
ATOM   1743 C CZ  . TYR B 2 30  ? 27.51800  16.87600 -5.83000  1.000 201.48741 ?  36  TYR D CZ  1 
ATOM   1744 O OH  . TYR B 2 30  ? 26.55200  16.43200 -4.95600  1.000 207.28108 ?  36  TYR D OH  1 
ATOM   1745 N N   . GLY B 2 31  ? 34.18800  18.71900 -8.78300  1.000 157.49854 ?  37  GLY D N   1 
ATOM   1746 C CA  . GLY B 2 31  ? 35.26600  18.90600 -9.74200  1.000 154.35709 ?  37  GLY D CA  1 
ATOM   1747 C C   . GLY B 2 31  ? 35.00400  19.96600 -10.78800 1.000 151.60320 ?  37  GLY D C   1 
ATOM   1748 O O   . GLY B 2 31  ? 35.38000  19.78400 -11.95300 1.000 148.46657 ?  37  GLY D O   1 
ATOM   1749 N N   . ARG B 2 32  ? 34.31200  21.04500 -10.42100 1.000 158.99405 ?  38  ARG D N   1 
ATOM   1750 C CA  . ARG B 2 32  ? 34.12000  22.21100 -11.29000 1.000 157.00706 ?  38  ARG D CA  1 
ATOM   1751 C C   . ARG B 2 32  ? 35.15100  23.27800 -10.91600 1.000 159.57582 ?  38  ARG D C   1 
ATOM   1752 O O   . ARG B 2 32  ? 34.92600  24.09700 -10.02400 1.000 163.29103 ?  38  ARG D O   1 
ATOM   1753 C CB  . ARG B 2 32  ? 32.69200  22.73700 -11.18200 1.000 157.51718 ?  38  ARG D CB  1 
ATOM   1754 N N   . VAL B 2 33  ? 36.29700  23.27200 -11.60300 1.000 162.96987 ?  39  VAL D N   1 
ATOM   1755 C CA  . VAL B 2 33  ? 37.42900  24.11700 -11.24000 1.000 165.89356 ?  39  VAL D CA  1 
ATOM   1756 C C   . VAL B 2 33  ? 37.94600  24.80300 -12.50000 1.000 163.62053 ?  39  VAL D C   1 
ATOM   1757 O O   . VAL B 2 33  ? 37.72700  24.34000 -13.62200 1.000 160.08625 ?  39  VAL D O   1 
ATOM   1758 C CB  . VAL B 2 33  ? 38.55700  23.32100 -10.54300 1.000 168.35071 ?  39  VAL D CB  1 
ATOM   1759 C CG1 . VAL B 2 33  ? 39.60500  24.25200 -9.94300  1.000 172.52672 ?  39  VAL D CG1 1 
ATOM   1760 C CG2 . VAL B 2 33  ? 37.98400  22.41200 -9.47700  1.000 170.25588 ?  39  VAL D CG2 1 
ATOM   1761 N N   . ALA B 2 34  ? 38.62600  25.93300 -12.30600 1.000 161.71394 ?  40  ALA D N   1 
ATOM   1762 C CA  . ALA B 2 34  ? 39.24900  26.64600 -13.41100 1.000 160.72599 ?  40  ALA D CA  1 
ATOM   1763 C C   . ALA B 2 34  ? 40.63500  27.12800 -13.00200 1.000 164.69536 ?  40  ALA D C   1 
ATOM   1764 O O   . ALA B 2 34  ? 40.96600  27.19700 -11.82000 1.000 168.38635 ?  40  ALA D O   1 
ATOM   1765 C CB  . ALA B 2 34  ? 38.39400  27.83900 -13.85900 1.000 159.79122 ?  40  ALA D CB  1 
ATOM   1766 N N   . TRP B 2 35  ? 41.44600  27.44700 -14.00700 1.000 161.42160 ?  41  TRP D N   1 
ATOM   1767 C CA  . TRP B 2 35  ? 42.76900  28.02700 -13.83200 1.000 165.60138 ?  41  TRP D CA  1 
ATOM   1768 C C   . TRP B 2 35  ? 42.87700  29.27000 -14.69900 1.000 166.01578 ?  41  TRP D C   1 
ATOM   1769 O O   . TRP B 2 35  ? 42.54500  29.22700 -15.89000 1.000 163.12680 ?  41  TRP D O   1 
ATOM   1770 C CB  . TRP B 2 35  ? 43.86600  27.02800 -14.20500 1.000 166.29349 ?  41  TRP D CB  1 
ATOM   1771 C CG  . TRP B 2 35  ? 44.09100  26.01500 -13.14000 1.000 167.53474 ?  41  TRP D CG  1 
ATOM   1772 C CD1 . TRP B 2 35  ? 43.66500  24.71900 -13.14500 1.000 164.76287 ?  41  TRP D CD1 1 
ATOM   1773 C CD2 . TRP B 2 35  ? 44.76200  26.21200 -11.89100 1.000 172.30399 ?  41  TRP D CD2 1 
ATOM   1774 N NE1 . TRP B 2 35  ? 44.04200  24.09400 -11.98400 1.000 167.37903 ?  41  TRP D NE1 1 
ATOM   1775 C CE2 . TRP B 2 35  ? 44.71600  24.98800 -11.19700 1.000 172.07942 ?  41  TRP D CE2 1 
ATOM   1776 C CE3 . TRP B 2 35  ? 45.40500  27.30000 -11.29400 1.000 177.10065 ?  41  TRP D CE3 1 
ATOM   1777 C CZ2 . TRP B 2 35  ? 45.28700  24.82200 -9.94000  1.000 176.43339 ?  41  TRP D CZ2 1 
ATOM   1778 C CZ3 . TRP B 2 35  ? 45.97100  27.13200 -10.04700 1.000 181.56675 ?  41  TRP D CZ3 1 
ATOM   1779 C CH2 . TRP B 2 35  ? 45.91000  25.90200 -9.38400  1.000 181.16000 ?  41  TRP D CH2 1 
ATOM   1780 N N   . TYR B 2 36  ? 43.40500  30.34400 -14.10400 1.000 160.28008 ?  42  TYR D N   1 
ATOM   1781 C CA  . TYR B 2 36  ? 43.54100  31.65400 -14.72300 1.000 163.10173 ?  42  TYR D CA  1 
ATOM   1782 C C   . TYR B 2 36  ? 44.97000  32.15500 -14.60000 1.000 167.40849 ?  42  TYR D C   1 
ATOM   1783 O O   . TYR B 2 36  ? 45.68300  31.82100 -13.64800 1.000 168.62592 ?  42  TYR D O   1 
ATOM   1784 C CB  . TYR B 2 36  ? 42.64600  32.70900 -14.06900 1.000 163.98998 ?  42  TYR D CB  1 
ATOM   1785 C CG  . TYR B 2 36  ? 41.17400  32.49000 -14.25000 1.000 160.77157 ?  42  TYR D CG  1 
ATOM   1786 C CD1 . TYR B 2 36  ? 40.51800  31.48500 -13.55300 1.000 157.97204 ?  42  TYR D CD1 1 
ATOM   1787 C CD2 . TYR B 2 36  ? 40.43800  33.27800 -15.11700 1.000 160.96884 ?  42  TYR D CD2 1 
ATOM   1788 C CE1 . TYR B 2 36  ? 39.17000  31.27800 -13.70600 1.000 155.61467 ?  42  TYR D CE1 1 
ATOM   1789 C CE2 . TYR B 2 36  ? 39.08800  33.07500 -15.27900 1.000 158.42440 ?  42  TYR D CE2 1 
ATOM   1790 C CZ  . TYR B 2 36  ? 38.46100  32.07600 -14.57300 1.000 155.82701 ?  42  TYR D CZ  1 
ATOM   1791 O OH  . TYR B 2 36  ? 37.11500  31.88000 -14.74000 1.000 153.87273 ?  42  TYR D OH  1 
ATOM   1792 N N   . GLN B 2 37  ? 45.33600  33.02700 -15.54000 1.000 170.18507 ?  43  GLN D N   1 
ATOM   1793 C CA  . GLN B 2 37  ? 46.65800  33.62900 -15.65000 1.000 175.12313 ?  43  GLN D CA  1 
ATOM   1794 C C   . GLN B 2 37  ? 46.50300  35.13600 -15.50300 1.000 178.80529 ?  43  GLN D C   1 
ATOM   1795 O O   . GLN B 2 37  ? 45.83100  35.77300 -16.32100 1.000 178.77200 ?  43  GLN D O   1 
ATOM   1796 C CB  . GLN B 2 37  ? 47.29300  33.29200 -17.00100 1.000 176.06892 ?  43  GLN D CB  1 
ATOM   1797 C CG  . GLN B 2 37  ? 48.62300  33.95500 -17.26800 1.000 181.88746 ?  43  GLN D CG  1 
ATOM   1798 C CD  . GLN B 2 37  ? 49.34700  33.32900 -18.44300 1.000 182.90113 ?  43  GLN D CD  1 
ATOM   1799 O OE1 . GLN B 2 37  ? 50.56000  33.11900 -18.40200 1.000 186.41810 ?  43  GLN D OE1 1 
ATOM   1800 N NE2 . GLN B 2 37  ? 48.60300  33.02500 -19.50000 1.000 180.18908 ?  43  GLN D NE2 1 
ATOM   1801 N N   . GLN B 2 38  ? 47.13100  35.70400 -14.48000 1.000 182.30403 ?  44  GLN D N   1 
ATOM   1802 C CA  . GLN B 2 38  ? 47.05000  37.12500 -14.17000 1.000 186.39812 ?  44  GLN D CA  1 
ATOM   1803 C C   . GLN B 2 38  ? 48.39300  37.74500 -14.52800 1.000 192.30423 ?  44  GLN D C   1 
ATOM   1804 O O   . GLN B 2 38  ? 49.34200  37.69400 -13.74100 1.000 195.25710 ?  44  GLN D O   1 
ATOM   1805 C CB  . GLN B 2 38  ? 46.70600  37.31000 -12.69300 1.000 186.48320 ?  44  GLN D CB  1 
ATOM   1806 C CG  . GLN B 2 38  ? 46.71900  38.73500 -12.16300 1.000 191.29959 ?  44  GLN D CG  1 
ATOM   1807 C CD  . GLN B 2 38  ? 45.88300  39.69200 -12.98600 1.000 191.84545 ?  44  GLN D CD  1 
ATOM   1808 O OE1 . GLN B 2 38  ? 44.82400  39.32900 -13.50300 1.000 187.67162 ?  44  GLN D OE1 1 
ATOM   1809 N NE2 . GLN B 2 38  ? 46.34200  40.93900 -13.08800 1.000 197.40644 ?  44  GLN D NE2 1 
ATOM   1810 N N   . LYS B 2 39  ? 48.45200  38.36900 -15.70000 1.000 180.89167 ?  45  LYS D N   1 
ATOM   1811 C CA  . LYS B 2 39  ? 49.63200  39.10400 -16.09000 1.000 183.36873 ?  45  LYS D CA  1 
ATOM   1812 C C   . LYS B 2 39  ? 49.72300  40.38100 -15.25900 1.000 182.65734 ?  45  LYS D C   1 
ATOM   1813 O O   . LYS B 2 39  ? 48.76000  40.76400 -14.59000 1.000 179.70107 ?  45  LYS D O   1 
ATOM   1814 C CB  . LYS B 2 39  ? 49.58400  39.42400 -17.58400 1.000 180.22760 ?  45  LYS D CB  1 
ATOM   1815 N N   . PRO B 2 40  ? 50.89100  41.03100 -15.24800 1.000 187.10171 ?  46  PRO D N   1 
ATOM   1816 C CA  . PRO B 2 40  ? 51.05800  42.25700 -14.45500 1.000 186.73672 ?  46  PRO D CA  1 
ATOM   1817 C C   . PRO B 2 40  ? 49.93600  43.26300 -14.63800 1.000 181.86730 ?  46  PRO D C   1 
ATOM   1818 O O   . PRO B 2 40  ? 49.80300  43.86500 -15.70700 1.000 179.63748 ?  46  PRO D O   1 
ATOM   1819 C CB  . PRO B 2 40  ? 52.37500  42.82200 -14.98800 1.000 188.90039 ?  46  PRO D CB  1 
ATOM   1820 C CG  . PRO B 2 40  ? 53.13900  41.62200 -15.38300 1.000 192.92813 ?  46  PRO D CG  1 
ATOM   1821 C CD  . PRO B 2 40  ? 52.17200  40.56000 -15.80200 1.000 191.59356 ?  46  PRO D CD  1 
ATOM   1822 N N   . GLY B 2 41  ? 49.14800  43.46700 -13.58400 1.000 184.10015 ?  47  GLY D N   1 
ATOM   1823 C CA  . GLY B 2 41  ? 48.05000  44.41600 -13.57600 1.000 180.00022 ?  47  GLY D CA  1 
ATOM   1824 C C   . GLY B 2 41  ? 47.16700  44.41200 -14.80800 1.000 176.13958 ?  47  GLY D C   1 
ATOM   1825 O O   . GLY B 2 41  ? 46.91400  45.47600 -15.38900 1.000 174.45105 ?  47  GLY D O   1 
ATOM   1826 N N   . LYS B 2 42  ? 46.69400  43.23300 -15.22300 1.000 171.24497 ?  48  LYS D N   1 
ATOM   1827 C CA  . LYS B 2 42  ? 45.87800  43.14500 -16.42800 1.000 168.35486 ?  48  LYS D CA  1 
ATOM   1828 C C   . LYS B 2 42  ? 44.66700  42.24700 -16.19500 1.000 166.07148 ?  48  LYS D C   1 
ATOM   1829 O O   . LYS B 2 42  ? 44.36100  41.90200 -15.05100 1.000 166.31535 ?  48  LYS D O   1 
ATOM   1830 C CB  . LYS B 2 42  ? 46.71500  42.64600 -17.60700 1.000 170.19261 ?  48  LYS D CB  1 
ATOM   1831 C CG  . LYS B 2 42  ? 47.72700  43.67400 -18.06800 1.000 172.06356 ?  48  LYS D CG  1 
ATOM   1832 C CD  . LYS B 2 42  ? 48.63100  43.18200 -19.17000 1.000 174.34441 ?  48  LYS D CD  1 
ATOM   1833 C CE  . LYS B 2 42  ? 47.84200  42.91000 -20.44200 1.000 172.84223 ?  48  LYS D CE  1 
ATOM   1834 N NZ  . LYS B 2 42  ? 48.74400  42.53300 -21.56400 1.000 175.55284 ?  48  LYS D NZ  1 
ATOM   1835 N N   . ALA B 2 43  ? 43.98200  41.86000 -17.25600 1.000 153.22765 ?  49  ALA D N   1 
ATOM   1836 C CA  . ALA B 2 43  ? 42.72100  41.14100 -17.09500 1.000 150.83403 ?  49  ALA D CA  1 
ATOM   1837 C C   . ALA B 2 43  ? 42.99100  39.65600 -16.90800 1.000 151.69801 ?  49  ALA D C   1 
ATOM   1838 O O   . ALA B 2 43  ? 43.72800  39.06500 -17.70300 1.000 153.50854 ?  49  ALA D O   1 
ATOM   1839 C CB  . ALA B 2 43  ? 41.81300  41.35200 -18.30400 1.000 149.77673 ?  49  ALA D CB  1 
ATOM   1840 N N   . PRO B 2 44  ? 42.44300  39.03000 -15.86500 1.000 142.68492 ?  50  PRO D N   1 
ATOM   1841 C CA  . PRO B 2 44  ? 42.60500  37.57500 -15.70400 1.000 143.76583 ?  50  PRO D CA  1 
ATOM   1842 C C   . PRO B 2 44  ? 42.02400  36.83000 -16.89400 1.000 143.00721 ?  50  PRO D C   1 
ATOM   1843 O O   . PRO B 2 44  ? 40.82000  36.88200 -17.15400 1.000 141.03829 ?  50  PRO D O   1 
ATOM   1844 C CB  . PRO B 2 44  ? 41.82600  37.27000 -14.41900 1.000 142.82049 ?  50  PRO D CB  1 
ATOM   1845 C CG  . PRO B 2 44  ? 41.69400  38.56000 -13.71000 1.000 142.20975 ?  50  PRO D CG  1 
ATOM   1846 C CD  . PRO B 2 44  ? 41.64000  39.61800 -14.78000 1.000 141.15276 ?  50  PRO D CD  1 
ATOM   1847 N N   . LYS B 2 45  ? 42.88800  36.13500 -17.62000 1.000 142.11319 ?  51  LYS D N   1 
ATOM   1848 C CA  . LYS B 2 45  ? 42.46600  35.26700 -18.70600 1.000 142.53668 ?  51  LYS D CA  1 
ATOM   1849 C C   . LYS B 2 45  ? 42.44500  33.84200 -18.18000 1.000 143.94551 ?  51  LYS D C   1 
ATOM   1850 O O   . LYS B 2 45  ? 43.27900  33.47100 -17.34800 1.000 145.66092 ?  51  LYS D O   1 
ATOM   1851 C CB  . LYS B 2 45  ? 43.40800  35.38200 -19.90500 1.000 144.27205 ?  51  LYS D CB  1 
ATOM   1852 N N   . LEU B 2 46  ? 41.50100  33.04200 -18.65500 1.000 149.87113 ?  52  LEU D N   1 
ATOM   1853 C CA  . LEU B 2 46  ? 41.42400  31.68000 -18.15500 1.000 151.01827 ?  52  LEU D CA  1 
ATOM   1854 C C   . LEU B 2 46  ? 42.27900  30.76700 -19.01300 1.000 153.73420 ?  52  LEU D C   1 
ATOM   1855 O O   . LEU B 2 46  ? 42.45800  30.98700 -20.21400 1.000 154.33567 ?  52  LEU D O   1 
ATOM   1856 C CB  . LEU B 2 46  ? 39.98800  31.14400 -18.10300 1.000 149.70140 ?  52  LEU D CB  1 
ATOM   1857 C CG  . LEU B 2 46  ? 39.24000  30.52800 -19.28800 1.000 150.11588 ?  52  LEU D CG  1 
ATOM   1858 C CD1 . LEU B 2 46  ? 39.55500  29.06100 -19.42600 1.000 152.43305 ?  52  LEU D CD1 1 
ATOM   1859 C CD2 . LEU B 2 46  ? 37.75400  30.67700 -19.05800 1.000 149.03186 ?  52  LEU D CD2 1 
ATOM   1860 N N   . LEU B 2 47  ? 42.81900  29.74500 -18.37300 1.000 158.97234 ?  53  LEU D N   1 
ATOM   1861 C CA  . LEU B 2 47  ? 43.60600  28.73200 -19.05000 1.000 161.96336 ?  53  LEU D CA  1 
ATOM   1862 C C   . LEU B 2 47  ? 42.95400  27.36700 -19.00100 1.000 162.36115 ?  53  LEU D C   1 
ATOM   1863 O O   . LEU B 2 47  ? 43.00800  26.63100 -19.98900 1.000 163.31094 ?  53  LEU D O   1 
ATOM   1864 C CB  . LEU B 2 47  ? 45.01200  28.64500 -18.44000 1.000 166.38310 ?  53  LEU D CB  1 
ATOM   1865 C CG  . LEU B 2 47  ? 45.64400  29.97300 -18.02500 1.000 166.94013 ?  53  LEU D CG  1 
ATOM   1866 C CD1 . LEU B 2 47  ? 46.95800  29.72200 -17.31300 1.000 172.84951 ?  53  LEU D CD1 1 
ATOM   1867 C CD2 . LEU B 2 47  ? 45.84300  30.88800 -19.22800 1.000 165.64724 ?  53  LEU D CD2 1 
ATOM   1868 N N   . ILE B 2 48  ? 42.30900  27.01900 -17.88900 1.000 156.31071 ?  54  ILE D N   1 
ATOM   1869 C CA  . ILE B 2 48  ? 41.74800  25.68300 -17.70800 1.000 158.10726 ?  54  ILE D CA  1 
ATOM   1870 C C   . ILE B 2 48  ? 40.31300  25.81200 -17.22300 1.000 155.97615 ?  54  ILE D C   1 
ATOM   1871 O O   . ILE B 2 48  ? 40.05700  26.48500 -16.22300 1.000 154.54239 ?  54  ILE D O   1 
ATOM   1872 C CB  . ILE B 2 48  ? 42.56500  24.85800 -16.69500 1.000 161.98159 ?  54  ILE D CB  1 
ATOM   1873 C CG1 . ILE B 2 48  ? 43.92000  24.46000 -17.28400 1.000 165.00769 ?  54  ILE D CG1 1 
ATOM   1874 C CG2 . ILE B 2 48  ? 41.79100  23.63100 -16.24400 1.000 164.47709 ?  54  ILE D CG2 1 
ATOM   1875 C CD1 . ILE B 2 48  ? 43.85900  23.82500 -18.65300 1.000 165.97727 ?  54  ILE D CD1 1 
ATOM   1876 N N   . TYR B 2 49  ? 39.38300  25.15900 -17.90900 1.000 156.23161 ?  55  TYR D N   1 
ATOM   1877 C CA  . TYR B 2 49  ? 38.00600  25.11100 -17.44400 1.000 154.99165 ?  55  TYR D CA  1 
ATOM   1878 C C   . TYR B 2 49  ? 37.57900  23.66400 -17.24100 1.000 158.53459 ?  55  TYR D C   1 
ATOM   1879 O O   . TYR B 2 49  ? 38.15400  22.73900 -17.82000 1.000 161.52023 ?  55  TYR D O   1 
ATOM   1880 C CB  . TYR B 2 49  ? 37.04600  25.79300 -18.42400 1.000 152.15846 ?  55  TYR D CB  1 
ATOM   1881 C CG  . TYR B 2 49  ? 37.16900  25.31800 -19.85300 1.000 153.32331 ?  55  TYR D CG  1 
ATOM   1882 C CD1 . TYR B 2 49  ? 38.21000  25.74400 -20.67200 1.000 153.31734 ?  55  TYR D CD1 1 
ATOM   1883 C CD2 . TYR B 2 49  ? 36.24900  24.42100 -20.37800 1.000 154.82306 ?  55  TYR D CD2 1 
ATOM   1884 C CE1 . TYR B 2 49  ? 38.31900  25.30400 -21.97900 1.000 154.68553 ?  55  TYR D CE1 1 
ATOM   1885 C CE2 . TYR B 2 49  ? 36.34600  23.97900 -21.67900 1.000 156.17689 ?  55  TYR D CE2 1 
ATOM   1886 C CZ  . TYR B 2 49  ? 37.38700  24.41900 -22.47400 1.000 156.09268 ?  55  TYR D CZ  1 
ATOM   1887 O OH  . TYR B 2 49  ? 37.49200  23.97500 -23.77100 1.000 157.73291 ?  55  TYR D OH  1 
ATOM   1888 N N   . LYS B 2 50  ? 36.55000  23.48000 -16.40600 1.000 158.49543 ?  56  LYS D N   1 
ATOM   1889 C CA  . LYS B 2 50  ? 36.08700  22.15200 -15.99100 1.000 162.30466 ?  56  LYS D CA  1 
ATOM   1890 C C   . LYS B 2 50  ? 37.22500  21.32100 -15.39700 1.000 166.43037 ?  56  LYS D C   1 
ATOM   1891 O O   . LYS B 2 50  ? 37.19000  20.08700 -15.42600 1.000 170.52443 ?  56  LYS D O   1 
ATOM   1892 C CB  . LYS B 2 50  ? 35.38600  21.43200 -17.15100 1.000 163.33851 ?  56  LYS D CB  1 
ATOM   1893 C CG  . LYS B 2 50  ? 33.93700  21.91600 -17.36500 1.000 160.82462 ?  56  LYS D CG  1 
ATOM   1894 C CD  . LYS B 2 50  ? 33.47300  21.83600 -18.81900 1.000 160.38960 ?  56  LYS D CD  1 
ATOM   1895 C CE  . LYS B 2 50  ? 34.16400  20.73700 -19.59500 1.000 163.90330 ?  56  LYS D CE  1 
ATOM   1896 N NZ  . LYS B 2 50  ? 33.58400  20.58500 -20.96000 1.000 163.97711 ?  56  LYS D NZ  1 
ATOM   1897 N N   . ALA B 2 51  ? 38.24800  22.01900 -14.89400 1.000 165.68577 ?  57  ALA D N   1 
ATOM   1898 C CA  . ALA B 2 51  ? 39.37700  21.47200 -14.14200 1.000 169.55677 ?  57  ALA D CA  1 
ATOM   1899 C C   . ALA B 2 51  ? 40.35000  20.62000 -14.94900 1.000 172.95577 ?  57  ALA D C   1 
ATOM   1900 O O   . ALA B 2 51  ? 41.41200  20.25300 -14.43900 1.000 176.33991 ?  57  ALA D O   1 
ATOM   1901 C CB  . ALA B 2 51  ? 38.85700  20.65000 -12.96100 1.000 173.00906 ?  57  ALA D CB  1 
ATOM   1902 N N   . SER B 2 52  ? 40.01900  20.29300 -16.19300 1.000 172.49280 ?  65  SER D N   1 
ATOM   1903 C CA  . SER B 2 52  ? 40.99500  19.63800 -17.06200 1.000 175.40097 ?  65  SER D CA  1 
ATOM   1904 C C   . SER B 2 52  ? 41.02600  20.17600 -18.48300 1.000 172.67578 ?  65  SER D C   1 
ATOM   1905 O O   . SER B 2 52  ? 42.06700  20.06100 -19.13700 1.000 174.21944 ?  65  SER D O   1 
ATOM   1906 C CB  . SER B 2 52  ? 40.74600  18.12700 -17.11800 1.000 180.40712 ?  65  SER D CB  1 
ATOM   1907 O OG  . SER B 2 52  ? 39.42300  17.83500 -17.52500 1.000 179.39673 ?  65  SER D OG  1 
ATOM   1908 N N   . GLU B 2 53  ? 39.93100  20.73200 -18.98800 1.000 169.17714 ?  66  GLU D N   1 
ATOM   1909 C CA  . GLU B 2 53  ? 39.89000  21.26400 -20.34000 1.000 167.03857 ?  66  GLU D CA  1 
ATOM   1910 C C   . GLU B 2 53  ? 40.73400  22.52700 -20.44500 1.000 164.37947 ?  66  GLU D C   1 
ATOM   1911 O O   . GLU B 2 53  ? 40.92900  23.25100 -19.46700 1.000 163.69719 ?  66  GLU D O   1 
ATOM   1912 C CB  . GLU B 2 53  ? 38.44800  21.56000 -20.73700 1.000 164.50175 ?  66  GLU D CB  1 
ATOM   1913 C CG  . GLU B 2 53  ? 37.52200  20.37700 -20.54500 1.000 167.23353 ?  66  GLU D CG  1 
ATOM   1914 C CD  . GLU B 2 53  ? 37.00900  19.81900 -21.85500 1.000 168.41166 ?  66  GLU D CD  1 
ATOM   1915 O OE1 . GLU B 2 53  ? 37.45800  20.29800 -22.92000 1.000 167.36905 ?  66  GLU D OE1 1 
ATOM   1916 O OE2 . GLU B 2 53  ? 36.15800  18.90200 -21.81400 1.000 170.70568 ?  66  GLU D OE2 1 
ATOM   1917 N N   . LEU B 2 54  ? 41.20300  22.81000 -21.65800 1.000 164.11227 ?  67  LEU D N   1 
ATOM   1918 C CA  . LEU B 2 54  ? 42.14900  23.88900 -21.91000 1.000 164.32843 ?  67  LEU D CA  1 
ATOM   1919 C C   . LEU B 2 54  ? 41.53300  24.91100 -22.85500 1.000 163.76865 ?  67  LEU D C   1 
ATOM   1920 O O   . LEU B 2 54  ? 40.97300  24.54900 -23.89400 1.000 164.83196 ?  67  LEU D O   1 
ATOM   1921 C CB  . LEU B 2 54  ? 43.46200  23.33100 -22.47600 1.000 167.73795 ?  67  LEU D CB  1 
ATOM   1922 C CG  . LEU B 2 54  ? 44.49700  24.29700 -23.05100 1.000 170.24320 ?  67  LEU D CG  1 
ATOM   1923 C CD1 . LEU B 2 54  ? 45.88200  23.91700 -22.57300 1.000 173.94910 ?  67  LEU D CD1 1 
ATOM   1924 C CD2 . LEU B 2 54  ? 44.45500  24.26900 -24.56800 1.000 172.30255 ?  67  LEU D CD2 1 
ATOM   1925 N N   . TYR B 2 55  ? 41.64200  26.18700 -22.48900 1.000 162.60643 ?  68  TYR D N   1 
ATOM   1926 C CA  . TYR B 2 55  ? 41.06900  27.25700 -23.28900 1.000 162.28932 ?  68  TYR D CA  1 
ATOM   1927 C C   . TYR B 2 55  ? 41.77300  27.37100 -24.63800 1.000 165.28490 ?  68  TYR D C   1 
ATOM   1928 O O   . TYR B 2 55  ? 42.93900  27.00400 -24.80000 1.000 167.48218 ?  68  TYR D O   1 
ATOM   1929 C CB  . TYR B 2 55  ? 41.15500  28.59100 -22.55100 1.000 160.30564 ?  68  TYR D CB  1 
ATOM   1930 C CG  . TYR B 2 55  ? 40.08200  29.56700 -22.96900 1.000 159.49306 ?  68  TYR D CG  1 
ATOM   1931 C CD1 . TYR B 2 55  ? 38.74400  29.20500 -22.92900 1.000 159.46159 ?  68  TYR D CD1 1 
ATOM   1932 C CD2 . TYR B 2 55  ? 40.40400  30.83300 -23.43000 1.000 159.64598 ?  68  TYR D CD2 1 
ATOM   1933 C CE1 . TYR B 2 55  ? 37.75600  30.07900 -23.31600 1.000 160.01337 ?  68  TYR D CE1 1 
ATOM   1934 C CE2 . TYR B 2 55  ? 39.41800  31.71800 -23.82400 1.000 159.75120 ?  68  TYR D CE2 1 
ATOM   1935 C CZ  . TYR B 2 55  ? 38.09500  31.33500 -23.76700 1.000 160.16877 ?  68  TYR D CZ  1 
ATOM   1936 O OH  . TYR B 2 55  ? 37.11300  32.22200 -24.16000 1.000 161.48837 ?  68  TYR D OH  1 
ATOM   1937 N N   . ALA B 2 56  ? 41.04100  27.90600 -25.61500 1.000 165.21220 ?  69  ALA D N   1 
ATOM   1938 C CA  . ALA B 2 56  ? 41.59900  28.10600 -26.94500 1.000 168.40791 ?  69  ALA D CA  1 
ATOM   1939 C C   . ALA B 2 56  ? 42.79000  29.05600 -26.89700 1.000 168.90713 ?  69  ALA D C   1 
ATOM   1940 O O   . ALA B 2 56  ? 42.77400  30.07400 -26.19800 1.000 166.93155 ?  69  ALA D O   1 
ATOM   1941 C CB  . ALA B 2 56  ? 40.52800  28.64400 -27.89100 1.000 170.11429 ?  69  ALA D CB  1 
ATOM   1942 N N   . GLY B 2 57  ? 43.83800  28.70500 -27.64000 1.000 176.34804 ?  70  GLY D N   1 
ATOM   1943 C CA  . GLY B 2 57  ? 45.06400  29.46200 -27.65600 1.000 177.37635 ?  70  GLY D CA  1 
ATOM   1944 C C   . GLY B 2 57  ? 46.06600  29.06800 -26.59000 1.000 178.01871 ?  70  GLY D C   1 
ATOM   1945 O O   . GLY B 2 57  ? 47.27500  29.23000 -26.80100 1.000 180.31070 ?  70  GLY D O   1 
ATOM   1946 N N   . VAL B 2 58  ? 45.59300  28.55700 -25.45600 1.000 175.52139 ?  71  VAL D N   1 
ATOM   1947 C CA  . VAL B 2 58  ? 46.48700  28.24300 -24.33500 1.000 177.11446 ?  71  VAL D CA  1 
ATOM   1948 C C   . VAL B 2 58  ? 47.51300  27.20600 -24.78000 1.000 181.85609 ?  71  VAL D C   1 
ATOM   1949 O O   . VAL B 2 58  ? 47.14700  26.21800 -25.45000 1.000 182.25274 ?  71  VAL D O   1 
ATOM   1950 C CB  . VAL B 2 58  ? 45.67800  27.74700 -23.12400 1.000 173.98259 ?  71  VAL D CB  1 
ATOM   1951 C CG1 . VAL B 2 58  ? 46.60100  27.43800 -21.95600 1.000 176.26212 ?  71  VAL D CG1 1 
ATOM   1952 C CG2 . VAL B 2 58  ? 44.66500  28.79300 -22.72100 1.000 169.66464 ?  71  VAL D CG2 1 
ATOM   1953 N N   . PRO B 2 59  ? 48.79300  27.38800 -24.44900 1.000 178.06007 ?  72  PRO D N   1 
ATOM   1954 C CA  . PRO B 2 59  ? 49.84000  26.49800 -24.96300 1.000 182.83136 ?  72  PRO D CA  1 
ATOM   1955 C C   . PRO B 2 59  ? 49.68100  25.05200 -24.52300 1.000 184.71508 ?  72  PRO D C   1 
ATOM   1956 O O   . PRO B 2 59  ? 49.14000  24.75300 -23.45500 1.000 182.50317 ?  72  PRO D O   1 
ATOM   1957 C CB  . PRO B 2 59  ? 51.12600  27.10300 -24.38900 1.000 186.62565 ?  72  PRO D CB  1 
ATOM   1958 C CG  . PRO B 2 59  ? 50.81500  28.55000 -24.25100 1.000 183.07675 ?  72  PRO D CG  1 
ATOM   1959 C CD  . PRO B 2 59  ? 49.35500  28.62300 -23.87400 1.000 178.28833 ?  72  PRO D CD  1 
ATOM   1960 N N   . SER B 2 60  ? 50.16700  24.15200 -25.38600 1.000 178.59760 ?  74  SER D N   1 
ATOM   1961 C CA  . SER B 2 60  ? 50.16800  22.72400 -25.08000 1.000 180.99906 ?  74  SER D CA  1 
ATOM   1962 C C   . SER B 2 60  ? 50.93200  22.42400 -23.79500 1.000 183.83132 ?  74  SER D C   1 
ATOM   1963 O O   . SER B 2 60  ? 50.65500  21.42200 -23.12800 1.000 185.70127 ?  74  SER D O   1 
ATOM   1964 C CB  . SER B 2 60  ? 50.77700  21.94300 -26.25000 1.000 184.76796 ?  74  SER D CB  1 
ATOM   1965 O OG  . SER B 2 60  ? 50.06400  22.15100 -27.45900 1.000 183.04442 ?  74  SER D OG  1 
ATOM   1966 N N   . ARG B 2 61  ? 51.89300  23.28100 -23.43500 1.000 187.17238 ?  75  ARG D N   1 
ATOM   1967 C CA  . ARG B 2 61  ? 52.67300  23.11200 -22.21500 1.000 190.36995 ?  75  ARG D CA  1 
ATOM   1968 C C   . ARG B 2 61  ? 51.82400  23.22200 -20.95300 1.000 184.12744 ?  75  ARG D C   1 
ATOM   1969 O O   . ARG B 2 61  ? 52.25000  22.75600 -19.89100 1.000 187.07650 ?  75  ARG D O   1 
ATOM   1970 C CB  . ARG B 2 61  ? 53.80400  24.14300 -22.22200 1.000 193.80768 ?  75  ARG D CB  1 
ATOM   1971 C CG  . ARG B 2 61  ? 53.40800  25.52000 -21.72600 1.000 191.64755 ?  75  ARG D CG  1 
ATOM   1972 C CD  . ARG B 2 61  ? 54.59800  26.45600 -21.78300 1.000 193.72812 ?  75  ARG D CD  1 
ATOM   1973 N NE  . ARG B 2 61  ? 54.21200  27.81000 -22.16400 1.000 190.33148 ?  75  ARG D NE  1 
ATOM   1974 C CZ  . ARG B 2 61  ? 54.38600  28.32100 -23.37500 1.000 186.33382 ?  75  ARG D CZ  1 
ATOM   1975 N NH1 . ARG B 2 61  ? 54.90300  27.60600 -24.36100 1.000 186.76047 ?  75  ARG D NH1 1 
ATOM   1976 N NH2 . ARG B 2 61  ? 54.02400  29.57900 -23.60700 1.000 181.20483 ?  75  ARG D NH2 1 
ATOM   1977 N N   . PHE B 2 62  ? 50.63700  23.81400 -21.04600 1.000 194.88497 ?  76  PHE D N   1 
ATOM   1978 C CA  . PHE B 2 62  ? 49.71200  23.93000 -19.92700 1.000 192.78042 ?  76  PHE D CA  1 
ATOM   1979 C C   . PHE B 2 62  ? 48.82100  22.69500 -19.84300 1.000 194.97158 ?  76  PHE D C   1 
ATOM   1980 O O   . PHE B 2 62  ? 48.45900  22.09800 -20.86100 1.000 195.53052 ?  76  PHE D O   1 
ATOM   1981 C CB  . PHE B 2 62  ? 48.86400  25.19300 -20.05900 1.000 186.15669 ?  76  PHE D CB  1 
ATOM   1982 C CG  . PHE B 2 62  ? 49.62100  26.46300 -19.79200 1.000 183.98971 ?  76  PHE D CG  1 
ATOM   1983 C CD1 . PHE B 2 62  ? 49.91800  26.85000 -18.49700 1.000 184.47863 ?  76  PHE D CD1 1 
ATOM   1984 C CD2 . PHE B 2 62  ? 50.03000  27.27100 -20.83600 1.000 181.75222 ?  76  PHE D CD2 1 
ATOM   1985 C CE1 . PHE B 2 62  ? 50.61100  28.02200 -18.25000 1.000 183.87740 ?  76  PHE D CE1 1 
ATOM   1986 C CE2 . PHE B 2 62  ? 50.71900  28.44000 -20.59700 1.000 182.81661 ?  76  PHE D CE2 1 
ATOM   1987 C CZ  . PHE B 2 62  ? 51.01000  28.81700 -19.30300 1.000 184.65273 ?  76  PHE D CZ  1 
ATOM   1988 N N   . SER B 2 63  ? 48.50000  22.29600 -18.61200 1.000 196.64201 ?  77  SER D N   1 
ATOM   1989 C CA  . SER B 2 63  ? 47.74300  21.07400 -18.35300 1.000 199.53967 ?  77  SER D CA  1 
ATOM   1990 C C   . SER B 2 63  ? 47.12900  21.14000 -16.95900 1.000 199.22240 ?  77  SER D C   1 
ATOM   1991 O O   . SER B 2 63  ? 47.57800  21.91200 -16.11600 1.000 198.42307 ?  77  SER D O   1 
ATOM   1992 C CB  . SER B 2 63  ? 48.63800  19.83400 -18.45800 1.000 206.51396 ?  77  SER D CB  1 
ATOM   1993 O OG  . SER B 2 63  ? 49.36000  19.81700 -19.67500 1.000 207.37027 ?  77  SER D OG  1 
ATOM   1994 N N   . GLY B 2 64  ? 46.08300  20.34200 -16.72900 1.000 199.99944 ?  78  GLY D N   1 
ATOM   1995 C CA  . GLY B 2 64  ? 45.45700  20.27200 -15.42500 1.000 200.40183 ?  78  GLY D CA  1 
ATOM   1996 C C   . GLY B 2 64  ? 45.27300  18.83900 -14.96100 1.000 206.24772 ?  78  GLY D C   1 
ATOM   1997 O O   . GLY B 2 64  ? 45.24700  17.90400 -15.75900 1.000 208.88005 ?  78  GLY D O   1 
ATOM   1998 N N   . SER B 2 65  ? 45.11700  18.68100 -13.64700 1.000 208.47521 ?  79  SER D N   1 
ATOM   1999 C CA  . SER B 2 65  ? 44.87600  17.36000 -13.07900 1.000 214.26137 ?  79  SER D CA  1 
ATOM   2000 C C   . SER B 2 65  ? 44.06800  17.48000 -11.79300 1.000 214.09125 ?  79  SER D C   1 
ATOM   2001 O O   . SER B 2 65  ? 43.93500  18.55800 -11.21200 1.000 210.39959 ?  79  SER D O   1 
ATOM   2002 C CB  . SER B 2 65  ? 46.19100  16.63100 -12.81300 1.000 221.08340 ?  79  SER D CB  1 
ATOM   2003 O OG  . SER B 2 65  ? 47.00700  17.40300 -11.95500 1.000 221.47599 ?  79  SER D OG  1 
ATOM   2004 N N   . ARG B 2 66  ? 43.56100  16.33600 -11.33600 1.000 218.59795 ?  80  ARG D N   1 
ATOM   2005 C CA  . ARG B 2 66  ? 42.62500  16.25100 -10.21700 1.000 219.01157 ?  80  ARG D CA  1 
ATOM   2006 C C   . ARG B 2 66  ? 42.99300  15.04100 -9.36100  1.000 226.94690 ?  80  ARG D C   1 
ATOM   2007 O O   . ARG B 2 66  ? 42.84400  13.89700 -9.80400  1.000 230.76686 ?  80  ARG D O   1 
ATOM   2008 C CB  . ARG B 2 66  ? 41.19900  16.14600 -10.75900 1.000 215.26928 ?  80  ARG D CB  1 
ATOM   2009 C CG  . ARG B 2 66  ? 40.13800  15.66300 -9.79900  1.000 217.05230 ?  80  ARG D CG  1 
ATOM   2010 C CD  . ARG B 2 66  ? 38.83300  15.49100 -10.57200 1.000 213.70518 ?  80  ARG D CD  1 
ATOM   2011 N NE  . ARG B 2 66  ? 37.63500  15.79800 -9.79700  1.000 211.73690 ?  80  ARG D NE  1 
ATOM   2012 C CZ  . ARG B 2 66  ? 37.18200  15.06100 -8.79000  1.000 216.15626 ?  80  ARG D CZ  1 
ATOM   2013 N NH1 . ARG B 2 66  ? 37.79200  13.94800 -8.41500  1.000 222.93285 ?  80  ARG D NH1 1 
ATOM   2014 N NH2 . ARG B 2 66  ? 36.07500  15.43700 -8.15600  1.000 214.03248 ?  80  ARG D NH2 1 
ATOM   2015 N N   . SER B 2 67  ? 43.46900  15.29500 -8.14200  1.000 229.71283 ?  83  SER D N   1 
ATOM   2016 C CA  . SER B 2 67  ? 43.81300  14.25400 -7.16300  1.000 237.63627 ?  83  SER D CA  1 
ATOM   2017 C C   . SER B 2 67  ? 42.71400  14.03700 -6.12900  1.000 238.57857 ?  83  SER D C   1 
ATOM   2018 O O   . SER B 2 67  ? 42.97400  14.04600 -4.92400  1.000 242.43168 ?  83  SER D O   1 
ATOM   2019 C CB  . SER B 2 67  ? 45.12600  14.60400 -6.47200  1.000 241.18308 ?  83  SER D CB  1 
ATOM   2020 O OG  . SER B 2 67  ? 45.26100  13.88100 -5.25600  1.000 248.19413 ?  83  SER D OG  1 
ATOM   2021 N N   . GLY B 2 68  ? 41.48100  13.80000 -6.56300  1.000 235.64557 ?  84  GLY D N   1 
ATOM   2022 C CA  . GLY B 2 68  ? 40.40800  13.68000 -5.60100  1.000 236.28994 ?  84  GLY D CA  1 
ATOM   2023 C C   . GLY B 2 68  ? 39.88300  15.06000 -5.26600  1.000 229.81274 ?  84  GLY D C   1 
ATOM   2024 O O   . GLY B 2 68  ? 38.99500  15.58300 -5.94400  1.000 223.92668 ?  84  GLY D O   1 
ATOM   2025 N N   . THR B 2 69  ? 40.44400  15.67700 -4.22900  1.000 231.09780 ?  85  THR D N   1 
ATOM   2026 C CA  . THR B 2 69  ? 40.08700  17.04200 -3.86800  1.000 225.37928 ?  85  THR D CA  1 
ATOM   2027 C C   . THR B 2 69  ? 41.22200  18.04000 -4.07600  1.000 222.99500 ?  85  THR D C   1 
ATOM   2028 O O   . THR B 2 69  ? 41.09800  19.19000 -3.64700  1.000 219.10909 ?  85  THR D O   1 
ATOM   2029 C CB  . THR B 2 69  ? 39.61600  17.10300 -2.41600  1.000 228.31380 ?  85  THR D CB  1 
ATOM   2030 O OG1 . THR B 2 69  ? 40.74100  16.93600 -1.54700  1.000 234.12541 ?  85  THR D OG1 1 
ATOM   2031 C CG2 . THR B 2 69  ? 38.59400  16.00800 -2.13500  1.000 231.82281 ?  85  THR D CG2 1 
ATOM   2032 N N   . ASP B 2 70  ? 42.32600  17.64000 -4.70100  1.000 225.47903 ?  86  ASP D N   1 
ATOM   2033 C CA  . ASP B 2 70  ? 43.49900  18.50400 -4.84400  1.000 224.19067 ?  86  ASP D CA  1 
ATOM   2034 C C   . ASP B 2 70  ? 43.79800  18.66000 -6.33400  1.000 220.36553 ?  86  ASP D C   1 
ATOM   2035 O O   . ASP B 2 70  ? 44.40100  17.77400 -6.94800  1.000 224.05886 ?  86  ASP D O   1 
ATOM   2036 C CB  . ASP B 2 70  ? 44.69600  17.94000 -4.07800  1.000 231.71599 ?  86  ASP D CB  1 
ATOM   2037 C CG  . ASP B 2 70  ? 44.66100  18.28700 -2.59300  1.000 234.49042 ?  86  ASP D CG  1 
ATOM   2038 O OD1 . ASP B 2 70  ? 44.07100  17.50400 -1.81800  1.000 238.78038 ?  86  ASP D OD1 1 
ATOM   2039 O OD2 . ASP B 2 70  ? 45.22800  19.32900 -2.19700  1.000 232.70996 ?  86  ASP D OD2 1 
ATOM   2040 N N   . PHE B 2 71  ? 43.38600  19.79100 -6.90900  1.000 213.31263 ?  87  PHE D N   1 
ATOM   2041 C CA  . PHE B 2 71  ? 43.55200  20.04600 -8.34100  1.000 209.36282 ?  87  PHE D CA  1 
ATOM   2042 C C   . PHE B 2 71  ? 44.85500  20.77900 -8.62600  1.000 208.89466 ?  87  PHE D C   1 
ATOM   2043 O O   . PHE B 2 71  ? 45.18400  21.74800 -7.95100  1.000 207.38828 ?  87  PHE D O   1 
ATOM   2044 C CB  . PHE B 2 71  ? 42.38300  20.86900 -8.88000  1.000 202.34510 ?  87  PHE D CB  1 
ATOM   2045 C CG  . PHE B 2 71  ? 41.05000  20.43800 -8.36100  1.000 202.33502 ?  87  PHE D CG  1 
ATOM   2046 C CD1 . PHE B 2 71  ? 40.33800  19.44000 -9.00100  1.000 203.48727 ?  87  PHE D CD1 1 
ATOM   2047 C CD2 . PHE B 2 71  ? 40.50600  21.02800 -7.23600  1.000 201.43426 ?  87  PHE D CD2 1 
ATOM   2048 C CE1 . PHE B 2 71  ? 39.10900  19.03800 -8.52600  1.000 203.72311 ?  87  PHE D CE1 1 
ATOM   2049 C CE2 . PHE B 2 71  ? 39.27700  20.62900 -6.76000  1.000 201.69409 ?  87  PHE D CE2 1 
ATOM   2050 C CZ  . PHE B 2 71  ? 38.57800  19.63300 -7.40300  1.000 202.83294 ?  87  PHE D CZ  1 
ATOM   2051 N N   . THR B 2 72  ? 45.56400  20.36000 -9.67500  1.000 210.06441 ?  88  THR D N   1 
ATOM   2052 C CA  . THR B 2 72  ? 46.87400  20.92600 -9.98300  1.000 210.50219 ?  88  THR D CA  1 
ATOM   2053 C C   . THR B 2 72  ? 46.95100  21.45000 -11.41400 1.000 205.85145 ?  88  THR D C   1 
ATOM   2054 O O   . THR B 2 72  ? 46.28100  20.95200 -12.32100 1.000 204.47725 ?  88  THR D O   1 
ATOM   2055 C CB  . THR B 2 72  ? 47.99800  19.90000 -9.75900  1.000 218.11178 ?  88  THR D CB  1 
ATOM   2056 O OG1 . THR B 2 72  ? 48.09400  19.03200 -10.89400 1.000 219.61739 ?  88  THR D OG1 1 
ATOM   2057 C CG2 . THR B 2 72  ? 47.72800  19.07100 -8.51200  1.000 223.56796 ?  88  THR D CG2 1 
ATOM   2058 N N   . LEU B 2 73  ? 47.75500  22.49700 -11.58400 1.000 203.59117 ?  89  LEU D N   1 
ATOM   2059 C CA  . LEU B 2 73  ? 48.10100  23.07400 -12.87600 1.000 200.07923 ?  89  LEU D CA  1 
ATOM   2060 C C   . LEU B 2 73  ? 49.55400  22.73500 -13.19900 1.000 204.72856 ?  89  LEU D C   1 
ATOM   2061 O O   . LEU B 2 73  ? 50.43800  22.89900 -12.35400 1.000 208.03628 ?  89  LEU D O   1 
ATOM   2062 C CB  . LEU B 2 73  ? 47.87200  24.58900 -12.87600 1.000 193.94364 ?  89  LEU D CB  1 
ATOM   2063 C CG  . LEU B 2 73  ? 48.21700  25.42300 -14.11500 1.000 189.98769 ?  89  LEU D CG  1 
ATOM   2064 C CD1 . LEU B 2 73  ? 47.72900  24.78600 -15.39600 1.000 189.26365 ?  89  LEU D CD1 1 
ATOM   2065 C CD2 . LEU B 2 73  ? 47.61400  26.80100 -13.97700 1.000 183.97123 ?  89  LEU D CD2 1 
ATOM   2066 N N   . THR B 2 74  ? 49.79000  22.24900 -14.41600 1.000 205.32033 ?  90  THR D N   1 
ATOM   2067 C CA  . THR B 2 74  ? 51.06100  21.68800 -14.85000 1.000 210.45023 ?  90  THR D CA  1 
ATOM   2068 C C   . THR B 2 74  ? 51.58300  22.45100 -16.05900 1.000 207.34436 ?  90  THR D C   1 
ATOM   2069 O O   . THR B 2 74  ? 50.85600  22.62700 -17.04000 1.000 203.37375 ?  90  THR D O   1 
ATOM   2070 C CB  . THR B 2 74  ? 50.87000  20.21300 -15.22000 1.000 215.18149 ?  90  THR D CB  1 
ATOM   2071 O OG1 . THR B 2 74  ? 50.77300  19.42300 -14.03000 1.000 219.95129 ?  90  THR D OG1 1 
ATOM   2072 C CG2 . THR B 2 74  ? 52.02000  19.71000 -16.08300 1.000 219.41243 ?  90  THR D CG2 1 
ATOM   2073 N N   . ILE B 2 75  ? 52.82500  22.92100 -15.99400 1.000 209.34749 ?  91  ILE D N   1 
ATOM   2074 C CA  . ILE B 2 75  ? 53.51300  23.50500 -17.14200 1.000 207.79957 ?  91  ILE D CA  1 
ATOM   2075 C C   . ILE B 2 75  ? 54.75300  22.66200 -17.41700 1.000 214.56156 ?  91  ILE D C   1 
ATOM   2076 O O   . ILE B 2 75  ? 55.65800  22.59800 -16.57700 1.000 218.83783 ?  91  ILE D O   1 
ATOM   2077 C CB  . ILE B 2 75  ? 53.87600  24.97800 -16.88900 1.000 203.81304 ?  91  ILE D CB  1 
ATOM   2078 C CG1 . ILE B 2 75  ? 52.68000  25.72900 -16.29200 1.000 198.25578 ?  91  ILE D CG1 1 
ATOM   2079 C CG2 . ILE B 2 75  ? 54.38500  25.63800 -18.16200 1.000 201.60975 ?  91  ILE D CG2 1 
ATOM   2080 C CD1 . ILE B 2 75  ? 52.80300  26.01600 -14.80800 1.000 199.58380 ?  91  ILE D CD1 1 
ATOM   2081 N N   . SER B 2 76  ? 54.80800  22.02400 -18.58800 1.000 215.87056 ?  92  SER D N   1 
ATOM   2082 C CA  . SER B 2 76  ? 55.90200  21.08800 -18.84600 1.000 222.85771 ?  92  SER D CA  1 
ATOM   2083 C C   . SER B 2 76  ? 57.18800  21.81100 -19.23700 1.000 223.95995 ?  92  SER D C   1 
ATOM   2084 O O   . SER B 2 76  ? 58.19000  21.74600 -18.51900 1.000 228.52531 ?  92  SER D O   1 
ATOM   2085 C CB  . SER B 2 76  ? 55.49800  20.07800 -19.92100 1.000 224.47609 ?  92  SER D CB  1 
ATOM   2086 O OG  . SER B 2 76  ? 55.09400  20.73800 -21.10300 1.000 219.51146 ?  92  SER D OG  1 
ATOM   2087 N N   . SER B 2 77  ? 57.18000  22.52200 -20.36100 1.000 220.09865 ?  93  SER D N   1 
ATOM   2088 C CA  . SER B 2 77  ? 58.35900  23.27900 -20.77400 1.000 220.94020 ?  93  SER D CA  1 
ATOM   2089 C C   . SER B 2 77  ? 58.02900  24.72800 -20.44800 1.000 214.66700 ?  93  SER D C   1 
ATOM   2090 O O   . SER B 2 77  ? 57.44900  25.45300 -21.25600 1.000 209.47043 ?  93  SER D O   1 
ATOM   2091 C CB  . SER B 2 77  ? 58.68100  23.07900 -22.25000 1.000 221.74834 ?  93  SER D CB  1 
ATOM   2092 O OG  . SER B 2 77  ? 57.53300  23.27100 -23.05200 1.000 216.61418 ?  93  SER D OG  1 
ATOM   2093 N N   . LEU B 2 78  ? 58.41700  25.14500 -19.24700 1.000 215.57748 ?  94  LEU D N   1 
ATOM   2094 C CA  . LEU B 2 78  ? 58.16300  26.50300 -18.78900 1.000 210.27329 ?  94  LEU D CA  1 
ATOM   2095 C C   . LEU B 2 78  ? 58.82100  27.50300 -19.72100 1.000 208.19294 ?  94  LEU D C   1 
ATOM   2096 O O   . LEU B 2 78  ? 60.04700  27.54400 -19.83300 1.000 212.28912 ?  94  LEU D O   1 
ATOM   2097 C CB  . LEU B 2 78  ? 58.67200  26.67600 -17.35900 1.000 213.01682 ?  94  LEU D CB  1 
ATOM   2098 C CG  . LEU B 2 78  ? 58.47800  28.05100 -16.72400 1.000 208.30312 ?  94  LEU D CG  1 
ATOM   2099 C CD1 . LEU B 2 78  ? 57.01200  28.42300 -16.74700 1.000 202.01262 ?  94  LEU D CD1 1 
ATOM   2100 C CD2 . LEU B 2 78  ? 59.00400  28.04800 -15.29700 1.000 212.09867 ?  94  LEU D CD2 1 
ATOM   2101 N N   . GLN B 2 79  ? 58.01200  28.28700 -20.40000 1.000 202.22969 ?  95  GLN D N   1 
ATOM   2102 C CA  . GLN B 2 79  ? 58.55300  29.30600 -21.27800 1.000 200.10977 ?  95  GLN D CA  1 
ATOM   2103 C C   . GLN B 2 79  ? 58.42900  30.66900 -20.62300 1.000 195.80860 ?  95  GLN D C   1 
ATOM   2104 O O   . GLN B 2 79  ? 57.57900  30.87600 -19.75200 1.000 192.99496 ?  95  GLN D O   1 
ATOM   2105 C CB  . GLN B 2 79  ? 57.81600  29.29700 -22.62400 1.000 196.98455 ?  95  GLN D CB  1 
ATOM   2106 C CG  . GLN B 2 79  ? 57.92800  27.98600 -23.39100 1.000 201.27773 ?  95  GLN D CG  1 
ATOM   2107 C CD  . GLN B 2 79  ? 59.36200  27.49300 -23.52200 1.000 207.69752 ?  95  GLN D CD  1 
ATOM   2108 O OE1 . GLN B 2 79  ? 59.75600  26.51500 -22.88400 1.000 212.69895 ?  95  GLN D OE1 1 
ATOM   2109 N NE2 . GLN B 2 79  ? 60.15000  28.17300 -24.35000 1.000 207.89405 ?  95  GLN D NE2 1 
ATOM   2110 N N   . PRO B 2 80  ? 59.29100  31.61700 -20.99600 1.000 200.97485 ?  96  PRO D N   1 
ATOM   2111 C CA  . PRO B 2 80  ? 59.33300  32.89900 -20.27100 1.000 196.11597 ?  96  PRO D CA  1 
ATOM   2112 C C   . PRO B 2 80  ? 58.03200  33.68900 -20.30400 1.000 190.91143 ?  96  PRO D C   1 
ATOM   2113 O O   . PRO B 2 80  ? 57.76000  34.45000 -19.36600 1.000 189.43453 ?  96  PRO D O   1 
ATOM   2114 C CB  . PRO B 2 80  ? 60.47300  33.65500 -20.97700 1.000 193.61135 ?  96  PRO D CB  1 
ATOM   2115 C CG  . PRO B 2 80  ? 60.59600  32.99200 -22.31000 1.000 195.24776 ?  96  PRO D CG  1 
ATOM   2116 C CD  . PRO B 2 80  ? 60.32600  31.55300 -22.04200 1.000 198.96210 ?  96  PRO D CD  1 
ATOM   2117 N N   . GLU B 2 81  ? 57.21800  33.53700 -21.35300 1.000 196.58509 ?  97  GLU D N   1 
ATOM   2118 C CA  . GLU B 2 81  ? 55.96700  34.28900 -21.44400 1.000 189.64187 ?  97  GLU D CA  1 
ATOM   2119 C C   . GLU B 2 81  ? 55.04600  34.04700 -20.25600 1.000 194.22940 ?  97  GLU D C   1 
ATOM   2120 O O   . GLU B 2 81  ? 54.25800  34.92800 -19.89500 1.000 188.86218 ?  97  GLU D O   1 
ATOM   2121 C CB  . GLU B 2 81  ? 55.22000  33.94500 -22.73100 1.000 184.63153 ?  97  GLU D CB  1 
ATOM   2122 C CG  . GLU B 2 81  ? 56.08000  33.75700 -23.96100 1.000 182.68815 ?  97  GLU D CG  1 
ATOM   2123 C CD  . GLU B 2 81  ? 55.31600  33.09300 -25.09800 1.000 180.04512 ?  97  GLU D CD  1 
ATOM   2124 O OE1 . GLU B 2 81  ? 54.84800  31.94900 -24.91200 1.000 185.22374 ?  97  GLU D OE1 1 
ATOM   2125 O OE2 . GLU B 2 81  ? 55.18300  33.71600 -26.17500 1.000 175.79165 ?  97  GLU D OE2 1 
ATOM   2126 N N   . ASP B 2 82  ? 55.15000  32.88500 -19.61600 1.000 187.47517 ?  98  ASP D N   1 
ATOM   2127 C CA  . ASP B 2 82  ? 54.16400  32.47100 -18.62700 1.000 188.16860 ?  98  ASP D CA  1 
ATOM   2128 C C   . ASP B 2 82  ? 54.46200  33.01100 -17.23700 1.000 189.06047 ?  98  ASP D C   1 
ATOM   2129 O O   . ASP B 2 82  ? 54.17200  32.34800 -16.23700 1.000 187.24248 ?  98  ASP D O   1 
ATOM   2130 C CB  . ASP B 2 82  ? 54.08400  30.94600 -18.57600 1.000 189.30720 ?  98  ASP D CB  1 
ATOM   2131 C CG  . ASP B 2 82  ? 53.99600  30.32900 -19.94800 1.000 189.67183 ?  98  ASP D CG  1 
ATOM   2132 O OD1 . ASP B 2 82  ? 53.40100  30.96200 -20.84600 1.000 183.99801 ?  98  ASP D OD1 1 
ATOM   2133 O OD2 . ASP B 2 82  ? 54.52000  29.21100 -20.12800 1.000 192.98540 ?  98  ASP D OD2 1 
ATOM   2134 N N   . PHE B 2 83  ? 55.01500  34.21600 -17.15900 1.000 201.46061 ?  99  PHE D N   1 
ATOM   2135 C CA  . PHE B 2 83  ? 55.22200  34.87800 -15.87800 1.000 199.28842 ?  99  PHE D CA  1 
ATOM   2136 C C   . PHE B 2 83  ? 53.93800  35.61700 -15.52600 1.000 196.07981 ?  99  PHE D C   1 
ATOM   2137 O O   . PHE B 2 83  ? 53.48200  36.47200 -16.29200 1.000 190.01807 ?  99  PHE D O   1 
ATOM   2138 C CB  . PHE B 2 83  ? 56.38600  35.86500 -15.92000 1.000 195.78744 ?  99  PHE D CB  1 
ATOM   2139 C CG  . PHE B 2 83  ? 56.16900  37.05200 -15.03400 1.000 191.56733 ?  99  PHE D CG  1 
ATOM   2140 C CD1 . PHE B 2 83  ? 56.31700  36.94100 -13.66500 1.000 193.20412 ?  99  PHE D CD1 1 
ATOM   2141 C CD2 . PHE B 2 83  ? 55.75900  38.26400 -15.56200 1.000 184.56041 ?  99  PHE D CD2 1 
ATOM   2142 C CE1 . PHE B 2 83  ? 56.08900  38.02400 -12.83600 1.000 189.86830 ?  99  PHE D CE1 1 
ATOM   2143 C CE2 . PHE B 2 83  ? 55.52800  39.34800 -14.74000 1.000 180.89571 ?  99  PHE D CE2 1 
ATOM   2144 C CZ  . PHE B 2 83  ? 55.69500  39.23000 -13.37500 1.000 184.22929 ?  99  PHE D CZ  1 
ATOM   2145 N N   . ALA B 2 84  ? 53.34700  35.26800 -14.39000 1.000 189.53666 ?  100 ALA D N   1 
ATOM   2146 C CA  . ALA B 2 84  ? 52.04600  35.79800 -13.99000 1.000 184.23142 ?  100 ALA D CA  1 
ATOM   2147 C C   . ALA B 2 84  ? 51.76200  35.35100 -12.56000 1.000 183.58293 ?  100 ALA D C   1 
ATOM   2148 O O   . ALA B 2 84  ? 52.63800  34.81900 -11.86900 1.000 186.47403 ?  100 ALA D O   1 
ATOM   2149 C CB  . ALA B 2 84  ? 50.94600  35.34100 -14.94700 1.000 178.73370 ?  100 ALA D CB  1 
ATOM   2150 N N   . THR B 2 85  ? 50.54700  35.62100 -12.09800 1.000 185.67230 ?  101 THR D N   1 
ATOM   2151 C CA  . THR B 2 85  ? 50.00700  35.02200 -10.88900 1.000 183.98417 ?  101 THR D CA  1 
ATOM   2152 C C   . THR B 2 85  ? 48.86100  34.11300 -11.31300 1.000 179.39580 ?  101 THR D C   1 
ATOM   2153 O O   . THR B 2 85  ? 47.96800  34.54400 -12.04600 1.000 175.15466 ?  101 THR D O   1 
ATOM   2154 C CB  . THR B 2 85  ? 49.53000  36.09900 -9.91200  1.000 183.00282 ?  101 THR D CB  1 
ATOM   2155 O OG1 . THR B 2 85  ? 50.43400  37.20900 -9.95900  1.000 186.43823 ?  101 THR D OG1 1 
ATOM   2156 C CG2 . THR B 2 85  ? 49.48800  35.56100 -8.49500  1.000 184.16231 ?  101 THR D CG2 1 
ATOM   2157 N N   . TYR B 2 86  ? 48.87500  32.86400 -10.86900 1.000 178.99203 ?  102 TYR D N   1 
ATOM   2158 C CA  . TYR B 2 86  ? 47.91200  31.89100 -11.36600 1.000 175.62535 ?  102 TYR D CA  1 
ATOM   2159 C C   . TYR B 2 86  ? 46.88300  31.60200 -10.28500 1.000 173.87372 ?  102 TYR D C   1 
ATOM   2160 O O   . TYR B 2 86  ? 47.24000  31.37600 -9.12400  1.000 176.79562 ?  102 TYR D O   1 
ATOM   2161 C CB  . TYR B 2 86  ? 48.60400  30.60100 -11.81700 1.000 178.27003 ?  102 TYR D CB  1 
ATOM   2162 C CG  . TYR B 2 86  ? 49.33700  30.70200 -13.14700 1.000 180.33078 ?  102 TYR D CG  1 
ATOM   2163 C CD1 . TYR B 2 86  ? 49.76000  31.92200 -13.65200 1.000 181.58009 ?  102 TYR D CD1 1 
ATOM   2164 C CD2 . TYR B 2 86  ? 49.58900  29.56800 -13.90100 1.000 181.61803 ?  102 TYR D CD2 1 
ATOM   2165 C CE1 . TYR B 2 86  ? 50.42400  32.00200 -14.86500 1.000 184.37081 ?  102 TYR D CE1 1 
ATOM   2166 C CE2 . TYR B 2 86  ? 50.24700  29.64200 -15.11200 1.000 184.35813 ?  102 TYR D CE2 1 
ATOM   2167 C CZ  . TYR B 2 86  ? 50.66300  30.86200 -15.59000 1.000 185.86913 ?  102 TYR D CZ  1 
ATOM   2168 O OH  . TYR B 2 86  ? 51.32100  30.94800 -16.79500 1.000 189.21004 ?  102 TYR D OH  1 
ATOM   2169 N N   . TYR B 2 87  ? 45.61100  31.59000 -10.67500 1.000 179.57662 ?  103 TYR D N   1 
ATOM   2170 C CA  . TYR B 2 87  ? 44.51400  31.42400 -9.73400  1.000 177.58283 ?  103 TYR D CA  1 
ATOM   2171 C C   . TYR B 2 87  ? 43.64800  30.23900 -10.13500 1.000 175.62048 ?  103 TYR D C   1 
ATOM   2172 O O   . TYR B 2 87  ? 43.54600  29.89900 -11.31400 1.000 174.28572 ?  103 TYR D O   1 
ATOM   2173 C CB  . TYR B 2 87  ? 43.64500  32.68500 -9.66000  1.000 174.29463 ?  103 TYR D CB  1 
ATOM   2174 C CG  . TYR B 2 87  ? 44.32600  33.90500 -9.07100  1.000 176.44340 ?  103 TYR D CG  1 
ATOM   2175 C CD1 . TYR B 2 87  ? 45.33500  34.56800 -9.76300  1.000 178.15156 ?  103 TYR D CD1 1 
ATOM   2176 C CD2 . TYR B 2 87  ? 43.94100  34.40800 -7.83700  1.000 177.38605 ?  103 TYR D CD2 1 
ATOM   2177 C CE1 . TYR B 2 87  ? 45.94700  35.68800 -9.23300  1.000 180.65195 ?  103 TYR D CE1 1 
ATOM   2178 C CE2 . TYR B 2 87  ? 44.54400  35.52500 -7.30100  1.000 179.88218 ?  103 TYR D CE2 1 
ATOM   2179 C CZ  . TYR B 2 87  ? 45.54500  36.16200 -8.00000  1.000 181.43340 ?  103 TYR D CZ  1 
ATOM   2180 O OH  . TYR B 2 87  ? 46.14000  37.27700 -7.45400  1.000 184.41005 ?  103 TYR D OH  1 
ATOM   2181 N N   . CYS B 2 88  ? 43.02500  29.60600 -9.14700  1.000 172.70273 ?  104 CYS D N   1 
ATOM   2182 C CA  . CYS B 2 88  ? 42.10100  28.50900 -9.39800  1.000 173.84447 ?  104 CYS D CA  1 
ATOM   2183 C C   . CYS B 2 88  ? 40.71500  28.91600 -8.93000  1.000 170.88134 ?  104 CYS D C   1 
ATOM   2184 O O   . CYS B 2 88  ? 40.55500  29.49000 -7.85300  1.000 170.91753 ?  104 CYS D O   1 
ATOM   2185 C CB  . CYS B 2 88  ? 42.49900  27.21100 -8.68200  1.000 180.19107 ?  104 CYS D CB  1 
ATOM   2186 S SG  . CYS B 2 88  ? 43.66900  27.35700 -7.31800  1.000 184.98885 ?  104 CYS D SG  1 
ATOM   2187 N N   . GLN B 2 89  ? 39.71500  28.58000 -9.71900  1.000 169.78524 ?  105 GLN D N   1 
ATOM   2188 C CA  . GLN B 2 89  ? 38.34400  28.97200 -9.45000  1.000 167.67294 ?  105 GLN D CA  1 
ATOM   2189 C C   . GLN B 2 89  ? 37.64300  27.71600 -8.97200  1.000 169.52645 ?  105 GLN D C   1 
ATOM   2190 O O   . GLN B 2 89  ? 37.42500  26.78200 -9.75200  1.000 170.76254 ?  105 GLN D O   1 
ATOM   2191 C CB  . GLN B 2 89  ? 37.67500  29.55600 -10.69400 1.000 164.17678 ?  105 GLN D CB  1 
ATOM   2192 C CG  . GLN B 2 89  ? 36.35500  30.28100 -10.43900 1.000 162.02219 ?  105 GLN D CG  1 
ATOM   2193 C CD  . GLN B 2 89  ? 35.20500  29.69600 -11.23400 1.000 160.90434 ?  105 GLN D CD  1 
ATOM   2194 O OE1 . GLN B 2 89  ? 35.22300  28.52200 -11.60000 1.000 162.25059 ?  105 GLN D OE1 1 
ATOM   2195 N NE2 . GLN B 2 89  ? 34.20700  30.52100 -11.52400 1.000 158.71949 ?  105 GLN D NE2 1 
ATOM   2196 N N   . GLN B 2 90  ? 37.30700  27.70400 -7.68000  1.000 176.21606 ?  106 GLN D N   1 
ATOM   2197 C CA  . GLN B 2 90  ? 36.64000  26.56400 -7.07000  1.000 178.18203 ?  106 GLN D CA  1 
ATOM   2198 C C   . GLN B 2 90  ? 35.19400  26.47700 -7.51400  1.000 176.48147 ?  106 GLN D C   1 
ATOM   2199 O O   . GLN B 2 90  ? 34.59300  25.39900 -7.42800  1.000 177.79006 ?  106 GLN D O   1 
ATOM   2200 C CB  . GLN B 2 90  ? 36.72300  26.65100 -5.54500  1.000 181.78644 ?  106 GLN D CB  1 
ATOM   2201 N N   . ARG B 2 91  ? 34.63500  27.59600 -7.97400  1.000 167.73092 ?  107 ARG D N   1 
ATOM   2202 C CA  . ARG B 2 91  ? 33.27300  27.65200 -8.47700  1.000 165.10789 ?  107 ARG D CA  1 
ATOM   2203 C C   . ARG B 2 91  ? 32.26100  27.28400 -7.39900  1.000 167.56401 ?  107 ARG D C   1 
ATOM   2204 O O   . ARG B 2 91  ? 32.55600  27.34500 -6.20100  1.000 170.38022 ?  107 ARG D O   1 
ATOM   2205 C CB  . ARG B 2 91  ? 33.11600  26.74700 -9.70300  1.000 165.59730 ?  107 ARG D CB  1 
ATOM   2206 N N   . GLY B 2 92  ? 31.06200  26.91100 -7.83000  1.000 166.79843 ?  108 GLY D N   1 
ATOM   2207 C CA  . GLY B 2 92  ? 29.92300  26.67400 -6.96600  1.000 169.27242 ?  108 GLY D CA  1 
ATOM   2208 C C   . GLY B 2 92  ? 28.74800  27.48000 -7.47200  1.000 167.30586 ?  108 GLY D C   1 
ATOM   2209 O O   . GLY B 2 92  ? 28.85800  28.69100 -7.68100  1.000 164.75757 ?  108 GLY D O   1 
ATOM   2210 N N   . TRP B 2 93  ? 27.61600  26.80400 -7.67200  1.000 164.80165 ?  109 TRP D N   1 
ATOM   2211 C CA  . TRP B 2 93  ? 26.39600  27.46100 -8.12700  1.000 163.13232 ?  109 TRP D CA  1 
ATOM   2212 C C   . TRP B 2 93  ? 26.05500  28.67100 -7.27400  1.000 162.61173 ?  109 TRP D C   1 
ATOM   2213 O O   . TRP B 2 93  ? 25.83100  29.77400 -7.78600  1.000 159.93968 ?  109 TRP D O   1 
ATOM   2214 C CB  . TRP B 2 93  ? 25.25800  26.44400 -8.10900  1.000 166.00446 ?  109 TRP D CB  1 
ATOM   2215 C CG  . TRP B 2 93  ? 24.03500  26.81300 -8.86900  1.000 164.86891 ?  109 TRP D CG  1 
ATOM   2216 C CD1 . TRP B 2 93  ? 22.75000  26.70900 -8.43100  1.000 165.69346 ?  109 TRP D CD1 1 
ATOM   2217 C CD2 . TRP B 2 93  ? 23.96300  27.33400 -10.20400 1.000 161.92151 ?  109 TRP D CD2 1 
ATOM   2218 N NE1 . TRP B 2 93  ? 21.88100  27.12800 -9.40400  1.000 163.09606 ?  109 TRP D NE1 1 
ATOM   2219 C CE2 . TRP B 2 93  ? 22.60200  27.51900 -10.50100 1.000 160.95533 ?  109 TRP D CE2 1 
ATOM   2220 C CE3 . TRP B 2 93  ? 24.91500  27.66000 -11.17700 1.000 159.79965 ?  109 TRP D CE3 1 
ATOM   2221 C CZ2 . TRP B 2 93  ? 22.16900  28.01000 -11.72300 1.000 158.43153 ?  109 TRP D CZ2 1 
ATOM   2222 C CZ3 . TRP B 2 93  ? 24.47700  28.15700 -12.39000 1.000 157.60000 ?  109 TRP D CZ3 1 
ATOM   2223 C CH2 . TRP B 2 93  ? 23.11800  28.32800 -12.65100 1.000 157.05286 ?  109 TRP D CH2 1 
ATOM   2224 N N   . TYR B 2 94  ? 26.03500  28.48200 -5.96000  1.000 166.47342 ?  114 TYR D N   1 
ATOM   2225 C CA  . TYR B 2 94  ? 25.65600  29.53300 -5.03100  1.000 166.85775 ?  114 TYR D CA  1 
ATOM   2226 C C   . TYR B 2 94  ? 26.80600  29.86200 -4.09000  1.000 167.87266 ?  114 TYR D C   1 
ATOM   2227 O O   . TYR B 2 94  ? 26.59800  30.54000 -3.07500  1.000 169.62771 ?  114 TYR D O   1 
ATOM   2228 C CB  . TYR B 2 94  ? 24.40600  29.06100 -4.28200  1.000 170.15598 ?  114 TYR D CB  1 
ATOM   2229 C CG  . TYR B 2 94  ? 23.13900  29.27600 -5.08500  1.000 168.93270 ?  114 TYR D CG  1 
ATOM   2230 C CD1 . TYR B 2 94  ? 23.20200  29.72600 -6.39600  1.000 165.52433 ?  114 TYR D CD1 1 
ATOM   2231 C CD2 . TYR B 2 94  ? 21.90700  28.88100 -4.59700  1.000 171.42065 ?  114 TYR D CD2 1 
ATOM   2232 C CE1 . TYR B 2 94  ? 22.07000  29.89000 -7.15300  1.000 164.60635 ?  114 TYR D CE1 1 
ATOM   2233 C CE2 . TYR B 2 94  ? 20.76000  29.03800 -5.34500  1.000 170.25921 ?  114 TYR D CE2 1 
ATOM   2234 C CZ  . TYR B 2 94  ? 20.84800  29.53800 -6.62900  1.000 166.67806 ?  114 TYR D CZ  1 
ATOM   2235 O OH  . TYR B 2 94  ? 19.71100  29.68800 -7.39200  1.000 164.93673 ?  114 TYR D OH  1 
ATOM   2236 N N   . LEU B 2 95  ? 28.00400  29.36500 -4.39500  1.000 171.93793 ?  115 LEU D N   1 
ATOM   2237 C CA  . LEU B 2 95  ? 29.17400  29.52500 -3.53800  1.000 173.57049 ?  115 LEU D CA  1 
ATOM   2238 C C   . LEU B 2 95  ? 30.45600  29.65700 -4.36900  1.000 170.94086 ?  115 LEU D C   1 
ATOM   2239 O O   . LEU B 2 95  ? 31.45000  28.97200 -4.12300  1.000 172.54691 ?  115 LEU D O   1 
ATOM   2240 C CB  . LEU B 2 95  ? 29.25700  28.36700 -2.54500  1.000 177.93617 ?  115 LEU D CB  1 
ATOM   2241 C CG  . LEU B 2 95  ? 28.66500  28.70000 -1.16900  1.000 181.73126 ?  115 LEU D CG  1 
ATOM   2242 C CD1 . LEU B 2 95  ? 28.60800  27.47800 -0.27000  1.000 186.16187 ?  115 LEU D CD1 1 
ATOM   2243 C CD2 . LEU B 2 95  ? 29.43000  29.83300 -0.48600  1.000 182.55203 ?  115 LEU D CD2 1 
ATOM   2244 N N   . PHE B 2 96  ? 30.44700  30.51300 -5.39500  1.000 163.72575 ?  116 PHE D N   1 
ATOM   2245 C CA  . PHE B 2 96  ? 31.67500  30.79000 -6.14400  1.000 161.46208 ?  116 PHE D CA  1 
ATOM   2246 C C   . PHE B 2 96  ? 32.75600  31.35400 -5.21800  1.000 163.43090 ?  116 PHE D C   1 
ATOM   2247 O O   . PHE B 2 96  ? 32.50700  32.30000 -4.46600  1.000 164.15240 ?  116 PHE D O   1 
ATOM   2248 C CB  . PHE B 2 96  ? 31.39600  31.77300 -7.29100  1.000 157.12626 ?  116 PHE D CB  1 
ATOM   2249 C CG  . PHE B 2 96  ? 30.71900  31.16100 -8.50200  1.000 155.76722 ?  116 PHE D CG  1 
ATOM   2250 C CD1 . PHE B 2 96  ? 31.43500  30.34700 -9.36500  1.000 155.60359 ?  116 PHE D CD1 1 
ATOM   2251 C CD2 . PHE B 2 96  ? 29.40100  31.45600 -8.81600  1.000 155.11737 ?  116 PHE D CD2 1 
ATOM   2252 C CE1 . PHE B 2 96  ? 30.84600  29.79600 -10.48300 1.000 155.07900 ?  116 PHE D CE1 1 
ATOM   2253 C CE2 . PHE B 2 96  ? 28.80900  30.90900 -9.94500  1.000 154.77276 ?  116 PHE D CE2 1 
ATOM   2254 C CZ  . PHE B 2 96  ? 29.53800  30.08200 -10.77700 1.000 154.80695 ?  116 PHE D CZ  1 
ATOM   2255 N N   . THR B 2 97  ? 33.96500  30.77700 -5.28900  1.000 167.89217 ?  117 THR D N   1 
ATOM   2256 C CA  . THR B 2 97  ? 35.10800  31.19400 -4.47000  1.000 170.43964 ?  117 THR D CA  1 
ATOM   2257 C C   . THR B 2 97  ? 36.41800  31.04500 -5.24100  1.000 169.68568 ?  117 THR D C   1 
ATOM   2258 O O   . THR B 2 97  ? 36.71800  29.96300 -5.76100  1.000 169.87433 ?  117 THR D O   1 
ATOM   2259 C CB  . THR B 2 97  ? 35.19400  30.37700 -3.17000  1.000 175.18426 ?  117 THR D CB  1 
ATOM   2260 O OG1 . THR B 2 97  ? 35.15600  28.97900 -3.47800  1.000 176.10151 ?  117 THR D OG1 1 
ATOM   2261 C CG2 . THR B 2 97  ? 34.07100  30.73500 -2.18800  1.000 177.20770 ?  117 THR D CG2 1 
ATOM   2262 N N   . PHE B 2 98  ? 37.19700  32.12700 -5.28800  1.000 166.29003 ?  118 PHE D N   1 
ATOM   2263 C CA  . PHE B 2 98  ? 38.47100  32.18100 -6.00400  1.000 166.13065 ?  118 PHE D CA  1 
ATOM   2264 C C   . PHE B 2 98  ? 39.62300  31.54400 -5.22800  1.000 170.62282 ?  118 PHE D C   1 
ATOM   2265 O O   . PHE B 2 98  ? 39.60800  31.47000 -3.99600  1.000 174.78744 ?  118 PHE D O   1 
ATOM   2266 C CB  . PHE B 2 98  ? 38.83800  33.62900 -6.31700  1.000 164.54278 ?  118 PHE D CB  1 
ATOM   2267 C CG  . PHE B 2 98  ? 38.11700  34.19400 -7.50000  1.000 159.63732 ?  118 PHE D CG  1 
ATOM   2268 C CD1 . PHE B 2 98  ? 38.43800  33.79100 -8.78600  1.000 157.71185 ?  118 PHE D CD1 1 
ATOM   2269 C CD2 . PHE B 2 98  ? 37.10900  35.12700 -7.32100  1.000 157.34804 ?  118 PHE D CD2 1 
ATOM   2270 C CE1 . PHE B 2 98  ? 37.77200  34.32200 -9.87500  1.000 153.69132 ?  118 PHE D CE1 1 
ATOM   2271 C CE2 . PHE B 2 98  ? 36.43800  35.65500 -8.39800  1.000 152.97064 ?  118 PHE D CE2 1 
ATOM   2272 C CZ  . PHE B 2 98  ? 36.76800  35.25800 -9.67900  1.000 151.20091 ?  118 PHE D CZ  1 
ATOM   2273 N N   . GLY B 2 99  ? 40.64000  31.07200 -5.98100  1.000 172.59894 ?  119 GLY D N   1 
ATOM   2274 C CA  . GLY B 2 99  ? 41.82500  30.47000 -5.39700  1.000 176.62737 ?  119 GLY D CA  1 
ATOM   2275 C C   . GLY B 2 99  ? 42.80400  31.49200 -4.82700  1.000 179.40744 ?  119 GLY D C   1 
ATOM   2276 O O   . GLY B 2 99  ? 42.72100  32.69000 -5.08700  1.000 178.10582 ?  119 GLY D O   1 
ATOM   2277 N N   . GLN B 2 100 ? 43.74900  30.98600 -4.02800  1.000 190.94886 ?  120 GLN D N   1 
ATOM   2278 C CA  . GLN B 2 100 ? 44.68800  31.86000 -3.32400  1.000 194.59250 ?  120 GLN D CA  1 
ATOM   2279 C C   . GLN B 2 100 ? 45.55600  32.67400 -4.27900  1.000 194.21014 ?  120 GLN D C   1 
ATOM   2280 O O   . GLN B 2 100 ? 45.80100  33.86200 -4.04200  1.000 195.44144 ?  120 GLN D O   1 
ATOM   2281 C CB  . GLN B 2 100 ? 45.56700  31.03200 -2.38600  1.000 198.76151 ?  120 GLN D CB  1 
ATOM   2282 N N   . GLY B 2 101 ? 46.03000  32.06200 -5.35900  1.000 194.25333 ?  121 GLY D N   1 
ATOM   2283 C CA  . GLY B 2 101 ? 46.92800  32.75500 -6.26600  1.000 194.84131 ?  121 GLY D CA  1 
ATOM   2284 C C   . GLY B 2 101 ? 48.36100  32.29900 -6.07800  1.000 199.02064 ?  121 GLY D C   1 
ATOM   2285 O O   . GLY B 2 101 ? 48.80100  32.06500 -4.94700  1.000 201.90737 ?  121 GLY D O   1 
ATOM   2286 N N   . THR B 2 102 ? 49.09900  32.16500 -7.17700  1.000 195.77853 ?  122 THR D N   1 
ATOM   2287 C CA  . THR B 2 102 ? 50.47000  31.66900 -7.14600  1.000 199.45955 ?  122 THR D CA  1 
ATOM   2288 C C   . THR B 2 102 ? 51.35500  32.56900 -7.99300  1.000 201.24793 ?  122 THR D C   1 
ATOM   2289 O O   . THR B 2 102 ? 51.17400  32.65100 -9.21200  1.000 200.19356 ?  122 THR D O   1 
ATOM   2290 C CB  . THR B 2 102 ? 50.53900  30.22300 -7.64000  1.000 199.23972 ?  122 THR D CB  1 
ATOM   2291 O OG1 . THR B 2 102 ? 49.95800  29.36400 -6.65300  1.000 198.67902 ?  122 THR D OG1 1 
ATOM   2292 C CG2 . THR B 2 102 ? 51.98700  29.81200 -7.89000  1.000 202.89212 ?  122 THR D CG2 1 
ATOM   2293 N N   . LYS B 2 103 ? 52.31900  33.22200 -7.35500  1.000 200.51759 ?  123 LYS D N   1 
ATOM   2294 C CA  . LYS B 2 103 ? 53.26300  34.05500 -8.08500  1.000 199.05055 ?  123 LYS D CA  1 
ATOM   2295 C C   . LYS B 2 103 ? 54.21300  33.18500 -8.89600  1.000 201.28976 ?  123 LYS D C   1 
ATOM   2296 O O   . LYS B 2 103 ? 54.83700  32.26200 -8.36300  1.000 205.65107 ?  123 LYS D O   1 
ATOM   2297 C CB  . LYS B 2 103 ? 54.05100  34.94000 -7.11800  1.000 199.43672 ?  123 LYS D CB  1 
ATOM   2298 N N   . VAL B 2 104 ? 54.34800  33.49900 -10.18000 1.000 200.31472 ?  124 VAL D N   1 
ATOM   2299 C CA  . VAL B 2 104 ? 55.21300  32.74200 -11.08100 1.000 202.57635 ?  124 VAL D CA  1 
ATOM   2300 C C   . VAL B 2 104 ? 56.47900  33.57600 -11.23400 1.000 202.57189 ?  124 VAL D C   1 
ATOM   2301 O O   . VAL B 2 104 ? 56.58900  34.43800 -12.10600 1.000 201.64114 ?  124 VAL D O   1 
ATOM   2302 C CB  . VAL B 2 104 ? 54.53900  32.45900 -12.42300 1.000 202.96750 ?  124 VAL D CB  1 
ATOM   2303 C CG1 . VAL B 2 104 ? 55.46400  31.64700 -13.32000 1.000 205.81881 ?  124 VAL D CG1 1 
ATOM   2304 C CG2 . VAL B 2 104 ? 53.21700  31.73600 -12.21300 1.000 202.28417 ?  124 VAL D CG2 1 
ATOM   2305 N N   . GLU B 2 105 ? 57.44900  33.30200 -10.36900 1.000 209.32189 ?  125 GLU D N   1 
ATOM   2306 C CA  . GLU B 2 105 ? 58.75900  33.92500 -10.43000 1.000 209.39102 ?  125 GLU D CA  1 
ATOM   2307 C C   . GLU B 2 105 ? 59.64900  33.15800 -11.40400 1.000 211.21387 ?  125 GLU D C   1 
ATOM   2308 O O   . GLU B 2 105 ? 59.39100  31.99700 -11.73700 1.000 212.95798 ?  125 GLU D O   1 
ATOM   2309 C CB  . GLU B 2 105 ? 59.38500  33.94700 -9.02800  1.000 210.19660 ?  125 GLU D CB  1 
ATOM   2310 C CG  . GLU B 2 105 ? 60.78400  34.54300 -8.91300  1.000 210.37379 ?  125 GLU D CG  1 
ATOM   2311 C CD  . GLU B 2 105 ? 60.76500  36.04400 -8.71100  1.000 208.01922 ?  125 GLU D CD  1 
ATOM   2312 O OE1 . GLU B 2 105 ? 60.36900  36.49200 -7.61500  1.000 207.92977 ?  125 GLU D OE1 1 
ATOM   2313 O OE2 . GLU B 2 105 ? 61.15100  36.77300 -9.65100  1.000 206.40247 ?  125 GLU D OE2 1 
ATOM   2314 N N   . ILE B 2 106 ? 60.69800  33.82300 -11.89000 1.000 211.38268 ?  126 ILE D N   1 
ATOM   2315 C CA  . ILE B 2 106 ? 61.65300  33.14700 -12.81500 1.000 212.91528 ?  126 ILE D CA  1 
ATOM   2316 C C   . ILE B 2 106 ? 63.06200  33.68700 -12.56100 1.000 212.19003 ?  126 ILE D C   1 
ATOM   2317 O O   . ILE B 2 106 ? 63.27900  34.88800 -12.80900 1.000 209.63115 ?  126 ILE D O   1 
ATOM   2318 C CB  . ILE B 2 106 ? 61.22200  33.35200 -14.28000 1.000 212.42382 ?  126 ILE D CB  1 
ATOM   2319 N N   . LYS B 2 107 ? 63.98000  32.83700 -12.08500 1.000 214.61594 ?  127 LYS D N   1 
ATOM   2320 C CA  . LYS B 2 107 ? 65.39100  33.27100 -11.90000 1.000 216.80827 ?  127 LYS D CA  1 
ATOM   2321 C C   . LYS B 2 107 ? 66.01200  33.47500 -13.28500 1.000 215.56615 ?  127 LYS D C   1 
ATOM   2322 O O   . LYS B 2 107 ? 65.75700  32.63300 -14.16700 1.000 215.53708 ?  127 LYS D O   1 
ATOM   2323 C CB  . LYS B 2 107 ? 66.16800  32.23700 -11.08100 1.000 221.86642 ?  127 LYS D CB  1 
ATOM   2324 N N   . ARG B 2 108 ? 66.78900  34.54600 -13.47100 1.000 214.97519 ?  128 ARG D N   1 
ATOM   2325 C CA  . ARG B 2 108 ? 67.33900  34.85500 -14.82000 1.000 213.84306 ?  128 ARG D CA  1 
ATOM   2326 C C   . ARG B 2 108 ? 68.76800  34.31500 -14.93100 1.000 217.55213 ?  128 ARG D C   1 
ATOM   2327 O O   . ARG B 2 108 ? 69.38100  34.04000 -13.88100 1.000 220.72500 ?  128 ARG D O   1 
ATOM   2328 C CB  . ARG B 2 108 ? 67.32800  36.36600 -15.06400 1.000 211.26342 ?  128 ARG D CB  1 
ATOM   2329 N N   . THR B 2 109 ? 69.27200  34.18000 -16.16200 1.000 217.37092 ?  129 THR D N   1 
ATOM   2330 C CA  . THR B 2 109 ? 70.66000  33.70900 -16.37500 1.000 220.73878 ?  129 THR D CA  1 
ATOM   2331 C C   . THR B 2 109 ? 71.61700  34.55000 -15.52500 1.000 222.58289 ?  129 THR D C   1 
ATOM   2332 O O   . THR B 2 109 ? 72.02100  35.61800 -16.02000 1.000 221.49584 ?  129 THR D O   1 
ATOM   2333 C CB  . THR B 2 109 ? 71.04700  33.78800 -17.86400 1.000 219.92938 ?  129 THR D CB  1 
ATOM   2334 O OG1 . THR B 2 109 ? 70.92700  35.13900 -18.32100 1.000 217.39516 ?  129 THR D OG1 1 
ATOM   2335 C CG2 . THR B 2 109 ? 70.03600  33.03700 -18.71900 1.000 218.45670 ?  129 THR D CG2 1 
ATOM   2336 N N   . ALA B 2 112 ? 73.31900  43.37700 -16.88200 1.000 226.77703 ?  132 ALA D N   1 
ATOM   2337 C CA  . ALA B 2 112 ? 73.89300  44.60200 -16.33700 1.000 228.82820 ?  132 ALA D CA  1 
ATOM   2338 C C   . ALA B 2 112 ? 72.84600  45.51900 -15.70100 1.000 226.90252 ?  132 ALA D C   1 
ATOM   2339 O O   . ALA B 2 112 ? 71.74600  45.67200 -16.22900 1.000 223.39008 ?  132 ALA D O   1 
ATOM   2340 C CB  . ALA B 2 112 ? 74.65100  45.34300 -17.42700 1.000 229.77103 ?  132 ALA D CB  1 
ATOM   2341 N N   . PRO B 2 113 ? 73.19700  46.12800 -14.56300 1.000 228.04852 ?  133 PRO D N   1 
ATOM   2342 C CA  . PRO B 2 113 ? 72.23500  47.01200 -13.88300 1.000 226.42285 ?  133 PRO D CA  1 
ATOM   2343 C C   . PRO B 2 113 ? 71.92300  48.29100 -14.64500 1.000 224.96335 ?  133 PRO D C   1 
ATOM   2344 O O   . PRO B 2 113 ? 70.78500  48.76900 -14.56500 1.000 221.77743 ?  133 PRO D O   1 
ATOM   2345 C CB  . PRO B 2 113 ? 72.91800  47.30500 -12.54000 1.000 230.91638 ?  133 PRO D CB  1 
ATOM   2346 C CG  . PRO B 2 113 ? 74.37800  47.11200 -12.81500 1.000 235.04597 ?  133 PRO D CG  1 
ATOM   2347 C CD  . PRO B 2 113 ? 74.45800  45.99300 -13.81400 1.000 233.06229 ?  133 PRO D CD  1 
ATOM   2348 N N   . SER B 2 114 ? 72.89300  48.86500 -15.35700 1.000 228.58973 ?  134 SER D N   1 
ATOM   2349 C CA  . SER B 2 114 ? 72.72000  50.04000 -16.22100 1.000 227.91271 ?  134 SER D CA  1 
ATOM   2350 C C   . SER B 2 114 ? 71.92200  51.15400 -15.52900 1.000 227.15557 ?  134 SER D C   1 
ATOM   2351 O O   . SER B 2 114 ? 70.78800  51.46800 -15.88600 1.000 223.35141 ?  134 SER D O   1 
ATOM   2352 C CB  . SER B 2 114 ? 72.06200  49.64500 -17.54900 1.000 224.16912 ?  134 SER D CB  1 
ATOM   2353 O OG  . SER B 2 114 ? 71.13600  48.58500 -17.38500 1.000 220.77855 ?  134 SER D OG  1 
ATOM   2354 N N   . VAL B 2 115 ? 72.56700  51.75100 -14.52400 1.000 228.86386 ?  135 VAL D N   1 
ATOM   2355 C CA  . VAL B 2 115 ? 71.94700  52.74400 -13.64800 1.000 230.00463 ?  135 VAL D CA  1 
ATOM   2356 C C   . VAL B 2 115 ? 71.92700  54.10800 -14.33400 1.000 229.00591 ?  135 VAL D C   1 
ATOM   2357 O O   . VAL B 2 115 ? 72.80500  54.43300 -15.13900 1.000 231.09924 ?  135 VAL D O   1 
ATOM   2358 C CB  . VAL B 2 115 ? 72.69400  52.78200 -12.29600 1.000 235.10149 ?  135 VAL D CB  1 
ATOM   2359 C CG1 . VAL B 2 115 ? 72.41300  54.07000 -11.52600 1.000 237.54670 ?  135 VAL D CG1 1 
ATOM   2360 C CG2 . VAL B 2 115 ? 72.32300  51.56800 -11.45900 1.000 236.05344 ?  135 VAL D CG2 1 
ATOM   2361 N N   . PHE B 2 116 ? 70.90800  54.91800 -14.02400 1.000 235.89239 ?  136 PHE D N   1 
ATOM   2362 C CA  . PHE B 2 116 ? 70.81000  56.28100 -14.54400 1.000 235.22758 ?  136 PHE D CA  1 
ATOM   2363 C C   . PHE B 2 116 ? 70.32200  57.23200 -13.45500 1.000 237.99486 ?  136 PHE D C   1 
ATOM   2364 O O   . PHE B 2 116 ? 69.84000  56.81100 -12.40400 1.000 239.74348 ?  136 PHE D O   1 
ATOM   2365 C CB  . PHE B 2 116 ? 69.88400  56.35800 -15.76300 1.000 230.56147 ?  136 PHE D CB  1 
ATOM   2366 C CG  . PHE B 2 116 ? 70.48200  55.78300 -17.00900 1.000 229.58685 ?  136 PHE D CG  1 
ATOM   2367 C CD1 . PHE B 2 116 ? 71.41900  56.50100 -17.73100 1.000 231.47638 ?  136 PHE D CD1 1 
ATOM   2368 C CD2 . PHE B 2 116 ? 70.10000  54.53400 -17.46900 1.000 227.56229 ?  136 PHE D CD2 1 
ATOM   2369 C CE1 . PHE B 2 116 ? 71.97400  55.97800 -18.87900 1.000 231.08758 ?  136 PHE D CE1 1 
ATOM   2370 C CE2 . PHE B 2 116 ? 70.64900  54.00800 -18.62200 1.000 227.28728 ?  136 PHE D CE2 1 
ATOM   2371 C CZ  . PHE B 2 116 ? 71.58800  54.73400 -19.32800 1.000 228.90287 ?  136 PHE D CZ  1 
ATOM   2372 N N   . ILE B 2 117 ? 70.48500  58.53300 -13.70300 1.000 229.59128 ?  137 ILE D N   1 
ATOM   2373 C CA  . ILE B 2 117 ? 70.02000  59.58100 -12.79700 1.000 232.49319 ?  137 ILE D CA  1 
ATOM   2374 C C   . ILE B 2 117 ? 69.46700  60.74400 -13.61300 1.000 230.49494 ?  137 ILE D C   1 
ATOM   2375 O O   . ILE B 2 117 ? 70.02800  61.10700 -14.65200 1.000 230.26903 ?  137 ILE D O   1 
ATOM   2376 C CB  . ILE B 2 117 ? 71.14300  60.06500 -11.85700 1.000 238.76183 ?  137 ILE D CB  1 
ATOM   2377 N N   . PHE B 2 118 ? 68.35700  61.32100 -13.15100 1.000 231.55563 ?  138 PHE D N   1 
ATOM   2378 C CA  . PHE B 2 118 ? 67.76700  62.48500 -13.80700 1.000 230.08959 ?  138 PHE D CA  1 
ATOM   2379 C C   . PHE B 2 118 ? 67.47300  63.55900 -12.76400 1.000 234.24715 ?  138 PHE D C   1 
ATOM   2380 O O   . PHE B 2 118 ? 66.79100  63.28300 -11.75500 1.000 235.13378 ?  138 PHE D O   1 
ATOM   2381 C CB  . PHE B 2 118 ? 66.49800  62.11900 -14.59500 1.000 224.08842 ?  138 PHE D CB  1 
ATOM   2382 C CG  . PHE B 2 118 ? 66.76600  61.41600 -15.91100 1.000 220.45194 ?  138 PHE D CG  1 
ATOM   2383 C CD1 . PHE B 2 118 ? 67.33000  60.14700 -15.94600 1.000 220.13743 ?  138 PHE D CD1 1 
ATOM   2384 C CD2 . PHE B 2 118 ? 66.44200  62.02400 -17.11100 1.000 218.39613 ?  138 PHE D CD2 1 
ATOM   2385 C CE1 . PHE B 2 118 ? 67.57000  59.50500 -17.15200 1.000 217.87210 ?  138 PHE D CE1 1 
ATOM   2386 C CE2 . PHE B 2 118 ? 66.67100  61.38300 -18.31500 1.000 216.49350 ?  138 PHE D CE2 1 
ATOM   2387 C CZ  . PHE B 2 118 ? 67.23800  60.12600 -18.33800 1.000 216.29863 ?  138 PHE D CZ  1 
ATOM   2388 N N   . PRO B 2 119 ? 67.98200  64.77700 -12.94700 1.000 233.20555 ?  139 PRO D N   1 
ATOM   2389 C CA  . PRO B 2 119 ? 67.78600  65.84000 -11.95000 1.000 236.68056 ?  139 PRO D CA  1 
ATOM   2390 C C   . PRO B 2 119 ? 66.39300  66.44000 -12.02700 1.000 232.37573 ?  139 PRO D C   1 
ATOM   2391 O O   . PRO B 2 119 ? 65.67400  66.24000 -13.01800 1.000 227.52911 ?  139 PRO D O   1 
ATOM   2392 C CB  . PRO B 2 119 ? 68.85600  66.86600 -12.34000 1.000 243.54774 ?  139 PRO D CB  1 
ATOM   2393 C CG  . PRO B 2 119 ? 68.93300  66.73400 -13.83100 1.000 241.42200 ?  139 PRO D CG  1 
ATOM   2394 C CD  . PRO B 2 119 ? 68.65700  65.27800 -14.15900 1.000 235.74126 ?  139 PRO D CD  1 
ATOM   2395 N N   . PRO B 2 120 ? 65.97900  67.20000 -11.01000 1.000 234.28350 ?  140 PRO D N   1 
ATOM   2396 C CA  . PRO B 2 120 ? 64.68600  67.89000 -11.09200 1.000 230.61192 ?  140 PRO D CA  1 
ATOM   2397 C C   . PRO B 2 120 ? 64.65300  68.87100 -12.24900 1.000 231.66719 ?  140 PRO D C   1 
ATOM   2398 O O   . PRO B 2 120 ? 65.63200  69.56600 -12.52400 1.000 237.60954 ?  140 PRO D O   1 
ATOM   2399 C CB  . PRO B 2 120 ? 64.58100  68.61600 -9.74400  1.000 234.43136 ?  140 PRO D CB  1 
ATOM   2400 C CG  . PRO B 2 120 ? 65.97200  68.67300 -9.21200  1.000 241.65521 ?  140 PRO D CG  1 
ATOM   2401 C CD  . PRO B 2 120 ? 66.64800  67.44100 -9.71900  1.000 240.05990 ?  140 PRO D CD  1 
ATOM   2402 N N   . SER B 2 121 ? 63.51200  68.92400 -12.93200 1.000 226.18093 ?  141 SER D N   1 
ATOM   2403 C CA  . SER B 2 121 ? 63.36200  69.90400 -13.99200 1.000 227.34042 ?  141 SER D CA  1 
ATOM   2404 C C   . SER B 2 121 ? 63.23300  71.28700 -13.37000 1.000 231.74476 ?  141 SER D C   1 
ATOM   2405 O O   . SER B 2 121 ? 62.63900  71.45600 -12.30100 1.000 230.93851 ?  141 SER D O   1 
ATOM   2406 C CB  . SER B 2 121 ? 62.13900  69.59900 -14.85400 1.000 220.64831 ?  141 SER D CB  1 
ATOM   2407 O OG  . SER B 2 121 ? 60.94300  69.82800 -14.12900 1.000 217.03508 ?  141 SER D OG  1 
ATOM   2408 N N   . ASP B 2 122 ? 63.77400  72.28600 -14.07600 1.000 236.66911 ?  142 ASP D N   1 
ATOM   2409 C CA  . ASP B 2 122 ? 63.72000  73.67000 -13.61000 1.000 241.71965 ?  142 ASP D CA  1 
ATOM   2410 C C   . ASP B 2 122 ? 62.29200  74.11300 -13.34000 1.000 237.23797 ?  142 ASP D C   1 
ATOM   2411 O O   . ASP B 2 122 ? 62.06200  74.95800 -12.46800 1.000 240.18104 ?  142 ASP D O   1 
ATOM   2412 C CB  . ASP B 2 122 ? 64.38800  74.58400 -14.63800 1.000 247.07984 ?  142 ASP D CB  1 
ATOM   2413 C CG  . ASP B 2 122 ? 63.85200  74.37200 -16.04900 1.000 242.85407 ?  142 ASP D CG  1 
ATOM   2414 O OD1 . ASP B 2 122 ? 64.11400  73.28300 -16.61000 1.000 239.70590 ?  142 ASP D OD1 1 
ATOM   2415 O OD2 . ASP B 2 122 ? 63.17300  75.27000 -16.59600 1.000 242.93235 -1 142 ASP D OD2 1 
ATOM   2416 N N   . GLU B 2 123 ? 61.33900  73.52100 -14.05800 1.000 230.35147 ?  143 GLU D N   1 
ATOM   2417 C CA  . GLU B 2 123 ? 59.91600  73.84000 -13.78600 1.000 225.53927 ?  143 GLU D CA  1 
ATOM   2418 C C   . GLU B 2 123 ? 59.57900  73.34200 -12.38200 1.000 223.74811 ?  143 GLU D C   1 
ATOM   2419 O O   . GLU B 2 123 ? 59.09700  74.14100 -11.56400 1.000 225.19248 ?  143 GLU D O   1 
ATOM   2420 C CB  . GLU B 2 123 ? 59.02200  73.16900 -14.82500 1.000 218.81277 ?  143 GLU D CB  1 
ATOM   2421 C CG  . GLU B 2 123 ? 57.54300  73.30000 -14.51400 1.000 213.29861 ?  143 GLU D CG  1 
ATOM   2422 C CD  . GLU B 2 123 ? 56.63300  72.52800 -15.45300 1.000 206.78044 ?  143 GLU D CD  1 
ATOM   2423 O OE1 . GLU B 2 123 ? 57.13500  72.02100 -16.47500 1.000 206.92552 ?  143 GLU D OE1 1 
ATOM   2424 O OE2 . GLU B 2 123 ? 55.42600  72.43600 -15.15800 1.000 201.84477 ?  143 GLU D OE2 1 
ATOM   2425 N N   . GLN B 2 124 ? 59.84700  72.06300 -12.12400 1.000 221.09914 ?  144 GLN D N   1 
ATOM   2426 C CA  . GLN B 2 124 ? 59.53300  71.47200 -10.80200 1.000 219.56037 ?  144 GLN D CA  1 
ATOM   2427 C C   . GLN B 2 124 ? 60.28100  72.26500 -9.73700  1.000 226.72971 ?  144 GLN D C   1 
ATOM   2428 O O   . GLN B 2 124 ? 59.68000  72.61900 -8.71300  1.000 226.82060 ?  144 GLN D O   1 
ATOM   2429 C CB  . GLN B 2 124 ? 59.98300  70.01500 -10.79000 1.000 217.24364 ?  144 GLN D CB  1 
ATOM   2430 C CG  . GLN B 2 124 ? 59.28100  69.18100 -9.73400  1.000 214.84594 ?  144 GLN D CG  1 
ATOM   2431 C CD  . GLN B 2 124 ? 60.25900  68.68300 -8.70400  1.000 222.12840 ?  144 GLN D CD  1 
ATOM   2432 O OE1 . GLN B 2 124 ? 61.44200  68.50500 -8.98000  1.000 224.37093 ?  144 GLN D OE1 1 
ATOM   2433 N NE2 . GLN B 2 124 ? 59.76700  68.47000 -7.49600  1.000 224.31380 ?  144 GLN D NE2 1 
ATOM   2434 N N   . LEU B 2 125 ? 61.55900  72.52400 -9.99100  1.000 232.81414 ?  145 LEU D N   1 
ATOM   2435 C CA  . LEU B 2 125 ? 62.34500  73.34800 -9.04500  1.000 240.65001 ?  145 LEU D CA  1 
ATOM   2436 C C   . LEU B 2 125 ? 61.57600  74.64400 -8.79700  1.000 242.05530 ?  145 LEU D C   1 
ATOM   2437 O O   . LEU B 2 125 ? 61.25300  74.92500 -7.62700  1.000 243.66299 ?  145 LEU D O   1 
ATOM   2438 C CB  . LEU B 2 125 ? 63.70000  73.62900 -9.69200  1.000 246.76207 ?  145 LEU D CB  1 
ATOM   2439 C CG  . LEU B 2 125 ? 64.84500  72.76000 -9.18400  1.000 249.88382 ?  145 LEU D CG  1 
ATOM   2440 C CD1 . LEU B 2 125 ? 65.80500  72.42100 -10.31200 1.000 251.16571 ?  145 LEU D CD1 1 
ATOM   2441 C CD2 . LEU B 2 125 ? 65.57200  73.46100 -8.05000  1.000 257.98209 ?  145 LEU D CD2 1 
ATOM   2442 N N   . LYS B 2 126 ? 61.28200  75.38800 -9.86600  1.000 241.63978 ?  146 LYS D N   1 
ATOM   2443 C CA  . LYS B 2 126 ? 60.58000  76.69000 -9.71900  1.000 243.43161 ?  146 LYS D CA  1 
ATOM   2444 C C   . LYS B 2 126 ? 59.24600  76.46900 -9.00200  1.000 237.49464 ?  146 LYS D C   1 
ATOM   2445 O O   . LYS B 2 126 ? 58.86600  77.33100 -8.18800  1.000 240.23361 ?  146 LYS D O   1 
ATOM   2446 C CB  . LYS B 2 126 ? 60.35200  77.33900 -11.08600 1.000 242.95196 ?  146 LYS D CB  1 
ATOM   2447 N N   . SER B 2 127 ? 58.56800  75.35600 -9.29800  1.000 229.96838 ?  147 SER D N   1 
ATOM   2448 C CA  . SER B 2 127 ? 57.27400  75.05100 -8.63800  1.000 224.10531 ?  147 SER D CA  1 
ATOM   2449 C C   . SER B 2 127 ? 57.41100  75.26400 -7.12800  1.000 227.96728 ?  147 SER D C   1 
ATOM   2450 O O   . SER B 2 127 ? 56.50700  75.88000 -6.53600  1.000 226.98614 ?  147 SER D O   1 
ATOM   2451 C CB  . SER B 2 127 ? 56.81700  73.65600 -8.95100  1.000 217.11343 ?  147 SER D CB  1 
ATOM   2452 O OG  . SER B 2 127 ? 57.26700  72.74400 -7.95900  1.000 219.24527 ?  147 SER D OG  1 
ATOM   2453 N N   . GLY B 2 128 ? 58.49800  74.76800 -6.53400  1.000 232.40557 ?  148 GLY D N   1 
ATOM   2454 C CA  . GLY B 2 128 ? 58.72700  75.00100 -5.09700  1.000 237.24336 ?  148 GLY D CA  1 
ATOM   2455 C C   . GLY B 2 128 ? 59.42600  73.82600 -4.44200  1.000 238.09191 ?  148 GLY D C   1 
ATOM   2456 O O   . GLY B 2 128 ? 59.96100  74.00200 -3.33100  1.000 243.92622 ?  148 GLY D O   1 
ATOM   2457 N N   . THR B 2 129 ? 59.42000  72.66700 -5.10300  1.000 229.10395 ?  149 THR D N   1 
ATOM   2458 C CA  . THR B 2 129 ? 60.03400  71.45400 -4.50200  1.000 227.73151 ?  149 THR D CA  1 
ATOM   2459 C C   . THR B 2 129 ? 60.94000  70.79700 -5.54500  1.000 230.52492 ?  149 THR D C   1 
ATOM   2460 O O   . THR B 2 129 ? 60.64100  70.92000 -6.74000  1.000 232.16093 ?  149 THR D O   1 
ATOM   2461 C CB  . THR B 2 129 ? 58.95300  70.53600 -3.91500  1.000 223.12797 ?  149 THR D CB  1 
ATOM   2462 O OG1 . THR B 2 129 ? 59.00200  70.68300 -2.49500  1.000 221.00481 ?  149 THR D OG1 1 
ATOM   2463 C CG2 . THR B 2 129 ? 59.12100  69.07800 -4.28000  1.000 221.18840 ?  149 THR D CG2 1 
ATOM   2464 N N   . ALA B 2 130 ? 62.02400  70.16300 -5.09900  1.000 227.31965 ?  150 ALA D N   1 
ATOM   2465 C CA  . ALA B 2 130 ? 62.96400  69.53600 -6.01700  1.000 231.07813 ?  150 ALA D CA  1 
ATOM   2466 C C   . ALA B 2 130 ? 62.90500  68.02200 -5.86200  1.000 229.49443 ?  150 ALA D C   1 
ATOM   2467 O O   . ALA B 2 130 ? 62.93700  67.50000 -4.73900  1.000 227.51004 ?  150 ALA D O   1 
ATOM   2468 C CB  . ALA B 2 130 ? 64.38800  70.05000 -5.78600  1.000 235.27894 ?  150 ALA D CB  1 
ATOM   2469 N N   . SER B 2 131 ? 62.83700  67.32200 -6.99600  1.000 225.68403 ?  151 SER D N   1 
ATOM   2470 C CA  . SER B 2 131 ? 62.76100  65.86600 -7.02700  1.000 224.85193 ?  151 SER D CA  1 
ATOM   2471 C C   . SER B 2 131 ? 63.86900  65.32200 -7.91900  1.000 227.12619 ?  151 SER D C   1 
ATOM   2472 O O   . SER B 2 131 ? 63.90600  65.61200 -9.11700  1.000 226.31542 ?  151 SER D O   1 
ATOM   2473 C CB  . SER B 2 131 ? 61.38900  65.40200 -7.52800  1.000 221.62477 ?  151 SER D CB  1 
ATOM   2474 O OG  . SER B 2 131 ? 60.34300  66.03900 -6.81300  1.000 217.72259 ?  151 SER D OG  1 
ATOM   2475 N N   . VAL B 2 132 ? 64.75600  64.52400 -7.32800  1.000 221.39982 ?  152 VAL D N   1 
ATOM   2476 C CA  . VAL B 2 132 ? 65.86100  63.85300 -8.00600  1.000 221.84930 ?  152 VAL D CA  1 
ATOM   2477 C C   . VAL B 2 132 ? 65.47200  62.39400 -8.20800  1.000 220.10199 ?  152 VAL D C   1 
ATOM   2478 O O   . VAL B 2 132 ? 64.86000  61.79100 -7.32200  1.000 221.24108 ?  152 VAL D O   1 
ATOM   2479 C CB  . VAL B 2 132 ? 67.14500  63.97400 -7.16200  1.000 225.60964 ?  152 VAL D CB  1 
ATOM   2480 C CG1 . VAL B 2 132 ? 68.34100  63.38200 -7.88400  1.000 225.57004 ?  152 VAL D CG1 1 
ATOM   2481 C CG2 . VAL B 2 132 ? 67.39000  65.42600 -6.76000  1.000 228.35574 ?  152 VAL D CG2 1 
ATOM   2482 N N   . VAL B 2 133 ? 65.76300  61.82000 -9.37800  1.000 228.86607 ?  153 VAL D N   1 
ATOM   2483 C CA  . VAL B 2 133 ? 65.35400  60.43500 -9.58800  1.000 227.01902 ?  153 VAL D CA  1 
ATOM   2484 C C   . VAL B 2 133 ? 66.56600  59.59700 -9.98200  1.000 225.63053 ?  153 VAL D C   1 
ATOM   2485 O O   . VAL B 2 133 ? 67.50300  60.08200 -10.62800 1.000 223.89806 ?  153 VAL D O   1 
ATOM   2486 C CB  . VAL B 2 133 ? 64.21600  60.30600 -10.62800 1.000 221.95818 ?  153 VAL D CB  1 
ATOM   2487 C CG1 . VAL B 2 133 ? 64.75500  60.40000 -12.03200 1.000 216.07495 ?  153 VAL D CG1 1 
ATOM   2488 C CG2 . VAL B 2 133 ? 63.44500  59.00600 -10.41500 1.000 222.10045 ?  153 VAL D CG2 1 
ATOM   2489 N N   . CYS B 2 134 ? 66.51900  58.31400 -9.60900  1.000 226.24310 ?  154 CYS D N   1 
ATOM   2490 C CA  . CYS B 2 134 ? 67.59200  57.35800 -9.86700  1.000 225.57074 ?  154 CYS D CA  1 
ATOM   2491 C C   . CYS B 2 134 ? 66.97400  56.06000 -10.37700 1.000 222.93023 ?  154 CYS D C   1 
ATOM   2492 O O   . CYS B 2 134 ? 66.10500  55.47600 -9.72100  1.000 225.63677 ?  154 CYS D O   1 
ATOM   2493 C CB  . CYS B 2 134 ? 68.42300  57.12100 -8.59600  1.000 231.92781 ?  154 CYS D CB  1 
ATOM   2494 S SG  . CYS B 2 134 ? 70.09700  56.44800 -8.84600  1.000 232.21112 ?  154 CYS D SG  1 
ATOM   2495 N N   . LEU B 2 135 ? 67.43200  55.62900 -11.55400 1.000 228.73558 ?  155 LEU D N   1 
ATOM   2496 C CA  . LEU B 2 135 ? 66.89800  54.51800 -12.33800 1.000 225.56739 ?  155 LEU D CA  1 
ATOM   2497 C C   . LEU B 2 135 ? 67.78700  53.28300 -12.26900 1.000 227.88003 ?  155 LEU D C   1 
ATOM   2498 O O   . LEU B 2 135 ? 69.00900  53.38700 -12.41000 1.000 228.79808 ?  155 LEU D O   1 
ATOM   2499 C CB  . LEU B 2 135 ? 66.77700  54.93300 -13.80700 1.000 219.55159 ?  155 LEU D CB  1 
ATOM   2500 C CG  . LEU B 2 135 ? 66.59600  53.79400 -14.82100 1.000 216.99920 ?  155 LEU D CG  1 
ATOM   2501 C CD1 . LEU B 2 135 ? 65.26600  53.07600 -14.63700 1.000 216.71081 ?  155 LEU D CD1 1 
ATOM   2502 C CD2 . LEU B 2 135 ? 66.78100  54.27400 -16.26300 1.000 213.48563 ?  155 LEU D CD2 1 
ATOM   2503 N N   . LEU B 2 136 ? 67.16800  52.11100 -12.09000 1.000 215.82706 ?  156 LEU D N   1 
ATOM   2504 C CA  . LEU B 2 136 ? 67.86600  50.82100 -12.12800 1.000 218.39132 ?  156 LEU D CA  1 
ATOM   2505 C C   . LEU B 2 136 ? 67.11900  49.87300 -13.06600 1.000 215.78363 ?  156 LEU D C   1 
ATOM   2506 O O   . LEU B 2 136 ? 66.09700  49.30600 -12.68500 1.000 216.83951 ?  156 LEU D O   1 
ATOM   2507 C CB  . LEU B 2 136 ? 67.98700  50.22500 -10.73100 1.000 224.18507 ?  156 LEU D CB  1 
ATOM   2508 N N   . ASN B 2 137 ? 67.67100  49.68000 -14.26800 1.000 217.11515 ?  157 ASN D N   1 
ATOM   2509 C CA  . ASN B 2 137 ? 66.93400  48.89900 -15.29500 1.000 215.21118 ?  157 ASN D CA  1 
ATOM   2510 C C   . ASN B 2 137 ? 67.49300  47.49600 -15.52400 1.000 219.00797 ?  157 ASN D C   1 
ATOM   2511 O O   . ASN B 2 137 ? 68.70800  47.30800 -15.40000 1.000 221.65318 ?  157 ASN D O   1 
ATOM   2512 C CB  . ASN B 2 137 ? 66.93300  49.63100 -16.63800 1.000 210.21251 ?  157 ASN D CB  1 
ATOM   2513 C CG  . ASN B 2 137 ? 65.65500  49.43800 -17.42500 1.000 207.11490 ?  157 ASN D CG  1 
ATOM   2514 O OD1 . ASN B 2 137 ? 65.07700  48.35300 -17.42900 1.000 209.84569 ?  157 ASN D OD1 1 
ATOM   2515 N ND2 . ASN B 2 137 ? 65.20600  50.48400 -18.09800 1.000 201.90940 ?  157 ASN D ND2 1 
ATOM   2516 N N   . ASN B 2 138 ? 66.61800  46.55500 -15.85600 1.000 213.02381 ?  158 ASN D N   1 
ATOM   2517 C CA  . ASN B 2 138 ? 66.99200  45.18700 -16.21200 1.000 216.73376 ?  158 ASN D CA  1 
ATOM   2518 C C   . ASN B 2 138 ? 67.91300  44.56200 -15.16000 1.000 221.26169 ?  158 ASN D C   1 
ATOM   2519 O O   . ASN B 2 138 ? 69.05400  44.18600 -15.42800 1.000 223.74617 ?  158 ASN D O   1 
ATOM   2520 C CB  . ASN B 2 138 ? 67.60600  45.14300 -17.61200 1.000 216.04366 ?  158 ASN D CB  1 
ATOM   2521 C CG  . ASN B 2 138 ? 66.78400  45.91900 -18.62200 1.000 211.22414 ?  158 ASN D CG  1 
ATOM   2522 O OD1 . ASN B 2 138 ? 67.20800  46.96400 -19.11400 1.000 208.08596 ?  158 ASN D OD1 1 
ATOM   2523 N ND2 . ASN B 2 138 ? 65.58200  45.42600 -18.91000 1.000 210.70305 ?  158 ASN D ND2 1 
ATOM   2524 N N   . PHE B 2 139 ? 67.37600  44.44400 -13.94300 1.000 214.56951 ?  159 PHE D N   1 
ATOM   2525 C CA  . PHE B 2 139 ? 68.11600  43.90000 -12.81500 1.000 218.76003 ?  159 PHE D CA  1 
ATOM   2526 C C   . PHE B 2 139 ? 67.27500  42.89300 -12.04300 1.000 220.83740 ?  159 PHE D C   1 
ATOM   2527 O O   . PHE B 2 139 ? 66.04400  42.95600 -12.03500 1.000 219.29440 ?  159 PHE D O   1 
ATOM   2528 C CB  . PHE B 2 139 ? 68.57400  45.00800 -11.86400 1.000 219.16705 ?  159 PHE D CB  1 
ATOM   2529 N N   . TYR B 2 140 ? 67.96600  41.95200 -11.40600 1.000 211.09218 ?  160 TYR D N   1 
ATOM   2530 C CA  . TYR B 2 140 ? 67.38900  40.95900 -10.51100 1.000 212.76576 ?  160 TYR D CA  1 
ATOM   2531 C C   . TYR B 2 140 ? 68.46000  40.57800 -9.50400  1.000 216.79297 ?  160 TYR D C   1 
ATOM   2532 O O   . TYR B 2 140 ? 69.65100  40.66800 -9.82500  1.000 218.57551 ?  160 TYR D O   1 
ATOM   2533 C CB  . TYR B 2 140 ? 66.91000  39.71900 -11.28000 1.000 212.45846 ?  160 TYR D CB  1 
ATOM   2534 N N   . PRO B 2 141 ? 68.09000  40.14900 -8.28400  1.000 211.83463 ?  161 PRO D N   1 
ATOM   2535 C CA  . PRO B 2 141 ? 66.77500  40.00300 -7.64800  1.000 209.69774 ?  161 PRO D CA  1 
ATOM   2536 C C   . PRO B 2 141 ? 66.29900  41.22500 -6.86200  1.000 209.16561 ?  161 PRO D C   1 
ATOM   2537 O O   . PRO B 2 141 ? 66.78500  42.34100 -7.02000  1.000 209.58020 ?  161 PRO D O   1 
ATOM   2538 C CB  . PRO B 2 141 ? 67.00400  38.81200 -6.71900  1.000 211.97314 ?  161 PRO D CB  1 
ATOM   2539 C CG  . PRO B 2 141 ? 68.41600  39.03100 -6.22700  1.000 216.61240 ?  161 PRO D CG  1 
ATOM   2540 C CD  . PRO B 2 141 ? 69.15200  39.78800 -7.32700  1.000 216.22912 ?  161 PRO D CD  1 
ATOM   2541 N N   . ARG B 2 142 ? 65.29600  41.00200 -6.01400  1.000 219.89438 ?  162 ARG D N   1 
ATOM   2542 C CA  . ARG B 2 142 ? 64.75400  42.03400 -5.13800  1.000 219.99637 ?  162 ARG D CA  1 
ATOM   2543 C C   . ARG B 2 142 ? 65.64500  42.15400 -3.89600  1.000 225.79768 ?  162 ARG D C   1 
ATOM   2544 O O   . ARG B 2 142 ? 66.75800  41.62200 -3.85300  1.000 229.46212 ?  162 ARG D O   1 
ATOM   2545 C CB  . ARG B 2 142 ? 63.30100  41.72000 -4.79400  1.000 212.08818 ?  162 ARG D CB  1 
ATOM   2546 N N   . GLU B 2 143 ? 65.15500  42.84900 -2.86400  1.000 230.58541 ?  163 GLU D N   1 
ATOM   2547 C CA  . GLU B 2 143 ? 65.90800  43.14700 -1.63900  1.000 237.11755 ?  163 GLU D CA  1 
ATOM   2548 C C   . GLU B 2 143 ? 67.19500  43.91200 -1.97200  1.000 243.53979 ?  163 GLU D C   1 
ATOM   2549 O O   . GLU B 2 143 ? 68.31500  43.41000 -1.87000  1.000 246.20606 ?  163 GLU D O   1 
ATOM   2550 C CB  . GLU B 2 143 ? 66.20300  41.87000 -0.84100  1.000 237.59676 ?  163 GLU D CB  1 
ATOM   2551 N N   . ALA B 2 144 ? 66.98100  45.16400 -2.37600  1.000 254.42290 ?  164 ALA D N   1 
ATOM   2552 C CA  . ALA B 2 144 ? 68.02800  46.05600 -2.87000  1.000 254.65123 ?  164 ALA D CA  1 
ATOM   2553 C C   . ALA B 2 144 ? 67.87300  47.43700 -2.23200  1.000 258.04593 ?  164 ALA D C   1 
ATOM   2554 O O   . ALA B 2 144 ? 67.60900  48.42100 -2.92100  1.000 254.90292 ?  164 ALA D O   1 
ATOM   2555 C CB  . ALA B 2 144 ? 67.99600  46.15300 -4.39400  1.000 248.08802 ?  164 ALA D CB  1 
ATOM   2556 N N   . LYS B 2 145 ? 68.01700  47.51100 -0.90500  1.000 260.81071 ?  165 LYS D N   1 
ATOM   2557 C CA  . LYS B 2 145 ? 67.79700  48.76300 -0.18700  1.000 263.47407 ?  165 LYS D CA  1 
ATOM   2558 C C   . LYS B 2 145 ? 68.63100  49.88400 -0.79300  1.000 260.54801 ?  165 LYS D C   1 
ATOM   2559 O O   . LYS B 2 145 ? 69.86000  49.91000 -0.67000  1.000 260.90060 ?  165 LYS D O   1 
ATOM   2560 C CB  . LYS B 2 145 ? 68.13000  48.59900 1.29800   1.000 266.14195 ?  165 LYS D CB  1 
ATOM   2561 N N   . VAL B 2 146 ? 67.94400  50.82300 -1.43400  1.000 259.81639 ?  166 VAL D N   1 
ATOM   2562 C CA  . VAL B 2 146 ? 68.57700  51.91300 -2.16300  1.000 255.69171 ?  166 VAL D CA  1 
ATOM   2563 C C   . VAL B 2 146 ? 69.07100  52.96600 -1.18500  1.000 257.82531 ?  166 VAL D C   1 
ATOM   2564 O O   . VAL B 2 146 ? 68.38600  53.30800 -0.21300  1.000 257.92171 ?  166 VAL D O   1 
ATOM   2565 C CB  . VAL B 2 146 ? 67.58400  52.51900 -3.17300  1.000 250.77811 ?  166 VAL D CB  1 
ATOM   2566 C CG1 . VAL B 2 146 ? 68.31600  53.34000 -4.22200  1.000 245.35938 ?  166 VAL D CG1 1 
ATOM   2567 C CG2 . VAL B 2 146 ? 66.73700  51.42800 -3.81100  1.000 248.78780 ?  166 VAL D CG2 1 
ATOM   2568 N N   . SER B 2 147 ? 70.26600  53.48700 -1.44300  1.000 257.28559 ?  167 SER D N   1 
ATOM   2569 C CA  . SER B 2 147 ? 70.92200  54.44100 -0.57200  1.000 259.06079 ?  167 SER D CA  1 
ATOM   2570 C C   . SER B 2 147 ? 71.08400  55.73200 -1.35400  1.000 255.02287 ?  167 SER D C   1 
ATOM   2571 O O   . SER B 2 147 ? 71.37500  55.71100 -2.55100  1.000 251.36116 ?  167 SER D O   1 
ATOM   2572 C CB  . SER B 2 147 ? 72.29300  53.92300 -0.12900  1.000 262.35217 ?  167 SER D CB  1 
ATOM   2573 O OG  . SER B 2 147 ? 72.18900  52.62800 0.43800   1.000 265.84348 ?  167 SER D OG  1 
ATOM   2574 N N   . TRP B 2 148 ? 70.85300  56.85100 -0.69200  1.000 251.14177 ?  168 TRP D N   1 
ATOM   2575 C CA  . TRP B 2 148 ? 70.98100  58.16000 -1.30900  1.000 247.90368 ?  168 TRP D CA  1 
ATOM   2576 C C   . TRP B 2 148 ? 71.99200  58.96600 -0.50500  1.000 249.74942 ?  168 TRP D C   1 
ATOM   2577 O O   . TRP B 2 148 ? 72.10300  58.79900 0.71400   1.000 251.78077 ?  168 TRP D O   1 
ATOM   2578 C CB  . TRP B 2 148 ? 69.62100  58.85900 -1.36100  1.000 243.74741 ?  168 TRP D CB  1 
ATOM   2579 C CG  . TRP B 2 148 ? 68.69600  58.42700 -2.47400  1.000 241.25048 ?  168 TRP D CG  1 
ATOM   2580 C CD1 . TRP B 2 148 ? 67.80900  57.39800 -2.42400  1.000 241.40163 ?  168 TRP D CD1 1 
ATOM   2581 C CD2 . TRP B 2 148 ? 68.45900  59.09100 -3.72900  1.000 237.54428 ?  168 TRP D CD2 1 
ATOM   2582 N NE1 . TRP B 2 148 ? 67.08500  57.33000 -3.58700  1.000 238.39699 ?  168 TRP D NE1 1 
ATOM   2583 C CE2 . TRP B 2 148 ? 67.46100  58.36200 -4.40300  1.000 235.56223 ?  168 TRP D CE2 1 
ATOM   2584 C CE3 . TRP B 2 148 ? 69.01600  60.20700 -4.36000  1.000 235.57501 ?  168 TRP D CE3 1 
ATOM   2585 C CZ2 . TRP B 2 148 ? 67.00800  58.71200 -5.67400  1.000 231.05671 ?  168 TRP D CZ2 1 
ATOM   2586 C CZ3 . TRP B 2 148 ? 68.56100  60.55300 -5.62600  1.000 231.34926 ?  168 TRP D CZ3 1 
ATOM   2587 C CH2 . TRP B 2 148 ? 67.56800  59.80800 -6.26500  1.000 228.83227 ?  168 TRP D CH2 1 
ATOM   2588 N N   . TYR B 2 149 ? 72.74400  59.82600 -1.18500  1.000 249.31018 ?  169 TYR D N   1 
ATOM   2589 C CA  . TYR B 2 149 ? 73.79300  60.61700 -0.54400  1.000 253.41890 ?  169 TYR D CA  1 
ATOM   2590 C C   . TYR B 2 149 ? 73.74300  62.03600 -1.10000  1.000 252.47939 ?  169 TYR D C   1 
ATOM   2591 O O   . TYR B 2 149 ? 74.21300  62.28900 -2.21100  1.000 251.95860 ?  169 TYR D O   1 
ATOM   2592 C CB  . TYR B 2 149 ? 75.16800  60.00600 -0.77300  1.000 256.92239 ?  169 TYR D CB  1 
ATOM   2593 C CG  . TYR B 2 149 ? 75.41500  58.69800 -0.06600  1.000 259.06984 ?  169 TYR D CG  1 
ATOM   2594 C CD1 . TYR B 2 149 ? 74.99200  57.49900 -0.62300  1.000 256.68974 ?  169 TYR D CD1 1 
ATOM   2595 C CD2 . TYR B 2 149 ? 76.09100  58.65800 1.14400   1.000 263.54393 ?  169 TYR D CD2 1 
ATOM   2596 C CE1 . TYR B 2 149 ? 75.22000  56.29700 0.01000   1.000 258.94753 ?  169 TYR D CE1 1 
ATOM   2597 C CE2 . TYR B 2 149 ? 76.32600  57.46100 1.78500   1.000 265.81146 ?  169 TYR D CE2 1 
ATOM   2598 C CZ  . TYR B 2 149 ? 75.88700  56.28200 1.21200   1.000 263.62046 ?  169 TYR D CZ  1 
ATOM   2599 O OH  . TYR B 2 149 ? 76.11500  55.08200 1.84500   1.000 266.37844 ?  169 TYR D OH  1 
ATOM   2600 N N   . VAL B 2 150 ? 73.20400  62.96500 -0.32200  1.000 250.58274 ?  170 VAL D N   1 
ATOM   2601 C CA  . VAL B 2 150 ? 73.25600  64.37500 -0.68000  1.000 250.52737 ?  170 VAL D CA  1 
ATOM   2602 C C   . VAL B 2 150 ? 74.54700  64.92400 -0.09000  1.000 255.35121 ?  170 VAL D C   1 
ATOM   2603 O O   . VAL B 2 150 ? 74.66300  65.09000 1.12700   1.000 257.02084 ?  170 VAL D O   1 
ATOM   2604 C CB  . VAL B 2 150 ? 72.02900  65.14100 -0.18100  1.000 246.92232 ?  170 VAL D CB  1 
ATOM   2605 C CG1 . VAL B 2 150 ? 72.19200  66.61900 -0.47500  1.000 247.63644 ?  170 VAL D CG1 1 
ATOM   2606 C CG2 . VAL B 2 150 ? 70.78300  64.61300 -0.85100  1.000 242.32871 ?  170 VAL D CG2 1 
ATOM   2607 N N   . ASP B 2 151 ? 75.51300  65.21100 -0.96400  1.000 252.53273 ?  171 ASP D N   1 
ATOM   2608 C CA  . ASP B 2 151 ? 76.88900  65.52300 -0.57300  1.000 255.94069 ?  171 ASP D CA  1 
ATOM   2609 C C   . ASP B 2 151 ? 77.48900  64.40500 0.27900   1.000 261.05670 ?  171 ASP D C   1 
ATOM   2610 O O   . ASP B 2 151 ? 78.07000  64.64200 1.33900   1.000 265.35488 ?  171 ASP D O   1 
ATOM   2611 C CB  . ASP B 2 151 ? 76.95000  66.86100 0.16100   1.000 256.92464 ?  171 ASP D CB  1 
ATOM   2612 C CG  . ASP B 2 151 ? 76.75600  68.02600 -0.76500  1.000 253.95900 ?  171 ASP D CG  1 
ATOM   2613 O OD1 . ASP B 2 151 ? 76.68100  67.79400 -1.99100  1.000 251.77425 ?  171 ASP D OD1 1 
ATOM   2614 O OD2 . ASP B 2 151 ? 76.66900  69.16900 -0.27200  1.000 257.09581 -1 171 ASP D OD2 1 
ATOM   2615 N N   . ASN B 2 152 ? 77.33200  63.17100 -0.20500  1.000 251.37587 ?  172 ASN D N   1 
ATOM   2616 C CA  . ASN B 2 152 ? 77.82500  61.96400 0.46800   1.000 256.24377 ?  172 ASN D CA  1 
ATOM   2617 C C   . ASN B 2 152 ? 77.32800  61.88000 1.91000   1.000 260.92200 ?  172 ASN D C   1 
ATOM   2618 O O   . ASN B 2 152 ? 78.07500  61.55600 2.83700   1.000 266.19588 ?  172 ASN D O   1 
ATOM   2619 C CB  . ASN B 2 152 ? 79.35000  61.86400 0.39600   1.000 258.58210 ?  172 ASN D CB  1 
ATOM   2620 C CG  . ASN B 2 152 ? 79.86900  61.82200 -1.03300  1.000 254.18347 ?  172 ASN D CG  1 
ATOM   2621 O OD1 . ASN B 2 152 ? 79.61900  62.72700 -1.83100  1.000 249.96641 ?  172 ASN D OD1 1 
ATOM   2622 N ND2 . ASN B 2 152 ? 80.58500  60.75500 -1.36500  1.000 255.30152 ?  172 ASN D ND2 1 
ATOM   2623 N N   . ALA B 2 153 ? 76.03700  62.14900 2.09100   1.000 253.15334 ?  173 ALA D N   1 
ATOM   2624 C CA  . ALA B 2 153 ? 75.35800  62.03600 3.37800   1.000 256.75644 ?  173 ALA D CA  1 
ATOM   2625 C C   . ALA B 2 153 ? 74.14700  61.14000 3.17600   1.000 255.48549 ?  173 ALA D C   1 
ATOM   2626 O O   . ALA B 2 153 ? 73.25900  61.47200 2.38400   1.000 249.93812 ?  173 ALA D O   1 
ATOM   2627 C CB  . ALA B 2 153 ? 74.94500  63.40800 3.91500   1.000 254.87922 ?  173 ALA D CB  1 
ATOM   2628 N N   . LEU B 2 154 ? 74.10900  60.01700 3.89400   1.000 250.33126 ?  174 LEU D N   1 
ATOM   2629 C CA  . LEU B 2 154 ? 73.07800  59.00800 3.67500   1.000 248.83640 ?  174 LEU D CA  1 
ATOM   2630 C C   . LEU B 2 154 ? 71.67400  59.59500 3.75300   1.000 244.55432 ?  174 LEU D C   1 
ATOM   2631 O O   . LEU B 2 154 ? 71.33100  60.30700 4.70100   1.000 244.86483 ?  174 LEU D O   1 
ATOM   2632 C CB  . LEU B 2 154 ? 73.23300  57.89500 4.71400   1.000 254.58585 ?  174 LEU D CB  1 
ATOM   2633 C CG  . LEU B 2 154 ? 73.93600  56.60900 4.28200   1.000 257.00072 ?  174 LEU D CG  1 
ATOM   2634 C CD1 . LEU B 2 154 ? 74.16700  55.70600 5.48200   1.000 264.61630 ?  174 LEU D CD1 1 
ATOM   2635 C CD2 . LEU B 2 154 ? 73.11700  55.89200 3.22700   1.000 253.03312 ?  174 LEU D CD2 1 
ATOM   2636 N N   . GLN B 2 155 ? 70.86600  59.29600 2.73600   1.000 253.14034 ?  175 GLN D N   1 
ATOM   2637 C CA  . GLN B 2 155 ? 69.49700  59.78700 2.64400   1.000 246.83621 ?  175 GLN D CA  1 
ATOM   2638 C C   . GLN B 2 155 ? 68.54800  58.59900 2.59200   1.000 246.29448 ?  175 GLN D C   1 
ATOM   2639 O O   . GLN B 2 155 ? 68.65000  57.75200 1.69800   1.000 246.74683 ?  175 GLN D O   1 
ATOM   2640 C CB  . GLN B 2 155 ? 69.30500  60.68100 1.41800   1.000 240.38630 ?  175 GLN D CB  1 
ATOM   2641 C CG  . GLN B 2 155 ? 70.04000  62.01000 1.45000   1.000 239.81249 ?  175 GLN D CG  1 
ATOM   2642 C CD  . GLN B 2 155 ? 69.84200  62.77200 2.74800   1.000 240.95223 ?  175 GLN D CD  1 
ATOM   2643 O OE1 . GLN B 2 155 ? 68.71500  62.94200 3.21500   1.000 237.66255 ?  175 GLN D OE1 1 
ATOM   2644 N NE2 . GLN B 2 155 ? 70.93700  63.25300 3.32500   1.000 245.02611 ?  175 GLN D NE2 1 
ATOM   2645 N N   . SER B 2 156 ? 67.62700  58.55200 3.54500   1.000 246.96682 ?  176 SER D N   1 
ATOM   2646 C CA  . SER B 2 156 ? 66.55100  57.58100 3.64000   1.000 244.14852 ?  176 SER D CA  1 
ATOM   2647 C C   . SER B 2 156 ? 65.25000  58.35800 3.79100   1.000 235.49114 ?  176 SER D C   1 
ATOM   2648 O O   . SER B 2 156 ? 65.25400  59.58700 3.86400   1.000 233.15752 ?  176 SER D O   1 
ATOM   2649 C CB  . SER B 2 156 ? 66.75600  56.61200 4.80700   1.000 250.14601 ?  176 SER D CB  1 
ATOM   2650 O OG  . SER B 2 156 ? 65.51300  56.10200 5.24800   1.000 244.26772 ?  176 SER D OG  1 
ATOM   2651 N N   . GLY B 2 157 ? 64.12100  57.65600 3.76200   1.000 243.25071 ?  177 GLY D N   1 
ATOM   2652 C CA  . GLY B 2 157 ? 62.83000  58.28100 4.02500   1.000 236.27943 ?  177 GLY D CA  1 
ATOM   2653 C C   . GLY B 2 157 ? 62.53700  59.52100 3.20300   1.000 232.12438 ?  177 GLY D C   1 
ATOM   2654 O O   . GLY B 2 157 ? 61.57300  60.25300 3.44600   1.000 227.98743 ?  177 GLY D O   1 
ATOM   2655 N N   . ASN B 2 158 ? 63.39500  59.75600 2.22000   1.000 233.93156 ?  178 ASN D N   1 
ATOM   2656 C CA  . ASN B 2 158 ? 63.19200  60.73700 1.17000   1.000 230.21566 ?  178 ASN D CA  1 
ATOM   2657 C C   . ASN B 2 158 ? 63.26900  60.03400 -0.17100  1.000 229.55137 ?  178 ASN D C   1 
ATOM   2658 O O   . ASN B 2 158 ? 63.25600  60.68900 -1.21600  1.000 227.22919 ?  178 ASN D O   1 
ATOM   2659 C CB  . ASN B 2 158 ? 64.21700  61.87300 1.26000   1.000 232.85852 ?  178 ASN D CB  1 
ATOM   2660 C CG  . ASN B 2 158 ? 65.62600  61.37200 1.51200   1.000 239.62359 ?  178 ASN D CG  1 
ATOM   2661 O OD1 . ASN B 2 158 ? 65.98400  60.25800 1.13100   1.000 242.47914 ?  178 ASN D OD1 1 
ATOM   2662 N ND2 . ASN B 2 158 ? 66.45000  62.22000 2.11300   1.000 242.57506 ?  178 ASN D ND2 1 
ATOM   2663 N N   . SER B 2 159 ? 63.35000  58.70700 -0.14000  1.000 229.04527 ?  179 SER D N   1 
ATOM   2664 C CA  . SER B 2 159 ? 63.50100  57.85500 -1.30500  1.000 229.54990 ?  179 SER D CA  1 
ATOM   2665 C C   . SER B 2 159 ? 62.22100  57.04800 -1.46900  1.000 224.97135 ?  179 SER D C   1 
ATOM   2666 O O   . SER B 2 159 ? 61.83500  56.30100 -0.56300  1.000 225.23436 ?  179 SER D O   1 
ATOM   2667 C CB  . SER B 2 159 ? 64.69400  56.92600 -1.11800  1.000 237.13626 ?  179 SER D CB  1 
ATOM   2668 O OG  . SER B 2 159 ? 65.78100  57.64200 -0.56200  1.000 241.37159 ?  179 SER D OG  1 
ATOM   2669 N N   . GLN B 2 160 ? 61.56500  57.19800 -2.61200  1.000 224.07919 ?  180 GLN D N   1 
ATOM   2670 C CA  . GLN B 2 160 ? 60.38800  56.40400 -2.94900  1.000 220.00663 ?  180 GLN D CA  1 
ATOM   2671 C C   . GLN B 2 160 ? 60.74400  55.45900 -4.09000  1.000 221.69242 ?  180 GLN D C   1 
ATOM   2672 O O   . GLN B 2 160 ? 61.14100  55.91200 -5.16600  1.000 221.79346 ?  180 GLN D O   1 
ATOM   2673 C CB  . GLN B 2 160 ? 59.20900  57.29800 -3.33900  1.000 214.84309 ?  180 GLN D CB  1 
ATOM   2674 N N   . GLU B 2 161 ? 60.59800  54.15700 -3.85700  1.000 216.74614 ?  181 GLU D N   1 
ATOM   2675 C CA  . GLU B 2 161 ? 60.97500  53.14200 -4.82900  1.000 219.44997 ?  181 GLU D CA  1 
ATOM   2676 C C   . GLU B 2 161 ? 59.75000  52.50600 -5.47500  1.000 214.29961 ?  181 GLU D C   1 
ATOM   2677 O O   . GLU B 2 161 ? 58.69300  52.36700 -4.85200  1.000 210.18228 ?  181 GLU D O   1 
ATOM   2678 C CB  . GLU B 2 161 ? 61.83300  52.05300 -4.18300  1.000 225.95214 ?  181 GLU D CB  1 
ATOM   2679 N N   . SER B 2 162 ? 59.92000  52.12100 -6.73900  1.000 210.68128 ?  182 SER D N   1 
ATOM   2680 C CA  . SER B 2 162 ? 58.91100  51.40200 -7.50700  1.000 207.00781 ?  182 SER D CA  1 
ATOM   2681 C C   . SER B 2 162 ? 59.58500  50.41800 -8.44900  1.000 209.48756 ?  182 SER D C   1 
ATOM   2682 O O   . SER B 2 162 ? 60.59200  50.74500 -9.07800  1.000 209.08512 ?  182 SER D O   1 
ATOM   2683 C CB  . SER B 2 162 ? 58.02100  52.34800 -8.31600  1.000 202.47713 ?  182 SER D CB  1 
ATOM   2684 O OG  . SER B 2 162 ? 57.08400  52.97900 -7.47200  1.000 198.96861 ?  182 SER D OG  1 
ATOM   2685 N N   . VAL B 2 163 ? 59.01600  49.21700 -8.55000  1.000 202.54021 ?  183 VAL D N   1 
ATOM   2686 C CA  . VAL B 2 163 ? 59.59200  48.13700 -9.34100  1.000 204.27632 ?  183 VAL D CA  1 
ATOM   2687 C C   . VAL B 2 163 ? 58.55900  47.65600 -10.34800 1.000 200.97067 ?  183 VAL D C   1 
ATOM   2688 O O   . VAL B 2 163 ? 57.37800  47.50200 -10.01500 1.000 198.67820 ?  183 VAL D O   1 
ATOM   2689 C CB  . VAL B 2 163 ? 60.06600  46.96800 -8.45300  1.000 208.57570 ?  183 VAL D CB  1 
ATOM   2690 C CG1 . VAL B 2 163 ? 61.10000  46.13300 -9.19500  1.000 212.03473 ?  183 VAL D CG1 1 
ATOM   2691 C CG2 . VAL B 2 163 ? 60.63000  47.48800 -7.13800  1.000 211.35949 ?  183 VAL D CG2 1 
ATOM   2692 N N   . THR B 2 164 ? 59.01400  47.39400 -11.57400 1.000 203.17881 ?  184 THR D N   1 
ATOM   2693 C CA  . THR B 2 164 ? 58.14100  46.90200 -12.63000 1.000 200.38175 ?  184 THR D CA  1 
ATOM   2694 C C   . THR B 2 164 ? 57.87600  45.41900 -12.39600 1.000 204.54421 ?  184 THR D C   1 
ATOM   2695 O O   . THR B 2 164 ? 58.21700  44.85500 -11.35300 1.000 207.59110 ?  184 THR D O   1 
ATOM   2696 C CB  . THR B 2 164 ? 58.75600  47.13400 -14.00900 1.000 196.95093 ?  184 THR D CB  1 
ATOM   2697 O OG1 . THR B 2 164 ? 60.00700  46.44000 -14.09400 1.000 201.17552 ?  184 THR D OG1 1 
ATOM   2698 C CG2 . THR B 2 164 ? 58.97200  48.61900 -14.25900 1.000 192.30750 ?  184 THR D CG2 1 
ATOM   2699 N N   . GLU B 2 165 ? 57.23800  44.77000 -13.35700 1.000 194.30318 ?  185 GLU D N   1 
ATOM   2700 C CA  . GLU B 2 165 ? 57.01000  43.33700 -13.29100 1.000 197.48293 ?  185 GLU D CA  1 
ATOM   2701 C C   . GLU B 2 165 ? 57.95600  42.60800 -14.23700 1.000 200.12570 ?  185 GLU D C   1 
ATOM   2702 O O   . GLU B 2 165 ? 58.45900  43.18100 -15.20700 1.000 197.62102 ?  185 GLU D O   1 
ATOM   2703 C CB  . GLU B 2 165 ? 55.56100  43.01500 -13.63200 1.000 195.12998 ?  185 GLU D CB  1 
ATOM   2704 N N   . GLN B 2 166 ? 58.20100  41.33200 -13.93100 1.000 194.20192 ?  186 GLN D N   1 
ATOM   2705 C CA  . GLN B 2 166 ? 59.11200  40.50400 -14.71400 1.000 197.78241 ?  186 GLN D CA  1 
ATOM   2706 C C   . GLN B 2 166 ? 58.80700  40.63400 -16.19300 1.000 195.82486 ?  186 GLN D C   1 
ATOM   2707 O O   . GLN B 2 166 ? 57.69700  40.33200 -16.63800 1.000 194.71673 ?  186 GLN D O   1 
ATOM   2708 C CB  . GLN B 2 166 ? 58.99400  39.03900 -14.29300 1.000 200.70530 ?  186 GLN D CB  1 
ATOM   2709 C CG  . GLN B 2 166 ? 59.80500  38.63500 -13.07900 1.000 203.46328 ?  186 GLN D CG  1 
ATOM   2710 C CD  . GLN B 2 166 ? 61.09700  37.93800 -13.43900 1.000 208.11211 ?  186 GLN D CD  1 
ATOM   2711 O OE1 . GLN B 2 166 ? 61.08500  36.82400 -13.95700 1.000 210.00555 ?  186 GLN D OE1 1 
ATOM   2712 N NE2 . GLN B 2 166 ? 62.22200  38.56900 -13.12400 1.000 209.73771 ?  186 GLN D NE2 1 
ATOM   2713 N N   . ASP B 2 167 ? 59.78400  41.11400 -16.95300 1.000 206.05532 ?  187 ASP D N   1 
ATOM   2714 C CA  . ASP B 2 167 ? 59.58300  41.22800 -18.38600 1.000 202.51670 ?  187 ASP D CA  1 
ATOM   2715 C C   . ASP B 2 167 ? 59.39700  39.83100 -18.96400 1.000 207.09844 ?  187 ASP D C   1 
ATOM   2716 O O   . ASP B 2 167 ? 60.04600  38.87400 -18.53300 1.000 212.31638 ?  187 ASP D O   1 
ATOM   2717 C CB  . ASP B 2 167 ? 60.77000  41.94600 -19.02200 1.000 198.74068 ?  187 ASP D CB  1 
ATOM   2718 C CG  . ASP B 2 167 ? 60.55600  42.25500 -20.48800 1.000 191.93542 ?  187 ASP D CG  1 
ATOM   2719 O OD1 . ASP B 2 167 ? 59.92000  41.45500 -21.20600 1.000 192.78235 ?  187 ASP D OD1 1 
ATOM   2720 O OD2 . ASP B 2 167 ? 61.01600  43.33500 -20.91300 1.000 185.33584 -1 187 ASP D OD2 1 
ATOM   2721 N N   . SER B 2 168 ? 58.49100  39.71600 -19.93500 1.000 203.25878 ?  188 SER D N   1 
ATOM   2722 C CA  . SER B 2 168 ? 58.15300  38.40300 -20.47400 1.000 208.39135 ?  188 SER D CA  1 
ATOM   2723 C C   . SER B 2 168 ? 59.35400  37.71800 -21.11600 1.000 211.31027 ?  188 SER D C   1 
ATOM   2724 O O   . SER B 2 168 ? 59.42800  36.48600 -21.11700 1.000 217.15721 ?  188 SER D O   1 
ATOM   2725 C CB  . SER B 2 168 ? 57.00900  38.52200 -21.47900 1.000 203.76114 ?  188 SER D CB  1 
ATOM   2726 O OG  . SER B 2 168 ? 57.35900  39.39900 -22.53100 1.000 195.02363 ?  188 SER D OG  1 
ATOM   2727 N N   . LYS B 2 169 ? 60.29000  38.48300 -21.67800 1.000 201.44308 ?  189 LYS D N   1 
ATOM   2728 C CA  . LYS B 2 169 ? 61.40300  37.88600 -22.41100 1.000 203.02885 ?  189 LYS D CA  1 
ATOM   2729 C C   . LYS B 2 169 ? 62.62700  37.66100 -21.52600 1.000 206.72157 ?  189 LYS D C   1 
ATOM   2730 O O   . LYS B 2 169 ? 63.05700  36.52000 -21.32600 1.000 212.72556 ?  189 LYS D O   1 
ATOM   2731 C CB  . LYS B 2 169 ? 61.76500  38.76500 -23.61300 1.000 194.44276 ?  189 LYS D CB  1 
ATOM   2732 N N   . ASP B 2 170 ? 63.19500  38.74000 -20.98600 1.000 207.68215 ?  190 ASP D N   1 
ATOM   2733 C CA  . ASP B 2 170 ? 64.42600  38.63800 -20.21300 1.000 210.37958 ?  190 ASP D CA  1 
ATOM   2734 C C   . ASP B 2 170 ? 64.20500  38.21800 -18.76700 1.000 215.45402 ?  190 ASP D C   1 
ATOM   2735 O O   . ASP B 2 170 ? 65.14900  37.73400 -18.13500 1.000 218.86286 ?  190 ASP D O   1 
ATOM   2736 C CB  . ASP B 2 170 ? 65.17600  39.97000 -20.25300 1.000 204.42902 ?  190 ASP D CB  1 
ATOM   2737 C CG  . ASP B 2 170 ? 64.35700  41.12700 -19.70300 1.000 200.75615 ?  190 ASP D CG  1 
ATOM   2738 O OD1 . ASP B 2 170 ? 63.75500  40.99700 -18.61600 1.000 204.47172 ?  190 ASP D OD1 1 
ATOM   2739 O OD2 . ASP B 2 170 ? 64.31000  42.17600 -20.37600 1.000 193.70591 -1 190 ASP D OD2 1 
ATOM   2740 N N   . SER B 2 171 ? 62.99800  38.41000 -18.23100 1.000 206.37596 ?  191 SER D N   1 
ATOM   2741 C CA  . SER B 2 171 ? 62.69000  38.10200 -16.83200 1.000 209.33709 ?  191 SER D CA  1 
ATOM   2742 C C   . SER B 2 171 ? 63.52400  38.94200 -15.86400 1.000 209.06694 ?  191 SER D C   1 
ATOM   2743 O O   . SER B 2 171 ? 63.86400  38.49100 -14.76800 1.000 212.24091 ?  191 SER D O   1 
ATOM   2744 C CB  . SER B 2 171 ? 62.85800  36.60800 -16.53500 1.000 214.04779 ?  191 SER D CB  1 
ATOM   2745 O OG  . SER B 2 171 ? 62.08800  35.82500 -17.43000 1.000 214.73930 ?  191 SER D OG  1 
ATOM   2746 N N   . THR B 2 172 ? 63.86500  40.16400 -16.26000 1.000 214.28764 ?  192 THR D N   1 
ATOM   2747 C CA  . THR B 2 172 ? 64.50400  41.13000 -15.37800 1.000 213.86947 ?  192 THR D CA  1 
ATOM   2748 C C   . THR B 2 172 ? 63.50300  42.20200 -14.96500 1.000 211.03524 ?  192 THR D C   1 
ATOM   2749 O O   . THR B 2 172 ? 62.42900  42.34300 -15.55400 1.000 207.82956 ?  192 THR D O   1 
ATOM   2750 C CB  . THR B 2 172 ? 65.70600  41.78700 -16.06000 1.000 210.36718 ?  192 THR D CB  1 
ATOM   2751 O OG1 . THR B 2 172 ? 65.24600  42.60400 -17.14400 1.000 203.86198 ?  192 THR D OG1 1 
ATOM   2752 C CG2 . THR B 2 172 ? 66.67100  40.73100 -16.58300 1.000 212.72457 ?  192 THR D CG2 1 
ATOM   2753 N N   . TYR B 2 173 ? 63.86400  42.95100 -13.92800 1.000 212.57888 ?  193 TYR D N   1 
ATOM   2754 C CA  . TYR B 2 173 ? 62.98500  43.94400 -13.33400 1.000 209.47470 ?  193 TYR D CA  1 
ATOM   2755 C C   . TYR B 2 173 ? 63.38800  45.36600 -13.73900 1.000 204.69720 ?  193 TYR D C   1 
ATOM   2756 O O   . TYR B 2 173 ? 64.26900  45.57600 -14.57100 1.000 202.40332 ?  193 TYR D O   1 
ATOM   2757 C CB  . TYR B 2 173 ? 62.97700  43.75000 -11.82200 1.000 212.97041 ?  193 TYR D CB  1 
ATOM   2758 C CG  . TYR B 2 173 ? 61.96000  42.73100 -11.39700 1.000 213.36800 ?  193 TYR D CG  1 
ATOM   2759 C CD1 . TYR B 2 173 ? 60.61300  42.92800 -11.65900 1.000 209.02664 ?  193 TYR D CD1 1 
ATOM   2760 C CD2 . TYR B 2 173 ? 62.34400  41.55900 -10.76600 1.000 217.61299 ?  193 TYR D CD2 1 
ATOM   2761 C CE1 . TYR B 2 173 ? 59.67500  42.00200 -11.28300 1.000 208.42148 ?  193 TYR D CE1 1 
ATOM   2762 C CE2 . TYR B 2 173 ? 61.41300  40.62300 -10.38600 1.000 216.56958 ?  193 TYR D CE2 1 
ATOM   2763 C CZ  . TYR B 2 173 ? 60.07700  40.85100 -10.64600 1.000 211.58677 ?  193 TYR D CZ  1 
ATOM   2764 O OH  . TYR B 2 173 ? 59.13500  39.92100 -10.27400 1.000 209.11948 ?  193 TYR D OH  1 
ATOM   2765 N N   . SER B 2 174 ? 62.71400  46.36100 -13.16500 1.000 212.74589 ?  194 SER D N   1 
ATOM   2766 C CA  . SER B 2 174 ? 63.09500  47.75700 -13.35500 1.000 208.34175 ?  194 SER D CA  1 
ATOM   2767 C C   . SER B 2 174 ? 62.64400  48.55800 -12.14300 1.000 208.92736 ?  194 SER D C   1 
ATOM   2768 O O   . SER B 2 174 ? 61.49100  48.44000 -11.72100 1.000 208.15619 ?  194 SER D O   1 
ATOM   2769 C CB  . SER B 2 174 ? 62.48200  48.32700 -14.63600 1.000 201.22619 ?  194 SER D CB  1 
ATOM   2770 O OG  . SER B 2 174 ? 63.26000  47.98300 -15.76500 1.000 199.57534 ?  194 SER D OG  1 
ATOM   2771 N N   . LEU B 2 175 ? 63.54700  49.36500 -11.59100 1.000 206.49774 ?  195 LEU D N   1 
ATOM   2772 C CA  . LEU B 2 175 ? 63.33100  50.10000 -10.35400 1.000 208.99563 ?  195 LEU D CA  1 
ATOM   2773 C C   . LEU B 2 175 ? 63.54500  51.59800 -10.54700 1.000 206.83260 ?  195 LEU D C   1 
ATOM   2774 O O   . LEU B 2 175 ? 64.30800  52.03200 -11.41700 1.000 204.49067 ?  195 LEU D O   1 
ATOM   2775 C CB  . LEU B 2 175 ? 64.26200  49.57900 -9.25600  1.000 214.38533 ?  195 LEU D CB  1 
ATOM   2776 N N   . SER B 2 176 ? 62.89100  52.37700 -9.68700  1.000 213.93171 ?  196 SER D N   1 
ATOM   2777 C CA  . SER B 2 176 ? 62.93700  53.83800 -9.74600  1.000 211.44699 ?  196 SER D CA  1 
ATOM   2778 C C   . SER B 2 176 ? 62.83000  54.37500 -8.32600  1.000 215.25670 ?  196 SER D C   1 
ATOM   2779 O O   . SER B 2 176 ? 61.80100  54.17300 -7.67100  1.000 215.70391 ?  196 SER D O   1 
ATOM   2780 C CB  . SER B 2 176 ? 61.81200  54.38900 -10.61200 1.000 206.15056 ?  196 SER D CB  1 
ATOM   2781 O OG  . SER B 2 176 ? 60.65100  53.58500 -10.48600 1.000 205.69028 ?  196 SER D OG  1 
ATOM   2782 N N   . SER B 2 177 ? 63.90000  55.00800 -7.84000  1.000 220.52838 ?  197 SER D N   1 
ATOM   2783 C CA  . SER B 2 177 ? 63.91500  55.64400 -6.52800  1.000 224.01935 ?  197 SER D CA  1 
ATOM   2784 C C   . SER B 2 177 ? 63.91200  57.16400 -6.67900  1.000 221.39455 ?  197 SER D C   1 
ATOM   2785 O O   . SER B 2 177 ? 64.62100  57.71600 -7.52500  1.000 219.54694 ?  197 SER D O   1 
ATOM   2786 C CB  . SER B 2 177 ? 65.13300  55.19200 -5.71900  1.000 230.10325 ?  197 SER D CB  1 
ATOM   2787 O OG  . SER B 2 177 ? 65.05100  55.65200 -4.38200  1.000 233.56311 ?  197 SER D OG  1 
ATOM   2788 N N   . THR B 2 178 ? 63.11000  57.83800 -5.85600  1.000 226.61192 ?  198 THR D N   1 
ATOM   2789 C CA  . THR B 2 178 ? 62.89400  59.28000 -5.95800  1.000 224.12619 ?  198 THR D CA  1 
ATOM   2790 C C   . THR B 2 178 ? 63.26800  59.97400 -4.65600  1.000 226.44671 ?  198 THR D C   1 
ATOM   2791 O O   . THR B 2 178 ? 62.69300  59.67400 -3.60600  1.000 226.43183 ?  198 THR D O   1 
ATOM   2792 C CB  . THR B 2 178 ? 61.44000  59.58600 -6.31500  1.000 219.78872 ?  198 THR D CB  1 
ATOM   2793 O OG1 . THR B 2 178 ? 61.06500  58.82600 -7.46900  1.000 218.04410 ?  198 THR D OG1 1 
ATOM   2794 C CG2 . THR B 2 178 ? 61.27400  61.06600 -6.60400  1.000 219.00271 ?  198 THR D CG2 1 
ATOM   2795 N N   . LEU B 2 179 ? 64.23800  60.88500 -4.73800  1.000 223.11335 ?  199 LEU D N   1 
ATOM   2796 C CA  . LEU B 2 179 ? 64.62000  61.79600 -3.66500  1.000 225.37527 ?  199 LEU D CA  1 
ATOM   2797 C C   . LEU B 2 179 ? 63.79100  63.07100 -3.75800  1.000 223.83885 ?  199 LEU D C   1 
ATOM   2798 O O   . LEU B 2 179 ? 64.00900  63.88700 -4.65300  1.000 223.83696 ?  199 LEU D O   1 
ATOM   2799 C CB  . LEU B 2 179 ? 66.10100  62.14700 -3.76600  1.000 228.32084 ?  199 LEU D CB  1 
ATOM   2800 C CG  . LEU B 2 179 ? 66.79600  62.62500 -2.49600  1.000 231.86174 ?  199 LEU D CG  1 
ATOM   2801 C CD1 . LEU B 2 179 ? 66.89400  61.47300 -1.54200  1.000 233.97404 ?  199 LEU D CD1 1 
ATOM   2802 C CD2 . LEU B 2 179 ? 68.16500  63.20600 -2.80300  1.000 234.20194 ?  199 LEU D CD2 1 
ATOM   2803 N N   . THR B 2 180 ? 62.86800  63.27100 -2.82800  1.000 228.70737 ?  200 THR D N   1 
ATOM   2804 C CA  . THR B 2 180 ? 62.00500  64.44100 -2.85600  1.000 226.98945 ?  200 THR D CA  1 
ATOM   2805 C C   . THR B 2 180 ? 62.34400  65.33700 -1.67700  1.000 228.93996 ?  200 THR D C   1 
ATOM   2806 O O   . THR B 2 180 ? 62.44700  64.86100 -0.54100  1.000 230.02983 ?  200 THR D O   1 
ATOM   2807 C CB  . THR B 2 180 ? 60.53200  64.03700 -2.80900  1.000 224.24074 ?  200 THR D CB  1 
ATOM   2808 O OG1 . THR B 2 180 ? 60.32100  62.91900 -3.68000  1.000 222.68416 ?  200 THR D OG1 1 
ATOM   2809 C CG2 . THR B 2 180 ? 59.64900  65.19400 -3.24300  1.000 223.94381 ?  200 THR D CG2 1 
ATOM   2810 N N   . LEU B 2 181 ? 62.50800  66.63200 -1.93900  1.000 229.32940 ?  201 LEU D N   1 
ATOM   2811 C CA  . LEU B 2 181 ? 62.89400  67.55900 -0.88500  1.000 231.50349 ?  201 LEU D CA  1 
ATOM   2812 C C   . LEU B 2 181 ? 62.45600  68.95300 -1.30500  1.000 232.23715 ?  201 LEU D C   1 
ATOM   2813 O O   . LEU B 2 181 ? 61.94800  69.15500 -2.41000  1.000 231.34790 ?  201 LEU D O   1 
ATOM   2814 C CB  . LEU B 2 181 ? 64.40300  67.50200 -0.61900  1.000 234.52804 ?  201 LEU D CB  1 
ATOM   2815 C CG  . LEU B 2 181 ? 65.33300  68.05700 -1.70300  1.000 235.89339 ?  201 LEU D CG  1 
ATOM   2816 C CD1 . LEU B 2 181 ? 66.56300  68.69500 -1.08400  1.000 239.33656 ?  201 LEU D CD1 1 
ATOM   2817 C CD2 . LEU B 2 181 ? 65.73700  66.97500 -2.69400  1.000 235.05699 ?  201 LEU D CD2 1 
ATOM   2818 N N   . SER B 2 182 ? 62.65600  69.91800 -0.41600  1.000 232.78028 ?  202 SER D N   1 
ATOM   2819 C CA  . SER B 2 182 ? 62.33200  71.28900 -0.76400  1.000 234.30379 ?  202 SER D CA  1 
ATOM   2820 C C   . SER B 2 182 ? 63.48600  71.89600 -1.54300  1.000 236.49084 ?  202 SER D C   1 
ATOM   2821 O O   . SER B 2 182 ? 64.64700  71.50400 -1.38300  1.000 237.33982 ?  202 SER D O   1 
ATOM   2822 C CB  . SER B 2 182 ? 62.05100  72.12200 0.49100   1.000 236.52124 ?  202 SER D CB  1 
ATOM   2823 O OG  . SER B 2 182 ? 63.24700  72.40500 1.20400   1.000 239.29057 ?  202 SER D OG  1 
ATOM   2824 N N   . LYS B 2 183 ? 63.15400  72.86600 -2.39700  1.000 238.17798 ?  203 LYS D N   1 
ATOM   2825 C CA  . LYS B 2 183 ? 64.19300  73.55800 -3.14200  1.000 242.20108 ?  203 LYS D CA  1 
ATOM   2826 C C   . LYS B 2 183 ? 65.14300  74.27900 -2.20000  1.000 247.66384 ?  203 LYS D C   1 
ATOM   2827 O O   . LYS B 2 183 ? 66.27400  74.58400 -2.58900  1.000 250.45229 ?  203 LYS D O   1 
ATOM   2828 C CB  . LYS B 2 183 ? 63.57200  74.53600 -4.14300  1.000 246.20273 ?  203 LYS D CB  1 
ATOM   2829 N N   . ALA B 2 184 ? 64.69700  74.55700 -0.97100  1.000 249.56931 ?  204 ALA D N   1 
ATOM   2830 C CA  . ALA B 2 184 ? 65.56700  75.16300 0.03000   1.000 254.55524 ?  204 ALA D CA  1 
ATOM   2831 C C   . ALA B 2 184 ? 66.70800  74.22500 0.40000   1.000 251.30727 ?  204 ALA D C   1 
ATOM   2832 O O   . ALA B 2 184 ? 67.88100  74.60800 0.34300   1.000 254.93194 ?  204 ALA D O   1 
ATOM   2833 C CB  . ALA B 2 184 ? 64.75500  75.53600 1.26900   1.000 256.87706 ?  204 ALA D CB  1 
ATOM   2834 N N   . ASP B 2 185 ? 66.38600  72.98800 0.79100   1.000 244.98356 ?  205 ASP D N   1 
ATOM   2835 C CA  . ASP B 2 185 ? 67.44700  72.02900 1.07100   1.000 244.91113 ?  205 ASP D CA  1 
ATOM   2836 C C   . ASP B 2 185 ? 68.15300  71.60900 -0.20500  1.000 244.69905 ?  205 ASP D C   1 
ATOM   2837 O O   . ASP B 2 185 ? 69.26400  71.07400 -0.14200  1.000 246.46191 ?  205 ASP D O   1 
ATOM   2838 C CB  . ASP B 2 185 ? 66.89100  70.79800 1.78500   1.000 243.22777 ?  205 ASP D CB  1 
ATOM   2839 C CG  . ASP B 2 185 ? 66.02700  71.15800 2.96800   1.000 242.93405 ?  205 ASP D CG  1 
ATOM   2840 O OD1 . ASP B 2 185 ? 65.01900  71.86500 2.75900   1.000 241.68235 ?  205 ASP D OD1 1 
ATOM   2841 O OD2 . ASP B 2 185 ? 66.35500  70.73500 4.09800   1.000 244.36379 -1 205 ASP D OD2 1 
ATOM   2842 N N   . TYR B 2 186 ? 67.52300  71.83800 -1.35300  1.000 244.93479 ?  206 TYR D N   1 
ATOM   2843 C CA  . TYR B 2 186 ? 68.15000  71.67800 -2.65000  1.000 244.75549 ?  206 TYR D CA  1 
ATOM   2844 C C   . TYR B 2 186 ? 68.94100  72.94700 -2.96300  1.000 247.79340 ?  206 TYR D C   1 
ATOM   2845 O O   . TYR B 2 186 ? 68.87400  73.93700 -2.23100  1.000 251.45893 ?  206 TYR D O   1 
ATOM   2846 C CB  . TYR B 2 186 ? 67.09500  71.39500 -3.72000  1.000 241.91205 ?  206 TYR D CB  1 
ATOM   2847 C CG  . TYR B 2 186 ? 67.65600  70.87000 -5.01900  1.000 241.00914 ?  206 TYR D CG  1 
ATOM   2848 C CD1 . TYR B 2 186 ? 68.07100  69.55200 -5.14300  1.000 239.70794 ?  206 TYR D CD1 1 
ATOM   2849 C CD2 . TYR B 2 186 ? 67.80800  71.70400 -6.11300  1.000 241.60352 ?  206 TYR D CD2 1 
ATOM   2850 C CE1 . TYR B 2 186 ? 68.59300  69.07700 -6.33400  1.000 238.43416 ?  206 TYR D CE1 1 
ATOM   2851 C CE2 . TYR B 2 186 ? 68.33800  71.24300 -7.29700  1.000 240.46362 ?  206 TYR D CE2 1 
ATOM   2852 C CZ  . TYR B 2 186 ? 68.72700  69.93100 -7.40600  1.000 238.60571 ?  206 TYR D CZ  1 
ATOM   2853 O OH  . TYR B 2 186 ? 69.25100  69.47200 -8.59200  1.000 236.94118 ?  206 TYR D OH  1 
ATOM   2854 N N   . GLU B 2 187 ? 69.74900  72.89100 -4.02200  1.000 248.61217 ?  207 GLU D N   1 
ATOM   2855 C CA  . GLU B 2 187 ? 70.53000  74.03400 -4.50000  1.000 254.38814 ?  207 GLU D CA  1 
ATOM   2856 C C   . GLU B 2 187 ? 71.60800  74.44800 -3.51000  1.000 259.28832 ?  207 GLU D C   1 
ATOM   2857 O O   . GLU B 2 187 ? 72.48400  75.25400 -3.84100  1.000 265.50751 ?  207 GLU D O   1 
ATOM   2858 C CB  . GLU B 2 187 ? 69.64500  75.25200 -4.77400  1.000 258.79460 ?  207 GLU D CB  1 
ATOM   2859 C CG  . GLU B 2 187 ? 68.50600  75.05100 -5.73400  1.000 255.24619 ?  207 GLU D CG  1 
ATOM   2860 C CD  . GLU B 2 187 ? 68.50800  76.11900 -6.80600  1.000 260.95045 ?  207 GLU D CD  1 
ATOM   2861 O OE1 . GLU B 2 187 ? 67.94000  77.19900 -6.54500  1.000 266.17046 ?  207 GLU D OE1 1 
ATOM   2862 O OE2 . GLU B 2 187 ? 69.08300  75.89500 -7.89300  1.000 260.74060 -1 207 GLU D OE2 1 
ATOM   2863 N N   . LYS B 2 188 ? 71.56800  73.88700 -2.31300  1.000 256.82122 ?  208 LYS D N   1 
ATOM   2864 C CA  . LYS B 2 188 ? 72.58900  74.13300 -1.31300  1.000 260.96702 ?  208 LYS D CA  1 
ATOM   2865 C C   . LYS B 2 188 ? 73.73300  73.15200 -1.45000  1.000 259.15339 ?  208 LYS D C   1 
ATOM   2866 O O   . LYS B 2 188 ? 74.73100  73.27000 -0.73400  1.000 262.84737 ?  208 LYS D O   1 
ATOM   2867 C CB  . LYS B 2 188 ? 71.98400  74.05100 0.09100   1.000 259.87405 ?  208 LYS D CB  1 
ATOM   2868 N N   . HIS B 2 189 ? 73.59600  72.19300 -2.36200  1.000 254.07202 ?  209 HIS D N   1 
ATOM   2869 C CA  . HIS B 2 189 ? 74.56500  71.13400 -2.55500  1.000 252.64762 ?  209 HIS D CA  1 
ATOM   2870 C C   . HIS B 2 189 ? 74.77500  70.92000 -4.04600  1.000 251.23183 ?  209 HIS D C   1 
ATOM   2871 O O   . HIS B 2 189 ? 73.91900  71.24100 -4.87200  1.000 249.83915 ?  209 HIS D O   1 
ATOM   2872 C CB  . HIS B 2 189 ? 74.12200  69.82600 -1.87800  1.000 251.85681 ?  209 HIS D CB  1 
ATOM   2873 C CG  . HIS B 2 189 ? 73.50300  70.01400 -0.52500  1.000 253.24486 ?  209 HIS D CG  1 
ATOM   2874 N ND1 . HIS B 2 189 ? 72.34100  70.72800 -0.32200  1.000 251.71059 ?  209 HIS D ND1 1 
ATOM   2875 C CD2 . HIS B 2 189 ? 73.91100  69.60800 0.70100   1.000 256.08227 ?  209 HIS D CD2 1 
ATOM   2876 C CE1 . HIS B 2 189 ? 72.04700  70.73300 0.96600   1.000 253.01993 ?  209 HIS D CE1 1 
ATOM   2877 N NE2 . HIS B 2 189 ? 72.98600  70.06300 1.60900   1.000 255.81626 ?  209 HIS D NE2 1 
ATOM   2878 N N   . LYS B 2 190 ? 75.93700  70.36800 -4.37700  1.000 252.99717 ?  210 LYS D N   1 
ATOM   2879 C CA  . LYS B 2 190 ? 76.33000  70.10500 -5.75400  1.000 252.68162 ?  210 LYS D CA  1 
ATOM   2880 C C   . LYS B 2 190 ? 76.30100  68.62000 -6.07200  1.000 246.61239 ?  210 LYS D C   1 
ATOM   2881 O O   . LYS B 2 190 ? 75.69100  68.20500 -7.06200  1.000 242.96316 ?  210 LYS D O   1 
ATOM   2882 C CB  . LYS B 2 190 ? 77.73200  70.67000 -6.02100  1.000 260.12286 ?  210 LYS D CB  1 
ATOM   2883 N N   . VAL B 2 191 ? 76.97200  67.81200 -5.26000  1.000 269.77100 ?  211 VAL D N   1 
ATOM   2884 C CA  . VAL B 2 191 ? 77.05800  66.37400 -5.48600  1.000 269.01199 ?  211 VAL D CA  1 
ATOM   2885 C C   . VAL B 2 191 ? 75.80400  65.69600 -4.94200  1.000 264.86089 ?  211 VAL D C   1 
ATOM   2886 O O   . VAL B 2 191 ? 75.46000  65.85200 -3.76600  1.000 268.87426 ?  211 VAL D O   1 
ATOM   2887 C CB  . VAL B 2 191 ? 78.31800  65.79400 -4.83200  1.000 279.50365 ?  211 VAL D CB  1 
ATOM   2888 C CG1 . VAL B 2 191 ? 78.24300  64.27800 -4.82200  1.000 279.28250 ?  211 VAL D CG1 1 
ATOM   2889 C CG2 . VAL B 2 191 ? 79.55900  66.28400 -5.55600  1.000 283.23250 ?  211 VAL D CG2 1 
ATOM   2890 N N   . TYR B 2 192 ? 75.11400  64.95000 -5.80400  1.000 257.23403 ?  212 TYR D N   1 
ATOM   2891 C CA  . TYR B 2 192 ? 73.96800  64.12200 -5.42100  1.000 253.69852 ?  212 TYR D CA  1 
ATOM   2892 C C   . TYR B 2 192 ? 74.27100  62.70000 -5.89800  1.000 253.76131 ?  212 TYR D C   1 
ATOM   2893 O O   . TYR B 2 192 ? 74.13500  62.41300 -7.08900  1.000 247.63660 ?  212 TYR D O   1 
ATOM   2894 C CB  . TYR B 2 192 ? 72.67000  64.64300 -6.03900  1.000 244.26457 ?  212 TYR D CB  1 
ATOM   2895 C CG  . TYR B 2 192 ? 72.21900  66.01000 -5.56500  1.000 243.61754 ?  212 TYR D CG  1 
ATOM   2896 C CD1 . TYR B 2 192 ? 71.72500  66.19900 -4.28100  1.000 247.15681 ?  212 TYR D CD1 1 
ATOM   2897 C CD2 . TYR B 2 192 ? 72.28100  67.10900 -6.41100  1.000 243.50159 ?  212 TYR D CD2 1 
ATOM   2898 C CE1 . TYR B 2 192 ? 71.30300  67.44700 -3.85300  1.000 250.55771 ?  212 TYR D CE1 1 
ATOM   2899 C CE2 . TYR B 2 192 ? 71.87200  68.35500 -5.99400  1.000 247.08837 ?  212 TYR D CE2 1 
ATOM   2900 C CZ  . TYR B 2 192 ? 71.38300  68.52400 -4.71300  1.000 250.48748 ?  212 TYR D CZ  1 
ATOM   2901 O OH  . TYR B 2 192 ? 70.97100  69.77200 -4.29600  1.000 258.53192 ?  212 TYR D OH  1 
ATOM   2902 N N   . ALA B 2 193 ? 74.67000  61.81000 -4.98800  1.000 260.91296 ?  213 ALA D N   1 
ATOM   2903 C CA  . ALA B 2 193 ? 75.04000  60.43700 -5.31200  1.000 262.29662 ?  213 ALA D CA  1 
ATOM   2904 C C   . ALA B 2 193 ? 73.92300  59.46200 -4.93400  1.000 260.15025 ?  213 ALA D C   1 
ATOM   2905 O O   . ALA B 2 193 ? 73.17200  59.69300 -3.98500  1.000 261.44898 ?  213 ALA D O   1 
ATOM   2906 C CB  . ALA B 2 193 ? 76.34400  60.05000 -4.60400  1.000 272.78450 ?  213 ALA D CB  1 
ATOM   2907 N N   . CYS B 2 194 ? 73.80800  58.36700 -5.69200  1.000 261.36957 ?  214 CYS D N   1 
ATOM   2908 C CA  . CYS B 2 194 ? 72.77900  57.35700 -5.42600  1.000 259.88185 ?  214 CYS D CA  1 
ATOM   2909 C C   . CYS B 2 194 ? 73.38700  55.95900 -5.52700  1.000 264.17710 ?  214 CYS D C   1 
ATOM   2910 O O   . CYS B 2 194 ? 73.74000  55.50900 -6.62100  1.000 260.68313 ?  214 CYS D O   1 
ATOM   2911 C CB  . CYS B 2 194 ? 71.59300  57.52400 -6.38400  1.000 250.05865 ?  214 CYS D CB  1 
ATOM   2912 S SG  . CYS B 2 194 ? 70.78800  56.00700 -6.97900  1.000 246.82127 ?  214 CYS D SG  1 
ATOM   2913 N N   . GLU B 2 195 ? 73.41000  55.29700 -4.36600  1.000 267.51250 ?  215 GLU D N   1 
ATOM   2914 C CA  . GLU B 2 195 ? 74.04100  53.96300 -4.26400  1.000 273.29506 ?  215 GLU D CA  1 
ATOM   2915 C C   . GLU B 2 195 ? 72.99200  52.85700 -4.18200  1.000 271.97020 ?  215 GLU D C   1 
ATOM   2916 O O   . GLU B 2 195 ? 71.86200  53.13600 -3.74800  1.000 269.51180 ?  215 GLU D O   1 
ATOM   2917 C CB  . GLU B 2 195 ? 74.88400  53.94200 -2.99100  1.000 284.26593 ?  215 GLU D CB  1 
ATOM   2918 C CG  . GLU B 2 195 ? 75.79000  52.73700 -2.85400  1.000 291.74258 ?  215 GLU D CG  1 
ATOM   2919 C CD  . GLU B 2 195 ? 77.08100  53.03500 -2.11200  1.000 301.40191 ?  215 GLU D CD  1 
ATOM   2920 O OE1 . GLU B 2 195 ? 77.32800  54.22000 -1.81800  1.000 302.12465 ?  215 GLU D OE1 1 
ATOM   2921 O OE2 . GLU B 2 195 ? 77.83500  52.08400 -1.83300  1.000 310.02748 -1 215 GLU D OE2 1 
ATOM   2922 N N   . VAL B 2 196 ? 73.37000  51.64800 -4.57300  1.000 275.86546 ?  216 VAL D N   1 
ATOM   2923 C CA  . VAL B 2 196 ? 72.51000  50.46600 -4.53600  1.000 277.37351 ?  216 VAL D CA  1 
ATOM   2924 C C   . VAL B 2 196 ? 73.21700  49.37000 -3.74300  1.000 288.67244 ?  216 VAL D C   1 
ATOM   2925 O O   . VAL B 2 196 ? 74.39200  49.07700 -3.99100  1.000 293.21255 ?  216 VAL D O   1 
ATOM   2926 C CB  . VAL B 2 196 ? 72.13900  49.97600 -5.94900  1.000 270.83724 ?  216 VAL D CB  1 
ATOM   2927 C CG1 . VAL B 2 196 ? 71.17500  50.94900 -6.60400  1.000 260.23532 ?  216 VAL D CG1 1 
ATOM   2928 C CG2 . VAL B 2 196 ? 73.38100  49.82800 -6.80500  1.000 271.72003 ?  216 VAL D CG2 1 
ATOM   2929 N N   . THR B 2 197 ? 72.50800  48.77500 -2.78100  1.000 293.48466 ?  217 THR D N   1 
ATOM   2930 C CA  . THR B 2 197 ? 73.09600  47.71800 -1.96300  1.000 304.54956 ?  217 THR D CA  1 
ATOM   2931 C C   . THR B 2 197 ? 73.26100  46.41800 -2.74100  1.000 306.27578 ?  217 THR D C   1 
ATOM   2932 O O   . THR B 2 197 ? 72.32900  45.61500 -2.85300  1.000 305.59666 ?  217 THR D O   1 
ATOM   2933 C CB  . THR B 2 197 ? 72.22800  47.46600 -0.72600  1.000 309.12819 ?  217 THR D CB  1 
ATOM   2934 O OG1 . THR B 2 197 ? 72.03100  48.69800 -0.02100  1.000 307.26248 ?  217 THR D OG1 1 
ATOM   2935 C CG2 . THR B 2 197 ? 72.89100  46.45500 0.19900   1.000 321.24798 ?  217 THR D CG2 1 
ATOM   2936 N N   . GLN B 2 198 ? 74.46100  46.21500 -3.28100  1.000 308.81021 ?  218 GLN D N   1 
ATOM   2937 C CA  . GLN B 2 198 ? 74.84100  45.01400 -4.02400  1.000 311.16428 ?  218 GLN D CA  1 
ATOM   2938 C C   . GLN B 2 198 ? 76.11200  44.44500 -3.40400  1.000 321.93425 ?  218 GLN D C   1 
ATOM   2939 O O   . GLN B 2 198 ? 77.19700  44.99900 -3.60100  1.000 323.16736 ?  218 GLN D O   1 
ATOM   2940 C CB  . GLN B 2 198 ? 75.02900  45.31300 -5.50900  1.000 302.77854 ?  218 GLN D CB  1 
ATOM   2941 C CG  . GLN B 2 198 ? 74.01600  46.28700 -6.07200  1.000 292.13536 ?  218 GLN D CG  1 
ATOM   2942 C CD  . GLN B 2 198 ? 72.62000  45.68900 -6.11000  1.000 289.57226 ?  218 GLN D CD  1 
ATOM   2943 O OE1 . GLN B 2 198 ? 71.64600  46.31500 -5.68800  1.000 285.77439 ?  218 GLN D OE1 1 
ATOM   2944 N NE2 . GLN B 2 198 ? 72.51800  44.46300 -6.61700  1.000 291.97441 ?  218 GLN D NE2 1 
ATOM   2945 N N   . GLY B 2 199 ? 75.97800  43.36700 -2.63400  1.000 330.11028 ?  219 GLY D N   1 
ATOM   2946 C CA  . GLY B 2 199 ? 77.11800  42.71600 -2.01100  1.000 341.11333 ?  219 GLY D CA  1 
ATOM   2947 C C   . GLY B 2 199 ? 78.29000  42.43000 -2.93500  1.000 341.90065 ?  219 GLY D C   1 
ATOM   2948 O O   . GLY B 2 199 ? 79.41400  42.22500 -2.46800  1.000 350.49985 ?  219 GLY D O   1 
ATOM   2949 N N   . THR B 2 200 ? 78.04600  42.41900 -4.24600  1.000 333.36777 ?  220 THR D N   1 
ATOM   2950 C CA  . THR B 2 200 ? 79.11800  42.22500 -5.21800  1.000 333.21411 ?  220 THR D CA  1 
ATOM   2951 C C   . THR B 2 200 ? 79.83200  43.54300 -5.53500  1.000 329.44938 ?  220 THR D C   1 
ATOM   2952 O O   . THR B 2 200 ? 81.03600  43.68000 -5.28900  1.000 335.86217 ?  220 THR D O   1 
ATOM   2953 C CB  . THR B 2 200 ? 78.55100  41.55700 -6.48300  1.000 326.53759 ?  220 THR D CB  1 
ATOM   2954 O OG1 . THR B 2 200 ? 79.57200  41.43400 -7.48100  1.000 325.79320 ?  220 THR D OG1 1 
ATOM   2955 C CG2 . THR B 2 200 ? 77.31700  42.28500 -7.03700  1.000 315.80899 ?  220 THR D CG2 1 
ATOM   2956 N N   . THR B 2 201 ? 79.10800  44.52300 -6.08000  1.000 319.47334 ?  221 THR D N   1 
ATOM   2957 C CA  . THR B 2 201 ? 79.64800  45.84800 -6.39100  1.000 315.19049 ?  221 THR D CA  1 
ATOM   2958 C C   . THR B 2 201 ? 78.53700  46.83300 -6.05800  1.000 308.35308 ?  221 THR D C   1 
ATOM   2959 O O   . THR B 2 201 ? 77.50100  46.84400 -6.73000  1.000 300.18873 ?  221 THR D O   1 
ATOM   2960 C CB  . THR B 2 201 ? 80.07800  46.00300 -7.85400  1.000 308.58198 ?  221 THR D CB  1 
ATOM   2961 O OG1 . THR B 2 201 ? 78.96100  46.44700 -8.63700  1.000 297.85719 ?  221 THR D OG1 1 
ATOM   2962 C CG2 . THR B 2 201 ? 80.61900  44.69900 -8.44500  1.000 312.60819 ?  221 THR D CG2 1 
ATOM   2963 N N   . SER B 2 202 ? 78.75400  47.67600 -5.04900  1.000 311.80665 ?  222 SER D N   1 
ATOM   2964 C CA  . SER B 2 202 ? 77.70700  48.56500 -4.54100  1.000 306.52992 ?  222 SER D CA  1 
ATOM   2965 C C   . SER B 2 202 ? 77.81300  49.91300 -5.25700  1.000 298.12918 ?  222 SER D C   1 
ATOM   2966 O O   . SER B 2 202 ? 78.19500  50.94300 -4.69700  1.000 299.39199 ?  222 SER D O   1 
ATOM   2967 C CB  . SER B 2 202 ? 77.81700  48.70100 -3.02800  1.000 315.11147 ?  222 SER D CB  1 
ATOM   2968 O OG  . SER B 2 202 ? 77.01900  49.75700 -2.53800  1.000 310.26054 ?  222 SER D OG  1 
ATOM   2969 N N   . VAL B 2 203 ? 77.45300  49.86800 -6.54400  1.000 289.67002 ?  225 VAL D N   1 
ATOM   2970 C CA  . VAL B 2 203 ? 77.65100  50.99100 -7.45700  1.000 281.68311 ?  225 VAL D CA  1 
ATOM   2971 C C   . VAL B 2 203 ? 76.78200  52.19600 -7.08800  1.000 275.36106 ?  225 VAL D C   1 
ATOM   2972 O O   . VAL B 2 203 ? 75.76600  52.09100 -6.38800  1.000 274.84214 ?  225 VAL D O   1 
ATOM   2973 C CB  . VAL B 2 203 ? 77.40000  50.56100 -8.91100  1.000 274.55537 ?  225 VAL D CB  1 
ATOM   2974 C CG1 . VAL B 2 203 ? 78.58300  49.75800 -9.43000  1.000 280.00797 ?  225 VAL D CG1 1 
ATOM   2975 C CG2 . VAL B 2 203 ? 76.12400  49.74600 -9.01600  1.000 271.67568 ?  225 VAL D CG2 1 
ATOM   2976 N N   . THR B 2 204 ? 77.20500  53.35900 -7.58600  1.000 274.73827 ?  226 THR D N   1 
ATOM   2977 C CA  . THR B 2 204 ? 76.63300  54.65900 -7.27200  1.000 270.72755 ?  226 THR D CA  1 
ATOM   2978 C C   . THR B 2 204 ? 76.73900  55.56700 -8.49100  1.000 263.61406 ?  226 THR D C   1 
ATOM   2979 O O   . THR B 2 204 ? 77.64700  55.41600 -9.31300  1.000 263.74572 ?  226 THR D O   1 
ATOM   2980 C CB  . THR B 2 204 ? 77.35700  55.28700 -6.07200  1.000 279.55202 ?  226 THR D CB  1 
ATOM   2981 O OG1 . THR B 2 204 ? 77.52900  54.30100 -5.04500  1.000 287.64993 ?  226 THR D OG1 1 
ATOM   2982 C CG2 . THR B 2 204 ? 76.59700  56.47800 -5.52000  1.000 277.33129 ?  226 THR D CG2 1 
ATOM   2983 N N   . LYS B 2 205 ? 75.78500  56.49200 -8.62100  1.000 258.21785 ?  227 LYS D N   1 
ATOM   2984 C CA  . LYS B 2 205 ? 75.80100  57.47800 -9.69700  1.000 251.99233 ?  227 LYS D CA  1 
ATOM   2985 C C   . LYS B 2 205 ? 75.46400  58.86200 -9.15600  1.000 251.64740 ?  227 LYS D C   1 
ATOM   2986 O O   . LYS B 2 205 ? 74.66000  58.99900 -8.23100  1.000 252.29611 ?  227 LYS D O   1 
ATOM   2987 C CB  . LYS B 2 205 ? 74.80800  57.11000 -10.80600 1.000 243.18684 ?  227 LYS D CB  1 
ATOM   2988 N N   . SER B 2 206 ? 76.06600  59.89400 -9.75500  1.000 246.07626 ?  228 SER D N   1 
ATOM   2989 C CA  . SER B 2 206 ? 75.92900  61.25100 -9.23900  1.000 246.90845 ?  228 SER D CA  1 
ATOM   2990 C C   . SER B 2 206 ? 75.89600  62.25700 -10.38900 1.000 241.24594 ?  228 SER D C   1 
ATOM   2991 O O   . SER B 2 206 ? 76.08800  61.90600 -11.55800 1.000 237.37787 ?  228 SER D O   1 
ATOM   2992 C CB  . SER B 2 206 ? 77.06000  61.57600 -8.26200  1.000 256.76532 ?  228 SER D CB  1 
ATOM   2993 O OG  . SER B 2 206 ? 76.91900  62.88600 -7.74700  1.000 257.94883 ?  228 SER D OG  1 
ATOM   2994 N N   . PHE B 2 207 ? 75.66400  63.52700 -10.03500 1.000 241.27188 ?  229 PHE D N   1 
ATOM   2995 C CA  . PHE B 2 207 ? 75.61400  64.64000 -10.97800 1.000 237.01915 ?  229 PHE D CA  1 
ATOM   2996 C C   . PHE B 2 207 ? 75.97500  65.93000 -10.25100 1.000 241.82432 ?  229 PHE D C   1 
ATOM   2997 O O   . PHE B 2 207 ? 76.06500  65.96800 -9.02300  1.000 247.40881 ?  229 PHE D O   1 
ATOM   2998 C CB  . PHE B 2 207 ? 74.23300  64.76300 -11.62400 1.000 227.99259 ?  229 PHE D CB  1 
ATOM   2999 N N   . ASN B 2 208 ? 76.20500  66.98900 -11.02600 1.000 240.18656 ?  230 ASN D N   1 
ATOM   3000 C CA  . ASN B 2 208 ? 76.56000  68.30300 -10.49500 1.000 244.71636 ?  230 ASN D CA  1 
ATOM   3001 C C   . ASN B 2 208 ? 75.53500  69.34400 -10.93200 1.000 238.21885 ?  230 ASN D C   1 
ATOM   3002 O O   . ASN B 2 208 ? 75.31600  69.53400 -12.13300 1.000 232.88145 ?  230 ASN D O   1 
ATOM   3003 C CB  . ASN B 2 208 ? 77.97100  68.69300 -10.95200 1.000 250.90956 ?  230 ASN D CB  1 
ATOM   3004 C CG  . ASN B 2 208 ? 78.98200  68.60300 -9.83500  1.000 261.15201 ?  230 ASN D CG  1 
ATOM   3005 O OD1 . ASN B 2 208 ? 78.62000  68.45600 -8.66700  1.000 263.91691 ?  230 ASN D OD1 1 
ATOM   3006 N ND2 . ASN B 2 208 ? 80.25800  68.66400 -10.18700 1.000 267.31461 ?  230 ASN D ND2 1 
ATOM   3007 N N   . ARG B 2 209 ? 74.90200  70.00300 -9.95600  1.000 238.96065 ?  231 ARG D N   1 
ATOM   3008 C CA  . ARG B 2 209 ? 73.92700  71.05500 -10.24800 1.000 233.75074 ?  231 ARG D CA  1 
ATOM   3009 C C   . ARG B 2 209 ? 74.50100  72.12800 -11.16100 1.000 234.30873 ?  231 ARG D C   1 
ATOM   3010 O O   . ARG B 2 209 ? 73.83700  72.58300 -12.10000 1.000 232.30804 ?  231 ARG D O   1 
ATOM   3011 C CB  . ARG B 2 209 ? 73.47500  71.72400 -8.95400  1.000 243.01079 ?  231 ARG D CB  1 
ATOM   3012 C CG  . ARG B 2 209 ? 72.44200  71.02200 -8.12000  1.000 241.64391 ?  231 ARG D CG  1 
ATOM   3013 C CD  . ARG B 2 209 ? 71.72000  72.07000 -7.28100  1.000 250.28631 ?  231 ARG D CD  1 
ATOM   3014 N NE  . ARG B 2 209 ? 72.59700  73.18900 -6.95200  1.000 258.91097 ?  231 ARG D NE  1 
ATOM   3015 C CZ  . ARG B 2 209 ? 72.43900  74.42900 -7.39700  1.000 263.78235 ?  231 ARG D CZ  1 
ATOM   3016 N NH1 . ARG B 2 209 ? 71.45700  74.74900 -8.22600  1.000 261.01261 ?  231 ARG D NH1 1 
ATOM   3017 N NH2 . ARG B 2 209 ? 73.29700  75.37000 -7.01100  1.000 267.47305 ?  231 ARG D NH2 1 
ATOM   3018 N N   . GLY B 2 210 ? 75.74900  72.52600 -10.90800 1.000 245.92661 ?  232 GLY D N   1 
ATOM   3019 C CA  . GLY B 2 210 ? 76.41200  73.54900 -11.70100 1.000 245.52724 ?  232 GLY D CA  1 
ATOM   3020 C C   . GLY B 2 210 ? 76.56400  73.17100 -13.15600 1.000 239.93804 ?  232 GLY D C   1 
ATOM   3021 O O   . GLY B 2 210 ? 76.74000  74.05100 -14.01000 1.000 239.57600 ?  232 GLY D O   1 
ATOM   3022 N N   . GLU B 2 211 ? 76.59300  71.87600 -13.44400 1.000 249.87876 ?  233 GLU D N   1 
ATOM   3023 C CA  . GLU B 2 211 ? 76.65600  71.35600 -14.79900 1.000 242.39886 ?  233 GLU D CA  1 
ATOM   3024 C C   . GLU B 2 211 ? 75.27100  70.98100 -15.32600 1.000 236.32245 ?  233 GLU D C   1 
ATOM   3025 O O   . GLU B 2 211 ? 74.33600  70.73800 -14.55900 1.000 239.21865 ?  233 GLU D O   1 
ATOM   3026 C CB  . GLU B 2 211 ? 77.58700  70.14100 -14.85000 1.000 240.94699 ?  233 GLU D CB  1 
ATOM   3027 N N   . CYS B 2 212 ? 75.14900  70.96700 -16.65200 1.000 246.86853 ?  234 CYS D N   1 
ATOM   3028 C CA  . CYS B 2 212 ? 73.89300  70.64700 -17.33400 1.000 241.28433 ?  234 CYS D CA  1 
ATOM   3029 C C   . CYS B 2 212 ? 74.17600  70.12000 -18.74100 1.000 234.20147 ?  234 CYS D C   1 
ATOM   3030 O O   . CYS B 2 212 ? 74.06600  70.84700 -19.73000 1.000 230.51072 ?  234 CYS D O   1 
ATOM   3031 C CB  . CYS B 2 212 ? 72.96700  71.86200 -17.39900 1.000 245.69187 ?  234 CYS D CB  1 
ATOM   3032 S SG  . CYS B 2 212 ? 73.71500  73.40200 -18.00000 1.000 243.30597 ?  234 CYS D SG  1 
ATOM   3033 N N   . HIS C 3 11  ? 6.06800   35.80500 1.75900   1.000 195.05533 ?  11  HIS E N   1 
ATOM   3034 C CA  . HIS C 3 11  ? 6.10900   35.67000 0.30600   1.000 194.81761 ?  11  HIS E CA  1 
ATOM   3035 C C   . HIS C 3 11  ? 5.24200   34.51200 -0.18000  1.000 189.15871 ?  11  HIS E C   1 
ATOM   3036 O O   . HIS C 3 11  ? 5.22600   33.43600 0.41600   1.000 191.54215 ?  11  HIS E O   1 
ATOM   3037 C CB  . HIS C 3 11  ? 7.55000   35.47700 -0.17800  1.000 206.62259 ?  11  HIS E CB  1 
ATOM   3038 C CG  . HIS C 3 11  ? 7.76600   35.90000 -1.59700  1.000 204.03900 ?  11  HIS E CG  1 
ATOM   3039 N ND1 . HIS C 3 11  ? 6.76400   35.86900 -2.54100  1.000 195.13023 ?  11  HIS E ND1 1 
ATOM   3040 C CD2 . HIS C 3 11  ? 8.86700   36.36600 -2.23400  1.000 208.37982 ?  11  HIS E CD2 1 
ATOM   3041 C CE1 . HIS C 3 11  ? 7.23600   36.29500 -3.69800  1.000 195.17311 ?  11  HIS E CE1 1 
ATOM   3042 N NE2 . HIS C 3 11  ? 8.51000   36.60400 -3.53900  1.000 202.89500 ?  11  HIS E NE2 1 
ATOM   3043 N N   . HIS C 3 12  ? 4.51500   34.75900 -1.26600  1.000 199.29368 ?  12  HIS E N   1 
ATOM   3044 C CA  . HIS C 3 12  ? 3.70000   33.74700 -1.91600  1.000 192.87689 ?  12  HIS E CA  1 
ATOM   3045 C C   . HIS C 3 12  ? 3.36200   34.25400 -3.31200  1.000 186.74127 ?  12  HIS E C   1 
ATOM   3046 O O   . HIS C 3 12  ? 3.36900   35.46100 -3.56500  1.000 184.77623 ?  12  HIS E O   1 
ATOM   3047 C CB  . HIS C 3 12  ? 2.44400   33.46300 -1.08400  1.000 182.60948 ?  12  HIS E CB  1 
ATOM   3048 C CG  . HIS C 3 12  ? 1.36700   32.74600 -1.82900  1.000 172.56248 ?  12  HIS E CG  1 
ATOM   3049 N ND1 . HIS C 3 12  ? 0.15800   33.33400 -2.12800  1.000 160.81858 ?  12  HIS E ND1 1 
ATOM   3050 C CD2 . HIS C 3 12  ? 1.31100   31.48900 -2.32700  1.000 172.75671 ?  12  HIS E CD2 1 
ATOM   3051 C CE1 . HIS C 3 12  ? -0.59900  32.46800 -2.77500  1.000 155.16587 ?  12  HIS E CE1 1 
ATOM   3052 N NE2 . HIS C 3 12  ? 0.07900   31.34400 -2.91700  1.000 160.14651 ?  12  HIS E NE2 1 
ATOM   3053 N N   . GLU C 3 13  ? 3.07000   33.32300 -4.22200  1.000 176.76288 ?  13  GLU E N   1 
ATOM   3054 C CA  . GLU C 3 13  ? 2.78600   33.67400 -5.60800  1.000 170.73021 ?  13  GLU E CA  1 
ATOM   3055 C C   . GLU C 3 13  ? 1.53000   32.95900 -6.09300  1.000 159.41563 ?  13  GLU E C   1 
ATOM   3056 O O   . GLU C 3 13  ? 1.28100   31.80500 -5.73000  1.000 159.28298 ?  13  GLU E O   1 
ATOM   3057 C CB  . GLU C 3 13  ? 3.97800   33.33500 -6.52000  1.000 179.33186 ?  13  GLU E CB  1 
ATOM   3058 N N   . VAL C 3 14  ? 0.75200   33.65900 -6.92600  1.000 163.46528 ?  14  VAL E N   1 
ATOM   3059 C CA  . VAL C 3 14  ? -0.46100  33.13800 -7.54700  1.000 151.65915 ?  14  VAL E CA  1 
ATOM   3060 C C   . VAL C 3 14  ? -0.45600  33.47100 -9.03200  1.000 147.91976 ?  14  VAL E C   1 
ATOM   3061 O O   . VAL C 3 14  ? 0.12200   34.47300 -9.46000  1.000 151.91248 ?  14  VAL E O   1 
ATOM   3062 C CB  . VAL C 3 14  ? -1.74100  33.71000 -6.88900  1.000 148.22063 ?  14  VAL E CB  1 
ATOM   3063 C CG1 . VAL C 3 14  ? -2.02100  33.02400 -5.56900  1.000 150.43871 ?  14  VAL E CG1 1 
ATOM   3064 C CG2 . VAL C 3 14  ? -1.62400  35.22100 -6.71900  1.000 149.27507 ?  14  VAL E CG2 1 
ATOM   3065 N N   . VAL C 3 15  ? -1.10000  32.61900 -9.82600  1.000 143.72177 ?  15  VAL E N   1 
ATOM   3066 C CA  . VAL C 3 15  ? -1.32600  32.88700 -11.24500 1.000 139.50424 ?  15  VAL E CA  1 
ATOM   3067 C C   . VAL C 3 15  ? -2.83200  32.97600 -11.45700 1.000 134.11267 ?  15  VAL E C   1 
ATOM   3068 O O   . VAL C 3 15  ? -3.56300  32.03800 -11.11100 1.000 133.69121 ?  15  VAL E O   1 
ATOM   3069 C CB  . VAL C 3 15  ? -0.69300  31.81100 -12.14700 1.000 139.60240 ?  15  VAL E CB  1 
ATOM   3070 C CG1 . VAL C 3 15  ? -0.69400  32.26400 -13.60400 1.000 136.06167 ?  15  VAL E CG1 1 
ATOM   3071 C CG2 . VAL C 3 15  ? 0.73000   31.48800 -11.68000 1.000 148.38123 ?  15  VAL E CG2 1 
ATOM   3072 N N   . LYS C 3 16  ? -3.29300  34.09600 -12.01700 1.000 143.35532 ?  16  LYS E N   1 
ATOM   3073 C CA  . LYS C 3 16  ? -4.71600  34.28000 -12.28100 1.000 141.79114 ?  16  LYS E CA  1 
ATOM   3074 C C   . LYS C 3 16  ? -5.19100  33.27200 -13.32300 1.000 141.16039 ?  16  LYS E C   1 
ATOM   3075 O O   . LYS C 3 16  ? -4.42600  32.84000 -14.18800 1.000 140.52504 ?  16  LYS E O   1 
ATOM   3076 C CB  . LYS C 3 16  ? -5.00400  35.70700 -12.75400 1.000 140.20635 ?  16  LYS E CB  1 
ATOM   3077 N N   . PHE C 3 17  ? -6.47000  32.89000 -13.22800 1.000 129.23815 ?  17  PHE E N   1 
ATOM   3078 C CA  . PHE C 3 17  ? -6.99100  31.84000 -14.10000 1.000 134.24795 ?  17  PHE E CA  1 
ATOM   3079 C C   . PHE C 3 17  ? -6.80000  32.19100 -15.56900 1.000 139.54851 ?  17  PHE E C   1 
ATOM   3080 O O   . PHE C 3 17  ? -6.38200  31.34500 -16.36700 1.000 140.15519 ?  17  PHE E O   1 
ATOM   3081 C CB  . PHE C 3 17  ? -8.46700  31.58100 -13.80000 1.000 139.05703 ?  17  PHE E CB  1 
ATOM   3082 C CG  . PHE C 3 17  ? -9.05400  30.44700 -14.59200 1.000 143.17870 ?  17  PHE E CG  1 
ATOM   3083 C CD1 . PHE C 3 17  ? -9.56900  30.66300 -15.86100 1.000 145.27724 ?  17  PHE E CD1 1 
ATOM   3084 C CD2 . PHE C 3 17  ? -9.07400  29.16300 -14.08000 1.000 140.41757 ?  17  PHE E CD2 1 
ATOM   3085 C CE1 . PHE C 3 17  ? -10.09600 29.62700 -16.59600 1.000 146.03177 ?  17  PHE E CE1 1 
ATOM   3086 C CE2 . PHE C 3 17  ? -9.60600  28.12700 -14.81400 1.000 144.37208 ?  17  PHE E CE2 1 
ATOM   3087 C CZ  . PHE C 3 17  ? -10.11800 28.36200 -16.07500 1.000 147.85780 ?  17  PHE E CZ  1 
ATOM   3088 N N   . MET C 3 18  ? -7.14600  33.42100 -15.95700 1.000 147.92677 ?  18  MET E N   1 
ATOM   3089 C CA  . MET C 3 18  ? -6.92500  33.82900 -17.34100 1.000 145.04017 ?  18  MET E CA  1 
ATOM   3090 C C   . MET C 3 18  ? -5.45700  33.67600 -17.71600 1.000 146.50865 ?  18  MET E C   1 
ATOM   3091 O O   . MET C 3 18  ? -5.12900  33.21600 -18.81900 1.000 145.52661 ?  18  MET E O   1 
ATOM   3092 C CB  . MET C 3 18  ? -7.39900  35.26600 -17.56600 1.000 137.25555 ?  18  MET E CB  1 
ATOM   3093 C CG  . MET C 3 18  ? -8.79400  35.55500 -17.03600 1.000 133.60234 ?  18  MET E CG  1 
ATOM   3094 S SD  . MET C 3 18  ? -10.06600 34.92200 -18.15700 1.000 127.73224 ?  18  MET E SD  1 
ATOM   3095 C CE  . MET C 3 18  ? -9.41700  35.41000 -19.75800 1.000 121.69922 ?  18  MET E CE  1 
ATOM   3096 N N   . ASP C 3 19  ? -4.56100  34.00900 -16.78200 1.000 145.89000 ?  19  ASP E N   1 
ATOM   3097 C CA  . ASP C 3 19  ? -3.12700  33.87800 -17.02700 1.000 138.55066 ?  19  ASP E CA  1 
ATOM   3098 C C   . ASP C 3 19  ? -2.71400  32.41900 -17.16300 1.000 133.97041 ?  19  ASP E C   1 
ATOM   3099 O O   . ASP C 3 19  ? -1.92900  32.07500 -18.05300 1.000 132.16643 ?  19  ASP E O   1 
ATOM   3100 C CB  . ASP C 3 19  ? -2.34000  34.55300 -15.90700 1.000 129.62214 ?  19  ASP E CB  1 
ATOM   3101 C CG  . ASP C 3 19  ? -2.31500  36.05700 -16.04300 1.000 132.68829 ?  19  ASP E CG  1 
ATOM   3102 O OD1 . ASP C 3 19  ? -2.74800  36.57200 -17.09700 1.000 139.10249 ?  19  ASP E OD1 1 
ATOM   3103 O OD2 . ASP C 3 19  ? -1.87100  36.71900 -15.08200 1.000 127.57052 ?  19  ASP E OD2 1 
ATOM   3104 N N   . VAL C 3 20  ? -3.19900  31.55300 -16.26700 1.000 130.50381 ?  20  VAL E N   1 
ATOM   3105 C CA  . VAL C 3 20  ? -2.89200  30.12700 -16.37100 1.000 127.32793 ?  20  VAL E CA  1 
ATOM   3106 C C   . VAL C 3 20  ? -3.33900  29.60500 -17.72700 1.000 135.54985 ?  20  VAL E C   1 
ATOM   3107 O O   . VAL C 3 20  ? -2.58000  28.95100 -18.45000 1.000 133.26368 ?  20  VAL E O   1 
ATOM   3108 C CB  . VAL C 3 20  ? -3.57600  29.33500 -15.24000 1.000 126.15106 ?  20  VAL E CB  1 
ATOM   3109 C CG1 . VAL C 3 20  ? -3.22500  27.85700 -15.34400 1.000 124.49137 ?  20  VAL E CG1 1 
ATOM   3110 C CG2 . VAL C 3 20  ? -3.22700  29.88100 -13.87600 1.000 120.79188 ?  20  VAL E CG2 1 
ATOM   3111 N N   . TYR C 3 21  ? -4.58600  29.90700 -18.08900 1.000 128.81911 ?  21  TYR E N   1 
ATOM   3112 C CA  . TYR C 3 21  ? -5.15400  29.45900 -19.35100 1.000 133.86346 ?  21  TYR E CA  1 
ATOM   3113 C C   . TYR C 3 21  ? -4.30600  29.90400 -20.53400 1.000 132.04282 ?  21  TYR E C   1 
ATOM   3114 O O   . TYR C 3 21  ? -3.98500  29.10500 -21.42000 1.000 131.15210 ?  21  TYR E O   1 
ATOM   3115 C CB  . TYR C 3 21  ? -6.58800  29.99100 -19.45900 1.000 133.98961 ?  21  TYR E CB  1 
ATOM   3116 C CG  . TYR C 3 21  ? -7.45000  29.28100 -20.47300 1.000 130.79885 ?  21  TYR E CG  1 
ATOM   3117 C CD1 . TYR C 3 21  ? -7.11000  29.26900 -21.81300 1.000 125.96779 ?  21  TYR E CD1 1 
ATOM   3118 C CD2 . TYR C 3 21  ? -8.58500  28.59400 -20.08400 1.000 131.79178 ?  21  TYR E CD2 1 
ATOM   3119 C CE1 . TYR C 3 21  ? -7.88400  28.61500 -22.74300 1.000 121.54246 ?  21  TYR E CE1 1 
ATOM   3120 C CE2 . TYR C 3 21  ? -9.36700  27.92900 -21.01400 1.000 127.79002 ?  21  TYR E CE2 1 
ATOM   3121 C CZ  . TYR C 3 21  ? -9.01100  27.94700 -22.34200 1.000 122.29984 ?  21  TYR E CZ  1 
ATOM   3122 O OH  . TYR C 3 21  ? -9.77600  27.29100 -23.27800 1.000 116.86131 ?  21  TYR E OH  1 
ATOM   3123 N N   . GLN C 3 22  ? -3.91600  31.17500 -20.55600 1.000 136.57577 ?  22  GLN E N   1 
ATOM   3124 C CA  . GLN C 3 22  ? -3.18400  31.68100 -21.71000 1.000 133.29703 ?  22  GLN E CA  1 
ATOM   3125 C C   . GLN C 3 22  ? -1.76800  31.11500 -21.76300 1.000 130.02850 ?  22  GLN E C   1 
ATOM   3126 O O   . GLN C 3 22  ? -1.30600  30.67100 -22.82200 1.000 128.00478 ?  22  GLN E O   1 
ATOM   3127 C CB  . GLN C 3 22  ? -3.18100  33.20600 -21.70200 1.000 130.57238 ?  22  GLN E CB  1 
ATOM   3128 C CG  . GLN C 3 22  ? -2.99800  33.76200 -23.08700 1.000 124.04333 ?  22  GLN E CG  1 
ATOM   3129 C CD  . GLN C 3 22  ? -4.31200  33.98100 -23.80400 1.000 117.85914 ?  22  GLN E CD  1 
ATOM   3130 O OE1 . GLN C 3 22  ? -5.36900  33.60000 -23.29700 1.000 118.32581 ?  22  GLN E OE1 1 
ATOM   3131 N NE2 . GLN C 3 22  ? -4.25100  34.54400 -25.01200 1.000 112.06981 ?  22  GLN E NE2 1 
ATOM   3132 N N   . ARG C 3 23  ? -1.06100  31.12200 -20.63200 1.000 141.78985 ?  23  ARG E N   1 
ATOM   3133 C CA  . ARG C 3 23  ? 0.32600   30.67500 -20.63700 1.000 131.48058 ?  23  ARG E CA  1 
ATOM   3134 C C   . ARG C 3 23  ? 0.41800   29.17500 -20.87600 1.000 130.68497 ?  23  ARG E C   1 
ATOM   3135 O O   . ARG C 3 23  ? 1.45000   28.69000 -21.35200 1.000 125.41763 ?  23  ARG E O   1 
ATOM   3136 C CB  . ARG C 3 23  ? 1.02400   31.06200 -19.33200 1.000 122.72513 ?  23  ARG E CB  1 
ATOM   3137 C CG  . ARG C 3 23  ? 1.02700   32.55400 -19.05200 1.000 123.07488 ?  23  ARG E CG  1 
ATOM   3138 C CD  . ARG C 3 23  ? 1.94700   32.91800 -17.89000 1.000 116.86764 ?  23  ARG E CD  1 
ATOM   3139 N NE  . ARG C 3 23  ? 3.18000   32.13200 -17.86200 1.000 113.79082 ?  23  ARG E NE  1 
ATOM   3140 C CZ  . ARG C 3 23  ? 3.66700   31.53800 -16.78000 1.000 113.36786 ?  23  ARG E CZ  1 
ATOM   3141 N NH1 . ARG C 3 23  ? 3.07600   31.65400 -15.60000 1.000 113.84711 ?  23  ARG E NH1 1 
ATOM   3142 N NH2 . ARG C 3 23  ? 4.78400   30.82400 -16.88200 1.000 113.32950 ?  23  ARG E NH2 1 
ATOM   3143 N N   . SER C 3 24  ? -0.62100  28.41700 -20.52700 1.000 121.61126 ?  24  SER E N   1 
ATOM   3144 C CA  . SER C 3 24  ? -0.64800  26.99800 -20.85000 1.000 125.23203 ?  24  SER E CA  1 
ATOM   3145 C C   . SER C 3 24  ? -1.56100  26.65200 -22.02000 1.000 133.21652 ?  24  SER E C   1 
ATOM   3146 O O   . SER C 3 24  ? -1.74600  25.46500 -22.29800 1.000 137.38074 ?  24  SER E O   1 
ATOM   3147 C CB  . SER C 3 24  ? -1.07500  26.18800 -19.62800 1.000 126.67393 ?  24  SER E CB  1 
ATOM   3148 O OG  . SER C 3 24  ? -2.36500  26.58000 -19.20000 1.000 131.52112 ?  24  SER E OG  1 
ATOM   3149 N N   . TYR C 3 25  ? -2.08300  27.63000 -22.75500 1.000 130.88636 ?  25  TYR E N   1 
ATOM   3150 C CA  . TYR C 3 25  ? -2.87200  27.25400 -23.91500 1.000 133.14460 ?  25  TYR E CA  1 
ATOM   3151 C C   . TYR C 3 25  ? -1.92700  26.84200 -25.04000 1.000 131.78887 ?  25  TYR E C   1 
ATOM   3152 O O   . TYR C 3 25  ? -0.74400  27.19800 -25.05800 1.000 128.60944 ?  25  TYR E O   1 
ATOM   3153 C CB  . TYR C 3 25  ? -3.80100  28.39900 -24.36400 1.000 129.32498 ?  25  TYR E CB  1 
ATOM   3154 C CG  . TYR C 3 25  ? -4.75200  28.02500 -25.49100 1.000 126.84554 ?  25  TYR E CG  1 
ATOM   3155 C CD1 . TYR C 3 25  ? -6.00100  27.46600 -25.22400 1.000 127.99248 ?  25  TYR E CD1 1 
ATOM   3156 C CD2 . TYR C 3 25  ? -4.39900  28.22200 -26.81700 1.000 123.16506 ?  25  TYR E CD2 1 
ATOM   3157 C CE1 . TYR C 3 25  ? -6.87100  27.11500 -26.25000 1.000 124.99920 ?  25  TYR E CE1 1 
ATOM   3158 C CE2 . TYR C 3 25  ? -5.25500  27.87100 -27.84600 1.000 120.88705 ?  25  TYR E CE2 1 
ATOM   3159 C CZ  . TYR C 3 25  ? -6.48800  27.31700 -27.56300 1.000 121.55179 ?  25  TYR E CZ  1 
ATOM   3160 O OH  . TYR C 3 25  ? -7.32100  26.97600 -28.61100 1.000 122.79350 ?  25  TYR E OH  1 
ATOM   3161 N N   . CYS C 3 26  ? -2.45700  26.03400 -25.95500 1.000 136.09479 ?  26  CYS E N   1 
ATOM   3162 C CA  . CYS C 3 26  ? -1.73400  25.46600 -27.08900 1.000 135.11655 ?  26  CYS E CA  1 
ATOM   3163 C C   . CYS C 3 26  ? -0.93700  26.54000 -27.82000 1.000 130.52141 ?  26  CYS E C   1 
ATOM   3164 O O   . CYS C 3 26  ? -1.52200  27.44800 -28.41800 1.000 126.73804 ?  26  CYS E O   1 
ATOM   3165 C CB  . CYS C 3 26  ? -2.74700  24.76300 -28.00600 1.000 134.21689 ?  26  CYS E CB  1 
ATOM   3166 S SG  . CYS C 3 26  ? -2.20900  24.15500 -29.60900 1.000 132.23582 ?  26  CYS E SG  1 
ATOM   3167 N N   . HIS C 3 27  ? 0.39300   26.43400 -27.79800 1.000 137.71781 ?  27  HIS E N   1 
ATOM   3168 C CA  . HIS C 3 27  ? 1.24600   27.48000 -28.34800 1.000 131.95128 ?  27  HIS E CA  1 
ATOM   3169 C C   . HIS C 3 27  ? 2.66000   26.93600 -28.50400 1.000 130.20018 ?  27  HIS E C   1 
ATOM   3170 O O   . HIS C 3 27  ? 3.05300   26.01400 -27.77500 1.000 131.84025 ?  27  HIS E O   1 
ATOM   3171 C CB  . HIS C 3 27  ? 1.22000   28.73600 -27.46200 1.000 129.12237 ?  27  HIS E CB  1 
ATOM   3172 C CG  . HIS C 3 27  ? 2.01800   28.61500 -26.21100 1.000 124.27945 ?  27  HIS E CG  1 
ATOM   3173 N ND1 . HIS C 3 27  ? 1.45100   28.28000 -25.00000 1.000 126.41893 ?  27  HIS E ND1 1 
ATOM   3174 C CD2 . HIS C 3 27  ? 3.33400   28.81700 -25.97300 1.000 115.31056 ?  27  HIS E CD2 1 
ATOM   3175 C CE1 . HIS C 3 27  ? 2.39100   28.26300 -24.07400 1.000 119.30873 ?  27  HIS E CE1 1 
ATOM   3176 N NE2 . HIS C 3 27  ? 3.54100   28.58800 -24.63700 1.000 112.92487 ?  27  HIS E NE2 1 
ATOM   3177 N N   . PRO C 3 28  ? 3.42600   27.44400 -29.46800 1.000 127.73514 ?  28  PRO E N   1 
ATOM   3178 C CA  . PRO C 3 28  ? 4.80100   26.94900 -29.65100 1.000 124.50824 ?  28  PRO E CA  1 
ATOM   3179 C C   . PRO C 3 28  ? 5.67000   27.29100 -28.45000 1.000 118.61732 ?  28  PRO E C   1 
ATOM   3180 O O   . PRO C 3 28  ? 5.80900   28.45900 -28.07400 1.000 113.07050 ?  28  PRO E O   1 
ATOM   3181 C CB  . PRO C 3 28  ? 5.26800   27.67900 -30.91000 1.000 119.21084 ?  28  PRO E CB  1 
ATOM   3182 C CG  . PRO C 3 28  ? 4.00700   28.09300 -31.59200 1.000 121.08607 ?  28  PRO E CG  1 
ATOM   3183 C CD  . PRO C 3 28  ? 3.03900   28.40200 -30.51700 1.000 123.90095 ?  28  PRO E CD  1 
ATOM   3184 N N   . ILE C 3 29  ? 6.26900   26.26300 -27.85500 1.000 125.86895 ?  29  ILE E N   1 
ATOM   3185 C CA  . ILE C 3 29  ? 7.12000   26.41000 -26.68300 1.000 124.53063 ?  29  ILE E CA  1 
ATOM   3186 C C   . ILE C 3 29  ? 8.49600   25.81100 -26.97200 1.000 125.85037 ?  29  ILE E C   1 
ATOM   3187 O O   . ILE C 3 29  ? 8.62000   24.82900 -27.71600 1.000 131.75717 ?  29  ILE E O   1 
ATOM   3188 C CB  . ILE C 3 29  ? 6.46800   25.75800 -25.44700 1.000 128.21616 ?  29  ILE E CB  1 
ATOM   3189 C CG1 . ILE C 3 29  ? 7.39100   25.82300 -24.23300 1.000 127.48197 ?  29  ILE E CG1 1 
ATOM   3190 C CG2 . ILE C 3 29  ? 6.06400   24.33000 -25.75000 1.000 132.83176 ?  29  ILE E CG2 1 
ATOM   3191 C CD1 . ILE C 3 29  ? 7.72100   27.24300 -23.80600 1.000 123.94380 ?  29  ILE E CD1 1 
ATOM   3192 N N   . GLU C 3 30  ? 9.53300   26.46000 -26.43900 1.000 123.43752 ?  30  GLU E N   1 
ATOM   3193 C CA  . GLU C 3 30  ? 10.88800  25.91500 -26.43700 1.000 127.93286 ?  30  GLU E CA  1 
ATOM   3194 C C   . GLU C 3 30  ? 10.92000  24.53600 -25.78500 1.000 135.36679 ?  30  GLU E C   1 
ATOM   3195 O O   . GLU C 3 30  ? 10.58900  24.39300 -24.60400 1.000 134.38663 ?  30  GLU E O   1 
ATOM   3196 C CB  . GLU C 3 30  ? 11.81800  26.86600 -25.68700 1.000 123.94756 ?  30  GLU E CB  1 
ATOM   3197 C CG  . GLU C 3 30  ? 13.25200  26.38700 -25.54800 1.000 127.86363 ?  30  GLU E CG  1 
ATOM   3198 C CD  . GLU C 3 30  ? 14.25300  27.50300 -25.78800 1.000 123.09743 ?  30  GLU E CD  1 
ATOM   3199 O OE1 . GLU C 3 30  ? 14.50200  27.84000 -26.96300 1.000 120.68502 ?  30  GLU E OE1 1 
ATOM   3200 O OE2 . GLU C 3 30  ? 14.78400  28.04800 -24.79400 1.000 121.30928 ?  30  GLU E OE2 1 
ATOM   3201 N N   . THR C 3 31  ? 11.30500  23.52500 -26.56000 1.000 122.63674 ?  31  THR E N   1 
ATOM   3202 C CA  . THR C 3 31  ? 11.44000  22.14800 -26.10700 1.000 129.25956 ?  31  THR E CA  1 
ATOM   3203 C C   . THR C 3 31  ? 12.83400  21.65700 -26.46800 1.000 133.90508 ?  31  THR E C   1 
ATOM   3204 O O   . THR C 3 31  ? 13.25300  21.78100 -27.62100 1.000 136.81240 ?  31  THR E O   1 
ATOM   3205 C CB  . THR C 3 31  ? 10.38500  21.24800 -26.75600 1.000 135.18525 ?  31  THR E CB  1 
ATOM   3206 O OG1 . THR C 3 31  ? 9.07300   21.70800 -26.40300 1.000 130.42114 ?  31  THR E OG1 1 
ATOM   3207 C CG2 . THR C 3 31  ? 10.56500  19.80800 -26.31100 1.000 141.27013 ?  31  THR E CG2 1 
ATOM   3208 N N   . LEU C 3 32  ? 13.56300  21.12600 -25.49100 1.000 129.84710 ?  32  LEU E N   1 
ATOM   3209 C CA  . LEU C 3 32  ? 14.89400  20.59000 -25.75800 1.000 132.89801 ?  32  LEU E CA  1 
ATOM   3210 C C   . LEU C 3 32  ? 14.78200  19.15600 -26.27000 1.000 139.82611 ?  32  LEU E C   1 
ATOM   3211 O O   . LEU C 3 32  ? 14.18600  18.29500 -25.61400 1.000 140.79214 ?  32  LEU E O   1 
ATOM   3212 C CB  . LEU C 3 32  ? 15.76100  20.68100 -24.50500 1.000 128.56809 ?  32  LEU E CB  1 
ATOM   3213 C CG  . LEU C 3 32  ? 15.64900  22.05000 -23.82800 1.000 121.71400 ?  32  LEU E CG  1 
ATOM   3214 C CD1 . LEU C 3 32  ? 16.10300  22.00600 -22.37800 1.000 119.04014 ?  32  LEU E CD1 1 
ATOM   3215 C CD2 . LEU C 3 32  ? 16.46900  23.06200 -24.62200 1.000 119.67752 ?  32  LEU E CD2 1 
ATOM   3216 N N   . VAL C 3 33  ? 15.36900  18.90000 -27.44100 1.000 127.52234 ?  33  VAL E N   1 
ATOM   3217 C CA  . VAL C 3 33  ? 15.18000  17.65500 -28.17700 1.000 133.77262 ?  33  VAL E CA  1 
ATOM   3218 C C   . VAL C 3 33  ? 16.54500  17.04900 -28.47700 1.000 133.58754 ?  33  VAL E C   1 
ATOM   3219 O O   . VAL C 3 33  ? 17.41100  17.72400 -29.04100 1.000 132.26724 ?  33  VAL E O   1 
ATOM   3220 C CB  . VAL C 3 33  ? 14.39700  17.90800 -29.48000 1.000 139.25007 ?  33  VAL E CB  1 
ATOM   3221 C CG1 . VAL C 3 33  ? 14.35000  16.66600 -30.35500 1.000 145.19544 ?  33  VAL E CG1 1 
ATOM   3222 C CG2 . VAL C 3 33  ? 12.99800  18.43700 -29.16500 1.000 137.80921 ?  33  VAL E CG2 1 
ATOM   3223 N N   . ASP C 3 34  ? 16.73300  15.78000 -28.12000 1.000 147.48781 ?  34  ASP E N   1 
ATOM   3224 C CA  . ASP C 3 34  ? 17.98100  15.10500 -28.45200 1.000 145.84826 ?  34  ASP E CA  1 
ATOM   3225 C C   . ASP C 3 34  ? 18.08500  14.95600 -29.96800 1.000 149.25226 ?  34  ASP E C   1 
ATOM   3226 O O   . ASP C 3 34  ? 17.11900  14.56900 -30.63400 1.000 153.88627 ?  34  ASP E O   1 
ATOM   3227 C CB  . ASP C 3 34  ? 18.05100  13.73800 -27.76900 1.000 144.35103 ?  34  ASP E CB  1 
ATOM   3228 C CG  . ASP C 3 34  ? 19.38800  13.03700 -27.97200 1.000 140.80960 ?  34  ASP E CG  1 
ATOM   3229 O OD1 . ASP C 3 34  ? 20.18700  13.46300 -28.83200 1.000 140.39190 ?  34  ASP E OD1 1 
ATOM   3230 O OD2 . ASP C 3 34  ? 19.63500  12.03900 -27.26200 1.000 137.56820 ?  34  ASP E OD2 1 
ATOM   3231 N N   . ILE C 3 35  ? 19.27500  15.24200 -30.50600 1.000 142.77437 ?  35  ILE E N   1 
ATOM   3232 C CA  . ILE C 3 35  ? 19.48900  15.24500 -31.95300 1.000 142.33335 ?  35  ILE E CA  1 
ATOM   3233 C C   . ILE C 3 35  ? 19.19800  13.88100 -32.56100 1.000 143.71054 ?  35  ILE E C   1 
ATOM   3234 O O   . ILE C 3 35  ? 18.82500  13.78700 -33.73800 1.000 143.07603 ?  35  ILE E O   1 
ATOM   3235 C CB  . ILE C 3 35  ? 20.92800  15.71200 -32.26600 1.000 135.61150 ?  35  ILE E CB  1 
ATOM   3236 C CG1 . ILE C 3 35  ? 21.25300  16.99500 -31.49800 1.000 134.19113 ?  35  ILE E CG1 1 
ATOM   3237 C CG2 . ILE C 3 35  ? 21.14900  15.88900 -33.76600 1.000 129.78661 ?  35  ILE E CG2 1 
ATOM   3238 C CD1 . ILE C 3 35  ? 22.63100  17.54000 -31.78600 1.000 127.59858 ?  35  ILE E CD1 1 
ATOM   3239 N N   . PHE C 3 36  ? 19.36700  12.80600 -31.78600 1.000 148.12543 ?  36  PHE E N   1 
ATOM   3240 C CA  . PHE C 3 36  ? 19.02700  11.48200 -32.29700 1.000 149.24614 ?  36  PHE E CA  1 
ATOM   3241 C C   . PHE C 3 36  ? 17.58500  11.41800 -32.77000 1.000 155.21186 ?  36  PHE E C   1 
ATOM   3242 O O   . PHE C 3 36  ? 17.29600  10.82900 -33.81800 1.000 155.52256 ?  36  PHE E O   1 
ATOM   3243 C CB  . PHE C 3 36  ? 19.23500  10.40900 -31.23600 1.000 147.44578 ?  36  PHE E CB  1 
ATOM   3244 C CG  . PHE C 3 36  ? 19.31100  9.02800  -31.81000 1.000 146.26890 ?  36  PHE E CG  1 
ATOM   3245 C CD1 . PHE C 3 36  ? 20.16700  8.74700  -32.86100 1.000 142.31518 ?  36  PHE E CD1 1 
ATOM   3246 C CD2 . PHE C 3 36  ? 18.45300  8.03500  -31.36600 1.000 149.02121 ?  36  PHE E CD2 1 
ATOM   3247 C CE1 . PHE C 3 36  ? 20.22700  7.48000  -33.40600 1.000 141.23640 ?  36  PHE E CE1 1 
ATOM   3248 C CE2 . PHE C 3 36  ? 18.50400  6.77100  -31.91200 1.000 148.40485 ?  36  PHE E CE2 1 
ATOM   3249 C CZ  . PHE C 3 36  ? 19.38900  6.49500  -32.93800 1.000 144.70254 ?  36  PHE E CZ  1 
ATOM   3250 N N   . GLN C 3 37  ? 16.66700  12.02500 -32.01200 1.000 153.25268 ?  37  GLN E N   1 
ATOM   3251 C CA  . GLN C 3 37  ? 15.24500  11.90400 -32.31700 1.000 158.89820 ?  37  GLN E CA  1 
ATOM   3252 C C   . GLN C 3 37  ? 14.91600  12.41800 -33.70900 1.000 160.03284 ?  37  GLN E C   1 
ATOM   3253 O O   . GLN C 3 37  ? 14.00000  11.89900 -34.35600 1.000 163.34410 ?  37  GLN E O   1 
ATOM   3254 C CB  . GLN C 3 37  ? 14.41800  12.64500 -31.26700 1.000 160.29345 ?  37  GLN E CB  1 
ATOM   3255 C CG  . GLN C 3 37  ? 14.95300  12.49800 -29.85100 1.000 155.51292 ?  37  GLN E CG  1 
ATOM   3256 C CD  . GLN C 3 37  ? 14.96400  11.05400 -29.38400 1.000 154.08146 ?  37  GLN E CD  1 
ATOM   3257 O OE1 . GLN C 3 37  ? 15.99700  10.38000 -29.42400 1.000 150.35459 ?  37  GLN E OE1 1 
ATOM   3258 N NE2 . GLN C 3 37  ? 13.80500  10.56400 -28.95500 1.000 156.08236 ?  37  GLN E NE2 1 
ATOM   3259 N N   . GLU C 3 38  ? 15.64100  13.42400 -34.19400 1.000 157.11879 ?  38  GLU E N   1 
ATOM   3260 C CA  . GLU C 3 38  ? 15.31200  13.96700 -35.50600 1.000 152.77889 ?  38  GLU E CA  1 
ATOM   3261 C C   . GLU C 3 38  ? 16.13400  13.31700 -36.61400 1.000 144.38767 ?  38  GLU E C   1 
ATOM   3262 O O   . GLU C 3 38  ? 15.58400  12.91600 -37.64400 1.000 141.85158 ?  38  GLU E O   1 
ATOM   3263 C CB  . GLU C 3 38  ? 15.51600  15.48500 -35.51600 1.000 147.17163 ?  38  GLU E CB  1 
ATOM   3264 C CG  . GLU C 3 38  ? 14.95300  16.18300 -34.29300 1.000 154.85743 ?  38  GLU E CG  1 
ATOM   3265 C CD  . GLU C 3 38  ? 13.46900  15.93000 -34.11300 1.000 163.21111 ?  38  GLU E CD  1 
ATOM   3266 O OE1 . GLU C 3 38  ? 13.10200  14.93100 -33.45800 1.000 167.53747 ?  38  GLU E OE1 1 
ATOM   3267 O OE2 . GLU C 3 38  ? 12.66600  16.73600 -34.62400 1.000 160.56111 ?  38  GLU E OE2 1 
ATOM   3268 N N   . TYR C 3 39  ? 17.44800  13.19300 -36.41200 1.000 138.55305 ?  39  TYR E N   1 
ATOM   3269 C CA  . TYR C 3 39  ? 18.36500  12.61900 -37.39500 1.000 144.84071 ?  39  TYR E CA  1 
ATOM   3270 C C   . TYR C 3 39  ? 19.00000  11.37900 -36.78100 1.000 140.98863 ?  39  TYR E C   1 
ATOM   3271 O O   . TYR C 3 39  ? 20.14600  11.43500 -36.30800 1.000 151.81568 ?  39  TYR E O   1 
ATOM   3272 C CB  . TYR C 3 39  ? 19.44300  13.62100 -37.80400 1.000 163.74864 ?  39  TYR E CB  1 
ATOM   3273 C CG  . TYR C 3 39  ? 18.97200  14.68300 -38.76800 1.000 168.48697 ?  39  TYR E CG  1 
ATOM   3274 C CD1 . TYR C 3 39  ? 17.62800  14.82800 -39.06200 1.000 157.09348 ?  39  TYR E CD1 1 
ATOM   3275 C CD2 . TYR C 3 39  ? 19.87100  15.55000 -39.37100 1.000 182.95335 ?  39  TYR E CD2 1 
ATOM   3276 C CE1 . TYR C 3 39  ? 17.18900  15.79500 -39.93400 1.000 162.89363 ?  39  TYR E CE1 1 
ATOM   3277 C CE2 . TYR C 3 39  ? 19.44200  16.52200 -40.24500 1.000 186.82660 ?  39  TYR E CE2 1 
ATOM   3278 C CZ  . TYR C 3 39  ? 18.09900  16.64000 -40.52300 1.000 176.80335 ?  39  TYR E CZ  1 
ATOM   3279 O OH  . TYR C 3 39  ? 17.66000  17.60800 -41.39400 1.000 180.95148 ?  39  TYR E OH  1 
ATOM   3280 N N   . PRO C 3 40  ? 18.29400  10.24200 -36.76000 1.000 161.03924 ?  40  PRO E N   1 
ATOM   3281 C CA  . PRO C 3 40  ? 18.86200  9.06900  -36.08200 1.000 154.77945 ?  40  PRO E CA  1 
ATOM   3282 C C   . PRO C 3 40  ? 19.92300  8.34800  -36.90300 1.000 165.04319 ?  40  PRO E C   1 
ATOM   3283 O O   . PRO C 3 40  ? 20.05300  7.12100  -36.83500 1.000 156.06975 ?  40  PRO E O   1 
ATOM   3284 C CB  . PRO C 3 40  ? 17.63600  8.17900  -35.85200 1.000 135.67760 ?  40  PRO E CB  1 
ATOM   3285 C CG  . PRO C 3 40  ? 16.71500  8.52200  -36.98100 1.000 135.46050 ?  40  PRO E CG  1 
ATOM   3286 C CD  . PRO C 3 40  ? 16.97000  9.96600  -37.34700 1.000 149.99146 ?  40  PRO E CD  1 
ATOM   3287 N N   . ASP C 3 41  ? 20.70300  9.11300  -37.65800 1.000 140.41368 ?  41  ASP E N   1 
ATOM   3288 C CA  . ASP C 3 41  ? 21.78600  8.60600  -38.48300 1.000 152.32686 ?  41  ASP E CA  1 
ATOM   3289 C C   . ASP C 3 41  ? 23.10700  8.77300  -37.74200 1.000 164.46020 ?  41  ASP E C   1 
ATOM   3290 O O   . ASP C 3 41  ? 23.21000  9.54700  -36.78500 1.000 166.33726 ?  41  ASP E O   1 
ATOM   3291 C CB  . ASP C 3 41  ? 21.83500  9.32800  -39.83200 1.000 162.27869 ?  41  ASP E CB  1 
ATOM   3292 N N   . GLU C 3 42  ? 24.12400  8.04200  -38.20200 1.000 149.39837 ?  42  GLU E N   1 
ATOM   3293 C CA  . GLU C 3 42  ? 25.49900  8.18600  -37.71800 1.000 159.67993 ?  42  GLU E CA  1 
ATOM   3294 C C   . GLU C 3 42  ? 25.58800  7.96100  -36.20500 1.000 149.91131 ?  42  GLU E C   1 
ATOM   3295 O O   . GLU C 3 42  ? 25.88200  8.86400  -35.41800 1.000 149.92139 ?  42  GLU E O   1 
ATOM   3296 C CB  . GLU C 3 42  ? 26.07200  9.55300  -38.11000 1.000 168.95007 ?  42  GLU E CB  1 
ATOM   3297 N N   . ILE C 3 43  ? 25.31900  6.71200  -35.82000 1.000 161.77215 ?  43  ILE E N   1 
ATOM   3298 C CA  . ILE C 3 43  ? 25.33100  6.35600  -34.40500 1.000 143.37196 ?  43  ILE E CA  1 
ATOM   3299 C C   . ILE C 3 43  ? 26.74300  6.46500  -33.83600 1.000 143.31765 ?  43  ILE E C   1 
ATOM   3300 O O   . ILE C 3 43  ? 26.94500  7.00500  -32.74100 1.000 138.63424 ?  43  ILE E O   1 
ATOM   3301 C CB  . ILE C 3 43  ? 24.74900  4.94400  -34.20900 1.000 119.15081 ?  43  ILE E CB  1 
ATOM   3302 N N   . GLU C 3 44  ? 27.74000  5.95900  -34.56500 1.000 157.15133 ?  44  GLU E N   1 
ATOM   3303 C CA  . GLU C 3 44  ? 29.13900  5.99900  -34.13400 1.000 145.44855 ?  44  GLU E CA  1 
ATOM   3304 C C   . GLU C 3 44  ? 29.74400  7.37700  -34.42600 1.000 157.65577 ?  44  GLU E C   1 
ATOM   3305 O O   . GLU C 3 44  ? 30.72000  7.52500  -35.15900 1.000 157.59767 ?  44  GLU E O   1 
ATOM   3306 C CB  . GLU C 3 44  ? 29.93000  4.88500  -34.80700 1.000 135.92675 ?  44  GLU E CB  1 
ATOM   3307 N N   . TYR C 3 45  ? 29.12900  8.39800  -33.83000 1.000 145.34202 ?  45  TYR E N   1 
ATOM   3308 C CA  . TYR C 3 45  ? 29.50200  9.79200  -34.06500 1.000 152.97444 ?  45  TYR E CA  1 
ATOM   3309 C C   . TYR C 3 45  ? 28.91200  10.61000 -32.92900 1.000 150.82859 ?  45  TYR E C   1 
ATOM   3310 O O   . TYR C 3 45  ? 27.69300  10.62300 -32.76100 1.000 156.58061 ?  45  TYR E O   1 
ATOM   3311 C CB  . TYR C 3 45  ? 28.97100  10.26800 -35.41500 1.000 169.34477 ?  45  TYR E CB  1 
ATOM   3312 C CG  . TYR C 3 45  ? 30.02400  10.41000 -36.48600 1.000 169.33672 ?  45  TYR E CG  1 
ATOM   3313 C CD1 . TYR C 3 45  ? 30.98000  11.41300 -36.42200 1.000 162.66429 ?  45  TYR E CD1 1 
ATOM   3314 C CD2 . TYR C 3 45  ? 30.06900  9.52600  -37.55700 1.000 174.73534 ?  45  TYR E CD2 1 
ATOM   3315 C CE1 . TYR C 3 45  ? 31.94500  11.54100 -37.40700 1.000 161.77630 ?  45  TYR E CE1 1 
ATOM   3316 C CE2 . TYR C 3 45  ? 31.02700  9.64300  -38.54200 1.000 174.55542 ?  45  TYR E CE2 1 
ATOM   3317 C CZ  . TYR C 3 45  ? 31.96600  10.65300 -38.46300 1.000 168.20869 ?  45  TYR E CZ  1 
ATOM   3318 O OH  . TYR C 3 45  ? 32.92600  10.77400 -39.44300 1.000 168.22598 ?  45  TYR E OH  1 
ATOM   3319 N N   . ILE C 3 46  ? 29.74800  11.27000 -32.14300 1.000 146.21576 ?  46  ILE E N   1 
ATOM   3320 C CA  . ILE C 3 46  ? 29.24500  12.05300 -31.01700 1.000 152.83299 ?  46  ILE E CA  1 
ATOM   3321 C C   . ILE C 3 46  ? 28.81800  13.44400 -31.47100 1.000 151.28385 ?  46  ILE E C   1 
ATOM   3322 O O   . ILE C 3 46  ? 29.44600  14.04600 -32.34000 1.000 144.96311 ?  46  ILE E O   1 
ATOM   3323 C CB  . ILE C 3 46  ? 30.31200  12.13000 -29.90900 1.000 157.03034 ?  46  ILE E CB  1 
ATOM   3324 C CG1 . ILE C 3 46  ? 30.75600  10.72100 -29.50600 1.000 157.27893 ?  46  ILE E CG1 1 
ATOM   3325 C CG2 . ILE C 3 46  ? 29.81700  12.92600 -28.70600 1.000 160.53747 ?  46  ILE E CG2 1 
ATOM   3326 C CD1 . ILE C 3 46  ? 29.62600  9.78900  -29.12600 1.000 157.92451 ?  46  ILE E CD1 1 
ATOM   3327 N N   . PHE C 3 47  ? 27.71000  13.93800 -30.92400 1.000 150.43607 ?  47  PHE E N   1 
ATOM   3328 C CA  . PHE C 3 47  ? 27.27500  15.31100 -31.15000 1.000 149.01661 ?  47  PHE E CA  1 
ATOM   3329 C C   . PHE C 3 47  ? 27.31700  16.04700 -29.81800 1.000 148.56419 ?  47  PHE E C   1 
ATOM   3330 O O   . PHE C 3 47  ? 26.75100  15.56800 -28.82800 1.000 147.47670 ?  47  PHE E O   1 
ATOM   3331 C CB  . PHE C 3 47  ? 25.85700  15.39200 -31.71800 1.000 149.62058 ?  47  PHE E CB  1 
ATOM   3332 C CG  . PHE C 3 47  ? 25.67800  14.76400 -33.07400 1.000 143.15849 ?  47  PHE E CG  1 
ATOM   3333 C CD1 . PHE C 3 47  ? 26.74000  14.54700 -33.93600 1.000 135.20497 ?  47  PHE E CD1 1 
ATOM   3334 C CD2 . PHE C 3 47  ? 24.40800  14.41500 -33.49000 1.000 145.18122 ?  47  PHE E CD2 1 
ATOM   3335 C CE1 . PHE C 3 47  ? 26.52300  13.96900 -35.18100 1.000 129.08741 ?  47  PHE E CE1 1 
ATOM   3336 C CE2 . PHE C 3 47  ? 24.18800  13.84800 -34.72200 1.000 139.73844 ?  47  PHE E CE2 1 
ATOM   3337 C CZ  . PHE C 3 47  ? 25.24100  13.62300 -35.57100 1.000 131.47631 ?  47  PHE E CZ  1 
ATOM   3338 N N   . LYS C 3 48  ? 27.96700  17.21100 -29.79800 1.000 142.26681 ?  48  LYS E N   1 
ATOM   3339 C CA  . LYS C 3 48  ? 27.95800  18.10000 -28.64000 1.000 137.04479 ?  48  LYS E CA  1 
ATOM   3340 C C   . LYS C 3 48  ? 27.42800  19.45800 -29.08700 1.000 132.11887 ?  48  LYS E C   1 
ATOM   3341 O O   . LYS C 3 48  ? 28.03100  20.08700 -29.97100 1.000 128.59634 ?  48  LYS E O   1 
ATOM   3342 C CB  . LYS C 3 48  ? 29.35600  18.23700 -28.02600 1.000 135.37628 ?  48  LYS E CB  1 
ATOM   3343 N N   . PRO C 3 49  ? 26.33100  19.96900 -28.52600 1.000 124.13432 ?  49  PRO E N   1 
ATOM   3344 C CA  . PRO C 3 49  ? 25.50700  19.37900 -27.47500 1.000 124.86882 ?  49  PRO E CA  1 
ATOM   3345 C C   . PRO C 3 49  ? 24.70800  18.17800 -27.95900 1.000 130.23627 ?  49  PRO E C   1 
ATOM   3346 O O   . PRO C 3 49  ? 24.54300  17.95800 -29.15500 1.000 134.40665 ?  49  PRO E O   1 
ATOM   3347 C CB  . PRO C 3 49  ? 24.59900  20.54900 -27.07400 1.000 120.25520 ?  49  PRO E CB  1 
ATOM   3348 C CG  . PRO C 3 49  ? 24.37000  21.26100 -28.36600 1.000 119.24428 ?  49  PRO E CG  1 
ATOM   3349 C CD  . PRO C 3 49  ? 25.68000  21.15600 -29.11500 1.000 119.26032 ?  49  PRO E CD  1 
ATOM   3350 N N   . SER C 3 50  ? 24.22000  17.36500 -27.02400 1.000 125.57647 ?  50  SER E N   1 
ATOM   3351 C CA  . SER C 3 50  ? 23.41300  16.21200 -27.39700 1.000 128.93286 ?  50  SER E CA  1 
ATOM   3352 C C   . SER C 3 50  ? 22.00900  16.62400 -27.81500 1.000 130.01660 ?  50  SER E C   1 
ATOM   3353 O O   . SER C 3 50  ? 21.37700  15.92400 -28.61300 1.000 134.58007 ?  50  SER E O   1 
ATOM   3354 C CB  . SER C 3 50  ? 23.35600  15.21100 -26.24500 1.000 124.99475 ?  50  SER E CB  1 
ATOM   3355 O OG  . SER C 3 50  ? 22.64200  15.73400 -25.14200 1.000 118.46884 ?  50  SER E OG  1 
ATOM   3356 N N   . CYS C 3 51  ? 21.50100  17.73400 -27.28500 1.000 122.89899 ?  51  CYS E N   1 
ATOM   3357 C CA  . CYS C 3 51  ? 20.17200  18.21700 -27.62500 1.000 124.14150 ?  51  CYS E CA  1 
ATOM   3358 C C   . CYS C 3 51  ? 20.27100  19.58900 -28.27100 1.000 123.30344 ?  51  CYS E C   1 
ATOM   3359 O O   . CYS C 3 51  ? 21.31400  20.24700 -28.25400 1.000 119.45193 ?  51  CYS E O   1 
ATOM   3360 C CB  . CYS C 3 51  ? 19.24300  18.31300 -26.40600 1.000 116.60905 ?  51  CYS E CB  1 
ATOM   3361 S SG  . CYS C 3 51  ? 19.96600  17.98200 -24.80700 1.000 108.54210 ?  51  CYS E SG  1 
ATOM   3362 N N   . VAL C 3 52  ? 19.15700  19.99300 -28.86800 1.000 125.28957 ?  52  VAL E N   1 
ATOM   3363 C CA  . VAL C 3 52  ? 19.00500  21.30400 -29.49000 1.000 119.95980 ?  52  VAL E CA  1 
ATOM   3364 C C   . VAL C 3 52  ? 17.69900  21.90400 -28.97800 1.000 117.33662 ?  52  VAL E C   1 
ATOM   3365 O O   . VAL C 3 52  ? 16.75600  21.16100 -28.66700 1.000 120.53773 ?  52  VAL E O   1 
ATOM   3366 C CB  . VAL C 3 52  ? 19.02100  21.21100 -31.02600 1.000 120.82468 ?  52  VAL E CB  1 
ATOM   3367 C CG1 . VAL C 3 52  ? 20.33400  20.63200 -31.50300 1.000 121.89181 ?  52  VAL E CG1 1 
ATOM   3368 C CG2 . VAL C 3 52  ? 17.87300  20.36500 -31.52600 1.000 128.59442 ?  52  VAL E CG2 1 
ATOM   3369 N N   . PRO C 3 53  ? 17.61500  23.22700 -28.83100 1.000 127.64609 ?  53  PRO E N   1 
ATOM   3370 C CA  . PRO C 3 53  ? 16.35500  23.85700 -28.41500 1.000 124.17754 ?  53  PRO E CA  1 
ATOM   3371 C C   . PRO C 3 53  ? 15.46800  24.12600 -29.62000 1.000 124.86380 ?  53  PRO E C   1 
ATOM   3372 O O   . PRO C 3 53  ? 15.89200  24.81400 -30.55400 1.000 119.10279 ?  53  PRO E O   1 
ATOM   3373 C CB  . PRO C 3 53  ? 16.81900  25.15400 -27.74400 1.000 115.15692 ?  53  PRO E CB  1 
ATOM   3374 C CG  . PRO C 3 53  ? 18.08400  25.48100 -28.44800 1.000 112.57478 ?  53  PRO E CG  1 
ATOM   3375 C CD  . PRO C 3 53  ? 18.73400  24.18600 -28.83900 1.000 120.38054 ?  53  PRO E CD  1 
ATOM   3376 N N   . LEU C 3 54  ? 14.25200  23.58000 -29.63600 1.000 120.68579 ?  54  LEU E N   1 
ATOM   3377 C CA  . LEU C 3 54  ? 13.37400  23.66600 -30.79200 1.000 121.80770 ?  54  LEU E CA  1 
ATOM   3378 C C   . LEU C 3 54  ? 12.00300  24.18200 -30.38700 1.000 119.38179 ?  54  LEU E C   1 
ATOM   3379 O O   . LEU C 3 54  ? 11.43900  23.74300 -29.38200 1.000 120.72450 ?  54  LEU E O   1 
ATOM   3380 C CB  . LEU C 3 54  ? 13.22200  22.30300 -31.47200 1.000 130.89336 ?  54  LEU E CB  1 
ATOM   3381 C CG  . LEU C 3 54  ? 14.50000  21.58800 -31.89800 1.000 134.78527 ?  54  LEU E CG  1 
ATOM   3382 C CD1 . LEU C 3 54  ? 14.20500  20.15000 -32.29600 1.000 145.26315 ?  54  LEU E CD1 1 
ATOM   3383 C CD2 . LEU C 3 54  ? 15.14800  22.33100 -33.04800 1.000 126.58748 ?  54  LEU E CD2 1 
ATOM   3384 N N   . MET C 3 55  ? 11.47000  25.10800 -31.17200 1.000 124.16910 ?  55  MET E N   1 
ATOM   3385 C CA  . MET C 3 55  ? 10.09800  25.56500 -30.98300 1.000 124.06266 ?  55  MET E CA  1 
ATOM   3386 C C   . MET C 3 55  ? 9.19400   24.40500 -31.37000 1.000 132.17077 ?  55  MET E C   1 
ATOM   3387 O O   . MET C 3 55  ? 8.87500   24.22300 -32.54900 1.000 134.76721 ?  55  MET E O   1 
ATOM   3388 C CB  . MET C 3 55  ? 9.82500   26.77100 -31.87600 1.000 119.08310 ?  55  MET E CB  1 
ATOM   3389 C CG  . MET C 3 55  ? 10.36000  28.10200 -31.38000 1.000 113.22589 ?  55  MET E CG  1 
ATOM   3390 S SD  . MET C 3 55  ? 9.96800   28.48100 -29.66100 1.000 115.11900 ?  55  MET E SD  1 
ATOM   3391 C CE  . MET C 3 55  ? 8.32000   29.15900 -29.85600 1.000 120.82511 ?  55  MET E CE  1 
ATOM   3392 N N   . ARG C 3 56  ? 8.77800   23.60200 -30.39500 1.000 126.46698 ?  56  ARG E N   1 
ATOM   3393 C CA  . ARG C 3 56  ? 7.84900   22.52400 -30.69100 1.000 134.13733 ?  56  ARG E CA  1 
ATOM   3394 C C   . ARG C 3 56  ? 6.47900   22.88700 -30.13800 1.000 133.43038 ?  56  ARG E C   1 
ATOM   3395 O O   . ARG C 3 56  ? 6.34800   23.75900 -29.27400 1.000 128.06912 ?  56  ARG E O   1 
ATOM   3396 C CB  . ARG C 3 56  ? 8.32700   21.19100 -30.10100 1.000 137.73391 ?  56  ARG E CB  1 
ATOM   3397 N N   . CYS C 3 57  ? 5.45200   22.20800 -30.64100 1.000 129.24663 ?  57  CYS E N   1 
ATOM   3398 C CA  . CYS C 3 57  ? 4.11400   22.48000 -30.14400 1.000 133.23761 ?  57  CYS E CA  1 
ATOM   3399 C C   . CYS C 3 57  ? 3.95500   21.92800 -28.73000 1.000 140.48604 ?  57  CYS E C   1 
ATOM   3400 O O   . CYS C 3 57  ? 4.76000   21.12900 -28.24100 1.000 143.35966 ?  57  CYS E O   1 
ATOM   3401 C CB  . CYS C 3 57  ? 3.05100   21.91000 -31.08500 1.000 133.89985 ?  57  CYS E CB  1 
ATOM   3402 S SG  . CYS C 3 57  ? 2.71200   22.92500 -32.57100 1.000 121.24781 ?  57  CYS E SG  1 
ATOM   3403 N N   . GLY C 3 58  ? 2.88700   22.36200 -28.07700 1.000 140.62581 ?  58  GLY E N   1 
ATOM   3404 C CA  . GLY C 3 58  ? 2.62200   21.95600 -26.71600 1.000 143.31889 ?  58  GLY E CA  1 
ATOM   3405 C C   . GLY C 3 58  ? 1.68800   22.91500 -26.01300 1.000 139.49067 ?  58  GLY E C   1 
ATOM   3406 O O   . GLY C 3 58  ? 1.66500   24.11000 -26.31600 1.000 131.63564 ?  58  GLY E O   1 
ATOM   3407 N N   . GLY C 3 59  ? 0.91300   22.40300 -25.06600 1.000 130.18759 ?  59  GLY E N   1 
ATOM   3408 C CA  . GLY C 3 59  ? -0.02800  23.23400 -24.34800 1.000 127.33877 ?  59  GLY E CA  1 
ATOM   3409 C C   . GLY C 3 59  ? -1.40700  22.62300 -24.40900 1.000 136.81968 ?  59  GLY E C   1 
ATOM   3410 O O   . GLY C 3 59  ? -1.67500  21.78400 -25.27500 1.000 143.65553 ?  59  GLY E O   1 
ATOM   3411 N N   . CYS C 3 60  ? -2.29600  23.03700 -23.51300 1.000 126.68216 ?  60  CYS E N   1 
ATOM   3412 C CA  . CYS C 3 60  ? -3.62200  22.44800 -23.47700 1.000 136.20846 ?  60  CYS E CA  1 
ATOM   3413 C C   . CYS C 3 60  ? -4.45300  22.95900 -24.64500 1.000 140.86408 ?  60  CYS E C   1 
ATOM   3414 O O   . CYS C 3 60  ? -4.45900  24.15500 -24.95700 1.000 133.83440 ?  60  CYS E O   1 
ATOM   3415 C CB  . CYS C 3 60  ? -4.33500  22.78500 -22.16800 1.000 135.00765 ?  60  CYS E CB  1 
ATOM   3416 S SG  . CYS C 3 60  ? -3.31900  23.22500 -20.74200 1.000 126.87198 ?  60  CYS E SG  1 
ATOM   3417 N N   . CYS C 3 61  ? -5.15800  22.03600 -25.29600 1.000 126.42818 ?  61  CYS E N   1 
ATOM   3418 C CA  . CYS C 3 61  ? -6.21200  22.40300 -26.22900 1.000 132.84174 ?  61  CYS E CA  1 
ATOM   3419 C C   . CYS C 3 61  ? -7.54500  22.59200 -25.51700 1.000 138.21174 ?  61  CYS E C   1 
ATOM   3420 O O   . CYS C 3 61  ? -8.48300  23.13800 -26.10700 1.000 141.97092 ?  61  CYS E O   1 
ATOM   3421 C CB  . CYS C 3 61  ? -6.33100  21.34800 -27.33400 1.000 134.96976 ?  61  CYS E CB  1 
ATOM   3422 S SG  . CYS C 3 61  ? -5.60600  21.86300 -28.89800 1.000 127.75939 ?  61  CYS E SG  1 
ATOM   3423 N N   . ASN C 3 62  ? -7.61500  22.16500 -24.25200 1.000 148.75396 ?  62  ASN E N   1 
ATOM   3424 C CA  . ASN C 3 62  ? -8.75700  22.36100 -23.35700 1.000 151.28768 ?  62  ASN E CA  1 
ATOM   3425 C C   . ASN C 3 62  ? -10.06300 21.82100 -23.92500 1.000 158.96020 ?  62  ASN E C   1 
ATOM   3426 O O   . ASN C 3 62  ? -11.12900 22.41200 -23.74900 1.000 162.72964 ?  62  ASN E O   1 
ATOM   3427 C CB  . ASN C 3 62  ? -8.88000  23.83100 -22.96900 1.000 145.67891 ?  62  ASN E CB  1 
ATOM   3428 C CG  . ASN C 3 62  ? -7.75700  24.26200 -22.06200 1.000 133.69143 ?  62  ASN E CG  1 
ATOM   3429 O OD1 . ASN C 3 62  ? -7.27400  23.46600 -21.25900 1.000 133.29221 ?  62  ASN E OD1 1 
ATOM   3430 N ND2 . ASN C 3 62  ? -7.29400  25.49600 -22.22000 1.000 122.05273 ?  62  ASN E ND2 1 
ATOM   3431 N N   . ASP C 3 63  ? -9.96700  20.69900 -24.63000 1.000 158.07496 ?  63  ASP E N   1 
ATOM   3432 C CA  . ASP C 3 63  ? -11.10500 19.86600 -24.99100 1.000 159.57050 ?  63  ASP E CA  1 
ATOM   3433 C C   . ASP C 3 63  ? -10.53500 18.56300 -25.53100 1.000 153.58384 ?  63  ASP E C   1 
ATOM   3434 O O   . ASP C 3 63  ? -9.69200  18.58000 -26.43600 1.000 151.22542 ?  63  ASP E O   1 
ATOM   3435 C CB  . ASP C 3 63  ? -12.03900 20.54600 -25.99400 1.000 164.22930 ?  63  ASP E CB  1 
ATOM   3436 C CG  . ASP C 3 63  ? -13.12600 19.61800 -26.49600 1.000 162.59079 ?  63  ASP E CG  1 
ATOM   3437 O OD1 . ASP C 3 63  ? -13.64400 18.82700 -25.68000 1.000 161.05292 ?  63  ASP E OD1 1 
ATOM   3438 O OD2 . ASP C 3 63  ? -13.45800 19.66900 -27.70000 1.000 159.40171 ?  63  ASP E OD2 1 
ATOM   3439 N N   . GLU C 3 64  ? -10.97400 17.43700 -24.96500 1.000 164.23928 ?  64  GLU E N   1 
ATOM   3440 C CA  . GLU C 3 64  ? -10.42000 16.13700 -25.33400 1.000 157.40140 ?  64  GLU E CA  1 
ATOM   3441 C C   . GLU C 3 64  ? -10.49600 15.88800 -26.83400 1.000 155.95906 ?  64  GLU E C   1 
ATOM   3442 O O   . GLU C 3 64  ? -9.55400  15.34600 -27.42400 1.000 152.68973 ?  64  GLU E O   1 
ATOM   3443 C CB  . GLU C 3 64  ? -11.14800 15.02300 -24.58200 1.000 163.50349 ?  64  GLU E CB  1 
ATOM   3444 N N   . GLY C 3 65  ? -11.61200 16.26500 -27.46300 1.000 151.91379 ?  65  GLY E N   1 
ATOM   3445 C CA  . GLY C 3 65  ? -11.80200 15.95500 -28.87200 1.000 151.37445 ?  65  GLY E CA  1 
ATOM   3446 C C   . GLY C 3 65  ? -10.68000 16.44300 -29.76800 1.000 145.48448 ?  65  GLY E C   1 
ATOM   3447 O O   . GLY C 3 65  ? -10.31200 15.77300 -30.73700 1.000 145.25273 ?  65  GLY E O   1 
ATOM   3448 N N   . LEU C 3 66  ? -10.12800 17.61600 -29.47500 1.000 141.99667 ?  66  LEU E N   1 
ATOM   3449 C CA  . LEU C 3 66  ? -9.09400  18.19200 -30.32200 1.000 140.80305 ?  66  LEU E CA  1 
ATOM   3450 C C   . LEU C 3 66  ? -7.75400  18.22500 -29.59700 1.000 136.77050 ?  66  LEU E C   1 
ATOM   3451 O O   . LEU C 3 66  ? -7.67800  18.14500 -28.36900 1.000 135.19562 ?  66  LEU E O   1 
ATOM   3452 C CB  . LEU C 3 66  ? -9.48200  19.59000 -30.82100 1.000 141.06852 ?  66  LEU E CB  1 
ATOM   3453 C CG  . LEU C 3 66  ? -9.50300  20.85500 -29.96400 1.000 137.83436 ?  66  LEU E CG  1 
ATOM   3454 C CD1 . LEU C 3 66  ? -9.94500  22.02300 -30.81700 1.000 137.51148 ?  66  LEU E CD1 1 
ATOM   3455 C CD2 . LEU C 3 66  ? -10.45400 20.69600 -28.84300 1.000 138.09756 ?  66  LEU E CD2 1 
ATOM   3456 N N   . GLU C 3 67  ? -6.69500  18.37500 -30.39100 1.000 141.96801 ?  67  GLU E N   1 
ATOM   3457 C CA  . GLU C 3 67  ? -5.32100  18.30600 -29.92500 1.000 137.99308 ?  67  GLU E CA  1 
ATOM   3458 C C   . GLU C 3 67  ? -4.50900  19.43400 -30.54900 1.000 137.39386 ?  67  GLU E C   1 
ATOM   3459 O O   . GLU C 3 67  ? -4.85400  19.97100 -31.61000 1.000 140.22889 ?  67  GLU E O   1 
ATOM   3460 C CB  . GLU C 3 67  ? -4.66200  16.96800 -30.27400 1.000 135.99057 ?  67  GLU E CB  1 
ATOM   3461 C CG  . GLU C 3 67  ? -5.13200  16.37900 -31.59200 1.000 139.61550 ?  67  GLU E CG  1 
ATOM   3462 C CD  . GLU C 3 67  ? -4.35300  15.13900 -31.98000 1.000 136.61393 ?  67  GLU E CD  1 
ATOM   3463 O OE1 . GLU C 3 67  ? -3.39300  14.80000 -31.25000 1.000 131.00658 ?  67  GLU E OE1 1 
ATOM   3464 O OE2 . GLU C 3 67  ? -4.69800  14.51000 -33.00800 1.000 139.63634 ?  67  GLU E OE2 1 
ATOM   3465 N N   . CYS C 3 68  ? -3.46900  19.82700 -29.81400 1.000 134.58838 ?  68  CYS E N   1 
ATOM   3466 C CA  . CYS C 3 68  ? -2.48100  20.83000 -30.21500 1.000 133.29094 ?  68  CYS E CA  1 
ATOM   3467 C C   . CYS C 3 68  ? -1.60000  20.25400 -31.31300 1.000 133.01375 ?  68  CYS E C   1 
ATOM   3468 O O   . CYS C 3 68  ? -0.72900  19.42700 -31.04500 1.000 128.74539 ?  68  CYS E O   1 
ATOM   3469 C CB  . CYS C 3 68  ? -1.64000  21.23700 -29.00700 1.000 129.55219 ?  68  CYS E CB  1 
ATOM   3470 S SG  . CYS C 3 68  ? -0.77100  22.81400 -29.14000 1.000 128.45826 ?  68  CYS E SG  1 
ATOM   3471 N N   . VAL C 3 69  ? -1.84200  20.66500 -32.55600 1.000 128.94451 ?  69  VAL E N   1 
ATOM   3472 C CA  . VAL C 3 69  ? -1.04500  20.21900 -33.70300 1.000 130.81511 ?  69  VAL E CA  1 
ATOM   3473 C C   . VAL C 3 69  ? -0.39800  21.40000 -34.42600 1.000 132.93629 ?  69  VAL E C   1 
ATOM   3474 O O   . VAL C 3 69  ? -0.96600  22.50100 -34.44400 1.000 133.30230 ?  69  VAL E O   1 
ATOM   3475 C CB  . VAL C 3 69  ? -1.89300  19.37100 -34.66800 1.000 135.81289 ?  69  VAL E CB  1 
ATOM   3476 C CG1 . VAL C 3 69  ? -2.13200  17.99000 -34.08500 1.000 132.60561 ?  69  VAL E CG1 1 
ATOM   3477 C CG2 . VAL C 3 69  ? -3.22300  20.05300 -34.97200 1.000 139.68740 ?  69  VAL E CG2 1 
ATOM   3478 N N   . PRO C 3 70  ? 0.78000   21.21700 -35.03100 1.000 125.84629 ?  70  PRO E N   1 
ATOM   3479 C CA  . PRO C 3 70  ? 1.38100   22.28600 -35.83800 1.000 129.13827 ?  70  PRO E CA  1 
ATOM   3480 C C   . PRO C 3 70  ? 0.61800   22.56200 -37.12600 1.000 135.38598 ?  70  PRO E C   1 
ATOM   3481 O O   . PRO C 3 70  ? -0.05300  21.69100 -37.68100 1.000 139.54274 ?  70  PRO E O   1 
ATOM   3482 C CB  . PRO C 3 70  ? 2.78800   21.75200 -36.13300 1.000 128.73723 ?  70  PRO E CB  1 
ATOM   3483 C CG  . PRO C 3 70  ? 2.65100   20.27200 -36.07100 1.000 126.06332 ?  70  PRO E CG  1 
ATOM   3484 C CD  . PRO C 3 70  ? 1.61800   20.00500 -35.00600 1.000 122.17213 ?  70  PRO E CD  1 
ATOM   3485 N N   . THR C 3 71  ? 0.72700   23.80700 -37.59500 1.000 137.23704 ?  71  THR E N   1 
ATOM   3486 C CA  . THR C 3 71  ? 0.05700   24.25900 -38.80800 1.000 140.37632 ?  71  THR E CA  1 
ATOM   3487 C C   . THR C 3 71  ? 1.03100   24.94700 -39.75700 1.000 141.21861 ?  71  THR E C   1 
ATOM   3488 O O   . THR C 3 71  ? 0.84600   24.91400 -40.97700 1.000 146.20717 ?  71  THR E O   1 
ATOM   3489 C CB  . THR C 3 71  ? -1.09100  25.20700 -38.45700 1.000 135.07129 ?  71  THR E CB  1 
ATOM   3490 O OG1 . THR C 3 71  ? -0.61700  26.23300 -37.57300 1.000 127.72018 ?  71  THR E OG1 1 
ATOM   3491 C CG2 . THR C 3 71  ? -2.21600  24.43700 -37.80300 1.000 136.08638 ?  71  THR E CG2 1 
ATOM   3492 N N   . GLU C 3 72  ? 2.05400   25.59600 -39.20700 1.000 134.49302 ?  72  GLU E N   1 
ATOM   3493 C CA  . GLU C 3 72  ? 3.09500   26.24600 -39.99100 1.000 133.99827 ?  72  GLU E CA  1 
ATOM   3494 C C   . GLU C 3 72  ? 4.44200   25.71600 -39.52300 1.000 136.02370 ?  72  GLU E C   1 
ATOM   3495 O O   . GLU C 3 72  ? 4.78000   25.83000 -38.34000 1.000 132.01529 ?  72  GLU E O   1 
ATOM   3496 C CB  . GLU C 3 72  ? 3.01500   27.76700 -39.84400 1.000 124.83632 ?  72  GLU E CB  1 
ATOM   3497 N N   . GLU C 3 73  ? 5.20100   25.12600 -40.43900 1.000 131.07314 ?  73  GLU E N   1 
ATOM   3498 C CA  . GLU C 3 73  ? 6.47700   24.51500 -40.10400 1.000 134.15597 ?  73  GLU E CA  1 
ATOM   3499 C C   . GLU C 3 73  ? 7.53900   24.90300 -41.12200 1.000 135.46172 ?  73  GLU E C   1 
ATOM   3500 O O   . GLU C 3 73  ? 7.23800   25.13400 -42.29300 1.000 137.60416 ?  73  GLU E O   1 
ATOM   3501 C CB  . GLU C 3 73  ? 6.34700   22.99100 -40.03600 1.000 141.71194 ?  73  GLU E CB  1 
ATOM   3502 N N   . SER C 3 74  ? 8.78100   25.02200 -40.65700 1.000 141.66145 ?  74  SER E N   1 
ATOM   3503 C CA  . SER C 3 74  ? 9.90500   25.23800 -41.57400 1.000 142.46070 ?  74  SER E CA  1 
ATOM   3504 C C   . SER C 3 74  ? 11.17400  24.69600 -40.91800 1.000 143.38132 ?  74  SER E C   1 
ATOM   3505 O O   . SER C 3 74  ? 11.12000  24.06200 -39.86100 1.000 143.25868 ?  74  SER E O   1 
ATOM   3506 C CB  . SER C 3 74  ? 9.99000   26.71000 -42.00100 1.000 134.38745 ?  74  SER E CB  1 
ATOM   3507 O OG  . SER C 3 74  ? 10.34800  27.55400 -40.92800 1.000 127.19994 ?  74  SER E OG  1 
ATOM   3508 N N   . ASN C 3 75  ? 12.32800  24.94100 -41.54000 1.000 144.83964 ?  75  ASN E N   1 
ATOM   3509 C CA  . ASN C 3 75  ? 13.58100  24.33500 -41.10000 1.000 145.57798 ?  75  ASN E CA  1 
ATOM   3510 C C   . ASN C 3 75  ? 14.55500  25.39000 -40.59500 1.000 140.82357 ?  75  ASN E C   1 
ATOM   3511 O O   . ASN C 3 75  ? 14.67700  26.47300 -41.17600 1.000 136.28354 ?  75  ASN E O   1 
ATOM   3512 C CB  . ASN C 3 75  ? 14.25900  23.54000 -42.23700 1.000 149.78638 ?  75  ASN E CB  1 
ATOM   3513 C CG  . ASN C 3 75  ? 13.71400  22.12200 -42.39000 1.000 152.04527 ?  75  ASN E CG  1 
ATOM   3514 O OD1 . ASN C 3 75  ? 12.75300  21.74300 -41.72600 1.000 150.13891 ?  75  ASN E OD1 1 
ATOM   3515 N ND2 . ASN C 3 75  ? 14.35600  21.32600 -43.26200 1.000 154.14904 ?  75  ASN E ND2 1 
ATOM   3516 N N   . ILE C 3 76  ? 15.26300  25.04400 -39.52100 1.000 142.17659 ?  76  ILE E N   1 
ATOM   3517 C CA  . ILE C 3 76  ? 16.32000  25.86300 -38.93700 1.000 139.86569 ?  76  ILE E CA  1 
ATOM   3518 C C   . ILE C 3 76  ? 17.60100  25.04200 -38.94500 1.000 142.51575 ?  76  ILE E C   1 
ATOM   3519 O O   . ILE C 3 76  ? 17.61800  23.90100 -38.47100 1.000 142.35930 ?  76  ILE E O   1 
ATOM   3520 C CB  . ILE C 3 76  ? 15.98100  26.33600 -37.50900 1.000 137.84059 ?  76  ILE E CB  1 
ATOM   3521 C CG1 . ILE C 3 76  ? 17.14300  27.14300 -36.93100 1.000 137.10924 ?  76  ILE E CG1 1 
ATOM   3522 C CG2 . ILE C 3 76  ? 15.69000  25.17600 -36.56900 1.000 132.11712 ?  76  ILE E CG2 1 
ATOM   3523 C CD1 . ILE C 3 76  ? 17.41700  28.43900 -37.65300 1.000 131.92828 ?  76  ILE E CD1 1 
ATOM   3524 N N   . THR C 3 77  ? 18.65800  25.59200 -39.53200 1.000 139.54756 ?  77  THR E N   1 
ATOM   3525 C CA  . THR C 3 77  ? 19.97000  24.96200 -39.47200 1.000 141.88837 ?  77  THR E CA  1 
ATOM   3526 C C   . THR C 3 77  ? 20.74200  25.54100 -38.29100 1.000 141.50680 ?  77  THR E C   1 
ATOM   3527 O O   . THR C 3 77  ? 20.82500  26.76200 -38.14200 1.000 138.17537 ?  77  THR E O   1 
ATOM   3528 C CB  . THR C 3 77  ? 20.72600  25.16900 -40.78600 1.000 140.41089 ?  77  THR E CB  1 
ATOM   3529 O OG1 . THR C 3 77  ? 20.80700  26.56600 -41.08000 1.000 133.50664 ?  77  THR E OG1 1 
ATOM   3530 C CG2 . THR C 3 77  ? 19.98700  24.48800 -41.92300 1.000 143.11872 ?  77  THR E CG2 1 
ATOM   3531 N N   . MET C 3 78  ? 21.28900  24.66300 -37.44900 1.000 143.42814 ?  78  MET E N   1 
ATOM   3532 C CA  . MET C 3 78  ? 22.04100  25.05500 -36.26900 1.000 142.58545 ?  78  MET E CA  1 
ATOM   3533 C C   . MET C 3 78  ? 23.38300  24.33400 -36.25300 1.000 145.53830 ?  78  MET E C   1 
ATOM   3534 O O   . MET C 3 78  ? 23.55100  23.26400 -36.84800 1.000 147.11011 ?  78  MET E O   1 
ATOM   3535 C CB  . MET C 3 78  ? 21.27600  24.73600 -34.97300 1.000 135.22771 ?  78  MET E CB  1 
ATOM   3536 C CG  . MET C 3 78  ? 19.76200  24.84400 -35.07800 1.000 130.53238 ?  78  MET E CG  1 
ATOM   3537 S SD  . MET C 3 78  ? 18.91500  24.23400 -33.61400 1.000 118.53771 ?  78  MET E SD  1 
ATOM   3538 C CE  . MET C 3 78  ? 20.07600  24.72700 -32.34900 1.000 116.74962 ?  78  MET E CE  1 
ATOM   3539 N N   . GLN C 3 79  ? 24.33100  24.92100 -35.53100 1.000 135.49137 ?  79  GLN E N   1 
ATOM   3540 C CA  . GLN C 3 79  ? 25.68400  24.39000 -35.43800 1.000 137.92675 ?  79  GLN E CA  1 
ATOM   3541 C C   . GLN C 3 79  ? 25.79000  23.38900 -34.29700 1.000 137.80278 ?  79  GLN E C   1 
ATOM   3542 O O   . GLN C 3 79  ? 25.43400  23.69800 -33.15600 1.000 134.18555 ?  79  GLN E O   1 
ATOM   3543 C CB  . GLN C 3 79  ? 26.69400  25.51200 -35.22600 1.000 137.04365 ?  79  GLN E CB  1 
ATOM   3544 C CG  . GLN C 3 79  ? 26.72600  26.52900 -36.32100 1.000 132.91266 ?  79  GLN E CG  1 
ATOM   3545 C CD  . GLN C 3 79  ? 27.68500  27.64200 -36.00500 1.000 129.98517 ?  79  GLN E CD  1 
ATOM   3546 O OE1 . GLN C 3 79  ? 28.41700  27.57900 -35.01700 1.000 132.64462 ?  79  GLN E OE1 1 
ATOM   3547 N NE2 . GLN C 3 79  ? 27.69100  28.67300 -36.83900 1.000 122.99110 ?  79  GLN E NE2 1 
ATOM   3548 N N   . ILE C 3 80  ? 26.27700  22.19200 -34.61400 1.000 141.80340 ?  80  ILE E N   1 
ATOM   3549 C CA  . ILE C 3 80  ? 26.49600  21.13500 -33.63800 1.000 141.62150 ?  80  ILE E CA  1 
ATOM   3550 C C   . ILE C 3 80  ? 27.92800  20.66500 -33.81800 1.000 144.99049 ?  80  ILE E C   1 
ATOM   3551 O O   . ILE C 3 80  ? 28.37600  20.46300 -34.94900 1.000 145.37947 ?  80  ILE E O   1 
ATOM   3552 C CB  . ILE C 3 80  ? 25.51900  19.95900 -33.82600 1.000 138.57449 ?  80  ILE E CB  1 
ATOM   3553 C CG1 . ILE C 3 80  ? 24.08600  20.46900 -33.91200 1.000 133.06310 ?  80  ILE E CG1 1 
ATOM   3554 C CG2 . ILE C 3 80  ? 25.66900  18.96300 -32.69400 1.000 136.89742 ?  80  ILE E CG2 1 
ATOM   3555 C CD1 . ILE C 3 80  ? 23.61700  21.09100 -32.63700 1.000 127.44149 ?  80  ILE E CD1 1 
ATOM   3556 N N   . MET C 3 81  ? 28.64200  20.45700 -32.71600 1.000 148.11880 ?  81  MET E N   1 
ATOM   3557 C CA  . MET C 3 81  ? 30.01000  19.95900 -32.77900 1.000 149.73662 ?  81  MET E CA  1 
ATOM   3558 C C   . MET C 3 81  ? 29.97700  18.45900 -33.02400 1.000 149.74791 ?  81  MET E C   1 
ATOM   3559 O O   . MET C 3 81  ? 29.64400  17.67300 -32.13300 1.000 149.96987 ?  81  MET E O   1 
ATOM   3560 C CB  . MET C 3 81  ? 30.76000  20.30200 -31.50000 1.000 151.62935 ?  81  MET E CB  1 
ATOM   3561 C CG  . MET C 3 81  ? 32.23300  20.03600 -31.61100 1.000 151.55169 ?  81  MET E CG  1 
ATOM   3562 S SD  . MET C 3 81  ? 33.19300  21.00500 -30.44300 1.000 153.79679 ?  81  MET E SD  1 
ATOM   3563 C CE  . MET C 3 81  ? 34.60300  21.40400 -31.45800 1.000 148.92992 ?  81  MET E CE  1 
ATOM   3564 N N   . ARG C 3 82  ? 30.31300  18.07000 -34.25000 1.000 164.40916 ?  82  ARG E N   1 
ATOM   3565 C CA  . ARG C 3 82  ? 30.46400  16.67000 -34.63100 1.000 164.19221 ?  82  ARG E CA  1 
ATOM   3566 C C   . ARG C 3 82  ? 31.81400  16.16200 -34.13400 1.000 163.92236 ?  82  ARG E C   1 
ATOM   3567 O O   . ARG C 3 82  ? 32.86600  16.58400 -34.62400 1.000 161.86498 ?  82  ARG E O   1 
ATOM   3568 C CB  . ARG C 3 82  ? 30.32200  16.52800 -36.14500 1.000 163.35876 ?  82  ARG E CB  1 
ATOM   3569 C CG  . ARG C 3 82  ? 29.10900  15.72500 -36.59300 1.000 162.85605 ?  82  ARG E CG  1 
ATOM   3570 C CD  . ARG C 3 82  ? 28.84800  15.89400 -38.08800 1.000 162.41927 ?  82  ARG E CD  1 
ATOM   3571 N NE  . ARG C 3 82  ? 27.46600  15.60000 -38.45200 1.000 160.50953 ?  82  ARG E NE  1 
ATOM   3572 C CZ  . ARG C 3 82  ? 27.02000  15.50300 -39.69800 1.000 159.69941 ?  82  ARG E CZ  1 
ATOM   3573 N NH1 . ARG C 3 82  ? 27.83200  15.62100 -40.73600 1.000 160.74108 ?  82  ARG E NH1 1 
ATOM   3574 N NH2 . ARG C 3 82  ? 25.72500  15.28400 -39.90800 1.000 156.86245 ?  82  ARG E NH2 1 
ATOM   3575 N N   . ILE C 3 83  ? 31.77700  15.27100 -33.14700 1.000 168.79170 ?  83  ILE E N   1 
ATOM   3576 C CA  . ILE C 3 83  ? 32.95900  14.63900 -32.57700 1.000 168.30906 ?  83  ILE E CA  1 
ATOM   3577 C C   . ILE C 3 83  ? 33.13000  13.32700 -33.33500 1.000 166.95673 ?  83  ILE E C   1 
ATOM   3578 O O   . ILE C 3 83  ? 32.31100  12.40800 -33.20600 1.000 167.11111 ?  83  ILE E O   1 
ATOM   3579 C CB  . ILE C 3 83  ? 32.79300  14.38500 -31.07200 1.000 170.17431 ?  83  ILE E CB  1 
ATOM   3580 C CG1 . ILE C 3 83  ? 32.50500  15.68200 -30.31100 1.000 172.51320 ?  83  ILE E CG1 1 
ATOM   3581 C CG2 . ILE C 3 83  ? 34.02000  13.69100 -30.50200 1.000 169.40367 ?  83  ILE E CG2 1 
ATOM   3582 C CD1 . ILE C 3 83  ? 33.43500  16.82200 -30.63400 1.000 172.00469 ?  83  ILE E CD1 1 
ATOM   3583 N N   . LYS C 3 84  ? 34.19800  13.25200 -34.12200 1.000 184.90628 ?  84  LYS E N   1 
ATOM   3584 C CA  . LYS C 3 84  ? 34.55400  12.07100 -34.89200 1.000 186.85836 ?  84  LYS E CA  1 
ATOM   3585 C C   . LYS C 3 84  ? 35.01600  10.91900 -33.99500 1.000 186.74926 ?  84  LYS E C   1 
ATOM   3586 O O   . LYS C 3 84  ? 35.55100  11.14600 -32.90800 1.000 193.33299 ?  84  LYS E O   1 
ATOM   3587 C CB  . LYS C 3 84  ? 35.64900  12.42700 -35.89400 1.000 204.44137 ?  84  LYS E CB  1 
ATOM   3588 N N   . PRO C 3 85  ? 34.80400  9.66500  -34.43300 1.000 191.55370 ?  85  PRO E N   1 
ATOM   3589 C CA  . PRO C 3 85  ? 35.14100  8.49600  -33.58700 1.000 187.59967 ?  85  PRO E CA  1 
ATOM   3590 C C   . PRO C 3 85  ? 36.53200  8.57600  -32.97700 1.000 207.77574 ?  85  PRO E C   1 
ATOM   3591 O O   . PRO C 3 85  ? 36.75600  8.13400  -31.84300 1.000 201.59249 ?  85  PRO E O   1 
ATOM   3592 C CB  . PRO C 3 85  ? 34.99800  7.32400  -34.57100 1.000 174.52265 ?  85  PRO E CB  1 
ATOM   3593 C CG  . PRO C 3 85  ? 34.08000  7.87200  -35.62900 1.000 175.59194 ?  85  PRO E CG  1 
ATOM   3594 C CD  . PRO C 3 85  ? 34.60800  9.23500  -35.82400 1.000 186.08142 ?  85  PRO E CD  1 
ATOM   3595 N N   . HIS C 3 86  ? 37.48100  9.11800  -33.72600 1.000 205.62894 ?  86  HIS E N   1 
ATOM   3596 C CA  . HIS C 3 86  ? 38.81400  9.42800  -33.23100 1.000 213.67846 ?  86  HIS E CA  1 
ATOM   3597 C C   . HIS C 3 86  ? 39.12100  10.81500 -33.78300 1.000 220.27834 ?  86  HIS E C   1 
ATOM   3598 O O   . HIS C 3 86  ? 38.19900  11.54200 -34.16600 1.000 217.81555 ?  86  HIS E O   1 
ATOM   3599 C CB  . HIS C 3 86  ? 39.82400  8.32000  -33.57200 1.000 212.02908 ?  86  HIS E CB  1 
ATOM   3600 C CG  . HIS C 3 86  ? 39.97900  7.30000  -32.48300 1.000 192.10503 ?  86  HIS E CG  1 
ATOM   3601 N ND1 . HIS C 3 86  ? 39.85900  7.62100  -31.14800 1.000 184.16457 ?  86  HIS E ND1 1 
ATOM   3602 C CD2 . HIS C 3 86  ? 40.24700  5.97300  -32.52500 1.000 188.17197 ?  86  HIS E CD2 1 
ATOM   3603 C CE1 . HIS C 3 86  ? 40.04700  6.53800  -30.41500 1.000 181.71542 ?  86  HIS E CE1 1 
ATOM   3604 N NE2 . HIS C 3 86  ? 40.28300  5.52300  -31.22700 1.000 184.13190 ?  86  HIS E NE2 1 
ATOM   3605 N N   . GLN C 3 87  ? 40.39700  11.20500 -33.80600 1.000 212.13459 ?  87  GLN E N   1 
ATOM   3606 C CA  . GLN C 3 87  ? 40.76400  12.60900 -33.97800 1.000 212.30796 ?  87  GLN E CA  1 
ATOM   3607 C C   . GLN C 3 87  ? 39.93300  13.34400 -35.02600 1.000 212.59067 ?  87  GLN E C   1 
ATOM   3608 O O   . GLN C 3 87  ? 39.98000  13.02800 -36.21900 1.000 214.73876 ?  87  GLN E O   1 
ATOM   3609 C CB  . GLN C 3 87  ? 42.24700  12.72000 -34.34300 1.000 212.32059 ?  87  GLN E CB  1 
ATOM   3610 N N   . GLY C 3 88  ? 39.13800  14.30100 -34.55200 1.000 205.44119 ?  88  GLY E N   1 
ATOM   3611 C CA  . GLY C 3 88  ? 38.31600  15.17600 -35.36400 1.000 205.92570 ?  88  GLY E CA  1 
ATOM   3612 C C   . GLY C 3 88  ? 37.29700  15.90500 -34.50900 1.000 200.13581 ?  88  GLY E C   1 
ATOM   3613 O O   . GLY C 3 88  ? 36.62800  15.29700 -33.66600 1.000 192.81145 ?  88  GLY E O   1 
ATOM   3614 N N   . GLN C 3 89  ? 37.13100  17.20700 -34.76100 1.000 203.61606 ?  89  GLN E N   1 
ATOM   3615 C CA  . GLN C 3 89  ? 36.24000  18.05500 -33.97600 1.000 198.95342 ?  89  GLN E CA  1 
ATOM   3616 C C   . GLN C 3 89  ? 35.45000  19.02000 -34.84800 1.000 202.77993 ?  89  GLN E C   1 
ATOM   3617 O O   . GLN C 3 89  ? 35.16600  20.14500 -34.42500 1.000 202.72051 ?  89  GLN E O   1 
ATOM   3618 C CB  . GLN C 3 89  ? 37.01400  18.85400 -32.92500 1.000 198.57155 ?  89  GLN E CB  1 
ATOM   3619 C CG  . GLN C 3 89  ? 36.86200  18.34400 -31.50300 1.000 190.52255 ?  89  GLN E CG  1 
ATOM   3620 C CD  . GLN C 3 89  ? 37.31900  16.91300 -31.33900 1.000 188.62654 ?  89  GLN E CD  1 
ATOM   3621 O OE1 . GLN C 3 89  ? 36.58000  16.06900 -30.82800 1.000 182.27078 ?  89  GLN E OE1 1 
ATOM   3622 N NE2 . GLN C 3 89  ? 38.53800  16.62400 -31.78200 1.000 194.39113 ?  89  GLN E NE2 1 
ATOM   3623 N N   . HIS C 3 90  ? 35.09700  18.61700 -36.06400 1.000 206.40884 ?  90  HIS E N   1 
ATOM   3624 C CA  . HIS C 3 90  ? 34.43900  19.54500 -36.97300 1.000 211.38885 ?  90  HIS E CA  1 
ATOM   3625 C C   . HIS C 3 90  ? 33.04200  19.88700 -36.47000 1.000 205.57266 ?  90  HIS E C   1 
ATOM   3626 O O   . HIS C 3 90  ? 32.30300  19.02200 -35.99100 1.000 198.40916 ?  90  HIS E O   1 
ATOM   3627 C CB  . HIS C 3 90  ? 34.35300  18.96100 -38.38100 1.000 216.43632 ?  90  HIS E CB  1 
ATOM   3628 C CG  . HIS C 3 90  ? 33.69700  17.61900 -38.44000 1.000 210.58256 ?  90  HIS E CG  1 
ATOM   3629 N ND1 . HIS C 3 90  ? 34.17900  16.51900 -37.76300 1.000 205.67844 ?  90  HIS E ND1 1 
ATOM   3630 C CD2 . HIS C 3 90  ? 32.58900  17.20100 -39.09600 1.000 209.01635 ?  90  HIS E CD2 1 
ATOM   3631 C CE1 . HIS C 3 90  ? 33.39500  15.48100 -37.99800 1.000 201.24141 ?  90  HIS E CE1 1 
ATOM   3632 N NE2 . HIS C 3 90  ? 32.42400  15.86800 -38.80500 1.000 202.98388 ?  90  HIS E NE2 1 
ATOM   3633 N N   . ILE C 3 91  ? 32.70000  21.16800 -36.56200 1.000 153.47868 ?  91  ILE E N   1 
ATOM   3634 C CA  . ILE C 3 91  ? 31.39800  21.68900 -36.16400 1.000 153.57306 ?  91  ILE E CA  1 
ATOM   3635 C C   . ILE C 3 91  ? 30.54200  21.79800 -37.42300 1.000 153.64763 ?  91  ILE E C   1 
ATOM   3636 O O   . ILE C 3 91  ? 30.82500  22.60700 -38.31400 1.000 153.60427 ?  91  ILE E O   1 
ATOM   3637 C CB  . ILE C 3 91  ? 31.53200  23.03300 -35.43600 1.000 153.31047 ?  91  ILE E CB  1 
ATOM   3638 C CG1 . ILE C 3 91  ? 32.62000  23.88800 -36.08400 1.000 153.00655 ?  91  ILE E CG1 1 
ATOM   3639 C CG2 . ILE C 3 91  ? 31.90200  22.80700 -33.98400 1.000 153.04504 ?  91  ILE E CG2 1 
ATOM   3640 C CD1 . ILE C 3 91  ? 32.71300  25.30300 -35.52500 1.000 152.29146 ?  91  ILE E CD1 1 
ATOM   3641 N N   . GLY C 3 92  ? 29.48900  20.98700 -37.50300 1.000 146.69202 ?  92  GLY E N   1 
ATOM   3642 C CA  . GLY C 3 92  ? 28.66600  20.88800 -38.69500 1.000 146.43424 ?  92  GLY E CA  1 
ATOM   3643 C C   . GLY C 3 92  ? 27.30000  21.52600 -38.53100 1.000 146.71733 ?  92  GLY E C   1 
ATOM   3644 O O   . GLY C 3 92  ? 26.77300  21.63300 -37.41900 1.000 146.95807 ?  92  GLY E O   1 
ATOM   3645 N N   . GLU C 3 93  ? 26.71600  21.92300 -39.66600 1.000 141.89294 ?  93  GLU E N   1 
ATOM   3646 C CA  . GLU C 3 93  ? 25.46700  22.68500 -39.70400 1.000 142.58412 ?  93  GLU E CA  1 
ATOM   3647 C C   . GLU C 3 93  ? 24.29300  21.72000 -39.85300 1.000 141.89149 ?  93  GLU E C   1 
ATOM   3648 O O   . GLU C 3 93  ? 23.69300  21.57000 -40.91900 1.000 141.39027 ?  93  GLU E O   1 
ATOM   3649 C CB  . GLU C 3 93  ? 25.50500  23.70800 -40.83600 1.000 143.35700 ?  93  GLU E CB  1 
ATOM   3650 N N   . MET C 3 94  ? 23.94600  21.07100 -38.74600 1.000 141.09704 ?  94  MET E N   1 
ATOM   3651 C CA  . MET C 3 94  ? 22.84000  20.12500 -38.76100 1.000 139.97538 ?  94  MET E CA  1 
ATOM   3652 C C   . MET C 3 94  ? 21.52300  20.89000 -38.80300 1.000 140.54702 ?  94  MET E C   1 
ATOM   3653 O O   . MET C 3 94  ? 21.33500  21.84700 -38.05000 1.000 141.85596 ?  94  MET E O   1 
ATOM   3654 C CB  . MET C 3 94  ? 22.90300  19.23500 -37.52400 1.000 139.59950 ?  94  MET E CB  1 
ATOM   3655 C CG  . MET C 3 94  ? 23.94500  18.13400 -37.61400 1.000 139.01377 ?  94  MET E CG  1 
ATOM   3656 S SD  . MET C 3 94  ? 23.60300  16.68600 -36.60200 1.000 137.97579 ?  94  MET E SD  1 
ATOM   3657 C CE  . MET C 3 94  ? 22.92100  15.57600 -37.82700 1.000 136.82295 ?  94  MET E CE  1 
ATOM   3658 N N   . SER C 3 95  ? 20.60700  20.47400 -39.67000 1.000 144.35576 ?  95  SER E N   1 
ATOM   3659 C CA  . SER C 3 95  ? 19.30000  21.11300 -39.75100 1.000 144.91907 ?  95  SER E CA  1 
ATOM   3660 C C   . SER C 3 95  ? 18.28600  20.35600 -38.90500 1.000 144.30226 ?  95  SER E C   1 
ATOM   3661 O O   . SER C 3 95  ? 18.43400  19.16400 -38.63000 1.000 143.45372 ?  95  SER E O   1 
ATOM   3662 C CB  . SER C 3 95  ? 18.81000  21.18800 -41.20100 1.000 144.26376 ?  95  SER E CB  1 
ATOM   3663 O OG  . SER C 3 95  ? 17.39800  21.08400 -41.26600 1.000 143.84290 ?  95  SER E OG  1 
ATOM   3664 N N   . PHE C 3 96  ? 17.24800  21.07500 -38.49000 1.000 141.06332 ?  96  PHE E N   1 
ATOM   3665 C CA  . PHE C 3 96  ? 16.15100  20.51000 -37.72500 1.000 141.11070 ?  96  PHE E CA  1 
ATOM   3666 C C   . PHE C 3 96  ? 14.86600  21.21700 -38.14000 1.000 142.05317 ?  96  PHE E C   1 
ATOM   3667 O O   . PHE C 3 96  ? 14.88900  22.31700 -38.69500 1.000 142.64409 ?  96  PHE E O   1 
ATOM   3668 C CB  . PHE C 3 96  ? 16.37200  20.63800 -36.20600 1.000 141.10499 ?  96  PHE E CB  1 
ATOM   3669 C CG  . PHE C 3 96  ? 17.74900  20.22100 -35.74200 1.000 140.31149 ?  96  PHE E CG  1 
ATOM   3670 C CD1 . PHE C 3 96  ? 18.79100  21.13500 -35.69300 1.000 141.02242 ?  96  PHE E CD1 1 
ATOM   3671 C CD2 . PHE C 3 96  ? 18.00300  18.91000 -35.36700 1.000 139.32450 ?  96  PHE E CD2 1 
ATOM   3672 C CE1 . PHE C 3 96  ? 20.05400  20.75300 -35.26700 1.000 140.70645 ?  96  PHE E CE1 1 
ATOM   3673 C CE2 . PHE C 3 96  ? 19.26500  18.52300 -34.94400 1.000 138.67501 ?  96  PHE E CE2 1 
ATOM   3674 C CZ  . PHE C 3 96  ? 20.29100  19.44700 -34.89500 1.000 139.40397 ?  96  PHE E CZ  1 
ATOM   3675 N N   . LEU C 3 97  ? 13.74100  20.56800 -37.87300 1.000 143.65812 ?  97  LEU E N   1 
ATOM   3676 C CA  . LEU C 3 97  ? 12.43300  21.12600 -38.17900 1.000 145.16989 ?  97  LEU E CA  1 
ATOM   3677 C C   . LEU C 3 97  ? 11.90700  21.88000 -36.96600 1.000 146.65392 ?  97  LEU E C   1 
ATOM   3678 O O   . LEU C 3 97  ? 12.12300  21.45500 -35.82700 1.000 146.51888 ?  97  LEU E O   1 
ATOM   3679 C CB  . LEU C 3 97  ? 11.46900  20.00300 -38.55700 1.000 146.54103 ?  97  LEU E CB  1 
ATOM   3680 C CG  . LEU C 3 97  ? 9.97700   20.28900 -38.70500 1.000 149.25886 ?  97  LEU E CG  1 
ATOM   3681 C CD1 . LEU C 3 97  ? 9.69700   21.27200 -39.82500 1.000 148.01091 ?  97  LEU E CD1 1 
ATOM   3682 C CD2 . LEU C 3 97  ? 9.25600   18.97900 -38.93800 1.000 151.65516 ?  97  LEU E CD2 1 
ATOM   3683 N N   . GLN C 3 98  ? 11.22000  23.00100 -37.19700 1.000 141.16745 ?  98  GLN E N   1 
ATOM   3684 C CA  . GLN C 3 98  ? 10.57300  23.69200 -36.09200 1.000 142.76823 ?  98  GLN E CA  1 
ATOM   3685 C C   . GLN C 3 98  ? 9.15500   24.07100 -36.49000 1.000 145.40580 ?  98  GLN E C   1 
ATOM   3686 O O   . GLN C 3 98  ? 8.81800   24.23300 -37.67500 1.000 145.24283 ?  98  GLN E O   1 
ATOM   3687 C CB  . GLN C 3 98  ? 11.32800  24.94900 -35.62700 1.000 141.87350 ?  98  GLN E CB  1 
ATOM   3688 C CG  . GLN C 3 98  ? 11.23700  26.14500 -36.53800 1.000 142.75220 ?  98  GLN E CG  1 
ATOM   3689 C CD  . GLN C 3 98  ? 12.20700  26.08600 -37.68400 1.000 141.90668 ?  98  GLN E CD  1 
ATOM   3690 O OE1 . GLN C 3 98  ? 12.94500  25.11400 -37.84600 1.000 140.50766 ?  98  GLN E OE1 1 
ATOM   3691 N NE2 . GLN C 3 98  ? 12.24400  27.15400 -38.47100 1.000 143.22625 ?  98  GLN E NE2 1 
ATOM   3692 N N   . HIS C 3 99  ? 8.35100   24.25700 -35.44500 1.000 132.80926 ?  99  HIS E N   1 
ATOM   3693 C CA  . HIS C 3 99  ? 6.92500   24.54700 -35.52700 1.000 135.83985 ?  99  HIS E CA  1 
ATOM   3694 C C   . HIS C 3 99  ? 6.72200   26.04400 -35.31300 1.000 139.97883 ?  99  HIS E C   1 
ATOM   3695 O O   . HIS C 3 99  ? 6.77100   26.53000 -34.18000 1.000 141.81481 ?  99  HIS E O   1 
ATOM   3696 C CB  . HIS C 3 99  ? 6.18300   23.73700 -34.46800 1.000 136.03417 ?  99  HIS E CB  1 
ATOM   3697 C CG  . HIS C 3 99  ? 6.16000   22.26200 -34.73700 1.000 135.04368 ?  99  HIS E CG  1 
ATOM   3698 N ND1 . HIS C 3 99  ? 5.91900   21.33100 -33.75000 1.000 137.38997 ?  99  HIS E ND1 1 
ATOM   3699 C CD2 . HIS C 3 99  ? 6.35100   21.55800 -35.87900 1.000 133.96432 ?  99  HIS E CD2 1 
ATOM   3700 C CE1 . HIS C 3 99  ? 5.95900   20.11800 -34.27100 1.000 138.12233 ?  99  HIS E CE1 1 
ATOM   3701 N NE2 . HIS C 3 99  ? 6.21700   20.22800 -35.56100 1.000 136.23098 ?  99  HIS E NE2 1 
ATOM   3702 N N   . ASN C 3 100 ? 6.48600   26.77500 -36.40300 1.000 128.53344 ?  100 ASN E N   1 
ATOM   3703 C CA  . ASN C 3 100 ? 6.18400   28.20100 -36.29800 1.000 128.01197 ?  100 ASN E CA  1 
ATOM   3704 C C   . ASN C 3 100 ? 4.85900   28.45300 -35.58900 1.000 128.02129 ?  100 ASN E C   1 
ATOM   3705 O O   . ASN C 3 100 ? 4.76000   29.32100 -34.71400 1.000 127.01342 ?  100 ASN E O   1 
ATOM   3706 C CB  . ASN C 3 100 ? 6.16300   28.83400 -37.68600 1.000 129.46883 ?  100 ASN E CB  1 
ATOM   3707 C CG  . ASN C 3 100 ? 7.43700   28.60300 -38.44200 1.000 130.39226 ?  100 ASN E CG  1 
ATOM   3708 O OD1 . ASN C 3 100 ? 7.87000   27.46400 -38.62400 1.000 130.48011 ?  100 ASN E OD1 1 
ATOM   3709 N ND2 . ASN C 3 100 ? 8.06100   29.68900 -38.88500 1.000 131.87853 ?  100 ASN E ND2 1 
ATOM   3710 N N   . LYS C 3 101 ? 3.82800   27.70300 -35.95200 1.000 127.60984 ?  101 LYS E N   1 
ATOM   3711 C CA  . LYS C 3 101 ? 2.48800   27.97100 -35.46300 1.000 128.50499 ?  101 LYS E CA  1 
ATOM   3712 C C   . LYS C 3 101 ? 1.80300   26.66700 -35.09100 1.000 130.43509 ?  101 LYS E C   1 
ATOM   3713 O O   . LYS C 3 101 ? 1.93600   25.66200 -35.79300 1.000 131.94173 ?  101 LYS E O   1 
ATOM   3714 C CB  . LYS C 3 101 ? 1.67700   28.72100 -36.52700 1.000 129.71933 ?  101 LYS E CB  1 
ATOM   3715 C CG  . LYS C 3 101 ? 1.66900   30.22600 -36.32900 1.000 129.24168 ?  101 LYS E CG  1 
ATOM   3716 C CD  . LYS C 3 101 ? 1.08400   30.96600 -37.51600 1.000 130.85954 ?  101 LYS E CD  1 
ATOM   3717 C CE  . LYS C 3 101 ? 1.50500   32.42100 -37.47300 1.000 131.11263 ?  101 LYS E CE  1 
ATOM   3718 N NZ  . LYS C 3 101 ? 1.05300   33.09300 -36.23800 1.000 130.95629 ?  101 LYS E NZ  1 
ATOM   3719 N N   . CYS C 3 102 ? 1.06100   26.69200 -33.99500 1.000 128.33955 ?  102 CYS E N   1 
ATOM   3720 C CA  . CYS C 3 102 ? 0.27200   25.55000 -33.57300 1.000 131.12975 ?  102 CYS E CA  1 
ATOM   3721 C C   . CYS C 3 102 ? -1.20500  25.89900 -33.68500 1.000 132.78583 ?  102 CYS E C   1 
ATOM   3722 O O   . CYS C 3 102 ? -1.58000  27.01600 -34.04900 1.000 131.82333 ?  102 CYS E O   1 
ATOM   3723 C CB  . CYS C 3 102 ? 0.63500   25.14300 -32.14300 1.000 130.68148 ?  102 CYS E CB  1 
ATOM   3724 S SG  . CYS C 3 102 ? 2.39800   24.81800 -31.87800 1.000 128.58234 ?  102 CYS E SG  1 
ATOM   3725 N N   . GLU C 3 103 ? -2.04700  24.93100 -33.35200 1.000 133.00566 ?  103 GLU E N   1 
ATOM   3726 C CA  . GLU C 3 103 ? -3.48600  25.11000 -33.47100 1.000 134.85431 ?  103 GLU E CA  1 
ATOM   3727 C C   . GLU C 3 103 ? -4.16400  23.97300 -32.72900 1.000 137.73096 ?  103 GLU E C   1 
ATOM   3728 O O   . GLU C 3 103 ? -3.53400  22.97700 -32.37000 1.000 139.08514 ?  103 GLU E O   1 
ATOM   3729 C CB  . GLU C 3 103 ? -3.92700  25.13300 -34.93300 1.000 136.39265 ?  103 GLU E CB  1 
ATOM   3730 C CG  . GLU C 3 103 ? -5.03000  26.11100 -35.27400 1.000 136.60535 ?  103 GLU E CG  1 
ATOM   3731 C CD  . GLU C 3 103 ? -5.07000  26.42100 -36.76000 1.000 137.15465 ?  103 GLU E CD  1 
ATOM   3732 O OE1 . GLU C 3 103 ? -4.06100  26.93900 -37.28500 1.000 135.01843 ?  103 GLU E OE1 1 
ATOM   3733 O OE2 . GLU C 3 103 ? -6.10000  26.12700 -37.40700 1.000 139.70691 ?  103 GLU E OE2 1 
ATOM   3734 N N   . CYS C 3 104 ? -5.45900  24.13300 -32.50900 1.000 129.45029 ?  104 CYS E N   1 
ATOM   3735 C CA  . CYS C 3 104 ? -6.27700  23.14200 -31.82700 1.000 132.01251 ?  104 CYS E CA  1 
ATOM   3736 C C   . CYS C 3 104 ? -7.20600  22.54300 -32.87500 1.000 135.49639 ?  104 CYS E C   1 
ATOM   3737 O O   . CYS C 3 104 ? -8.13700  23.21200 -33.33500 1.000 135.34653 ?  104 CYS E O   1 
ATOM   3738 C CB  . CYS C 3 104 ? -7.04800  23.78800 -30.67700 1.000 130.10764 ?  104 CYS E CB  1 
ATOM   3739 S SG  . CYS C 3 104 ? -6.16200  23.79300 -29.11600 1.000 126.97055 ?  104 CYS E SG  1 
ATOM   3740 N N   . ARG C 3 105 ? -6.93800  21.30400 -33.27500 1.000 136.18718 ?  105 ARG E N   1 
ATOM   3741 C CA  . ARG C 3 105 ? -7.68400  20.64800 -34.33900 1.000 139.80152 ?  105 ARG E CA  1 
ATOM   3742 C C   . ARG C 3 105 ? -8.10100  19.24200 -33.93500 1.000 144.22121 ?  105 ARG E C   1 
ATOM   3743 O O   . ARG C 3 105 ? -7.45300  18.61700 -33.09400 1.000 144.84849 ?  105 ARG E O   1 
ATOM   3744 C CB  . ARG C 3 105 ? -6.86000  20.59600 -35.63500 1.000 140.19199 ?  105 ARG E CB  1 
ATOM   3745 C CG  . ARG C 3 105 ? -6.63700  21.96500 -36.27500 1.000 136.42732 ?  105 ARG E CG  1 
ATOM   3746 C CD  . ARG C 3 105 ? -6.45700  21.85200 -37.79300 1.000 137.47005 ?  105 ARG E CD  1 
ATOM   3747 N NE  . ARG C 3 105 ? -6.27000  23.14200 -38.45200 1.000 134.41046 ?  105 ARG E NE  1 
ATOM   3748 C CZ  . ARG C 3 105 ? -5.63900  23.29900 -39.61000 1.000 133.76022 ?  105 ARG E CZ  1 
ATOM   3749 N NH1 . ARG C 3 105 ? -5.17500  22.26400 -40.29200 1.000 135.25813 ?  105 ARG E NH1 1 
ATOM   3750 N NH2 . ARG C 3 105 ? -5.45700  24.52400 -40.09200 1.000 131.61018 ?  105 ARG E NH2 1 
ATOM   3751 N N   . PRO C 3 106 ? -9.17000  18.70700 -34.53700 1.000 147.01677 ?  106 PRO E N   1 
ATOM   3752 C CA  . PRO C 3 106 ? -9.72300  17.42200 -34.08100 1.000 151.23337 ?  106 PRO E CA  1 
ATOM   3753 C C   . PRO C 3 106 ? -8.75400  16.25500 -34.22100 1.000 154.97586 ?  106 PRO E C   1 
ATOM   3754 O O   . PRO C 3 106 ? -7.82100  16.26700 -35.02800 1.000 155.36049 ?  106 PRO E O   1 
ATOM   3755 C CB  . PRO C 3 106 ? -10.95200 17.23200 -34.97600 1.000 153.59920 ?  106 PRO E CB  1 
ATOM   3756 C CG  . PRO C 3 106 ? -11.37400 18.62300 -35.29600 1.000 149.32938 ?  106 PRO E CG  1 
ATOM   3757 C CD  . PRO C 3 106 ? -10.07900 19.37000 -35.49200 1.000 146.30116 ?  106 PRO E CD  1 
ATOM   3758 N N   . LYS C 3 107 ? -9.00100  15.23100 -33.40600 1.000 163.26419 ?  107 LYS E N   1 
ATOM   3759 C CA  . LYS C 3 107 ? -8.18100  14.03100 -33.33100 1.000 162.07252 ?  107 LYS E CA  1 
ATOM   3760 C C   . LYS C 3 107 ? -8.54000  13.05100 -34.45100 1.000 167.43325 ?  107 LYS E C   1 
ATOM   3761 O O   . LYS C 3 107 ? -9.43200  13.29600 -35.26800 1.000 172.23608 ?  107 LYS E O   1 
ATOM   3762 C CB  . LYS C 3 107 ? -8.35800  13.36600 -31.96600 1.000 152.40072 ?  107 LYS E CB  1 
ATOM   3763 C CG  . LYS C 3 107 ? -7.19500  12.48500 -31.52800 1.000 145.38179 ?  107 LYS E CG  1 
ATOM   3764 C CD  . LYS C 3 107 ? -7.25200  12.16900 -30.04800 1.000 133.52040 ?  107 LYS E CD  1 
ATOM   3765 C CE  . LYS C 3 107 ? -7.47600  13.41900 -29.22300 1.000 131.19100 ?  107 LYS E CE  1 
ATOM   3766 N NZ  . LYS C 3 107 ? -7.70300  13.07700 -27.79300 1.000 123.04083 ?  107 LYS E NZ  1 
ATOM   3767 N N   . LYS C 3 108 ? -7.83600  11.91700 -34.47700 1.000 160.41178 ?  108 LYS E N   1 
ATOM   3768 C CA  . LYS C 3 108 ? -8.06400  10.84500 -35.44900 1.000 164.03679 ?  108 LYS E CA  1 
ATOM   3769 C C   . LYS C 3 108 ? -7.58000  9.49500  -34.90900 1.000 156.72322 ?  108 LYS E C   1 
ATOM   3770 O O   . LYS C 3 108 ? -6.93800  8.71700  -35.62300 1.000 158.69188 ?  108 LYS E O   1 
ATOM   3771 C CB  . LYS C 3 108 ? -7.36400  11.15800 -36.77300 1.000 171.13592 ?  108 LYS E CB  1 
ATOM   3772 N N   . HIS D 3 11  ? 17.19300  34.03400 -47.16500 1.000 193.45156 ?  11  HIS F N   1 
ATOM   3773 C CA  . HIS D 3 11  ? 15.87300  33.93600 -46.55000 1.000 199.11504 ?  11  HIS F CA  1 
ATOM   3774 C C   . HIS D 3 11  ? 15.86800  32.94000 -45.39300 1.000 195.65677 ?  11  HIS F C   1 
ATOM   3775 O O   . HIS D 3 11  ? 14.80900  32.55900 -44.89600 1.000 200.72570 ?  11  HIS F O   1 
ATOM   3776 C CB  . HIS D 3 11  ? 14.82700  33.53500 -47.59200 1.000 209.42220 ?  11  HIS F CB  1 
ATOM   3777 N N   . HIS D 3 12  ? 17.05600  32.52900 -44.96000 1.000 187.02765 ?  12  HIS F N   1 
ATOM   3778 C CA  . HIS D 3 12  ? 17.21200  31.47800 -43.96800 1.000 182.80877 ?  12  HIS F CA  1 
ATOM   3779 C C   . HIS D 3 12  ? 18.07900  31.99000 -42.81900 1.000 173.09476 ?  12  HIS F C   1 
ATOM   3780 O O   . HIS D 3 12  ? 18.79300  32.98900 -42.95100 1.000 169.13106 ?  12  HIS F O   1 
ATOM   3781 C CB  . HIS D 3 12  ? 17.84500  30.23100 -44.58000 1.000 191.19829 ?  12  HIS F CB  1 
ATOM   3782 C CG  . HIS D 3 12  ? 19.30400  30.11700 -44.29400 1.000 177.71716 ?  12  HIS F CG  1 
ATOM   3783 N ND1 . HIS D 3 12  ? 20.26800  30.71500 -45.07600 1.000 169.18727 ?  12  HIS F ND1 1 
ATOM   3784 C CD2 . HIS D 3 12  ? 19.96900  29.44200 -43.32800 1.000 168.49123 ?  12  HIS F CD2 1 
ATOM   3785 C CE1 . HIS D 3 12  ? 21.46100  30.45100 -44.57600 1.000 160.25772 ?  12  HIS F CE1 1 
ATOM   3786 N NE2 . HIS D 3 12  ? 21.30900  29.66300 -43.52900 1.000 156.81685 ?  12  HIS F NE2 1 
ATOM   3787 N N   . GLU D 3 13  ? 18.01000  31.29400 -41.68100 1.000 173.48486 ?  13  GLU F N   1 
ATOM   3788 C CA  . GLU D 3 13  ? 18.69600  31.69700 -40.45600 1.000 160.80355 ?  13  GLU F CA  1 
ATOM   3789 C C   . GLU D 3 13  ? 19.50000  30.53800 -39.86900 1.000 153.26158 ?  13  GLU F C   1 
ATOM   3790 O O   . GLU D 3 13  ? 19.13600  29.36900 -40.02700 1.000 164.70866 ?  13  GLU F O   1 
ATOM   3791 C CB  . GLU D 3 13  ? 17.69500  32.21600 -39.41300 1.000 163.90914 ?  13  GLU F CB  1 
ATOM   3792 N N   . VAL D 3 14  ? 20.61300  30.87900 -39.20400 1.000 160.68208 ?  14  VAL F N   1 
ATOM   3793 C CA  . VAL D 3 14  ? 21.49800  29.92400 -38.54100 1.000 151.07597 ?  14  VAL F CA  1 
ATOM   3794 C C   . VAL D 3 14  ? 21.78000  30.39200 -37.11400 1.000 136.17769 ?  14  VAL F C   1 
ATOM   3795 O O   . VAL D 3 14  ? 21.81300  31.59200 -36.82900 1.000 129.35006 ?  14  VAL F O   1 
ATOM   3796 C CB  . VAL D 3 14  ? 22.81900  29.74700 -39.33700 1.000 139.55589 ?  14  VAL F CB  1 
ATOM   3797 C CG1 . VAL D 3 14  ? 23.82700  28.89800 -38.57300 1.000 124.84847 ?  14  VAL F CG1 1 
ATOM   3798 C CG2 . VAL D 3 14  ? 22.53700  29.13600 -40.69000 1.000 156.92810 ?  14  VAL F CG2 1 
ATOM   3799 N N   . VAL D 3 15  ? 22.00400  29.43000 -36.21800 1.000 146.17854 ?  15  VAL F N   1 
ATOM   3800 C CA  . VAL D 3 15  ? 22.36000  29.68100 -34.82400 1.000 132.94152 ?  15  VAL F CA  1 
ATOM   3801 C C   . VAL D 3 15  ? 23.78200  29.19400 -34.58100 1.000 116.70294 ?  15  VAL F C   1 
ATOM   3802 O O   . VAL D 3 15  ? 24.10700  28.03400 -34.87000 1.000 116.01330 ?  15  VAL F O   1 
ATOM   3803 C CB  . VAL D 3 15  ? 21.38200  28.98800 -33.85900 1.000 140.75113 ?  15  VAL F CB  1 
ATOM   3804 C CG1 . VAL D 3 15  ? 21.73300  29.32800 -32.41500 1.000 126.92446 ?  15  VAL F CG1 1 
ATOM   3805 C CG2 . VAL D 3 15  ? 19.95100  29.39500 -34.17500 1.000 155.71088 ?  15  VAL F CG2 1 
ATOM   3806 N N   . LYS D 3 16  ? 24.62500  30.08100 -34.05100 1.000 139.31850 ?  16  LYS F N   1 
ATOM   3807 C CA  . LYS D 3 16  ? 26.01600  29.74600 -33.77100 1.000 125.17958 ?  16  LYS F CA  1 
ATOM   3808 C C   . LYS D 3 16  ? 26.12500  28.68000 -32.68100 1.000 119.85931 ?  16  LYS F C   1 
ATOM   3809 O O   . LYS D 3 16  ? 25.30300  28.60600 -31.76300 1.000 122.88939 ?  16  LYS F O   1 
ATOM   3810 C CB  . LYS D 3 16  ? 26.78400  31.00300 -33.35900 1.000 120.75822 ?  16  LYS F CB  1 
ATOM   3811 N N   . PHE D 3 17  ? 27.18300  27.86700 -32.78700 1.000 115.27607 ?  17  PHE F N   1 
ATOM   3812 C CA  . PHE D 3 17  ? 27.37800  26.72700 -31.89300 1.000 121.96365 ?  17  PHE F CA  1 
ATOM   3813 C C   . PHE D 3 17  ? 27.43100  27.15100 -30.43100 1.000 137.21987 ?  17  PHE F C   1 
ATOM   3814 O O   . PHE D 3 17  ? 26.86200  26.47600 -29.56400 1.000 140.86896 ?  17  PHE F O   1 
ATOM   3815 C CB  . PHE D 3 17  ? 28.65000  25.97200 -32.27900 1.000 117.67661 ?  17  PHE F CB  1 
ATOM   3816 C CG  . PHE D 3 17  ? 29.07800  24.94100 -31.27000 1.000 124.03516 ?  17  PHE F CG  1 
ATOM   3817 C CD1 . PHE D 3 17  ? 28.16800  24.04100 -30.73400 1.000 124.27122 ?  17  PHE F CD1 1 
ATOM   3818 C CD2 . PHE D 3 17  ? 30.39300  24.88000 -30.84900 1.000 127.66568 ?  17  PHE F CD2 1 
ATOM   3819 C CE1 . PHE D 3 17  ? 28.56700  23.10400 -29.80200 1.000 127.44299 ?  17  PHE F CE1 1 
ATOM   3820 C CE2 . PHE D 3 17  ? 30.79600  23.94400 -29.91700 1.000 131.30245 ?  17  PHE F CE2 1 
ATOM   3821 C CZ  . PHE D 3 17  ? 29.88000  23.05500 -29.39400 1.000 131.18433 ?  17  PHE F CZ  1 
ATOM   3822 N N   . MET D 3 18  ? 28.14800  28.23800 -30.12800 1.000 125.07773 ?  18  MET F N   1 
ATOM   3823 C CA  . MET D 3 18  ? 28.22500  28.70100 -28.74800 1.000 128.48674 ?  18  MET F CA  1 
ATOM   3824 C C   . MET D 3 18  ? 26.82400  28.87900 -28.17600 1.000 130.86334 ?  18  MET F C   1 
ATOM   3825 O O   . MET D 3 18  ? 26.52400  28.41300 -27.06700 1.000 130.80911 ?  18  MET F O   1 
ATOM   3826 C CB  . MET D 3 18  ? 29.00400  30.02200 -28.69100 1.000 127.36452 ?  18  MET F CB  1 
ATOM   3827 C CG  . MET D 3 18  ? 30.47400  29.89900 -28.29600 1.000 125.77698 ?  18  MET F CG  1 
ATOM   3828 S SD  . MET D 3 18  ? 30.83500  29.14800 -26.69900 1.000 127.09912 ?  18  MET F SD  1 
ATOM   3829 C CE  . MET D 3 18  ? 29.49600  29.79000 -25.70100 1.000 129.99183 ?  18  MET F CE  1 
ATOM   3830 N N   . ASP D 3 19  ? 25.92300  29.43700 -28.98300 1.000 128.50433 ?  19  ASP F N   1 
ATOM   3831 C CA  . ASP D 3 19  ? 24.53900  29.62000 -28.56800 1.000 130.95634 ?  19  ASP F CA  1 
ATOM   3832 C C   . ASP D 3 19  ? 23.81700  28.28700 -28.42600 1.000 129.38286 ?  19  ASP F C   1 
ATOM   3833 O O   . ASP D 3 19  ? 23.05100  28.09100 -27.48000 1.000 127.83209 ?  19  ASP F O   1 
ATOM   3834 C CB  . ASP D 3 19  ? 23.81900  30.51000 -29.57100 1.000 131.14724 ?  19  ASP F CB  1 
ATOM   3835 C CG  . ASP D 3 19  ? 24.54700  31.80200 -29.80500 1.000 128.62706 ?  19  ASP F CG  1 
ATOM   3836 O OD1 . ASP D 3 19  ? 25.27200  32.23300 -28.88300 1.000 128.80589 ?  19  ASP F OD1 1 
ATOM   3837 O OD2 . ASP D 3 19  ? 24.40600  32.37400 -30.90900 1.000 122.53604 ?  19  ASP F OD2 1 
ATOM   3838 N N   . VAL D 3 20  ? 24.00500  27.37400 -29.38300 1.000 139.70346 ?  20  VAL F N   1 
ATOM   3839 C CA  . VAL D 3 20  ? 23.32700  26.07800 -29.31500 1.000 132.03087 ?  20  VAL F CA  1 
ATOM   3840 C C   . VAL D 3 20  ? 23.68700  25.35600 -28.02100 1.000 135.65416 ?  20  VAL F C   1 
ATOM   3841 O O   . VAL D 3 20  ? 22.81000  24.89300 -27.28300 1.000 132.28563 ?  20  VAL F O   1 
ATOM   3842 C CB  . VAL D 3 20  ? 23.66400  25.22000 -30.54700 1.000 117.66974 ?  20  VAL F CB  1 
ATOM   3843 C CG1 . VAL D 3 20  ? 22.90500  23.90500 -30.48000 1.000 114.22493 ?  20  VAL F CG1 1 
ATOM   3844 C CG2 . VAL D 3 20  ? 23.35000  25.97300 -31.83600 1.000 106.07991 ?  20  VAL F CG2 1 
ATOM   3845 N N   . TYR D 3 21  ? 24.98700  25.24700 -27.72900 1.000 120.23574 ?  21  TYR F N   1 
ATOM   3846 C CA  . TYR D 3 21  ? 25.40900  24.62900 -26.47700 1.000 121.33353 ?  21  TYR F CA  1 
ATOM   3847 C C   . TYR D 3 21  ? 24.79800  25.36400 -25.29400 1.000 121.42880 ?  21  TYR F C   1 
ATOM   3848 O O   . TYR D 3 21  ? 24.35500  24.73700 -24.32400 1.000 118.92774 ?  21  TYR F O   1 
ATOM   3849 C CB  . TYR D 3 21  ? 26.93600  24.60000 -26.38000 1.000 122.89372 ?  21  TYR F CB  1 
ATOM   3850 C CG  . TYR D 3 21  ? 27.49900  23.69200 -25.29600 1.000 120.53423 ?  21  TYR F CG  1 
ATOM   3851 C CD1 . TYR D 3 21  ? 27.31500  23.98100 -23.95100 1.000 119.91981 ?  21  TYR F CD1 1 
ATOM   3852 C CD2 . TYR D 3 21  ? 28.24000  22.56200 -25.62300 1.000 119.00205 ?  21  TYR F CD2 1 
ATOM   3853 C CE1 . TYR D 3 21  ? 27.82700  23.16200 -22.96300 1.000 118.14284 ?  21  TYR F CE1 1 
ATOM   3854 C CE2 . TYR D 3 21  ? 28.76500  21.74300 -24.63900 1.000 116.80085 ?  21  TYR F CE2 1 
ATOM   3855 C CZ  . TYR D 3 21  ? 28.55600  22.04900 -23.31300 1.000 116.62117 ?  21  TYR F CZ  1 
ATOM   3856 O OH  . TYR D 3 21  ? 29.07600  21.23700 -22.33200 1.000 115.38367 ?  21  TYR F OH  1 
ATOM   3857 N N   . GLN D 3 22  ? 24.76900  26.69700 -25.35400 1.000 126.76736 ?  22  GLN F N   1 
ATOM   3858 C CA  . GLN D 3 22  ? 24.31900  27.46800 -24.20000 1.000 126.08828 ?  22  GLN F CA  1 
ATOM   3859 C C   . GLN D 3 22  ? 22.82800  27.27500 -23.93300 1.000 122.95566 ?  22  GLN F C   1 
ATOM   3860 O O   . GLN D 3 22  ? 22.42200  26.98300 -22.80300 1.000 119.65803 ?  22  GLN F O   1 
ATOM   3861 C CB  . GLN D 3 22  ? 24.62600  28.94200 -24.43400 1.000 128.54244 ?  22  GLN F CB  1 
ATOM   3862 C CG  . GLN D 3 22  ? 24.84900  29.71400 -23.17800 1.000 129.16122 ?  22  GLN F CG  1 
ATOM   3863 C CD  . GLN D 3 22  ? 26.16800  29.35400 -22.54700 1.000 130.59018 ?  22  GLN F CD  1 
ATOM   3864 O OE1 . GLN D 3 22  ? 26.27400  29.22800 -21.33200 1.000 130.01050 ?  22  GLN F OE1 1 
ATOM   3865 N NE2 . GLN D 3 22  ? 27.17700  29.12200 -23.38400 1.000 131.12767 ?  22  GLN F NE2 1 
ATOM   3866 N N   . ARG D 3 23  ? 22.00100  27.42700 -24.96700 1.000 133.42724 ?  23  ARG F N   1 
ATOM   3867 C CA  . ARG D 3 23  ? 20.55200  27.41500 -24.79300 1.000 130.02971 ?  23  ARG F CA  1 
ATOM   3868 C C   . ARG D 3 23  ? 19.99900  26.02100 -24.53500 1.000 122.78494 ?  23  ARG F C   1 
ATOM   3869 O O   . ARG D 3 23  ? 18.96900  25.88400 -23.86600 1.000 121.22772 ?  23  ARG F O   1 
ATOM   3870 C CB  . ARG D 3 23  ? 19.88900  28.01600 -26.02500 1.000 130.44913 ?  23  ARG F CB  1 
ATOM   3871 C CG  . ARG D 3 23  ? 20.19100  29.48300 -26.21700 1.000 136.17407 ?  23  ARG F CG  1 
ATOM   3872 C CD  . ARG D 3 23  ? 19.66000  29.89900 -27.55300 1.000 131.52128 ?  23  ARG F CD  1 
ATOM   3873 N NE  . ARG D 3 23  ? 18.22200  29.68100 -27.60300 1.000 121.63942 ?  23  ARG F NE  1 
ATOM   3874 C CZ  . ARG D 3 23  ? 17.49900  29.72500 -28.71200 1.000 110.65879 ?  23  ARG F CZ  1 
ATOM   3875 N NH1 . ARG D 3 23  ? 18.04500  30.02400 -29.87800 1.000 106.15735 ?  23  ARG F NH1 1 
ATOM   3876 N NH2 . ARG D 3 23  ? 16.19600  29.47000 -28.64800 1.000 105.43451 ?  23  ARG F NH2 1 
ATOM   3877 N N   . SER D 3 24  ? 20.63300  24.98600 -25.07400 1.000 112.96966 ?  24  SER F N   1 
ATOM   3878 C CA  . SER D 3 24  ? 20.23300  23.60800 -24.79400 1.000 118.07865 ?  24  SER F CA  1 
ATOM   3879 C C   . SER D 3 24  ? 21.12200  23.00600 -23.72400 1.000 116.88864 ?  24  SER F C   1 
ATOM   3880 O O   . SER D 3 24  ? 21.68400  21.93300 -23.90300 1.000 119.13467 ?  24  SER F O   1 
ATOM   3881 C CB  . SER D 3 24  ? 20.27200  22.77000 -26.06300 1.000 121.77762 ?  24  SER F CB  1 
ATOM   3882 O OG  . SER D 3 24  ? 21.53200  22.87000 -26.70100 1.000 117.96337 ?  24  SER F OG  1 
ATOM   3883 N N   . TYR D 3 25  ? 21.27700  23.74400 -22.63900 1.000 123.45974 ?  25  TYR F N   1 
ATOM   3884 C CA  . TYR D 3 25  ? 22.04400  23.14100 -21.53400 1.000 122.45125 ?  25  TYR F CA  1 
ATOM   3885 C C   . TYR D 3 25  ? 21.08300  22.82200 -20.40100 1.000 121.80562 ?  25  TYR F C   1 
ATOM   3886 O O   . TYR D 3 25  ? 19.88900  23.04900 -20.54400 1.000 122.19149 ?  25  TYR F O   1 
ATOM   3887 C CB  . TYR D 3 25  ? 23.17600  24.05600 -21.06500 1.000 118.64062 ?  25  TYR F CB  1 
ATOM   3888 C CG  . TYR D 3 25  ? 24.26500  23.32800 -20.32100 1.000 119.40773 ?  25  TYR F CG  1 
ATOM   3889 C CD1 . TYR D 3 25  ? 25.11000  22.45200 -20.97800 1.000 123.79510 ?  25  TYR F CD1 1 
ATOM   3890 C CD2 . TYR D 3 25  ? 24.42700  23.48400 -18.95600 1.000 118.10547 ?  25  TYR F CD2 1 
ATOM   3891 C CE1 . TYR D 3 25  ? 26.10100  21.76200 -20.30100 1.000 126.51353 ?  25  TYR F CE1 1 
ATOM   3892 C CE2 . TYR D 3 25  ? 25.41100  22.80100 -18.26300 1.000 121.29313 ?  25  TYR F CE2 1 
ATOM   3893 C CZ  . TYR D 3 25  ? 26.25400  21.94000 -18.93900 1.000 125.44566 ?  25  TYR F CZ  1 
ATOM   3894 O OH  . TYR D 3 25  ? 27.23600  21.26400 -18.25900 1.000 130.19942 ?  25  TYR F OH  1 
ATOM   3895 N N   . CYS D 3 26  ? 21.58600  22.18800 -19.36800 1.000 130.23534 ?  26  CYS F N   1 
ATOM   3896 C CA  . CYS D 3 26  ? 20.82800  21.88700 -18.16000 1.000 128.61030 ?  26  CYS F CA  1 
ATOM   3897 C C   . CYS D 3 26  ? 20.39000  23.16700 -17.45900 1.000 123.93549 ?  26  CYS F C   1 
ATOM   3898 O O   . CYS D 3 26  ? 21.22800  23.91600 -16.94200 1.000 121.56234 ?  26  CYS F O   1 
ATOM   3899 C CB  . CYS D 3 26  ? 21.67800  21.03900 -17.21500 1.000 132.10186 ?  26  CYS F CB  1 
ATOM   3900 S SG  . CYS D 3 26  ? 20.74900  20.28700 -15.89100 1.000 133.42933 ?  26  CYS F SG  1 
ATOM   3901 N N   . HIS D 3 27  ? 19.07800  23.42200 -17.44300 1.000 123.24073 ?  27  HIS F N   1 
ATOM   3902 C CA  . HIS D 3 27  ? 18.52600  24.65800 -16.90500 1.000 117.90174 ?  27  HIS F CA  1 
ATOM   3903 C C   . HIS D 3 27  ? 17.00600  24.59500 -16.81300 1.000 116.90311 ?  27  HIS F C   1 
ATOM   3904 O O   . HIS D 3 27  ? 16.36300  23.90600 -17.61600 1.000 119.18154 ?  27  HIS F O   1 
ATOM   3905 C CB  . HIS D 3 27  ? 18.94400  25.84600 -17.77200 1.000 118.23840 ?  27  HIS F CB  1 
ATOM   3906 C CG  . HIS D 3 27  ? 18.21600  25.93200 -19.07400 1.000 120.44476 ?  27  HIS F CG  1 
ATOM   3907 N ND1 . HIS D 3 27  ? 18.69200  25.35100 -20.22700 1.000 127.50484 ?  27  HIS F ND1 1 
ATOM   3908 C CD2 . HIS D 3 27  ? 17.05100  26.53300 -19.40700 1.000 112.08127 ?  27  HIS F CD2 1 
ATOM   3909 C CE1 . HIS D 3 27  ? 17.84700  25.58300 -21.21400 1.000 126.87045 ?  27  HIS F CE1 1 
ATOM   3910 N NE2 . HIS D 3 27  ? 16.84400  26.30100 -20.74400 1.000 113.97468 ?  27  HIS F NE2 1 
ATOM   3911 N N   . PRO D 3 28  ? 16.39500  25.29300 -15.85800 1.000 127.27583 ?  28  PRO F N   1 
ATOM   3912 C CA  . PRO D 3 28  ? 14.92800  25.31800 -15.79300 1.000 125.94403 ?  28  PRO F CA  1 
ATOM   3913 C C   . PRO D 3 28  ? 14.34000  26.02400 -17.00600 1.000 122.27854 ?  28  PRO F C   1 
ATOM   3914 O O   . PRO D 3 28  ? 14.69600  27.16200 -17.31600 1.000 119.33316 ?  28  PRO F O   1 
ATOM   3915 C CB  . PRO D 3 28  ? 14.64000  26.09000 -14.50200 1.000 123.08622 ?  28  PRO F CB  1 
ATOM   3916 C CG  . PRO D 3 28  ? 15.87200  25.92700 -13.69900 1.000 124.80889 ?  28  PRO F CG  1 
ATOM   3917 C CD  . PRO D 3 28  ? 17.00500  25.92600 -14.67900 1.000 125.53089 ?  28  PRO F CD  1 
ATOM   3918 N N   . ILE D 3 29  ? 13.43200  25.33700 -17.68400 1.000 128.86724 ?  29  ILE F N   1 
ATOM   3919 C CA  . ILE D 3 29  ? 12.73300  25.83400 -18.85800 1.000 125.29532 ?  29  ILE F CA  1 
ATOM   3920 C C   . ILE D 3 29  ? 11.24200  25.81800 -18.55900 1.000 125.10867 ?  29  ILE F C   1 
ATOM   3921 O O   . ILE D 3 29  ? 10.74900  24.90800 -17.88000 1.000 128.00755 ?  29  ILE F O   1 
ATOM   3922 C CB  . ILE D 3 29  ? 13.04800  24.97500 -20.10200 1.000 125.40888 ?  29  ILE F CB  1 
ATOM   3923 C CG1 . ILE D 3 29  ? 12.11900  25.32800 -21.26500 1.000 122.59813 ?  29  ILE F CG1 1 
ATOM   3924 C CG2 . ILE D 3 29  ? 12.93800  23.49400 -19.77400 1.000 129.75343 ?  29  ILE F CG2 1 
ATOM   3925 C CD1 . ILE D 3 29  ? 12.24500  26.75200 -21.74900 1.000 119.62619 ?  29  ILE F CD1 1 
ATOM   3926 N N   . GLU D 3 30  ? 10.53000  26.84400 -19.02600 1.000 130.60990 ?  30  GLU F N   1 
ATOM   3927 C CA  . GLU D 3 30  ? 9.07800   26.77600 -19.01000 1.000 130.98890 ?  30  GLU F CA  1 
ATOM   3928 C C   . GLU D 3 30  ? 8.65600   25.51300 -19.73800 1.000 131.89296 ?  30  GLU F C   1 
ATOM   3929 O O   . GLU D 3 30  ? 8.88800   25.37200 -20.94000 1.000 131.01399 ?  30  GLU F O   1 
ATOM   3930 C CB  . GLU D 3 30  ? 8.46500   28.00600 -19.67900 1.000 129.57401 ?  30  GLU F CB  1 
ATOM   3931 C CG  . GLU D 3 30  ? 6.98600   27.83200 -19.99800 1.000 130.09209 ?  30  GLU F CG  1 
ATOM   3932 C CD  . GLU D 3 30  ? 6.23800   29.14600 -20.10300 1.000 129.94079 ?  30  GLU F CD  1 
ATOM   3933 O OE1 . GLU D 3 30  ? 6.18000   29.89200 -19.09800 1.000 130.73390 ?  30  GLU F OE1 1 
ATOM   3934 O OE2 . GLU D 3 30  ? 5.71600   29.43000 -21.20500 1.000 129.55628 ?  30  GLU F OE2 1 
ATOM   3935 N N   . THR D 3 31  ? 8.04200   24.59700 -19.00000 1.000 130.30224 ?  31  THR F N   1 
ATOM   3936 C CA  . THR D 3 31  ? 7.59700   23.31000 -19.50000 1.000 133.37605 ?  31  THR F CA  1 
ATOM   3937 C C   . THR D 3 31  ? 6.11300   23.19300 -19.20800 1.000 134.68434 ?  31  THR F C   1 
ATOM   3938 O O   . THR D 3 31  ? 5.68500   23.38400 -18.06400 1.000 135.85708 ?  31  THR F O   1 
ATOM   3939 C CB  . THR D 3 31  ? 8.36400   22.17000 -18.81800 1.000 137.87945 ?  31  THR F CB  1 
ATOM   3940 O OG1 . THR D 3 31  ? 9.77200   22.36300 -19.00300 1.000 136.81152 ?  31  THR F OG1 1 
ATOM   3941 C CG2 . THR D 3 31  ? 7.95900   20.82900 -19.39900 1.000 142.20059 ?  31  THR F CG2 1 
ATOM   3942 N N   . LEU D 3 32  ? 5.33100   22.90900 -20.23800 1.000 132.95382 ?  32  LEU F N   1 
ATOM   3943 C CA  . LEU D 3 32  ? 3.89800   22.75600 -20.05800 1.000 134.52561 ?  32  LEU F CA  1 
ATOM   3944 C C   . LEU D 3 32  ? 3.61700   21.33400 -19.59400 1.000 140.46561 ?  32  LEU F C   1 
ATOM   3945 O O   . LEU D 3 32  ? 4.01900   20.37000 -20.25300 1.000 142.99953 ?  32  LEU F O   1 
ATOM   3946 C CB  . LEU D 3 32  ? 3.17800   23.06900 -21.37100 1.000 132.38017 ?  32  LEU F CB  1 
ATOM   3947 C CG  . LEU D 3 32  ? 3.34400   24.55000 -21.72400 1.000 128.66881 ?  32  LEU F CG  1 
ATOM   3948 C CD1 . LEU D 3 32  ? 3.04200   24.83700 -23.18700 1.000 128.03885 ?  32  LEU F CD1 1 
ATOM   3949 C CD2 . LEU D 3 32  ? 2.49700   25.41400 -20.80300 1.000 128.39640 ?  32  LEU F CD2 1 
ATOM   3950 N N   . VAL D 3 33  ? 2.94600   21.20400 -18.45100 1.000 136.26874 ?  33  VAL F N   1 
ATOM   3951 C CA  . VAL D 3 33  ? 2.75500   19.91700 -17.79300 1.000 143.09533 ?  33  VAL F CA  1 
ATOM   3952 C C   . VAL D 3 33  ? 1.26600   19.71800 -17.57600 1.000 145.60692 ?  33  VAL F C   1 
ATOM   3953 O O   . VAL D 3 33  ? 0.61800   20.54900 -16.93400 1.000 143.96683 ?  33  VAL F O   1 
ATOM   3954 C CB  . VAL D 3 33  ? 3.49700   19.84900 -16.44300 1.000 145.53591 ?  33  VAL F CB  1 
ATOM   3955 C CG1 . VAL D 3 33  ? 3.36800   18.46300 -15.83500 1.000 153.82100 ?  33  VAL F CG1 1 
ATOM   3956 C CG2 . VAL D 3 33  ? 4.95500   20.25400 -16.60500 1.000 142.05015 ?  33  VAL F CG2 1 
ATOM   3957 N N   . ASP D 3 34  ? 0.72900   18.60700 -18.07100 1.000 139.99593 ?  34  ASP F N   1 
ATOM   3958 C CA  . ASP D 3 34  ? -0.67000  18.31400 -17.80700 1.000 142.49688 ?  34  ASP F CA  1 
ATOM   3959 C C   . ASP D 3 34  ? -0.85900  18.04300 -16.32300 1.000 147.84062 ?  34  ASP F C   1 
ATOM   3960 O O   . ASP D 3 34  ? -0.04300  17.36500 -15.69300 1.000 152.63137 ?  34  ASP F O   1 
ATOM   3961 C CB  . ASP D 3 34  ? -1.14300  17.12100 -18.63300 1.000 145.48946 ?  34  ASP F CB  1 
ATOM   3962 C CG  . ASP D 3 34  ? -0.19600  15.94800 -18.55200 1.000 150.73432 ?  34  ASP F CG  1 
ATOM   3963 O OD1 . ASP D 3 34  ? 0.94700   16.14200 -18.08200 1.000 151.17170 ?  34  ASP F OD1 1 
ATOM   3964 O OD2 . ASP D 3 34  ? -0.59500  14.83200 -18.94800 1.000 154.40313 ?  34  ASP F OD2 1 
ATOM   3965 N N   . ILE D 3 35  ? -1.91700  18.62600 -15.75400 1.000 138.49750 ?  35  ILE F N   1 
ATOM   3966 C CA  . ILE D 3 35  ? -2.15600  18.47600 -14.32300 1.000 143.78915 ?  35  ILE F CA  1 
ATOM   3967 C C   . ILE D 3 35  ? -2.39400  17.01400 -13.97600 1.000 151.00885 ?  35  ILE F C   1 
ATOM   3968 O O   . ILE D 3 35  ? -2.08500  16.56900 -12.86300 1.000 157.23744 ?  35  ILE F O   1 
ATOM   3969 C CB  . ILE D 3 35  ? -3.34200  19.35100 -13.87400 1.000 142.09891 ?  35  ILE F CB  1 
ATOM   3970 C CG1 . ILE D 3 35  ? -3.14300  20.80800 -14.29700 1.000 134.91346 ?  35  ILE F CG1 1 
ATOM   3971 C CG2 . ILE D 3 35  ? -3.49800  19.26400 -12.36900 1.000 146.76582 ?  35  ILE F CG2 1 
ATOM   3972 C CD1 . ILE D 3 35  ? -4.21200  21.75400 -13.78000 1.000 133.71124 ?  35  ILE F CD1 1 
ATOM   3973 N N   . PHE D 3 36  ? -2.93200  16.24000 -14.92600 1.000 149.34646 ?  36  PHE F N   1 
ATOM   3974 C CA  . PHE D 3 36  ? -3.16300  14.81900 -14.68800 1.000 156.08406 ?  36  PHE F CA  1 
ATOM   3975 C C   . PHE D 3 36  ? -1.88000  14.11800 -14.26000 1.000 162.19864 ?  36  PHE F C   1 
ATOM   3976 O O   . PHE D 3 36  ? -1.89600  13.27400 -13.35700 1.000 168.56171 ?  36  PHE F O   1 
ATOM   3977 C CB  . PHE D 3 36  ? -3.74900  14.17100 -15.94300 1.000 153.87196 ?  36  PHE F CB  1 
ATOM   3978 N N   . GLN D 3 37  ? -0.75800  14.44800 -14.90400 1.000 155.38447 ?  37  GLN F N   1 
ATOM   3979 C CA  . GLN D 3 37  ? 0.50700   13.81900 -14.54600 1.000 161.36029 ?  37  GLN F CA  1 
ATOM   3980 C C   . GLN D 3 37  ? 0.90000   14.12900 -13.10600 1.000 165.40317 ?  37  GLN F C   1 
ATOM   3981 O O   . GLN D 3 37  ? 1.53900   13.30100 -12.44600 1.000 170.20149 ?  37  GLN F O   1 
ATOM   3982 C CB  . GLN D 3 37  ? 1.60900   14.27000 -15.50700 1.000 155.47205 ?  37  GLN F CB  1 
ATOM   3983 N N   . GLU D 3 38  ? 0.51300   15.30400 -12.59700 1.000 171.33972 ?  38  GLU F N   1 
ATOM   3984 C CA  . GLU D 3 38  ? 0.92200   15.77100 -11.27400 1.000 167.98694 ?  38  GLU F CA  1 
ATOM   3985 C C   . GLU D 3 38  ? -0.06000  15.38300 -10.17000 1.000 170.93970 ?  38  GLU F C   1 
ATOM   3986 O O   . GLU D 3 38  ? 0.36900   14.97600 -9.08300  1.000 172.25349 ?  38  GLU F O   1 
ATOM   3987 C CB  . GLU D 3 38  ? 1.13100   17.28800 -11.29800 1.000 158.81597 ?  38  GLU F CB  1 
ATOM   3988 C CG  . GLU D 3 38  ? 2.02200   17.76800 -12.44500 1.000 153.41823 ?  38  GLU F CG  1 
ATOM   3989 C CD  . GLU D 3 38  ? 3.40000   17.11200 -12.44500 1.000 154.77629 ?  38  GLU F CD  1 
ATOM   3990 O OE1 . GLU D 3 38  ? 3.55900   16.04300 -13.08100 1.000 160.14954 ?  38  GLU F OE1 1 
ATOM   3991 O OE2 . GLU D 3 38  ? 4.31900   17.66200 -11.80000 1.000 151.30114 ?  38  GLU F OE2 1 
ATOM   3992 N N   . TYR D 3 39  ? -1.36900  15.50200 -10.41000 1.000 160.94488 ?  39  TYR F N   1 
ATOM   3993 C CA  . TYR D 3 39  ? -2.36500  15.11900 -9.41500  1.000 161.71699 ?  39  TYR F CA  1 
ATOM   3994 C C   . TYR D 3 39  ? -3.16100  13.92900 -9.93200  1.000 167.77367 ?  39  TYR F C   1 
ATOM   3995 O O   . TYR D 3 39  ? -4.28800  14.10300 -10.41600 1.000 166.90015 ?  39  TYR F O   1 
ATOM   3996 C CB  . TYR D 3 39  ? -3.32600  16.26900 -9.09600  1.000 156.14075 ?  39  TYR F CB  1 
ATOM   3997 C CG  . TYR D 3 39  ? -2.85100  17.31800 -8.10900  1.000 147.70934 ?  39  TYR F CG  1 
ATOM   3998 C CD1 . TYR D 3 39  ? -2.61400  16.99600 -6.77700  1.000 145.93545 ?  39  TYR F CD1 1 
ATOM   3999 C CD2 . TYR D 3 39  ? -2.70300  18.64400 -8.49700  1.000 140.58682 ?  39  TYR F CD2 1 
ATOM   4000 C CE1 . TYR D 3 39  ? -2.20900  17.95700 -5.87000  1.000 137.28058 ?  39  TYR F CE1 1 
ATOM   4001 C CE2 . TYR D 3 39  ? -2.29800  19.61300 -7.59900  1.000 130.91458 ?  39  TYR F CE2 1 
ATOM   4002 C CZ  . TYR D 3 39  ? -2.05000  19.26800 -6.28900  1.000 129.42854 ?  39  TYR F CZ  1 
ATOM   4003 O OH  . TYR D 3 39  ? -1.64700  20.24100 -5.39900  1.000 120.66337 ?  39  TYR F OH  1 
ATOM   4004 N N   . PRO D 3 40  ? -2.62000  12.70900 -9.86100  1.000 160.45278 ?  40  PRO F N   1 
ATOM   4005 C CA  . PRO D 3 40  ? -3.32800  11.56200 -10.44700 1.000 163.76667 ?  40  PRO F CA  1 
ATOM   4006 C C   . PRO D 3 40  ? -4.49000  11.05100 -9.61400  1.000 164.59155 ?  40  PRO F C   1 
ATOM   4007 O O   . PRO D 3 40  ? -5.34600  10.34100 -10.15300 1.000 165.08191 ?  40  PRO F O   1 
ATOM   4008 C CB  . PRO D 3 40  ? -2.23100  10.48300 -10.53300 1.000 167.70987 ?  40  PRO F CB  1 
ATOM   4009 C CG  . PRO D 3 40  ? -0.92900  11.21300 -10.29500 1.000 166.11241 ?  40  PRO F CG  1 
ATOM   4010 C CD  . PRO D 3 40  ? -1.30300  12.31200 -9.35100  1.000 161.54784 ?  40  PRO F CD  1 
ATOM   4011 N N   . ASP D 3 41  ? -4.58900  11.43900 -8.34200  1.000 166.13417 ?  41  ASP F N   1 
ATOM   4012 C CA  . ASP D 3 41  ? -5.61300  10.85600 -7.48500  1.000 166.33443 ?  41  ASP F CA  1 
ATOM   4013 C C   . ASP D 3 41  ? -6.95100  11.56400 -7.62200  1.000 164.16158 ?  41  ASP F C   1 
ATOM   4014 O O   . ASP D 3 41  ? -7.99800  10.92800 -7.46300  1.000 164.96326 ?  41  ASP F O   1 
ATOM   4015 C CB  . ASP D 3 41  ? -5.15600  10.88100 -6.02700  1.000 164.89012 ?  41  ASP F CB  1 
ATOM   4016 N N   . GLU D 3 42  ? -6.94700  12.85200 -7.94700  1.000 158.62643 ?  42  GLU F N   1 
ATOM   4017 C CA  . GLU D 3 42  ? -8.20400  13.54500 -8.19200  1.000 156.68444 ?  42  GLU F CA  1 
ATOM   4018 C C   . GLU D 3 42  ? -8.74700  13.13000 -9.55300  1.000 156.90122 ?  42  GLU F C   1 
ATOM   4019 O O   . GLU D 3 42  ? -8.83900  13.95400 -10.46700 1.000 153.76648 ?  42  GLU F O   1 
ATOM   4020 C CB  . GLU D 3 42  ? -8.00500  15.06200 -8.11900  1.000 152.36986 ?  42  GLU F CB  1 
ATOM   4021 N N   . ILE D 3 43  ? -9.09600  11.84900 -9.69700  1.000 163.53921 ?  43  ILE F N   1 
ATOM   4022 C CA  . ILE D 3 43  ? -9.56300  11.32400 -10.97900 1.000 162.29415 ?  43  ILE F CA  1 
ATOM   4023 C C   . ILE D 3 43  ? -10.95700 11.84000 -11.31200 1.000 159.73171 ?  43  ILE F C   1 
ATOM   4024 O O   . ILE D 3 43  ? -11.23000 12.24000 -12.45000 1.000 156.22227 ?  43  ILE F O   1 
ATOM   4025 C CB  . ILE D 3 43  ? -9.52600  9.78700  -10.97600 1.000 165.09121 ?  43  ILE F CB  1 
ATOM   4026 N N   . GLU D 3 44  ? -11.86900 11.81800 -10.33800 1.000 163.39548 ?  44  GLU F N   1 
ATOM   4027 C CA  . GLU D 3 44  ? -13.24500 12.21300 -10.61500 1.000 161.98266 ?  44  GLU F CA  1 
ATOM   4028 C C   . GLU D 3 44  ? -13.39700 13.73000 -10.63000 1.000 159.30439 ?  44  GLU F C   1 
ATOM   4029 O O   . GLU D 3 44  ? -14.26700 14.28700 -9.95100  1.000 159.59198 ?  44  GLU F O   1 
ATOM   4030 C CB  . GLU D 3 44  ? -14.18900 11.59000 -9.58400  1.000 167.20081 ?  44  GLU F CB  1 
ATOM   4031 N N   . TYR D 3 45  ? -12.56700 14.39100 -11.43000 1.000 157.39360 ?  45  TYR F N   1 
ATOM   4032 C CA  . TYR D 3 45  ? -12.55700 15.83700 -11.56900 1.000 154.05761 ?  45  TYR F CA  1 
ATOM   4033 C C   . TYR D 3 45  ? -11.76200 16.16600 -12.83000 1.000 149.71181 ?  45  TYR F C   1 
ATOM   4034 O O   . TYR D 3 45  ? -10.55400 15.90600 -12.88400 1.000 150.28136 ?  45  TYR F O   1 
ATOM   4035 C CB  . TYR D 3 45  ? -11.91100 16.50900 -10.34500 1.000 154.82561 ?  45  TYR F CB  1 
ATOM   4036 C CG  . TYR D 3 45  ? -12.81800 16.87700 -9.17500  1.000 155.92468 ?  45  TYR F CG  1 
ATOM   4037 C CD1 . TYR D 3 45  ? -13.69900 17.95500 -9.24200  1.000 153.47985 ?  45  TYR F CD1 1 
ATOM   4038 C CD2 . TYR D 3 45  ? -12.74100 16.17500 -7.97900  1.000 158.62739 ?  45  TYR F CD2 1 
ATOM   4039 C CE1 . TYR D 3 45  ? -14.50100 18.30000 -8.15200  1.000 154.43753 ?  45  TYR F CE1 1 
ATOM   4040 C CE2 . TYR D 3 45  ? -13.53200 16.50700 -6.89500  1.000 158.64354 ?  45  TYR F CE2 1 
ATOM   4041 C CZ  . TYR D 3 45  ? -14.40900 17.56700 -6.98100  1.000 156.89401 ?  45  TYR F CZ  1 
ATOM   4042 O OH  . TYR D 3 45  ? -15.19100 17.88200 -5.88900  1.000 157.08105 ?  45  TYR F OH  1 
ATOM   4043 N N   . ILE D 3 46  ? -12.40800 16.71800 -13.84900 1.000 156.50156 ?  46  ILE F N   1 
ATOM   4044 C CA  . ILE D 3 46  ? -11.68600 17.21100 -15.01800 1.000 152.26729 ?  46  ILE F CA  1 
ATOM   4045 C C   . ILE D 3 46  ? -11.21100 18.62000 -14.68700 1.000 148.81432 ?  46  ILE F C   1 
ATOM   4046 O O   . ILE D 3 46  ? -11.83800 19.34000 -13.90000 1.000 148.46788 ?  46  ILE F O   1 
ATOM   4047 C CB  . ILE D 3 46  ? -12.54100 17.15700 -16.30100 1.000 148.88780 ?  46  ILE F CB  1 
ATOM   4048 C CG1 . ILE D 3 46  ? -11.64300 17.01500 -17.53900 1.000 143.53657 ?  46  ILE F CG1 1 
ATOM   4049 C CG2 . ILE D 3 46  ? -13.43800 18.37800 -16.43400 1.000 146.26407 ?  46  ILE F CG2 1 
ATOM   4050 C CD1 . ILE D 3 46  ? -10.86800 15.71100 -17.58500 1.000 145.94948 ?  46  ILE F CD1 1 
ATOM   4051 N N   . PHE D 3 47  ? -10.04500 18.99500 -15.19000 1.000 144.78801 ?  47  PHE F N   1 
ATOM   4052 C CA  . PHE D 3 47  ? -9.47500  20.29700 -14.87400 1.000 140.08869 ?  47  PHE F CA  1 
ATOM   4053 C C   . PHE D 3 47  ? -9.39900  21.17900 -16.11200 1.000 130.64968 ?  47  PHE F C   1 
ATOM   4054 O O   . PHE D 3 47  ? -8.98400  20.72800 -17.18400 1.000 126.91419 ?  47  PHE F O   1 
ATOM   4055 C CB  . PHE D 3 47  ? -8.09500  20.13200 -14.24300 1.000 140.81631 ?  47  PHE F CB  1 
ATOM   4056 C CG  . PHE D 3 47  ? -8.11900  19.35000 -12.96400 1.000 146.51308 ?  47  PHE F CG  1 
ATOM   4057 C CD1 . PHE D 3 47  ? -8.92100  19.75100 -11.91100 1.000 146.01277 ?  47  PHE F CD1 1 
ATOM   4058 C CD2 . PHE D 3 47  ? -7.35200  18.20700 -12.81700 1.000 150.55684 ?  47  PHE F CD2 1 
ATOM   4059 C CE1 . PHE D 3 47  ? -8.95400  19.03200 -10.73300 1.000 148.77463 ?  47  PHE F CE1 1 
ATOM   4060 C CE2 . PHE D 3 47  ? -7.38200  17.48600 -11.63600 1.000 154.22563 ?  47  PHE F CE2 1 
ATOM   4061 C CZ  . PHE D 3 47  ? -8.18500  17.90100 -10.59600 1.000 152.91410 ?  47  PHE F CZ  1 
ATOM   4062 N N   . LYS D 3 48  ? -9.81500  22.43500 -15.96000 1.000 148.93421 ?  48  LYS F N   1 
ATOM   4063 C CA  . LYS D 3 48  ? -9.70900  23.43100 -17.01700 1.000 135.39915 ?  48  LYS F CA  1 
ATOM   4064 C C   . LYS D 3 48  ? -8.83000  24.57400 -16.52800 1.000 125.41702 ?  48  LYS F C   1 
ATOM   4065 O O   . LYS D 3 48  ? -9.16100  25.20600 -15.51300 1.000 125.72925 ?  48  LYS F O   1 
ATOM   4066 C CB  . LYS D 3 48  ? -11.09300 23.95600 -17.41000 1.000 132.44849 ?  48  LYS F CB  1 
ATOM   4067 N N   . PRO D 3 49  ? -7.69000  24.86100 -17.17200 1.000 130.90121 ?  49  PRO F N   1 
ATOM   4068 C CA  . PRO D 3 49  ? -7.11400  24.13900 -18.30900 1.000 129.78623 ?  49  PRO F CA  1 
ATOM   4069 C C   . PRO D 3 49  ? -6.58500  22.79400 -17.84400 1.000 142.41816 ?  49  PRO F C   1 
ATOM   4070 O O   . PRO D 3 49  ? -6.43000  22.56500 -16.64600 1.000 150.81927 ?  49  PRO F O   1 
ATOM   4071 C CB  . PRO D 3 49  ? -6.00600  25.08300 -18.80300 1.000 116.25493 ?  49  PRO F CB  1 
ATOM   4072 C CG  . PRO D 3 49  ? -5.61400  25.85800 -17.59600 1.000 113.84486 ?  49  PRO F CG  1 
ATOM   4073 C CD  . PRO D 3 49  ? -6.89600  26.05300 -16.82700 1.000 118.68094 ?  49  PRO F CD  1 
ATOM   4074 N N   . SER D 3 50  ? -6.33600  21.86500 -18.76300 1.000 126.48605 ?  50  SER F N   1 
ATOM   4075 C CA  . SER D 3 50  ? -5.83400  20.56200 -18.35100 1.000 136.99747 ?  50  SER F CA  1 
ATOM   4076 C C   . SER D 3 50  ? -4.36200  20.61800 -17.96100 1.000 135.61564 ?  50  SER F C   1 
ATOM   4077 O O   . SER D 3 50  ? -3.92000  19.82600 -17.12000 1.000 144.51895 ?  50  SER F O   1 
ATOM   4078 C CB  . SER D 3 50  ? -6.06000  19.53200 -19.45900 1.000 136.99804 ?  50  SER F CB  1 
ATOM   4079 O OG  . SER D 3 50  ? -5.64200  20.01300 -20.72600 1.000 125.10794 ?  50  SER F OG  1 
ATOM   4080 N N   . CYS D 3 51  ? -3.59100  21.52200 -18.55600 1.000 137.72428 ?  51  CYS F N   1 
ATOM   4081 C CA  . CYS D 3 51  ? -2.16900  21.62700 -18.26700 1.000 135.33140 ?  51  CYS F CA  1 
ATOM   4082 C C   . CYS D 3 51  ? -1.80200  23.01300 -17.73700 1.000 132.01677 ?  51  CYS F C   1 
ATOM   4083 O O   . CYS D 3 51  ? -2.55500  23.97800 -17.87800 1.000 130.14300 ?  51  CYS F O   1 
ATOM   4084 C CB  . CYS D 3 51  ? -1.34400  21.24900 -19.51300 1.000 130.82142 ?  51  CYS F CB  1 
ATOM   4085 S SG  . CYS D 3 51  ? -1.56700  22.23800 -21.00400 1.000 124.46104 ?  51  CYS F SG  1 
ATOM   4086 N N   . VAL D 3 52  ? -0.62800  23.09200 -17.11000 1.000 131.88705 ?  52  VAL F N   1 
ATOM   4087 C CA  . VAL D 3 52  ? -0.09900  24.32000 -16.50400 1.000 128.46530 ?  52  VAL F CA  1 
ATOM   4088 C C   . VAL D 3 52  ? 1.35100   24.57200 -16.91400 1.000 124.03056 ?  52  VAL F C   1 
ATOM   4089 O O   . VAL D 3 52  ? 2.11600   23.61800 -17.12800 1.000 124.73236 ?  52  VAL F O   1 
ATOM   4090 C CB  . VAL D 3 52  ? -0.21800  24.28000 -14.96500 1.000 132.66086 ?  52  VAL F CB  1 
ATOM   4091 C CG1 . VAL D 3 52  ? -1.65000  24.07700 -14.53600 1.000 138.12047 ?  52  VAL F CG1 1 
ATOM   4092 C CG2 . VAL D 3 52  ? 0.63300   23.15300 -14.38800 1.000 135.76061 ?  52  VAL F CG2 1 
ATOM   4093 N N   . PRO D 3 53  ? 1.77000   25.84200 -17.03700 1.000 124.11102 ?  53  PRO F N   1 
ATOM   4094 C CA  . PRO D 3 53  ? 3.17100   26.13700 -17.36200 1.000 121.54771 ?  53  PRO F CA  1 
ATOM   4095 C C   . PRO D 3 53  ? 4.03900   26.17900 -16.11600 1.000 121.98277 ?  53  PRO F C   1 
ATOM   4096 O O   . PRO D 3 53  ? 3.79900   26.99800 -15.22500 1.000 122.61662 ?  53  PRO F O   1 
ATOM   4097 C CB  . PRO D 3 53  ? 3.08900   27.51300 -18.03700 1.000 119.82225 ?  53  PRO F CB  1 
ATOM   4098 C CG  . PRO D 3 53  ? 1.87700   28.14700 -17.44100 1.000 121.45268 ?  53  PRO F CG  1 
ATOM   4099 C CD  . PRO D 3 53  ? 0.93600   27.05700 -17.00500 1.000 123.80840 ?  53  PRO F CD  1 
ATOM   4100 N N   . LEU D 3 54  ? 5.03200   25.29400 -16.02700 1.000 127.01305 ?  54  LEU F N   1 
ATOM   4101 C CA  . LEU D 3 54  ? 5.88600   25.18600 -14.85200 1.000 127.81845 ?  54  LEU F CA  1 
ATOM   4102 C C   . LEU D 3 54  ? 7.33500   25.18000 -15.30700 1.000 125.93970 ?  54  LEU F C   1 
ATOM   4103 O O   . LEU D 3 54  ? 7.68500   24.45600 -16.23900 1.000 125.72503 ?  54  LEU F O   1 
ATOM   4104 C CB  . LEU D 3 54  ? 5.57500   23.91700 -14.06300 1.000 131.72011 ?  54  LEU F CB  1 
ATOM   4105 C CG  . LEU D 3 54  ? 4.11500   23.84200 -13.62400 1.000 135.19417 ?  54  LEU F CG  1 
ATOM   4106 C CD1 . LEU D 3 54  ? 3.79900   22.48400 -13.03700 1.000 140.20770 ?  54  LEU F CD1 1 
ATOM   4107 C CD2 . LEU D 3 54  ? 3.76800   24.95800 -12.64800 1.000 134.69601 ?  54  LEU F CD2 1 
ATOM   4108 N N   . MET D 3 55  ? 8.17300   25.98200 -14.66700 1.000 135.69397 ?  55  MET F N   1 
ATOM   4109 C CA  . MET D 3 55  ? 9.60100   25.94200 -14.96800 1.000 135.13992 ?  55  MET F CA  1 
ATOM   4110 C C   . MET D 3 55  ? 10.17200  24.63500 -14.43200 1.000 137.16912 ?  55  MET F C   1 
ATOM   4111 O O   . MET D 3 55  ? 10.46000  24.50900 -13.23900 1.000 138.44344 ?  55  MET F O   1 
ATOM   4112 C CB  . MET D 3 55  ? 10.30700  27.16100 -14.38300 1.000 134.99503 ?  55  MET F CB  1 
ATOM   4113 C CG  . MET D 3 55  ? 9.58000   28.45300 -14.68800 1.000 134.42164 ?  55  MET F CG  1 
ATOM   4114 S SD  . MET D 3 55  ? 10.06600  29.13000 -16.28700 1.000 133.17723 ?  55  MET F SD  1 
ATOM   4115 C CE  . MET D 3 55  ? 8.59300   30.06100 -16.71300 1.000 134.07274 ?  55  MET F CE  1 
ATOM   4116 N N   . ARG D 3 56  ? 10.31100  23.66600 -15.33100 1.000 128.94555 ?  56  ARG F N   1 
ATOM   4117 C CA  . ARG D 3 56  ? 10.86500  22.36100 -14.90500 1.000 131.47840 ?  56  ARG F CA  1 
ATOM   4118 C C   . ARG D 3 56  ? 12.26400  22.18600 -15.48800 1.000 131.48199 ?  56  ARG F C   1 
ATOM   4119 O O   . ARG D 3 56  ? 12.62900  22.96200 -16.38700 1.000 129.46493 ?  56  ARG F O   1 
ATOM   4120 C CB  . ARG D 3 56  ? 9.94000   21.21800 -15.32800 1.000 133.69011 ?  56  ARG F CB  1 
ATOM   4121 C CG  . ARG D 3 56  ? 9.28400   20.50000 -14.15900 1.000 136.11036 ?  56  ARG F CG  1 
ATOM   4122 C CD  . ARG D 3 56  ? 9.11800   21.41400 -12.96100 1.000 136.17133 ?  56  ARG F CD  1 
ATOM   4123 N NE  . ARG D 3 56  ? 8.56400   20.72800 -11.80500 1.000 139.11435 ?  56  ARG F NE  1 
ATOM   4124 C CZ  . ARG D 3 56  ? 7.53600   19.89100 -11.85200 1.000 141.66640 ?  56  ARG F CZ  1 
ATOM   4125 N NH1 . ARG D 3 56  ? 6.32600   20.34500 -12.12300 1.000 142.30067 ?  56  ARG F NH1 1 
ATOM   4126 N NH2 . ARG D 3 56  ? 7.71900   18.60200 -11.62300 1.000 144.22685 ?  56  ARG F NH2 1 
ATOM   4127 N N   . CYS D 3 57  ? 13.00200  21.19700 -14.99700 1.000 124.32216 ?  57  CYS F N   1 
ATOM   4128 C CA  . CYS D 3 57  ? 14.35400  20.91800 -15.44400 1.000 126.48454 ?  57  CYS F CA  1 
ATOM   4129 C C   . CYS D 3 57  ? 14.37300  20.43600 -16.88600 1.000 125.30124 ?  57  CYS F C   1 
ATOM   4130 O O   . CYS D 3 57  ? 13.34300  20.12600 -17.48900 1.000 123.32516 ?  57  CYS F O   1 
ATOM   4131 C CB  . CYS D 3 57  ? 15.00500  19.86000 -14.56600 1.000 131.60892 ?  57  CYS F CB  1 
ATOM   4132 S SG  . CYS D 3 57  ? 15.77400  20.52100 -13.10900 1.000 134.15911 ?  57  CYS F SG  1 
ATOM   4133 N N   . GLY D 3 58  ? 15.58100  20.39100 -17.43800 1.000 126.10544 ?  58  GLY F N   1 
ATOM   4134 C CA  . GLY D 3 58  ? 15.77500  19.93600 -18.79600 1.000 125.35432 ?  58  GLY F CA  1 
ATOM   4135 C C   . GLY D 3 58  ? 17.06800  20.42200 -19.41600 1.000 125.31167 ?  58  GLY F C   1 
ATOM   4136 O O   . GLY D 3 58  ? 17.56500  21.49300 -19.06000 1.000 123.77949 ?  58  GLY F O   1 
ATOM   4137 N N   . GLY D 3 59  ? 17.62900  19.63300 -20.33200 1.000 121.70772 ?  59  GLY F N   1 
ATOM   4138 C CA  . GLY D 3 59  ? 18.83200  20.02400 -21.04400 1.000 121.55312 ?  59  GLY F CA  1 
ATOM   4139 C C   . GLY D 3 59  ? 19.97800  19.03200 -21.04300 1.000 126.69074 ?  59  GLY F C   1 
ATOM   4140 O O   . GLY D 3 59  ? 20.05200  18.15300 -20.17900 1.000 131.80657 ?  59  GLY F O   1 
ATOM   4141 N N   . CYS D 3 60  ? 20.88800  19.18100 -22.00900 1.000 122.82074 ?  60  CYS F N   1 
ATOM   4142 C CA  . CYS D 3 60  ? 22.02300  18.27600 -22.13600 1.000 127.58376 ?  60  CYS F CA  1 
ATOM   4143 C C   . CYS D 3 60  ? 23.08300  18.60900 -21.09900 1.000 130.20177 ?  60  CYS F C   1 
ATOM   4144 O O   . CYS D 3 60  ? 23.41700  19.78100 -20.89200 1.000 126.84398 ?  60  CYS F O   1 
ATOM   4145 C CB  . CYS D 3 60  ? 22.65500  18.35800 -23.52900 1.000 125.35731 ?  60  CYS F CB  1 
ATOM   4146 S SG  . CYS D 3 60  ? 21.67200  19.06100 -24.84700 1.000 118.99545 ?  60  CYS F SG  1 
ATOM   4147 N N   . CYS D 3 61  ? 23.61000  17.57800 -20.44700 1.000 123.09983 ?  61  CYS F N   1 
ATOM   4148 C CA  . CYS D 3 61  ? 24.83700  17.72700 -19.68500 1.000 126.24824 ?  61  CYS F CA  1 
ATOM   4149 C C   . CYS D 3 61  ? 26.07600  17.43400 -20.52100 1.000 127.41681 ?  61  CYS F C   1 
ATOM   4150 O O   . CYS D 3 61  ? 27.17900  17.81500 -20.11700 1.000 128.33003 ?  61  CYS F O   1 
ATOM   4151 C CB  . CYS D 3 61  ? 24.81300  16.80400 -18.45900 1.000 133.61194 ?  61  CYS F CB  1 
ATOM   4152 S SG  . CYS D 3 61  ? 23.80200  17.39900 -17.08700 1.000 132.15847 ?  61  CYS F SG  1 
ATOM   4153 N N   . ASN D 3 62  ? 25.91000  16.79200 -21.68400 1.000 133.93327 ?  62  ASN F N   1 
ATOM   4154 C CA  . ASN D 3 62  ? 27.01100  16.49600 -22.60300 1.000 133.85781 ?  62  ASN F CA  1 
ATOM   4155 C C   . ASN D 3 62  ? 28.13300  15.75600 -21.87900 1.000 140.17255 ?  62  ASN F C   1 
ATOM   4156 O O   . ASN D 3 62  ? 29.32100  15.97700 -22.12400 1.000 139.93895 ?  62  ASN F O   1 
ATOM   4157 C CB  . ASN D 3 62  ? 27.52100  17.77200 -23.27400 1.000 127.99771 ?  62  ASN F CB  1 
ATOM   4158 C CG  . ASN D 3 62  ? 26.46500  18.41900 -24.15300 1.000 122.11093 ?  62  ASN F CG  1 
ATOM   4159 O OD1 . ASN D 3 62  ? 25.77800  17.74000 -24.91400 1.000 121.28193 ?  62  ASN F OD1 1 
ATOM   4160 N ND2 . ASN D 3 62  ? 26.32200  19.73500 -24.04000 1.000 118.22773 ?  62  ASN F ND2 1 
ATOM   4161 N N   . ASP D 3 63  ? 27.74100  14.85400 -20.98100 1.000 135.69431 ?  63  ASP F N   1 
ATOM   4162 C CA  . ASP D 3 63  ? 28.68800  14.00000 -20.27300 1.000 143.25276 ?  63  ASP F CA  1 
ATOM   4163 C C   . ASP D 3 63  ? 27.92900  12.85500 -19.62600 1.000 149.88162 ?  63  ASP F C   1 
ATOM   4164 O O   . ASP D 3 63  ? 26.98500  13.08700 -18.86500 1.000 149.43996 ?  63  ASP F O   1 
ATOM   4165 C CB  . ASP D 3 63  ? 29.44000  14.81700 -19.22300 1.000 143.47111 ?  63  ASP F CB  1 
ATOM   4166 C CG  . ASP D 3 63  ? 30.38800  13.98500 -18.41300 1.000 150.96395 ?  63  ASP F CG  1 
ATOM   4167 O OD1 . ASP D 3 63  ? 31.48200  13.68300 -18.92800 1.000 151.88226 ?  63  ASP F OD1 1 
ATOM   4168 O OD2 . ASP D 3 63  ? 30.03700  13.63000 -17.27000 1.000 154.98654 ?  63  ASP F OD2 1 
ATOM   4169 N N   . GLU D 3 64  ? 28.33600  11.62300 -19.94200 1.000 148.86624 ?  64  GLU F N   1 
ATOM   4170 C CA  . GLU D 3 64  ? 27.63400  10.44500 -19.44200 1.000 154.34123 ?  64  GLU F CA  1 
ATOM   4171 C C   . GLU D 3 64  ? 27.60200  10.41200 -17.92200 1.000 158.73354 ?  64  GLU F C   1 
ATOM   4172 O O   . GLU D 3 64  ? 26.57900  10.07100 -17.32000 1.000 158.87739 ?  64  GLU F O   1 
ATOM   4173 C CB  . GLU D 3 64  ? 28.27800  9.17800  -19.99200 1.000 158.67633 ?  64  GLU F CB  1 
ATOM   4174 C CG  . GLU D 3 64  ? 27.53900  8.68600  -21.18900 1.000 154.97930 ?  64  GLU F CG  1 
ATOM   4175 C CD  . GLU D 3 64  ? 26.07100  8.59800  -20.86700 1.000 153.21262 ?  64  GLU F CD  1 
ATOM   4176 O OE1 . GLU D 3 64  ? 25.71200  7.83700  -19.94100 1.000 157.55706 ?  64  GLU F OE1 1 
ATOM   4177 O OE2 . GLU D 3 64  ? 25.27600  9.32600  -21.50300 1.000 146.80774 ?  64  GLU F OE2 1 
ATOM   4178 N N   . GLY D 3 65  ? 28.72900  10.72300 -17.28600 1.000 146.77807 ?  65  GLY F N   1 
ATOM   4179 C CA  . GLY D 3 65  ? 28.79000  10.65000 -15.84000 1.000 149.88219 ?  65  GLY F CA  1 
ATOM   4180 C C   . GLY D 3 65  ? 27.71300  11.46800 -15.16000 1.000 145.71631 ?  65  GLY F C   1 
ATOM   4181 O O   . GLY D 3 65  ? 27.16600  11.05000 -14.13600 1.000 147.82525 ?  65  GLY F O   1 
ATOM   4182 N N   . LEU D 3 66  ? 27.34400  12.60100 -15.75100 1.000 151.14518 ?  66  LEU F N   1 
ATOM   4183 C CA  . LEU D 3 66  ? 26.44200  13.56400 -15.13900 1.000 146.55274 ?  66  LEU F CA  1 
ATOM   4184 C C   . LEU D 3 66  ? 25.07300  13.56600 -15.81300 1.000 142.34231 ?  66  LEU F C   1 
ATOM   4185 O O   . LEU D 3 66  ? 24.90800  13.12600 -16.95500 1.000 141.48155 ?  66  LEU F O   1 
ATOM   4186 C CB  . LEU D 3 66  ? 27.04500  14.97000 -15.22800 1.000 141.34181 ?  66  LEU F CB  1 
ATOM   4187 C CG  . LEU D 3 66  ? 28.49800  15.11400 -14.77300 1.000 143.87066 ?  66  LEU F CG  1 
ATOM   4188 C CD1 . LEU D 3 66  ? 29.16200  16.25900 -15.52100 1.000 137.70554 ?  66  LEU F CD1 1 
ATOM   4189 C CD2 . LEU D 3 66  ? 28.58500  15.34300 -13.27300 1.000 145.98422 ?  66  LEU F CD2 1 
ATOM   4190 N N   . GLU D 3 67  ? 24.09300  14.07800 -15.07600 1.000 150.42664 ?  67  GLU F N   1 
ATOM   4191 C CA  . GLU D 3 67  ? 22.69700  14.12200 -15.48000 1.000 146.08980 ?  67  GLU F CA  1 
ATOM   4192 C C   . GLU D 3 67  ? 22.07300  15.43000 -15.00300 1.000 140.62174 ?  67  GLU F C   1 
ATOM   4193 O O   . GLU D 3 67  ? 22.49900  16.00200 -13.99300 1.000 141.40035 ?  67  GLU F O   1 
ATOM   4194 C CB  . GLU D 3 67  ? 21.91500  12.91500 -14.93100 1.000 148.82382 ?  67  GLU F CB  1 
ATOM   4195 C CG  . GLU D 3 67  ? 21.46100  13.04900 -13.48300 1.000 148.82061 ?  67  GLU F CG  1 
ATOM   4196 C CD  . GLU D 3 67  ? 21.25600  11.70800 -12.79700 1.000 152.31456 ?  67  GLU F CD  1 
ATOM   4197 O OE1 . GLU D 3 67  ? 22.23000  10.93800 -12.70000 1.000 158.13640 ?  67  GLU F OE1 1 
ATOM   4198 O OE2 . GLU D 3 67  ? 20.12300  11.42600 -12.34600 1.000 148.70029 ?  67  GLU F OE2 1 
ATOM   4199 N N   . CYS D 3 68  ? 21.07900  15.90900 -15.76000 1.000 153.21105 ?  68  CYS F N   1 
ATOM   4200 C CA  . CYS D 3 68  ? 20.29700  17.10200 -15.44400 1.000 147.70270 ?  68  CYS F CA  1 
ATOM   4201 C C   . CYS D 3 68  ? 19.35100  16.80500 -14.28900 1.000 148.10301 ?  68  CYS F C   1 
ATOM   4202 O O   . CYS D 3 68  ? 18.28500  16.21200 -14.48200 1.000 146.45811 ?  68  CYS F O   1 
ATOM   4203 C CB  . CYS D 3 68  ? 19.50900  17.54600 -16.67200 1.000 142.15662 ?  68  CYS F CB  1 
ATOM   4204 S SG  . CYS D 3 68  ? 19.34200  19.31300 -16.98100 1.000 135.19701 ?  68  CYS F SG  1 
ATOM   4205 N N   . VAL D 3 69  ? 19.71600  17.23800 -13.08600 1.000 145.97764 ?  69  VAL F N   1 
ATOM   4206 C CA  . VAL D 3 69  ? 18.85400  17.03900 -11.92800 1.000 145.38735 ?  69  VAL F CA  1 
ATOM   4207 C C   . VAL D 3 69  ? 18.45600  18.38900 -11.35000 1.000 141.47925 ?  69  VAL F C   1 
ATOM   4208 O O   . VAL D 3 69  ? 19.25200  19.33800 -11.38200 1.000 141.33252 ?  69  VAL F O   1 
ATOM   4209 C CB  . VAL D 3 69  ? 19.54400  16.18700 -10.85600 1.000 150.81491 ?  69  VAL F CB  1 
ATOM   4210 C CG1 . VAL D 3 69  ? 19.42200  14.72300 -11.19400 1.000 153.51248 ?  69  VAL F CG1 1 
ATOM   4211 C CG2 . VAL D 3 69  ? 21.00200  16.59500 -10.71500 1.000 154.95518 ?  69  VAL F CG2 1 
ATOM   4212 N N   . PRO D 3 70  ? 17.24900  18.51900 -10.80700 1.000 145.83921 ?  70  PRO F N   1 
ATOM   4213 C CA  . PRO D 3 70  ? 16.90000  19.74300 -10.08100 1.000 142.94788 ?  70  PRO F CA  1 
ATOM   4214 C C   . PRO D 3 70  ? 17.66200  19.83900 -8.77200  1.000 145.80824 ?  70  PRO F C   1 
ATOM   4215 O O   . PRO D 3 70  ? 18.03900  18.83400 -8.16700  1.000 149.02815 ?  70  PRO F O   1 
ATOM   4216 C CB  . PRO D 3 70  ? 15.39100  19.60500 -9.85400  1.000 139.23257 ?  70  PRO F CB  1 
ATOM   4217 C CG  . PRO D 3 70  ? 15.11700  18.14200 -9.95800  1.000 140.90590 ?  70  PRO F CG  1 
ATOM   4218 C CD  . PRO D 3 70  ? 16.09300  17.62300 -10.97600 1.000 144.03229 ?  70  PRO F CD  1 
ATOM   4219 N N   . THR D 3 71  ? 17.89100  21.07400 -8.33900  1.000 144.71410 ?  71  THR F N   1 
ATOM   4220 C CA  . THR D 3 71  ? 18.64100  21.31600 -7.11800  1.000 146.60289 ?  71  THR F CA  1 
ATOM   4221 C C   . THR D 3 71  ? 17.89000  22.25400 -6.18400  1.000 142.16003 ?  71  THR F C   1 
ATOM   4222 O O   . THR D 3 71  ? 18.01600  22.14900 -4.96200  1.000 141.72572 ?  71  THR F O   1 
ATOM   4223 C CB  . THR D 3 71  ? 20.01700  21.89200 -7.45600  1.000 148.51176 ?  71  THR F CB  1 
ATOM   4224 O OG1 . THR D 3 71  ? 19.87500  22.93400 -8.43200  1.000 144.34648 ?  71  THR F OG1 1 
ATOM   4225 C CG2 . THR D 3 71  ? 20.92200  20.80900 -7.99600  1.000 153.81973 ?  71  THR F CG2 1 
ATOM   4226 N N   . GLU D 3 72  ? 17.11000  23.17100 -6.74700  1.000 156.14868 ?  72  GLU F N   1 
ATOM   4227 C CA  . GLU D 3 72  ? 16.30000  24.10600 -5.97600  1.000 151.83014 ?  72  GLU F CA  1 
ATOM   4228 C C   . GLU D 3 72  ? 14.85900  23.97000 -6.43400  1.000 149.60176 ?  72  GLU F C   1 
ATOM   4229 O O   . GLU D 3 72  ? 14.57000  24.13000 -7.62500  1.000 148.95271 ?  72  GLU F O   1 
ATOM   4230 C CB  . GLU D 3 72  ? 16.79200  25.54100 -6.16200  1.000 149.15706 ?  72  GLU F CB  1 
ATOM   4231 N N   . GLU D 3 73  ? 13.95400  23.67800 -5.50400  1.000 149.60355 ?  73  GLU F N   1 
ATOM   4232 C CA  . GLU D 3 73  ? 12.56300  23.47600 -5.87100  1.000 148.54342 ?  73  GLU F CA  1 
ATOM   4233 C C   . GLU D 3 73  ? 11.64800  24.28200 -4.96600  1.000 146.80439 ?  73  GLU F C   1 
ATOM   4234 O O   . GLU D 3 73  ? 11.90300  24.44100 -3.76800  1.000 146.68727 ?  73  GLU F O   1 
ATOM   4235 C CB  . GLU D 3 73  ? 12.18500  22.00400 -5.82000  1.000 150.29740 ?  73  GLU F CB  1 
ATOM   4236 C CG  . GLU D 3 73  ? 12.47400  21.32100 -7.13100  1.000 151.47025 ?  73  GLU F CG  1 
ATOM   4237 C CD  . GLU D 3 73  ? 12.11000  19.86300 -7.12300  1.000 152.82729 ?  73  GLU F CD  1 
ATOM   4238 O OE1 . GLU D 3 73  ? 11.44900  19.43600 -6.15800  1.000 152.77573 ?  73  GLU F OE1 1 
ATOM   4239 O OE2 . GLU D 3 73  ? 12.48700  19.14800 -8.07600  1.000 154.00905 ?  73  GLU F OE2 1 
ATOM   4240 N N   . SER D 3 74  ? 10.56100  24.76800 -5.55800  1.000 150.49014 ?  74  SER F N   1 
ATOM   4241 C CA  . SER D 3 74  ? 9.56200   25.52900 -4.81900  1.000 150.20910 ?  74  SER F CA  1 
ATOM   4242 C C   . SER D 3 74  ? 8.20100   25.29100 -5.46000  1.000 151.50320 ?  74  SER F C   1 
ATOM   4243 O O   . SER D 3 74  ? 8.06700   24.48100 -6.37600  1.000 152.03044 ?  74  SER F O   1 
ATOM   4244 C CB  . SER D 3 74  ? 9.93700   27.01600 -4.77600  1.000 148.11378 ?  74  SER F CB  1 
ATOM   4245 O OG  . SER D 3 74  ? 9.86600   27.61000 -6.06300  1.000 146.64430 ?  74  SER F OG  1 
ATOM   4246 N N   . ASN D 3 75  ? 7.17500   25.95900 -4.93700  1.000 150.51905 ?  75  ASN F N   1 
ATOM   4247 C CA  . ASN D 3 75  ? 5.81300   25.70300 -5.38800  1.000 152.96526 ?  75  ASN F CA  1 
ATOM   4248 C C   . ASN D 3 75  ? 5.11200   26.97600 -5.83600  1.000 153.63746 ?  75  ASN F C   1 
ATOM   4249 O O   . ASN D 3 75  ? 5.29200   28.04400 -5.24400  1.000 153.47176 ?  75  ASN F O   1 
ATOM   4250 C CB  . ASN D 3 75  ? 5.00500   24.99800 -4.30300  1.000 155.74067 ?  75  ASN F CB  1 
ATOM   4251 C CG  . ASN D 3 75  ? 5.41200   23.55000 -4.15200  1.000 155.53347 ?  75  ASN F CG  1 
ATOM   4252 O OD1 . ASN D 3 75  ? 6.14000   23.01500 -4.98800  1.000 154.06214 ?  75  ASN F OD1 1 
ATOM   4253 N ND2 . ASN D 3 75  ? 4.95500   22.90000 -3.09700  1.000 157.24632 ?  75  ASN F ND2 1 
ATOM   4254 N N   . ILE D 3 76  ? 4.30000   26.84200 -6.87900  1.000 140.16024 ?  76  ILE F N   1 
ATOM   4255 C CA  . ILE D 3 76  ? 3.45500   27.91800 -7.38000  1.000 141.94488 ?  76  ILE F CA  1 
ATOM   4256 C C   . ILE D 3 76  ? 2.01000   27.45200 -7.31600  1.000 146.49636 ?  76  ILE F C   1 
ATOM   4257 O O   . ILE D 3 76  ? 1.66900   26.38200 -7.83600  1.000 147.31668 ?  76  ILE F O   1 
ATOM   4258 C CB  . ILE D 3 76  ? 3.83300   28.34500 -8.80900  1.000 139.15075 ?  76  ILE F CB  1 
ATOM   4259 C CG1 . ILE D 3 76  ? 2.84700   29.40000 -9.31200  1.000 139.73049 ?  76  ILE F CG1 1 
ATOM   4260 C CG2 . ILE D 3 76  ? 3.88400   27.15400 -9.75900  1.000 138.66443 ?  76  ILE F CG2 1 
ATOM   4261 C CD1 . ILE D 3 76  ? 2.88000   30.68900 -8.52700  1.000 139.81373 ?  76  ILE F CD1 1 
ATOM   4262 N N   . THR D 3 77  ? 1.17100   28.23200 -6.64300  1.000 135.34647 ?  77  THR F N   1 
ATOM   4263 C CA  . THR D 3 77  ? -0.26400  27.98600 -6.62900  1.000 139.71493 ?  77  THR F CA  1 
ATOM   4264 C C   . THR D 3 77  ? -0.89300  28.77700 -7.76400  1.000 139.23205 ?  77  THR F C   1 
ATOM   4265 O O   . THR D 3 77  ? -0.61200  29.96600 -7.93000  1.000 137.13368 ?  77  THR F O   1 
ATOM   4266 C CB  . THR D 3 77  ? -0.88300  28.38000 -5.28600  1.000 142.56824 ?  77  THR F CB  1 
ATOM   4267 O OG1 . THR D 3 77  ? -1.11500  29.79200 -5.25800  1.000 141.37403 ?  77  THR F OG1 1 
ATOM   4268 C CG2 . THR D 3 77  ? 0.03900   28.01000 -4.15000  1.000 141.33286 ?  77  THR F CG2 1 
ATOM   4269 N N   . MET D 3 78  ? -1.71700  28.10400 -8.55600  1.000 135.55190 ?  78  MET F N   1 
ATOM   4270 C CA  . MET D 3 78  ? -2.36400  28.71000 -9.70300  1.000 135.84878 ?  78  MET F CA  1 
ATOM   4271 C C   . MET D 3 78  ? -3.86000  28.44400 -9.62000  1.000 142.74360 ?  78  MET F C   1 
ATOM   4272 O O   . MET D 3 78  ? -4.30800  27.49900 -8.96400  1.000 145.57587 ?  78  MET F O   1 
ATOM   4273 C CB  . MET D 3 78  ? -1.79400  28.14900 -11.01800 1.000 129.36618 ?  78  MET F CB  1 
ATOM   4274 C CG  . MET D 3 78  ? -0.29000  27.87600 -10.98000 1.000 122.75318 ?  78  MET F CG  1 
ATOM   4275 S SD  . MET D 3 78  ? 0.35800   27.06500 -12.45600 1.000 116.11505 ?  78  MET F SD  1 
ATOM   4276 C CE  . MET D 3 78  ? -0.11100  28.23200 -13.73400 1.000 114.39226 ?  78  MET F CE  1 
ATOM   4277 N N   . GLN D 3 79  ? -4.63800  29.28500 -10.29400 1.000 141.06603 ?  79  GLN F N   1 
ATOM   4278 C CA  . GLN D 3 79  ? -6.09100  29.17000 -10.26700 1.000 145.06858 ?  79  GLN F CA  1 
ATOM   4279 C C   . GLN D 3 79  ? -6.51700  28.21500 -11.37600 1.000 145.89217 ?  79  GLN F C   1 
ATOM   4280 O O   . GLN D 3 79  ? -6.22100  28.44900 -12.55400 1.000 142.93019 ?  79  GLN F O   1 
ATOM   4281 C CB  . GLN D 3 79  ? -6.73800  30.54100 -10.43800 1.000 144.35088 ?  79  GLN F CB  1 
ATOM   4282 C CG  . GLN D 3 79  ? -6.64000  31.40500 -9.20300  1.000 143.36465 ?  79  GLN F CG  1 
ATOM   4283 C CD  . GLN D 3 79  ? -6.32400  32.83900 -9.55100  1.000 139.38967 ?  79  GLN F CD  1 
ATOM   4284 O OE1 . GLN D 3 79  ? -7.10200  33.51000 -10.22700 1.000 139.10360 ?  79  GLN F OE1 1 
ATOM   4285 N NE2 . GLN D 3 79  ? -5.16300  33.31300 -9.11100  1.000 136.12912 ?  79  GLN F NE2 1 
ATOM   4286 N N   . ILE D 3 80  ? -7.21600  27.14500 -10.99300 1.000 144.99048 ?  80  ILE F N   1 
ATOM   4287 C CA  . ILE D 3 80  ? -7.65200  26.09500 -11.90700 1.000 143.38158 ?  80  ILE F CA  1 
ATOM   4288 C C   . ILE D 3 80  ? -9.13100  25.82500 -11.69900 1.000 145.20151 ?  80  ILE F C   1 
ATOM   4289 O O   . ILE D 3 80  ? -9.59300  25.72600 -10.56200 1.000 146.64900 ?  80  ILE F O   1 
ATOM   4290 C CB  . ILE D 3 80  ? -6.85700  24.79300 -11.67900 1.000 138.95661 ?  80  ILE F CB  1 
ATOM   4291 C CG1 . ILE D 3 80  ? -5.39400  25.08500 -11.33600 1.000 136.11724 ?  80  ILE F CG1 1 
ATOM   4292 C CG2 . ILE D 3 80  ? -6.98700  23.87300 -12.87900 1.000 133.92529 ?  80  ILE F CG2 1 
ATOM   4293 C CD1 . ILE D 3 80  ? -4.57700  25.58000 -12.51000 1.000 131.38871 ?  80  ILE F CD1 1 
ATOM   4294 N N   . MET D 3 81  ? -9.86900  25.65400 -12.78800 1.000 143.46439 ?  81  MET F N   1 
ATOM   4295 C CA  . MET D 3 81  ? -11.27100 25.26800 -12.71100 1.000 144.32913 ?  81  MET F CA  1 
ATOM   4296 C C   . MET D 3 81  ? -11.34400 23.76500 -12.48000 1.000 142.08487 ?  81  MET F C   1 
ATOM   4297 O O   . MET D 3 81  ? -11.08400 22.98200 -13.39900 1.000 139.63085 ?  81  MET F O   1 
ATOM   4298 C CB  . MET D 3 81  ? -11.98300 25.65100 -14.00600 1.000 143.82620 ?  81  MET F CB  1 
ATOM   4299 C CG  . MET D 3 81  ? -13.49000 25.77300 -13.92100 1.000 145.40576 ?  81  MET F CG  1 
ATOM   4300 S SD  . MET D 3 81  ? -14.09900 27.12500 -14.94800 1.000 146.83593 ?  81  MET F SD  1 
ATOM   4301 C CE  . MET D 3 81  ? -13.42900 26.65400 -16.54200 1.000 142.54051 ?  81  MET F CE  1 
ATOM   4302 N N   . ARG D 3 82  ? -11.65700 23.35000 -11.25600 1.000 144.02313 ?  82  ARG F N   1 
ATOM   4303 C CA  . ARG D 3 82  ? -11.99000 21.95500 -11.00800 1.000 144.37787 ?  82  ARG F CA  1 
ATOM   4304 C C   . ARG D 3 82  ? -13.43200 21.78700 -11.46300 1.000 145.83533 ?  82  ARG F C   1 
ATOM   4305 O O   . ARG D 3 82  ? -14.35500 22.28700 -10.81000 1.000 148.05595 ?  82  ARG F O   1 
ATOM   4306 C CB  . ARG D 3 82  ? -11.85300 21.59400 -9.52900  1.000 145.76619 ?  82  ARG F CB  1 
ATOM   4307 C CG  . ARG D 3 82  ? -10.87500 22.43800 -8.72400  1.000 145.31722 ?  82  ARG F CG  1 
ATOM   4308 C CD  . ARG D 3 82  ? -10.37700 21.70000 -7.47700  1.000 145.49329 ?  82  ARG F CD  1 
ATOM   4309 N NE  . ARG D 3 82  ? -9.24200  22.39000 -6.87600  1.000 144.36687 ?  82  ARG F NE  1 
ATOM   4310 C CZ  . ARG D 3 82  ? -8.97400  22.42000 -5.57600  1.000 144.97762 ?  82  ARG F CZ  1 
ATOM   4311 N NH1 . ARG D 3 82  ? -9.71100  21.75600 -4.69900  1.000 146.76317 ?  82  ARG F NH1 1 
ATOM   4312 N NH2 . ARG D 3 82  ? -7.93900  23.13500 -5.14500  1.000 143.63372 ?  82  ARG F NH2 1 
ATOM   4313 N N   . ILE D 3 83  ? -13.63000 21.15400 -12.61100 1.000 144.18909 ?  83  ILE F N   1 
ATOM   4314 C CA  . ILE D 3 83  ? -14.95300 20.86500 -13.13900 1.000 145.09750 ?  83  ILE F CA  1 
ATOM   4315 C C   . ILE D 3 83  ? -15.25500 19.40000 -12.88400 1.000 145.13399 ?  83  ILE F C   1 
ATOM   4316 O O   . ILE D 3 83  ? -14.57700 18.52800 -13.43900 1.000 142.86031 ?  83  ILE F O   1 
ATOM   4317 C CB  . ILE D 3 83  ? -15.03100 21.16100 -14.64300 1.000 143.00099 ?  83  ILE F CB  1 
ATOM   4318 C CG1 . ILE D 3 83  ? -14.44100 22.53200 -14.94900 1.000 141.96680 ?  83  ILE F CG1 1 
ATOM   4319 C CG2 . ILE D 3 83  ? -16.47000 21.04200 -15.14800 1.000 143.85991 ?  83  ILE F CG2 1 
ATOM   4320 C CD1 . ILE D 3 83  ? -14.83700 23.05700 -16.28800 1.000 140.04976 ?  83  ILE F CD1 1 
ATOM   4321 N N   . LYS D 3 84  ? -16.26300 19.10200 -12.06800 1.000 147.70330 ?  84  LYS F N   1 
ATOM   4322 C CA  . LYS D 3 84  ? -16.73100 17.73300 -12.02300 1.000 147.34939 ?  84  LYS F CA  1 
ATOM   4323 C C   . LYS D 3 84  ? -17.36100 17.40700 -13.37800 1.000 146.14895 ?  84  LYS F C   1 
ATOM   4324 O O   . LYS D 3 84  ? -17.98600 18.28000 -13.99400 1.000 146.33168 ?  84  LYS F O   1 
ATOM   4325 C CB  . LYS D 3 84  ? -17.71000 17.53800 -10.85900 1.000 150.07340 ?  84  LYS F CB  1 
ATOM   4326 C CG  . LYS D 3 84  ? -18.21000 16.10700 -10.68300 1.000 150.85630 ?  84  LYS F CG  1 
ATOM   4327 C CD  . LYS D 3 84  ? -18.71700 15.83800 -9.29900  1.000 153.50354 ?  84  LYS F CD  1 
ATOM   4328 C CE  . LYS D 3 84  ? -17.80300 16.51700 -8.30600  1.000 153.17540 ?  84  LYS F CE  1 
ATOM   4329 N NZ  . LYS D 3 84  ? -18.28700 16.40600 -6.91600  1.000 156.79984 ?  84  LYS F NZ  1 
ATOM   4330 N N   . PRO D 3 85  ? -17.20400 16.17300 -13.87200 1.000 155.10371 ?  85  PRO F N   1 
ATOM   4331 C CA  . PRO D 3 85  ? -17.54200 15.90000 -15.28000 1.000 151.28661 ?  85  PRO F CA  1 
ATOM   4332 C C   . PRO D 3 85  ? -18.88100 16.40800 -15.78600 1.000 153.10312 ?  85  PRO F C   1 
ATOM   4333 O O   . PRO D 3 85  ? -18.92900 16.99300 -16.87200 1.000 151.04525 ?  85  PRO F O   1 
ATOM   4334 C CB  . PRO D 3 85  ? -17.47500 14.37300 -15.33200 1.000 146.02072 ?  85  PRO F CB  1 
ATOM   4335 C CG  . PRO D 3 85  ? -16.45600 14.00600 -14.32700 1.000 140.31506 ?  85  PRO F CG  1 
ATOM   4336 C CD  . PRO D 3 85  ? -16.49100 15.04300 -13.24800 1.000 145.09370 ?  85  PRO F CD  1 
ATOM   4337 N N   . HIS D 3 86  ? -19.96900 16.23400 -15.02400 1.000 152.57090 ?  86  HIS F N   1 
ATOM   4338 C CA  . HIS D 3 86  ? -21.25900 16.75300 -15.46400 1.000 152.97292 ?  86  HIS F CA  1 
ATOM   4339 C C   . HIS D 3 86  ? -22.06700 17.38000 -14.33500 1.000 156.00682 ?  86  HIS F C   1 
ATOM   4340 O O   . HIS D 3 86  ? -23.24400 17.69900 -14.54200 1.000 156.14270 ?  86  HIS F O   1 
ATOM   4341 C CB  . HIS D 3 86  ? -22.08800 15.64000 -16.13300 1.000 151.04609 ?  86  HIS F CB  1 
ATOM   4342 C CG  . HIS D 3 86  ? -21.75000 15.41200 -17.57600 1.000 146.37475 ?  86  HIS F CG  1 
ATOM   4343 N ND1 . HIS D 3 86  ? -21.21200 14.22900 -18.03400 1.000 142.65786 ?  86  HIS F ND1 1 
ATOM   4344 C CD2 . HIS D 3 86  ? -21.86000 16.21500 -18.66100 1.000 143.37085 ?  86  HIS F CD2 1 
ATOM   4345 C CE1 . HIS D 3 86  ? -21.01200 14.31100 -19.33800 1.000 137.07905 ?  86  HIS F CE1 1 
ATOM   4346 N NE2 . HIS D 3 86  ? -21.39700 15.50700 -19.74300 1.000 137.46602 ?  86  HIS F NE2 1 
ATOM   4347 N N   . GLN D 3 87  ? -21.49600 17.54000 -13.14400 1.000 152.23484 ?  87  GLN F N   1 
ATOM   4348 C CA  . GLN D 3 87  ? -22.27800 17.91800 -11.97700 1.000 152.67611 ?  87  GLN F CA  1 
ATOM   4349 C C   . GLN D 3 87  ? -22.09400 19.36000 -11.52800 1.000 152.00785 ?  87  GLN F C   1 
ATOM   4350 O O   . GLN D 3 87  ? -23.04100 19.94700 -11.00600 1.000 151.73157 ?  87  GLN F O   1 
ATOM   4351 C CB  . GLN D 3 87  ? -21.96200 16.99900 -10.79100 1.000 149.05006 ?  87  GLN F CB  1 
ATOM   4352 C CG  . GLN D 3 87  ? -22.68900 15.66600 -10.82300 1.000 148.73621 ?  87  GLN F CG  1 
ATOM   4353 C CD  . GLN D 3 87  ? -21.83000 14.51200 -10.33500 1.000 141.38611 ?  87  GLN F CD  1 
ATOM   4354 O OE1 . GLN D 3 87  ? -21.60800 14.35500 -9.13300  1.000 132.30899 ?  87  GLN F OE1 1 
ATOM   4355 N NE2 . GLN D 3 87  ? -21.36400 13.68400 -11.26300 1.000 143.24363 ?  87  GLN F NE2 1 
ATOM   4356 N N   . GLY D 3 88  ? -20.91700 19.94900 -11.70000 1.000 153.28193 ?  88  GLY F N   1 
ATOM   4357 C CA  . GLY D 3 88  ? -20.71100 21.30000 -11.21400 1.000 152.51649 ?  88  GLY F CA  1 
ATOM   4358 C C   . GLY D 3 88  ? -19.24000 21.65300 -11.19200 1.000 151.54901 ?  88  GLY F C   1 
ATOM   4359 O O   . GLY D 3 88  ? -18.39900 20.75700 -11.14200 1.000 150.45594 ?  88  GLY F O   1 
ATOM   4360 N N   . GLN D 3 89  ? -18.89900 22.93500 -11.26100 1.000 147.44196 ?  89  GLN F N   1 
ATOM   4361 C CA  . GLN D 3 89  ? -17.50100 23.33200 -11.31200 1.000 146.59663 ?  89  GLN F CA  1 
ATOM   4362 C C   . GLN D 3 89  ? -17.22500 24.42200 -10.28600 1.000 145.09538 ?  89  GLN F C   1 
ATOM   4363 O O   . GLN D 3 89  ? -18.13600 25.02600 -9.71400  1.000 144.88922 ?  89  GLN F O   1 
ATOM   4364 C CB  . GLN D 3 89  ? -17.10900 23.81900 -12.71400 1.000 147.05460 ?  89  GLN F CB  1 
ATOM   4365 C CG  . GLN D 3 89  ? -17.29800 25.30800 -12.94600 1.000 146.58225 ?  89  GLN F CG  1 
ATOM   4366 C CD  . GLN D 3 89  ? -17.22900 25.66200 -14.41900 1.000 145.13228 ?  89  GLN F CD  1 
ATOM   4367 O OE1 . GLN D 3 89  ? -17.30100 24.78300 -15.28000 1.000 144.33743 ?  89  GLN F OE1 1 
ATOM   4368 N NE2 . GLN D 3 89  ? -17.06200 26.94600 -14.71600 1.000 143.98399 ?  89  GLN F NE2 1 
ATOM   4369 N N   . HIS D 3 90  ? -15.93600 24.64800 -10.04800 1.000 143.20269 ?  90  HIS F N   1 
ATOM   4370 C CA  . HIS D 3 90  ? -15.48200 25.59400 -9.04100  1.000 141.32926 ?  90  HIS F CA  1 
ATOM   4371 C C   . HIS D 3 90  ? -14.02300 25.90000 -9.32400  1.000 140.92074 ?  90  HIS F C   1 
ATOM   4372 O O   . HIS D 3 90  ? -13.25900 24.99200 -9.63400  1.000 139.60997 ?  90  HIS F O   1 
ATOM   4373 C CB  . HIS D 3 90  ? -15.64600 25.02800 -7.62600  1.000 137.54857 ?  90  HIS F CB  1 
ATOM   4374 N N   . ILE D 3 91  ? -13.62800 27.15900 -9.19600  1.000 147.16674 ?  91  ILE F N   1 
ATOM   4375 C CA  . ILE D 3 91  ? -12.24800 27.53500 -9.47900  1.000 147.09391 ?  91  ILE F CA  1 
ATOM   4376 C C   . ILE D 3 91  ? -11.44500 27.49300 -8.17900  1.000 143.48892 ?  91  ILE F C   1 
ATOM   4377 O O   . ILE D 3 91  ? -11.59000 28.35500 -7.30700  1.000 142.88149 ?  91  ILE F O   1 
ATOM   4378 C CB  . ILE D 3 91  ? -12.17800 28.90900 -10.15900 1.000 148.90911 ?  91  ILE F CB  1 
ATOM   4379 C CG1 . ILE D 3 91  ? -13.09500 29.90700 -9.44900  1.000 148.84089 ?  91  ILE F CG1 1 
ATOM   4380 C CG2 . ILE D 3 91  ? -12.55800 28.79000 -11.63400 1.000 149.82750 ?  91  ILE F CG2 1 
ATOM   4381 C CD1 . ILE D 3 91  ? -13.16200 31.26500 -10.11700 1.000 149.46226 ?  91  ILE F CD1 1 
ATOM   4382 N N   . GLY D 3 92  ? -10.58200 26.48300 -8.06100  1.000 147.69252 ?  92  GLY F N   1 
ATOM   4383 C CA  . GLY D 3 92  ? -9.78000  26.22200 -6.88200  1.000 141.84669 ?  92  GLY F CA  1 
ATOM   4384 C C   . GLY D 3 92  ? -8.30100  26.46300 -7.10100  1.000 141.29243 ?  92  GLY F C   1 
ATOM   4385 O O   . GLY D 3 92  ? -7.81600  26.41000 -8.23800  1.000 144.04186 ?  92  GLY F O   1 
ATOM   4386 N N   . GLU D 3 93  ? -7.57500  26.72800 -6.01200  1.000 145.46259 ?  93  GLU F N   1 
ATOM   4387 C CA  . GLU D 3 93  ? -6.16100  27.11000 -6.06400  1.000 145.66799 ?  93  GLU F CA  1 
ATOM   4388 C C   . GLU D 3 93  ? -5.28200  25.87700 -5.86500  1.000 138.21084 ?  93  GLU F C   1 
ATOM   4389 O O   . GLU D 3 93  ? -4.71900  25.64300 -4.79600  1.000 133.55307 ?  93  GLU F O   1 
ATOM   4390 C CB  . GLU D 3 93  ? -5.86400  28.18200 -5.02100  1.000 146.96142 ?  93  GLU F CB  1 
ATOM   4391 N N   . MET D 3 94  ? -5.17100  25.07300 -6.91700  1.000 142.02638 ?  94  MET F N   1 
ATOM   4392 C CA  . MET D 3 94  ? -4.27600  23.92700 -6.86700  1.000 133.34774 ?  94  MET F CA  1 
ATOM   4393 C C   . MET D 3 94  ? -2.82900  24.38800 -6.99100  1.000 134.42224 ?  94  MET F C   1 
ATOM   4394 O O   . MET D 3 94  ? -2.50100  25.23700 -7.82300  1.000 141.39446 ?  94  MET F O   1 
ATOM   4395 C CB  . MET D 3 94  ? -4.59600  22.93000 -7.97600  1.000 129.97740 ?  94  MET F CB  1 
ATOM   4396 C CG  . MET D 3 94  ? -5.72300  21.95900 -7.67700  1.000 125.50118 ?  94  MET F CG  1 
ATOM   4397 S SD  . MET D 3 94  ? -6.64900  21.65900 -9.18400  1.000 130.49035 ?  94  MET F SD  1 
ATOM   4398 C CE  . MET D 3 94  ? -5.27900  21.45600 -10.31300 1.000 126.92130 ?  94  MET F CE  1 
ATOM   4399 N N   . SER D 3 95  ? -1.96300  23.81800 -6.16100  1.000 139.79656 ?  95  SER F N   1 
ATOM   4400 C CA  . SER D 3 95  ? -0.54400  24.13800 -6.18700  1.000 142.39127 ?  95  SER F CA  1 
ATOM   4401 C C   . SER D 3 95  ? 0.20700   23.13500 -7.05700  1.000 135.77685 ?  95  SER F C   1 
ATOM   4402 O O   . SER D 3 95  ? -0.26100  22.02400 -7.31400  1.000 127.55377 ?  95  SER F O   1 
ATOM   4403 C CB  . SER D 3 95  ? 0.04400   24.14500 -4.77600  1.000 142.02769 ?  95  SER F CB  1 
ATOM   4404 O OG  . SER D 3 95  ? 0.43000   22.84200 -4.38000  1.000 133.72165 ?  95  SER F OG  1 
ATOM   4405 N N   . PHE D 3 96  ? 1.38200   23.55000 -7.51900  1.000 138.42425 ?  96  PHE F N   1 
ATOM   4406 C CA  . PHE D 3 96  ? 2.23900   22.70100 -8.32800  1.000 132.05309 ?  96  PHE F CA  1 
ATOM   4407 C C   . PHE D 3 96  ? 3.69000   22.97000 -7.96200  1.000 135.98098 ?  96  PHE F C   1 
ATOM   4408 O O   . PHE D 3 96  ? 4.03500   24.01900 -7.41300  1.000 145.56237 ?  96  PHE F O   1 
ATOM   4409 C CB  . PHE D 3 96  ? 2.02700   22.93600 -9.83300  1.000 132.06464 ?  96  PHE F CB  1 
ATOM   4410 C CG  . PHE D 3 96  ? 0.58500   22.93700 -10.25400 1.000 132.07960 ?  96  PHE F CG  1 
ATOM   4411 C CD1 . PHE D 3 96  ? -0.15900  24.10700 -10.23000 1.000 141.93560 ?  96  PHE F CD1 1 
ATOM   4412 C CD2 . PHE D 3 96  ? -0.02700  21.76600 -10.66900 1.000 123.90849 ?  96  PHE F CD2 1 
ATOM   4413 C CE1 . PHE D 3 96  ? -1.48500  24.11000 -10.61600 1.000 143.59531 ?  96  PHE F CE1 1 
ATOM   4414 C CE2 . PHE D 3 96  ? -1.35200  21.76000 -11.05300 1.000 125.87175 ?  96  PHE F CE2 1 
ATOM   4415 C CZ  . PHE D 3 96  ? -2.08300  22.93500 -11.02800 1.000 135.73401 ?  96  PHE F CZ  1 
ATOM   4416 N N   . LEU D 3 97  ? 4.54100   22.00300 -8.27700  1.000 138.25180 ?  97  LEU F N   1 
ATOM   4417 C CA  . LEU D 3 97  ? 5.96300   22.11400 -8.01100  1.000 142.61460 ?  97  LEU F CA  1 
ATOM   4418 C C   . LEU D 3 97  ? 6.66800   22.68200 -9.23600  1.000 145.23317 ?  97  LEU F C   1 
ATOM   4419 O O   . LEU D 3 97  ? 6.27800   22.40300 -10.37300 1.000 138.88889 ?  97  LEU F O   1 
ATOM   4420 C CB  . LEU D 3 97  ? 6.53300   20.74700 -7.63700  1.000 135.44894 ?  97  LEU F CB  1 
ATOM   4421 C CG  . LEU D 3 97  ? 8.02300   20.63300 -7.32800  1.000 140.30106 ?  97  LEU F CG  1 
ATOM   4422 C CD1 . LEU D 3 97  ? 8.21000   19.89000 -6.02400  1.000 139.90107 ?  97  LEU F CD1 1 
ATOM   4423 C CD2 . LEU D 3 97  ? 8.75400   19.92500 -8.45200  1.000 135.02892 ?  97  LEU F CD2 1 
ATOM   4424 N N   . GLN D 3 98  ? 7.68200   23.51000 -8.99300  1.000 132.97602 ?  98  GLN F N   1 
ATOM   4425 C CA  . GLN D 3 98  ? 8.53000   24.05700 -10.03400 1.000 135.26244 ?  98  GLN F CA  1 
ATOM   4426 C C   . GLN D 3 98  ? 9.98500   23.93400 -9.60900  1.000 139.39592 ?  98  GLN F C   1 
ATOM   4427 O O   . GLN D 3 98  ? 10.31900  23.88300 -8.41500  1.000 144.88510 ?  98  GLN F O   1 
ATOM   4428 C CB  . GLN D 3 98  ? 8.25600   25.53600 -10.32200 1.000 144.93197 ?  98  GLN F CB  1 
ATOM   4429 C CG  . GLN D 3 98  ? 8.66500   26.45700 -9.18400  1.000 157.26758 ?  98  GLN F CG  1 
ATOM   4430 C CD  . GLN D 3 98  ? 7.91700   27.76900 -9.20200  1.000 166.47041 ?  98  GLN F CD  1 
ATOM   4431 O OE1 . GLN D 3 98  ? 7.20500   28.11300 -8.25800  1.000 170.37442 ?  98  GLN F OE1 1 
ATOM   4432 N NE2 . GLN D 3 98  ? 8.08200   28.51900 -10.28600 1.000 168.39883 ?  98  GLN F NE2 1 
ATOM   4433 N N   . HIS D 3 99  ? 10.84500  23.95900 -10.62000 1.000 148.74919 ?  99  HIS F N   1 
ATOM   4434 C CA  . HIS D 3 99  ? 12.28800  23.84300 -10.46500 1.000 152.33144 ?  99  HIS F CA  1 
ATOM   4435 C C   . HIS D 3 99  ? 12.86300  25.25000 -10.57200 1.000 161.68003 ?  99  HIS F C   1 
ATOM   4436 O O   . HIS D 3 99  ? 12.91100  25.82800 -11.66100 1.000 159.28214 ?  99  HIS F O   1 
ATOM   4437 C CB  . HIS D 3 99  ? 12.86300  22.92000 -11.53500 1.000 143.03731 ?  99  HIS F CB  1 
ATOM   4438 C CG  . HIS D 3 99  ? 12.50800  21.47900 -11.33700 1.000 134.99835 ?  99  HIS F CG  1 
ATOM   4439 N ND1 . HIS D 3 99  ? 12.84700  20.49700 -12.24100 1.000 127.56843 ?  99  HIS F ND1 1 
ATOM   4440 C CD2 . HIS D 3 99  ? 11.80500  20.86200 -10.35700 1.000 133.79438 ?  99  HIS F CD2 1 
ATOM   4441 C CE1 . HIS D 3 99  ? 12.38700  19.33300 -11.81800 1.000 123.91973 ?  99  HIS F CE1 1 
ATOM   4442 N NE2 . HIS D 3 99  ? 11.75400  19.52600 -10.67600 1.000 126.30010 ?  99  HIS F NE2 1 
ATOM   4443 N N   . ASN D 3 100 ? 13.26000  25.82200 -9.43500  1.000 157.52361 ?  100 ASN F N   1 
ATOM   4444 C CA  . ASN D 3 100 ? 13.95400  27.10200 -9.48300  1.000 149.12079 ?  100 ASN F CA  1 
ATOM   4445 C C   . ASN D 3 100 ? 15.28400  26.96400 -10.21300 1.000 141.83443 ?  100 ASN F C   1 
ATOM   4446 O O   . ASN D 3 100 ? 15.61200  27.76500 -11.09600 1.000 136.37451 ?  100 ASN F O   1 
ATOM   4447 C CB  . ASN D 3 100 ? 14.16700  27.64900 -8.07000  1.000 145.61442 ?  100 ASN F CB  1 
ATOM   4448 C CG  . ASN D 3 100 ? 12.89500  27.66100 -7.24700  1.000 154.05893 ?  100 ASN F CG  1 
ATOM   4449 O OD1 . ASN D 3 100 ? 12.15300  26.68100 -7.20800  1.000 162.27930 ?  100 ASN F OD1 1 
ATOM   4450 N ND2 . ASN D 3 100 ? 12.64200  28.77700 -6.57300  1.000 151.72983 ?  100 ASN F ND2 1 
ATOM   4451 N N   . LYS D 3 101 ? 16.05200  25.93200 -9.87600  1.000 146.77145 ?  101 LYS F N   1 
ATOM   4452 C CA  . LYS D 3 101 ? 17.39000  25.74700 -10.41500 1.000 141.61681 ?  101 LYS F CA  1 
ATOM   4453 C C   . LYS D 3 101 ? 17.65300  24.27000 -10.67400 1.000 146.42459 ?  101 LYS F C   1 
ATOM   4454 O O   . LYS D 3 101 ? 17.21800  23.40900 -9.90400  1.000 149.72983 ?  101 LYS F O   1 
ATOM   4455 C CB  . LYS D 3 101 ? 18.44500  26.31100 -9.45700  1.000 133.67293 ?  101 LYS F CB  1 
ATOM   4456 N N   . CYS D 3 102 ? 18.34700  23.98100 -11.77200 1.000 146.33067 ?  102 CYS F N   1 
ATOM   4457 C CA  . CYS D 3 102 ? 18.82600  22.64000 -12.09600 1.000 148.78035 ?  102 CYS F CA  1 
ATOM   4458 C C   . CYS D 3 102 ? 20.35400  22.63700 -12.08700 1.000 146.04999 ?  102 CYS F C   1 
ATOM   4459 O O   . CYS D 3 102 ? 20.99300  23.66500 -11.85400 1.000 139.86928 ?  102 CYS F O   1 
ATOM   4460 C CB  . CYS D 3 102 ? 18.27600  22.17300 -13.44500 1.000 145.94137 ?  102 CYS F CB  1 
ATOM   4461 S SG  . CYS D 3 102 ? 16.49300  22.35300 -13.63100 1.000 148.40639 ?  102 CYS F SG  1 
ATOM   4462 N N   . GLU D 3 103 ? 20.93800  21.46800 -12.35500 1.000 153.16782 ?  103 GLU F N   1 
ATOM   4463 C CA  . GLU D 3 103 ? 22.38800  21.29300 -12.30600 1.000 151.13582 ?  103 GLU F CA  1 
ATOM   4464 C C   . GLU D 3 103 ? 22.74000  19.95700 -12.95400 1.000 148.24805 ?  103 GLU F C   1 
ATOM   4465 O O   . GLU D 3 103 ? 21.86800  19.13000 -13.23000 1.000 149.21103 ?  103 GLU F O   1 
ATOM   4466 C CB  . GLU D 3 103 ? 22.90900  21.35700 -10.87000 1.000 150.80731 ?  103 GLU F CB  1 
ATOM   4467 C CG  . GLU D 3 103 ? 24.26900  22.01200 -10.71400 1.000 146.16604 ?  103 GLU F CG  1 
ATOM   4468 C CD  . GLU D 3 103 ? 24.68300  22.13700 -9.25800  1.000 140.82969 ?  103 GLU F CD  1 
ATOM   4469 O OE1 . GLU D 3 103 ? 23.78800  22.27400 -8.39300  1.000 138.97676 ?  103 GLU F OE1 1 
ATOM   4470 O OE2 . GLU D 3 103 ? 25.90300  22.09800 -8.97900  1.000 138.24520 ?  103 GLU F OE2 1 
ATOM   4471 N N   . CYS D 3 104 ? 24.03500  19.76200 -13.20500 1.000 146.61566 ?  104 CYS F N   1 
ATOM   4472 C CA  . CYS D 3 104 ? 24.56700  18.55000 -13.82700 1.000 143.33475 ?  104 CYS F CA  1 
ATOM   4473 C C   . CYS D 3 104 ? 25.34700  17.79300 -12.75800 1.000 145.99650 ?  104 CYS F C   1 
ATOM   4474 O O   . CYS D 3 104 ? 26.42100  18.23900 -12.33900 1.000 144.16457 ?  104 CYS F O   1 
ATOM   4475 C CB  . CYS D 3 104 ? 25.47500  18.88900 -15.00500 1.000 136.24106 ?  104 CYS F CB  1 
ATOM   4476 S SG  . CYS D 3 104 ? 24.65100  19.16900 -16.59100 1.000 131.88798 ?  104 CYS F SG  1 
ATOM   4477 N N   . ARG D 3 105 ? 24.81500  16.65700 -12.31200 1.000 152.87547 ?  105 ARG F N   1 
ATOM   4478 C CA  . ARG D 3 105 ? 25.48300  15.92600 -11.24500 1.000 154.67399 ?  105 ARG F CA  1 
ATOM   4479 C C   . ARG D 3 105 ? 25.64600  14.45900 -11.61100 1.000 153.90431 ?  105 ARG F C   1 
ATOM   4480 O O   . ARG D 3 105 ? 24.86300  13.92600 -12.39200 1.000 154.10101 ?  105 ARG F O   1 
ATOM   4481 C CB  . ARG D 3 105 ? 24.70800  16.05500 -9.92600  1.000 158.75964 ?  105 ARG F CB  1 
ATOM   4482 C CG  . ARG D 3 105 ? 24.76000  17.45400 -9.35000  1.000 157.61632 ?  105 ARG F CG  1 
ATOM   4483 C CD  . ARG D 3 105 ? 24.14600  17.51500 -7.97300  1.000 155.88473 ?  105 ARG F CD  1 
ATOM   4484 N NE  . ARG D 3 105 ? 24.20400  18.87200 -7.44500  1.000 151.26353 ?  105 ARG F NE  1 
ATOM   4485 C CZ  . ARG D 3 105 ? 23.69500  19.24500 -6.27900  1.000 146.98303 ?  105 ARG F CZ  1 
ATOM   4486 N NH1 . ARG D 3 105 ? 23.12000  18.37400 -5.46700  1.000 147.56373 ?  105 ARG F NH1 1 
ATOM   4487 N NH2 . ARG D 3 105 ? 23.77700  20.52000 -5.91400  1.000 141.54127 ?  105 ARG F NH2 1 
ATOM   4488 N N   . PRO D 3 106 ? 26.63200  13.77500 -11.02900 1.000 150.57376 ?  106 PRO F N   1 
ATOM   4489 C CA  . PRO D 3 106 ? 26.96700  12.42600 -11.49600 1.000 149.15790 ?  106 PRO F CA  1 
ATOM   4490 C C   . PRO D 3 106 ? 25.81500  11.43500 -11.37300 1.000 153.48776 ?  106 PRO F C   1 
ATOM   4491 O O   . PRO D 3 106 ? 24.90100  11.58800 -10.55900 1.000 157.46848 ?  106 PRO F O   1 
ATOM   4492 C CB  . PRO D 3 106 ? 28.14600  12.02300 -10.60000 1.000 146.97965 ?  106 PRO F CB  1 
ATOM   4493 C CG  . PRO D 3 106 ? 28.73700  13.31700 -10.16200 1.000 145.03628 ?  106 PRO F CG  1 
ATOM   4494 C CD  . PRO D 3 106 ? 27.56800  14.23200 -9.98500  1.000 149.10961 ?  106 PRO F CD  1 
ATOM   4495 N N   . LYS D 3 107 ? 25.87400  10.40300 -12.21800 1.000 153.68802 ?  107 LYS F N   1 
ATOM   4496 C CA  . LYS D 3 107 ? 24.84800  9.36300  -12.29000 1.000 157.09356 ?  107 LYS F CA  1 
ATOM   4497 C C   . LYS D 3 107 ? 25.10500  8.35400  -11.17900 1.000 159.22951 ?  107 LYS F C   1 
ATOM   4498 O O   . LYS D 3 107 ? 25.88700  7.41300  -11.32700 1.000 157.16998 ?  107 LYS F O   1 
ATOM   4499 C CB  . LYS D 3 107 ? 24.84900  8.69800  -13.66300 1.000 153.59764 ?  107 LYS F CB  1 
ATOM   4500 N N   . LYS D 3 108 ? 24.43200  8.56000  -10.04600 1.000 162.65877 ?  108 LYS F N   1 
ATOM   4501 C CA  . LYS D 3 108 ? 24.55000  7.67400  -8.89600  1.000 162.92630 ?  108 LYS F CA  1 
ATOM   4502 C C   . LYS D 3 108 ? 24.10800  6.26000  -9.25100  1.000 164.69686 ?  108 LYS F C   1 
ATOM   4503 O O   . LYS D 3 108 ? 22.92400  6.01200  -9.51000  1.000 167.72750 ?  108 LYS F O   1 
ATOM   4504 C CB  . LYS D 3 108 ? 23.72600  8.20600  -7.72200  1.000 164.14299 ?  108 LYS F CB  1 
ATOM   4505 N N   . ASP D 3 109 ? 25.05700  5.33200  -9.25200  1.000 164.23854 ?  109 ASP F N   1 
ATOM   4506 C CA  . ASP D 3 109 ? 24.78500  3.93400  -9.56700  1.000 165.37801 ?  109 ASP F CA  1 
ATOM   4507 C C   . ASP D 3 109 ? 25.91900  3.02200  -9.08000  1.000 162.38884 ?  109 ASP F C   1 
ATOM   4508 O O   . ASP D 3 109 ? 27.10100  3.37600  -9.16700  1.000 158.55185 ?  109 ASP F O   1 
ATOM   4509 C CB  . ASP D 3 109 ? 24.57700  3.75800  -11.07400 1.000 164.75195 ?  109 ASP F CB  1 
ATOM   4510 N N   . GLU E 1 1   ? -10.24000 44.43400 -13.53900 1.000 138.92988 ?  1   GLU A N   1 
ATOM   4511 C CA  . GLU E 1 1   ? -9.17100  45.42100 -13.42000 1.000 146.57053 ?  1   GLU A CA  1 
ATOM   4512 C C   . GLU E 1 1   ? -8.54500  45.70800 -14.78200 1.000 144.43147 ?  1   GLU A C   1 
ATOM   4513 O O   . GLU E 1 1   ? -7.79300  46.67300 -14.93500 1.000 147.75715 ?  1   GLU A O   1 
ATOM   4514 C CB  . GLU E 1 1   ? -8.09600  44.94500 -12.43300 1.000 152.10628 ?  1   GLU A CB  1 
ATOM   4515 N N   . VAL E 1 2   ? -8.85700  44.85700 -15.76100 1.000 149.57840 ?  2   VAL A N   1 
ATOM   4516 C CA  . VAL E 1 2   ? -8.27300  44.97300 -17.09400 1.000 143.35079 ?  2   VAL A CA  1 
ATOM   4517 C C   . VAL E 1 2   ? -8.81600  46.21100 -17.79500 1.000 147.75014 ?  2   VAL A C   1 
ATOM   4518 O O   . VAL E 1 2   ? -10.03500 46.39800 -17.90200 1.000 145.07802 ?  2   VAL A O   1 
ATOM   4519 C CB  . VAL E 1 2   ? -8.56200  43.70600 -17.91400 1.000 131.26511 ?  2   VAL A CB  1 
ATOM   4520 C CG1 . VAL E 1 2   ? -8.34900  43.96600 -19.40400 1.000 125.31697 ?  2   VAL A CG1 1 
ATOM   4521 C CG2 . VAL E 1 2   ? -7.69000  42.55600 -17.43800 1.000 125.08655 ?  2   VAL A CG2 1 
ATOM   4522 N N   . GLN E 1 3   ? -7.91200  47.07600 -18.26000 1.000 144.28573 ?  3   GLN A N   1 
ATOM   4523 C CA  . GLN E 1 3   ? -8.30500  48.22800 -19.06100 1.000 144.75962 ?  3   GLN A CA  1 
ATOM   4524 C C   . GLN E 1 3   ? -7.34000  48.44000 -20.21500 1.000 138.18921 ?  3   GLN A C   1 
ATOM   4525 O O   . GLN E 1 3   ? -6.13000  48.25600 -20.06900 1.000 136.55330 ?  3   GLN A O   1 
ATOM   4526 C CB  . GLN E 1 3   ? -8.38300  49.53200 -18.25400 1.000 151.69437 ?  3   GLN A CB  1 
ATOM   4527 C CG  . GLN E 1 3   ? -8.96000  49.43400 -16.86400 1.000 156.75936 ?  3   GLN A CG  1 
ATOM   4528 C CD  . GLN E 1 3   ? -9.08700  50.80500 -16.23700 1.000 159.22617 ?  3   GLN A CD  1 
ATOM   4529 O OE1 . GLN E 1 3   ? -9.06500  51.81700 -16.94100 1.000 156.39157 ?  3   GLN A OE1 1 
ATOM   4530 N NE2 . GLN E 1 3   ? -9.22400  50.85100 -14.91600 1.000 163.46152 ?  3   GLN A NE2 1 
ATOM   4531 N N   . LEU E 1 4   ? -7.88600  48.86000 -21.35100 1.000 145.52165 ?  4   LEU A N   1 
ATOM   4532 C CA  . LEU E 1 4   ? -7.10300  49.34200 -22.47900 1.000 141.89764 ?  4   LEU A CA  1 
ATOM   4533 C C   . LEU E 1 4   ? -7.40100  50.82100 -22.67000 1.000 146.12122 ?  4   LEU A C   1 
ATOM   4534 O O   . LEU E 1 4   ? -8.56600  51.22900 -22.67900 1.000 145.04708 ?  4   LEU A O   1 
ATOM   4535 C CB  . LEU E 1 4   ? -7.42400  48.55300 -23.75200 1.000 132.92277 ?  4   LEU A CB  1 
ATOM   4536 C CG  . LEU E 1 4   ? -6.81900  47.14700 -23.81500 1.000 125.04973 ?  4   LEU A CG  1 
ATOM   4537 C CD1 . LEU E 1 4   ? -7.11000  46.49200 -25.15100 1.000 120.56003 ?  4   LEU A CD1 1 
ATOM   4538 C CD2 . LEU E 1 4   ? -5.31600  47.22900 -23.60400 1.000 123.16539 ?  4   LEU A CD2 1 
ATOM   4539 N N   . VAL E 1 5   ? -6.34800  51.61500 -22.82800 1.000 133.09618 ?  5   VAL A N   1 
ATOM   4540 C CA  . VAL E 1 5   ? -6.46000  53.06200 -22.94000 1.000 136.20156 ?  5   VAL A CA  1 
ATOM   4541 C C   . VAL E 1 5   ? -5.75300  53.49900 -24.21300 1.000 134.37537 ?  5   VAL A C   1 
ATOM   4542 O O   . VAL E 1 5   ? -4.59100  53.14600 -24.44000 1.000 132.04544 ?  5   VAL A O   1 
ATOM   4543 C CB  . VAL E 1 5   ? -5.87100  53.76300 -21.70200 1.000 142.06972 ?  5   VAL A CB  1 
ATOM   4544 C CG1 . VAL E 1 5   ? -6.69000  53.41400 -20.47700 1.000 144.60711 ?  5   VAL A CG1 1 
ATOM   4545 C CG2 . VAL E 1 5   ? -4.44100  53.32700 -21.47100 1.000 141.30803 ?  5   VAL A CG2 1 
ATOM   4546 N N   . GLU E 1 6   ? -6.45100  54.26000 -25.04700 1.000 144.25882 ?  6   GLU A N   1 
ATOM   4547 C CA  . GLU E 1 6   ? -5.90000  54.68300 -26.32000 1.000 143.92997 ?  6   GLU A CA  1 
ATOM   4548 C C   . GLU E 1 6   ? -5.71300  56.18700 -26.38000 1.000 147.78386 ?  6   GLU A C   1 
ATOM   4549 O O   . GLU E 1 6   ? -6.42200  56.95400 -25.71900 1.000 148.39452 ?  6   GLU A O   1 
ATOM   4550 C CB  . GLU E 1 6   ? -6.77100  54.30400 -27.51000 1.000 139.46115 ?  6   GLU A CB  1 
ATOM   4551 C CG  . GLU E 1 6   ? -7.69800  53.14700 -27.35300 1.000 133.07672 ?  6   GLU A CG  1 
ATOM   4552 C CD  . GLU E 1 6   ? -8.63400  53.07200 -28.53900 1.000 126.60821 ?  6   GLU A CD  1 
ATOM   4553 O OE1 . GLU E 1 6   ? -8.17400  52.66500 -29.63000 1.000 125.94993 ?  6   GLU A OE1 1 
ATOM   4554 O OE2 . GLU E 1 6   ? -9.81800  53.44800 -28.38700 1.000 121.83418 -1 6   GLU A OE2 1 
ATOM   4555 N N   . SER E 1 7   ? -4.76600  56.58600 -27.21900 1.000 134.09722 ?  7   SER A N   1 
ATOM   4556 C CA  . SER E 1 7   ? -4.58200  57.99200 -27.55700 1.000 137.19273 ?  7   SER A CA  1 
ATOM   4557 C C   . SER E 1 7   ? -3.79700  58.07800 -28.86200 1.000 136.92618 ?  7   SER A C   1 
ATOM   4558 O O   . SER E 1 7   ? -3.40100  57.06100 -29.44400 1.000 133.17960 ?  7   SER A O   1 
ATOM   4559 C CB  . SER E 1 7   ? -3.90800  58.76200 -26.41800 1.000 136.34529 ?  7   SER A CB  1 
ATOM   4560 O OG  . SER E 1 7   ? -2.54400  58.41000 -26.29100 1.000 132.67426 ?  7   SER A OG  1 
ATOM   4561 N N   . GLY E 1 8   ? -3.54700  59.31700 -29.29500 1.000 130.91321 ?  8   GLY A N   1 
ATOM   4562 C CA  . GLY E 1 8   ? -2.90000  59.60500 -30.55600 1.000 130.37870 ?  8   GLY A CA  1 
ATOM   4563 C C   . GLY E 1 8   ? -3.79700  60.11100 -31.66800 1.000 134.90455 ?  8   GLY A C   1 
ATOM   4564 O O   . GLY E 1 8   ? -3.28300  60.47600 -32.72600 1.000 135.43878 ?  8   GLY A O   1 
ATOM   4565 N N   . GLY E 1 9   ? -5.10500  60.17900 -31.46300 1.000 139.80554 ?  9   GLY A N   1 
ATOM   4566 C CA  . GLY E 1 9   ? -5.98400  60.61100 -32.53000 1.000 141.21307 ?  9   GLY A CA  1 
ATOM   4567 C C   . GLY E 1 9   ? -5.77800  62.06000 -32.92000 1.000 144.58072 ?  9   GLY A C   1 
ATOM   4568 O O   . GLY E 1 9   ? -5.32000  62.89800 -32.14200 1.000 140.84360 ?  9   GLY A O   1 
ATOM   4569 N N   . GLY E 1 10  ? -6.14700  62.35100 -34.16300 1.000 145.91850 ?  11  GLY A N   1 
ATOM   4570 C CA  . GLY E 1 10  ? -6.00600  63.69000 -34.69800 1.000 148.13329 ?  11  GLY A CA  1 
ATOM   4571 C C   . GLY E 1 10  ? -6.20800  63.68400 -36.20000 1.000 153.45636 ?  11  GLY A C   1 
ATOM   4572 O O   . GLY E 1 10  ? -6.84800  62.78700 -36.75100 1.000 153.14033 ?  11  GLY A O   1 
ATOM   4573 N N   . LEU E 1 11  ? -5.67300  64.71800 -36.84100 1.000 151.49406 ?  12  LEU A N   1 
ATOM   4574 C CA  . LEU E 1 11  ? -5.77000  64.91900 -38.28000 1.000 156.66644 ?  12  LEU A CA  1 
ATOM   4575 C C   . LEU E 1 11  ? -4.38700  64.81200 -38.91100 1.000 151.80956 ?  12  LEU A C   1 
ATOM   4576 O O   . LEU E 1 11  ? -3.39000  65.21700 -38.30700 1.000 143.56564 ?  12  LEU A O   1 
ATOM   4577 C CB  . LEU E 1 11  ? -6.39200  66.28400 -38.59200 1.000 157.67077 ?  12  LEU A CB  1 
ATOM   4578 C CG  . LEU E 1 11  ? -6.22400  66.88200 -39.98900 1.000 161.54681 ?  12  LEU A CG  1 
ATOM   4579 C CD1 . LEU E 1 11  ? -7.12300  66.18400 -41.00300 1.000 167.24179 ?  12  LEU A CD1 1 
ATOM   4580 C CD2 . LEU E 1 11  ? -6.48600  68.37700 -39.95300 1.000 157.89597 ?  12  LEU A CD2 1 
ATOM   4581 N N   . VAL E 1 12  ? -4.33100  64.25100 -40.11800 1.000 158.09948 ?  13  VAL A N   1 
ATOM   4582 C CA  . VAL E 1 12  ? -3.09500  64.13200 -40.88900 1.000 151.22301 ?  13  VAL A CA  1 
ATOM   4583 C C   . VAL E 1 12  ? -3.42200  64.30000 -42.36500 1.000 153.32574 ?  13  VAL A C   1 
ATOM   4584 O O   . VAL E 1 12  ? -4.36700  63.69100 -42.87000 1.000 156.06708 ?  13  VAL A O   1 
ATOM   4585 C CB  . VAL E 1 12  ? -2.39500  62.77800 -40.65700 1.000 146.37548 ?  13  VAL A CB  1 
ATOM   4586 C CG1 . VAL E 1 12  ? -1.34100  62.54900 -41.71600 1.000 140.61253 ?  13  VAL A CG1 1 
ATOM   4587 C CG2 . VAL E 1 12  ? -1.77100  62.72000 -39.28500 1.000 141.46781 ?  13  VAL A CG2 1 
ATOM   4588 N N   . GLN E 1 13  ? -2.64600  65.12800 -43.05900 1.000 158.76463 ?  14  GLN A N   1 
ATOM   4589 C CA  . GLN E 1 13  ? -2.84100  65.27000 -44.49000 1.000 158.84193 ?  14  GLN A CA  1 
ATOM   4590 C C   . GLN E 1 13  ? -2.40800  63.99100 -45.20600 1.000 154.00568 ?  14  GLN A C   1 
ATOM   4591 O O   . GLN E 1 13  ? -1.50000  63.29300 -44.74800 1.000 150.03030 ?  14  GLN A O   1 
ATOM   4592 C CB  . GLN E 1 13  ? -2.05900  66.45800 -45.04200 1.000 154.30481 ?  14  GLN A CB  1 
ATOM   4593 C CG  . GLN E 1 13  ? -2.10400  67.72100 -44.20600 1.000 153.63633 ?  14  GLN A CG  1 
ATOM   4594 C CD  . GLN E 1 13  ? -1.84900  68.95400 -45.05500 1.000 149.94178 ?  14  GLN A CD  1 
ATOM   4595 O OE1 . GLN E 1 13  ? -2.70300  69.83600 -45.17100 1.000 154.29227 ?  14  GLN A OE1 1 
ATOM   4596 N NE2 . GLN E 1 13  ? -0.66800  69.01300 -45.66600 1.000 141.76132 ?  14  GLN A NE2 1 
ATOM   4597 N N   . PRO E 1 14  ? -3.06400  63.65300 -46.31600 1.000 162.75627 ?  15  PRO A N   1 
ATOM   4598 C CA  . PRO E 1 14  ? -2.65700  62.48000 -47.09700 1.000 156.11803 ?  15  PRO A CA  1 
ATOM   4599 C C   . PRO E 1 14  ? -1.15600  62.44400 -47.35600 1.000 152.90905 ?  15  PRO A C   1 
ATOM   4600 O O   . PRO E 1 14  ? -0.56500  63.40500 -47.85700 1.000 152.31497 ?  15  PRO A O   1 
ATOM   4601 C CB  . PRO E 1 14  ? -3.45700  62.63800 -48.39000 1.000 152.07635 ?  15  PRO A CB  1 
ATOM   4602 C CG  . PRO E 1 14  ? -4.73000  63.27300 -47.92700 1.000 156.28229 ?  15  PRO A CG  1 
ATOM   4603 C CD  . PRO E 1 14  ? -4.33400  64.22000 -46.80600 1.000 165.02354 ?  15  PRO A CD  1 
ATOM   4604 N N   . GLY E 1 15  ? -0.54600  61.30800 -47.01600 1.000 155.89343 ?  16  GLY A N   1 
ATOM   4605 C CA  . GLY E 1 15  ? 0.88400   61.10500 -47.09400 1.000 155.34911 ?  16  GLY A CA  1 
ATOM   4606 C C   . GLY E 1 15  ? 1.61200   61.14000 -45.76400 1.000 154.29947 ?  16  GLY A C   1 
ATOM   4607 O O   . GLY E 1 15  ? 2.76600   60.69600 -45.70300 1.000 153.61304 ?  16  GLY A O   1 
ATOM   4608 N N   . GLY E 1 16  ? 0.97800   61.63900 -44.70200 1.000 152.01761 ?  17  GLY A N   1 
ATOM   4609 C CA  . GLY E 1 16  ? 1.61700   61.77400 -43.41000 1.000 149.11554 ?  17  GLY A CA  1 
ATOM   4610 C C   . GLY E 1 16  ? 1.49900   60.53700 -42.53400 1.000 149.02214 ?  17  GLY A C   1 
ATOM   4611 O O   . GLY E 1 16  ? 1.01200   59.48200 -42.94500 1.000 151.03450 ?  17  GLY A O   1 
ATOM   4612 N N   . SER E 1 17  ? 1.91700   60.70200 -41.27800 1.000 155.22523 ?  18  SER A N   1 
ATOM   4613 C CA  . SER E 1 17  ? 2.04200   59.61000 -40.32000 1.000 153.95581 ?  18  SER A CA  1 
ATOM   4614 C C   . SER E 1 17  ? 1.42000   60.00500 -38.98800 1.000 153.27388 ?  18  SER A C   1 
ATOM   4615 O O   . SER E 1 17  ? 1.09100   61.17000 -38.74900 1.000 154.02946 ?  18  SER A O   1 
ATOM   4616 C CB  . SER E 1 17  ? 3.50900   59.22400 -40.09100 1.000 149.91313 ?  18  SER A CB  1 
ATOM   4617 O OG  . SER E 1 17  ? 4.20700   59.11100 -41.31700 1.000 153.90013 ?  18  SER A OG  1 
ATOM   4618 N N   . LEU E 1 18  ? 1.26800   59.00400 -38.12000 1.000 133.17330 ?  19  LEU A N   1 
ATOM   4619 C CA  . LEU E 1 18  ? 0.73900   59.14100 -36.77100 1.000 134.35410 ?  19  LEU A CA  1 
ATOM   4620 C C   . LEU E 1 18  ? 0.87500   57.79700 -36.06800 1.000 136.44879 ?  19  LEU A C   1 
ATOM   4621 O O   . LEU E 1 18  ? 0.67000   56.75600 -36.68600 1.000 136.09414 ?  19  LEU A O   1 
ATOM   4622 C CB  . LEU E 1 18  ? -0.72400  59.61200 -36.81300 1.000 131.05339 ?  19  LEU A CB  1 
ATOM   4623 C CG  . LEU E 1 18  ? -1.42100  60.13200 -35.55900 1.000 132.28085 ?  19  LEU A CG  1 
ATOM   4624 C CD1 . LEU E 1 18  ? -2.74500  60.78100 -35.92400 1.000 128.63965 ?  19  LEU A CD1 1 
ATOM   4625 C CD2 . LEU E 1 18  ? -1.67800  58.99000 -34.62400 1.000 133.54268 ?  19  LEU A CD2 1 
ATOM   4626 N N   . ARG E 1 19  ? 1.19100   57.82200 -34.77500 1.000 128.41465 ?  20  ARG A N   1 
ATOM   4627 C CA  . ARG E 1 19  ? 1.27800   56.60500 -33.97800 1.000 130.15404 ?  20  ARG A CA  1 
ATOM   4628 C C   . ARG E 1 19  ? 0.12400   56.60900 -32.98500 1.000 129.37192 ?  20  ARG A C   1 
ATOM   4629 O O   . ARG E 1 19  ? -0.08600  57.59400 -32.26400 1.000 129.54675 ?  20  ARG A O   1 
ATOM   4630 C CB  . ARG E 1 19  ? 2.62400   56.48100 -33.25300 1.000 132.26106 ?  20  ARG A CB  1 
ATOM   4631 C CG  . ARG E 1 19  ? 2.62200   56.84500 -31.76200 1.000 132.56861 ?  20  ARG A CG  1 
ATOM   4632 C CD  . ARG E 1 19  ? 3.91400   56.47900 -31.05300 1.000 134.38579 ?  20  ARG A CD  1 
ATOM   4633 N NE  . ARG E 1 19  ? 4.28200   55.07600 -31.19600 1.000 135.71861 ?  20  ARG A NE  1 
ATOM   4634 C CZ  . ARG E 1 19  ? 5.48100   54.59700 -30.89700 1.000 137.78669 ?  20  ARG A CZ  1 
ATOM   4635 N NH1 . ARG E 1 19  ? 6.43900   55.37900 -30.43000 1.000 138.53530 ?  20  ARG A NH1 1 
ATOM   4636 N NH2 . ARG E 1 19  ? 5.72700   53.30200 -31.07600 1.000 139.43987 ?  20  ARG A NH2 1 
ATOM   4637 N N   . LEU E 1 20  ? -0.67400  55.54900 -33.02000 1.000 124.16123 ?  21  LEU A N   1 
ATOM   4638 C CA  . LEU E 1 20  ? -1.69500  55.30900 -32.02000 1.000 123.46533 ?  21  LEU A CA  1 
ATOM   4639 C C   . LEU E 1 20  ? -1.10100  54.50300 -30.87700 1.000 125.03556 ?  21  LEU A C   1 
ATOM   4640 O O   . LEU E 1 20  ? -0.20100  53.68300 -31.08000 1.000 126.07988 ?  21  LEU A O   1 
ATOM   4641 C CB  . LEU E 1 20  ? -2.86500  54.56500 -32.65400 1.000 120.90037 ?  21  LEU A CB  1 
ATOM   4642 C CG  . LEU E 1 20  ? -3.41900  55.35300 -33.83900 1.000 117.37756 ?  21  LEU A CG  1 
ATOM   4643 C CD1 . LEU E 1 20  ? -4.49200  54.58900 -34.58900 1.000 113.20310 ?  21  LEU A CD1 1 
ATOM   4644 C CD2 . LEU E 1 20  ? -3.96900  56.67200 -33.33500 1.000 116.59190 ?  21  LEU A CD2 1 
ATOM   4645 N N   . SER E 1 21  ? -1.65500  54.68800 -29.68400 1.000 126.77391 ?  22  SER A N   1 
ATOM   4646 C CA  . SER E 1 21  ? -1.13900  54.02300 -28.49900 1.000 128.61631 ?  22  SER A CA  1 
ATOM   4647 C C   . SER E 1 21  ? -2.28100  53.35600 -27.74500 1.000 129.16158 ?  22  SER A C   1 
ATOM   4648 O O   . SER E 1 21  ? -3.33200  53.97200 -27.52200 1.000 129.59715 ?  22  SER A O   1 
ATOM   4649 C CB  . SER E 1 21  ? -0.40000  55.01300 -27.58800 1.000 131.07798 ?  22  SER A CB  1 
ATOM   4650 O OG  . SER E 1 21  ? 0.32300   55.95800 -28.36600 1.000 130.26728 ?  22  SER A OG  1 
ATOM   4651 N N   . CYS E 1 22  ? -2.04300  52.10000 -27.34300 1.000 120.95206 ?  23  CYS A N   1 
ATOM   4652 C CA  . CYS E 1 22  ? -2.97600  51.25600 -26.59300 1.000 122.16326 ?  23  CYS A CA  1 
ATOM   4653 C C   . CYS E 1 22  ? -2.23300  50.68700 -25.38700 1.000 126.45210 ?  23  CYS A C   1 
ATOM   4654 O O   . CYS E 1 22  ? -1.52400  49.68700 -25.51000 1.000 125.86846 ?  23  CYS A O   1 
ATOM   4655 C CB  . CYS E 1 22  ? -3.51600  50.13200 -27.48300 1.000 119.03494 ?  23  CYS A CB  1 
ATOM   4656 S SG  . CYS E 1 22  ? -4.66200  48.94300 -26.71000 1.000 119.65936 ?  23  CYS A SG  1 
ATOM   4657 N N   . ALA E 1 23  ? -2.38600  51.31700 -24.22900 1.000 115.10872 ?  24  ALA A N   1 
ATOM   4658 C CA  . ALA E 1 23  ? -1.75700  50.86700 -22.99700 1.000 121.05257 ?  24  ALA A CA  1 
ATOM   4659 C C   . ALA E 1 23  ? -2.72100  50.00700 -22.19500 1.000 125.58845 ?  24  ALA A C   1 
ATOM   4660 O O   . ALA E 1 23  ? -3.93700  50.16800 -22.28800 1.000 124.48157 ?  24  ALA A O   1 
ATOM   4661 C CB  . ALA E 1 23  ? -1.29600  52.05500 -22.15900 1.000 125.10969 ?  24  ALA A CB  1 
ATOM   4662 N N   . ALA E 1 24  ? -2.17500  49.07200 -21.41800 1.000 121.11653 ?  25  ALA A N   1 
ATOM   4663 C CA  . ALA E 1 24  ? -3.00300  48.09200 -20.72900 1.000 125.79142 ?  25  ALA A CA  1 
ATOM   4664 C C   . ALA E 1 24  ? -2.71100  48.08600 -19.23900 1.000 134.77865 ?  25  ALA A C   1 
ATOM   4665 O O   . ALA E 1 24  ? -1.56500  48.24800 -18.81200 1.000 140.31768 ?  25  ALA A O   1 
ATOM   4666 C CB  . ALA E 1 24  ? -2.79400  46.68800 -21.27300 1.000 119.75134 ?  25  ALA A CB  1 
ATOM   4667 N N   . SER E 1 25  ? -3.76900  47.88900 -18.46000 1.000 141.29248 ?  26  SER A N   1 
ATOM   4668 C CA  . SER E 1 25  ? -3.71100  47.87100 -17.01000 1.000 145.99106 ?  26  SER A CA  1 
ATOM   4669 C C   . SER E 1 25  ? -4.35500  46.58900 -16.51000 1.000 143.79804 ?  26  SER A C   1 
ATOM   4670 O O   . SER E 1 25  ? -5.37100  46.14200 -17.05500 1.000 136.54347 ?  26  SER A O   1 
ATOM   4671 C CB  . SER E 1 25  ? -4.42700  49.07500 -16.39800 1.000 142.10089 ?  26  SER A CB  1 
ATOM   4672 O OG  . SER E 1 25  ? -3.97500  50.28700 -16.96900 1.000 141.57139 ?  26  SER A OG  1 
ATOM   4673 N N   . GLY E 1 26  ? -3.77800  46.03700 -15.44300 1.000 147.97259 ?  27  GLY A N   1 
ATOM   4674 C CA  . GLY E 1 26  ? -4.27400  44.85600 -14.76000 1.000 146.84748 ?  27  GLY A CA  1 
ATOM   4675 C C   . GLY E 1 26  ? -4.10100  43.52400 -15.45800 1.000 145.16247 ?  27  GLY A C   1 
ATOM   4676 O O   . GLY E 1 26  ? -4.76000  42.55700 -15.07000 1.000 142.44101 ?  27  GLY A O   1 
ATOM   4677 N N   . PHE E 1 27  ? -3.23500  43.43700 -16.46700 1.000 150.64534 ?  28  PHE A N   1 
ATOM   4678 C CA  . PHE E 1 27  ? -2.98200  42.19000 -17.19100 1.000 146.51594 ?  28  PHE A CA  1 
ATOM   4679 C C   . PHE E 1 27  ? -1.79000  42.39900 -18.12100 1.000 146.74918 ?  28  PHE A C   1 
ATOM   4680 O O   . PHE E 1 27  ? -1.73000  43.40000 -18.84300 1.000 144.56092 ?  28  PHE A O   1 
ATOM   4681 C CB  . PHE E 1 27  ? -4.19400  41.68600 -17.98300 1.000 137.19954 ?  28  PHE A CB  1 
ATOM   4682 C CG  . PHE E 1 27  ? -4.38500  42.36800 -19.28700 1.000 131.03268 ?  28  PHE A CG  1 
ATOM   4683 C CD1 . PHE E 1 27  ? -4.85900  43.66000 -19.34200 1.000 130.66794 ?  28  PHE A CD1 1 
ATOM   4684 C CD2 . PHE E 1 27  ? -4.04100  41.72600 -20.46500 1.000 125.45986 ?  28  PHE A CD2 1 
ATOM   4685 C CE1 . PHE E 1 27  ? -5.02400  44.28700 -20.55300 1.000 124.99990 ?  28  PHE A CE1 1 
ATOM   4686 C CE2 . PHE E 1 27  ? -4.19100  42.35100 -21.67600 1.000 119.85432 ?  28  PHE A CE2 1 
ATOM   4687 C CZ  . PHE E 1 27  ? -4.68900  43.63100 -21.72600 1.000 119.59874 ?  28  PHE A CZ  1 
ATOM   4688 N N   . ASP E 1 28  ? -0.82100  41.49000 -18.10300 1.000 138.73915 ?  29  ASP A N   1 
ATOM   4689 C CA  . ASP E 1 28  ? 0.36900   41.69500 -18.91200 1.000 137.15466 ?  29  ASP A CA  1 
ATOM   4690 C C   . ASP E 1 28  ? 0.04500   41.46400 -20.38300 1.000 125.11276 ?  29  ASP A C   1 
ATOM   4691 O O   . ASP E 1 28  ? -0.69600  40.54900 -20.74200 1.000 120.19287 ?  29  ASP A O   1 
ATOM   4692 C CB  . ASP E 1 28  ? 1.48700   40.74700 -18.47300 1.000 141.88344 ?  29  ASP A CB  1 
ATOM   4693 C CG  . ASP E 1 28  ? 2.80000   40.99200 -19.21300 1.000 139.65747 ?  29  ASP A CG  1 
ATOM   4694 O OD1 . ASP E 1 28  ? 2.85400   41.90700 -20.06000 1.000 133.90829 ?  29  ASP A OD1 1 
ATOM   4695 O OD2 . ASP E 1 28  ? 3.78600   40.27100 -18.94300 1.000 143.25178 ?  29  ASP A OD2 1 
ATOM   4696 N N   . LEU E 1 29  ? 0.58200   42.33400 -21.23600 1.000 136.66260 ?  30  LEU A N   1 
ATOM   4697 C CA  . LEU E 1 29  ? 0.40500   42.16500 -22.67300 1.000 127.61251 ?  30  LEU A CA  1 
ATOM   4698 C C   . LEU E 1 29  ? 1.23800   41.02200 -23.21900 1.000 125.97421 ?  30  LEU A C   1 
ATOM   4699 O O   . LEU E 1 29  ? 0.84600   40.39200 -24.21100 1.000 121.58638 ?  30  LEU A O   1 
ATOM   4700 C CB  . LEU E 1 29  ? 0.74800   43.45000 -23.42100 1.000 124.69709 ?  30  LEU A CB  1 
ATOM   4701 C CG  . LEU E 1 29  ? -0.21100  44.60500 -23.17600 1.000 125.18271 ?  30  LEU A CG  1 
ATOM   4702 C CD1 . LEU E 1 29  ? -0.03100  45.65700 -24.25100 1.000 120.42938 ?  30  LEU A CD1 1 
ATOM   4703 C CD2 . LEU E 1 29  ? -1.61200  44.03000 -23.23200 1.000 122.90051 ?  30  LEU A CD2 1 
ATOM   4704 N N   . TRP E 1 30  ? 2.39500   40.75800 -22.60200 1.000 123.93720 ?  35  TRP A N   1 
ATOM   4705 C CA  . TRP E 1 30  ? 3.36000   39.82600 -23.17800 1.000 123.04778 ?  35  TRP A CA  1 
ATOM   4706 C C   . TRP E 1 30  ? 2.70400   38.49700 -23.52700 1.000 120.55610 ?  35  TRP A C   1 
ATOM   4707 O O   . TRP E 1 30  ? 2.75600   38.05600 -24.67900 1.000 117.41883 ?  35  TRP A O   1 
ATOM   4708 C CB  . TRP E 1 30  ? 4.53000   39.63900 -22.21100 1.000 130.12197 ?  35  TRP A CB  1 
ATOM   4709 C CG  . TRP E 1 30  ? 5.53300   38.62700 -22.65200 1.000 130.20082 ?  35  TRP A CG  1 
ATOM   4710 C CD1 . TRP E 1 30  ? 5.74500   37.40800 -22.09800 1.000 133.19290 ?  35  TRP A CD1 1 
ATOM   4711 C CD2 . TRP E 1 30  ? 6.43900   38.72700 -23.75500 1.000 128.10462 ?  35  TRP A CD2 1 
ATOM   4712 N NE1 . TRP E 1 30  ? 6.73800   36.74200 -22.76700 1.000 132.78731 ?  35  TRP A NE1 1 
ATOM   4713 C CE2 . TRP E 1 30  ? 7.18100   37.53000 -23.79400 1.000 130.28016 ?  35  TRP A CE2 1 
ATOM   4714 C CE3 . TRP E 1 30  ? 6.70300   39.71400 -24.70800 1.000 125.66070 ?  35  TRP A CE3 1 
ATOM   4715 C CZ2 . TRP E 1 30  ? 8.16600   37.29000 -24.74500 1.000 130.80598 ?  35  TRP A CZ2 1 
ATOM   4716 C CZ3 . TRP E 1 30  ? 7.68400   39.47300 -25.65500 1.000 126.71102 ?  35  TRP A CZ3 1 
ATOM   4717 C CH2 . TRP E 1 30  ? 8.40400   38.26900 -25.66500 1.000 129.57672 ?  35  TRP A CH2 1 
ATOM   4718 N N   . TYR E 1 31  ? 2.01500   37.88300 -22.56900 1.000 122.03637 ?  36  TYR A N   1 
ATOM   4719 C CA  . TYR E 1 31  ? 1.35700   36.60000 -22.81800 1.000 120.02371 ?  36  TYR A CA  1 
ATOM   4720 C C   . TYR E 1 31  ? -0.03200  36.75600 -23.43300 1.000 115.95221 ?  36  TYR A C   1 
ATOM   4721 O O   . TYR E 1 31  ? -0.94800  36.02800 -23.04600 1.000 116.27390 ?  36  TYR A O   1 
ATOM   4722 C CB  . TYR E 1 31  ? 1.25600   35.82400 -21.50400 1.000 124.92581 ?  36  TYR A CB  1 
ATOM   4723 C CG  . TYR E 1 31  ? 2.45900   35.85300 -20.58100 1.000 131.59219 ?  36  TYR A CG  1 
ATOM   4724 C CD1 . TYR E 1 31  ? 3.65600   35.25400 -20.94100 1.000 132.14120 ?  36  TYR A CD1 1 
ATOM   4725 C CD2 . TYR E 1 31  ? 2.38200   36.46300 -19.33300 1.000 138.80729 ?  36  TYR A CD2 1 
ATOM   4726 C CE1 . TYR E 1 31  ? 4.74400   35.26200 -20.08300 1.000 139.22067 ?  36  TYR A CE1 1 
ATOM   4727 C CE2 . TYR E 1 31  ? 3.46500   36.48200 -18.47300 1.000 147.17873 ?  36  TYR A CE2 1 
ATOM   4728 C CZ  . TYR E 1 31  ? 4.64300   35.88500 -18.85300 1.000 147.14766 ?  36  TYR A CZ  1 
ATOM   4729 O OH  . TYR E 1 31  ? 5.71800   35.90700 -17.99300 1.000 156.32485 ?  36  TYR A OH  1 
ATOM   4730 N N   . TYR E 1 32  ? -0.23300  37.65500 -24.39100 1.000 119.70446 ?  37  TYR A N   1 
ATOM   4731 C CA  . TYR E 1 32  ? -1.58400  37.92500 -24.89100 1.000 117.09331 ?  37  TYR A CA  1 
ATOM   4732 C C   . TYR E 1 32  ? -1.48700  38.47400 -26.31000 1.000 114.89173 ?  37  TYR A C   1 
ATOM   4733 O O   . TYR E 1 32  ? -0.46500  38.31600 -26.98600 1.000 115.69256 ?  37  TYR A O   1 
ATOM   4734 C CB  . TYR E 1 32  ? -2.33500  38.87800 -23.94800 1.000 117.97693 ?  37  TYR A CB  1 
ATOM   4735 C CG  . TYR E 1 32  ? -2.96500  38.20300 -22.75000 1.000 121.21835 ?  37  TYR A CG  1 
ATOM   4736 C CD1 . TYR E 1 32  ? -4.14100  37.48200 -22.86500 1.000 120.22695 ?  37  TYR A CD1 1 
ATOM   4737 C CD2 . TYR E 1 32  ? -2.37500  38.28800 -21.49900 1.000 126.52840 ?  37  TYR A CD2 1 
ATOM   4738 C CE1 . TYR E 1 32  ? -4.70800  36.87100 -21.76200 1.000 123.29189 ?  37  TYR A CE1 1 
ATOM   4739 C CE2 . TYR E 1 32  ? -2.93200  37.68200 -20.39600 1.000 130.24069 ?  37  TYR A CE2 1 
ATOM   4740 C CZ  . TYR E 1 32  ? -4.09700  36.97500 -20.53100 1.000 127.99016 ?  37  TYR A CZ  1 
ATOM   4741 O OH  . TYR E 1 32  ? -4.65400  36.36900 -19.43000 1.000 131.10738 ?  37  TYR A OH  1 
ATOM   4742 N N   . SER E 1 33  ? -2.57200  39.09900 -26.77400 1.000 115.73702 ?  38  SER A N   1 
ATOM   4743 C CA  . SER E 1 33  ? -2.69400  39.56800 -28.15000 1.000 115.49729 ?  38  SER A CA  1 
ATOM   4744 C C   . SER E 1 33  ? -3.33200  40.94600 -28.15900 1.000 113.79070 ?  38  SER A C   1 
ATOM   4745 O O   . SER E 1 33  ? -4.33600  41.15600 -27.47600 1.000 113.02023 ?  38  SER A O   1 
ATOM   4746 C CB  . SER E 1 33  ? -3.54200  38.60600 -28.97600 1.000 117.16619 ?  38  SER A CB  1 
ATOM   4747 O OG  . SER E 1 33  ? -2.90600  37.35300 -29.05000 1.000 118.96267 ?  38  SER A OG  1 
ATOM   4748 N N   . ILE E 1 34  ? -2.76200  41.88400 -28.91500 1.000 109.86350 ?  39  ILE A N   1 
ATOM   4749 C CA  . ILE E 1 34  ? -3.39600  43.18000 -29.13300 1.000 110.28770 ?  39  ILE A CA  1 
ATOM   4750 C C   . ILE E 1 34  ? -3.71800  43.30900 -30.61400 1.000 114.30577 ?  39  ILE A C   1 
ATOM   4751 O O   . ILE E 1 34  ? -2.84200  43.13900 -31.46600 1.000 117.22973 ?  39  ILE A O   1 
ATOM   4752 C CB  . ILE E 1 34  ? -2.52700  44.35800 -28.65300 1.000 108.56448 ?  39  ILE A CB  1 
ATOM   4753 C CG1 . ILE E 1 34  ? -2.47900  44.40300 -27.12100 1.000 106.34454 ?  39  ILE A CG1 1 
ATOM   4754 C CG2 . ILE E 1 34  ? -3.05400  45.67200 -29.20900 1.000 110.00820 ?  39  ILE A CG2 1 
ATOM   4755 C CD1 . ILE E 1 34  ? -3.80300  44.07500 -26.44400 1.000 107.67495 ?  39  ILE A CD1 1 
ATOM   4756 N N   . HIS E 1 35  ? -4.97700  43.59300 -30.91500 1.000 108.84592 ?  40  HIS A N   1 
ATOM   4757 C CA  . HIS E 1 35  ? -5.43500  43.80500 -32.27800 1.000 113.85812 ?  40  HIS A CA  1 
ATOM   4758 C C   . HIS E 1 35  ? -5.91600  45.23900 -32.44700 1.000 115.49246 ?  40  HIS A C   1 
ATOM   4759 O O   . HIS E 1 35  ? -6.37600  45.87700 -31.49600 1.000 112.81633 ?  40  HIS A O   1 
ATOM   4760 C CB  . HIS E 1 35  ? -6.55500  42.81400 -32.61800 1.000 115.70309 ?  40  HIS A CB  1 
ATOM   4761 C CG  . HIS E 1 35  ? -6.17700  41.37900 -32.40300 1.000 114.04031 ?  40  HIS A CG  1 
ATOM   4762 N ND1 . HIS E 1 35  ? -5.95100  40.50300 -33.44400 1.000 116.92972 ?  40  HIS A ND1 1 
ATOM   4763 C CD2 . HIS E 1 35  ? -5.90600  40.69100 -31.26800 1.000 110.40977 ?  40  HIS A CD2 1 
ATOM   4764 C CE1 . HIS E 1 35  ? -5.60400  39.32400 -32.95800 1.000 114.86202 ?  40  HIS A CE1 1 
ATOM   4765 N NE2 . HIS E 1 35  ? -5.56300  39.41400 -31.64100 1.000 111.07760 ?  40  HIS A NE2 1 
ATOM   4766 N N   . TRP E 1 36  ? -5.82600  45.72500 -33.68400 1.000 117.63360 ?  41  TRP A N   1 
ATOM   4767 C CA  . TRP E 1 36  ? -6.39100  47.00600 -34.08900 1.000 120.73028 ?  41  TRP A CA  1 
ATOM   4768 C C   . TRP E 1 36  ? -7.44000  46.77900 -35.16300 1.000 126.96950 ?  41  TRP A C   1 
ATOM   4769 O O   . TRP E 1 36  ? -7.15300  46.13200 -36.18300 1.000 130.16762 ?  41  TRP A O   1 
ATOM   4770 C CB  . TRP E 1 36  ? -5.33100  47.97300 -34.62600 1.000 122.82042 ?  41  TRP A CB  1 
ATOM   4771 C CG  . TRP E 1 36  ? -4.28200  48.32500 -33.64200 1.000 117.01746 ?  41  TRP A CG  1 
ATOM   4772 C CD1 . TRP E 1 36  ? -3.18400  47.58700 -33.32200 1.000 114.87790 ?  41  TRP A CD1 1 
ATOM   4773 C CD2 . TRP E 1 36  ? -4.23300  49.49600 -32.82100 1.000 113.32577 ?  41  TRP A CD2 1 
ATOM   4774 N NE1 . TRP E 1 36  ? -2.44300  48.22800 -32.35900 1.000 110.04341 ?  41  TRP A NE1 1 
ATOM   4775 C CE2 . TRP E 1 36  ? -3.06900  49.40300 -32.03200 1.000 109.09342 ?  41  TRP A CE2 1 
ATOM   4776 C CE3 . TRP E 1 36  ? -5.05900  50.61500 -32.67800 1.000 113.93604 ?  41  TRP A CE3 1 
ATOM   4777 C CZ2 . TRP E 1 36  ? -2.71100  50.38500 -31.11300 1.000 105.72086 ?  41  TRP A CZ2 1 
ATOM   4778 C CZ3 . TRP E 1 36  ? -4.70300  51.58800 -31.76700 1.000 110.56368 ?  41  TRP A CZ3 1 
ATOM   4779 C CH2 . TRP E 1 36  ? -3.53900  51.46600 -30.99400 1.000 106.62460 ?  41  TRP A CH2 1 
ATOM   4780 N N   . VAL E 1 37  ? -8.63500  47.33200 -34.91700 1.000 115.81565 ?  42  VAL A N   1 
ATOM   4781 C CA  . VAL E 1 37  ? -9.79600  47.32800 -35.81100 1.000 121.61840 ?  42  VAL A CA  1 
ATOM   4782 C C   . VAL E 1 37  ? -10.22800 48.77200 -36.05100 1.000 123.51904 ?  42  VAL A C   1 
ATOM   4783 O O   . VAL E 1 37  ? -10.52200 49.50000 -35.09500 1.000 121.19933 ?  42  VAL A O   1 
ATOM   4784 C CB  . VAL E 1 37  ? -10.97700 46.52200 -35.23600 1.000 122.12530 ?  42  VAL A CB  1 
ATOM   4785 C CG1 . VAL E 1 37  ? -12.13500 46.48900 -36.22400 1.000 128.38494 ?  42  VAL A CG1 1 
ATOM   4786 C CG2 . VAL E 1 37  ? -10.55500 45.09800 -34.90400 1.000 118.56773 ?  42  VAL A CG2 1 
ATOM   4787 N N   . ARG E 1 38  ? -10.25600 49.18700 -37.31700 1.000 127.34690 ?  43  ARG A N   1 
ATOM   4788 C CA  . ARG E 1 38  ? -10.65700 50.53400 -37.70600 1.000 128.46390 ?  43  ARG A CA  1 
ATOM   4789 C C   . ARG E 1 38  ? -12.09500 50.52500 -38.21900 1.000 131.35778 ?  43  ARG A C   1 
ATOM   4790 O O   . ARG E 1 38  ? -12.53200 49.56800 -38.86400 1.000 134.37883 ?  43  ARG A O   1 
ATOM   4791 C CB  . ARG E 1 38  ? -9.71300  51.10500 -38.77200 1.000 129.96632 ?  43  ARG A CB  1 
ATOM   4792 C CG  . ARG E 1 38  ? -10.18200 50.86000 -40.18600 1.000 134.25799 ?  43  ARG A CG  1 
ATOM   4793 C CD  . ARG E 1 38  ? -9.61600  51.82200 -41.20800 1.000 136.28876 ?  43  ARG A CD  1 
ATOM   4794 N NE  . ARG E 1 38  ? -8.18800  51.63900 -41.43600 1.000 135.22017 ?  43  ARG A NE  1 
ATOM   4795 C CZ  . ARG E 1 38  ? -7.59400  51.83700 -42.60600 1.000 137.64049 ?  43  ARG A CZ  1 
ATOM   4796 N NH1 . ARG E 1 38  ? -8.29100  52.09700 -43.70000 1.000 140.72785 ?  43  ARG A NH1 1 
ATOM   4797 N NH2 . ARG E 1 38  ? -6.27100  51.75200 -42.68600 1.000 136.39832 ?  43  ARG A NH2 1 
ATOM   4798 N N   . GLN E 1 39  ? -12.84800 51.56200 -37.85300 1.000 132.29114 ?  44  GLN A N   1 
ATOM   4799 C CA  . GLN E 1 39  ? -14.23000 51.76900 -38.27600 1.000 134.90107 ?  44  GLN A CA  1 
ATOM   4800 C C   . GLN E 1 39  ? -14.29900 53.08400 -39.04600 1.000 136.91566 ?  44  GLN A C   1 
ATOM   4801 O O   . GLN E 1 39  ? -14.15100 54.15900 -38.45200 1.000 135.86228 ?  44  GLN A O   1 
ATOM   4802 C CB  . GLN E 1 39  ? -15.15000 51.77900 -37.05400 1.000 132.93561 ?  44  GLN A CB  1 
ATOM   4803 C CG  . GLN E 1 39  ? -16.63200 51.60400 -37.32100 1.000 135.14727 ?  44  GLN A CG  1 
ATOM   4804 C CD  . GLN E 1 39  ? -17.40900 51.44300 -36.02800 1.000 132.87502 ?  44  GLN A CD  1 
ATOM   4805 O OE1 . GLN E 1 39  ? -16.97700 51.91500 -34.97600 1.000 130.51485 ?  44  GLN A OE1 1 
ATOM   4806 N NE2 . GLN E 1 39  ? -18.55000 50.76200 -36.09400 1.000 134.12080 ?  44  GLN A NE2 1 
ATOM   4807 N N   . ALA E 1 40  ? -14.48800 53.00100 -40.36300 1.000 128.86870 ?  45  ALA A N   1 
ATOM   4808 C CA  . ALA E 1 40  ? -14.62800 54.20800 -41.16500 1.000 131.03326 ?  45  ALA A CA  1 
ATOM   4809 C C   . ALA E 1 40  ? -15.96800 54.88300 -40.87400 1.000 131.70076 ?  45  ALA A C   1 
ATOM   4810 O O   . ALA E 1 40  ? -16.92100 54.22000 -40.45200 1.000 131.40475 ?  45  ALA A O   1 
ATOM   4811 C CB  . ALA E 1 40  ? -14.52100 53.88000 -42.65400 1.000 135.13855 ?  45  ALA A CB  1 
ATOM   4812 N N   . PRO E 1 41  ? -16.06300 56.21100 -41.07800 1.000 131.46178 ?  46  PRO A N   1 
ATOM   4813 C CA  . PRO E 1 41  ? -17.31600 56.91500 -40.77000 1.000 132.37650 ?  46  PRO A CA  1 
ATOM   4814 C C   . PRO E 1 41  ? -18.51900 56.25700 -41.41800 1.000 133.87364 ?  46  PRO A C   1 
ATOM   4815 O O   . PRO E 1 41  ? -18.65300 56.24900 -42.64600 1.000 136.79915 ?  46  PRO A O   1 
ATOM   4816 C CB  . PRO E 1 41  ? -17.08600 58.32700 -41.32500 1.000 134.24682 ?  46  PRO A CB  1 
ATOM   4817 C CG  . PRO E 1 41  ? -15.78800 58.28600 -42.06100 1.000 134.27105 ?  46  PRO A CG  1 
ATOM   4818 C CD  . PRO E 1 41  ? -15.01300 57.13500 -41.52800 1.000 131.80905 ?  46  PRO A CD  1 
ATOM   4819 N N   . GLY E 1 42  ? -19.40900 55.71800 -40.59100 1.000 134.97478 ?  47  GLY A N   1 
ATOM   4820 C CA  . GLY E 1 42  ? -20.59400 55.07400 -41.10900 1.000 136.62521 ?  47  GLY A CA  1 
ATOM   4821 C C   . GLY E 1 42  ? -20.35800 53.76700 -41.82900 1.000 139.42185 ?  47  GLY A C   1 
ATOM   4822 O O   . GLY E 1 42  ? -21.26700 53.28400 -42.51100 1.000 142.72848 ?  47  GLY A O   1 
ATOM   4823 N N   . LYS E 1 43  ? -19.16700 53.18500 -41.71900 1.000 130.33986 ?  48  LYS A N   1 
ATOM   4824 C CA  . LYS E 1 43  ? -18.84300 51.94700 -42.41200 1.000 134.00664 ?  48  LYS A CA  1 
ATOM   4825 C C   . LYS E 1 43  ? -18.68700 50.81200 -41.40100 1.000 132.13869 ?  48  LYS A C   1 
ATOM   4826 O O   . LYS E 1 43  ? -18.80200 51.00300 -40.18600 1.000 127.69982 ?  48  LYS A O   1 
ATOM   4827 C CB  . LYS E 1 43  ? -17.58000 52.12700 -43.25500 1.000 135.70360 ?  48  LYS A CB  1 
ATOM   4828 C CG  . LYS E 1 43  ? -17.78700 53.06300 -44.43200 1.000 138.41176 ?  48  LYS A CG  1 
ATOM   4829 C CD  . LYS E 1 43  ? -18.87100 52.55900 -45.37600 1.000 143.60613 ?  48  LYS A CD  1 
ATOM   4830 C CE  . LYS E 1 43  ? -18.44900 51.30300 -46.09900 1.000 149.48933 ?  48  LYS A CE  1 
ATOM   4831 N NZ  . LYS E 1 43  ? -17.06700 51.46000 -46.61200 1.000 149.47372 ?  48  LYS A NZ  1 
ATOM   4832 N N   . GLY E 1 44  ? -18.41500 49.61600 -41.91900 1.000 144.64774 ?  49  GLY A N   1 
ATOM   4833 C CA  . GLY E 1 44  ? -18.28700 48.43700 -41.09100 1.000 143.56899 ?  49  GLY A CA  1 
ATOM   4834 C C   . GLY E 1 44  ? -16.93700 48.33900 -40.40500 1.000 138.98241 ?  49  GLY A C   1 
ATOM   4835 O O   . GLY E 1 44  ? -16.07400 49.20800 -40.51700 1.000 136.37549 ?  49  GLY A O   1 
ATOM   4836 N N   . LEU E 1 45  ? -16.75500 47.24500 -39.67600 1.000 141.40145 ?  50  LEU A N   1 
ATOM   4837 C CA  . LEU E 1 45  ? -15.48200 47.05000 -39.01000 1.000 136.90296 ?  50  LEU A CA  1 
ATOM   4838 C C   . LEU E 1 45  ? -14.44100 46.49600 -39.97800 1.000 140.11339 ?  50  LEU A C   1 
ATOM   4839 O O   . LEU E 1 45  ? -14.75800 45.84800 -40.97700 1.000 146.78135 ?  50  LEU A O   1 
ATOM   4840 C CB  . LEU E 1 45  ? -15.63500 46.11600 -37.80900 1.000 134.49463 ?  50  LEU A CB  1 
ATOM   4841 C CG  . LEU E 1 45  ? -16.17700 46.77800 -36.54000 1.000 129.52390 ?  50  LEU A CG  1 
ATOM   4842 C CD1 . LEU E 1 45  ? -15.80700 45.97500 -35.30500 1.000 126.41936 ?  50  LEU A CD1 1 
ATOM   4843 C CD2 . LEU E 1 45  ? -15.64600 48.20200 -36.42700 1.000 126.08913 ?  50  LEU A CD2 1 
ATOM   4844 N N   . GLU E 1 46  ? -13.17600 46.75200 -39.64700 1.000 135.48561 ?  51  GLU A N   1 
ATOM   4845 C CA  . GLU E 1 46  ? -12.03500 46.34600 -40.46600 1.000 136.45888 ?  51  GLU A CA  1 
ATOM   4846 C C   . GLU E 1 46  ? -10.89700 46.02600 -39.51400 1.000 130.24552 ?  51  GLU A C   1 
ATOM   4847 O O   . GLU E 1 46  ? -10.36900 46.93000 -38.86000 1.000 125.84813 ?  51  GLU A O   1 
ATOM   4848 C CB  . GLU E 1 46  ? -11.63100 47.44400 -41.44600 1.000 137.42377 ?  51  GLU A CB  1 
ATOM   4849 C CG  . GLU E 1 46  ? -10.23100 47.28700 -42.03700 1.000 135.90143 ?  51  GLU A CG  1 
ATOM   4850 C CD  . GLU E 1 46  ? -9.98500  48.23400 -43.20200 1.000 138.28093 ?  51  GLU A CD  1 
ATOM   4851 O OE1 . GLU E 1 46  ? -10.08000 49.46200 -43.00800 1.000 137.08168 ?  51  GLU A OE1 1 
ATOM   4852 O OE2 . GLU E 1 46  ? -9.67600  47.75400 -44.31300 1.000 141.19884 -1 51  GLU A OE2 1 
ATOM   4853 N N   . TRP E 1 47  ? -10.52400 44.75000 -39.43000 1.000 137.90767 ?  52  TRP A N   1 
ATOM   4854 C CA  . TRP E 1 47  ? -9.35500  44.38300 -38.64900 1.000 131.28402 ?  52  TRP A CA  1 
ATOM   4855 C C   . TRP E 1 47  ? -8.12000  44.93100 -39.34600 1.000 130.62588 ?  52  TRP A C   1 
ATOM   4856 O O   . TRP E 1 47  ? -7.86600  44.61300 -40.51200 1.000 133.57889 ?  52  TRP A O   1 
ATOM   4857 C CB  . TRP E 1 47  ? -9.25900  42.86800 -38.47600 1.000 129.13323 ?  52  TRP A CB  1 
ATOM   4858 C CG  . TRP E 1 47  ? -7.89300  42.42900 -38.01400 1.000 123.38704 ?  52  TRP A CG  1 
ATOM   4859 C CD1 . TRP E 1 47  ? -7.42100  42.42100 -36.73200 1.000 117.79363 ?  52  TRP A CD1 1 
ATOM   4860 C CD2 . TRP E 1 47  ? -6.83000  41.93300 -38.83700 1.000 123.88796 ?  52  TRP A CD2 1 
ATOM   4861 N NE1 . TRP E 1 47  ? -6.12700  41.96100 -36.71000 1.000 115.87606 ?  52  TRP A NE1 1 
ATOM   4862 C CE2 . TRP E 1 47  ? -5.74300  41.65400 -37.99000 1.000 119.72252 ?  52  TRP A CE2 1 
ATOM   4863 C CE3 . TRP E 1 47  ? -6.69300  41.70300 -40.20800 1.000 127.94376 ?  52  TRP A CE3 1 
ATOM   4864 C CZ2 . TRP E 1 47  ? -4.53400  41.15600 -38.47100 1.000 120.61171 ?  52  TRP A CZ2 1 
ATOM   4865 C CZ3 . TRP E 1 47  ? -5.49300  41.20800 -40.68200 1.000 127.36029 ?  52  TRP A CZ3 1 
ATOM   4866 C CH2 . TRP E 1 47  ? -4.43100  40.93900 -39.81800 1.000 124.23867 ?  52  TRP A CH2 1 
ATOM   4867 N N   . VAL E 1 48  ? -7.37200  45.77600 -38.64400 1.000 124.11782 ?  53  VAL A N   1 
ATOM   4868 C CA  . VAL E 1 48  ? -6.18200  46.38900 -39.21600 1.000 124.66170 ?  53  VAL A CA  1 
ATOM   4869 C C   . VAL E 1 48  ? -4.99700  45.46100 -39.01400 1.000 123.11346 ?  53  VAL A C   1 
ATOM   4870 O O   . VAL E 1 48  ? -4.33300  45.06700 -39.98000 1.000 124.85381 ?  53  VAL A O   1 
ATOM   4871 C CB  . VAL E 1 48  ? -5.90700  47.77800 -38.61100 1.000 123.79540 ?  53  VAL A CB  1 
ATOM   4872 C CG1 . VAL E 1 48  ? -4.68900  48.40400 -39.26900 1.000 124.90410 ?  53  VAL A CG1 1 
ATOM   4873 C CG2 . VAL E 1 48  ? -7.11500  48.66900 -38.79100 1.000 124.92019 ?  53  VAL A CG2 1 
ATOM   4874 N N   . ALA E 1 49  ? -4.71600  45.10100 -37.76600 1.000 123.37736 ?  54  ALA A N   1 
ATOM   4875 C CA  . ALA E 1 49  ? -3.49700  44.32800 -37.53800 1.000 122.77991 ?  54  ALA A CA  1 
ATOM   4876 C C   . ALA E 1 49  ? -3.55000  43.65500 -36.17500 1.000 117.38231 ?  54  ALA A C   1 
ATOM   4877 O O   . ALA E 1 49  ? -4.47700  43.86500 -35.39100 1.000 113.68509 ?  54  ALA A O   1 
ATOM   4878 C CB  . ALA E 1 49  ? -2.25400  45.21500 -37.65600 1.000 126.32967 ?  54  ALA A CB  1 
ATOM   4879 N N   . TYR E 1 50  ? -2.52600  42.85000 -35.89200 1.000 125.13674 ?  55  TYR A N   1 
ATOM   4880 C CA  . TYR E 1 50  ? -2.39800  42.25600 -34.57200 1.000 119.42028 ?  55  TYR A CA  1 
ATOM   4881 C C   . TYR E 1 50  ? -0.93400  42.07000 -34.21100 1.000 120.26472 ?  55  TYR A C   1 
ATOM   4882 O O   . TYR E 1 50  ? -0.05600  42.02200 -35.07400 1.000 127.09566 ?  55  TYR A O   1 
ATOM   4883 C CB  . TYR E 1 50  ? -3.13500  40.91400 -34.46100 1.000 116.59048 ?  55  TYR A CB  1 
ATOM   4884 C CG  . TYR E 1 50  ? -2.61400  39.73800 -35.27300 1.000 119.88513 ?  55  TYR A CG  1 
ATOM   4885 C CD1 . TYR E 1 50  ? -1.35700  39.18500 -35.03800 1.000 121.96681 ?  55  TYR A CD1 1 
ATOM   4886 C CD2 . TYR E 1 50  ? -3.41800  39.13400 -36.22700 1.000 121.24964 ?  55  TYR A CD2 1 
ATOM   4887 C CE1 . TYR E 1 50  ? -0.90700  38.10500 -35.76300 1.000 125.34760 ?  55  TYR A CE1 1 
ATOM   4888 C CE2 . TYR E 1 50  ? -2.97600  38.05700 -36.95500 1.000 123.55919 ?  55  TYR A CE2 1 
ATOM   4889 C CZ  . TYR E 1 50  ? -1.72500  37.54500 -36.71700 1.000 125.40140 ?  55  TYR A CZ  1 
ATOM   4890 O OH  . TYR E 1 50  ? -1.29100  36.46900 -37.45000 1.000 128.03094 ?  55  TYR A OH  1 
ATOM   4891 N N   . ILE E 1 51  ? -0.69700  41.94400 -32.91000 1.000 121.71138 ?  56  ILE A N   1 
ATOM   4892 C CA  . ILE E 1 51  ? 0.60400   41.58800 -32.36400 1.000 121.17041 ?  56  ILE A CA  1 
ATOM   4893 C C   . ILE E 1 51  ? 0.40100   40.57000 -31.24900 1.000 116.06705 ?  56  ILE A C   1 
ATOM   4894 O O   . ILE E 1 51  ? -0.52400  40.69500 -30.43500 1.000 111.25648 ?  56  ILE A O   1 
ATOM   4895 C CB  . ILE E 1 51  ? 1.35700   42.83800 -31.85600 1.000 118.28186 ?  56  ILE A CB  1 
ATOM   4896 C CG1 . ILE E 1 51  ? 2.71100   42.45000 -31.25600 1.000 117.50844 ?  56  ILE A CG1 1 
ATOM   4897 C CG2 . ILE E 1 51  ? 0.50800   43.60700 -30.84700 1.000 111.73692 ?  56  ILE A CG2 1 
ATOM   4898 C CD1 . ILE E 1 51  ? 3.72600   43.59000 -31.22300 1.000 116.96651 ?  56  ILE A CD1 1 
ATOM   4899 N N   . TYR E 1 52  ? 1.26600   39.55300 -31.22300 1.000 123.70761 ?  57  TYR A N   1 
ATOM   4900 C CA  . TYR E 1 52  ? 1.21600   38.46800 -30.24300 1.000 120.39262 ?  57  TYR A CA  1 
ATOM   4901 C C   . TYR E 1 52  ? 2.57600   38.42700 -29.56000 1.000 120.15519 ?  57  TYR A C   1 
ATOM   4902 O O   . TYR E 1 52  ? 3.43800   37.61300 -29.92500 1.000 124.98403 ?  57  TYR A O   1 
ATOM   4903 C CB  . TYR E 1 52  ? 0.89400   37.13700 -30.92300 1.000 124.19110 ?  57  TYR A CB  1 
ATOM   4904 C CG  . TYR E 1 52  ? -0.56900  36.93900 -31.25300 1.000 122.37897 ?  57  TYR A CG  1 
ATOM   4905 C CD1 . TYR E 1 52  ? -1.28700  37.92500 -31.91400 1.000 122.84782 ?  57  TYR A CD1 1 
ATOM   4906 C CD2 . TYR E 1 52  ? -1.21600  35.74900 -30.95900 1.000 120.92011 ?  57  TYR A CD2 1 
ATOM   4907 C CE1 . TYR E 1 52  ? -2.61700  37.75600 -32.22900 1.000 121.81816 ?  57  TYR A CE1 1 
ATOM   4908 C CE2 . TYR E 1 52  ? -2.55000  35.56700 -31.27500 1.000 119.87639 ?  57  TYR A CE2 1 
ATOM   4909 C CZ  . TYR E 1 52  ? -3.24500  36.57600 -31.91100 1.000 120.43801 ?  57  TYR A CZ  1 
ATOM   4910 O OH  . TYR E 1 52  ? -4.57300  36.40100 -32.22600 1.000 120.49029 ?  57  TYR A OH  1 
ATOM   4911 N N   . PRO E 1 53  ? 2.79600   39.28300 -28.53900 1.000 123.19358 ?  58  PRO A N   1 
ATOM   4912 C CA  . PRO E 1 53  ? 4.15400   39.50300 -28.01300 1.000 122.96799 ?  58  PRO A CA  1 
ATOM   4913 C C   . PRO E 1 53  ? 4.94200   38.24500 -27.68000 1.000 125.34546 ?  58  PRO A C   1 
ATOM   4914 O O   . PRO E 1 53  ? 6.02000   38.02300 -28.24600 1.000 130.00894 ?  58  PRO A O   1 
ATOM   4915 C CB  . PRO E 1 53  ? 3.89300   40.32400 -26.74500 1.000 117.24297 ?  58  PRO A CB  1 
ATOM   4916 C CG  . PRO E 1 53  ? 2.67600   41.09800 -27.05700 1.000 116.07131 ?  58  PRO A CG  1 
ATOM   4917 C CD  . PRO E 1 53  ? 1.82500   40.22600 -27.95600 1.000 118.83175 ?  58  PRO A CD  1 
ATOM   4918 N N   . SER E 1 54  ? 4.40700   37.40500 -26.78800 1.000 119.80320 ?  59  SER A N   1 
ATOM   4919 C CA  . SER E 1 54  ? 5.15100   36.22700 -26.34800 1.000 121.65480 ?  59  SER A CA  1 
ATOM   4920 C C   . SER E 1 54  ? 5.21600   35.14600 -27.40400 1.000 126.98893 ?  59  SER A C   1 
ATOM   4921 O O   . SER E 1 54  ? 5.78700   34.08300 -27.12800 1.000 128.87410 ?  59  SER A O   1 
ATOM   4922 C CB  . SER E 1 54  ? 4.54000   35.65200 -25.07000 1.000 118.56680 ?  59  SER A CB  1 
ATOM   4923 O OG  . SER E 1 54  ? 3.17500   35.32900 -25.26200 1.000 117.66764 ?  59  SER A OG  1 
ATOM   4924 N N   . TYR E 1 55  ? 4.66200   35.39100 -28.59200 1.000 118.81427 ?  62  TYR A N   1 
ATOM   4925 C CA  . TYR E 1 55  ? 4.63500   34.41400 -29.66700 1.000 125.98069 ?  62  TYR A CA  1 
ATOM   4926 C C   . TYR E 1 55  ? 5.49400   34.83800 -30.84600 1.000 134.78295 ?  62  TYR A C   1 
ATOM   4927 O O   . TYR E 1 55  ? 5.91400   33.97800 -31.62600 1.000 143.73644 ?  62  TYR A O   1 
ATOM   4928 C CB  . TYR E 1 55  ? 3.19300   34.21400 -30.16900 1.000 124.51987 ?  62  TYR A CB  1 
ATOM   4929 C CG  . TYR E 1 55  ? 2.25500   33.48400 -29.21500 1.000 118.59152 ?  62  TYR A CG  1 
ATOM   4930 C CD1 . TYR E 1 55  ? 2.13600   33.87800 -27.88800 1.000 112.88290 ?  62  TYR A CD1 1 
ATOM   4931 C CD2 . TYR E 1 55  ? 1.44500   32.44200 -29.65500 1.000 119.57816 ?  62  TYR A CD2 1 
ATOM   4932 C CE1 . TYR E 1 55  ? 1.27200   33.23100 -27.01700 1.000 109.76011 ?  62  TYR A CE1 1 
ATOM   4933 C CE2 . TYR E 1 55  ? 0.57200   31.79600 -28.78600 1.000 115.21055 ?  62  TYR A CE2 1 
ATOM   4934 C CZ  . TYR E 1 55  ? 0.49500   32.19300 -27.47300 1.000 110.91711 ?  62  TYR A CZ  1 
ATOM   4935 O OH  . TYR E 1 55  ? -0.36500  31.54800 -26.61600 1.000 108.65766 ?  62  TYR A OH  1 
ATOM   4936 N N   . GLY E 1 56  ? 5.78100   36.12900 -30.97100 1.000 120.35429 ?  63  GLY A N   1 
ATOM   4937 C CA  . GLY E 1 56  ? 6.50300   36.65400 -32.11100 1.000 128.38947 ?  63  GLY A CA  1 
ATOM   4938 C C   . GLY E 1 56  ? 5.68000   36.69400 -33.37900 1.000 134.70983 ?  63  GLY A C   1 
ATOM   4939 O O   . GLY E 1 56  ? 6.19800   36.37400 -34.45500 1.000 144.85535 ?  63  GLY A O   1 
ATOM   4940 N N   . TYR E 1 57  ? 4.40800   37.07500 -33.28000 1.000 129.03227 ?  64  TYR A N   1 
ATOM   4941 C CA  . TYR E 1 57  ? 3.49300   37.10600 -34.41400 1.000 132.33581 ?  64  TYR A CA  1 
ATOM   4942 C C   . TYR E 1 57  ? 3.08600   38.54300 -34.70300 1.000 130.80687 ?  64  TYR A C   1 
ATOM   4943 O O   . TYR E 1 57  ? 2.54600   39.22400 -33.82400 1.000 122.75625 ?  64  TYR A O   1 
ATOM   4944 C CB  . TYR E 1 57  ? 2.25600   36.25500 -34.14000 1.000 126.01202 ?  64  TYR A CB  1 
ATOM   4945 C CG  . TYR E 1 57  ? 2.51600   34.78300 -33.92800 1.000 126.65909 ?  64  TYR A CG  1 
ATOM   4946 C CD1 . TYR E 1 57  ? 3.70700   34.19700 -34.32900 1.000 134.59646 ?  64  TYR A CD1 1 
ATOM   4947 C CD2 . TYR E 1 57  ? 1.55300   33.97600 -33.34200 1.000 119.80116 ?  64  TYR A CD2 1 
ATOM   4948 C CE1 . TYR E 1 57  ? 3.93300   32.85300 -34.14100 1.000 135.46390 ?  64  TYR A CE1 1 
ATOM   4949 C CE2 . TYR E 1 57  ? 1.76700   32.63300 -33.15600 1.000 120.73204 ?  64  TYR A CE2 1 
ATOM   4950 C CZ  . TYR E 1 57  ? 2.95800   32.07500 -33.55600 1.000 128.39259 ?  64  TYR A CZ  1 
ATOM   4951 O OH  . TYR E 1 57  ? 3.17900   30.73000 -33.36900 1.000 129.53631 ?  64  TYR A OH  1 
ATOM   4952 N N   . THR E 1 58  ? 3.34800   39.00400 -35.93000 1.000 124.88057 ?  65  THR A N   1 
ATOM   4953 C CA  . THR E 1 58  ? 2.92100   40.32900 -36.40100 1.000 124.91770 ?  65  THR A CA  1 
ATOM   4954 C C   . THR E 1 58  ? 2.41300   40.17000 -37.83500 1.000 123.86867 ?  65  THR A C   1 
ATOM   4955 O O   . THR E 1 58  ? 3.19500   40.21800 -38.78800 1.000 126.70037 ?  65  THR A O   1 
ATOM   4956 C CB  . THR E 1 58  ? 4.04700   41.35500 -36.32600 1.000 126.16991 ?  65  THR A CB  1 
ATOM   4957 O OG1 . THR E 1 58  ? 5.26500   40.77600 -36.81200 1.000 130.70767 ?  65  THR A OG1 1 
ATOM   4958 C CG2 . THR E 1 58  ? 4.24400   41.83700 -34.89800 1.000 116.42703 ?  65  THR A CG2 1 
ATOM   4959 N N   . TYR E 1 59  ? 1.10600   39.98900 -37.98600 1.000 129.89448 ?  66  TYR A N   1 
ATOM   4960 C CA  . TYR E 1 59  ? 0.46800   39.94700 -39.29400 1.000 129.01261 ?  66  TYR A CA  1 
ATOM   4961 C C   . TYR E 1 59  ? -0.45600  41.14700 -39.43800 1.000 127.51768 ?  66  TYR A C   1 
ATOM   4962 O O   . TYR E 1 59  ? -1.12900  41.54100 -38.48000 1.000 124.76036 ?  66  TYR A O   1 
ATOM   4963 C CB  . TYR E 1 59  ? -0.31600  38.65300 -39.50900 1.000 126.21207 ?  66  TYR A CB  1 
ATOM   4964 C CG  . TYR E 1 59  ? -0.91700  38.54600 -40.89000 1.000 126.96686 ?  66  TYR A CG  1 
ATOM   4965 C CD1 . TYR E 1 59  ? -0.15300  38.81400 -42.01700 1.000 130.21764 ?  66  TYR A CD1 1 
ATOM   4966 C CD2 . TYR E 1 59  ? -2.24200  38.17400 -41.06900 1.000 125.08857 ?  66  TYR A CD2 1 
ATOM   4967 C CE1 . TYR E 1 59  ? -0.69000  38.71700 -43.28400 1.000 131.24180 ?  66  TYR A CE1 1 
ATOM   4968 C CE2 . TYR E 1 59  ? -2.78700  38.07600 -42.33600 1.000 127.33762 ?  66  TYR A CE2 1 
ATOM   4969 C CZ  . TYR E 1 59  ? -2.00500  38.34800 -43.43700 1.000 130.21356 ?  66  TYR A CZ  1 
ATOM   4970 O OH  . TYR E 1 59  ? -2.53200  38.25500 -44.70200 1.000 132.66528 ?  66  TYR A OH  1 
ATOM   4971 N N   . TYR E 1 60  ? -0.47000  41.72900 -40.63600 1.000 127.30148 ?  67  TYR A N   1 
ATOM   4972 C CA  . TYR E 1 60  ? -1.22500  42.93400 -40.93300 1.000 127.17090 ?  67  TYR A CA  1 
ATOM   4973 C C   . TYR E 1 60  ? -2.26400  42.67000 -42.01800 1.000 127.52962 ?  67  TYR A C   1 
ATOM   4974 O O   . TYR E 1 60  ? -2.16200  41.71100 -42.78600 1.000 128.32173 ?  67  TYR A O   1 
ATOM   4975 C CB  . TYR E 1 60  ? -0.29200  44.06600 -41.38700 1.000 129.61874 ?  67  TYR A CB  1 
ATOM   4976 C CG  . TYR E 1 60  ? 0.79200   44.44400 -40.39400 1.000 130.76977 ?  67  TYR A CG  1 
ATOM   4977 C CD1 . TYR E 1 60  ? 1.85100   43.58900 -40.11300 1.000 132.63177 ?  67  TYR A CD1 1 
ATOM   4978 C CD2 . TYR E 1 60  ? 0.75700   45.66300 -39.74600 1.000 130.16547 ?  67  TYR A CD2 1 
ATOM   4979 C CE1 . TYR E 1 60  ? 2.83900   43.94400 -39.20700 1.000 133.98504 ?  67  TYR A CE1 1 
ATOM   4980 C CE2 . TYR E 1 60  ? 1.73200   46.01900 -38.84700 1.000 130.11203 ?  67  TYR A CE2 1 
ATOM   4981 C CZ  . TYR E 1 60  ? 2.77400   45.16400 -38.57700 1.000 131.83913 ?  67  TYR A CZ  1 
ATOM   4982 O OH  . TYR E 1 60  ? 3.75000   45.53300 -37.67300 1.000 129.81377 ?  67  TYR A OH  1 
ATOM   4983 N N   . ALA E 1 61  ? -3.27000  43.54400 -42.07200 1.000 126.75757 ?  68  ALA A N   1 
ATOM   4984 C CA  . ALA E 1 61  ? -4.28200  43.48700 -43.11900 1.000 129.17893 ?  68  ALA A CA  1 
ATOM   4985 C C   . ALA E 1 61  ? -3.69600  43.90700 -44.46700 1.000 131.62547 ?  68  ALA A C   1 
ATOM   4986 O O   . ALA E 1 61  ? -2.63500  44.53100 -44.55200 1.000 131.26560 ?  68  ALA A O   1 
ATOM   4987 C CB  . ALA E 1 61  ? -5.47300  44.37900 -42.77300 1.000 129.98026 ?  68  ALA A CB  1 
ATOM   4988 N N   . ASP E 1 62  ? -4.41900  43.55600 -45.53300 1.000 136.92419 ?  69  ASP A N   1 
ATOM   4989 C CA  . ASP E 1 62  ? -3.93100  43.81700 -46.88500 1.000 138.87153 ?  69  ASP A CA  1 
ATOM   4990 C C   . ASP E 1 62  ? -3.94000  45.30300 -47.23000 1.000 139.35337 ?  69  ASP A C   1 
ATOM   4991 O O   . ASP E 1 62  ? -3.04400  45.78400 -47.93500 1.000 138.86093 ?  69  ASP A O   1 
ATOM   4992 C CB  . ASP E 1 62  ? -4.77000  43.03900 -47.89300 1.000 142.74193 ?  69  ASP A CB  1 
ATOM   4993 C CG  . ASP E 1 62  ? -4.23600  41.65300 -48.14200 1.000 142.03772 ?  69  ASP A CG  1 
ATOM   4994 O OD1 . ASP E 1 62  ? -3.09800  41.38200 -47.70600 1.000 139.17583 ?  69  ASP A OD1 1 
ATOM   4995 O OD2 . ASP E 1 62  ? -4.94900  40.84400 -48.77700 1.000 144.93105 -1 69  ASP A OD2 1 
ATOM   4996 N N   . SER E 1 63  ? -4.95500  46.04200 -46.77300 1.000 139.60706 ?  70  SER A N   1 
ATOM   4997 C CA  . SER E 1 63  ? -5.03100  47.46600 -47.09800 1.000 139.81731 ?  70  SER A CA  1 
ATOM   4998 C C   . SER E 1 63  ? -3.88400  48.25700 -46.48200 1.000 136.41308 ?  70  SER A C   1 
ATOM   4999 O O   . SER E 1 63  ? -3.41300  49.23100 -47.07600 1.000 135.92802 ?  70  SER A O   1 
ATOM   5000 C CB  . SER E 1 63  ? -6.36400  48.04900 -46.63200 1.000 141.83463 ?  70  SER A CB  1 
ATOM   5001 O OG  . SER E 1 63  ? -6.29200  48.45800 -45.27800 1.000 138.96293 ?  70  SER A OG  1 
ATOM   5002 N N   . VAL E 1 64  ? -3.43500  47.85600 -45.29100 1.000 138.26265 ?  71  VAL A N   1 
ATOM   5003 C CA  . VAL E 1 64  ? -2.45500  48.60800 -44.52200 1.000 136.76559 ?  71  VAL A CA  1 
ATOM   5004 C C   . VAL E 1 64  ? -1.05200  48.02600 -44.60600 1.000 136.20466 ?  71  VAL A C   1 
ATOM   5005 O O   . VAL E 1 64  ? -0.13900  48.55800 -43.95900 1.000 135.82553 ?  71  VAL A O   1 
ATOM   5006 C CB  . VAL E 1 64  ? -2.89500  48.69000 -43.05000 1.000 136.00192 ?  71  VAL A CB  1 
ATOM   5007 C CG1 . VAL E 1 64  ? -4.21300  49.40700 -42.94600 1.000 136.71155 ?  71  VAL A CG1 1 
ATOM   5008 C CG2 . VAL E 1 64  ? -3.00600  47.29100 -42.46700 1.000 134.75832 ?  71  VAL A CG2 1 
ATOM   5009 N N   . LYS E 1 65  ? -0.85200  46.94900 -45.36400 1.000 141.03234 ?  72  LYS A N   1 
ATOM   5010 C CA  . LYS E 1 65  ? 0.44100   46.27700 -45.38200 1.000 141.00835 ?  72  LYS A CA  1 
ATOM   5011 C C   . LYS E 1 65  ? 1.53700   47.21900 -45.86700 1.000 140.65438 ?  72  LYS A C   1 
ATOM   5012 O O   . LYS E 1 65  ? 1.38800   47.89400 -46.89000 1.000 140.48411 ?  72  LYS A O   1 
ATOM   5013 C CB  . LYS E 1 65  ? 0.37200   45.03800 -46.27700 1.000 141.81461 ?  72  LYS A CB  1 
ATOM   5014 N N   . GLY E 1 66  ? 2.63400   47.27200 -45.12300 1.000 147.83989 ?  74  GLY A N   1 
ATOM   5015 C CA  . GLY E 1 66  ? 3.72000   48.20100 -45.44100 1.000 147.08116 ?  74  GLY A CA  1 
ATOM   5016 C C   . GLY E 1 66  ? 3.54100   49.61900 -44.94600 1.000 145.91391 ?  74  GLY A C   1 
ATOM   5017 O O   . GLY E 1 66  ? 4.46700   50.19800 -44.37000 1.000 145.11296 ?  74  GLY A O   1 
ATOM   5018 N N   . ARG E 1 67  ? 2.36300   50.20400 -45.16900 1.000 140.65210 ?  75  ARG A N   1 
ATOM   5019 C CA  . ARG E 1 67  ? 2.10700   51.55400 -44.68000 1.000 139.81156 ?  75  ARG A CA  1 
ATOM   5020 C C   . ARG E 1 67  ? 2.07100   51.60300 -43.15700 1.000 139.70971 ?  75  ARG A C   1 
ATOM   5021 O O   . ARG E 1 67  ? 2.58400   52.55200 -42.55200 1.000 138.21853 ?  75  ARG A O   1 
ATOM   5022 C CB  . ARG E 1 67  ? 0.81000   52.09600 -45.28400 1.000 140.20258 ?  75  ARG A CB  1 
ATOM   5023 C CG  . ARG E 1 67  ? 0.76700   52.00700 -46.80600 1.000 140.38333 ?  75  ARG A CG  1 
ATOM   5024 C CD  . ARG E 1 67  ? -0.42000  52.74800 -47.40800 1.000 141.05459 ?  75  ARG A CD  1 
ATOM   5025 N NE  . ARG E 1 67  ? -1.69700  52.32400 -46.84700 1.000 142.32377 ?  75  ARG A NE  1 
ATOM   5026 C CZ  . ARG E 1 67  ? -2.38700  53.00400 -45.94100 1.000 142.50924 ?  75  ARG A CZ  1 
ATOM   5027 N NH1 . ARG E 1 67  ? -1.94900  54.15400 -45.45600 1.000 141.64235 ?  75  ARG A NH1 1 
ATOM   5028 N NH2 . ARG E 1 67  ? -3.54700  52.51700 -45.51200 1.000 143.84790 ?  75  ARG A NH2 1 
ATOM   5029 N N   . PHE E 1 68  ? 1.46900   50.60500 -42.51800 1.000 141.35858 ?  76  PHE A N   1 
ATOM   5030 C CA  . PHE E 1 68  ? 1.29900   50.60800 -41.07200 1.000 144.96242 ?  76  PHE A CA  1 
ATOM   5031 C C   . PHE E 1 68  ? 2.26100   49.61800 -40.42400 1.000 145.79596 ?  76  PHE A C   1 
ATOM   5032 O O   . PHE E 1 68  ? 2.77600   48.70500 -41.07300 1.000 140.65712 ?  76  PHE A O   1 
ATOM   5033 C CB  . PHE E 1 68  ? -0.14700  50.27500 -40.67400 1.000 136.51394 ?  76  PHE A CB  1 
ATOM   5034 C CG  . PHE E 1 68  ? -1.16700  51.31100 -41.09500 1.000 134.96496 ?  76  PHE A CG  1 
ATOM   5035 C CD1 . PHE E 1 68  ? -0.85500  52.31500 -42.00100 1.000 140.90208 ?  76  PHE A CD1 1 
ATOM   5036 C CD2 . PHE E 1 68  ? -2.43800  51.28900 -40.55200 1.000 124.62950 ?  76  PHE A CD2 1 
ATOM   5037 C CE1 . PHE E 1 68  ? -1.79500  53.25400 -42.37400 1.000 138.79007 ?  76  PHE A CE1 1 
ATOM   5038 C CE2 . PHE E 1 68  ? -3.37800  52.22900 -40.91800 1.000 119.63376 ?  76  PHE A CE2 1 
ATOM   5039 C CZ  . PHE E 1 68  ? -3.05600  53.21200 -41.82900 1.000 126.49218 ?  76  PHE A CZ  1 
ATOM   5040 N N   . THR E 1 69  ? 2.49600   49.81000 -39.12400 1.000 130.78006 ?  77  THR A N   1 
ATOM   5041 C CA  . THR E 1 69  ? 3.34200   48.89800 -38.35800 1.000 131.78480 ?  77  THR A CA  1 
ATOM   5042 C C   . THR E 1 69  ? 2.85400   48.81400 -36.92000 1.000 135.10965 ?  77  THR A C   1 
ATOM   5043 O O   . THR E 1 69  ? 2.73600   49.83700 -36.24200 1.000 141.97035 ?  77  THR A O   1 
ATOM   5044 C CB  . THR E 1 69  ? 4.80600   49.33700 -38.38800 1.000 138.20530 ?  77  THR A CB  1 
ATOM   5045 O OG1 . THR E 1 69  ? 5.36600   49.05200 -39.67600 1.000 134.15470 ?  77  THR A OG1 1 
ATOM   5046 C CG2 . THR E 1 69  ? 5.59400   48.59900 -37.31300 1.000 140.22195 ?  77  THR A CG2 1 
ATOM   5047 N N   . ILE E 1 70  ? 2.60000   47.60000 -36.45300 1.000 132.37990 ?  78  ILE A N   1 
ATOM   5048 C CA  . ILE E 1 70  ? 2.20900   47.35100 -35.07200 1.000 134.93494 ?  78  ILE A CA  1 
ATOM   5049 C C   . ILE E 1 70  ? 3.45400   46.98500 -34.27400 1.000 141.45036 ?  78  ILE A C   1 
ATOM   5050 O O   . ILE E 1 70  ? 4.44500   46.48600 -34.81800 1.000 138.80466 ?  78  ILE A O   1 
ATOM   5051 C CB  . ILE E 1 70  ? 1.13100   46.24600 -34.99700 1.000 119.25104 ?  78  ILE A CB  1 
ATOM   5052 C CG1 . ILE E 1 70  ? 0.26200   46.41500 -33.74900 1.000 118.09560 ?  78  ILE A CG1 1 
ATOM   5053 C CG2 . ILE E 1 70  ? 1.76400   44.86300 -35.01600 1.000 112.53690 ?  78  ILE A CG2 1 
ATOM   5054 C CD1 . ILE E 1 70  ? -0.84000  45.39700 -33.64200 1.000 99.73239  ?  78  ILE A CD1 1 
ATOM   5055 N N   . SER E 1 71  ? 3.41300   47.25000 -32.97300 1.000 122.51323 ?  79  SER A N   1 
ATOM   5056 C CA  . SER E 1 71  ? 4.56600   47.01700 -32.11500 1.000 126.47773 ?  79  SER A CA  1 
ATOM   5057 C C   . SER E 1 71  ? 4.06900   46.95900 -30.67900 1.000 128.93609 ?  79  SER A C   1 
ATOM   5058 O O   . SER E 1 71  ? 2.92600   47.31100 -30.39000 1.000 127.35848 ?  79  SER A O   1 
ATOM   5059 C CB  . SER E 1 71  ? 5.62000   48.11500 -32.29100 1.000 131.45567 ?  79  SER A CB  1 
ATOM   5060 O OG  . SER E 1 71  ? 5.02500   49.39900 -32.21800 1.000 133.57915 ?  79  SER A OG  1 
ATOM   5061 N N   . ALA E 1 72  ? 4.95800   46.56600 -29.76700 1.000 126.46069 ?  80  ALA A N   1 
ATOM   5062 C CA  . ALA E 1 72  ? 4.57900   46.47900 -28.36400 1.000 128.54288 ?  80  ALA A CA  1 
ATOM   5063 C C   . ALA E 1 72  ? 5.81900   46.62100 -27.49600 1.000 132.19738 ?  80  ALA A C   1 
ATOM   5064 O O   . ALA E 1 72  ? 6.87800   46.08600 -27.82500 1.000 130.95157 ?  80  ALA A O   1 
ATOM   5065 C CB  . ALA E 1 72  ? 3.87400   45.15300 -28.05500 1.000 124.47698 ?  80  ALA A CB  1 
ATOM   5066 N N   . ASP E 1 73  ? 5.68200   47.36500 -26.40400 1.000 131.37050 ?  81  ASP A N   1 
ATOM   5067 C CA  . ASP E 1 73  ? 6.73000   47.50700 -25.40200 1.000 134.97095 ?  81  ASP A CA  1 
ATOM   5068 C C   . ASP E 1 73  ? 6.18600   46.89300 -24.11800 1.000 134.34065 ?  81  ASP A C   1 
ATOM   5069 O O   . ASP E 1 73  ? 5.16800   47.35400 -23.57900 1.000 132.97076 ?  81  ASP A O   1 
ATOM   5070 C CB  . ASP E 1 73  ? 7.16100   48.96600 -25.23300 1.000 138.27339 ?  81  ASP A CB  1 
ATOM   5071 C CG  . ASP E 1 73  ? 7.99100   49.19700 -23.98000 1.000 141.60683 ?  81  ASP A CG  1 
ATOM   5072 O OD1 . ASP E 1 73  ? 8.86200   48.35300 -23.68800 1.000 142.80567 ?  81  ASP A OD1 1 
ATOM   5073 O OD2 . ASP E 1 73  ? 7.81100   50.24500 -23.32100 1.000 145.85130 -1 81  ASP A OD2 1 
ATOM   5074 N N   . THR E 1 74  ? 6.82100   45.79300 -23.69900 1.000 140.18159 ?  82  THR A N   1 
ATOM   5075 C CA  . THR E 1 74  ? 6.35100   44.99900 -22.56800 1.000 139.35581 ?  82  THR A CA  1 
ATOM   5076 C C   . THR E 1 74  ? 6.35800   45.79700 -21.27000 1.000 142.50524 ?  82  THR A C   1 
ATOM   5077 O O   . THR E 1 74  ? 5.44500   45.66600 -20.44600 1.000 141.11331 ?  82  THR A O   1 
ATOM   5078 C CB  . THR E 1 74  ? 7.22000   43.74600 -22.41100 1.000 136.69133 ?  82  THR A CB  1 
ATOM   5079 O OG1 . THR E 1 74  ? 8.38100   44.06800 -21.63100 1.000 139.65856 ?  82  THR A OG1 1 
ATOM   5080 C CG2 . THR E 1 74  ? 7.66200   43.21800 -23.77100 1.000 131.83274 ?  82  THR A CG2 1 
ATOM   5081 N N   . SER E 1 75  ? 7.40200   46.60200 -21.06000 1.000 137.09465 ?  83  SER A N   1 
ATOM   5082 C CA  . SER E 1 75  ? 7.55800   47.31400 -19.79700 1.000 141.61227 ?  83  SER A CA  1 
ATOM   5083 C C   . SER E 1 75  ? 6.41900   48.29600 -19.57200 1.000 141.12732 ?  83  SER A C   1 
ATOM   5084 O O   . SER E 1 75  ? 5.89300   48.40400 -18.45800 1.000 142.14787 ?  83  SER A O   1 
ATOM   5085 C CB  . SER E 1 75  ? 8.89900   48.03800 -19.77800 1.000 149.71639 ?  83  SER A CB  1 
ATOM   5086 O OG  . SER E 1 75  ? 8.73900   49.39200 -20.15900 1.000 153.24334 ?  83  SER A OG  1 
ATOM   5087 N N   . LYS E 1 76  ? 6.01200   49.00900 -20.61500 1.000 147.68142 ?  84  LYS A N   1 
ATOM   5088 C CA  . LYS E 1 76  ? 4.91500   49.95000 -20.49000 1.000 143.40408 ?  84  LYS A CA  1 
ATOM   5089 C C   . LYS E 1 76  ? 3.57700   49.27500 -20.72500 1.000 137.96603 ?  84  LYS A C   1 
ATOM   5090 O O   . LYS E 1 76  ? 2.54100   49.94900 -20.70700 1.000 131.80180 ?  84  LYS A O   1 
ATOM   5091 C CB  . LYS E 1 76  ? 5.09400   51.11700 -21.46900 1.000 143.61714 ?  84  LYS A CB  1 
ATOM   5092 N N   . ASN E 1 77  ? 3.58400   47.95800 -20.93800 1.000 148.07020 ?  85  ASN A N   1 
ATOM   5093 C CA  . ASN E 1 77  ? 2.36400   47.18700 -21.14300 1.000 142.21267 ?  85  ASN A CA  1 
ATOM   5094 C C   . ASN E 1 77  ? 1.53800   47.81900 -22.25500 1.000 135.28138 ?  85  ASN A C   1 
ATOM   5095 O O   . ASN E 1 77  ? 0.31800   47.97000 -22.14400 1.000 124.98637 ?  85  ASN A O   1 
ATOM   5096 C CB  . ASN E 1 77  ? 1.56400   47.08100 -19.83900 1.000 136.79907 ?  85  ASN A CB  1 
ATOM   5097 C CG  . ASN E 1 77  ? 0.81600   45.76300 -19.70500 1.000 133.09848 ?  85  ASN A CG  1 
ATOM   5098 O OD1 . ASN E 1 77  ? 1.40900   44.68700 -19.77800 1.000 138.40841 ?  85  ASN A OD1 1 
ATOM   5099 N ND2 . ASN E 1 77  ? -0.48200  45.84600 -19.44300 1.000 122.05603 ?  85  ASN A ND2 1 
ATOM   5100 N N   . THR E 1 78  ? 2.21400   48.22400 -23.33300 1.000 134.87899 ?  86  THR A N   1 
ATOM   5101 C CA  . THR E 1 78  ? 1.55100   49.10300 -24.28900 1.000 128.91400 ?  86  THR A CA  1 
ATOM   5102 C C   . THR E 1 78  ? 1.93500   48.73600 -25.71400 1.000 132.26107 ?  86  THR A C   1 
ATOM   5103 O O   . THR E 1 78  ? 3.11500   48.56000 -26.01800 1.000 140.21277 ?  86  THR A O   1 
ATOM   5104 C CB  . THR E 1 78  ? 1.89700   50.57100 -23.99500 1.000 129.67176 ?  86  THR A CB  1 
ATOM   5105 O OG1 . THR E 1 78  ? 1.58500   50.86000 -22.62600 1.000 127.50642 ?  86  THR A OG1 1 
ATOM   5106 C CG2 . THR E 1 78  ? 1.11800   51.52200 -24.90400 1.000 123.24068 ?  86  THR A CG2 1 
ATOM   5107 N N   . ALA E 1 79  ? 0.93600   48.63400 -26.58200 1.000 127.21758 ?  87  ALA A N   1 
ATOM   5108 C CA  . ALA E 1 79  ? 1.13500   48.42400 -28.00500 1.000 129.42608 ?  87  ALA A CA  1 
ATOM   5109 C C   . ALA E 1 79  ? 0.99600   49.74900 -28.74400 1.000 127.40708 ?  87  ALA A C   1 
ATOM   5110 O O   . ALA E 1 79  ? 0.32000   50.67400 -28.28800 1.000 120.42823 ?  87  ALA A O   1 
ATOM   5111 C CB  . ALA E 1 79  ? 0.13100   47.40600 -28.54700 1.000 119.78565 ?  87  ALA A CB  1 
ATOM   5112 N N   . TYR E 1 80  ? 1.65100   49.83600 -29.89800 1.000 124.95975 ?  88  TYR A N   1 
ATOM   5113 C CA  . TYR E 1 80  ? 1.59800   51.03200 -30.72800 1.000 123.84572 ?  88  TYR A CA  1 
ATOM   5114 C C   . TYR E 1 80  ? 1.37200   50.67400 -32.18600 1.000 123.53653 ?  88  TYR A C   1 
ATOM   5115 O O   . TYR E 1 80  ? 1.97200   49.73400 -32.70900 1.000 127.68875 ?  88  TYR A O   1 
ATOM   5116 C CB  . TYR E 1 80  ? 2.87300   51.86800 -30.60500 1.000 131.03678 ?  88  TYR A CB  1 
ATOM   5117 C CG  . TYR E 1 80  ? 3.37500   52.02100 -29.19800 1.000 133.56463 ?  88  TYR A CG  1 
ATOM   5118 C CD1 . TYR E 1 80  ? 2.91400   53.05500 -28.40100 1.000 129.57016 ?  88  TYR A CD1 1 
ATOM   5119 C CD2 . TYR E 1 80  ? 4.32400   51.15800 -28.67600 1.000 139.09116 ?  88  TYR A CD2 1 
ATOM   5120 C CE1 . TYR E 1 80  ? 3.36500   53.21700 -27.11900 1.000 132.11244 ?  88  TYR A CE1 1 
ATOM   5121 C CE2 . TYR E 1 80  ? 4.78500   51.31200 -27.39000 1.000 141.24490 ?  88  TYR A CE2 1 
ATOM   5122 C CZ  . TYR E 1 80  ? 4.30300   52.34600 -26.61400 1.000 138.00620 ?  88  TYR A CZ  1 
ATOM   5123 O OH  . TYR E 1 80  ? 4.75700   52.51400 -25.32600 1.000 139.84776 ?  88  TYR A OH  1 
ATOM   5124 N N   . LEU E 1 81  ? 0.51400   51.44400 -32.83700 1.000 137.13152 ?  89  LEU A N   1 
ATOM   5125 C CA  . LEU E 1 81  ? 0.25800   51.30600 -34.26900 1.000 137.07714 ?  89  LEU A CA  1 
ATOM   5126 C C   . LEU E 1 81  ? 0.76200   52.56600 -34.96900 1.000 139.76261 ?  89  LEU A C   1 
ATOM   5127 O O   . LEU E 1 81  ? 0.08300   53.59400 -34.97500 1.000 133.57037 ?  89  LEU A O   1 
ATOM   5128 C CB  . LEU E 1 81  ? -1.22200  51.06400 -34.54200 1.000 122.44484 ?  89  LEU A CB  1 
ATOM   5129 C CG  . LEU E 1 81  ? -1.57100  50.87700 -36.02300 1.000 118.85659 ?  89  LEU A CG  1 
ATOM   5130 C CD1 . LEU E 1 81  ? -0.51100  50.06100 -36.75900 1.000 126.28712 ?  89  LEU A CD1 1 
ATOM   5131 C CD2 . LEU E 1 81  ? -2.93800  50.24600 -36.18800 1.000 98.51118  ?  89  LEU A CD2 1 
ATOM   5132 N N   . GLN E 1 82  ? 1.97000   52.48700 -35.52500 1.000 137.83990 ?  90  GLN A N   1 
ATOM   5133 C CA  . GLN E 1 82  ? 2.59400   53.58500 -36.26100 1.000 139.32875 ?  90  GLN A CA  1 
ATOM   5134 C C   . GLN E 1 82  ? 2.14600   53.48000 -37.71900 1.000 136.43999 ?  90  GLN A C   1 
ATOM   5135 O O   . GLN E 1 82  ? 2.61600   52.61800 -38.46400 1.000 136.50820 ?  90  GLN A O   1 
ATOM   5136 C CB  . GLN E 1 82  ? 4.11200   53.49100 -36.11500 1.000 145.06942 ?  90  GLN A CB  1 
ATOM   5137 C CG  . GLN E 1 82  ? 4.98300   54.48600 -36.88100 1.000 146.80654 ?  90  GLN A CG  1 
ATOM   5138 C CD  . GLN E 1 82  ? 4.53900   55.93300 -36.74300 1.000 144.83116 ?  90  GLN A CD  1 
ATOM   5139 O OE1 . GLN E 1 82  ? 3.92700   56.50700 -37.64800 1.000 141.23342 ?  90  GLN A OE1 1 
ATOM   5140 N NE2 . GLN E 1 82  ? 4.84400   56.52800 -35.59700 1.000 146.39315 ?  90  GLN A NE2 1 
ATOM   5141 N N   . MET E 1 83  ? 1.22700   54.35800 -38.12200 1.000 151.60637 ?  91  MET A N   1 
ATOM   5142 C CA  . MET E 1 83  ? 0.76700   54.47900 -39.50100 1.000 148.50270 ?  91  MET A CA  1 
ATOM   5143 C C   . MET E 1 83  ? 1.57800   55.57000 -40.19700 1.000 150.05561 ?  91  MET A C   1 
ATOM   5144 O O   . MET E 1 83  ? 1.68800   56.67800 -39.67200 1.000 149.74405 ?  91  MET A O   1 
ATOM   5145 C CB  . MET E 1 83  ? -0.72400  54.81700 -39.48700 1.000 140.34904 ?  91  MET A CB  1 
ATOM   5146 C CG  . MET E 1 83  ? -1.48300  53.99600 -38.44500 1.000 135.66882 ?  91  MET A CG  1 
ATOM   5147 S SD  . MET E 1 83  ? -3.09300  54.64000 -37.93700 1.000 119.47947 ?  91  MET A SD  1 
ATOM   5148 C CE  . MET E 1 83  ? -2.73600  56.36400 -37.60600 1.000 120.76334 ?  91  MET A CE  1 
ATOM   5149 N N   . ASN E 1 84  ? 2.13200   55.28500 -41.38100 1.000 142.17613 ?  92  ASN A N   1 
ATOM   5150 C CA  . ASN E 1 84  ? 3.12200   56.22300 -41.91500 1.000 148.64148 ?  92  ASN A CA  1 
ATOM   5151 C C   . ASN E 1 84  ? 2.80800   56.90800 -43.24200 1.000 156.24762 ?  92  ASN A C   1 
ATOM   5152 O O   . ASN E 1 84  ? 3.32600   58.00500 -43.45900 1.000 160.09360 ?  92  ASN A O   1 
ATOM   5153 C CB  . ASN E 1 84  ? 4.48900   55.54600 -42.01500 1.000 151.89525 ?  92  ASN A CB  1 
ATOM   5154 C CG  . ASN E 1 84  ? 4.90800   54.92600 -40.70700 1.000 146.21229 ?  92  ASN A CG  1 
ATOM   5155 O OD1 . ASN E 1 84  ? 5.58300   55.57000 -39.90500 1.000 145.57691 ?  92  ASN A OD1 1 
ATOM   5156 N ND2 . ASN E 1 84  ? 4.50400   53.67800 -40.47200 1.000 142.40910 ?  92  ASN A ND2 1 
ATOM   5157 N N   . SER E 1 85  ? 2.01300   56.32600 -44.14400 1.000 143.07558 ?  93  SER A N   1 
ATOM   5158 C CA  . SER E 1 85  ? 1.67000   57.01700 -45.39600 1.000 151.83163 ?  93  SER A CA  1 
ATOM   5159 C C   . SER E 1 85  ? 0.14600   57.00200 -45.52000 1.000 149.52486 ?  93  SER A C   1 
ATOM   5160 O O   . SER E 1 85  ? -0.44500  56.32500 -46.36400 1.000 150.58670 ?  93  SER A O   1 
ATOM   5161 C CB  . SER E 1 85  ? 2.36100   56.39000 -46.62100 1.000 160.09474 ?  93  SER A CB  1 
ATOM   5162 O OG  . SER E 1 85  ? 2.26700   54.97500 -46.63500 1.000 155.48220 ?  93  SER A OG  1 
ATOM   5163 N N   . LEU E 1 86  ? -0.47900  57.80600 -44.66800 1.000 152.81082 ?  94  LEU A N   1 
ATOM   5164 C CA  . LEU E 1 86  ? -1.92500  57.82700 -44.51900 1.000 150.66250 ?  94  LEU A CA  1 
ATOM   5165 C C   . LEU E 1 86  ? -2.58000  58.42400 -45.75700 1.000 158.03685 ?  94  LEU A C   1 
ATOM   5166 O O   . LEU E 1 86  ? -2.26700  59.55200 -46.14600 1.000 162.71643 ?  94  LEU A O   1 
ATOM   5167 C CB  . LEU E 1 86  ? -2.29400  58.61900 -43.27100 1.000 145.11039 ?  94  LEU A CB  1 
ATOM   5168 C CG  . LEU E 1 86  ? -2.07800  57.81600 -41.98800 1.000 136.72224 ?  94  LEU A CG  1 
ATOM   5169 C CD1 . LEU E 1 86  ? -1.84900  58.74900 -40.81000 1.000 132.34576 ?  94  LEU A CD1 1 
ATOM   5170 C CD2 . LEU E 1 86  ? -3.23600  56.86200 -41.72100 1.000 133.81792 ?  94  LEU A CD2 1 
ATOM   5171 N N   . ARG E 1 87  ? -3.46900  57.66800 -46.38900 1.000 152.96407 ?  95  ARG A N   1 
ATOM   5172 C CA  . ARG E 1 87  ? -4.27600  58.19900 -47.47600 1.000 154.18131 ?  95  ARG A CA  1 
ATOM   5173 C C   . ARG E 1 87  ? -5.68300  58.49600 -46.96000 1.000 152.95663 ?  95  ARG A C   1 
ATOM   5174 O O   . ARG E 1 87  ? -6.06600  58.08300 -45.86400 1.000 151.20136 ?  95  ARG A O   1 
ATOM   5175 C CB  . ARG E 1 87  ? -4.30200  57.22300 -48.65900 1.000 153.75878 ?  95  ARG A CB  1 
ATOM   5176 C CG  . ARG E 1 87  ? -4.47600  57.88800 -50.03400 1.000 154.85384 ?  95  ARG A CG  1 
ATOM   5177 C CD  . ARG E 1 87  ? -3.47100  59.01500 -50.29100 1.000 155.52614 ?  95  ARG A CD  1 
ATOM   5178 N NE  . ARG E 1 87  ? -2.17400  58.78100 -49.67200 1.000 157.54036 ?  95  ARG A NE  1 
ATOM   5179 C CZ  . ARG E 1 87  ? -1.19400  58.08300 -50.22600 1.000 158.51915 ?  95  ARG A CZ  1 
ATOM   5180 N NH1 . ARG E 1 87  ? -1.30300  57.58500 -51.44800 1.000 157.60123 ?  95  ARG A NH1 1 
ATOM   5181 N NH2 . ARG E 1 87  ? -0.07000  57.88900 -49.54400 1.000 161.09747 ?  95  ARG A NH2 1 
ATOM   5182 N N   . ALA E 1 88  ? -6.45200  59.22600 -47.77100 1.000 151.90842 ?  96  ALA A N   1 
ATOM   5183 C CA  . ALA E 1 88  ? -7.75300  59.73600 -47.33600 1.000 150.92629 ?  96  ALA A CA  1 
ATOM   5184 C C   . ALA E 1 88  ? -8.64500  58.63200 -46.77900 1.000 151.31694 ?  96  ALA A C   1 
ATOM   5185 O O   . ALA E 1 88  ? -9.20700  58.76100 -45.68500 1.000 150.46055 ?  96  ALA A O   1 
ATOM   5186 C CB  . ALA E 1 88  ? -8.44500  60.44900 -48.49800 1.000 149.93647 ?  96  ALA A CB  1 
ATOM   5187 N N   . GLU E 1 89  ? -8.78800  57.53900 -47.53100 1.000 153.91840 ?  97  GLU A N   1 
ATOM   5188 C CA  . GLU E 1 89  ? -9.67500  56.44100 -47.15400 1.000 155.53251 ?  97  GLU A CA  1 
ATOM   5189 C C   . GLU E 1 89  ? -9.37800  55.88100 -45.76300 1.000 152.82366 ?  97  GLU A C   1 
ATOM   5190 O O   . GLU E 1 89  ? -10.28000 55.34200 -45.11100 1.000 153.56334 ?  97  GLU A O   1 
ATOM   5191 C CB  . GLU E 1 89  ? -9.59200  55.32500 -48.20700 1.000 157.87125 ?  97  GLU A CB  1 
ATOM   5192 C CG  . GLU E 1 89  ? -9.50700  55.80400 -49.67100 1.000 159.25961 ?  97  GLU A CG  1 
ATOM   5193 C CD  . GLU E 1 89  ? -8.15600  56.41300 -50.04800 1.000 156.78276 ?  97  GLU A CD  1 
ATOM   5194 O OE1 . GLU E 1 89  ? -7.21400  56.31000 -49.23400 1.000 154.75583 ?  97  GLU A OE1 1 
ATOM   5195 O OE2 . GLU E 1 89  ? -8.04900  57.01200 -51.14200 1.000 156.41702 -1 97  GLU A OE2 1 
ATOM   5196 N N   . ASP E 1 90  ? -8.13200  56.00000 -45.29000 1.000 155.20571 ?  98  ASP A N   1 
ATOM   5197 C CA  . ASP E 1 90  ? -7.76300  55.49100 -43.96700 1.000 149.44723 ?  98  ASP A CA  1 
ATOM   5198 C C   . ASP E 1 90  ? -8.49600  56.19000 -42.82500 1.000 147.82416 ?  98  ASP A C   1 
ATOM   5199 O O   . ASP E 1 90  ? -8.48700  55.67600 -41.70100 1.000 142.23278 ?  98  ASP A O   1 
ATOM   5200 C CB  . ASP E 1 90  ? -6.25200  55.61500 -43.74600 1.000 145.58812 ?  98  ASP A CB  1 
ATOM   5201 C CG  . ASP E 1 90  ? -5.44600  54.75300 -44.70100 1.000 146.09492 ?  98  ASP A CG  1 
ATOM   5202 O OD1 . ASP E 1 90  ? -6.06000  54.06600 -45.54600 1.000 148.41228 ?  98  ASP A OD1 1 
ATOM   5203 O OD2 . ASP E 1 90  ? -4.19900  54.74200 -44.58700 1.000 144.27709 -1 98  ASP A OD2 1 
ATOM   5204 N N   . THR E 1 91  ? -9.08900  57.35800 -43.07500 1.000 143.97340 ?  99  THR A N   1 
ATOM   5205 C CA  . THR E 1 91  ? -9.85300  58.07000 -42.05400 1.000 142.07175 ?  99  THR A CA  1 
ATOM   5206 C C   . THR E 1 91  ? -10.85700 57.14000 -41.38600 1.000 141.53416 ?  99  THR A C   1 
ATOM   5207 O O   . THR E 1 91  ? -11.67400 56.49800 -42.05500 1.000 146.45352 ?  99  THR A O   1 
ATOM   5208 C CB  . THR E 1 91  ? -10.54600 59.29500 -42.67700 1.000 145.72410 ?  99  THR A CB  1 
ATOM   5209 O OG1 . THR E 1 91  ? -11.13500 60.10300 -41.64800 1.000 144.04325 ?  99  THR A OG1 1 
ATOM   5210 C CG2 . THR E 1 91  ? -11.60700 58.90900 -43.71400 1.000 147.90129 ?  99  THR A CG2 1 
ATOM   5211 N N   . ALA E 1 92  ? -10.75400 57.03000 -40.06500 1.000 139.12432 ?  100 ALA A N   1 
ATOM   5212 C CA  . ALA E 1 92  ? -11.57900 56.10300 -39.30100 1.000 138.78112 ?  100 ALA A CA  1 
ATOM   5213 C C   . ALA E 1 92  ? -11.29800 56.30700 -37.82000 1.000 132.07043 ?  100 ALA A C   1 
ATOM   5214 O O   . ALA E 1 92  ? -10.32800 56.96400 -37.43400 1.000 127.52397 ?  100 ALA A O   1 
ATOM   5215 C CB  . ALA E 1 92  ? -11.30100 54.65200 -39.70400 1.000 139.33383 ?  100 ALA A CB  1 
ATOM   5216 N N   . VAL E 1 93  ? -12.16700 55.74100 -36.99500 1.000 132.28486 ?  101 VAL A N   1 
ATOM   5217 C CA  . VAL E 1 93  ? -11.89500 55.58200 -35.57200 1.000 126.68933 ?  101 VAL A CA  1 
ATOM   5218 C C   . VAL E 1 93  ? -11.25300 54.21700 -35.33900 1.000 124.16188 ?  101 VAL A C   1 
ATOM   5219 O O   . VAL E 1 93  ? -11.72400 53.19800 -35.85000 1.000 127.76273 ?  101 VAL A O   1 
ATOM   5220 C CB  . VAL E 1 93  ? -13.17700 55.76400 -34.74300 1.000 128.58907 ?  101 VAL A CB  1 
ATOM   5221 C CG1 . VAL E 1 93  ? -14.24200 54.75400 -35.14600 1.000 134.42461 ?  101 VAL A CG1 1 
ATOM   5222 C CG2 . VAL E 1 93  ? -12.85600 55.63600 -33.27100 1.000 123.85994 ?  101 VAL A CG2 1 
ATOM   5223 N N   . TYR E 1 94  ? -10.16500 54.18800 -34.58300 1.000 127.33854 ?  102 TYR A N   1 
ATOM   5224 C CA  . TYR E 1 94  ? -9.36600  52.98100 -34.40800 1.000 124.35821 ?  102 TYR A CA  1 
ATOM   5225 C C   . TYR E 1 94  ? -9.52600  52.47700 -32.97700 1.000 122.69015 ?  102 TYR A C   1 
ATOM   5226 O O   . TYR E 1 94  ? -9.34900  53.24200 -32.02000 1.000 120.88989 ?  102 TYR A O   1 
ATOM   5227 C CB  . TYR E 1 94  ? -7.90100  53.26600 -34.75100 1.000 120.51586 ?  102 TYR A CB  1 
ATOM   5228 C CG  . TYR E 1 94  ? -7.66700  53.43200 -36.24800 1.000 123.16798 ?  102 TYR A CG  1 
ATOM   5229 C CD1 . TYR E 1 94  ? -8.17300  54.53200 -36.92800 1.000 127.20370 ?  102 TYR A CD1 1 
ATOM   5230 C CD2 . TYR E 1 94  ? -6.94500  52.49400 -36.98000 1.000 122.24307 ?  102 TYR A CD2 1 
ATOM   5231 C CE1 . TYR E 1 94  ? -7.97500  54.69400 -38.29000 1.000 131.12827 ?  102 TYR A CE1 1 
ATOM   5232 C CE2 . TYR E 1 94  ? -6.73600  52.65400 -38.35700 1.000 125.52802 ?  102 TYR A CE2 1 
ATOM   5233 C CZ  . TYR E 1 94  ? -7.25900  53.75600 -39.00200 1.000 130.38881 ?  102 TYR A CZ  1 
ATOM   5234 O OH  . TYR E 1 94  ? -7.06800  53.93400 -40.35600 1.000 134.77446 ?  102 TYR A OH  1 
ATOM   5235 N N   . TYR E 1 95  ? -9.93000  51.21500 -32.84200 1.000 120.08369 ?  103 TYR A N   1 
ATOM   5236 C CA  . TYR E 1 95  ? -10.09100 50.54100 -31.56500 1.000 119.90466 ?  103 TYR A CA  1 
ATOM   5237 C C   . TYR E 1 95  ? -9.01200  49.47300 -31.41600 1.000 116.94390 ?  103 TYR A C   1 
ATOM   5238 O O   . TYR E 1 95  ? -8.60200  48.84200 -32.39800 1.000 115.96945 ?  103 TYR A O   1 
ATOM   5239 C CB  . TYR E 1 95  ? -11.47700 49.89200 -31.44100 1.000 125.06810 ?  103 TYR A CB  1 
ATOM   5240 C CG  . TYR E 1 95  ? -12.66600 50.80800 -31.68400 1.000 129.03991 ?  103 TYR A CG  1 
ATOM   5241 C CD1 . TYR E 1 95  ? -13.10900 51.08800 -32.97300 1.000 132.61649 ?  103 TYR A CD1 1 
ATOM   5242 C CD2 . TYR E 1 95  ? -13.35600 51.37600 -30.62200 1.000 129.70248 ?  103 TYR A CD2 1 
ATOM   5243 C CE1 . TYR E 1 95  ? -14.20200 51.91700 -33.19400 1.000 136.78194 ?  103 TYR A CE1 1 
ATOM   5244 C CE2 . TYR E 1 95  ? -14.44400 52.20500 -30.83500 1.000 132.75197 ?  103 TYR A CE2 1 
ATOM   5245 C CZ  . TYR E 1 95  ? -14.86200 52.47300 -32.12100 1.000 136.24525 ?  103 TYR A CZ  1 
ATOM   5246 O OH  . TYR E 1 95  ? -15.94500 53.29800 -32.32400 1.000 139.40966 ?  103 TYR A OH  1 
ATOM   5247 N N   . CYS E 1 96  ? -8.56900  49.25700 -30.17800 1.000 121.91744 ?  104 CYS A N   1 
ATOM   5248 C CA  . CYS E 1 96  ? -7.63600  48.18700 -29.85800 1.000 120.58192 ?  104 CYS A CA  1 
ATOM   5249 C C   . CYS E 1 96  ? -8.28600  47.20600 -28.89000 1.000 124.00579 ?  104 CYS A C   1 
ATOM   5250 O O   . CYS E 1 96  ? -9.15600  47.57600 -28.09600 1.000 126.83133 ?  104 CYS A O   1 
ATOM   5251 C CB  . CYS E 1 96  ? -6.33600  48.72800 -29.25600 1.000 118.48804 ?  104 CYS A CB  1 
ATOM   5252 S SG  . CYS E 1 96  ? -6.46900  49.35600 -27.55800 1.000 121.12079 ?  104 CYS A SG  1 
ATOM   5253 N N   . ALA E 1 97  ? -7.88100  45.94000 -28.98000 1.000 114.45131 ?  105 ALA A N   1 
ATOM   5254 C CA  . ALA E 1 97  ? -8.53200  44.89100 -28.20500 1.000 118.01206 ?  105 ALA A CA  1 
ATOM   5255 C C   . ALA E 1 97  ? -7.53100  43.80200 -27.84700 1.000 117.66303 ?  105 ALA A C   1 
ATOM   5256 O O   . ALA E 1 97  ? -6.46300  43.68700 -28.45000 1.000 114.59011 ?  105 ALA A O   1 
ATOM   5257 C CB  . ALA E 1 97  ? -9.71700  44.28700 -28.96800 1.000 119.93088 ?  105 ALA A CB  1 
ATOM   5258 N N   . ARG E 1 98  ? -7.90500  42.99100 -26.85500 1.000 109.67533 ?  106 ARG A N   1 
ATOM   5259 C CA  . ARG E 1 98  ? -7.13500  41.84300 -26.39600 1.000 110.58547 ?  106 ARG A CA  1 
ATOM   5260 C C   . ARG E 1 98  ? -7.78100  40.57500 -26.93300 1.000 110.32714 ?  106 ARG A C   1 
ATOM   5261 O O   . ARG E 1 98  ? -9.00700  40.47500 -26.97300 1.000 112.11107 ?  106 ARG A O   1 
ATOM   5262 C CB  . ARG E 1 98  ? -7.07200  41.78800 -24.86300 1.000 115.19925 ?  106 ARG A CB  1 
ATOM   5263 C CG  . ARG E 1 98  ? -6.73800  40.40600 -24.29900 1.000 117.68793 ?  106 ARG A CG  1 
ATOM   5264 C CD  . ARG E 1 98  ? -6.59600  40.43400 -22.78600 1.000 123.81756 ?  106 ARG A CD  1 
ATOM   5265 N NE  . ARG E 1 98  ? -7.83600  40.18900 -22.05500 1.000 126.08345 ?  106 ARG A NE  1 
ATOM   5266 C CZ  . ARG E 1 98  ? -7.90100  39.52200 -20.91100 1.000 130.56648 ?  106 ARG A CZ  1 
ATOM   5267 N NH1 . ARG E 1 98  ? -6.81300  39.05400 -20.32000 1.000 134.40806 ?  106 ARG A NH1 1 
ATOM   5268 N NH2 . ARG E 1 98  ? -9.08400  39.33100 -20.33700 1.000 131.50977 ?  106 ARG A NH2 1 
ATOM   5269 N N   . HIS E 1 99  ? -6.96400  39.60600 -27.34700 1.000 123.19072 ?  107 HIS A N   1 
ATOM   5270 C CA  . HIS E 1 99  ? -7.45400  38.29000 -27.76800 1.000 122.45689 ?  107 HIS A CA  1 
ATOM   5271 C C   . HIS E 1 99  ? -6.92700  37.25000 -26.78000 1.000 125.03275 ?  107 HIS A C   1 
ATOM   5272 O O   . HIS E 1 99  ? -5.76100  36.84800 -26.84900 1.000 124.25422 ?  107 HIS A O   1 
ATOM   5273 C CB  . HIS E 1 99  ? -7.03100  37.97100 -29.20200 1.000 117.64296 ?  107 HIS A CB  1 
ATOM   5274 C CG  . HIS E 1 99  ? -7.17500  36.52500 -29.57600 1.000 116.65004 ?  107 HIS A CG  1 
ATOM   5275 N ND1 . HIS E 1 99  ? -6.33000  35.90100 -30.47100 1.000 113.08287 ?  107 HIS A ND1 1 
ATOM   5276 C CD2 . HIS E 1 99  ? -8.06100  35.58200 -29.17700 1.000 118.90220 ?  107 HIS A CD2 1 
ATOM   5277 C CE1 . HIS E 1 99  ? -6.69000  34.63700 -30.60500 1.000 113.04426 ?  107 HIS A CE1 1 
ATOM   5278 N NE2 . HIS E 1 99  ? -7.73700  34.41700 -29.83000 1.000 116.41487 ?  107 HIS A NE2 1 
ATOM   5279 N N   . ALA E 1 100 ? -7.79100  36.80200 -25.87200 1.000 122.98930 ?  108 ALA A N   1 
ATOM   5280 C CA  . ALA E 1 100 ? -7.43900  35.79700 -24.87800 1.000 125.84798 ?  108 ALA A CA  1 
ATOM   5281 C C   . ALA E 1 100 ? -7.98100  34.42900 -25.27800 1.000 124.12482 ?  108 ALA A C   1 
ATOM   5282 O O   . ALA E 1 100 ? -9.05400  34.32700 -25.87900 1.000 123.17531 ?  108 ALA A O   1 
ATOM   5283 C CB  . ALA E 1 100 ? -7.96100  36.19200 -23.49700 1.000 130.77137 ?  108 ALA A CB  1 
ATOM   5284 N N   . TRP E 1 101 ? -7.21600  33.37600 -24.96400 1.000 130.03599 ?  109 TRP A N   1 
ATOM   5285 C CA  . TRP E 1 101 ? -7.62200  32.02800 -25.35500 1.000 128.11129 ?  109 TRP A CA  1 
ATOM   5286 C C   . TRP E 1 101 ? -8.77600  31.49300 -24.51800 1.000 130.66509 ?  109 TRP A C   1 
ATOM   5287 O O   . TRP E 1 101 ? -9.54900  30.66600 -25.01200 1.000 129.37359 ?  109 TRP A O   1 
ATOM   5288 C CB  . TRP E 1 101 ? -6.43200  31.06600 -25.30400 1.000 127.60193 ?  109 TRP A CB  1 
ATOM   5289 C CG  . TRP E 1 101 ? -5.40600  31.36900 -26.35900 1.000 124.53371 ?  109 TRP A CG  1 
ATOM   5290 C CD1 . TRP E 1 101 ? -4.11600  31.75500 -26.16700 1.000 126.24540 ?  109 TRP A CD1 1 
ATOM   5291 C CD2 . TRP E 1 101 ? -5.60400  31.32800 -27.77900 1.000 119.99047 ?  109 TRP A CD2 1 
ATOM   5292 N NE1 . TRP E 1 101 ? -3.49400  31.95100 -27.37700 1.000 122.54559 ?  109 TRP A NE1 1 
ATOM   5293 C CE2 . TRP E 1 101 ? -4.38700  31.69400 -28.38200 1.000 118.48310 ?  109 TRP A CE2 1 
ATOM   5294 C CE3 . TRP E 1 101 ? -6.69200  31.01800 -28.59700 1.000 117.94305 ?  109 TRP A CE3 1 
ATOM   5295 C CZ2 . TRP E 1 101 ? -4.22900  31.75400 -29.76600 1.000 114.44098 ?  109 TRP A CZ2 1 
ATOM   5296 C CZ3 . TRP E 1 101 ? -6.53200  31.07900 -29.96700 1.000 114.39099 ?  109 TRP A CZ3 1 
ATOM   5297 C CH2 . TRP E 1 101 ? -5.31200  31.44300 -30.53700 1.000 112.39836 ?  109 TRP A CH2 1 
ATOM   5298 N N   . TYR E 1 102 ? -8.91900  31.93200 -23.26300 1.000 126.89038 ?  110 TYR A N   1 
ATOM   5299 C CA  . TYR E 1 102 ? -10.06100 31.46500 -22.47900 1.000 128.72911 ?  110 TYR A CA  1 
ATOM   5300 C C   . TYR E 1 102 ? -11.37500 31.84700 -23.14600 1.000 128.41439 ?  110 TYR A C   1 
ATOM   5301 O O   . TYR E 1 102 ? -12.38700 31.16400 -22.96300 1.000 129.20694 ?  110 TYR A O   1 
ATOM   5302 C CB  . TYR E 1 102 ? -10.01000 32.00600 -21.04500 1.000 132.44360 ?  110 TYR A CB  1 
ATOM   5303 C CG  . TYR E 1 102 ? -11.24300 31.65700 -20.22300 1.000 133.61772 ?  110 TYR A CG  1 
ATOM   5304 C CD1 . TYR E 1 102 ? -11.40000 30.39300 -19.66700 1.000 133.36381 ?  110 TYR A CD1 1 
ATOM   5305 C CD2 . TYR E 1 102 ? -12.24800 32.59600 -19.99800 1.000 134.74668 ?  110 TYR A CD2 1 
ATOM   5306 C CE1 . TYR E 1 102 ? -12.52200 30.06600 -18.92100 1.000 133.97616 ?  110 TYR A CE1 1 
ATOM   5307 C CE2 . TYR E 1 102 ? -13.37300 32.27800 -19.25100 1.000 135.49194 ?  110 TYR A CE2 1 
ATOM   5308 C CZ  . TYR E 1 102 ? -13.50200 31.01000 -18.71500 1.000 135.00389 ?  110 TYR A CZ  1 
ATOM   5309 O OH  . TYR E 1 102 ? -14.61600 30.68900 -17.97100 1.000 135.37334 ?  110 TYR A OH  1 
ATOM   5310 N N   . TYR E 1 103 ? -11.37800 32.93600 -23.91200 1.000 124.56308 ?  111 TYR A N   1 
ATOM   5311 C CA  . TYR E 1 103 ? -12.52200 33.32800 -24.71700 1.000 125.01703 ?  111 TYR A CA  1 
ATOM   5312 C C   . TYR E 1 103 ? -12.34500 32.97200 -26.19200 1.000 122.31710 ?  111 TYR A C   1 
ATOM   5313 O O   . TYR E 1 103 ? -13.05100 33.52000 -27.04400 1.000 123.14478 ?  111 TYR A O   1 
ATOM   5314 C CB  . TYR E 1 103 ? -12.80800 34.81700 -24.52500 1.000 126.56913 ?  111 TYR A CB  1 
ATOM   5315 C CG  . TYR E 1 103 ? -13.08200 35.17000 -23.08000 1.000 129.11039 ?  111 TYR A CG  1 
ATOM   5316 C CD1 . TYR E 1 103 ? -14.24200 34.73400 -22.45200 1.000 130.93090 ?  111 TYR A CD1 1 
ATOM   5317 C CD2 . TYR E 1 103 ? -12.17800 35.92200 -22.34000 1.000 129.80351 ?  111 TYR A CD2 1 
ATOM   5318 C CE1 . TYR E 1 103 ? -14.50400 35.04700 -21.13000 1.000 132.52168 ?  111 TYR A CE1 1 
ATOM   5319 C CE2 . TYR E 1 103 ? -12.43200 36.24200 -21.01800 1.000 132.41652 ?  111 TYR A CE2 1 
ATOM   5320 C CZ  . TYR E 1 103 ? -13.59400 35.79900 -20.41800 1.000 133.32359 ?  111 TYR A CZ  1 
ATOM   5321 O OH  . TYR E 1 103 ? -13.85400 36.10900 -19.10100 1.000 135.32718 ?  111 TYR A OH  1 
ATOM   5322 N N   . GLY E 1 104 ? -11.39000 32.09900 -26.51000 1.000 126.65548 ?  112 GLY A N   1 
ATOM   5323 C CA  . GLY E 1 104 ? -11.23000 31.59600 -27.86500 1.000 124.06701 ?  112 GLY A CA  1 
ATOM   5324 C C   . GLY E 1 104 ? -10.73100 32.63400 -28.85600 1.000 121.46522 ?  112 GLY A C   1 
ATOM   5325 O O   . GLY E 1 104 ? -10.07600 33.61300 -28.50200 1.000 120.66245 ?  112 GLY A O   1 
ATOM   5326 N N   . TRP E 1 105 ? -11.04500 32.38700 -30.13200 1.000 136.16498 ?  113 TRP A N   1 
ATOM   5327 C CA  . TRP E 1 105 ? -10.75200 33.35100 -31.18400 1.000 134.11477 ?  113 TRP A CA  1 
ATOM   5328 C C   . TRP E 1 105 ? -11.71600 34.51400 -31.04400 1.000 138.08712 ?  113 TRP A C   1 
ATOM   5329 O O   . TRP E 1 105 ? -12.81000 34.48900 -31.61800 1.000 141.02079 ?  113 TRP A O   1 
ATOM   5330 C CB  . TRP E 1 105 ? -10.91400 32.74300 -32.57500 1.000 131.92497 ?  113 TRP A CB  1 
ATOM   5331 C CG  . TRP E 1 105 ? -9.89000  31.73600 -32.96100 1.000 128.16848 ?  113 TRP A CG  1 
ATOM   5332 C CD1 . TRP E 1 105 ? -10.00300 30.37700 -32.87900 1.000 128.34858 ?  113 TRP A CD1 1 
ATOM   5333 C CD2 . TRP E 1 105 ? -8.58800  32.00300 -33.48000 1.000 124.59384 ?  113 TRP A CD2 1 
ATOM   5334 N NE1 . TRP E 1 105 ? -8.85400  29.78200 -33.33600 1.000 125.40846 ?  113 TRP A NE1 1 
ATOM   5335 C CE2 . TRP E 1 105 ? -7.96600  30.76000 -33.70500 1.000 123.27100 ?  113 TRP A CE2 1 
ATOM   5336 C CE3 . TRP E 1 105 ? -7.88800  33.17300 -33.77800 1.000 122.80874 ?  113 TRP A CE3 1 
ATOM   5337 C CZ2 . TRP E 1 105 ? -6.67200  30.65600 -34.21700 1.000 120.90822 ?  113 TRP A CZ2 1 
ATOM   5338 C CZ3 . TRP E 1 105 ? -6.60400  33.07300 -34.28600 1.000 120.08049 ?  113 TRP A CZ3 1 
ATOM   5339 C CH2 . TRP E 1 105 ? -6.01000  31.82300 -34.50100 1.000 119.49773 ?  113 TRP A CH2 1 
ATOM   5340 N N   . GLY E 1 106 ? -11.31200 35.54100 -30.31200 1.000 115.92982 ?  114 GLY A N   1 
ATOM   5341 C CA  . GLY E 1 106 ? -12.22600 36.59900 -29.95700 1.000 120.13570 ?  114 GLY A CA  1 
ATOM   5342 C C   . GLY E 1 106 ? -11.55400 37.72600 -29.20600 1.000 119.60735 ?  114 GLY A C   1 
ATOM   5343 O O   . GLY E 1 106 ? -10.54500 37.53300 -28.51700 1.000 117.83890 ?  114 GLY A O   1 
ATOM   5344 N N   . LEU E 1 107 ? -12.12600 38.91300 -29.34100 1.000 102.34699 ?  115 LEU A N   1 
ATOM   5345 C CA  . LEU E 1 107 ? -11.57200 40.14100 -28.79100 1.000 112.29791 ?  115 LEU A CA  1 
ATOM   5346 C C   . LEU E 1 107 ? -12.38900 40.53400 -27.56500 1.000 120.51937 ?  115 LEU A C   1 
ATOM   5347 O O   . LEU E 1 107 ? -13.47800 41.10300 -27.69100 1.000 122.46020 ?  115 LEU A O   1 
ATOM   5348 C CB  . LEU E 1 107 ? -11.57700 41.22400 -29.86400 1.000 113.10587 ?  115 LEU A CB  1 
ATOM   5349 C CG  . LEU E 1 107 ? -10.68400 40.85400 -31.05100 1.000 105.14403 ?  115 LEU A CG  1 
ATOM   5350 C CD1 . LEU E 1 107 ? -10.97100 41.70600 -32.27600 1.000 104.46546 ?  115 LEU A CD1 1 
ATOM   5351 C CD2 . LEU E 1 107 ? -9.22200  40.96600 -30.64000 1.000 105.61863 ?  115 LEU A CD2 1 
ATOM   5352 N N   . ASP E 1 108 ? -11.85900 40.24200 -26.37200 1.000 116.57399 ?  116 ASP A N   1 
ATOM   5353 C CA  . ASP E 1 108 ? -12.46300 40.74800 -25.14100 1.000 124.22350 ?  116 ASP A CA  1 
ATOM   5354 C C   . ASP E 1 108 ? -12.03600 42.19800 -24.97300 1.000 128.80986 ?  116 ASP A C   1 
ATOM   5355 O O   . ASP E 1 108 ? -11.68300 42.84800 -25.96400 1.000 127.10830 ?  116 ASP A O   1 
ATOM   5356 C CB  . ASP E 1 108 ? -12.12700 39.92300 -23.88900 1.000 125.47185 ?  116 ASP A CB  1 
ATOM   5357 C CG  . ASP E 1 108 ? -10.64600 39.73800 -23.65300 1.000 121.63967 ?  116 ASP A CG  1 
ATOM   5358 O OD1 . ASP E 1 108 ? -9.82600  40.46800 -24.24000 1.000 120.26195 ?  116 ASP A OD1 1 
ATOM   5359 O OD2 . ASP E 1 108 ? -10.30800 38.87600 -22.81400 1.000 119.59346 -1 116 ASP A OD2 1 
ATOM   5360 N N   . TYR E 1 109 ? -12.02800 42.69000 -23.72700 1.000 124.16306 ?  117 TYR A N   1 
ATOM   5361 C CA  . TYR E 1 109 ? -12.11800 44.10700 -23.39100 1.000 127.37686 ?  117 TYR A CA  1 
ATOM   5362 C C   . TYR E 1 109 ? -11.53500 45.00600 -24.47400 1.000 125.63953 ?  117 TYR A C   1 
ATOM   5363 O O   . TYR E 1 109 ? -10.34300 44.92000 -24.79500 1.000 123.50620 ?  117 TYR A O   1 
ATOM   5364 C CB  . TYR E 1 109 ? -11.36200 44.41000 -22.08900 1.000 128.58992 ?  117 TYR A CB  1 
ATOM   5365 C CG  . TYR E 1 109 ? -11.59800 43.53100 -20.87100 1.000 130.23449 ?  117 TYR A CG  1 
ATOM   5366 C CD1 . TYR E 1 109 ? -11.10000 42.23700 -20.80500 1.000 128.30447 ?  117 TYR A CD1 1 
ATOM   5367 C CD2 . TYR E 1 109 ? -12.26700 44.02900 -19.76000 1.000 133.21501 ?  117 TYR A CD2 1 
ATOM   5368 C CE1 . TYR E 1 109 ? -11.29400 41.45500 -19.67600 1.000 129.87858 ?  117 TYR A CE1 1 
ATOM   5369 C CE2 . TYR E 1 109 ? -12.46500 43.25700 -18.63100 1.000 134.83557 ?  117 TYR A CE2 1 
ATOM   5370 C CZ  . TYR E 1 109 ? -11.97600 41.97000 -18.59300 1.000 133.49589 ?  117 TYR A CZ  1 
ATOM   5371 O OH  . TYR E 1 109 ? -12.17100 41.19400 -17.47000 1.000 135.20385 ?  117 TYR A OH  1 
ATOM   5372 N N   . TRP E 1 110 ? -12.37400 45.88400 -25.02100 1.000 134.74204 ?  118 TRP A N   1 
ATOM   5373 C CA  . TRP E 1 110 ? -12.05500 46.72200 -26.16800 1.000 133.15982 ?  118 TRP A CA  1 
ATOM   5374 C C   . TRP E 1 110 ? -11.63500 48.11100 -25.70300 1.000 134.74892 ?  118 TRP A C   1 
ATOM   5375 O O   . TRP E 1 110 ? -11.76300 48.46800 -24.52900 1.000 136.52966 ?  118 TRP A O   1 
ATOM   5376 C CB  . TRP E 1 110 ? -13.26400 46.82800 -27.10900 1.000 131.48967 ?  118 TRP A CB  1 
ATOM   5377 C CG  . TRP E 1 110 ? -13.41600 45.69500 -28.11700 1.000 126.57304 ?  118 TRP A CG  1 
ATOM   5378 C CD1 . TRP E 1 110 ? -13.67200 44.37700 -27.84300 1.000 124.24160 ?  118 TRP A CD1 1 
ATOM   5379 C CD2 . TRP E 1 110 ? -13.36400 45.79700 -29.55000 1.000 122.19068 ?  118 TRP A CD2 1 
ATOM   5380 N NE1 . TRP E 1 110 ? -13.76400 43.65800 -29.00900 1.000 117.65101 ?  118 TRP A NE1 1 
ATOM   5381 C CE2 . TRP E 1 110 ? -13.57900 44.50300 -30.07000 1.000 116.33845 ?  118 TRP A CE2 1 
ATOM   5382 C CE3 . TRP E 1 110 ? -13.14600 46.85200 -30.44300 1.000 122.10731 ?  118 TRP A CE3 1 
ATOM   5383 C CZ2 . TRP E 1 110 ? -13.58200 44.23700 -31.44000 1.000 109.85259 ?  118 TRP A CZ2 1 
ATOM   5384 C CZ3 . TRP E 1 110 ? -13.15300 46.58300 -31.80700 1.000 116.84814 ?  118 TRP A CZ3 1 
ATOM   5385 C CH2 . TRP E 1 110 ? -13.36900 45.28600 -32.28900 1.000 110.51730 ?  118 TRP A CH2 1 
ATOM   5386 N N   . GLY E 1 111 ? -11.14400 48.90600 -26.65300 1.000 136.01887 ?  119 GLY A N   1 
ATOM   5387 C CA  . GLY E 1 111 ? -10.75800 50.27700 -26.38700 1.000 136.79929 ?  119 GLY A CA  1 
ATOM   5388 C C   . GLY E 1 111 ? -11.96200 51.19300 -26.32000 1.000 138.67088 ?  119 GLY A C   1 
ATOM   5389 O O   . GLY E 1 111 ? -13.10000 50.76000 -26.12900 1.000 139.43599 ?  119 GLY A O   1 
ATOM   5390 N N   . GLN E 1 112 ? -11.69900 52.48900 -26.46900 1.000 133.99466 ?  120 GLN A N   1 
ATOM   5391 C CA  . GLN E 1 112 ? -12.76100 53.48900 -26.50000 1.000 135.42088 ?  120 GLN A CA  1 
ATOM   5392 C C   . GLN E 1 112 ? -13.00700 53.99000 -27.90700 1.000 134.32843 ?  120 GLN A C   1 
ATOM   5393 O O   . GLN E 1 112 ? -14.14900 54.26000 -28.28600 1.000 134.10470 ?  120 GLN A O   1 
ATOM   5394 C CB  . GLN E 1 112 ? -12.43500 54.71000 -25.62200 1.000 136.83462 ?  120 GLN A CB  1 
ATOM   5395 C CG  . GLN E 1 112 ? -11.80700 54.46000 -24.25600 1.000 136.82186 ?  120 GLN A CG  1 
ATOM   5396 C CD  . GLN E 1 112 ? -10.40900 53.88400 -24.35200 1.000 134.41134 ?  120 GLN A CD  1 
ATOM   5397 O OE1 . GLN E 1 112 ? -9.53800  54.46300 -25.00600 1.000 133.47004 ?  120 GLN A OE1 1 
ATOM   5398 N NE2 . GLN E 1 112 ? -10.19200 52.72700 -23.73100 1.000 133.35670 ?  120 GLN A NE2 1 
ATOM   5399 N N   . GLY E 1 113 ? -11.94000 54.11100 -28.68100 1.000 133.58257 ?  121 GLY A N   1 
ATOM   5400 C CA  . GLY E 1 113 ? -12.02200 54.65100 -30.01300 1.000 132.77384 ?  121 GLY A CA  1 
ATOM   5401 C C   . GLY E 1 113 ? -11.15600 55.88200 -30.08800 1.000 134.38080 ?  121 GLY A C   1 
ATOM   5402 O O   . GLY E 1 113 ? -11.39700 56.86000 -29.37600 1.000 135.98339 ?  121 GLY A O   1 
ATOM   5403 N N   . THR E 1 114 ? -10.13600 55.84800 -30.93000 1.000 132.35227 ?  122 THR A N   1 
ATOM   5404 C CA  . THR E 1 114 ? -9.27500  57.00100 -31.13200 1.000 134.26846 ?  122 THR A CA  1 
ATOM   5405 C C   . THR E 1 114 ? -9.37800  57.39400 -32.59800 1.000 134.69336 ?  122 THR A C   1 
ATOM   5406 O O   . THR E 1 114 ? -9.12200  56.57500 -33.48200 1.000 133.38933 ?  122 THR A O   1 
ATOM   5407 C CB  . THR E 1 114 ? -7.84300  56.66600 -30.70800 1.000 133.92822 ?  122 THR A CB  1 
ATOM   5408 O OG1 . THR E 1 114 ? -7.75800  56.66600 -29.27400 1.000 133.27047 ?  122 THR A OG1 1 
ATOM   5409 C CG2 . THR E 1 114 ? -6.87300  57.63800 -31.28100 1.000 135.97969 ?  122 THR A CG2 1 
ATOM   5410 N N   . LEU E 1 115 ? -9.75300  58.64200 -32.85400 1.000 131.84587 ?  123 LEU A N   1 
ATOM   5411 C CA  . LEU E 1 115 ? -10.15000 59.06000 -34.19100 1.000 131.55342 ?  123 LEU A CA  1 
ATOM   5412 C C   . LEU E 1 115 ? -8.95400  59.57400 -34.98000 1.000 134.15179 ?  123 LEU A C   1 
ATOM   5413 O O   . LEU E 1 115 ? -8.14500  60.34000 -34.45300 1.000 136.77699 ?  123 LEU A O   1 
ATOM   5414 C CB  . LEU E 1 115 ? -11.23400 60.13400 -34.10800 1.000 131.75817 ?  123 LEU A CB  1 
ATOM   5415 C CG  . LEU E 1 115 ? -11.38700 60.93900 -35.39200 1.000 132.03994 ?  123 LEU A CG  1 
ATOM   5416 C CD1 . LEU E 1 115 ? -12.04000 60.09300 -36.45900 1.000 128.35570 ?  123 LEU A CD1 1 
ATOM   5417 C CD2 . LEU E 1 115 ? -12.21100 62.16100 -35.12500 1.000 132.93387 ?  123 LEU A CD2 1 
ATOM   5418 N N   . VAL E 1 116 ? -8.82200  59.11800 -36.22800 1.000 135.85811 ?  124 VAL A N   1 
ATOM   5419 C CA  . VAL E 1 116 ? -7.77500  59.56900 -37.13900 1.000 138.96019 ?  124 VAL A CA  1 
ATOM   5420 C C   . VAL E 1 116 ? -8.44100  60.03100 -38.43100 1.000 138.21631 ?  124 VAL A C   1 
ATOM   5421 O O   . VAL E 1 116 ? -9.18100  59.26200 -39.06000 1.000 134.36368 ?  124 VAL A O   1 
ATOM   5422 C CB  . VAL E 1 116 ? -6.74000  58.46500 -37.40400 1.000 139.06868 ?  124 VAL A CB  1 
ATOM   5423 C CG1 . VAL E 1 116 ? -5.98400  58.71900 -38.70400 1.000 141.96173 ?  124 VAL A CG1 1 
ATOM   5424 C CG2 . VAL E 1 116 ? -5.78700  58.36300 -36.21900 1.000 140.12428 ?  124 VAL A CG2 1 
ATOM   5425 N N   . THR E 1 117 ? -8.18600  61.28000 -38.82300 1.000 143.90358 ?  125 THR A N   1 
ATOM   5426 C CA  . THR E 1 117 ? -8.80300  61.89000 -39.99800 1.000 143.28440 ?  125 THR A CA  1 
ATOM   5427 C C   . THR E 1 117 ? -7.74600  62.21900 -41.03800 1.000 147.28568 ?  125 THR A C   1 
ATOM   5428 O O   . THR E 1 117 ? -6.81900  62.98400 -40.75700 1.000 151.68593 ?  125 THR A O   1 
ATOM   5429 C CB  . THR E 1 117 ? -9.54900  63.16900 -39.59600 1.000 143.68563 ?  125 THR A CB  1 
ATOM   5430 O OG1 . THR E 1 117 ? -10.54800 62.85300 -38.62300 1.000 140.73537 ?  125 THR A OG1 1 
ATOM   5431 C CG2 . THR E 1 117 ? -10.19500 63.82200 -40.81300 1.000 142.73995 ?  125 THR A CG2 1 
ATOM   5432 N N   . VAL E 1 118 ? -7.90500  61.68700 -42.24600 1.000 146.49610 ?  126 VAL A N   1 
ATOM   5433 C CA  . VAL E 1 118 ? -6.94500  61.99700 -43.30300 1.000 150.72705 ?  126 VAL A CA  1 
ATOM   5434 C C   . VAL E 1 118 ? -7.52500  62.99200 -44.29900 1.000 150.67425 ?  126 VAL A C   1 
ATOM   5435 O O   . VAL E 1 118 ? -8.20200  62.60500 -45.26000 1.000 146.64935 ?  126 VAL A O   1 
ATOM   5436 C CB  . VAL E 1 118 ? -6.46200  60.73100 -44.03500 1.000 149.57044 ?  126 VAL A CB  1 
ATOM   5437 C CG1 . VAL E 1 118 ? -5.22000  61.07100 -44.82500 1.000 155.48884 ?  126 VAL A CG1 1 
ATOM   5438 C CG2 . VAL E 1 118 ? -6.17000  59.62700 -43.03800 1.000 148.04206 ?  126 VAL A CG2 1 
ATOM   5439 N N   . SER E 1 119 ? -7.24800  64.27600 -44.07900 1.000 152.11832 ?  127 SER A N   1 
ATOM   5440 C CA  . SER E 1 119 ? -7.69500  65.33600 -44.96900 1.000 152.62806 ?  127 SER A CA  1 
ATOM   5441 C C   . SER E 1 119 ? -6.69000  66.47600 -44.92300 1.000 158.84775 ?  127 SER A C   1 
ATOM   5442 O O   . SER E 1 119 ? -5.99500  66.67000 -43.92200 1.000 161.42606 ?  127 SER A O   1 
ATOM   5443 C CB  . SER E 1 119 ? -9.08200  65.87100 -44.60000 1.000 148.28822 ?  127 SER A CB  1 
ATOM   5444 O OG  . SER E 1 119 ? -9.17400  67.25500 -44.89900 1.000 150.71417 ?  127 SER A OG  1 
ATOM   5445 N N   . SER E 1 120 ? -6.58000  67.19800 -46.03800 1.000 151.93577 ?  128 SER A N   1 
ATOM   5446 C CA  . SER E 1 120 ? -5.69600  68.35400 -46.13400 1.000 157.29508 ?  128 SER A CA  1 
ATOM   5447 C C   . SER E 1 120 ? -6.34700  69.63500 -45.62200 1.000 156.69696 ?  128 SER A C   1 
ATOM   5448 O O   . SER E 1 120 ? -5.68700  70.68000 -45.59700 1.000 160.36304 ?  128 SER A O   1 
ATOM   5449 C CB  . SER E 1 120 ? -5.21700  68.55000 -47.58100 1.000 159.89880 ?  128 SER A CB  1 
ATOM   5450 O OG  . SER E 1 120 ? -6.22900  68.24000 -48.52500 1.000 155.51339 ?  128 SER A OG  1 
ATOM   5451 N N   . ALA E 1 121 ? -7.61400  69.57700 -45.20700 1.000 159.12683 ?  129 ALA A N   1 
ATOM   5452 C CA  . ALA E 1 121 ? -8.28600  70.74800 -44.66200 1.000 158.43633 ?  129 ALA A CA  1 
ATOM   5453 C C   . ALA E 1 121 ? -7.67200  71.13600 -43.31600 1.000 160.84262 ?  129 ALA A C   1 
ATOM   5454 O O   . ALA E 1 121 ? -6.93800  70.36900 -42.68500 1.000 161.91483 ?  129 ALA A O   1 
ATOM   5455 C CB  . ALA E 1 121 ? -9.78700  70.49500 -44.52100 1.000 152.68817 ?  129 ALA A CB  1 
ATOM   5456 N N   . SER E 1 122 ? -7.98800  72.35000 -42.87800 1.000 146.91784 ?  130 SER A N   1 
ATOM   5457 C CA  . SER E 1 122 ? -7.35900  72.95400 -41.71400 1.000 149.08753 ?  130 SER A CA  1 
ATOM   5458 C C   . SER E 1 122 ? -8.28200  72.96700 -40.50300 1.000 146.59855 ?  130 SER A C   1 
ATOM   5459 O O   . SER E 1 122 ? -9.50000  73.11400 -40.62600 1.000 143.79808 ?  130 SER A O   1 
ATOM   5460 C CB  . SER E 1 122 ? -6.91700  74.38400 -42.03000 1.000 151.82924 ?  130 SER A CB  1 
ATOM   5461 O OG  . SER E 1 122 ? -6.35300  75.00800 -40.89000 1.000 153.34596 ?  130 SER A OG  1 
ATOM   5462 N N   . THR E 1 123 ? -7.67800  72.82800 -39.32600 1.000 143.51702 ?  131 THR A N   1 
ATOM   5463 C CA  . THR E 1 123 ? -8.43000  72.89200 -38.07900 1.000 142.43402 ?  131 THR A CA  1 
ATOM   5464 C C   . THR E 1 123 ? -9.05200  74.26700 -37.86900 1.000 143.72068 ?  131 THR A C   1 
ATOM   5465 O O   . THR E 1 123 ? -8.38000  75.29300 -38.00000 1.000 146.43366 ?  131 THR A O   1 
ATOM   5466 C CB  . THR E 1 123 ? -7.52500  72.55400 -36.90100 1.000 143.56331 ?  131 THR A CB  1 
ATOM   5467 O OG1 . THR E 1 123 ? -6.86700  71.31000 -37.15300 1.000 142.51620 ?  131 THR A OG1 1 
ATOM   5468 C CG2 . THR E 1 123 ? -8.33300  72.46200 -35.62700 1.000 142.45001 ?  131 THR A CG2 1 
ATOM   5469 N N   . LYS E 1 124 ? -10.33600 74.28400 -37.52000 1.000 153.17083 ?  132 LYS A N   1 
ATOM   5470 C CA  . LYS E 1 124 ? -11.03600 75.51000 -37.16400 1.000 153.70878 ?  132 LYS A CA  1 
ATOM   5471 C C   . LYS E 1 124 ? -11.59300 75.36400 -35.75800 1.000 153.28552 ?  132 LYS A C   1 
ATOM   5472 O O   . LYS E 1 124 ? -12.28300 74.38500 -35.45700 1.000 150.85464 ?  132 LYS A O   1 
ATOM   5473 C CB  . LYS E 1 124 ? -12.16400 75.83000 -38.15000 1.000 151.41826 ?  132 LYS A CB  1 
ATOM   5474 N N   . GLY E 1 125 ? -11.29900 76.33500 -34.90200 1.000 170.96061 ?  133 GLY A N   1 
ATOM   5475 C CA  . GLY E 1 125 ? -11.88000 76.34900 -33.58500 1.000 171.00760 ?  133 GLY A CA  1 
ATOM   5476 C C   . GLY E 1 125 ? -13.36500 76.61100 -33.72000 1.000 169.45276 ?  133 GLY A C   1 
ATOM   5477 O O   . GLY E 1 125 ? -13.81500 77.22100 -34.69500 1.000 168.85685 ?  133 GLY A O   1 
ATOM   5478 N N   . PRO E 1 126 ? -14.15700 76.16600 -32.75400 1.000 169.71819 ?  134 PRO A N   1 
ATOM   5479 C CA  . PRO E 1 126 ? -15.61000 76.27000 -32.89100 1.000 168.07524 ?  134 PRO A CA  1 
ATOM   5480 C C   . PRO E 1 126 ? -16.10700 77.64000 -32.45700 1.000 170.26678 ?  134 PRO A C   1 
ATOM   5481 O O   . PRO E 1 126 ? -15.38800 78.43900 -31.85500 1.000 172.90760 ?  134 PRO A O   1 
ATOM   5482 C CB  . PRO E 1 126 ? -16.12200 75.18100 -31.95000 1.000 166.85614 ?  134 PRO A CB  1 
ATOM   5483 C CG  . PRO E 1 126 ? -15.09600 75.15800 -30.85100 1.000 169.06961 ?  134 PRO A CG  1 
ATOM   5484 C CD  . PRO E 1 126 ? -13.76900 75.57600 -31.46100 1.000 170.39012 ?  134 PRO A CD  1 
ATOM   5485 N N   . SER E 1 127 ? -17.37400 77.89100 -32.76400 1.000 173.19129 ?  135 SER A N   1 
ATOM   5486 C CA  . SER E 1 127 ? -18.08000 79.03800 -32.21600 1.000 175.14408 ?  135 SER A CA  1 
ATOM   5487 C C   . SER E 1 127 ? -19.36200 78.51500 -31.59700 1.000 174.29036 ?  135 SER A C   1 
ATOM   5488 O O   . SER E 1 127 ? -19.99100 77.60400 -32.13700 1.000 171.28406 ?  135 SER A O   1 
ATOM   5489 C CB  . SER E 1 127 ? -18.38300 80.10200 -33.28200 1.000 175.43506 ?  135 SER A CB  1 
ATOM   5490 O OG  . SER E 1 127 ? -18.68900 79.50600 -34.52800 1.000 172.33122 ?  135 SER A OG  1 
ATOM   5491 N N   . VAL E 1 128 ? -19.74100 79.07200 -30.45400 1.000 172.81141 ?  136 VAL A N   1 
ATOM   5492 C CA  . VAL E 1 128 ? -20.87600 78.56700 -29.69300 1.000 173.41343 ?  136 VAL A CA  1 
ATOM   5493 C C   . VAL E 1 128 ? -21.90900 79.66800 -29.52900 1.000 178.68866 ?  136 VAL A C   1 
ATOM   5494 O O   . VAL E 1 128 ? -21.63500 80.70200 -28.90600 1.000 182.96939 ?  136 VAL A O   1 
ATOM   5495 C CB  . VAL E 1 128 ? -20.44400 78.01500 -28.32700 1.000 173.05312 ?  136 VAL A CB  1 
ATOM   5496 C CG1 . VAL E 1 128 ? -21.57500 77.22700 -27.70100 1.000 172.77849 ?  136 VAL A CG1 1 
ATOM   5497 C CG2 . VAL E 1 128 ? -19.23400 77.13000 -28.49100 1.000 168.36714 ?  136 VAL A CG2 1 
ATOM   5498 N N   . PHE E 1 129 ? -23.09300 79.44100 -30.08200 1.000 178.50576 ?  137 PHE A N   1 
ATOM   5499 C CA  . PHE E 1 129 ? -24.20800 80.33800 -29.83900 1.000 183.41349 ?  137 PHE A CA  1 
ATOM   5500 C C   . PHE E 1 129 ? -25.29300 79.64700 -29.01400 1.000 183.88216 ?  137 PHE A C   1 
ATOM   5501 O O   . PHE E 1 129 ? -25.54400 78.44600 -29.18600 1.000 179.90680 ?  137 PHE A O   1 
ATOM   5502 C CB  . PHE E 1 129 ? -24.80900 80.86700 -31.14800 1.000 183.93523 ?  137 PHE A CB  1 
ATOM   5503 C CG  . PHE E 1 129 ? -23.78200 81.26300 -32.17800 1.000 182.48499 ?  137 PHE A CG  1 
ATOM   5504 C CD1 . PHE E 1 129 ? -23.17800 82.50800 -32.12500 1.000 186.30099 ?  137 PHE A CD1 1 
ATOM   5505 C CD2 . PHE E 1 129 ? -23.43300 80.40100 -33.20600 1.000 177.60187 ?  137 PHE A CD2 1 
ATOM   5506 C CE1 . PHE E 1 129 ? -22.24400 82.88400 -33.07000 1.000 185.31527 ?  137 PHE A CE1 1 
ATOM   5507 C CE2 . PHE E 1 129 ? -22.49800 80.77700 -34.15600 1.000 176.60357 ?  137 PHE A CE2 1 
ATOM   5508 C CZ  . PHE E 1 129 ? -21.90400 82.02200 -34.08500 1.000 180.49692 ?  137 PHE A CZ  1 
ATOM   5509 N N   . PRO E 1 130 ? -25.94700 80.37700 -28.11400 1.000 188.89725 ?  138 PRO A N   1 
ATOM   5510 C CA  . PRO E 1 130 ? -26.98900 79.77300 -27.28000 1.000 189.93721 ?  138 PRO A CA  1 
ATOM   5511 C C   . PRO E 1 130 ? -28.23600 79.42900 -28.08200 1.000 189.28486 ?  138 PRO A C   1 
ATOM   5512 O O   . PRO E 1 130 ? -28.51900 80.01100 -29.13200 1.000 189.75450 ?  138 PRO A O   1 
ATOM   5513 C CB  . PRO E 1 130 ? -27.28100 80.85800 -26.24000 1.000 196.11102 ?  138 PRO A CB  1 
ATOM   5514 C CG  . PRO E 1 130 ? -26.99300 82.13300 -26.95300 1.000 198.76596 ?  138 PRO A CG  1 
ATOM   5515 C CD  . PRO E 1 130 ? -25.88000 81.83900 -27.93800 1.000 194.23279 ?  138 PRO A CD  1 
ATOM   5516 N N   . LEU E 1 131 ? -28.98500 78.45400 -27.57100 1.000 188.27701 ?  139 LEU A N   1 
ATOM   5517 C CA  . LEU E 1 131 ? -30.32200 78.12300 -28.05100 1.000 188.61654 ?  139 LEU A CA  1 
ATOM   5518 C C   . LEU E 1 131 ? -31.25000 78.38700 -26.87000 1.000 193.50002 ?  139 LEU A C   1 
ATOM   5519 O O   . LEU E 1 131 ? -31.51600 77.49400 -26.05800 1.000 192.82410 ?  139 LEU A O   1 
ATOM   5520 C CB  . LEU E 1 131 ? -30.39100 76.69400 -28.55000 1.000 183.26886 ?  139 LEU A CB  1 
ATOM   5521 C CG  . LEU E 1 131 ? -29.28700 76.37300 -29.55400 1.000 178.49879 ?  139 LEU A CG  1 
ATOM   5522 C CD1 . LEU E 1 131 ? -29.38100 74.93300 -30.02800 1.000 173.42252 ?  139 LEU A CD1 1 
ATOM   5523 C CD2 . LEU E 1 131 ? -29.37300 77.33600 -30.72400 1.000 179.59259 ?  139 LEU A CD2 1 
ATOM   5524 N N   . ALA E 1 132 ? -31.71300 79.63300 -26.78000 1.000 178.11900 ?  140 ALA A N   1 
ATOM   5525 C CA  . ALA E 1 132 ? -32.38500 80.12600 -25.58700 1.000 178.68194 ?  140 ALA A CA  1 
ATOM   5526 C C   . ALA E 1 132 ? -33.73000 79.43300 -25.37800 1.000 183.00235 ?  140 ALA A C   1 
ATOM   5527 O O   . ALA E 1 132 ? -34.47600 79.21400 -26.33800 1.000 188.21303 ?  140 ALA A O   1 
ATOM   5528 C CB  . ALA E 1 132 ? -32.59300 81.63600 -25.68000 1.000 181.20441 ?  140 ALA A CB  1 
ATOM   5529 N N   . PRO E 1 133 ? -34.07500 79.10200 -24.13300 1.000 182.20024 ?  141 PRO A N   1 
ATOM   5530 C CA  . PRO E 1 133 ? -35.40500 78.54900 -23.84900 1.000 186.89095 ?  141 PRO A CA  1 
ATOM   5531 C C   . PRO E 1 133 ? -36.48400 79.61900 -23.89600 1.000 192.29653 ?  141 PRO A C   1 
ATOM   5532 O O   . PRO E 1 133 ? -36.84300 80.20100 -22.86700 1.000 192.27968 ?  141 PRO A O   1 
ATOM   5533 C CB  . PRO E 1 133 ? -35.24700 77.97500 -22.43700 1.000 183.40096 ?  141 PRO A CB  1 
ATOM   5534 C CG  . PRO E 1 133 ? -34.19100 78.83100 -21.81600 1.000 178.69178 ?  141 PRO A CG  1 
ATOM   5535 C CD  . PRO E 1 133 ? -33.23700 79.18500 -22.92400 1.000 176.87824 ?  141 PRO A CD  1 
ATOM   5536 N N   . SER E 1 134 ? -36.98800 79.90500 -25.09200 1.000 182.94348 ?  142 SER A N   1 
ATOM   5537 C CA  . SER E 1 134 ? -38.03700 80.90200 -25.23000 1.000 188.27381 ?  142 SER A CA  1 
ATOM   5538 C C   . SER E 1 134 ? -39.32600 80.40800 -24.58800 1.000 191.69932 ?  142 SER A C   1 
ATOM   5539 O O   . SER E 1 134 ? -39.60100 79.20600 -24.53700 1.000 191.88867 ?  142 SER A O   1 
ATOM   5540 C CB  . SER E 1 134 ? -38.28000 81.22900 -26.70200 1.000 193.06063 ?  142 SER A CB  1 
ATOM   5541 O OG  . SER E 1 134 ? -39.49300 81.94200 -26.87600 1.000 198.82471 ?  142 SER A OG  1 
ATOM   5542 N N   . SER E 1 135 ? -40.12700 81.35900 -24.10200 1.000 178.99656 ?  143 SER A N   1 
ATOM   5543 C CA  . SER E 1 135 ? -41.41400 81.01100 -23.50900 1.000 183.29745 ?  143 SER A CA  1 
ATOM   5544 C C   . SER E 1 135 ? -42.29300 80.24800 -24.49100 1.000 187.63557 ?  143 SER A C   1 
ATOM   5545 O O   . SER E 1 135 ? -43.16800 79.47800 -24.07500 1.000 189.99653 ?  143 SER A O   1 
ATOM   5546 C CB  . SER E 1 135 ? -42.12400 82.27500 -23.02600 1.000 188.48023 ?  143 SER A CB  1 
ATOM   5547 O OG  . SER E 1 135 ? -43.06900 82.71300 -23.98400 1.000 192.17480 ?  143 SER A OG  1 
ATOM   5548 N N   . LYS E 1 136 ? -42.08400 80.45700 -25.79300 1.000 185.64581 ?  144 LYS A N   1 
ATOM   5549 C CA  . LYS E 1 136 ? -42.76000 79.64900 -26.80400 1.000 189.60777 ?  144 LYS A CA  1 
ATOM   5550 C C   . LYS E 1 136 ? -42.22000 78.22600 -26.83000 1.000 186.51716 ?  144 LYS A C   1 
ATOM   5551 O O   . LYS E 1 136 ? -42.98600 77.26900 -26.98600 1.000 188.97925 ?  144 LYS A O   1 
ATOM   5552 C CB  . LYS E 1 136 ? -42.61500 80.29700 -28.17900 1.000 192.53247 ?  144 LYS A CB  1 
ATOM   5553 N N   . SER E 1 137 ? -40.90300 78.06900 -26.68900 1.000 190.04116 ?  145 SER A N   1 
ATOM   5554 C CA  . SER E 1 137 ? -40.29900 76.74500 -26.61500 1.000 186.86118 ?  145 SER A CA  1 
ATOM   5555 C C   . SER E 1 137 ? -40.65700 76.00800 -25.33300 1.000 184.68499 ?  145 SER A C   1 
ATOM   5556 O O   . SER E 1 137 ? -40.35700 74.81700 -25.22000 1.000 182.72557 ?  145 SER A O   1 
ATOM   5557 C CB  . SER E 1 137 ? -38.77800 76.85700 -26.74700 1.000 181.70446 ?  145 SER A CB  1 
ATOM   5558 O OG  . SER E 1 137 ? -38.41400 77.43000 -27.99300 1.000 184.01571 ?  145 SER A OG  1 
ATOM   5559 N N   . THR E 1 138 ? -41.24500 76.68500 -24.35700 1.000 187.77036 ?  146 THR A N   1 
ATOM   5560 C CA  . THR E 1 138 ? -41.69500 76.02800 -23.13400 1.000 187.75369 ?  146 THR A CA  1 
ATOM   5561 C C   . THR E 1 138 ? -42.92900 75.17400 -23.40600 1.000 192.31887 ?  146 THR A C   1 
ATOM   5562 O O   . THR E 1 138 ? -43.99200 75.69700 -23.75400 1.000 196.88958 ?  146 THR A O   1 
ATOM   5563 C CB  . THR E 1 138 ? -41.98800 77.07400 -22.06900 1.000 188.31364 ?  146 THR A CB  1 
ATOM   5564 O OG1 . THR E 1 138 ? -40.85900 77.94700 -21.95200 1.000 183.97998 ?  146 THR A OG1 1 
ATOM   5565 C CG2 . THR E 1 138 ? -42.25400 76.40200 -20.74000 1.000 188.14570 ?  146 THR A CG2 1 
ATOM   5566 N N   . SER E 1 139 ? -42.80400 73.85900 -23.26000 1.000 181.50446 ?  147 SER A N   1 
ATOM   5567 C CA  . SER E 1 139 ? -43.96900 72.98300 -23.37200 1.000 186.21760 ?  147 SER A CA  1 
ATOM   5568 C C   . SER E 1 139 ? -44.53000 72.68400 -21.98100 1.000 191.56596 ?  147 SER A C   1 
ATOM   5569 O O   . SER E 1 139 ? -44.42400 71.57800 -21.45300 1.000 192.26435 ?  147 SER A O   1 
ATOM   5570 C CB  . SER E 1 139 ? -43.60800 71.70700 -24.12900 1.000 183.43764 ?  147 SER A CB  1 
ATOM   5571 O OG  . SER E 1 139 ? -44.57700 70.69800 -23.89800 1.000 188.45229 ?  147 SER A OG  1 
ATOM   5572 N N   . GLY E 1 140 ? -45.15400 73.70100 -21.39700 1.000 195.98021 ?  148 GLY A N   1 
ATOM   5573 C CA  . GLY E 1 140 ? -45.76000 73.52300 -20.08100 1.000 202.13133 ?  148 GLY A CA  1 
ATOM   5574 C C   . GLY E 1 140 ? -44.70000 73.28600 -19.02800 1.000 199.44731 ?  148 GLY A C   1 
ATOM   5575 O O   . GLY E 1 140 ? -43.75600 74.06900 -18.88800 1.000 195.36763 ?  148 GLY A O   1 
ATOM   5576 N N   . GLY E 1 141 ? -44.84900 72.19800 -18.27300 1.000 202.30212 ?  149 GLY A N   1 
ATOM   5577 C CA  . GLY E 1 141 ? -43.83800 71.82900 -17.29400 1.000 200.10343 ?  149 GLY A CA  1 
ATOM   5578 C C   . GLY E 1 141 ? -42.51300 71.42500 -17.90500 1.000 191.99084 ?  149 GLY A C   1 
ATOM   5579 O O   . GLY E 1 141 ? -41.50900 71.35000 -17.18500 1.000 189.46447 ?  149 GLY A O   1 
ATOM   5580 N N   . THR E 1 142 ? -42.48400 71.18800 -19.21200 1.000 188.86866 ?  150 THR A N   1 
ATOM   5581 C CA  . THR E 1 142 ? -41.30500 70.72100 -19.92700 1.000 184.66854 ?  150 THR A CA  1 
ATOM   5582 C C   . THR E 1 142 ? -40.74200 71.87000 -20.75500 1.000 182.63910 ?  150 THR A C   1 
ATOM   5583 O O   . THR E 1 142 ? -41.42000 72.37300 -21.65700 1.000 185.42750 ?  150 THR A O   1 
ATOM   5584 C CB  . THR E 1 142 ? -41.67700 69.54900 -20.83400 1.000 185.76269 ?  150 THR A CB  1 
ATOM   5585 O OG1 . THR E 1 142 ? -42.68700 68.75300 -20.19500 1.000 188.94327 ?  150 THR A OG1 1 
ATOM   5586 C CG2 . THR E 1 142 ? -40.45900 68.69000 -21.10600 1.000 181.82506 ?  150 THR A CG2 1 
ATOM   5587 N N   . ALA E 1 143 ? -39.50400 72.27500 -20.47500 1.000 178.90546 ?  151 ALA A N   1 
ATOM   5588 C CA  . ALA E 1 143 ? -38.87300 73.39100 -21.15800 1.000 176.69819 ?  151 ALA A CA  1 
ATOM   5589 C C   . ALA E 1 143 ? -37.67400 72.88200 -21.94400 1.000 172.88122 ?  151 ALA A C   1 
ATOM   5590 O O   . ALA E 1 143 ? -37.01700 71.92500 -21.53800 1.000 169.82829 ?  151 ALA A O   1 
ATOM   5591 C CB  . ALA E 1 143 ? -38.43200 74.46100 -20.15700 1.000 173.88326 ?  151 ALA A CB  1 
ATOM   5592 N N   . ALA E 1 144 ? -37.39600 73.51700 -23.08000 1.000 171.74302 ?  152 ALA A N   1 
ATOM   5593 C CA  . ALA E 1 144 ? -36.31600 73.10600 -23.96600 1.000 168.57079 ?  152 ALA A CA  1 
ATOM   5594 C C   . ALA E 1 144 ? -35.28100 74.21600 -24.07200 1.000 163.98796 ?  152 ALA A C   1 
ATOM   5595 O O   . ALA E 1 144 ? -35.63100 75.36800 -24.34600 1.000 166.34315 ?  152 ALA A O   1 
ATOM   5596 C CB  . ALA E 1 144 ? -36.85100 72.75700 -25.35700 1.000 173.64546 ?  152 ALA A CB  1 
ATOM   5597 N N   . LEU E 1 145 ? -34.01000 73.86500 -23.86800 1.000 176.98715 ?  153 LEU A N   1 
ATOM   5598 C CA  . LEU E 1 145 ? -32.90300 74.79900 -24.04100 1.000 172.20894 ?  153 LEU A CA  1 
ATOM   5599 C C   . LEU E 1 145 ? -31.68400 74.04400 -24.54600 1.000 166.78521 ?  153 LEU A C   1 
ATOM   5600 O O   . LEU E 1 145 ? -31.52000 72.85600 -24.26000 1.000 164.90939 ?  153 LEU A O   1 
ATOM   5601 C CB  . LEU E 1 145 ? -32.55400 75.52300 -22.73200 1.000 168.94530 ?  153 LEU A CB  1 
ATOM   5602 C CG  . LEU E 1 145 ? -31.84100 74.75400 -21.61200 1.000 163.87412 ?  153 LEU A CG  1 
ATOM   5603 C CD1 . LEU E 1 145 ? -30.34900 74.88800 -21.71100 1.000 157.53281 ?  153 LEU A CD1 1 
ATOM   5604 C CD2 . LEU E 1 145 ? -32.27200 75.31000 -20.28000 1.000 164.77614 ?  153 LEU A CD2 1 
ATOM   5605 N N   . GLY E 1 146 ? -30.79900 74.74400 -25.25100 1.000 168.95409 ?  154 GLY A N   1 
ATOM   5606 C CA  . GLY E 1 146 ? -29.62800 74.05400 -25.75200 1.000 164.29544 ?  154 GLY A CA  1 
ATOM   5607 C C   . GLY E 1 146 ? -28.46600 74.95200 -26.12900 1.000 161.13451 ?  154 GLY A C   1 
ATOM   5608 O O   . GLY E 1 146 ? -28.46900 76.16100 -25.88300 1.000 162.01570 ?  154 GLY A O   1 
ATOM   5609 N N   . CYS E 1 147 ? -27.47300 74.32500 -26.76200 1.000 164.54726 ?  155 CYS A N   1 
ATOM   5610 C CA  . CYS E 1 147 ? -26.27200 74.97600 -27.26100 1.000 162.23466 ?  155 CYS A CA  1 
ATOM   5611 C C   . CYS E 1 147 ? -26.07500 74.59300 -28.72000 1.000 163.90982 ?  155 CYS A C   1 
ATOM   5612 O O   . CYS E 1 147 ? -26.43500 73.48400 -29.14200 1.000 164.41268 ?  155 CYS A O   1 
ATOM   5613 C CB  . CYS E 1 147 ? -25.02700 74.57800 -26.44900 1.000 157.11812 ?  155 CYS A CB  1 
ATOM   5614 S SG  . CYS E 1 147 ? -24.73600 75.56900 -24.96600 1.000 157.48548 ?  155 CYS A SG  1 
ATOM   5615 N N   . LEU E 1 148 ? -25.48400 75.51500 -29.48300 1.000 156.34930 ?  156 LEU A N   1 
ATOM   5616 C CA  . LEU E 1 148 ? -25.19800 75.32800 -30.90100 1.000 158.61603 ?  156 LEU A CA  1 
ATOM   5617 C C   . LEU E 1 148 ? -23.70400 75.52100 -31.11900 1.000 155.69349 ?  156 LEU A C   1 
ATOM   5618 O O   . LEU E 1 148 ? -23.18500 76.62900 -30.92700 1.000 155.84910 ?  156 LEU A O   1 
ATOM   5619 C CB  . LEU E 1 148 ? -26.00000 76.31900 -31.73800 1.000 164.83488 ?  156 LEU A CB  1 
ATOM   5620 C CG  . LEU E 1 148 ? -25.73200 76.32000 -33.23900 1.000 168.59895 ?  156 LEU A CG  1 
ATOM   5621 C CD1 . LEU E 1 148 ? -25.98500 74.94300 -33.81800 1.000 168.97056 ?  156 LEU A CD1 1 
ATOM   5622 C CD2 . LEU E 1 148 ? -26.57100 77.37900 -33.94200 1.000 175.59808 ?  156 LEU A CD2 1 
ATOM   5623 N N   . VAL E 1 149 ? -23.01700 74.45400 -31.52700 1.000 157.42356 ?  157 VAL A N   1 
ATOM   5624 C CA  . VAL E 1 149 ? -21.58400 74.49000 -31.80100 1.000 155.88456 ?  157 VAL A CA  1 
ATOM   5625 C C   . VAL E 1 149 ? -21.39900 74.46600 -33.31200 1.000 159.79724 ?  157 VAL A C   1 
ATOM   5626 O O   . VAL E 1 149 ? -21.68200 73.46000 -33.97100 1.000 160.75139 ?  157 VAL A O   1 
ATOM   5627 C CB  . VAL E 1 149 ? -20.85500 73.32900 -31.12100 1.000 152.50384 ?  157 VAL A CB  1 
ATOM   5628 C CG1 . VAL E 1 149 ? -19.41800 73.27000 -31.60000 1.000 153.63388 ?  157 VAL A CG1 1 
ATOM   5629 C CG2 . VAL E 1 149 ? -20.91600 73.50100 -29.61700 1.000 151.14101 ?  157 VAL A CG2 1 
ATOM   5630 N N   . LYS E 1 150 ? -20.93200 75.57900 -33.86200 1.000 153.58359 ?  158 LYS A N   1 
ATOM   5631 C CA  . LYS E 1 150 ? -20.92800 75.82100 -35.29200 1.000 158.85429 ?  158 LYS A CA  1 
ATOM   5632 C C   . LYS E 1 150 ? -19.51000 76.00900 -35.81700 1.000 159.49849 ?  158 LYS A C   1 
ATOM   5633 O O   . LYS E 1 150 ? -18.65300 76.60200 -35.14300 1.000 157.27527 ?  158 LYS A O   1 
ATOM   5634 C CB  . LYS E 1 150 ? -21.77600 77.06200 -35.59400 1.000 163.28693 ?  158 LYS A CB  1 
ATOM   5635 C CG  . LYS E 1 150 ? -21.79500 77.50400 -37.03900 1.000 170.03005 ?  158 LYS A CG  1 
ATOM   5636 C CD  . LYS E 1 150 ? -23.06700 77.03600 -37.72600 1.000 175.26656 ?  158 LYS A CD  1 
ATOM   5637 C CE  . LYS E 1 150 ? -23.33000 77.84300 -38.98400 1.000 183.64390 ?  158 LYS A CE  1 
ATOM   5638 N NZ  . LYS E 1 150 ? -22.22400 77.66500 -39.96500 1.000 185.88840 ?  158 LYS A NZ  1 
ATOM   5639 N N   . ASP E 1 151 ? -19.28800 75.50200 -37.03400 1.000 158.94650 ?  159 ASP A N   1 
ATOM   5640 C CA  . ASP E 1 151 ? -18.09000 75.74000 -37.84100 1.000 161.21153 ?  159 ASP A CA  1 
ATOM   5641 C C   . ASP E 1 151 ? -16.80900 75.35000 -37.09700 1.000 157.05887 ?  159 ASP A C   1 
ATOM   5642 O O   . ASP E 1 151 ? -15.94300 76.17400 -36.79100 1.000 157.81300 ?  159 ASP A O   1 
ATOM   5643 C CB  . ASP E 1 151 ? -18.03100 77.19100 -38.32600 1.000 164.51473 ?  159 ASP A CB  1 
ATOM   5644 C CG  . ASP E 1 151 ? -19.16900 77.53100 -39.26800 1.000 170.75843 ?  159 ASP A CG  1 
ATOM   5645 O OD1 . ASP E 1 151 ? -19.65200 76.61600 -39.96900 1.000 174.29311 ?  159 ASP A OD1 1 
ATOM   5646 O OD2 . ASP E 1 151 ? -19.56100 78.71600 -39.32700 1.000 173.13652 -1 159 ASP A OD2 1 
ATOM   5647 N N   . TYR E 1 152 ? -16.70200 74.05300 -36.83900 1.000 157.52413 ?  160 TYR A N   1 
ATOM   5648 C CA  . TYR E 1 152 ? -15.49700 73.48600 -36.26000 1.000 155.34279 ?  160 TYR A CA  1 
ATOM   5649 C C   . TYR E 1 152 ? -15.03600 72.32100 -37.11800 1.000 158.21247 ?  160 TYR A C   1 
ATOM   5650 O O   . TYR E 1 152 ? -15.83500 71.67200 -37.79700 1.000 160.41069 ?  160 TYR A O   1 
ATOM   5651 C CB  . TYR E 1 152 ? -15.71900 73.04100 -34.81100 1.000 150.77438 ?  160 TYR A CB  1 
ATOM   5652 C CG  . TYR E 1 152 ? -16.50400 71.76300 -34.63900 1.000 149.17141 ?  160 TYR A CG  1 
ATOM   5653 C CD1 . TYR E 1 152 ? -15.87500 70.52600 -34.66300 1.000 149.39137 ?  160 TYR A CD1 1 
ATOM   5654 C CD2 . TYR E 1 152 ? -17.87900 71.79500 -34.45900 1.000 148.24850 ?  160 TYR A CD2 1 
ATOM   5655 C CE1 . TYR E 1 152 ? -16.59200 69.36400 -34.50400 1.000 148.04880 ?  160 TYR A CE1 1 
ATOM   5656 C CE2 . TYR E 1 152 ? -18.60600 70.63500 -34.29800 1.000 147.01323 ?  160 TYR A CE2 1 
ATOM   5657 C CZ  . TYR E 1 152 ? -17.95600 69.42200 -34.31900 1.000 146.55341 ?  160 TYR A CZ  1 
ATOM   5658 O OH  . TYR E 1 152 ? -18.66400 68.25200 -34.16500 1.000 145.29145 ?  160 TYR A OH  1 
ATOM   5659 N N   . PHE E 1 153 ? -13.72700 72.07900 -37.09600 1.000 145.51097 ?  161 PHE A N   1 
ATOM   5660 C CA  . PHE E 1 153 ? -13.09400 71.01800 -37.86100 1.000 146.09622 ?  161 PHE A CA  1 
ATOM   5661 C C   . PHE E 1 153 ? -11.75400 70.77000 -37.19500 1.000 149.83430 ?  161 PHE A C   1 
ATOM   5662 O O   . PHE E 1 153 ? -11.13500 71.73400 -36.72700 1.000 151.37071 ?  161 PHE A O   1 
ATOM   5663 C CB  . PHE E 1 153 ? -12.90800 71.43100 -39.32700 1.000 144.62914 ?  161 PHE A CB  1 
ATOM   5664 C CG  . PHE E 1 153 ? -12.49700 70.30800 -40.24700 1.000 145.43606 ?  161 PHE A CG  1 
ATOM   5665 C CD1 . PHE E 1 153 ? -13.44500 69.46500 -40.80300 1.000 141.80218 ?  161 PHE A CD1 1 
ATOM   5666 C CD2 . PHE E 1 153 ? -11.16400 70.11700 -40.57900 1.000 149.08133 ?  161 PHE A CD2 1 
ATOM   5667 C CE1 . PHE E 1 153 ? -13.07000 68.43700 -41.65600 1.000 142.15671 ?  161 PHE A CE1 1 
ATOM   5668 C CE2 . PHE E 1 153 ? -10.78300 69.09500 -41.43100 1.000 150.53100 ?  161 PHE A CE2 1 
ATOM   5669 C CZ  . PHE E 1 153 ? -11.73700 68.25500 -41.97300 1.000 147.55818 ?  161 PHE A CZ  1 
ATOM   5670 N N   . PRO E 1 154 ? -11.30000 69.51800 -37.07600 1.000 144.71866 ?  162 PRO A N   1 
ATOM   5671 C CA  . PRO E 1 154 ? -11.99200 68.27500 -37.40500 1.000 143.19532 ?  162 PRO A CA  1 
ATOM   5672 C C   . PRO E 1 154 ? -12.66400 67.68900 -36.17600 1.000 143.55277 ?  162 PRO A C   1 
ATOM   5673 O O   . PRO E 1 154 ? -12.64600 68.27200 -35.09700 1.000 145.63394 ?  162 PRO A O   1 
ATOM   5674 C CB  . PRO E 1 154 ? -10.85500 67.39400 -37.91400 1.000 144.61995 ?  162 PRO A CB  1 
ATOM   5675 C CG  . PRO E 1 154 ? -9.71100  67.77200 -36.99700 1.000 146.86893 ?  162 PRO A CG  1 
ATOM   5676 C CD  . PRO E 1 154 ? -9.90200  69.25300 -36.68500 1.000 147.26721 ?  162 PRO A CD  1 
ATOM   5677 N N   . GLU E 1 155 ? -13.28200 66.52800 -36.33000 1.000 142.74966 ?  163 GLU A N   1 
ATOM   5678 C CA  . GLU E 1 155 ? -13.82100 65.81400 -35.19500 1.000 143.52601 ?  163 GLU A CA  1 
ATOM   5679 C C   . GLU E 1 155 ? -12.67600 65.32800 -34.30100 1.000 146.66798 ?  163 GLU A C   1 
ATOM   5680 O O   . GLU E 1 155 ? -11.53700 65.19800 -34.75400 1.000 146.81957 ?  163 GLU A O   1 
ATOM   5681 C CB  . GLU E 1 155 ? -14.68500 64.65400 -35.68400 1.000 140.12793 ?  163 GLU A CB  1 
ATOM   5682 C CG  . GLU E 1 155 ? -16.08100 65.09600 -36.05000 1.000 136.19494 ?  163 GLU A CG  1 
ATOM   5683 C CD  . GLU E 1 155 ? -16.99500 65.13900 -34.84600 1.000 137.41892 ?  163 GLU A CD  1 
ATOM   5684 O OE1 . GLU E 1 155 ? -16.99000 66.16700 -34.14100 1.000 140.34063 ?  163 GLU A OE1 1 
ATOM   5685 O OE2 . GLU E 1 155 ? -17.73000 64.16100 -34.60300 1.000 135.45656 -1 163 GLU A OE2 1 
ATOM   5686 N N   . PRO E 1 156 ? -12.94600 65.07400 -33.00900 1.000 142.81135 ?  164 PRO A N   1 
ATOM   5687 C CA  . PRO E 1 156 ? -14.23100 65.13800 -32.30400 1.000 143.57114 ?  164 PRO A CA  1 
ATOM   5688 C C   . PRO E 1 156 ? -14.42500 66.36000 -31.41500 1.000 147.41299 ?  164 PRO A C   1 
ATOM   5689 O O   . PRO E 1 156 ? -13.49600 67.10800 -31.12400 1.000 150.02905 ?  164 PRO A O   1 
ATOM   5690 C CB  . PRO E 1 156 ? -14.18800 63.86500 -31.46200 1.000 145.15080 ?  164 PRO A CB  1 
ATOM   5691 C CG  . PRO E 1 156 ? -12.73700 63.80200 -31.02500 1.000 148.19388 ?  164 PRO A CG  1 
ATOM   5692 C CD  . PRO E 1 156 ? -11.93100 64.40800 -32.17300 1.000 145.53683 ?  164 PRO A CD  1 
ATOM   5693 N N   . VAL E 1 157 ? -15.65600 66.55400 -30.95400 1.000 144.90892 ?  165 VAL A N   1 
ATOM   5694 C CA  . VAL E 1 157 ? -16.00000 67.58500 -29.98400 1.000 148.75261 ?  165 VAL A CA  1 
ATOM   5695 C C   . VAL E 1 157 ? -16.79500 66.93800 -28.86000 1.000 152.27473 ?  165 VAL A C   1 
ATOM   5696 O O   . VAL E 1 157 ? -17.71900 66.15600 -29.11600 1.000 149.46323 ?  165 VAL A O   1 
ATOM   5697 C CB  . VAL E 1 157 ? -16.79600 68.73500 -30.62800 1.000 145.53911 ?  165 VAL A CB  1 
ATOM   5698 C CG1 . VAL E 1 157 ? -17.45600 69.59600 -29.56300 1.000 149.48887 ?  165 VAL A CG1 1 
ATOM   5699 C CG2 . VAL E 1 157 ? -15.87900 69.58500 -31.47700 1.000 143.90028 ?  165 VAL A CG2 1 
ATOM   5700 N N   . THR E 1 158 ? -16.42900 67.25100 -27.62000 1.000 152.03090 ?  166 THR A N   1 
ATOM   5701 C CA  . THR E 1 158 ? -17.11600 66.72800 -26.44600 1.000 157.58778 ?  166 THR A CA  1 
ATOM   5702 C C   . THR E 1 158 ? -17.96900 67.83300 -25.83800 1.000 160.67716 ?  166 THR A C   1 
ATOM   5703 O O   . THR E 1 158 ? -17.49500 68.95800 -25.66200 1.000 162.96074 ?  166 THR A O   1 
ATOM   5704 C CB  . THR E 1 158 ? -16.11600 66.20300 -25.41200 1.000 165.09849 ?  166 THR A CB  1 
ATOM   5705 O OG1 . THR E 1 158 ? -15.71000 67.27300 -24.55100 1.000 171.72305 ?  166 THR A OG1 1 
ATOM   5706 C CG2 . THR E 1 158 ? -14.88600 65.63200 -26.10700 1.000 162.22141 ?  166 THR A CG2 1 
ATOM   5707 N N   . VAL E 1 159 ? -19.22600 67.52000 -25.52600 1.000 159.50272 ?  167 VAL A N   1 
ATOM   5708 C CA  . VAL E 1 159 ? -20.17500 68.49300 -24.97900 1.000 162.54391 ?  167 VAL A CA  1 
ATOM   5709 C C   . VAL E 1 159 ? -20.80700 67.90800 -23.71800 1.000 169.66310 ?  167 VAL A C   1 
ATOM   5710 O O   . VAL E 1 159 ? -21.74300 67.10400 -23.79900 1.000 166.94508 ?  167 VAL A O   1 
ATOM   5711 C CB  . VAL E 1 159 ? -21.25300 68.89200 -25.99400 1.000 155.11337 ?  167 VAL A CB  1 
ATOM   5712 C CG1 . VAL E 1 159 ? -22.12600 69.99700 -25.42600 1.000 158.67211 ?  167 VAL A CG1 1 
ATOM   5713 C CG2 . VAL E 1 159 ? -20.61800 69.34500 -27.30300 1.000 148.08505 ?  167 VAL A CG2 1 
ATOM   5714 N N   . SER E 1 160 ? -20.27900 68.28200 -22.55400 1.000 164.56618 ?  168 SER A N   1 
ATOM   5715 C CA  . SER E 1 160 ? -20.91600 67.99100 -21.27700 1.000 172.64867 ?  168 SER A CA  1 
ATOM   5716 C C   . SER E 1 160 ? -21.85300 69.13800 -20.88600 1.000 176.07427 ?  168 SER A C   1 
ATOM   5717 O O   . SER E 1 160 ? -21.87100 70.19900 -21.51000 1.000 173.03138 ?  168 SER A O   1 
ATOM   5718 C CB  . SER E 1 160 ? -19.86200 67.74700 -20.19500 1.000 182.61117 ?  168 SER A CB  1 
ATOM   5719 O OG  . SER E 1 160 ? -20.41100 67.88600 -18.89600 1.000 192.06268 ?  168 SER A OG  1 
ATOM   5720 N N   . TRP E 1 161 ? -22.62200 68.93000 -19.81800 1.000 179.34422 ?  169 TRP A N   1 
ATOM   5721 C CA  . TRP E 1 161 ? -23.54000 69.94700 -19.31200 1.000 183.91313 ?  169 TRP A CA  1 
ATOM   5722 C C   . TRP E 1 161 ? -23.32700 70.16900 -17.82300 1.000 195.77904 ?  169 TRP A C   1 
ATOM   5723 O O   . TRP E 1 161 ? -23.36300 69.21400 -17.04100 1.000 198.14721 ?  169 TRP A O   1 
ATOM   5724 C CB  . TRP E 1 161 ? -24.99900 69.56400 -19.56400 1.000 178.75482 ?  169 TRP A CB  1 
ATOM   5725 C CG  . TRP E 1 161 ? -25.50900 69.94400 -20.91300 1.000 170.16191 ?  169 TRP A CG  1 
ATOM   5726 C CD1 . TRP E 1 161 ? -25.41500 69.21700 -22.05700 1.000 160.94078 ?  169 TRP A CD1 1 
ATOM   5727 C CD2 . TRP E 1 161 ? -26.19600 71.15200 -21.25800 1.000 169.88176 ?  169 TRP A CD2 1 
ATOM   5728 N NE1 . TRP E 1 161 ? -26.00800 69.89100 -23.09900 1.000 154.63190 ?  169 TRP A NE1 1 
ATOM   5729 C CE2 . TRP E 1 161 ? -26.49300 71.08400 -22.63300 1.000 159.35619 ?  169 TRP A CE2 1 
ATOM   5730 C CE3 . TRP E 1 161 ? -26.58800 72.28300 -20.53800 1.000 176.94638 ?  169 TRP A CE3 1 
ATOM   5731 C CZ2 . TRP E 1 161 ? -27.16500 72.10300 -23.30200 1.000 154.18686 ?  169 TRP A CZ2 1 
ATOM   5732 C CZ3 . TRP E 1 161 ? -27.25300 73.29400 -21.20300 1.000 171.54714 ?  169 TRP A CZ3 1 
ATOM   5733 C CH2 . TRP E 1 161 ? -27.53300 73.19700 -22.57200 1.000 159.48582 ?  169 TRP A CH2 1 
ATOM   5734 N N   . ASN E 1 162 ? -23.11100 71.43000 -17.44100 1.000 186.13539 ?  170 ASN A N   1 
ATOM   5735 C CA  . ASN E 1 162 ? -22.96800 71.83300 -16.03900 1.000 197.73567 ?  170 ASN A CA  1 
ATOM   5736 C C   . ASN E 1 162 ? -21.87800 71.02700 -15.34000 1.000 204.23705 ?  170 ASN A C   1 
ATOM   5737 O O   . ASN E 1 162 ? -22.04900 70.53800 -14.22000 1.000 208.73440 ?  170 ASN A O   1 
ATOM   5738 C CB  . ASN E 1 162 ? -24.29400 71.71600 -15.28800 1.000 195.88341 ?  170 ASN A CB  1 
ATOM   5739 C CG  . ASN E 1 162 ? -25.43100 72.41100 -16.00100 1.000 189.49538 ?  170 ASN A CG  1 
ATOM   5740 O OD1 . ASN E 1 162 ? -25.76500 72.08300 -17.14000 1.000 181.96313 ?  170 ASN A OD1 1 
ATOM   5741 N ND2 . ASN E 1 162 ? -26.02400 73.39500 -15.33500 1.000 191.34555 ?  170 ASN A ND2 1 
ATOM   5742 N N   . SER E 1 163 ? -20.73600 70.90800 -16.01200 1.000 192.20267 ?  171 SER A N   1 
ATOM   5743 C CA  . SER E 1 163 ? -19.58800 70.15400 -15.51100 1.000 198.25464 ?  171 SER A CA  1 
ATOM   5744 C C   . SER E 1 163 ? -19.98900 68.72600 -15.14300 1.000 194.96606 ?  171 SER A C   1 
ATOM   5745 O O   . SER E 1 163 ? -19.65900 68.21400 -14.07100 1.000 202.94489 ?  171 SER A O   1 
ATOM   5746 C CB  . SER E 1 163 ? -18.92400 70.86300 -14.32600 1.000 213.74348 ?  171 SER A CB  1 
ATOM   5747 O OG  . SER E 1 163 ? -19.84900 71.15300 -13.29100 1.000 217.77709 ?  171 SER A OG  1 
ATOM   5748 N N   . GLY E 1 164 ? -20.72000 68.08300 -16.05500 1.000 197.70521 ?  172 GLY A N   1 
ATOM   5749 C CA  . GLY E 1 164 ? -21.07800 66.68500 -15.94600 1.000 193.01407 ?  172 GLY A CA  1 
ATOM   5750 C C   . GLY E 1 164 ? -22.33300 66.36900 -15.15300 1.000 192.39952 ?  172 GLY A C   1 
ATOM   5751 O O   . GLY E 1 164 ? -22.94800 65.32300 -15.38600 1.000 185.76673 ?  172 GLY A O   1 
ATOM   5752 N N   . ALA E 1 165 ? -22.73200 67.24300 -14.22700 1.000 189.08443 ?  173 ALA A N   1 
ATOM   5753 C CA  . ALA E 1 165 ? -23.82200 66.90300 -13.31500 1.000 189.19120 ?  173 ALA A CA  1 
ATOM   5754 C C   . ALA E 1 165 ? -25.14900 66.75500 -14.05300 1.000 180.66876 ?  173 ALA A C   1 
ATOM   5755 O O   . ALA E 1 165 ? -25.84700 65.74600 -13.89800 1.000 177.20130 ?  173 ALA A O   1 
ATOM   5756 C CB  . ALA E 1 165 ? -23.92800 67.95900 -12.21200 1.000 196.76213 ?  173 ALA A CB  1 
ATOM   5757 N N   . LEU E 1 166 ? -25.51000 67.74300 -14.86700 1.000 190.91278 ?  174 LEU A N   1 
ATOM   5758 C CA  . LEU E 1 166 ? -26.77400 67.71200 -15.59900 1.000 183.48476 ?  174 LEU A CA  1 
ATOM   5759 C C   . LEU E 1 166 ? -26.65700 66.73600 -16.76600 1.000 175.70406 ?  174 LEU A C   1 
ATOM   5760 O O   . LEU E 1 166 ? -26.00400 67.03700 -17.77000 1.000 172.65701 ?  174 LEU A O   1 
ATOM   5761 C CB  . LEU E 1 166 ? -27.14600 69.10800 -16.09100 1.000 183.76922 ?  174 LEU A CB  1 
ATOM   5762 C CG  . LEU E 1 166 ? -28.42500 69.16900 -16.93400 1.000 177.52108 ?  174 LEU A CG  1 
ATOM   5763 C CD1 . LEU E 1 166 ? -29.56300 68.44300 -16.22400 1.000 176.64115 ?  174 LEU A CD1 1 
ATOM   5764 C CD2 . LEU E 1 166 ? -28.82100 70.59700 -17.26200 1.000 178.60790 ?  174 LEU A CD2 1 
ATOM   5765 N N   . THR E 1 167 ? -27.28200 65.56400 -16.64200 1.000 180.30771 ?  175 THR A N   1 
ATOM   5766 C CA  . THR E 1 167 ? -27.20700 64.55300 -17.69200 1.000 172.93821 ?  175 THR A CA  1 
ATOM   5767 C C   . THR E 1 167 ? -28.59300 64.07600 -18.11500 1.000 168.07809 ?  175 THR A C   1 
ATOM   5768 O O   . THR E 1 167 ? -28.81400 63.75300 -19.28800 1.000 161.97882 ?  175 THR A O   1 
ATOM   5769 C CB  . THR E 1 167 ? -26.37600 63.35600 -17.22400 1.000 173.91413 ?  175 THR A CB  1 
ATOM   5770 O OG1 . THR E 1 167 ? -26.70600 63.04600 -15.86300 1.000 179.28030 ?  175 THR A OG1 1 
ATOM   5771 C CG2 . THR E 1 167 ? -24.89000 63.67600 -17.30800 1.000 177.63284 ?  175 THR A CG2 1 
ATOM   5772 N N   . SER E 1 168 ? -29.52400 64.03000 -17.16400 1.000 164.90361 ?  176 SER A N   1 
ATOM   5773 C CA  . SER E 1 168 ? -30.86900 63.52900 -17.43200 1.000 162.51512 ?  176 SER A CA  1 
ATOM   5774 C C   . SER E 1 168 ? -31.56400 64.35800 -18.50500 1.000 160.60276 ?  176 SER A C   1 
ATOM   5775 O O   . SER E 1 168 ? -31.67100 65.58200 -18.39100 1.000 163.38942 ?  176 SER A O   1 
ATOM   5776 C CB  . SER E 1 168 ? -31.69500 63.54300 -16.14600 1.000 167.77689 ?  176 SER A CB  1 
ATOM   5777 O OG  . SER E 1 168 ? -31.54100 64.76500 -15.44300 1.000 171.78107 ?  176 SER A OG  1 
ATOM   5778 N N   . GLY E 1 169 ? -32.02500 63.68500 -19.55600 1.000 162.85944 ?  177 GLY A N   1 
ATOM   5779 C CA  . GLY E 1 169 ? -32.78000 64.34700 -20.60000 1.000 162.15247 ?  177 GLY A CA  1 
ATOM   5780 C C   . GLY E 1 169 ? -31.97100 65.23300 -21.51900 1.000 159.72923 ?  177 GLY A C   1 
ATOM   5781 O O   . GLY E 1 169 ? -32.53900 66.12800 -22.14800 1.000 159.62023 ?  177 GLY A O   1 
ATOM   5782 N N   . VAL E 1 170 ? -30.66000 65.00900 -21.61800 1.000 158.84385 ?  178 VAL A N   1 
ATOM   5783 C CA  . VAL E 1 170 ? -29.81500 65.72800 -22.56400 1.000 154.91907 ?  178 VAL A CA  1 
ATOM   5784 C C   . VAL E 1 170 ? -29.66400 64.88300 -23.81800 1.000 146.10061 ?  178 VAL A C   1 
ATOM   5785 O O   . VAL E 1 170 ? -29.45800 63.66600 -23.75200 1.000 144.17472 ?  178 VAL A O   1 
ATOM   5786 C CB  . VAL E 1 170 ? -28.44300 66.07700 -21.95800 1.000 157.93862 ?  178 VAL A CB  1 
ATOM   5787 C CG1 . VAL E 1 170 ? -27.71000 67.02600 -22.88900 1.000 154.57336 ?  178 VAL A CG1 1 
ATOM   5788 C CG2 . VAL E 1 170 ? -28.59000 66.67800 -20.56900 1.000 166.28584 ?  178 VAL A CG2 1 
ATOM   5789 N N   . HIS E 1 171 ? -29.79800 65.53700 -24.96800 1.000 162.84885 ?  179 HIS A N   1 
ATOM   5790 C CA  . HIS E 1 171 ? -29.73700 64.92200 -26.28900 1.000 152.01416 ?  179 HIS A CA  1 
ATOM   5791 C C   . HIS E 1 171 ? -28.74200 65.72500 -27.12700 1.000 147.39818 ?  179 HIS A C   1 
ATOM   5792 O O   . HIS E 1 171 ? -29.09300 66.72100 -27.77400 1.000 142.00920 ?  179 HIS A O   1 
ATOM   5793 C CB  . HIS E 1 171 ? -31.12400 64.84800 -26.91100 1.000 144.16183 ?  179 HIS A CB  1 
ATOM   5794 C CG  . HIS E 1 171 ? -32.17700 64.37500 -25.95500 1.000 150.49633 ?  179 HIS A CG  1 
ATOM   5795 N ND1 . HIS E 1 171 ? -32.55400 63.05300 -25.85100 1.000 149.40572 ?  179 HIS A ND1 1 
ATOM   5796 C CD2 . HIS E 1 171 ? -32.92600 65.05000 -25.05100 1.000 158.03703 ?  179 HIS A CD2 1 
ATOM   5797 C CE1 . HIS E 1 171 ? -33.49300 62.93500 -24.93000 1.000 156.42750 ?  179 HIS A CE1 1 
ATOM   5798 N NE2 . HIS E 1 171 ? -33.73800 64.13200 -24.42900 1.000 161.93586 ?  179 HIS A NE2 1 
ATOM   5799 N N   . THR E 1 172 ? -27.46500 65.40800 -26.94400 1.000 144.85178 ?  180 THR A N   1 
ATOM   5800 C CA  . THR E 1 172 ? -26.42300 65.88700 -27.83700 1.000 140.39503 ?  180 THR A CA  1 
ATOM   5801 C C   . THR E 1 172 ? -26.59500 65.21900 -29.19700 1.000 130.01339 ?  180 THR A C   1 
ATOM   5802 O O   . THR E 1 172 ? -26.31700 64.02700 -29.35000 1.000 128.23808 ?  180 THR A O   1 
ATOM   5803 C CB  . THR E 1 172 ? -25.04700 65.58200 -27.25400 1.000 145.32010 ?  180 THR A CB  1 
ATOM   5804 O OG1 . THR E 1 172 ? -24.98500 66.05100 -25.90100 1.000 153.95622 ?  180 THR A OG1 1 
ATOM   5805 C CG2 . THR E 1 172 ? -23.96400 66.24900 -28.07700 1.000 142.21290 ?  180 THR A CG2 1 
ATOM   5806 N N   . PHE E 1 173 ? -27.05600 65.97700 -30.18200 1.000 134.50536 ?  181 PHE A N   1 
ATOM   5807 C CA  . PHE E 1 173 ? -27.30200 65.41400 -31.49800 1.000 142.17053 ?  181 PHE A CA  1 
ATOM   5808 C C   . PHE E 1 173 ? -25.97400 65.14100 -32.20300 1.000 142.17244 ?  181 PHE A C   1 
ATOM   5809 O O   . PHE E 1 173 ? -24.95500 65.75300 -31.87500 1.000 137.82252 ?  181 PHE A O   1 
ATOM   5810 C CB  . PHE E 1 173 ? -28.15500 66.36600 -32.32200 1.000 151.59420 ?  181 PHE A CB  1 
ATOM   5811 C CG  . PHE E 1 173 ? -29.60100 66.33600 -31.95000 1.000 152.80641 ?  181 PHE A CG  1 
ATOM   5812 C CD1 . PHE E 1 173 ? -30.07800 67.13200 -30.92600 1.000 150.67908 ?  181 PHE A CD1 1 
ATOM   5813 C CD2 . PHE E 1 173 ? -30.47400 65.47100 -32.58300 1.000 152.80093 ?  181 PHE A CD2 1 
ATOM   5814 C CE1 . PHE E 1 173 ? -31.41100 67.09900 -30.56800 1.000 150.80359 ?  181 PHE A CE1 1 
ATOM   5815 C CE2 . PHE E 1 173 ? -31.81000 65.43800 -32.23100 1.000 153.52613 ?  181 PHE A CE2 1 
ATOM   5816 C CZ  . PHE E 1 173 ? -32.27700 66.25000 -31.22200 1.000 152.72305 ?  181 PHE A CZ  1 
ATOM   5817 N N   . PRO E 1 174 ? -25.94800 64.20500 -33.15000 1.000 142.71181 ?  182 PRO A N   1 
ATOM   5818 C CA  . PRO E 1 174 ? -24.72400 63.99400 -33.93000 1.000 143.39469 ?  182 PRO A CA  1 
ATOM   5819 C C   . PRO E 1 174 ? -24.35300 65.23700 -34.72200 1.000 150.16005 ?  182 PRO A C   1 
ATOM   5820 O O   . PRO E 1 174 ? -25.13900 66.17000 -34.89000 1.000 155.14672 ?  182 PRO A O   1 
ATOM   5821 C CB  . PRO E 1 174 ? -25.09400 62.83400 -34.85900 1.000 143.15577 ?  182 PRO A CB  1 
ATOM   5822 C CG  . PRO E 1 174 ? -26.13800 62.08600 -34.11600 1.000 139.14627 ?  182 PRO A CG  1 
ATOM   5823 C CD  . PRO E 1 174 ? -26.93600 63.13900 -33.38800 1.000 141.69316 ?  182 PRO A CD  1 
ATOM   5824 N N   . ALA E 1 175 ? -23.12700 65.23400 -35.22800 1.000 149.93250 ?  183 ALA A N   1 
ATOM   5825 C CA  . ALA E 1 175 ? -22.63100 66.35200 -36.01100 1.000 155.33895 ?  183 ALA A CA  1 
ATOM   5826 C C   . ALA E 1 175 ? -23.02900 66.18800 -37.47000 1.000 157.67896 ?  183 ALA A C   1 
ATOM   5827 O O   . ALA E 1 175 ? -23.33500 65.09000 -37.94000 1.000 154.68595 ?  183 ALA A O   1 
ATOM   5828 C CB  . ALA E 1 175 ? -21.11100 66.47600 -35.89500 1.000 150.14733 ?  183 ALA A CB  1 
ATOM   5829 N N   . VAL E 1 176 ? -23.03600 67.30300 -38.18800 1.000 160.99256 ?  184 VAL A N   1 
ATOM   5830 C CA  . VAL E 1 176 ? -23.23000 67.29000 -39.62900 1.000 161.65112 ?  184 VAL A CA  1 
ATOM   5831 C C   . VAL E 1 176 ? -22.05300 68.00100 -40.27300 1.000 162.27243 ?  184 VAL A C   1 
ATOM   5832 O O   . VAL E 1 176 ? -21.64000 69.07500 -39.82500 1.000 163.51434 ?  184 VAL A O   1 
ATOM   5833 C CB  . VAL E 1 176 ? -24.56800 67.93800 -40.05100 1.000 164.58152 ?  184 VAL A CB  1 
ATOM   5834 C CG1 . VAL E 1 176 ? -25.73400 67.05400 -39.64500 1.000 162.99757 ?  184 VAL A CG1 1 
ATOM   5835 C CG2 . VAL E 1 176 ? -24.72000 69.32800 -39.44100 1.000 167.67834 ?  184 VAL A CG2 1 
ATOM   5836 N N   . LEU E 1 177 ? -21.51100 67.39600 -41.32200 1.000 162.84503 ?  185 LEU A N   1 
ATOM   5837 C CA  . LEU E 1 177 ? -20.49700 68.06200 -42.12800 1.000 163.05593 ?  185 LEU A CA  1 
ATOM   5838 C C   . LEU E 1 177 ? -21.25200 68.98700 -43.06100 1.000 166.00275 ?  185 LEU A C   1 
ATOM   5839 O O   . LEU E 1 177 ? -21.72600 68.58200 -44.12400 1.000 166.06975 ?  185 LEU A O   1 
ATOM   5840 C CB  . LEU E 1 177 ? -19.64100 67.06200 -42.89300 1.000 159.75356 ?  185 LEU A CB  1 
ATOM   5841 C CG  . LEU E 1 177 ? -18.22700 67.53800 -43.23000 1.000 158.50006 ?  185 LEU A CG  1 
ATOM   5842 C CD1 . LEU E 1 177 ? -17.63500 68.35300 -42.08800 1.000 158.75351 ?  185 LEU A CD1 1 
ATOM   5843 C CD2 . LEU E 1 177 ? -17.33200 66.36100 -43.58600 1.000 154.56202 ?  185 LEU A CD2 1 
ATOM   5844 N N   . GLN E 1 178 ? -21.39500 70.24000 -42.63900 1.000 164.87753 ?  186 GLN A N   1 
ATOM   5845 C CA  . GLN E 1 178 ? -22.08600 71.21500 -43.46500 1.000 167.30735 ?  186 GLN A CA  1 
ATOM   5846 C C   . GLN E 1 178 ? -21.38300 71.30900 -44.80900 1.000 166.30781 ?  186 GLN A C   1 
ATOM   5847 O O   . GLN E 1 178 ? -20.15500 71.21400 -44.88900 1.000 164.02463 ?  186 GLN A O   1 
ATOM   5848 C CB  . GLN E 1 178 ? -22.10400 72.58100 -42.78100 1.000 168.43606 ?  186 GLN A CB  1 
ATOM   5849 C CG  . GLN E 1 178 ? -22.11100 72.50600 -41.27000 1.000 167.57856 ?  186 GLN A CG  1 
ATOM   5850 C CD  . GLN E 1 178 ? -21.72500 73.82400 -40.62300 1.000 165.48629 ?  186 GLN A CD  1 
ATOM   5851 O OE1 . GLN E 1 178 ? -22.56800 74.69400 -40.40100 1.000 166.52086 ?  186 GLN A OE1 1 
ATOM   5852 N NE2 . GLN E 1 178 ? -20.43800 73.98000 -40.32800 1.000 161.07778 ?  186 GLN A NE2 1 
ATOM   5853 N N   . SER E 1 179 ? -22.17800 71.46400 -45.86900 1.000 168.58850 ?  187 SER A N   1 
ATOM   5854 C CA  . SER E 1 179 ? -21.63500 71.50800 -47.22200 1.000 167.57572 ?  187 SER A CA  1 
ATOM   5855 C C   . SER E 1 179 ? -20.44800 72.45700 -47.34000 1.000 166.03692 ?  187 SER A C   1 
ATOM   5856 O O   . SER E 1 179 ? -19.60500 72.28700 -48.22700 1.000 164.61360 ?  187 SER A O   1 
ATOM   5857 C CB  . SER E 1 179 ? -22.72900 71.89100 -48.21600 1.000 169.62050 ?  187 SER A CB  1 
ATOM   5858 O OG  . SER E 1 179 ? -22.89700 73.29400 -48.27900 1.000 170.53955 ?  187 SER A OG  1 
ATOM   5859 N N   . SER E 1 180 ? -20.36500 73.45900 -46.46100 1.000 172.05230 ?  188 SER A N   1 
ATOM   5860 C CA  . SER E 1 180 ? -19.17900 74.30900 -46.41400 1.000 169.51865 ?  188 SER A CA  1 
ATOM   5861 C C   . SER E 1 180 ? -17.90900 73.49700 -46.18000 1.000 166.62280 ?  188 SER A C   1 
ATOM   5862 O O   . SER E 1 180 ? -16.84000 73.86100 -46.68200 1.000 163.97595 ?  188 SER A O   1 
ATOM   5863 C CB  . SER E 1 180 ? -19.34300 75.36500 -45.31900 1.000 169.41210 ?  188 SER A CB  1 
ATOM   5864 O OG  . SER E 1 180 ? -19.43700 74.76400 -44.04000 1.000 169.44076 ?  188 SER A OG  1 
ATOM   5865 N N   . GLY E 1 181 ? -18.00100 72.40200 -45.43300 1.000 165.74601 ?  189 GLY A N   1 
ATOM   5866 C CA  . GLY E 1 181 ? -16.84000 71.61900 -45.06600 1.000 162.67699 ?  189 GLY A CA  1 
ATOM   5867 C C   . GLY E 1 181 ? -16.46000 71.71200 -43.60800 1.000 161.46270 ?  189 GLY A C   1 
ATOM   5868 O O   . GLY E 1 181 ? -15.42000 71.16500 -43.21700 1.000 158.66066 ?  189 GLY A O   1 
ATOM   5869 N N   . LEU E 1 182 ? -17.25700 72.39500 -42.79800 1.000 163.06449 ?  190 LEU A N   1 
ATOM   5870 C CA  . LEU E 1 182 ? -17.04000 72.49100 -41.36700 1.000 160.66791 ?  190 LEU A CA  1 
ATOM   5871 C C   . LEU E 1 182 ? -18.07700 71.63300 -40.65500 1.000 162.65374 ?  190 LEU A C   1 
ATOM   5872 O O   . LEU E 1 182 ? -19.17100 71.40100 -41.17600 1.000 166.21716 ?  190 LEU A O   1 
ATOM   5873 C CB  . LEU E 1 182 ? -17.13000 73.95400 -40.91600 1.000 158.34630 ?  190 LEU A CB  1 
ATOM   5874 C CG  . LEU E 1 182 ? -15.86300 74.77200 -41.19900 1.000 154.09801 ?  190 LEU A CG  1 
ATOM   5875 C CD1 . LEU E 1 182 ? -16.13900 76.26600 -41.18800 1.000 152.89894 ?  190 LEU A CD1 1 
ATOM   5876 C CD2 . LEU E 1 182 ? -14.76100 74.42700 -40.21500 1.000 149.06342 ?  190 LEU A CD2 1 
ATOM   5877 N N   . TYR E 1 183 ? -17.72600 71.15000 -39.47000 1.000 158.92216 ?  191 TYR A N   1 
ATOM   5878 C CA  . TYR E 1 183 ? -18.64800 70.33500 -38.69400 1.000 159.66859 ?  191 TYR A CA  1 
ATOM   5879 C C   . TYR E 1 183 ? -19.58400 71.24200 -37.89800 1.000 158.35994 ?  191 TYR A C   1 
ATOM   5880 O O   . TYR E 1 183 ? -19.26700 72.39700 -37.60600 1.000 154.29667 ?  191 TYR A O   1 
ATOM   5881 C CB  . TYR E 1 183 ? -17.88800 69.40900 -37.74000 1.000 153.32248 ?  191 TYR A CB  1 
ATOM   5882 C CG  . TYR E 1 183 ? -17.19300 68.21600 -38.37300 1.000 155.14625 ?  191 TYR A CG  1 
ATOM   5883 C CD1 . TYR E 1 183 ? -17.90500 67.08800 -38.76400 1.000 158.50716 ?  191 TYR A CD1 1 
ATOM   5884 C CD2 . TYR E 1 183 ? -15.81400 68.20900 -38.54700 1.000 151.48228 ?  191 TYR A CD2 1 
ATOM   5885 C CE1 . TYR E 1 183 ? -17.26300 65.99400 -39.32900 1.000 156.15799 ?  191 TYR A CE1 1 
ATOM   5886 C CE2 . TYR E 1 183 ? -15.16500 67.12100 -39.11000 1.000 152.70437 ?  191 TYR A CE2 1 
ATOM   5887 C CZ  . TYR E 1 183 ? -15.89300 66.01700 -39.49900 1.000 154.22447 ?  191 TYR A CZ  1 
ATOM   5888 O OH  . TYR E 1 183 ? -15.24600 64.93600 -40.05800 1.000 151.07367 ?  191 TYR A OH  1 
ATOM   5889 N N   . SER E 1 184 ? -20.75900 70.71500 -37.55700 1.000 155.89233 ?  192 SER A N   1 
ATOM   5890 C CA  . SER E 1 184 ? -21.71600 71.48100 -36.76700 1.000 154.52612 ?  192 SER A CA  1 
ATOM   5891 C C   . SER E 1 184 ? -22.60600 70.54000 -35.96800 1.000 154.41420 ?  192 SER A C   1 
ATOM   5892 O O   . SER E 1 184 ? -23.03900 69.50600 -36.48500 1.000 159.45380 ?  192 SER A O   1 
ATOM   5893 C CB  . SER E 1 184 ? -22.58000 72.38300 -37.65600 1.000 160.87526 ?  192 SER A CB  1 
ATOM   5894 O OG  . SER E 1 184 ? -23.24700 73.36700 -36.88500 1.000 158.39306 ?  192 SER A OG  1 
ATOM   5895 N N   . LEU E 1 185 ? -22.89800 70.91600 -34.72200 1.000 160.53568 ?  193 LEU A N   1 
ATOM   5896 C CA  . LEU E 1 185 ? -23.75300 70.09300 -33.87900 1.000 159.03886 ?  193 LEU A CA  1 
ATOM   5897 C C   . LEU E 1 185 ? -24.60300 70.98400 -32.98000 1.000 156.42236 ?  193 LEU A C   1 
ATOM   5898 O O   . LEU E 1 185 ? -24.40100 72.20200 -32.88900 1.000 154.61705 ?  193 LEU A O   1 
ATOM   5899 C CB  . LEU E 1 185 ? -22.93000 69.11800 -33.02900 1.000 150.71934 ?  193 LEU A CB  1 
ATOM   5900 C CG  . LEU E 1 185 ? -21.98200 69.74200 -32.00000 1.000 142.10580 ?  193 LEU A CG  1 
ATOM   5901 C CD1 . LEU E 1 185 ? -22.63300 69.82100 -30.62600 1.000 137.35521 ?  193 LEU A CD1 1 
ATOM   5902 C CD2 . LEU E 1 185 ? -20.67700 68.97200 -31.92600 1.000 137.64179 ?  193 LEU A CD2 1 
ATOM   5903 N N   . SER E 1 186 ? -25.52100 70.33600 -32.26500 1.000 149.99875 ?  194 SER A N   1 
ATOM   5904 C CA  . SER E 1 186 ? -26.49700 71.01300 -31.41500 1.000 148.53937 ?  194 SER A CA  1 
ATOM   5905 C C   . SER E 1 186 ? -26.89600 70.07000 -30.28900 1.000 143.21929 ?  194 SER A C   1 
ATOM   5906 O O   . SER E 1 186 ? -27.40900 68.97800 -30.55100 1.000 146.01781 ?  194 SER A O   1 
ATOM   5907 C CB  . SER E 1 186 ? -27.72400 71.43300 -32.22800 1.000 158.47624 ?  194 SER A CB  1 
ATOM   5908 O OG  . SER E 1 186 ? -28.08900 70.42600 -33.15700 1.000 165.78705 ?  194 SER A OG  1 
ATOM   5909 N N   . SER E 1 187 ? -26.65800 70.47900 -29.04600 1.000 159.38053 ?  195 SER A N   1 
ATOM   5910 C CA  . SER E 1 187 ? -27.03200 69.68100 -27.88100 1.000 154.28780 ?  195 SER A CA  1 
ATOM   5911 C C   . SER E 1 187 ? -28.15500 70.36200 -27.11100 1.000 155.02580 ?  195 SER A C   1 
ATOM   5912 O O   . SER E 1 187 ? -28.05000 71.54400 -26.78200 1.000 154.70242 ?  195 SER A O   1 
ATOM   5913 C CB  . SER E 1 187 ? -25.83300 69.45000 -26.96300 1.000 147.75358 ?  195 SER A CB  1 
ATOM   5914 O OG  . SER E 1 187 ? -26.25800 68.94900 -25.70900 1.000 143.75194 ?  195 SER A OG  1 
ATOM   5915 N N   . VAL E 1 188 ? -29.21000 69.61800 -26.77800 1.000 155.11718 ?  196 VAL A N   1 
ATOM   5916 C CA  . VAL E 1 188 ? -30.34500 70.20500 -26.06600 1.000 156.21641 ?  196 VAL A CA  1 
ATOM   5917 C C   . VAL E 1 188 ? -30.60700 69.40200 -24.79900 1.000 150.75615 ?  196 VAL A C   1 
ATOM   5918 O O   . VAL E 1 188 ? -30.08200 68.31000 -24.61100 1.000 146.69920 ?  196 VAL A O   1 
ATOM   5919 C CB  . VAL E 1 188 ? -31.62900 70.27100 -26.92100 1.000 164.24076 ?  196 VAL A CB  1 
ATOM   5920 C CG1 . VAL E 1 188 ? -31.50200 71.33800 -28.00600 1.000 170.46420 ?  196 VAL A CG1 1 
ATOM   5921 C CG2 . VAL E 1 188 ? -31.94400 68.91100 -27.51100 1.000 166.67697 ?  196 VAL A CG2 1 
ATOM   5922 N N   . VAL E 1 189 ? -31.39100 69.99000 -23.89600 1.000 163.44964 ?  197 VAL A N   1 
ATOM   5923 C CA  . VAL E 1 189 ? -31.78000 69.30500 -22.66700 1.000 159.20629 ?  197 VAL A CA  1 
ATOM   5924 C C   . VAL E 1 189 ? -33.15600 69.76000 -22.20100 1.000 162.04292 ?  197 VAL A C   1 
ATOM   5925 O O   . VAL E 1 189 ? -33.39200 70.95100 -21.97200 1.000 163.76116 ?  197 VAL A O   1 
ATOM   5926 C CB  . VAL E 1 189 ? -30.72700 69.50100 -21.55600 1.000 154.13186 ?  197 VAL A CB  1 
ATOM   5927 C CG1 . VAL E 1 189 ? -30.40300 70.96800 -21.36500 1.000 155.84225 ?  197 VAL A CG1 1 
ATOM   5928 C CG2 . VAL E 1 189 ? -31.23400 68.91700 -20.23900 1.000 150.80015 ?  197 VAL A CG2 1 
ATOM   5929 N N   . THR E 1 190 ? -34.07800 68.80700 -22.06700 1.000 164.99658 ?  198 THR A N   1 
ATOM   5930 C CA  . THR E 1 190 ? -35.38600 69.12700 -21.51700 1.000 167.39635 ?  198 THR A CA  1 
ATOM   5931 C C   . THR E 1 190 ? -35.21400 69.33800 -20.01900 1.000 162.39266 ?  198 THR A C   1 
ATOM   5932 O O   . THR E 1 190 ? -34.86300 68.40900 -19.28300 1.000 157.67097 ?  198 THR A O   1 
ATOM   5933 C CB  . THR E 1 190 ? -36.39200 68.01400 -21.80700 1.000 169.07534 ?  198 THR A CB  1 
ATOM   5934 O OG1 . THR E 1 190 ? -36.02000 66.82800 -21.09600 1.000 163.01182 ?  198 THR A OG1 1 
ATOM   5935 C CG2 . THR E 1 190 ? -36.43200 67.71600 -23.30100 1.000 173.99422 ?  198 THR A CG2 1 
ATOM   5936 N N   . VAL E 1 191 ? -35.44700 70.56800 -19.58300 1.000 174.72605 ?  199 VAL A N   1 
ATOM   5937 C CA  . VAL E 1 191 ? -35.22900 71.02200 -18.21600 1.000 171.18896 ?  199 VAL A CA  1 
ATOM   5938 C C   . VAL E 1 191 ? -36.58400 71.44200 -17.66200 1.000 172.78580 ?  199 VAL A C   1 
ATOM   5939 O O   . VAL E 1 191 ? -37.47500 71.82800 -18.43500 1.000 176.84241 ?  199 VAL A O   1 
ATOM   5940 C CB  . VAL E 1 191 ? -34.21800 72.17900 -18.16300 1.000 170.83037 ?  199 VAL A CB  1 
ATOM   5941 C CG1 . VAL E 1 191 ? -32.85400 71.72400 -18.67200 1.000 169.35625 ?  199 VAL A CG1 1 
ATOM   5942 C CG2 . VAL E 1 191 ? -34.73700 73.36000 -18.96700 1.000 174.46717 ?  199 VAL A CG2 1 
ATOM   5943 N N   . PRO E 1 192 ? -36.81700 71.32100 -16.35800 1.000 184.35464 ?  200 PRO A N   1 
ATOM   5944 C CA  . PRO E 1 192 ? -38.11000 71.74900 -15.82200 1.000 185.68261 ?  200 PRO A CA  1 
ATOM   5945 C C   . PRO E 1 192 ? -38.31700 73.23400 -16.08600 1.000 187.57807 ?  200 PRO A C   1 
ATOM   5946 O O   . PRO E 1 192 ? -37.40000 74.04600 -15.94400 1.000 186.62106 ?  200 PRO A O   1 
ATOM   5947 C CB  . PRO E 1 192 ? -37.99600 71.43800 -14.32300 1.000 182.78771 ?  200 PRO A CB  1 
ATOM   5948 C CG  . PRO E 1 192 ? -36.87700 70.42800 -14.22900 1.000 180.22083 ?  200 PRO A CG  1 
ATOM   5949 C CD  . PRO E 1 192 ? -35.92100 70.81700 -15.30500 1.000 180.79992 ?  200 PRO A CD  1 
ATOM   5950 N N   . SER E 1 193 ? -39.53900 73.57800 -16.49700 1.000 195.65339 ?  201 SER A N   1 
ATOM   5951 C CA  . SER E 1 193 ? -39.87500 74.98100 -16.71100 1.000 190.24532 ?  201 SER A CA  1 
ATOM   5952 C C   . SER E 1 193 ? -39.81200 75.75000 -15.40100 1.000 201.34507 ?  201 SER A C   1 
ATOM   5953 O O   . SER E 1 193 ? -39.41200 76.92000 -15.37700 1.000 202.56452 ?  201 SER A O   1 
ATOM   5954 C CB  . SER E 1 193 ? -41.25300 75.10700 -17.35600 1.000 185.30248 ?  201 SER A CB  1 
ATOM   5955 O OG  . SER E 1 193 ? -41.41100 74.16100 -18.39700 1.000 175.88294 ?  201 SER A OG  1 
ATOM   5956 N N   . SER E 1 194 ? -40.23200 75.11400 -14.30600 1.000 207.95586 ?  202 SER A N   1 
ATOM   5957 C CA  . SER E 1 194 ? -40.10300 75.72300 -12.98600 1.000 219.27474 ?  202 SER A CA  1 
ATOM   5958 C C   . SER E 1 194 ? -38.66500 76.13900 -12.69900 1.000 220.47896 ?  202 SER A C   1 
ATOM   5959 O O   . SER E 1 194 ? -38.42700 77.17900 -12.07200 1.000 226.98143 ?  202 SER A O   1 
ATOM   5960 C CB  . SER E 1 194 ? -40.59500 74.75100 -11.91200 1.000 226.95415 ?  202 SER A CB  1 
ATOM   5961 O OG  . SER E 1 194 ? -39.70500 73.65400 -11.76500 1.000 225.15978 ?  202 SER A OG  1 
ATOM   5962 N N   . SER E 1 195 ? -37.69200 75.33100 -13.13800 1.000 214.58352 ?  203 SER A N   1 
ATOM   5963 C CA  . SER E 1 195 ? -36.29000 75.68000 -12.91600 1.000 215.47378 ?  203 SER A CA  1 
ATOM   5964 C C   . SER E 1 195 ? -35.93900 76.99600 -13.60200 1.000 212.32828 ?  203 SER A C   1 
ATOM   5965 O O   . SER E 1 195 ? -35.16100 77.79000 -13.06400 1.000 217.18266 ?  203 SER A O   1 
ATOM   5966 C CB  . SER E 1 195 ? -35.37400 74.54900 -13.39200 1.000 209.19428 ?  203 SER A CB  1 
ATOM   5967 O OG  . SER E 1 195 ? -35.26200 74.53200 -14.80300 1.000 199.80842 ?  203 SER A OG  1 
ATOM   5968 N N   . LEU E 1 196 ? -36.50400 77.23700 -14.79100 1.000 214.06644 ?  204 LEU A N   1 
ATOM   5969 C CA  . LEU E 1 196 ? -36.38300 78.50800 -15.50800 1.000 203.21907 ?  204 LEU A CA  1 
ATOM   5970 C C   . LEU E 1 196 ? -34.95700 79.04900 -15.49200 1.000 205.70138 ?  204 LEU A C   1 
ATOM   5971 O O   . LEU E 1 196 ? -34.06700 78.50500 -16.15400 1.000 205.58120 ?  204 LEU A O   1 
ATOM   5972 C CB  . LEU E 1 196 ? -37.35100 79.53500 -14.91200 1.000 208.69260 ?  204 LEU A CB  1 
ATOM   5973 N N   . GLY E 1 197 ? -34.73600 80.12800 -14.74300 1.000 209.26599 ?  205 GLY A N   1 
ATOM   5974 C CA  . GLY E 1 197 ? -33.40300 80.63400 -14.50400 1.000 211.31201 ?  205 GLY A CA  1 
ATOM   5975 C C   . GLY E 1 197 ? -32.96700 80.44900 -13.07000 1.000 220.93744 ?  205 GLY A C   1 
ATOM   5976 O O   . GLY E 1 197 ? -31.91500 80.97600 -12.68300 1.000 224.23278 ?  205 GLY A O   1 
ATOM   5977 N N   . THR E 1 198 ? -33.75200 79.73800 -12.25700 1.000 225.90535 ?  206 THR A N   1 
ATOM   5978 C CA  . THR E 1 198 ? -33.37300 79.45600 -10.87700 1.000 235.22878 ?  206 THR A CA  1 
ATOM   5979 C C   . THR E 1 198 ? -32.22200 78.46000 -10.81900 1.000 232.73249 ?  206 THR A C   1 
ATOM   5980 O O   . THR E 1 198 ? -31.28900 78.62100 -10.02200 1.000 238.17588 ?  206 THR A O   1 
ATOM   5981 C CB  . THR E 1 198 ? -34.58000 78.93400 -10.10100 1.000 241.19824 ?  206 THR A CB  1 
ATOM   5982 O OG1 . THR E 1 198 ? -34.71900 77.52300 -10.32100 1.000 236.96158 ?  206 THR A OG1 1 
ATOM   5983 C CG2 . THR E 1 198 ? -35.85000 79.65000 -10.55000 1.000 240.58705 ?  206 THR A CG2 1 
ATOM   5984 N N   . GLN E 1 199 ? -32.27400 77.42300 -11.65100 1.000 224.70987 ?  207 GLN A N   1 
ATOM   5985 C CA  . GLN E 1 199 ? -31.16700 76.49100 -11.80300 1.000 221.21044 ?  207 GLN A CA  1 
ATOM   5986 C C   . GLN E 1 199 ? -30.23500 77.00700 -12.88800 1.000 214.01090 ?  207 GLN A C   1 
ATOM   5987 O O   . GLN E 1 199 ? -30.67600 77.30600 -14.00300 1.000 206.95913 ?  207 GLN A O   1 
ATOM   5988 C CB  . GLN E 1 199 ? -31.67600 75.09400 -12.16200 1.000 216.52257 ?  207 GLN A CB  1 
ATOM   5989 N N   . THR E 1 200 ? -28.95100 77.10800 -12.56100 1.000 216.02967 ?  208 THR A N   1 
ATOM   5990 C CA  . THR E 1 200 ? -27.98400 77.55600 -13.54800 1.000 209.96207 ?  208 THR A CA  1 
ATOM   5991 C C   . THR E 1 200 ? -27.80000 76.49300 -14.62400 1.000 201.32575 ?  208 THR A C   1 
ATOM   5992 O O   . THR E 1 200 ? -27.93000 75.29200 -14.37300 1.000 202.45672 ?  208 THR A O   1 
ATOM   5993 C CB  . THR E 1 200 ? -26.65400 77.87200 -12.86500 1.000 215.01156 ?  208 THR A CB  1 
ATOM   5994 O OG1 . THR E 1 200 ? -26.26100 76.75800 -12.05400 1.000 218.30353 ?  208 THR A OG1 1 
ATOM   5995 C CG2 . THR E 1 200 ? -26.80700 79.09200 -11.97300 1.000 223.37391 ?  208 THR A CG2 1 
ATOM   5996 N N   . TYR E 1 201 ? -27.48200 76.95400 -15.83400 1.000 203.00706 ?  209 TYR A N   1 
ATOM   5997 C CA  . TYR E 1 201 ? -27.38900 76.08800 -17.00900 1.000 202.63663 ?  209 TYR A CA  1 
ATOM   5998 C C   . TYR E 1 201 ? -26.22500 76.53500 -17.88600 1.000 201.13335 ?  209 TYR A C   1 
ATOM   5999 O O   . TYR E 1 201 ? -26.31600 77.57100 -18.55200 1.000 188.73223 ?  209 TYR A O   1 
ATOM   6000 C CB  . TYR E 1 201 ? -28.69900 76.10100 -17.79200 1.000 193.09178 ?  209 TYR A CB  1 
ATOM   6001 C CG  . TYR E 1 201 ? -29.81100 75.33100 -17.11800 1.000 194.91542 ?  209 TYR A CG  1 
ATOM   6002 C CD1 . TYR E 1 201 ? -29.59500 74.05100 -16.62800 1.000 198.00455 ?  209 TYR A CD1 1 
ATOM   6003 C CD2 . TYR E 1 201 ? -31.07700 75.88200 -16.97700 1.000 189.20057 ?  209 TYR A CD2 1 
ATOM   6004 C CE1 . TYR E 1 201 ? -30.60600 73.34400 -16.01100 1.000 195.14306 ?  209 TYR A CE1 1 
ATOM   6005 C CE2 . TYR E 1 201 ? -32.09700 75.18100 -16.36500 1.000 191.73099 ?  209 TYR A CE2 1 
ATOM   6006 C CZ  . TYR E 1 201 ? -31.85500 73.91200 -15.88400 1.000 195.35214 ?  209 TYR A CZ  1 
ATOM   6007 O OH  . TYR E 1 201 ? -32.86500 73.20600 -15.27300 1.000 194.35370 ?  209 TYR A OH  1 
ATOM   6008 N N   . ILE E 1 202 ? -25.14000 75.76500 -17.89400 1.000 193.13552 ?  210 ILE A N   1 
ATOM   6009 C CA  . ILE E 1 202 ? -23.95600 76.07900 -18.68500 1.000 190.91926 ?  210 ILE A CA  1 
ATOM   6010 C C   . ILE E 1 202 ? -23.51700 74.81500 -19.41400 1.000 187.58751 ?  210 ILE A C   1 
ATOM   6011 O O   . ILE E 1 202 ? -23.30900 73.77200 -18.78400 1.000 186.25089 ?  210 ILE A O   1 
ATOM   6012 C CB  . ILE E 1 202 ? -22.81700 76.62200 -17.80000 1.000 192.88617 ?  210 ILE A CB  1 
ATOM   6013 C CG1 . ILE E 1 202 ? -23.26700 77.89100 -17.06400 1.000 189.75040 ?  210 ILE A CG1 1 
ATOM   6014 C CG2 . ILE E 1 202 ? -21.57300 76.90100 -18.63100 1.000 189.74399 ?  210 ILE A CG2 1 
ATOM   6015 C CD1 . ILE E 1 202 ? -23.64700 77.65900 -15.61500 1.000 197.76672 ?  210 ILE A CD1 1 
ATOM   6016 N N   . CYS E 1 203 ? -23.35900 74.91000 -20.73400 1.000 195.89349 ?  211 CYS A N   1 
ATOM   6017 C CA  . CYS E 1 203 ? -22.86500 73.78600 -21.52100 1.000 183.17638 ?  211 CYS A CA  1 
ATOM   6018 C C   . CYS E 1 203 ? -21.36100 73.91700 -21.72600 1.000 189.06780 ?  211 CYS A C   1 
ATOM   6019 O O   . CYS E 1 203 ? -20.85900 74.99500 -22.07300 1.000 192.29358 ?  211 CYS A O   1 
ATOM   6020 C CB  . CYS E 1 203 ? -23.59500 73.68400 -22.86500 1.000 157.59835 ?  211 CYS A CB  1 
ATOM   6021 S SG  . CYS E 1 203 ? -23.03100 74.80600 -24.16400 1.000 144.19769 ?  211 CYS A SG  1 
ATOM   6022 N N   . ASN E 1 204 ? -20.67400 72.79800 -21.46900 1.000 182.94821 ?  212 ASN A N   1 
ATOM   6023 C CA  . ASN E 1 204 ? -19.19400 72.76600 -21.54600 1.000 188.50115 ?  212 ASN A CA  1 
ATOM   6024 C C   . ASN E 1 204 ? -18.75100 72.07300 -22.83300 1.000 172.18791 ?  212 ASN A C   1 
ATOM   6025 O O   . ASN E 1 204 ? -18.85400 70.83500 -22.89600 1.000 159.23389 ?  212 ASN A O   1 
ATOM   6026 C CB  . ASN E 1 204 ? -18.61900 72.05900 -20.31800 1.000 193.43238 ?  212 ASN A CB  1 
ATOM   6027 C CG  . ASN E 1 204 ? -19.60200 71.99900 -19.16700 1.000 196.60970 ?  212 ASN A CG  1 
ATOM   6028 O OD1 . ASN E 1 204 ? -20.17200 70.94800 -18.88400 1.000 187.89972 ?  212 ASN A OD1 1 
ATOM   6029 N ND2 . ASN E 1 204 ? -19.81200 73.12200 -18.50000 1.000 206.13117 ?  212 ASN A ND2 1 
ATOM   6030 N N   . VAL E 1 205 ? -18.29700 72.84100 -23.81600 1.000 193.66895 ?  213 VAL A N   1 
ATOM   6031 C CA  . VAL E 1 205 ? -17.79100 72.32400 -25.07900 1.000 173.12868 ?  213 VAL A CA  1 
ATOM   6032 C C   . VAL E 1 205 ? -16.27200 72.28300 -25.03400 1.000 184.81670 ?  213 VAL A C   1 
ATOM   6033 O O   . VAL E 1 205 ? -15.61700 73.23300 -24.57600 1.000 201.95390 ?  213 VAL A O   1 
ATOM   6034 C CB  . VAL E 1 205 ? -18.28800 73.18500 -26.25600 1.000 150.70553 ?  213 VAL A CB  1 
ATOM   6035 C CG1 . VAL E 1 205 ? -18.21500 72.41300 -27.56500 1.000 131.88448 ?  213 VAL A CG1 1 
ATOM   6036 C CG2 . VAL E 1 205 ? -19.70700 73.67600 -25.99000 1.000 146.44399 ?  213 VAL A CG2 1 
ATOM   6037 N N   . ASN E 1 206 ? -15.71400 71.20600 -25.57800 1.000 183.16666 ?  214 ASN A N   1 
ATOM   6038 C CA  . ASN E 1 206 ? -14.28100 71.01700 -25.70900 1.000 190.98421 ?  214 ASN A CA  1 
ATOM   6039 C C   . ASN E 1 206 ? -13.97000 70.50600 -27.10300 1.000 167.47120 ?  214 ASN A C   1 
ATOM   6040 O O   . ASN E 1 206 ? -14.65700 69.61400 -27.61700 1.000 150.07294 ?  214 ASN A O   1 
ATOM   6041 C CB  . ASN E 1 206 ? -13.72500 70.03100 -24.67600 1.000 200.76272 ?  214 ASN A CB  1 
ATOM   6042 C CG  . ASN E 1 206 ? -12.30700 69.60300 -24.99600 1.000 204.17723 ?  214 ASN A CG  1 
ATOM   6043 O OD1 . ASN E 1 206 ? -11.34200 70.26000 -24.61000 1.000 219.22053 ?  214 ASN A OD1 1 
ATOM   6044 N ND2 . ASN E 1 206 ? -12.17600 68.48700 -25.71100 1.000 189.13771 ?  214 ASN A ND2 1 
ATOM   6045 N N   . HIS E 1 207 ? -12.93200 71.09200 -27.71100 1.000 201.03447 ?  215 HIS A N   1 
ATOM   6046 C CA  . HIS E 1 207 ? -12.43900 70.69700 -29.02600 1.000 182.64393 ?  215 HIS A CA  1 
ATOM   6047 C C   . HIS E 1 207 ? -10.94900 70.45400 -28.80900 1.000 196.26425 ?  215 HIS A C   1 
ATOM   6048 O O   . HIS E 1 207 ? -10.12100 71.35300 -28.98800 1.000 197.41699 ?  215 HIS A O   1 
ATOM   6049 C CB  . HIS E 1 207 ? -12.72000 71.75800 -30.09400 1.000 164.72190 ?  215 HIS A CB  1 
ATOM   6050 C CG  . HIS E 1 207 ? -12.59400 71.25200 -31.50100 1.000 148.12452 ?  215 HIS A CG  1 
ATOM   6051 N ND1 . HIS E 1 207 ? -12.76000 72.06400 -32.60300 1.000 138.88976 ?  215 HIS A ND1 1 
ATOM   6052 C CD2 . HIS E 1 207 ? -12.36300 70.00800 -31.98400 1.000 145.66130 ?  215 HIS A CD2 1 
ATOM   6053 C CE1 . HIS E 1 207 ? -12.61100 71.34900 -33.70400 1.000 133.25290 ?  215 HIS A CE1 1 
ATOM   6054 N NE2 . HIS E 1 207 ? -12.37100 70.09700 -33.35500 1.000 133.93887 ?  215 HIS A NE2 1 
ATOM   6055 N N   . LYS E 1 208 ? -10.63800 69.26200 -28.29700 1.000 180.72227 ?  216 LYS A N   1 
ATOM   6056 C CA  . LYS E 1 208 ? -9.29200  68.76000 -28.05400 1.000 174.95095 ?  216 LYS A CA  1 
ATOM   6057 C C   . LYS E 1 208 ? -8.43000  68.80100 -29.31400 1.000 168.74866 ?  216 LYS A C   1 
ATOM   6058 O O   . LYS E 1 208 ? -7.22800  69.08200 -29.21200 1.000 170.72261 ?  216 LYS A O   1 
ATOM   6059 C CB  . LYS E 1 208 ? -9.35700  67.33000 -27.49900 1.000 161.33199 ?  216 LYS A CB  1 
ATOM   6060 N N   . PRO E 1 209 ? -8.97600  68.51900 -30.50600 1.000 173.04659 ?  217 PRO A N   1 
ATOM   6061 C CA  . PRO E 1 209 ? -8.18100  68.74200 -31.72700 1.000 163.65154 ?  217 PRO A CA  1 
ATOM   6062 C C   . PRO E 1 209 ? -7.68600  70.16600 -31.90200 1.000 172.71214 ?  217 PRO A C   1 
ATOM   6063 O O   . PRO E 1 209 ? -6.58200  70.35700 -32.42000 1.000 169.18818 ?  217 PRO A O   1 
ATOM   6064 C CB  . PRO E 1 209 ? -9.15500  68.35500 -32.84400 1.000 148.70723 ?  217 PRO A CB  1 
ATOM   6065 C CG  . PRO E 1 209 ? -9.96800  67.29800 -32.24000 1.000 144.81318 ?  217 PRO A CG  1 
ATOM   6066 C CD  . PRO E 1 209 ? -10.13500 67.64800 -30.78600 1.000 162.41984 ?  217 PRO A CD  1 
ATOM   6067 N N   . SER E 1 210 ? -8.45700  71.17600 -31.50700 1.000 163.66282 ?  218 SER A N   1 
ATOM   6068 C CA  . SER E 1 210 ? -7.99600  72.55600 -31.59200 1.000 168.12081 ?  218 SER A CA  1 
ATOM   6069 C C   . SER E 1 210 ? -7.62200  73.15000 -30.24100 1.000 180.50683 ?  218 SER A C   1 
ATOM   6070 O O   . SER E 1 210 ? -7.29100  74.33600 -30.17800 1.000 182.88157 ?  218 SER A O   1 
ATOM   6071 C CB  . SER E 1 210 ? -9.05600  73.43300 -32.25900 1.000 164.27247 ?  218 SER A CB  1 
ATOM   6072 O OG  . SER E 1 210 ? -10.22000 73.51200 -31.46100 1.000 171.63098 ?  218 SER A OG  1 
ATOM   6073 N N   . ASN E 1 211 ? -7.68900  72.36300 -29.16300 1.000 172.63164 ?  219 ASN A N   1 
ATOM   6074 C CA  . ASN E 1 211 ? -7.37100  72.83500 -27.81100 1.000 179.04316 ?  219 ASN A CA  1 
ATOM   6075 C C   . ASN E 1 211 ? -8.24600  74.02600 -27.42200 1.000 183.77142 ?  219 ASN A C   1 
ATOM   6076 O O   . ASN E 1 211 ? -7.80600  74.94500 -26.72800 1.000 187.53273 ?  219 ASN A O   1 
ATOM   6077 C CB  . ASN E 1 211 ? -5.88600  73.18700 -27.66700 1.000 180.01962 ?  219 ASN A CB  1 
ATOM   6078 C CG  . ASN E 1 211 ? -5.26300  72.61300 -26.40200 1.000 180.01179 ?  219 ASN A CG  1 
ATOM   6079 O OD1 . ASN E 1 211 ? -5.83600  72.70700 -25.31500 1.000 181.80483 ?  219 ASN A OD1 1 
ATOM   6080 N ND2 . ASN E 1 211 ? -4.07300  72.02900 -26.53800 1.000 177.54269 ?  219 ASN A ND2 1 
ATOM   6081 N N   . THR E 1 212 ? -9.50600  74.00500 -27.84900 1.000 189.94980 ?  220 THR A N   1 
ATOM   6082 C CA  . THR E 1 212 ? -10.43100 75.08700 -27.53800 1.000 192.53253 ?  220 THR A CA  1 
ATOM   6083 C C   . THR E 1 212 ? -11.39400 74.65500 -26.44000 1.000 196.56299 ?  220 THR A C   1 
ATOM   6084 O O   . THR E 1 212 ? -11.86900 73.51300 -26.42300 1.000 196.00041 ?  220 THR A O   1 
ATOM   6085 C CB  . THR E 1 212 ? -11.20500 75.54100 -28.77700 1.000 186.83794 ?  220 THR A CB  1 
ATOM   6086 O OG1 . THR E 1 212 ? -10.31700 75.59400 -29.90200 1.000 179.85007 ?  220 THR A OG1 1 
ATOM   6087 C CG2 . THR E 1 212 ? -11.79800 76.92300 -28.54200 1.000 187.93002 ?  220 THR A CG2 1 
ATOM   6088 N N   . LYS E 1 213 ? -11.68500 75.58500 -25.53100 1.000 191.44035 ?  221 LYS A N   1 
ATOM   6089 C CA  . LYS E 1 213 ? -12.51800 75.32900 -24.36200 1.000 193.50282 ?  221 LYS A CA  1 
ATOM   6090 C C   . LYS E 1 213 ? -13.54300 76.44700 -24.25300 1.000 194.99288 ?  221 LYS A C   1 
ATOM   6091 O O   . LYS E 1 213 ? -13.16800 77.60300 -24.03200 1.000 195.79773 ?  221 LYS A O   1 
ATOM   6092 C CB  . LYS E 1 213 ? -11.64600 75.29900 -23.10100 1.000 193.16808 ?  221 LYS A CB  1 
ATOM   6093 C CG  . LYS E 1 213 ? -12.04600 74.30500 -22.03800 1.000 190.94285 ?  221 LYS A CG  1 
ATOM   6094 C CD  . LYS E 1 213 ? -11.92300 72.90100 -22.59200 1.000 187.07789 ?  221 LYS A CD  1 
ATOM   6095 C CE  . LYS E 1 213 ? -12.07900 71.85900 -21.50600 1.000 180.92932 ?  221 LYS A CE  1 
ATOM   6096 N NZ  . LYS E 1 213 ? -10.83500 71.74600 -20.69000 1.000 177.75873 ?  221 LYS A NZ  1 
ATOM   6097 N N   . VAL E 1 214 ? -14.82600 76.11600 -24.40700 1.000 187.04117 ?  222 VAL A N   1 
ATOM   6098 C CA  . VAL E 1 214 ? -15.89500 77.11500 -24.38900 1.000 187.28246 ?  222 VAL A CA  1 
ATOM   6099 C C   . VAL E 1 214 ? -17.04100 76.61700 -23.51100 1.000 188.95677 ?  222 VAL A C   1 
ATOM   6100 O O   . VAL E 1 214 ? -17.65400 75.59200 -23.81100 1.000 188.18346 ?  222 VAL A O   1 
ATOM   6101 C CB  . VAL E 1 214 ? -16.38700 77.44000 -25.80900 1.000 183.31485 ?  222 VAL A CB  1 
ATOM   6102 C CG1 . VAL E 1 214 ? -15.43500 78.40800 -26.47800 1.000 182.84868 ?  222 VAL A CG1 1 
ATOM   6103 C CG2 . VAL E 1 214 ? -16.42200 76.17000 -26.63400 1.000 180.57309 ?  222 VAL A CG2 1 
ATOM   6104 N N   . ASP E 1 215 ? -17.33400 77.33900 -22.43300 1.000 191.71239 ?  223 ASP A N   1 
ATOM   6105 C CA  . ASP E 1 215 ? -18.41900 76.98300 -21.51500 1.000 192.61699 ?  223 ASP A CA  1 
ATOM   6106 C C   . ASP E 1 215 ? -19.47300 78.09500 -21.52500 1.000 193.45586 ?  223 ASP A C   1 
ATOM   6107 O O   . ASP E 1 215 ? -19.35700 79.08100 -20.79300 1.000 195.19224 ?  223 ASP A O   1 
ATOM   6108 C CB  . ASP E 1 215 ? -17.87300 76.71200 -20.12800 1.000 193.13491 ?  223 ASP A CB  1 
ATOM   6109 C CG  . ASP E 1 215 ? -17.26400 75.32700 -20.01000 1.000 190.35580 ?  223 ASP A CG  1 
ATOM   6110 O OD1 . ASP E 1 215 ? -16.57800 74.88700 -20.96200 1.000 189.44713 ?  223 ASP A OD1 1 
ATOM   6111 O OD2 . ASP E 1 215 ? -17.47300 74.67500 -18.96700 1.000 187.89311 -1 223 ASP A OD2 1 
ATOM   6112 N N   . LYS E 1 216 ? -20.51100 77.92400 -22.34300 1.000 192.29766 ?  224 LYS A N   1 
ATOM   6113 C CA  . LYS E 1 216 ? -21.49800 78.97500 -22.58200 1.000 190.80284 ?  224 LYS A CA  1 
ATOM   6114 C C   . LYS E 1 216 ? -22.74000 78.82700 -21.70500 1.000 191.74812 ?  224 LYS A C   1 
ATOM   6115 O O   . LYS E 1 216 ? -23.24100 77.71900 -21.49600 1.000 191.39267 ?  224 LYS A O   1 
ATOM   6116 C CB  . LYS E 1 216 ? -21.91200 78.99000 -24.05400 1.000 185.48606 ?  224 LYS A CB  1 
ATOM   6117 N N   . LYS E 1 217 ? -23.23900 79.96500 -21.21300 1.000 194.86100 ?  225 LYS A N   1 
ATOM   6118 C CA  . LYS E 1 217 ? -24.42000 80.01900 -20.35500 1.000 194.85836 ?  225 LYS A CA  1 
ATOM   6119 C C   . LYS E 1 217 ? -25.68900 80.21300 -21.18100 1.000 189.80066 ?  225 LYS A C   1 
ATOM   6120 O O   . LYS E 1 217 ? -25.74100 81.07400 -22.06700 1.000 187.30041 ?  225 LYS A O   1 
ATOM   6121 C CB  . LYS E 1 217 ? -24.28600 81.14400 -19.32800 1.000 197.17280 ?  225 LYS A CB  1 
ATOM   6122 N N   . VAL E 1 218 ? -26.71200 79.41700 -20.87500 1.000 196.85095 ?  226 VAL A N   1 
ATOM   6123 C CA  . VAL E 1 218 ? -28.01700 79.48600 -21.52800 1.000 190.00882 ?  226 VAL A CA  1 
ATOM   6124 C C   . VAL E 1 218 ? -28.98500 80.14900 -20.55800 1.000 187.57354 ?  226 VAL A C   1 
ATOM   6125 O O   . VAL E 1 218 ? -29.14500 79.68900 -19.42200 1.000 186.08885 ?  226 VAL A O   1 
ATOM   6126 C CB  . VAL E 1 218 ? -28.51400 78.09300 -21.94700 1.000 184.27414 ?  226 VAL A CB  1 
ATOM   6127 C CG1 . VAL E 1 218 ? -29.79200 78.20700 -22.76600 1.000 175.07833 ?  226 VAL A CG1 1 
ATOM   6128 C CG2 . VAL E 1 218 ? -27.43300 77.34600 -22.71200 1.000 187.71057 ?  226 VAL A CG2 1 
ATOM   6129 N N   . GLU E 1 219 ? -29.62700 81.22800 -20.99800 1.000 199.21685 ?  227 GLU A N   1 
ATOM   6130 C CA  . GLU E 1 219 ? -30.49700 82.00000 -20.12600 1.000 196.94527 ?  227 GLU A CA  1 
ATOM   6131 C C   . GLU E 1 219 ? -31.77300 82.39600 -20.85600 1.000 191.28151 ?  227 GLU A C   1 
ATOM   6132 O O   . GLU E 1 219 ? -31.78200 82.50100 -22.08900 1.000 190.42301 ?  227 GLU A O   1 
ATOM   6133 C CB  . GLU E 1 219 ? -29.75400 83.24400 -19.61600 1.000 204.06530 ?  227 GLU A CB  1 
ATOM   6134 C CG  . GLU E 1 219 ? -29.12600 83.04000 -18.24700 1.000 207.58442 ?  227 GLU A CG  1 
ATOM   6135 C CD  . GLU E 1 219 ? -28.11700 84.11900 -17.90100 1.000 213.96836 ?  227 GLU A CD  1 
ATOM   6136 O OE1 . GLU E 1 219 ? -27.87600 85.00500 -18.74700 1.000 215.41472 ?  227 GLU A OE1 1 
ATOM   6137 O OE2 . GLU E 1 219 ? -27.55100 84.07100 -16.78800 1.000 216.48521 -1 227 GLU A OE2 1 
ATOM   6138 N N   . PRO E 1 220 ? -32.86700 82.61500 -20.11700 1.000 202.36911 ?  228 PRO A N   1 
ATOM   6139 C CA  . PRO E 1 220 ? -34.16700 82.87400 -20.75400 1.000 196.51816 ?  228 PRO A CA  1 
ATOM   6140 C C   . PRO E 1 220 ? -34.14500 84.06100 -21.70400 1.000 200.88879 ?  228 PRO A C   1 
ATOM   6141 O O   . PRO E 1 220 ? -33.44400 85.05300 -21.49100 1.000 207.70006 ?  228 PRO A O   1 
ATOM   6142 C CB  . PRO E 1 220 ? -35.09500 83.14400 -19.56400 1.000 192.26610 ?  228 PRO A CB  1 
ATOM   6143 C CG  . PRO E 1 220 ? -34.46000 82.43700 -18.42400 1.000 191.96223 ?  228 PRO A CG  1 
ATOM   6144 C CD  . PRO E 1 220 ? -32.97900 82.55800 -18.65000 1.000 201.17472 ?  228 PRO A CD  1 
ATOM   6145 N N   . LYS E 1 221 ? -34.93000 83.93800 -22.76900 1.000 196.01790 ?  229 LYS A N   1 
ATOM   6146 C CA  . LYS E 1 221 ? -35.07000 84.99400 -23.75800 1.000 199.17150 ?  229 LYS A CA  1 
ATOM   6147 C C   . LYS E 1 221 ? -36.29700 85.85000 -23.46400 1.000 198.07962 ?  229 LYS A C   1 
ATOM   6148 O O   . LYS E 1 221 ? -36.27700 87.06600 -23.65200 1.000 203.27282 ?  229 LYS A O   1 
ATOM   6149 C CB  . LYS E 1 221 ? -35.16400 84.39900 -25.16400 1.000 195.10581 ?  229 LYS A CB  1 
ATOM   6150 N N   . THR F 2 5   ? -20.88800 37.22100 -45.41100 1.000 162.63395 ?  5   THR B N   1 
ATOM   6151 C CA  . THR F 2 5   ? -22.03900 38.12200 -45.41900 1.000 166.40329 ?  5   THR B CA  1 
ATOM   6152 C C   . THR F 2 5   ? -22.85800 37.99900 -44.14200 1.000 170.62732 ?  5   THR B C   1 
ATOM   6153 O O   . THR F 2 5   ? -22.76200 37.00400 -43.42200 1.000 168.24616 ?  5   THR B O   1 
ATOM   6154 C CB  . THR F 2 5   ? -22.98600 37.84100 -46.60300 1.000 160.31857 ?  5   THR B CB  1 
ATOM   6155 O OG1 . THR F 2 5   ? -23.87600 36.77200 -46.25600 1.000 157.45827 ?  5   THR B OG1 1 
ATOM   6156 C CG2 . THR F 2 5   ? -22.19800 37.44500 -47.84800 1.000 153.89552 ?  5   THR B CG2 1 
ATOM   6157 N N   . GLN F 2 6   ? -23.67400 39.01200 -43.87300 1.000 154.66660 ?  6   GLN B N   1 
ATOM   6158 C CA  . GLN F 2 6   ? -24.64100 38.96400 -42.79200 1.000 156.27211 ?  6   GLN B CA  1 
ATOM   6159 C C   . GLN F 2 6   ? -26.03400 39.07700 -43.38600 1.000 154.50117 ?  6   GLN B C   1 
ATOM   6160 O O   . GLN F 2 6   ? -26.22200 39.63800 -44.47100 1.000 153.23493 ?  6   GLN B O   1 
ATOM   6161 C CB  . GLN F 2 6   ? -24.42300 40.07700 -41.77100 1.000 160.82850 ?  6   GLN B CB  1 
ATOM   6162 C CG  . GLN F 2 6   ? -24.21200 39.55800 -40.36400 1.000 158.95917 ?  6   GLN B CG  1 
ATOM   6163 C CD  . GLN F 2 6   ? -23.77200 40.64100 -39.40100 1.000 162.21850 ?  6   GLN B CD  1 
ATOM   6164 O OE1 . GLN F 2 6   ? -22.57700 40.90100 -39.25200 1.000 163.51799 ?  6   GLN B OE1 1 
ATOM   6165 N NE2 . GLN F 2 6   ? -24.73200 41.27500 -38.73700 1.000 163.71798 ?  6   GLN B NE2 1 
ATOM   6166 N N   . SER F 2 7   ? -27.00200 38.53600 -42.67100 1.000 161.86401 ?  7   SER B N   1 
ATOM   6167 C CA  . SER F 2 7   ? -28.37700 38.58100 -43.12600 1.000 160.42686 ?  7   SER B CA  1 
ATOM   6168 C C   . SER F 2 7   ? -29.28800 38.43600 -41.91900 1.000 160.81787 ?  7   SER B C   1 
ATOM   6169 O O   . SER F 2 7   ? -29.10300 37.51900 -41.10600 1.000 157.81698 ?  7   SER B O   1 
ATOM   6170 C CB  . SER F 2 7   ? -28.64000 37.47800 -44.15200 1.000 154.75206 ?  7   SER B CB  1 
ATOM   6171 O OG  . SER F 2 7   ? -28.05000 36.25600 -43.73800 1.000 151.31409 ?  7   SER B OG  1 
ATOM   6172 N N   . PRO F 2 8   ? -30.27100 39.32500 -41.76200 1.000 156.13154 ?  8   PRO B N   1 
ATOM   6173 C CA  . PRO F 2 8   ? -30.68100 40.37600 -42.69900 1.000 157.45415 ?  8   PRO B CA  1 
ATOM   6174 C C   . PRO F 2 8   ? -29.78300 41.60400 -42.62800 1.000 161.20210 ?  8   PRO B C   1 
ATOM   6175 O O   . PRO F 2 8   ? -29.04800 41.81000 -41.66500 1.000 163.90616 ?  8   PRO B O   1 
ATOM   6176 C CB  . PRO F 2 8   ? -32.10600 40.68600 -42.23900 1.000 158.12606 ?  8   PRO B CB  1 
ATOM   6177 C CG  . PRO F 2 8   ? -32.03300 40.50900 -40.73900 1.000 159.68546 ?  8   PRO B CG  1 
ATOM   6178 C CD  . PRO F 2 8   ? -31.04100 39.38300 -40.50700 1.000 156.82733 ?  8   PRO B CD  1 
ATOM   6179 N N   . SER F 2 9   ? -29.83400 42.44000 -43.66700 1.000 158.07973 ?  9   SER B N   1 
ATOM   6180 C CA  . SER F 2 9   ? -29.07000 43.68300 -43.66200 1.000 161.64381 ?  9   SER B CA  1 
ATOM   6181 C C   . SER F 2 9   ? -29.55700 44.62600 -42.56600 1.000 166.55099 ?  9   SER B C   1 
ATOM   6182 O O   . SER F 2 9   ? -28.75000 45.29600 -41.91300 1.000 171.14731 ?  9   SER B O   1 
ATOM   6183 C CB  . SER F 2 9   ? -29.15600 44.35700 -45.03300 1.000 158.61977 ?  9   SER B CB  1 
ATOM   6184 O OG  . SER F 2 9   ? -28.72400 43.49200 -46.07300 1.000 153.82266 ?  9   SER B OG  1 
ATOM   6185 N N   . SER F 2 10  ? -30.87100 44.68500 -42.34400 1.000 156.84017 ?  10  SER B N   1 
ATOM   6186 C CA  . SER F 2 10  ? -31.45600 45.57200 -41.34300 1.000 161.45272 ?  10  SER B CA  1 
ATOM   6187 C C   . SER F 2 10  ? -32.84200 45.06500 -40.96100 1.000 159.80445 ?  10  SER B C   1 
ATOM   6188 O O   . SER F 2 10  ? -33.53400 44.45400 -41.77900 1.000 155.73730 ?  10  SER B O   1 
ATOM   6189 C CB  . SER F 2 10  ? -31.52900 47.00300 -41.87800 1.000 163.54284 ?  10  SER B CB  1 
ATOM   6190 O OG  . SER F 2 10  ? -31.76900 46.98400 -43.27400 1.000 162.18628 ?  10  SER B OG  1 
ATOM   6191 N N   . LEU F 2 11  ? -33.24500 45.33400 -39.71500 1.000 165.18994 ?  11  LEU B N   1 
ATOM   6192 C CA  . LEU F 2 11  ? -34.48100 44.76000 -39.18500 1.000 163.74602 ?  11  LEU B CA  1 
ATOM   6193 C C   . LEU F 2 11  ? -35.04200 45.59200 -38.03000 1.000 168.78796 ?  11  LEU B C   1 
ATOM   6194 O O   . LEU F 2 11  ? -34.29500 46.21500 -37.27100 1.000 173.49680 ?  11  LEU B O   1 
ATOM   6195 C CB  . LEU F 2 11  ? -34.24600 43.30800 -38.74900 1.000 160.60256 ?  11  LEU B CB  1 
ATOM   6196 C CG  . LEU F 2 11  ? -33.55500 43.07200 -37.40000 1.000 162.44132 ?  11  LEU B CG  1 
ATOM   6197 C CD1 . LEU F 2 11  ? -34.56100 42.83300 -36.27900 1.000 162.88164 ?  11  LEU B CD1 1 
ATOM   6198 C CD2 . LEU F 2 11  ? -32.55900 41.92700 -37.48000 1.000 158.25830 ?  11  LEU B CD2 1 
ATOM   6199 N N   . SER F 2 12  ? -36.37700 45.59400 -37.92300 1.000 175.83842 ?  12  SER B N   1 
ATOM   6200 C CA  . SER F 2 12  ? -37.12400 46.23800 -36.83900 1.000 180.74291 ?  12  SER B CA  1 
ATOM   6201 C C   . SER F 2 12  ? -38.17700 45.27600 -36.29000 1.000 179.38010 ?  12  SER B C   1 
ATOM   6202 O O   . SER F 2 12  ? -39.10000 44.88900 -37.01500 1.000 179.88300 ?  12  SER B O   1 
ATOM   6203 C CB  . SER F 2 12  ? -37.77900 47.53500 -37.31100 1.000 191.68627 ?  12  SER B CB  1 
ATOM   6204 O OG  . SER F 2 12  ? -36.80200 48.49500 -37.67300 1.000 193.80550 ?  12  SER B OG  1 
ATOM   6205 N N   . ALA F 2 13  ? -38.02300 44.86300 -35.03000 1.000 177.88350 ?  13  ALA B N   1 
ATOM   6206 C CA  . ALA F 2 13  ? -39.04800 44.13300 -34.29300 1.000 178.47034 ?  13  ALA B CA  1 
ATOM   6207 C C   . ALA F 2 13  ? -39.61200 44.99900 -33.16200 1.000 188.94583 ?  13  ALA B C   1 
ATOM   6208 O O   . ALA F 2 13  ? -39.33000 46.19400 -33.07000 1.000 196.45690 ?  13  ALA B O   1 
ATOM   6209 C CB  . ALA F 2 13  ? -38.47800 42.81800 -33.76100 1.000 168.46682 ?  13  ALA B CB  1 
ATOM   6210 N N   . SER F 2 14  ? -40.43200 44.39600 -32.30200 1.000 190.15201 ?  14  SER B N   1 
ATOM   6211 C CA  . SER F 2 14  ? -40.98700 45.08400 -31.13900 1.000 200.39035 ?  14  SER B CA  1 
ATOM   6212 C C   . SER F 2 14  ? -40.50200 44.40100 -29.86100 1.000 196.53155 ?  14  SER B C   1 
ATOM   6213 O O   . SER F 2 14  ? -39.75300 43.42200 -29.89900 1.000 186.16201 ?  14  SER B O   1 
ATOM   6214 C CB  . SER F 2 14  ? -42.51700 45.13200 -31.19500 1.000 208.03182 ?  14  SER B CB  1 
ATOM   6215 O OG  . SER F 2 14  ? -43.05000 43.95800 -31.77800 1.000 200.71337 ?  14  SER B OG  1 
ATOM   6216 N N   . VAL F 2 15  ? -40.94800 44.92400 -28.71700 1.000 205.80328 ?  15  VAL B N   1 
ATOM   6217 C CA  . VAL F 2 15  ? -40.45500 44.45100 -27.42700 1.000 204.18979 ?  15  VAL B CA  1 
ATOM   6218 C C   . VAL F 2 15  ? -40.90100 43.01500 -27.17800 1.000 196.20010 ?  15  VAL B C   1 
ATOM   6219 O O   . VAL F 2 15  ? -42.07600 42.66800 -27.35900 1.000 198.29510 ?  15  VAL B O   1 
ATOM   6220 C CB  . VAL F 2 15  ? -40.90700 45.38800 -26.29400 1.000 217.53162 ?  15  VAL B CB  1 
ATOM   6221 C CG1 . VAL F 2 15  ? -42.41200 45.65600 -26.35600 1.000 226.52590 ?  15  VAL B CG1 1 
ATOM   6222 C CG2 . VAL F 2 15  ? -40.49300 44.82600 -24.93600 1.000 216.52006 ?  15  VAL B CG2 1 
ATOM   6223 N N   . GLY F 2 16  ? -39.95600 42.17400 -26.75300 1.000 189.98699 ?  16  GLY B N   1 
ATOM   6224 C CA  . GLY F 2 16  ? -40.19300 40.77800 -26.46000 1.000 182.42052 ?  16  GLY B CA  1 
ATOM   6225 C C   . GLY F 2 16  ? -39.92600 39.80800 -27.59500 1.000 173.69194 ?  16  GLY B C   1 
ATOM   6226 O O   . GLY F 2 16  ? -39.60000 38.64800 -27.33400 1.000 165.69255 ?  16  GLY B O   1 
ATOM   6227 N N   . ASP F 2 17  ? -40.05200 40.25100 -28.84300 1.000 173.39213 ?  17  ASP B N   1 
ATOM   6228 C CA  . ASP F 2 17  ? -39.87300 39.37200 -29.99600 1.000 166.35427 ?  17  ASP B CA  1 
ATOM   6229 C C   . ASP F 2 17  ? -38.47000 38.77500 -30.06100 1.000 158.93680 ?  17  ASP B C   1 
ATOM   6230 O O   . ASP F 2 17  ? -37.47400 39.50400 -30.09500 1.000 161.64009 ?  17  ASP B O   1 
ATOM   6231 C CB  . ASP F 2 17  ? -40.17500 40.14800 -31.27400 1.000 169.93279 ?  17  ASP B CB  1 
ATOM   6232 C CG  . ASP F 2 17  ? -41.61100 40.61500 -31.33600 1.000 176.64368 ?  17  ASP B CG  1 
ATOM   6233 O OD1 . ASP F 2 17  ? -42.18500 40.87300 -30.25800 1.000 181.45794 ?  17  ASP B OD1 1 
ATOM   6234 O OD2 . ASP F 2 17  ? -42.15800 40.73200 -32.45300 1.000 177.41440 -1 17  ASP B OD2 1 
ATOM   6235 N N   . ARG F 2 18  ? -38.39700 37.44300 -30.08100 1.000 163.21589 ?  18  ARG B N   1 
ATOM   6236 C CA  . ARG F 2 18  ? -37.13200 36.75600 -30.31600 1.000 155.54830 ?  18  ARG B CA  1 
ATOM   6237 C C   . ARG F 2 18  ? -36.62900 37.06300 -31.72500 1.000 157.50143 ?  18  ARG B C   1 
ATOM   6238 O O   . ARG F 2 18  ? -37.41300 37.14200 -32.67500 1.000 160.19125 ?  18  ARG B O   1 
ATOM   6239 C CB  . ARG F 2 18  ? -37.30300 35.24500 -30.11900 1.000 145.00486 ?  18  ARG B CB  1 
ATOM   6240 N N   . VAL F 2 19  ? -35.31700 37.28300 -31.85300 1.000 170.93399 ?  19  VAL B N   1 
ATOM   6241 C CA  . VAL F 2 19  ? -34.71500 37.69700 -33.12000 1.000 168.44769 ?  19  VAL B CA  1 
ATOM   6242 C C   . VAL F 2 19  ? -33.41700 36.92900 -33.35700 1.000 162.20306 ?  19  VAL B C   1 
ATOM   6243 O O   . VAL F 2 19  ? -32.60600 36.75500 -32.44400 1.000 158.09764 ?  19  VAL B O   1 
ATOM   6244 C CB  . VAL F 2 19  ? -34.47200 39.22300 -33.15200 1.000 168.38375 ?  19  VAL B CB  1 
ATOM   6245 C CG1 . VAL F 2 19  ? -33.52600 39.64700 -32.03400 1.000 164.09438 ?  19  VAL B CG1 1 
ATOM   6246 C CG2 . VAL F 2 19  ? -33.93800 39.65800 -34.51500 1.000 166.99442 ?  19  VAL B CG2 1 
ATOM   6247 N N   . THR F 2 20  ? -33.20900 36.48100 -34.59400 1.000 170.58909 ?  20  THR B N   1 
ATOM   6248 C CA  . THR F 2 20  ? -32.03100 35.68400 -34.91900 1.000 165.85270 ?  20  THR B CA  1 
ATOM   6249 C C   . THR F 2 20  ? -31.41200 36.17800 -36.21800 1.000 165.50616 ?  20  THR B C   1 
ATOM   6250 O O   . THR F 2 20  ? -32.07500 36.20600 -37.25900 1.000 169.58839 ?  20  THR B O   1 
ATOM   6251 C CB  . THR F 2 20  ? -32.37700 34.19700 -35.02500 1.000 167.30609 ?  20  THR B CB  1 
ATOM   6252 O OG1 . THR F 2 20  ? -32.56100 33.65700 -33.71200 1.000 167.01998 ?  20  THR B OG1 1 
ATOM   6253 C CG2 . THR F 2 20  ? -31.26700 33.45200 -35.72000 1.000 164.04361 ?  20  THR B CG2 1 
ATOM   6254 N N   . ILE F 2 21  ? -30.13900 36.55800 -36.14100 1.000 150.95582 ?  21  ILE B N   1 
ATOM   6255 C CA  . ILE F 2 21  ? -29.33000 36.92300 -37.29700 1.000 150.84378 ?  21  ILE B CA  1 
ATOM   6256 C C   . ILE F 2 21  ? -28.54000 35.69200 -37.70400 1.000 150.03829 ?  21  ILE B C   1 
ATOM   6257 O O   . ILE F 2 21  ? -28.21100 34.84600 -36.86600 1.000 147.01429 ?  21  ILE B O   1 
ATOM   6258 C CB  . ILE F 2 21  ? -28.38200 38.10500 -36.98900 1.000 150.81570 ?  21  ILE B CB  1 
ATOM   6259 C CG1 . ILE F 2 21  ? -29.14400 39.24900 -36.32100 1.000 150.89140 ?  21  ILE B CG1 1 
ATOM   6260 C CG2 . ILE F 2 21  ? -27.71500 38.60900 -38.26500 1.000 157.00805 ?  21  ILE B CG2 1 
ATOM   6261 C CD1 . ILE F 2 21  ? -28.25000 40.40000 -35.87600 1.000 151.22999 ?  21  ILE B CD1 1 
ATOM   6262 N N   . THR F 2 22  ? -28.24500 35.57400 -38.99200 1.000 146.96173 ?  22  THR B N   1 
ATOM   6263 C CA  . THR F 2 22  ? -27.44300 34.46900 -39.48400 1.000 147.99781 ?  22  THR B CA  1 
ATOM   6264 C C   . THR F 2 22  ? -26.27000 35.02100 -40.28400 1.000 154.33593 ?  22  THR B C   1 
ATOM   6265 O O   . THR F 2 22  ? -26.40300 36.00000 -41.02400 1.000 160.25551 ?  22  THR B O   1 
ATOM   6266 C CB  . THR F 2 22  ? -28.28100 33.50100 -40.32600 1.000 149.31702 ?  22  THR B CB  1 
ATOM   6267 O OG1 . THR F 2 22  ? -29.34900 32.99700 -39.51700 1.000 146.85549 ?  22  THR B OG1 1 
ATOM   6268 C CG2 . THR F 2 22  ? -27.43400 32.32300 -40.78800 1.000 150.39367 ?  22  THR B CG2 1 
ATOM   6269 N N   . CYS F 2 23  ? -25.12500 34.37100 -40.11200 1.000 150.36365 ?  23  CYS B N   1 
ATOM   6270 C CA  . CYS F 2 23  ? -23.83800 34.73700 -40.67300 1.000 158.42660 ?  23  CYS B CA  1 
ATOM   6271 C C   . CYS F 2 23  ? -23.31400 33.55500 -41.47700 1.000 162.07574 ?  23  CYS B C   1 
ATOM   6272 O O   . CYS F 2 23  ? -23.41400 32.40100 -41.03700 1.000 155.29931 ?  23  CYS B O   1 
ATOM   6273 C CB  . CYS F 2 23  ? -22.85900 35.10500 -39.54600 1.000 155.02871 ?  23  CYS B CB  1 
ATOM   6274 S SG  . CYS F 2 23  ? -21.31400 35.87600 -40.05000 1.000 166.49142 ?  23  CYS B SG  1 
ATOM   6275 N N   . ARG F 2 24  ? -22.77000 33.84200 -42.65700 1.000 164.88832 ?  24  ARG B N   1 
ATOM   6276 C CA  . ARG F 2 24  ? -22.23400 32.81900 -43.54300 1.000 170.44750 ?  24  ARG B CA  1 
ATOM   6277 C C   . ARG F 2 24  ? -20.72700 32.69600 -43.36400 1.000 174.29036 ?  24  ARG B C   1 
ATOM   6278 O O   . ARG F 2 24  ? -20.02500 33.69600 -43.19400 1.000 180.15569 ?  24  ARG B O   1 
ATOM   6279 C CB  . ARG F 2 24  ? -22.55800 33.13700 -45.00500 1.000 183.56636 ?  24  ARG B CB  1 
ATOM   6280 C CG  . ARG F 2 24  ? -22.30700 31.99100 -45.97600 1.000 188.66777 ?  24  ARG B CG  1 
ATOM   6281 C CD  . ARG F 2 24  ? -22.77100 30.65900 -45.41500 1.000 175.90217 ?  24  ARG B CD  1 
ATOM   6282 N NE  . ARG F 2 24  ? -24.22300 30.54500 -45.39900 1.000 170.24575 ?  24  ARG B NE  1 
ATOM   6283 C CZ  . ARG F 2 24  ? -24.93000 29.98800 -46.37200 1.000 173.98871 ?  24  ARG B CZ  1 
ATOM   6284 N NH1 . ARG F 2 24  ? -24.34600 29.46400 -47.43900 1.000 183.09165 ?  24  ARG B NH1 1 
ATOM   6285 N NH2 . ARG F 2 24  ? -26.25300 29.93600 -46.26500 1.000 168.98323 ?  24  ARG B NH2 1 
ATOM   6286 N N   . ALA F 2 25  ? -20.23700 31.45600 -43.40200 1.000 172.85108 ?  25  ALA B N   1 
ATOM   6287 C CA  . ALA F 2 25  ? -18.81800 31.13900 -43.26700 1.000 175.06100 ?  25  ALA B CA  1 
ATOM   6288 C C   . ALA F 2 25  ? -18.42600 30.12700 -44.34700 1.000 181.09819 ?  25  ALA B C   1 
ATOM   6289 O O   . ALA F 2 25  ? -17.99600 29.01300 -44.05100 1.000 175.54186 ?  25  ALA B O   1 
ATOM   6290 C CB  . ALA F 2 25  ? -18.50000 30.61300 -41.87000 1.000 163.52212 ?  25  ALA B CB  1 
ATOM   6291 N N   . SER F 2 26  ? -18.63000 30.51300 -45.61300 1.000 180.96065 ?  26  SER B N   1 
ATOM   6292 C CA  . SER F 2 26  ? -18.33500 29.62600 -46.73900 1.000 188.21104 ?  26  SER B CA  1 
ATOM   6293 C C   . SER F 2 26  ? -16.93900 29.02200 -46.64000 1.000 188.51815 ?  26  SER B C   1 
ATOM   6294 O O   . SER F 2 26  ? -16.73400 27.85700 -47.00200 1.000 185.68682 ?  26  SER B O   1 
ATOM   6295 C CB  . SER F 2 26  ? -18.50100 30.37900 -48.06000 1.000 205.53378 ?  26  SER B CB  1 
ATOM   6296 O OG  . SER F 2 26  ? -17.90600 31.65900 -47.99500 1.000 216.17789 ?  26  SER B OG  1 
ATOM   6297 N N   . GLN F 2 27  ? -15.96600 29.78700 -46.15100 1.000 197.09912 ?  27  GLN B N   1 
ATOM   6298 C CA  . GLN F 2 27  ? -14.71300 29.18200 -45.71600 1.000 192.27914 ?  27  GLN B CA  1 
ATOM   6299 C C   . GLN F 2 27  ? -14.98600 28.46100 -44.40200 1.000 175.33578 ?  27  GLN B C   1 
ATOM   6300 O O   . GLN F 2 27  ? -15.24900 29.10200 -43.37800 1.000 168.70349 ?  27  GLN B O   1 
ATOM   6301 C CB  . GLN F 2 27  ? -13.61000 30.22400 -45.55000 1.000 198.46362 ?  27  GLN B CB  1 
ATOM   6302 C CG  . GLN F 2 27  ? -13.13500 30.85900 -46.84300 1.000 216.49858 ?  27  GLN B CG  1 
ATOM   6303 C CD  . GLN F 2 27  ? -14.04100 31.96900 -47.33200 1.000 228.43215 ?  27  GLN B CD  1 
ATOM   6304 O OE1 . GLN F 2 27  ? -15.25700 31.80300 -47.44600 1.000 226.82146 ?  27  GLN B OE1 1 
ATOM   6305 N NE2 . GLN F 2 27  ? -13.44700 33.11600 -47.62800 1.000 239.41218 ?  27  GLN B NE2 1 
ATOM   6306 N N   . ALA F 2 28  ? -14.91800 27.12900 -44.42400 1.000 174.08881 ?  28  ALA B N   1 
ATOM   6307 C CA  . ALA F 2 28  ? -15.16500 26.37000 -43.20600 1.000 160.69725 ?  28  ALA B CA  1 
ATOM   6308 C C   . ALA F 2 28  ? -14.04600 26.62000 -42.20600 1.000 156.33440 ?  28  ALA B C   1 
ATOM   6309 O O   . ALA F 2 28  ? -13.07400 25.86000 -42.14100 1.000 154.91450 ?  28  ALA B O   1 
ATOM   6310 C CB  . ALA F 2 28  ? -15.28400 24.87400 -43.50300 1.000 157.11926 ?  28  ALA B CB  1 
ATOM   6311 N N   . ALA F 2 29  ? -14.17100 27.69600 -41.42900 1.000 152.08616 ?  29  ALA B N   1 
ATOM   6312 C CA  . ALA F 2 29  ? -13.19300 28.00900 -40.39700 1.000 147.44195 ?  29  ALA B CA  1 
ATOM   6313 C C   . ALA F 2 29  ? -13.72500 27.54300 -39.04400 1.000 137.46334 ?  29  ALA B C   1 
ATOM   6314 O O   . ALA F 2 29  ? -14.11800 28.33500 -38.18600 1.000 134.25293 ?  29  ALA B O   1 
ATOM   6315 C CB  . ALA F 2 29  ? -12.88900 29.50500 -40.38900 1.000 152.58446 ?  29  ALA B CB  1 
ATOM   6316 N N   . TYR F 2 30  ? -13.81900 26.21900 -38.92000 1.000 141.58569 ?  36  TYR B N   1 
ATOM   6317 C CA  . TYR F 2 30  ? -13.90300 25.49200 -37.65600 1.000 134.70641 ?  36  TYR B CA  1 
ATOM   6318 C C   . TYR F 2 30  ? -14.75200 26.13800 -36.57000 1.000 130.69069 ?  36  TYR B C   1 
ATOM   6319 O O   . TYR F 2 30  ? -14.41800 26.01900 -35.38600 1.000 127.72219 ?  36  TYR B O   1 
ATOM   6320 C CB  . TYR F 2 30  ? -12.50000 25.25400 -37.09600 1.000 134.07549 ?  36  TYR B CB  1 
ATOM   6321 C CG  . TYR F 2 30  ? -11.51100 24.77000 -38.12600 1.000 138.49472 ?  36  TYR B CG  1 
ATOM   6322 C CD1 . TYR F 2 30  ? -10.75100 25.66600 -38.87200 1.000 143.91105 ?  36  TYR B CD1 1 
ATOM   6323 C CD2 . TYR F 2 30  ? -11.35400 23.41200 -38.37200 1.000 138.01382 ?  36  TYR B CD2 1 
ATOM   6324 C CE1 . TYR F 2 30  ? -9.84500  25.21700 -39.81800 1.000 148.87039 ?  36  TYR B CE1 1 
ATOM   6325 C CE2 . TYR F 2 30  ? -10.45400 22.95900 -39.31400 1.000 142.32145 ?  36  TYR B CE2 1 
ATOM   6326 C CZ  . TYR F 2 30  ? -9.70600  23.86900 -40.03300 1.000 147.86861 ?  36  TYR B CZ  1 
ATOM   6327 O OH  . TYR F 2 30  ? -8.81200  23.43800 -40.97700 1.000 152.96805 ?  36  TYR B OH  1 
ATOM   6328 N N   . GLY F 2 31  ? -15.84900 26.79100 -36.93300 1.000 140.39292 ?  37  GLY B N   1 
ATOM   6329 C CA  . GLY F 2 31  ? -16.69000 27.35400 -35.89200 1.000 136.72125 ?  37  GLY B CA  1 
ATOM   6330 C C   . GLY F 2 31  ? -15.97000 28.33600 -34.99300 1.000 136.33124 ?  37  GLY B C   1 
ATOM   6331 O O   . GLY F 2 31  ? -16.19900 28.34400 -33.77600 1.000 133.00505 ?  37  GLY B O   1 
ATOM   6332 N N   . ARG F 2 32  ? -15.10300 29.17100 -35.56500 1.000 135.40041 ?  38  ARG B N   1 
ATOM   6333 C CA  . ARG F 2 32  ? -14.43000 30.20300 -34.79100 1.000 133.65375 ?  38  ARG B CA  1 
ATOM   6334 C C   . ARG F 2 32  ? -15.26500 31.46800 -34.69400 1.000 134.86430 ?  38  ARG B C   1 
ATOM   6335 O O   . ARG F 2 32  ? -14.77900 32.47500 -34.16800 1.000 131.28182 ?  38  ARG B O   1 
ATOM   6336 C CB  . ARG F 2 32  ? -13.07600 30.57200 -35.40700 1.000 136.70552 ?  38  ARG B CB  1 
ATOM   6337 C CG  . ARG F 2 32  ? -12.30500 29.47600 -36.11700 1.000 139.24441 ?  38  ARG B CG  1 
ATOM   6338 C CD  . ARG F 2 32  ? -11.62500 28.53300 -35.15800 1.000 133.84651 ?  38  ARG B CD  1 
ATOM   6339 N NE  . ARG F 2 32  ? -10.43700 27.92400 -35.74500 1.000 136.30607 ?  38  ARG B NE  1 
ATOM   6340 C CZ  . ARG F 2 32  ? -9.60400  27.13100 -35.08500 1.000 133.71456 ?  38  ARG B CZ  1 
ATOM   6341 N NH1 . ARG F 2 32  ? -9.83300  26.78400 -33.82800 1.000 129.37787 ?  38  ARG B NH1 1 
ATOM   6342 N NH2 . ARG F 2 32  ? -8.51400  26.67200 -35.69900 1.000 136.44142 ?  38  ARG B NH2 1 
ATOM   6343 N N   . VAL F 2 33  ? -16.50800 31.43100 -35.18700 1.000 139.71216 ?  39  VAL B N   1 
ATOM   6344 C CA  . VAL F 2 33  ? -17.30400 32.64200 -35.29900 1.000 142.33905 ?  39  VAL B CA  1 
ATOM   6345 C C   . VAL F 2 33  ? -17.56400 33.21900 -33.91000 1.000 136.13738 ?  39  VAL B C   1 
ATOM   6346 O O   . VAL F 2 33  ? -17.68900 32.49200 -32.91500 1.000 127.05529 ?  39  VAL B O   1 
ATOM   6347 C CB  . VAL F 2 33  ? -18.62000 32.33400 -36.03800 1.000 141.70989 ?  39  VAL B CB  1 
ATOM   6348 C CG1 . VAL F 2 33  ? -19.62800 33.46900 -35.90100 1.000 141.63174 ?  39  VAL B CG1 1 
ATOM   6349 C CG2 . VAL F 2 33  ? -18.34600 32.04600 -37.50600 1.000 148.45829 ?  39  VAL B CG2 1 
ATOM   6350 N N   . ALA F 2 34  ? -17.67200 34.54400 -33.85600 1.000 133.10856 ?  40  ALA B N   1 
ATOM   6351 C CA  . ALA F 2 34  ? -18.00500 35.27700 -32.64700 1.000 123.78895 ?  40  ALA B CA  1 
ATOM   6352 C C   . ALA F 2 34  ? -18.97500 36.38300 -33.03100 1.000 129.06656 ?  40  ALA B C   1 
ATOM   6353 O O   . ALA F 2 34  ? -19.07700 36.76600 -34.19900 1.000 137.88083 ?  40  ALA B O   1 
ATOM   6354 C CB  . ALA F 2 34  ? -16.76000 35.86600 -31.97100 1.000 115.28875 ?  40  ALA B CB  1 
ATOM   6355 N N   . TRP F 2 35  ? -19.67000 36.91000 -32.02800 1.000 134.91177 ?  41  TRP B N   1 
ATOM   6356 C CA  . TRP F 2 35  ? -20.58600 38.02600 -32.22300 1.000 138.52240 ?  41  TRP B CA  1 
ATOM   6357 C C   . TRP F 2 35  ? -20.26000 39.16600 -31.28100 1.000 133.66517 ?  41  TRP B C   1 
ATOM   6358 O O   . TRP F 2 35  ? -20.03900 38.94100 -30.07900 1.000 124.43141 ?  41  TRP B O   1 
ATOM   6359 C CB  . TRP F 2 35  ? -22.05300 37.64300 -32.00400 1.000 137.26121 ?  41  TRP B CB  1 
ATOM   6360 C CG  . TRP F 2 35  ? -22.50300 36.46100 -32.74900 1.000 138.38187 ?  41  TRP B CG  1 
ATOM   6361 C CD1 . TRP F 2 35  ? -22.33700 35.16300 -32.39800 1.000 135.89073 ?  41  TRP B CD1 1 
ATOM   6362 C CD2 . TRP F 2 35  ? -23.19700 36.46100 -33.99700 1.000 141.44067 ?  41  TRP B CD2 1 
ATOM   6363 N NE1 . TRP F 2 35  ? -22.89500 34.34400 -33.34300 1.000 137.08257 ?  41  TRP B NE1 1 
ATOM   6364 C CE2 . TRP F 2 35  ? -23.42800 35.11800 -34.34000 1.000 140.09750 ?  41  TRP B CE2 1 
ATOM   6365 C CE3 . TRP F 2 35  ? -23.64900 37.46700 -34.85400 1.000 145.45715 ?  41  TRP B CE3 1 
ATOM   6366 C CZ2 . TRP F 2 35  ? -24.09500 34.74900 -35.50900 1.000 142.28675 ?  41  TRP B CZ2 1 
ATOM   6367 C CZ3 . TRP F 2 35  ? -24.30800 37.10300 -36.01400 1.000 148.16523 ?  41  TRP B CZ3 1 
ATOM   6368 C CH2 . TRP F 2 35  ? -24.52400 35.75300 -36.33200 1.000 146.43371 ?  41  TRP B CH2 1 
ATOM   6369 N N   . TYR F 2 36  ? -20.31600 40.38600 -31.84100 1.000 136.45998 ?  42  TYR B N   1 
ATOM   6370 C CA  . TYR F 2 36  ? -20.02800 41.63800 -31.15600 1.000 133.55853 ?  42  TYR B CA  1 
ATOM   6371 C C   . TYR F 2 36  ? -21.22600 42.58000 -31.28900 1.000 137.64073 ?  42  TYR B C   1 
ATOM   6372 O O   . TYR F 2 36  ? -21.94900 42.55700 -32.29700 1.000 142.69070 ?  42  TYR B O   1 
ATOM   6373 C CB  . TYR F 2 36  ? -18.78300 42.34700 -31.73900 1.000 135.85125 ?  42  TYR B CB  1 
ATOM   6374 C CG  . TYR F 2 36  ? -17.47300 41.57500 -31.69700 1.000 130.67990 ?  42  TYR B CG  1 
ATOM   6375 C CD1 . TYR F 2 36  ? -16.70400 41.52400 -30.53800 1.000 118.26807 ?  42  TYR B CD1 1 
ATOM   6376 C CD2 . TYR F 2 36  ? -16.98500 40.93200 -32.83300 1.000 138.39757 ?  42  TYR B CD2 1 
ATOM   6377 C CE1 . TYR F 2 36  ? -15.49600 40.83000 -30.50800 1.000 112.04884 ?  42  TYR B CE1 1 
ATOM   6378 C CE2 . TYR F 2 36  ? -15.78200 40.24000 -32.80900 1.000 133.65534 ?  42  TYR B CE2 1 
ATOM   6379 C CZ  . TYR F 2 36  ? -15.04500 40.19100 -31.64600 1.000 119.58002 ?  42  TYR B CZ  1 
ATOM   6380 O OH  . TYR F 2 36  ? -13.85700 39.49900 -31.63200 1.000 114.24032 ?  42  TYR B OH  1 
ATOM   6381 N N   . GLN F 2 37  ? -21.38000 43.45300 -30.28700 1.000 143.20687 ?  43  GLN B N   1 
ATOM   6382 C CA  . GLN F 2 37  ? -22.48700 44.40200 -30.15900 1.000 146.06027 ?  43  GLN B CA  1 
ATOM   6383 C C   . GLN F 2 37  ? -21.94200 45.82600 -30.14300 1.000 147.82714 ?  43  GLN B C   1 
ATOM   6384 O O   . GLN F 2 37  ? -21.15700 46.17800 -29.25400 1.000 143.85779 ?  43  GLN B O   1 
ATOM   6385 C CB  . GLN F 2 37  ? -23.27100 44.13800 -28.86900 1.000 143.23278 ?  43  GLN B CB  1 
ATOM   6386 C CG  . GLN F 2 37  ? -24.51100 45.00600 -28.70100 1.000 146.09211 ?  43  GLN B CG  1 
ATOM   6387 C CD  . GLN F 2 37  ? -25.33300 44.64200 -27.47300 1.000 145.76409 ?  43  GLN B CD  1 
ATOM   6388 O OE1 . GLN F 2 37  ? -26.56500 44.69000 -27.49800 1.000 147.31066 ?  43  GLN B OE1 1 
ATOM   6389 N NE2 . GLN F 2 37  ? -24.65200 44.28000 -26.38800 1.000 143.68583 ?  43  GLN B NE2 1 
ATOM   6390 N N   . GLN F 2 38  ? -22.34100 46.64500 -31.12700 1.000 136.91343 ?  44  GLN B N   1 
ATOM   6391 C CA  . GLN F 2 38  ? -21.89100 48.03400 -31.23900 1.000 139.71354 ?  44  GLN B CA  1 
ATOM   6392 C C   . GLN F 2 38  ? -23.08200 48.94600 -30.94200 1.000 141.07311 ?  44  GLN B C   1 
ATOM   6393 O O   . GLN F 2 38  ? -23.99700 49.07800 -31.76500 1.000 144.20131 ?  44  GLN B O   1 
ATOM   6394 C CB  . GLN F 2 38  ? -21.29100 48.31200 -32.61600 1.000 146.33364 ?  44  GLN B CB  1 
ATOM   6395 C CG  . GLN F 2 38  ? -20.92900 49.78000 -32.87300 1.000 150.27459 ?  44  GLN B CG  1 
ATOM   6396 C CD  . GLN F 2 38  ? -19.58300 50.19400 -32.28800 1.000 146.56532 ?  44  GLN B CD  1 
ATOM   6397 O OE1 . GLN F 2 38  ? -18.62400 50.41900 -33.02800 1.000 149.71321 ?  44  GLN B OE1 1 
ATOM   6398 N NE2 . GLN F 2 38  ? -19.50900 50.30600 -30.96400 1.000 139.86442 ?  44  GLN B NE2 1 
ATOM   6399 N N   . LYS F 2 39  ? -23.08200 49.52500 -29.73800 1.000 142.14033 ?  45  LYS B N   1 
ATOM   6400 C CA  . LYS F 2 39  ? -24.04600 50.54000 -29.33400 1.000 144.44657 ?  45  LYS B CA  1 
ATOM   6401 C C   . LYS F 2 39  ? -23.73300 51.87200 -30.01600 1.000 148.50625 ?  45  LYS B C   1 
ATOM   6402 O O   . LYS F 2 39  ? -22.65600 52.04500 -30.59300 1.000 149.50818 ?  45  LYS B O   1 
ATOM   6403 C CB  . LYS F 2 39  ? -24.04200 50.69000 -27.81300 1.000 142.68236 ?  45  LYS B CB  1 
ATOM   6404 N N   . PRO F 2 40  ? -24.67900 52.83700 -29.98100 1.000 155.70225 ?  46  PRO B N   1 
ATOM   6405 C CA  . PRO F 2 40  ? -24.45600 54.13000 -30.64500 1.000 159.89015 ?  46  PRO B CA  1 
ATOM   6406 C C   . PRO F 2 40  ? -23.11100 54.77500 -30.35900 1.000 160.31003 ?  46  PRO B C   1 
ATOM   6407 O O   . PRO F 2 40  ? -22.84100 55.19800 -29.23300 1.000 158.60482 ?  46  PRO B O   1 
ATOM   6408 C CB  . PRO F 2 40  ? -25.58900 54.99800 -30.08700 1.000 161.05890 ?  46  PRO B CB  1 
ATOM   6409 C CG  . PRO F 2 40  ? -26.68700 54.05200 -29.82600 1.000 161.25489 ?  46  PRO B CG  1 
ATOM   6410 C CD  . PRO F 2 40  ? -26.09800 52.66600 -29.62700 1.000 154.86589 ?  46  PRO B CD  1 
ATOM   6411 N N   . GLY F 2 41  ? -22.27700 54.86400 -31.39400 1.000 167.07637 ?  47  GLY B N   1 
ATOM   6412 C CA  . GLY F 2 41  ? -20.98000 55.51300 -31.33700 1.000 167.24588 ?  47  GLY B CA  1 
ATOM   6413 C C   . GLY F 2 41  ? -20.14100 55.20900 -30.11100 1.000 161.41080 ?  47  GLY B C   1 
ATOM   6414 O O   . GLY F 2 41  ? -19.59900 56.11700 -29.47100 1.000 160.70055 ?  47  GLY B O   1 
ATOM   6415 N N   . LYS F 2 42  ? -19.99900 53.92500 -29.80500 1.000 154.73036 ?  48  LYS B N   1 
ATOM   6416 C CA  . LYS F 2 42  ? -19.29700 53.48300 -28.60900 1.000 148.28904 ?  48  LYS B CA  1 
ATOM   6417 C C   . LYS F 2 42  ? -18.37200 52.32900 -28.98900 1.000 143.70960 ?  48  LYS B C   1 
ATOM   6418 O O   . LYS F 2 42  ? -18.08600 52.07500 -30.16900 1.000 146.97487 ?  48  LYS B O   1 
ATOM   6419 C CB  . LYS F 2 42  ? -20.29700 53.10200 -27.51500 1.000 147.07881 ?  48  LYS B CB  1 
ATOM   6420 N N   . ALA F 2 43  ? -17.87400 51.61000 -27.96000 1.000 142.68482 ?  49  ALA B N   1 
ATOM   6421 C CA  . ALA F 2 43  ? -16.89200 50.54100 -28.10900 1.000 136.15696 ?  49  ALA B CA  1 
ATOM   6422 C C   . ALA F 2 43  ? -17.58700 49.21200 -28.37600 1.000 136.06985 ?  49  ALA B C   1 
ATOM   6423 O O   . ALA F 2 43  ? -18.50600 48.84600 -27.63800 1.000 135.90192 ?  49  ALA B O   1 
ATOM   6424 C CB  . ALA F 2 43  ? -16.03300 50.42100 -26.86300 1.000 132.33883 ?  49  ALA B CB  1 
ATOM   6425 N N   . PRO F 2 44  ? -17.19800 48.48900 -29.42500 1.000 132.77123 ?  50  PRO B N   1 
ATOM   6426 C CA  . PRO F 2 44  ? -17.76000 47.14600 -29.66500 1.000 132.77008 ?  50  PRO B CA  1 
ATOM   6427 C C   . PRO F 2 44  ? -17.47900 46.19500 -28.50800 1.000 123.37387 ?  50  PRO B C   1 
ATOM   6428 O O   . PRO F 2 44  ? -16.32800 45.95800 -28.14000 1.000 119.53797 ?  50  PRO B O   1 
ATOM   6429 C CB  . PRO F 2 44  ? -17.05700 46.69700 -30.95100 1.000 136.74719 ?  50  PRO B CB  1 
ATOM   6430 C CG  . PRO F 2 44  ? -16.71300 47.97600 -31.64500 1.000 142.80319 ?  50  PRO B CG  1 
ATOM   6431 C CD  . PRO F 2 44  ? -16.39300 48.96900 -30.56200 1.000 137.04758 ?  50  PRO B CD  1 
ATOM   6432 N N   . LYS F 2 45  ? -18.54800 45.68700 -27.90300 1.000 136.19441 ?  51  LYS B N   1 
ATOM   6433 C CA  . LYS F 2 45  ? -18.45800 44.67000 -26.86400 1.000 131.80468 ?  51  LYS B CA  1 
ATOM   6434 C C   . LYS F 2 45  ? -18.73200 43.29400 -27.45800 1.000 130.48968 ?  51  LYS B C   1 
ATOM   6435 O O   . LYS F 2 45  ? -19.50500 43.15300 -28.40800 1.000 135.79806 ?  51  LYS B O   1 
ATOM   6436 C CB  . LYS F 2 45  ? -19.44500 44.95100 -25.72700 1.000 134.10892 ?  51  LYS B CB  1 
ATOM   6437 N N   . LEU F 2 46  ? -18.08200 42.27500 -26.90100 1.000 134.23409 ?  52  LEU B N   1 
ATOM   6438 C CA  . LEU F 2 46  ? -18.24900 40.91500 -27.39400 1.000 133.07982 ?  52  LEU B CA  1 
ATOM   6439 C C   . LEU F 2 46  ? -19.39100 40.22500 -26.66700 1.000 134.12292 ?  52  LEU B C   1 
ATOM   6440 O O   . LEU F 2 46  ? -19.56800 40.39500 -25.45700 1.000 134.63097 ?  52  LEU B O   1 
ATOM   6441 C CB  . LEU F 2 46  ? -16.96100 40.10900 -27.21800 1.000 129.65380 ?  52  LEU B CB  1 
ATOM   6442 N N   . LEU F 2 47  ? -20.14600 39.41900 -27.40700 1.000 126.03804 ?  53  LEU B N   1 
ATOM   6443 C CA  . LEU F 2 47  ? -21.26100 38.69600 -26.81400 1.000 127.69274 ?  53  LEU B CA  1 
ATOM   6444 C C   . LEU F 2 47  ? -21.13100 37.18600 -26.89800 1.000 126.07413 ?  53  LEU B C   1 
ATOM   6445 O O   . LEU F 2 47  ? -21.44000 36.49800 -25.91800 1.000 126.55193 ?  53  LEU B O   1 
ATOM   6446 C CB  . LEU F 2 47  ? -22.58000 39.12900 -27.47800 1.000 131.97864 ?  53  LEU B CB  1 
ATOM   6447 N N   . ILE F 2 48  ? -20.66800 36.63700 -28.02200 1.000 125.17201 ?  54  ILE B N   1 
ATOM   6448 C CA  . ILE F 2 48  ? -20.64100 35.18100 -28.16700 1.000 124.55086 ?  54  ILE B CA  1 
ATOM   6449 C C   . ILE F 2 48  ? -19.28900 34.74300 -28.72200 1.000 122.27140 ?  54  ILE B C   1 
ATOM   6450 O O   . ILE F 2 48  ? -18.85000 35.26400 -29.75400 1.000 123.05445 ?  54  ILE B O   1 
ATOM   6451 C CB  . ILE F 2 48  ? -21.79100 34.67900 -29.06700 1.000 128.00367 ?  54  ILE B CB  1 
ATOM   6452 C CG1 . ILE F 2 48  ? -23.14500 34.95900 -28.41000 1.000 130.91552 ?  54  ILE B CG1 1 
ATOM   6453 C CG2 . ILE F 2 48  ? -21.66400 33.18500 -29.33500 1.000 127.81194 ?  54  ILE B CG2 1 
ATOM   6454 C CD1 . ILE F 2 48  ? -23.35100 34.24800 -27.09400 1.000 130.35520 ?  54  ILE B CD1 1 
ATOM   6455 N N   . TYR F 2 49  ? -18.63500 33.78900 -28.04100 1.000 130.05124 ?  55  TYR B N   1 
ATOM   6456 C CA  . TYR F 2 49  ? -17.38800 33.19500 -28.51200 1.000 130.18854 ?  55  TYR B CA  1 
ATOM   6457 C C   . TYR F 2 49  ? -17.54900 31.68500 -28.67700 1.000 130.96574 ?  55  TYR B C   1 
ATOM   6458 O O   . TYR F 2 49  ? -18.49300 31.08000 -28.16400 1.000 131.05641 ?  55  TYR B O   1 
ATOM   6459 C CB  . TYR F 2 49  ? -16.19500 33.46800 -27.57500 1.000 128.89554 ?  55  TYR B CB  1 
ATOM   6460 C CG  . TYR F 2 49  ? -16.29600 32.91900 -26.16400 1.000 128.69043 ?  55  TYR B CG  1 
ATOM   6461 C CD1 . TYR F 2 49  ? -17.16500 33.45900 -25.22700 1.000 129.26468 ?  55  TYR B CD1 1 
ATOM   6462 C CD2 . TYR F 2 49  ? -15.49600 31.84800 -25.77600 1.000 128.87937 ?  55  TYR B CD2 1 
ATOM   6463 C CE1 . TYR F 2 49  ? -17.23100 32.94300 -23.93500 1.000 130.77133 ?  55  TYR B CE1 1 
ATOM   6464 C CE2 . TYR F 2 49  ? -15.55700 31.32500 -24.49600 1.000 129.78454 ?  55  TYR B CE2 1 
ATOM   6465 C CZ  . TYR F 2 49  ? -16.42600 31.87600 -23.57800 1.000 131.06568 ?  55  TYR B CZ  1 
ATOM   6466 O OH  . TYR F 2 49  ? -16.50000 31.36500 -22.30000 1.000 133.39328 ?  55  TYR B OH  1 
ATOM   6467 N N   . LYS F 2 50  ? -16.62200 31.08200 -29.43000 1.000 137.41350 ?  56  LYS B N   1 
ATOM   6468 C CA  . LYS F 2 50  ? -16.68400 29.67200 -29.83500 1.000 138.48659 ?  56  LYS B CA  1 
ATOM   6469 C C   . LYS F 2 50  ? -17.99000 29.35000 -30.54900 1.000 139.88887 ?  56  LYS B C   1 
ATOM   6470 O O   . LYS F 2 50  ? -18.41900 28.18600 -30.58400 1.000 140.27900 ?  56  LYS B O   1 
ATOM   6471 C CB  . LYS F 2 50  ? -16.49300 28.71200 -28.65000 1.000 137.43981 ?  56  LYS B CB  1 
ATOM   6472 C CG  . LYS F 2 50  ? -15.40200 29.08200 -27.64900 1.000 136.30879 ?  56  LYS B CG  1 
ATOM   6473 C CD  . LYS F 2 50  ? -14.85600 27.83100 -26.94900 1.000 136.70616 ?  56  LYS B CD  1 
ATOM   6474 C CE  . LYS F 2 50  ? -13.95100 28.17600 -25.77100 1.000 135.92567 ?  56  LYS B CE  1 
ATOM   6475 N NZ  . LYS F 2 50  ? -14.65700 28.08400 -24.45800 1.000 137.00897 ?  56  LYS B NZ  1 
ATOM   6476 N N   . ALA F 2 51  ? -18.63900 30.38500 -31.08400 1.000 133.06282 ?  57  ALA B N   1 
ATOM   6477 C CA  . ALA F 2 51  ? -19.86600 30.29400 -31.86900 1.000 135.20981 ?  57  ALA B CA  1 
ATOM   6478 C C   . ALA F 2 51  ? -21.05200 29.84700 -31.01700 1.000 133.84585 ?  57  ALA B C   1 
ATOM   6479 O O   . ALA F 2 51  ? -22.19400 29.88400 -31.48600 1.000 135.51070 ?  57  ALA B O   1 
ATOM   6480 C CB  . ALA F 2 51  ? -19.68700 29.35500 -33.07100 1.000 138.27140 ?  57  ALA B CB  1 
ATOM   6481 N N   . SER F 2 52  ? -20.80100 29.41900 -29.77400 1.000 134.28425 ?  65  SER B N   1 
ATOM   6482 C CA  . SER F 2 52  ? -21.88200 29.17300 -28.81800 1.000 135.57549 ?  65  SER B CA  1 
ATOM   6483 C C   . SER F 2 52  ? -21.60300 29.62600 -27.39000 1.000 135.50890 ?  65  SER B C   1 
ATOM   6484 O O   . SER F 2 52  ? -22.56300 29.90100 -26.66500 1.000 138.66336 ?  65  SER B O   1 
ATOM   6485 C CB  . SER F 2 52  ? -22.25100 27.68600 -28.79200 1.000 139.61747 ?  65  SER B CB  1 
ATOM   6486 O OG  . SER F 2 52  ? -21.14400 26.87900 -28.42900 1.000 138.42366 ?  65  SER B OG  1 
ATOM   6487 N N   . GLU F 2 53  ? -20.35000 29.71100 -26.94700 1.000 133.46345 ?  66  GLU B N   1 
ATOM   6488 C CA  . GLU F 2 53  ? -20.05900 30.13000 -25.58200 1.000 133.71686 ?  66  GLU B CA  1 
ATOM   6489 C C   . GLU F 2 53  ? -20.41700 31.60700 -25.40900 1.000 133.51678 ?  66  GLU B C   1 
ATOM   6490 O O   . GLU F 2 53  ? -20.44500 32.38000 -26.37000 1.000 132.65665 ?  66  GLU B O   1 
ATOM   6491 C CB  . GLU F 2 53  ? -18.58000 29.92500 -25.24300 1.000 133.16781 ?  66  GLU B CB  1 
ATOM   6492 C CG  . GLU F 2 53  ? -18.01800 28.48200 -25.13300 1.000 133.89251 ?  66  GLU B CG  1 
ATOM   6493 C CD  . GLU F 2 53  ? -18.89400 27.49600 -24.36500 1.000 136.68770 ?  66  GLU B CD  1 
ATOM   6494 O OE1 . GLU F 2 53  ? -19.18000 27.74000 -23.17200 1.000 139.16582 ?  66  GLU B OE1 1 
ATOM   6495 O OE2 . GLU F 2 53  ? -19.23700 26.43800 -24.94100 1.000 138.85353 ?  66  GLU B OE2 1 
ATOM   6496 N N   . LEU F 2 54  ? -20.68800 31.99400 -24.16200 1.000 140.50071 ?  67  LEU B N   1 
ATOM   6497 C CA  . LEU F 2 54  ? -21.19300 33.32100 -23.81900 1.000 141.42417 ?  67  LEU B CA  1 
ATOM   6498 C C   . LEU F 2 54  ? -20.24100 34.01300 -22.84800 1.000 142.17881 ?  67  LEU B C   1 
ATOM   6499 O O   . LEU F 2 54  ? -19.78500 33.39500 -21.88100 1.000 144.04962 ?  67  LEU B O   1 
ATOM   6500 C CB  . LEU F 2 54  ? -22.60500 33.19100 -23.22500 1.000 144.57709 ?  67  LEU B CB  1 
ATOM   6501 C CG  . LEU F 2 54  ? -23.40000 34.29500 -22.52600 1.000 147.93020 ?  67  LEU B CG  1 
ATOM   6502 C CD1 . LEU F 2 54  ? -24.84800 34.22400 -22.97500 1.000 149.40166 ?  67  LEU B CD1 1 
ATOM   6503 C CD2 . LEU F 2 54  ? -23.31000 34.13900 -21.02100 1.000 152.52045 ?  67  LEU B CD2 1 
ATOM   6504 N N   . TYR F 2 55  ? -19.91600 35.27800 -23.11900 1.000 141.46745 ?  68  TYR B N   1 
ATOM   6505 C CA  . TYR F 2 55  ? -19.02800 36.02400 -22.23400 1.000 142.12521 ?  68  TYR B CA  1 
ATOM   6506 C C   . TYR F 2 55  ? -19.69200 36.25500 -20.88300 1.000 147.02823 ?  68  TYR B C   1 
ATOM   6507 O O   . TYR F 2 55  ? -20.92000 36.31300 -20.77100 1.000 149.88573 ?  68  TYR B O   1 
ATOM   6508 C CB  . TYR F 2 55  ? -18.65200 37.37400 -22.85200 1.000 140.01852 ?  68  TYR B CB  1 
ATOM   6509 C CG  . TYR F 2 55  ? -17.33500 37.96900 -22.38400 1.000 138.81483 ?  68  TYR B CG  1 
ATOM   6510 C CD1 . TYR F 2 55  ? -16.13700 37.59500 -22.97600 1.000 136.21768 ?  68  TYR B CD1 1 
ATOM   6511 C CD2 . TYR F 2 55  ? -17.29300 38.92300 -21.37200 1.000 140.57732 ?  68  TYR B CD2 1 
ATOM   6512 C CE1 . TYR F 2 55  ? -14.93100 38.13800 -22.56700 1.000 134.94084 ?  68  TYR B CE1 1 
ATOM   6513 C CE2 . TYR F 2 55  ? -16.08500 39.47500 -20.95600 1.000 138.84990 ?  68  TYR B CE2 1 
ATOM   6514 C CZ  . TYR F 2 55  ? -14.91000 39.07800 -21.55600 1.000 135.86195 ?  68  TYR B CZ  1 
ATOM   6515 O OH  . TYR F 2 55  ? -13.71400 39.62700 -21.13900 1.000 134.06663 ?  68  TYR B OH  1 
ATOM   6516 N N   . ALA F 2 56  ? -18.86400 36.39600 -19.84800 1.000 140.42819 ?  69  ALA B N   1 
ATOM   6517 C CA  . ALA F 2 56  ? -19.39000 36.68100 -18.52200 1.000 146.29904 ?  69  ALA B CA  1 
ATOM   6518 C C   . ALA F 2 56  ? -20.10000 38.02900 -18.51300 1.000 148.14162 ?  69  ALA B C   1 
ATOM   6519 O O   . ALA F 2 56  ? -19.61200 39.01400 -19.07400 1.000 144.44474 ?  69  ALA B O   1 
ATOM   6520 C CB  . ALA F 2 56  ? -18.27000 36.66300 -17.48200 1.000 146.64382 ?  69  ALA B CB  1 
ATOM   6521 N N   . GLY F 2 57  ? -21.25900 38.07000 -17.86100 1.000 145.47469 ?  70  GLY B N   1 
ATOM   6522 C CA  . GLY F 2 57  ? -22.09100 39.24700 -17.82600 1.000 148.54151 ?  70  GLY B CA  1 
ATOM   6523 C C   . GLY F 2 57  ? -23.09600 39.34700 -18.95700 1.000 146.97957 ?  70  GLY B C   1 
ATOM   6524 O O   . GLY F 2 57  ? -24.15900 39.95100 -18.77200 1.000 151.91368 ?  70  GLY B O   1 
ATOM   6525 N N   . VAL F 2 58  ? -22.78700 38.78200 -20.12300 1.000 143.90567 ?  71  VAL B N   1 
ATOM   6526 C CA  . VAL F 2 58  ? -23.71100 38.89300 -21.25700 1.000 142.17734 ?  71  VAL B CA  1 
ATOM   6527 C C   . VAL F 2 58  ? -25.03700 38.24400 -20.88600 1.000 146.75180 ?  71  VAL B C   1 
ATOM   6528 O O   . VAL F 2 58  ? -25.04400 37.15300 -20.28000 1.000 148.44699 ?  71  VAL B O   1 
ATOM   6529 C CB  . VAL F 2 58  ? -23.11200 38.24900 -22.51700 1.000 136.32711 ?  71  VAL B CB  1 
ATOM   6530 C CG1 . VAL F 2 58  ? -24.03200 38.44300 -23.70000 1.000 135.40904 ?  71  VAL B CG1 1 
ATOM   6531 C CG2 . VAL F 2 58  ? -21.76500 38.85500 -22.81700 1.000 132.64299 ?  71  VAL B CG2 1 
ATOM   6532 N N   . PRO F 2 59  ? -26.17600 38.86400 -21.19200 1.000 149.75992 ?  72  PRO B N   1 
ATOM   6533 C CA  . PRO F 2 59  ? -27.46200 38.32000 -20.73800 1.000 155.03520 ?  72  PRO B CA  1 
ATOM   6534 C C   . PRO F 2 59  ? -27.74900 36.94500 -21.32500 1.000 151.47098 ?  72  PRO B C   1 
ATOM   6535 O O   . PRO F 2 59  ? -27.34400 36.62400 -22.44500 1.000 148.45672 ?  72  PRO B O   1 
ATOM   6536 C CB  . PRO F 2 59  ? -28.47100 39.35800 -21.23700 1.000 158.10740 ?  72  PRO B CB  1 
ATOM   6537 C CG  . PRO F 2 59  ? -27.69000 40.62900 -21.27200 1.000 157.19718 ?  72  PRO B CG  1 
ATOM   6538 C CD  . PRO F 2 59  ? -26.30800 40.24000 -21.70200 1.000 149.84625 ?  72  PRO B CD  1 
ATOM   6539 N N   . SER F 2 60  ? -28.46200 36.12700 -20.54400 1.000 158.99667 ?  74  SER B N   1 
ATOM   6540 C CA  . SER F 2 60  ? -28.84900 34.79300 -20.99100 1.000 159.68512 ?  74  SER B CA  1 
ATOM   6541 C C   . SER F 2 60  ? -29.67800 34.81700 -22.26500 1.000 159.85496 ?  74  SER B C   1 
ATOM   6542 O O   . SER F 2 60  ? -29.68800 33.82300 -22.99900 1.000 160.43189 ?  74  SER B O   1 
ATOM   6543 C CB  . SER F 2 60  ? -29.62300 34.08200 -19.88600 1.000 166.57731 ?  74  SER B CB  1 
ATOM   6544 O OG  . SER F 2 60  ? -28.96300 34.23200 -18.64300 1.000 167.04416 ?  74  SER B OG  1 
ATOM   6545 N N   . ARG F 2 61  ? -30.37400 35.92100 -22.54200 1.000 159.69391 ?  75  ARG B N   1 
ATOM   6546 C CA  . ARG F 2 61  ? -31.18900 35.99500 -23.74600 1.000 160.27462 ?  75  ARG B CA  1 
ATOM   6547 C C   . ARG F 2 61  ? -30.34300 35.88500 -25.01000 1.000 155.30500 ?  75  ARG B C   1 
ATOM   6548 O O   . ARG F 2 61  ? -30.88600 35.58600 -26.07800 1.000 156.22547 ?  75  ARG B O   1 
ATOM   6549 C CB  . ARG F 2 61  ? -32.01200 37.28800 -23.74100 1.000 160.98136 ?  75  ARG B CB  1 
ATOM   6550 C CG  . ARG F 2 61  ? -31.38300 38.46200 -24.48200 1.000 155.56861 ?  75  ARG B CG  1 
ATOM   6551 C CD  . ARG F 2 61  ? -31.93200 39.80400 -23.98700 1.000 161.07757 ?  75  ARG B CD  1 
ATOM   6552 N NE  . ARG F 2 61  ? -31.13000 40.35000 -22.89700 1.000 162.03183 ?  75  ARG B NE  1 
ATOM   6553 C CZ  . ARG F 2 61  ? -31.47100 41.39500 -22.15300 1.000 168.48185 ?  75  ARG B CZ  1 
ATOM   6554 N NH1 . ARG F 2 61  ? -32.60800 42.03700 -22.34200 1.000 174.39991 ?  75  ARG B NH1 1 
ATOM   6555 N NH2 . ARG F 2 61  ? -30.65100 41.80100 -21.19000 1.000 169.67455 ?  75  ARG B NH2 1 
ATOM   6556 N N   . PHE F 2 62  ? -29.03200 36.10900 -24.91200 1.000 150.53948 ?  76  PHE B N   1 
ATOM   6557 C CA  . PHE F 2 62  ? -28.12500 35.95200 -26.04200 1.000 146.19643 ?  76  PHE B CA  1 
ATOM   6558 C C   . PHE F 2 62  ? -27.61600 34.52200 -26.13600 1.000 146.72601 ?  76  PHE B C   1 
ATOM   6559 O O   . PHE F 2 62  ? -27.26700 33.90600 -25.12600 1.000 148.11168 ?  76  PHE B O   1 
ATOM   6560 C CB  . PHE F 2 62  ? -26.93900 36.90700 -25.90400 1.000 141.33163 ?  76  PHE B CB  1 
ATOM   6561 C CG  . PHE F 2 62  ? -27.31800 38.35100 -25.98100 1.000 141.71769 ?  76  PHE B CG  1 
ATOM   6562 C CD1 . PHE F 2 62  ? -27.41400 38.99100 -27.20300 1.000 141.52314 ?  76  PHE B CD1 1 
ATOM   6563 C CD2 . PHE F 2 62  ? -27.62100 39.05900 -24.83600 1.000 144.99175 ?  76  PHE B CD2 1 
ATOM   6564 C CE1 . PHE F 2 62  ? -27.75900 40.32400 -27.27800 1.000 143.79487 ?  76  PHE B CE1 1 
ATOM   6565 C CE2 . PHE F 2 62  ? -27.98200 40.38500 -24.90400 1.000 147.39487 ?  76  PHE B CE2 1 
ATOM   6566 C CZ  . PHE F 2 62  ? -28.05300 41.02100 -26.12800 1.000 146.44987 ?  76  PHE B CZ  1 
ATOM   6567 N N   . SER F 2 63  ? -27.56100 34.00000 -27.36000 1.000 148.56212 ?  77  SER B N   1 
ATOM   6568 C CA  . SER F 2 63  ? -27.11600 32.62800 -27.57200 1.000 146.71191 ?  77  SER B CA  1 
ATOM   6569 C C   . SER F 2 63  ? -26.78200 32.43900 -29.04400 1.000 146.63172 ?  77  SER B C   1 
ATOM   6570 O O   . SER F 2 63  ? -27.18900 33.23200 -29.88800 1.000 148.85360 ?  77  SER B O   1 
ATOM   6571 C CB  . SER F 2 63  ? -28.16600 31.61700 -27.10700 1.000 152.80389 ?  77  SER B CB  1 
ATOM   6572 O OG  . SER F 2 63  ? -29.46100 32.04000 -27.47800 1.000 156.12537 ?  77  SER B OG  1 
ATOM   6573 N N   . GLY F 2 64  ? -25.97600 31.41900 -29.34000 1.000 144.69605 ?  78  GLY B N   1 
ATOM   6574 C CA  . GLY F 2 64  ? -25.64300 31.10300 -30.71100 1.000 145.70914 ?  78  GLY B CA  1 
ATOM   6575 C C   . GLY F 2 64  ? -25.79700 29.62700 -31.02400 1.000 146.25207 ?  78  GLY B C   1 
ATOM   6576 O O   . GLY F 2 64  ? -25.79400 28.77300 -30.13700 1.000 147.35896 ?  78  GLY B O   1 
ATOM   6577 N N   . SER F 2 65  ? -25.92800 29.34300 -32.32000 1.000 149.00950 ?  79  SER B N   1 
ATOM   6578 C CA  . SER F 2 65  ? -25.94600 27.97000 -32.81800 1.000 149.55229 ?  79  SER B CA  1 
ATOM   6579 C C   . SER F 2 65  ? -25.37900 27.97300 -34.23300 1.000 152.70740 ?  79  SER B C   1 
ATOM   6580 O O   . SER F 2 65  ? -25.19500 29.02500 -34.84000 1.000 155.33435 ?  79  SER B O   1 
ATOM   6581 C CB  . SER F 2 65  ? -27.35200 27.35200 -32.77000 1.000 154.31734 ?  79  SER B CB  1 
ATOM   6582 O OG  . SER F 2 65  ? -28.33100 28.23300 -33.28900 1.000 155.62671 ?  79  SER B OG  1 
ATOM   6583 N N   . ARG F 2 66  ? -25.07700 26.78100 -34.74900 1.000 150.07889 ?  80  ARG B N   1 
ATOM   6584 C CA  . ARG F 2 66  ? -24.37100 26.63700 -36.02100 1.000 153.37499 ?  80  ARG B CA  1 
ATOM   6585 C C   . ARG F 2 66  ? -24.97300 25.49700 -36.82400 1.000 155.22721 ?  80  ARG B C   1 
ATOM   6586 O O   . ARG F 2 66  ? -24.99200 24.35600 -36.35700 1.000 152.45052 ?  80  ARG B O   1 
ATOM   6587 C CB  . ARG F 2 66  ? -22.87400 26.39200 -35.80700 1.000 151.34240 ?  80  ARG B CB  1 
ATOM   6588 C CG  . ARG F 2 66  ? -22.10500 25.91600 -37.04700 1.000 154.55334 ?  80  ARG B CG  1 
ATOM   6589 C CD  . ARG F 2 66  ? -21.01600 24.90300 -36.67700 1.000 151.40987 ?  80  ARG B CD  1 
ATOM   6590 N NE  . ARG F 2 66  ? -20.08000 24.69700 -37.77700 1.000 154.11993 ?  80  ARG B NE  1 
ATOM   6591 C CZ  . ARG F 2 66  ? -18.77300 24.51800 -37.62500 1.000 152.58546 ?  80  ARG B CZ  1 
ATOM   6592 N NH1 . ARG F 2 66  ? -18.20600 24.52700 -36.42800 1.000 148.78690 ?  80  ARG B NH1 1 
ATOM   6593 N NH2 . ARG F 2 66  ? -18.01100 24.34300 -38.70200 1.000 155.08206 ?  80  ARG B NH2 1 
ATOM   6594 N N   . SER F 2 67  ? -25.50500 25.81800 -38.00200 1.000 153.29503 ?  83  SER B N   1 
ATOM   6595 C CA  . SER F 2 67  ? -26.02400 24.80900 -38.92800 1.000 155.62006 ?  83  SER B CA  1 
ATOM   6596 C C   . SER F 2 67  ? -25.00100 24.48700 -40.02300 1.000 157.90589 ?  83  SER B C   1 
ATOM   6597 O O   . SER F 2 67  ? -25.27200 24.60900 -41.21800 1.000 162.94813 ?  83  SER B O   1 
ATOM   6598 C CB  . SER F 2 67  ? -27.35300 25.27200 -39.51900 1.000 159.78390 ?  83  SER B CB  1 
ATOM   6599 O OG  . SER F 2 67  ? -27.80000 24.37800 -40.52200 1.000 164.15699 ?  83  SER B OG  1 
ATOM   6600 N N   . GLY F 2 68  ? -23.80400 24.07500 -39.60600 1.000 157.77738 ?  84  GLY B N   1 
ATOM   6601 C CA  . GLY F 2 68  ? -22.73800 23.76700 -40.54800 1.000 159.59736 ?  84  GLY B CA  1 
ATOM   6602 C C   . GLY F 2 68  ? -21.90400 24.94500 -41.01800 1.000 163.80387 ?  84  GLY B C   1 
ATOM   6603 O O   . GLY F 2 68  ? -20.80300 25.17100 -40.50800 1.000 161.67846 ?  84  GLY B O   1 
ATOM   6604 N N   . THR F 2 69  ? -22.39200 25.68400 -42.01600 1.000 157.71212 ?  85  THR B N   1 
ATOM   6605 C CA  . THR F 2 69  ? -21.73600 26.90300 -42.47900 1.000 163.25740 ?  85  THR B CA  1 
ATOM   6606 C C   . THR F 2 69  ? -22.56600 28.14100 -42.17000 1.000 166.45291 ?  85  THR B C   1 
ATOM   6607 O O   . THR F 2 69  ? -22.23900 29.23700 -42.63700 1.000 172.19444 ?  85  THR B O   1 
ATOM   6608 C CB  . THR F 2 69  ? -21.43100 26.83400 -43.98000 1.000 167.53163 ?  85  THR B CB  1 
ATOM   6609 O OG1 . THR F 2 69  ? -22.57100 27.27000 -44.73300 1.000 170.64698 ?  85  THR B OG1 1 
ATOM   6610 C CG2 . THR F 2 69  ? -21.06000 25.41100 -44.39200 1.000 162.28985 ?  85  THR B CG2 1 
ATOM   6611 N N   . ASP F 2 70  ? -23.63200 27.98300 -41.39200 1.000 159.56383 ?  86  ASP B N   1 
ATOM   6612 C CA  . ASP F 2 70  ? -24.60200 29.03600 -41.09800 1.000 161.59684 ?  86  ASP B CA  1 
ATOM   6613 C C   . ASP F 2 70  ? -24.67500 29.23500 -39.58700 1.000 153.99760 ?  86  ASP B C   1 
ATOM   6614 O O   . ASP F 2 70  ? -25.34400 28.46800 -38.88900 1.000 149.38274 ?  86  ASP B O   1 
ATOM   6615 C CB  . ASP F 2 70  ? -25.96800 28.66900 -41.66100 1.000 164.44551 ?  86  ASP B CB  1 
ATOM   6616 C CG  . ASP F 2 70  ? -26.27400 29.38600 -42.94700 1.000 173.00304 ?  86  ASP B CG  1 
ATOM   6617 O OD1 . ASP F 2 70  ? -25.56700 30.37100 -43.25400 1.000 176.85249 ?  86  ASP B OD1 1 
ATOM   6618 O OD2 . ASP F 2 70  ? -27.21400 28.95400 -43.64800 1.000 174.29781 -1 86  ASP B OD2 1 
ATOM   6619 N N   . PHE F 2 71  ? -23.99000 30.25500 -39.07900 1.000 157.97196 ?  87  PHE B N   1 
ATOM   6620 C CA  . PHE F 2 71  ? -23.99900 30.53600 -37.64900 1.000 150.84131 ?  87  PHE B CA  1 
ATOM   6621 C C   . PHE F 2 71  ? -25.06700 31.57300 -37.34100 1.000 151.89024 ?  87  PHE B C   1 
ATOM   6622 O O   . PHE F 2 71  ? -25.13500 32.60100 -38.00700 1.000 157.39672 ?  87  PHE B O   1 
ATOM   6623 C CB  . PHE F 2 71  ? -22.63600 31.04500 -37.18700 1.000 148.26920 ?  87  PHE B CB  1 
ATOM   6624 C CG  . PHE F 2 71  ? -21.51200 30.09800 -37.45900 1.000 147.70197 ?  87  PHE B CG  1 
ATOM   6625 C CD1 . PHE F 2 71  ? -21.06400 29.87500 -38.75000 1.000 153.94528 ?  87  PHE B CD1 1 
ATOM   6626 C CD2 . PHE F 2 71  ? -20.90400 29.42400 -36.41800 1.000 141.60669 ?  87  PHE B CD2 1 
ATOM   6627 C CE1 . PHE F 2 71  ? -20.02800 29.00600 -38.99300 1.000 153.12160 ?  87  PHE B CE1 1 
ATOM   6628 C CE2 . PHE F 2 71  ? -19.86800 28.55400 -36.65300 1.000 141.21254 ?  87  PHE B CE2 1 
ATOM   6629 C CZ  . PHE F 2 71  ? -19.42800 28.34100 -37.94200 1.000 146.48643 ?  87  PHE B CZ  1 
ATOM   6630 N N   . THR F 2 72  ? -25.85200 31.35200 -36.29600 1.000 152.67783 ?  88  THR B N   1 
ATOM   6631 C CA  . THR F 2 72  ? -26.91800 32.28100 -35.96500 1.000 153.94829 ?  88  THR B CA  1 
ATOM   6632 C C   . THR F 2 72  ? -26.76400 32.76100 -34.53300 1.000 148.08749 ?  88  THR B C   1 
ATOM   6633 O O   . THR F 2 72  ? -26.39700 31.98800 -33.63600 1.000 143.37091 ?  88  THR B O   1 
ATOM   6634 C CB  . THR F 2 72  ? -28.31000 31.65300 -36.12700 1.000 156.11351 ?  88  THR B CB  1 
ATOM   6635 O OG1 . THR F 2 72  ? -28.60400 30.83700 -34.98600 1.000 150.80953 ?  88  THR B OG1 1 
ATOM   6636 C CG2 . THR F 2 72  ? -28.38300 30.80900 -37.38100 1.000 160.59754 ?  88  THR B CG2 1 
ATOM   6637 N N   . LEU F 2 73  ? -27.08800 34.03500 -34.34600 1.000 151.05620 ?  89  LEU B N   1 
ATOM   6638 C CA  . LEU F 2 73  ? -27.17100 34.68800 -33.05000 1.000 147.01798 ?  89  LEU B CA  1 
ATOM   6639 C C   . LEU F 2 73  ? -28.63800 34.91700 -32.73300 1.000 149.71799 ?  89  LEU B C   1 
ATOM   6640 O O   . LEU F 2 73  ? -29.37600 35.48500 -33.54600 1.000 155.22628 ?  89  LEU B O   1 
ATOM   6641 C CB  . LEU F 2 73  ? -26.41500 36.01800 -33.05400 1.000 146.68462 ?  89  LEU B CB  1 
ATOM   6642 C CG  . LEU F 2 73  ? -26.50000 36.87800 -31.79500 1.000 143.54478 ?  89  LEU B CG  1 
ATOM   6643 C CD1 . LEU F 2 73  ? -25.97700 36.10900 -30.59800 1.000 138.69624 ?  89  LEU B CD1 1 
ATOM   6644 C CD2 . LEU F 2 73  ? -25.72300 38.17500 -31.98400 1.000 143.39085 ?  89  LEU B CD2 1 
ATOM   6645 N N   . THR F 2 74  ? -29.04700 34.48100 -31.54900 1.000 153.30509 ?  90  THR B N   1 
ATOM   6646 C CA  . THR F 2 74  ? -30.43500 34.44200 -31.13200 1.000 156.22192 ?  90  THR B CA  1 
ATOM   6647 C C   . THR F 2 74  ? -30.58800 35.24900 -29.85400 1.000 155.58557 ?  90  THR B C   1 
ATOM   6648 O O   . THR F 2 74  ? -29.83800 35.05500 -28.88900 1.000 151.96538 ?  90  THR B O   1 
ATOM   6649 C CB  . THR F 2 74  ? -30.90200 32.99900 -30.92700 1.000 156.21768 ?  90  THR B CB  1 
ATOM   6650 O OG1 . THR F 2 74  ? -30.87100 32.31000 -32.18400 1.000 156.96148 ?  90  THR B OG1 1 
ATOM   6651 C CG2 . THR F 2 74  ? -32.31800 32.96300 -30.37800 1.000 162.12582 ?  90  THR B CG2 1 
ATOM   6652 N N   . ILE F 2 75  ? -31.55600 36.15700 -29.86800 1.000 153.67252 ?  91  ILE B N   1 
ATOM   6653 C CA  . ILE F 2 75  ? -31.96300 36.94600 -28.71700 1.000 154.80052 ?  91  ILE B CA  1 
ATOM   6654 C C   . ILE F 2 75  ? -33.36400 36.48600 -28.36000 1.000 161.15200 ?  91  ILE B C   1 
ATOM   6655 O O   . ILE F 2 75  ? -34.27600 36.54600 -29.19600 1.000 163.81525 ?  91  ILE B O   1 
ATOM   6656 C CB  . ILE F 2 75  ? -31.94800 38.45300 -29.01700 1.000 155.00801 ?  91  ILE B CB  1 
ATOM   6657 C CG1 . ILE F 2 75  ? -30.53600 39.03200 -28.97600 1.000 150.58147 ?  91  ILE B CG1 1 
ATOM   6658 C CG2 . ILE F 2 75  ? -32.83400 39.20200 -28.03700 1.000 159.22664 ?  91  ILE B CG2 1 
ATOM   6659 C CD1 . ILE F 2 75  ? -30.52800 40.54500 -29.12600 1.000 152.67749 ?  91  ILE B CD1 1 
ATOM   6660 N N   . SER F 2 76  ? -33.53000 36.01100 -27.12600 1.000 164.07015 ?  92  SER B N   1 
ATOM   6661 C CA  . SER F 2 76  ? -34.80100 35.42000 -26.72800 1.000 170.94003 ?  92  SER B CA  1 
ATOM   6662 C C   . SER F 2 76  ? -35.86200 36.49300 -26.50100 1.000 173.47276 ?  92  SER B C   1 
ATOM   6663 O O   . SER F 2 76  ? -36.87400 36.53700 -27.20900 1.000 176.78826 ?  92  SER B O   1 
ATOM   6664 C CB  . SER F 2 76  ? -34.59300 34.56600 -25.47600 1.000 173.80344 ?  92  SER B CB  1 
ATOM   6665 O OG  . SER F 2 76  ? -34.71000 35.33700 -24.29400 1.000 174.57811 ?  92  SER B OG  1 
ATOM   6666 N N   . SER F 2 77  ? -35.65300 37.37000 -25.52300 1.000 172.24503 ?  93  SER B N   1 
ATOM   6667 C CA  . SER F 2 77  ? -36.58000 38.46500 -25.23400 1.000 174.44822 ?  93  SER B CA  1 
ATOM   6668 C C   . SER F 2 77  ? -35.94000 39.79000 -25.64000 1.000 168.86968 ?  93  SER B C   1 
ATOM   6669 O O   . SER F 2 77  ? -35.11700 40.33800 -24.89800 1.000 167.52159 ?  93  SER B O   1 
ATOM   6670 C CB  . SER F 2 77  ? -36.96600 38.48100 -23.75900 1.000 178.52172 ?  93  SER B CB  1 
ATOM   6671 O OG  . SER F 2 77  ? -35.81800 38.55100 -22.93300 1.000 175.07598 ?  93  SER B OG  1 
ATOM   6672 N N   . LEU F 2 78  ? -36.28200 40.29400 -26.82700 1.000 167.89437 ?  94  LEU B N   1 
ATOM   6673 C CA  . LEU F 2 78  ? -35.75800 41.59800 -27.22000 1.000 163.53669 ?  94  LEU B CA  1 
ATOM   6674 C C   . LEU F 2 78  ? -36.20300 42.67900 -26.24500 1.000 167.45136 ?  94  LEU B C   1 
ATOM   6675 O O   . LEU F 2 78  ? -37.38200 43.04700 -26.20900 1.000 172.72863 ?  94  LEU B O   1 
ATOM   6676 C CB  . LEU F 2 78  ? -36.20700 41.97600 -28.63300 1.000 165.26085 ?  94  LEU B CB  1 
ATOM   6677 C CG  . LEU F 2 78  ? -35.57200 43.24500 -29.21200 1.000 165.66685 ?  94  LEU B CG  1 
ATOM   6678 C CD1 . LEU F 2 78  ? -34.10400 43.38100 -28.81800 1.000 159.19252 ?  94  LEU B CD1 1 
ATOM   6679 C CD2 . LEU F 2 78  ? -35.74200 43.28800 -30.72000 1.000 168.09770 ?  94  LEU B CD2 1 
ATOM   6680 N N   . GLN F 2 79  ? -35.27200 43.19800 -25.46600 1.000 167.51156 ?  95  GLN B N   1 
ATOM   6681 C CA  . GLN F 2 79  ? -35.60800 44.29300 -24.58100 1.000 172.77784 ?  95  GLN B CA  1 
ATOM   6682 C C   . GLN F 2 79  ? -34.98400 45.57800 -25.11400 1.000 172.00209 ?  95  GLN B C   1 
ATOM   6683 O O   . GLN F 2 79  ? -33.98000 45.52700 -25.82700 1.000 165.88066 ?  95  GLN B O   1 
ATOM   6684 C CB  . GLN F 2 79  ? -35.13800 44.02900 -23.14500 1.000 173.38494 ?  95  GLN B CB  1 
ATOM   6685 C CG  . GLN F 2 79  ? -35.53900 42.65700 -22.60300 1.000 173.50090 ?  95  GLN B CG  1 
ATOM   6686 C CD  . GLN F 2 79  ? -37.03300 42.40400 -22.60900 1.000 177.37531 ?  95  GLN B CD  1 
ATOM   6687 O OE1 . GLN F 2 79  ? -37.57500 41.89200 -23.58700 1.000 176.14584 ?  95  GLN B OE1 1 
ATOM   6688 N NE2 . GLN F 2 79  ? -37.70200 42.73400 -21.50800 1.000 181.20599 ?  95  GLN B NE2 1 
ATOM   6689 N N   . PRO F 2 80  ? -35.55100 46.74500 -24.79800 1.000 173.76296 ?  96  PRO B N   1 
ATOM   6690 C CA  . PRO F 2 80  ? -35.08100 47.97600 -25.45300 1.000 172.81574 ?  96  PRO B CA  1 
ATOM   6691 C C   . PRO F 2 80  ? -33.61000 48.25800 -25.22300 1.000 166.15742 ?  96  PRO B C   1 
ATOM   6692 O O   . PRO F 2 80  ? -32.98400 48.91300 -26.06500 1.000 161.88370 ?  96  PRO B O   1 
ATOM   6693 C CB  . PRO F 2 80  ? -35.98600 49.06600 -24.85600 1.000 177.68023 ?  96  PRO B CB  1 
ATOM   6694 C CG  . PRO F 2 80  ? -37.14000 48.33000 -24.24300 1.000 181.13443 ?  96  PRO B CG  1 
ATOM   6695 C CD  . PRO F 2 80  ? -36.58900 47.02500 -23.79300 1.000 179.66737 ?  96  PRO B CD  1 
ATOM   6696 N N   . GLU F 2 81  ? -33.03000 47.79200 -24.10900 1.000 170.65762 ?  97  GLU B N   1 
ATOM   6697 C CA  . GLU F 2 81  ? -31.60400 48.02300 -23.89200 1.000 163.39535 ?  97  GLU B CA  1 
ATOM   6698 C C   . GLU F 2 81  ? -30.76800 47.45000 -25.02700 1.000 155.53818 ?  97  GLU B C   1 
ATOM   6699 O O   . GLU F 2 81  ? -29.69000 47.97500 -25.32600 1.000 149.84024 ?  97  GLU B O   1 
ATOM   6700 C CB  . GLU F 2 81  ? -31.14900 47.41900 -22.56400 1.000 164.19690 ?  97  GLU B CB  1 
ATOM   6701 C CG  . GLU F 2 81  ? -32.08700 47.64600 -21.40500 1.000 173.88595 ?  97  GLU B CG  1 
ATOM   6702 C CD  . GLU F 2 81  ? -33.09900 46.53300 -21.25800 1.000 177.71293 ?  97  GLU B CD  1 
ATOM   6703 O OE1 . GLU F 2 81  ? -32.76000 45.52200 -20.61100 1.000 177.04090 ?  97  GLU B OE1 1 
ATOM   6704 O OE2 . GLU F 2 81  ? -34.23300 46.67700 -21.77000 1.000 181.07764 -1 97  GLU B OE2 1 
ATOM   6705 N N   . ASP F 2 82  ? -31.23900 46.38100 -25.66900 1.000 160.71042 ?  98  ASP B N   1 
ATOM   6706 C CA  . ASP F 2 82  ? -30.45600 45.69700 -26.69600 1.000 154.29844 ?  98  ASP B CA  1 
ATOM   6707 C C   . ASP F 2 82  ? -30.63400 46.34600 -28.05700 1.000 155.60133 ?  98  ASP B C   1 
ATOM   6708 O O   . ASP F 2 82  ? -30.78000 45.65300 -29.06600 1.000 155.64109 ?  98  ASP B O   1 
ATOM   6709 C CB  . ASP F 2 82  ? -30.85500 44.22600 -26.75800 1.000 153.79647 ?  98  ASP B CB  1 
ATOM   6710 C CG  . ASP F 2 82  ? -30.93800 43.58500 -25.39100 1.000 154.89016 ?  98  ASP B CG  1 
ATOM   6711 O OD1 . ASP F 2 82  ? -30.17000 43.98200 -24.49400 1.000 153.77494 ?  98  ASP B OD1 1 
ATOM   6712 O OD2 . ASP F 2 82  ? -31.76700 42.67000 -25.21300 1.000 157.46267 -1 98  ASP B OD2 1 
ATOM   6713 N N   . PHE F 2 83  ? -30.63600 47.67200 -28.12500 1.000 151.78053 ?  99  PHE B N   1 
ATOM   6714 C CA  . PHE F 2 83  ? -30.70400 48.38900 -29.39100 1.000 153.71470 ?  99  PHE B CA  1 
ATOM   6715 C C   . PHE F 2 83  ? -29.28700 48.72700 -29.84600 1.000 147.73740 ?  99  PHE B C   1 
ATOM   6716 O O   . PHE F 2 83  ? -28.58400 49.48500 -29.16800 1.000 144.39322 ?  99  PHE B O   1 
ATOM   6717 C CB  . PHE F 2 83  ? -31.56600 49.64300 -29.23600 1.000 159.25151 ?  99  PHE B CB  1 
ATOM   6718 C CG  . PHE F 2 83  ? -31.33700 50.67400 -30.29300 1.000 160.04556 ?  99  PHE B CG  1 
ATOM   6719 C CD1 . PHE F 2 83  ? -31.89400 50.53300 -31.55300 1.000 164.81307 ?  99  PHE B CD1 1 
ATOM   6720 C CD2 . PHE F 2 83  ? -30.58300 51.79700 -30.02100 1.000 156.75241 ?  99  PHE B CD2 1 
ATOM   6721 C CE1 . PHE F 2 83  ? -31.68900 51.48700 -32.52900 1.000 166.65929 ?  99  PHE B CE1 1 
ATOM   6722 C CE2 . PHE F 2 83  ? -30.37600 52.74800 -30.98600 1.000 158.05519 ?  99  PHE B CE2 1 
ATOM   6723 C CZ  . PHE F 2 83  ? -30.93100 52.60000 -32.24300 1.000 163.31536 ?  99  PHE B CZ  1 
ATOM   6724 N N   . ALA F 2 84  ? -28.87700 48.18600 -30.99200 1.000 148.54945 ?  100 ALA B N   1 
ATOM   6725 C CA  . ALA F 2 84  ? -27.50100 48.34600 -31.46100 1.000 144.91134 ?  100 ALA B CA  1 
ATOM   6726 C C   . ALA F 2 84  ? -27.38300 47.80500 -32.88200 1.000 150.08884 ?  100 ALA B C   1 
ATOM   6727 O O   . ALA F 2 84  ? -28.37300 47.43200 -33.51700 1.000 155.44549 ?  100 ALA B O   1 
ATOM   6728 C CB  . ALA F 2 84  ? -26.51200 47.63800 -30.53500 1.000 137.60439 ?  100 ALA B CB  1 
ATOM   6729 N N   . THR F 2 85  ? -26.15200 47.78400 -33.38400 1.000 142.74840 ?  101 THR B N   1 
ATOM   6730 C CA  . THR F 2 85  ? -25.82400 47.07100 -34.60900 1.000 146.65913 ?  101 THR B CA  1 
ATOM   6731 C C   . THR F 2 85  ? -24.88900 45.91700 -34.26700 1.000 144.58129 ?  101 THR B C   1 
ATOM   6732 O O   . THR F 2 85  ? -23.91500 46.09700 -33.52600 1.000 137.85810 ?  101 THR B O   1 
ATOM   6733 C CB  . THR F 2 85  ? -25.19900 48.00200 -35.64800 1.000 146.08414 ?  101 THR B CB  1 
ATOM   6734 O OG1 . THR F 2 85  ? -26.10200 49.08200 -35.92000 1.000 146.93168 ?  101 THR B OG1 1 
ATOM   6735 C CG2 . THR F 2 85  ? -24.94000 47.25200 -36.94300 1.000 149.90365 ?  101 THR B CG2 1 
ATOM   6736 N N   . TYR F 2 86  ? -25.20400 44.73000 -34.78200 1.000 143.07775 ?  102 TYR B N   1 
ATOM   6737 C CA  . TYR F 2 86  ? -24.49300 43.50600 -34.43100 1.000 141.09517 ?  102 TYR B CA  1 
ATOM   6738 C C   . TYR F 2 86  ? -23.64700 42.99100 -35.59100 1.000 143.72453 ?  102 TYR B C   1 
ATOM   6739 O O   . TYR F 2 86  ? -24.08300 43.01300 -36.75000 1.000 148.72899 ?  102 TYR B O   1 
ATOM   6740 C CB  . TYR F 2 86  ? -25.46700 42.41300 -33.98100 1.000 143.67917 ?  102 TYR B CB  1 
ATOM   6741 C CG  . TYR F 2 86  ? -26.21800 42.74600 -32.71000 1.000 139.73316 ?  102 TYR B CG  1 
ATOM   6742 C CD1 . TYR F 2 86  ? -27.23500 43.69000 -32.69700 1.000 143.30708 ?  102 TYR B CD1 1 
ATOM   6743 C CD2 . TYR F 2 86  ? -25.88100 42.13700 -31.51300 1.000 130.37785 ?  102 TYR B CD2 1 
ATOM   6744 C CE1 . TYR F 2 86  ? -27.91200 43.99600 -31.53200 1.000 140.04973 ?  102 TYR B CE1 1 
ATOM   6745 C CE2 . TYR F 2 86  ? -26.54900 42.43900 -30.34300 1.000 125.40567 ?  102 TYR B CE2 1 
ATOM   6746 C CZ  . TYR F 2 86  ? -27.56400 43.36800 -30.35800 1.000 131.07175 ?  102 TYR B CZ  1 
ATOM   6747 O OH  . TYR F 2 86  ? -28.23100 43.67000 -29.19400 1.000 126.66681 ?  102 TYR B OH  1 
ATOM   6748 N N   . TYR F 2 87  ? -22.42600 42.54000 -35.26600 1.000 142.25225 ?  103 TYR B N   1 
ATOM   6749 C CA  . TYR F 2 87  ? -21.47900 42.03500 -36.25600 1.000 144.53039 ?  103 TYR B CA  1 
ATOM   6750 C C   . TYR F 2 87  ? -21.03600 40.61700 -35.90100 1.000 142.74025 ?  103 TYR B C   1 
ATOM   6751 O O   . TYR F 2 87  ? -20.95600 40.25300 -34.72000 1.000 135.10863 ?  103 TYR B O   1 
ATOM   6752 C CB  . TYR F 2 87  ? -20.22300 42.91400 -36.35500 1.000 140.00640 ?  103 TYR B CB  1 
ATOM   6753 C CG  . TYR F 2 87  ? -20.42400 44.31600 -36.88200 1.000 140.88810 ?  103 TYR B CG  1 
ATOM   6754 C CD1 . TYR F 2 87  ? -20.37500 44.58700 -38.24100 1.000 144.90358 ?  103 TYR B CD1 1 
ATOM   6755 C CD2 . TYR F 2 87  ? -20.62100 45.37900 -36.00800 1.000 136.40184 ?  103 TYR B CD2 1 
ATOM   6756 C CE1 . TYR F 2 87  ? -20.53600 45.87900 -38.71500 1.000 144.38751 ?  103 TYR B CE1 1 
ATOM   6757 C CE2 . TYR F 2 87  ? -20.78700 46.67000 -36.47100 1.000 136.73577 ?  103 TYR B CE2 1 
ATOM   6758 C CZ  . TYR F 2 87  ? -20.74200 46.91500 -37.82600 1.000 140.62619 ?  103 TYR B CZ  1 
ATOM   6759 O OH  . TYR F 2 87  ? -20.90600 48.19800 -38.30000 1.000 140.07838 ?  103 TYR B OH  1 
ATOM   6760 N N   . CYS F 2 88  ? -20.70900 39.82700 -36.93300 1.000 143.61216 ?  104 CYS B N   1 
ATOM   6761 C CA  . CYS F 2 88  ? -20.18400 38.47600 -36.77100 1.000 142.07635 ?  104 CYS B CA  1 
ATOM   6762 C C   . CYS F 2 88  ? -18.78100 38.38000 -37.35800 1.000 141.36936 ?  104 CYS B C   1 
ATOM   6763 O O   . CYS F 2 88  ? -18.51800 38.87800 -38.45600 1.000 145.93071 ?  104 CYS B O   1 
ATOM   6764 C CB  . CYS F 2 88  ? -21.08600 37.43400 -37.44400 1.000 149.21160 ?  104 CYS B CB  1 
ATOM   6765 S SG  . CYS F 2 88  ? -21.38700 37.72300 -39.20500 1.000 156.72769 ?  104 CYS B SG  1 
ATOM   6766 N N   . GLN F 2 89  ? -17.88700 37.73900 -36.60900 1.000 145.56685 ?  105 GLN B N   1 
ATOM   6767 C CA  . GLN F 2 89  ? -16.46700 37.63400 -36.92300 1.000 143.68250 ?  105 GLN B CA  1 
ATOM   6768 C C   . GLN F 2 89  ? -16.09100 36.17700 -37.15100 1.000 144.25983 ?  105 GLN B C   1 
ATOM   6769 O O   . GLN F 2 89  ? -16.19500 35.36400 -36.22700 1.000 136.67674 ?  105 GLN B O   1 
ATOM   6770 C CB  . GLN F 2 89  ? -15.64900 38.23700 -35.78600 1.000 132.83055 ?  105 GLN B CB  1 
ATOM   6771 C CG  . GLN F 2 89  ? -14.18200 38.38500 -36.04400 1.000 130.82041 ?  105 GLN B CG  1 
ATOM   6772 C CD  . GLN F 2 89  ? -13.44600 38.56600 -34.74800 1.000 119.46332 ?  105 GLN B CD  1 
ATOM   6773 O OE1 . GLN F 2 89  ? -13.78800 37.93800 -33.74400 1.000 113.11426 ?  105 GLN B OE1 1 
ATOM   6774 N NE2 . GLN F 2 89  ? -12.45100 39.44700 -34.74100 1.000 116.87109 ?  105 GLN B NE2 1 
ATOM   6775 N N   . GLN F 2 90  ? -15.66200 35.84400 -38.37200 1.000 153.12250 ?  106 GLN B N   1 
ATOM   6776 C CA  . GLN F 2 90  ? -15.32400 34.45200 -38.66400 1.000 154.07763 ?  106 GLN B CA  1 
ATOM   6777 C C   . GLN F 2 90  ? -13.99000 34.01700 -38.05100 1.000 146.18461 ?  106 GLN B C   1 
ATOM   6778 O O   . GLN F 2 90  ? -13.81100 32.82500 -37.77400 1.000 142.16386 ?  106 GLN B O   1 
ATOM   6779 C CB  . GLN F 2 90  ? -15.31100 34.22600 -40.17700 1.000 163.26290 ?  106 GLN B CB  1 
ATOM   6780 N N   . ARG F 2 91  ? -13.05100 34.94500 -37.83900 1.000 149.55098 ?  107 ARG B N   1 
ATOM   6781 C CA  . ARG F 2 91  ? -11.74100 34.67100 -37.23500 1.000 142.21244 ?  107 ARG B CA  1 
ATOM   6782 C C   . ARG F 2 91  ? -10.92700 33.61000 -37.96600 1.000 146.12211 ?  107 ARG B C   1 
ATOM   6783 O O   . ARG F 2 91  ? -11.29400 33.16700 -39.05800 1.000 154.86452 ?  107 ARG B O   1 
ATOM   6784 C CB  . ARG F 2 91  ? -11.85100 34.23400 -35.77000 1.000 130.69873 ?  107 ARG B CB  1 
ATOM   6785 C CG  . ARG F 2 91  ? -12.04700 35.35300 -34.76700 1.000 124.12034 ?  107 ARG B CG  1 
ATOM   6786 C CD  . ARG F 2 91  ? -11.04200 36.52500 -34.90400 1.000 123.49131 ?  107 ARG B CD  1 
ATOM   6787 N NE  . ARG F 2 91  ? -9.68100  36.24700 -35.34800 1.000 124.66066 ?  107 ARG B NE  1 
ATOM   6788 C CZ  . ARG F 2 91  ? -8.62000  36.19700 -34.54900 1.000 117.75559 ?  107 ARG B CZ  1 
ATOM   6789 N NH1 . ARG F 2 91  ? -8.72800  36.34700 -33.23700 1.000 109.87999 ?  107 ARG B NH1 1 
ATOM   6790 N NH2 . ARG F 2 91  ? -7.41500  36.02200 -35.08100 1.000 120.14979 ?  107 ARG B NH2 1 
ATOM   6791 N N   . GLY F 2 92  ? -9.83600  33.17200 -37.33800 1.000 134.39290 ?  108 GLY B N   1 
ATOM   6792 C CA  . GLY F 2 92  ? -8.92200  32.24300 -38.00900 1.000 137.98226 ?  108 GLY B CA  1 
ATOM   6793 C C   . GLY F 2 92  ? -7.55200  32.88100 -38.13100 1.000 138.08701 ?  108 GLY B C   1 
ATOM   6794 O O   . GLY F 2 92  ? -7.43000  34.07400 -38.41200 1.000 140.34995 ?  108 GLY B O   1 
ATOM   6795 N N   . TRP F 2 93  ? -6.50300  32.10100 -37.85000 1.000 138.61136 ?  109 TRP B N   1 
ATOM   6796 C CA  . TRP F 2 93  ? -5.15900  32.60100 -38.11800 1.000 140.04178 ?  109 TRP B CA  1 
ATOM   6797 C C   . TRP F 2 93  ? -5.12900  33.18000 -39.51900 1.000 150.58020 ?  109 TRP B C   1 
ATOM   6798 O O   . TRP F 2 93  ? -5.49600  32.49600 -40.47800 1.000 157.60144 ?  109 TRP B O   1 
ATOM   6799 C CB  . TRP F 2 93  ? -4.10200  31.49300 -38.03100 1.000 138.72662 ?  109 TRP B CB  1 
ATOM   6800 C CG  . TRP F 2 93  ? -3.42300  31.25600 -36.71500 1.000 129.01900 ?  109 TRP B CG  1 
ATOM   6801 C CD1 . TRP F 2 93  ? -3.15100  30.04100 -36.16000 1.000 124.99683 ?  109 TRP B CD1 1 
ATOM   6802 C CD2 . TRP F 2 93  ? -2.93200  32.23800 -35.79000 1.000 122.57219 ?  109 TRP B CD2 1 
ATOM   6803 N NE1 . TRP F 2 93  ? -2.51200  30.20000 -34.95900 1.000 117.87726 ?  109 TRP B NE1 1 
ATOM   6804 C CE2 . TRP F 2 93  ? -2.37000  31.53700 -34.70300 1.000 116.08847 ?  109 TRP B CE2 1 
ATOM   6805 C CE3 . TRP F 2 93  ? -2.91800  33.63300 -35.77100 1.000 121.83140 ?  109 TRP B CE3 1 
ATOM   6806 C CZ2 . TRP F 2 93  ? -1.80400  32.17800 -33.61200 1.000 110.91588 ?  109 TRP B CZ2 1 
ATOM   6807 C CZ3 . TRP F 2 93  ? -2.35100  34.26900 -34.68400 1.000 114.30255 ?  109 TRP B CZ3 1 
ATOM   6808 C CH2 . TRP F 2 93  ? -1.79800  33.53900 -33.61900 1.000 110.27305 ?  109 TRP B CH2 1 
ATOM   6809 N N   . TYR F 2 94  ? -4.72700  34.44900 -39.63200 1.000 138.80557 ?  114 TYR B N   1 
ATOM   6810 C CA  . TYR F 2 94  ? -4.65000  35.15200 -40.90700 1.000 146.88633 ?  114 TYR B CA  1 
ATOM   6811 C C   . TYR F 2 94  ? -6.02800  35.47800 -41.48100 1.000 151.14380 ?  114 TYR B C   1 
ATOM   6812 O O   . TYR F 2 94  ? -6.14600  35.76200 -42.67600 1.000 155.59605 ?  114 TYR B O   1 
ATOM   6813 C CB  . TYR F 2 94  ? -3.85900  34.34100 -41.94000 1.000 152.46735 ?  114 TYR B CB  1 
ATOM   6814 C CG  . TYR F 2 94  ? -2.46000  33.96200 -41.52300 1.000 149.75100 ?  114 TYR B CG  1 
ATOM   6815 C CD1 . TYR F 2 94  ? -1.79600  34.64100 -40.51400 1.000 142.66282 ?  114 TYR B CD1 1 
ATOM   6816 C CD2 . TYR F 2 94  ? -1.82600  32.87900 -42.10900 1.000 152.93053 ?  114 TYR B CD2 1 
ATOM   6817 C CE1 . TYR F 2 94  ? -0.52300  34.27500 -40.13200 1.000 139.78857 ?  114 TYR B CE1 1 
ATOM   6818 C CE2 . TYR F 2 94  ? -0.56500  32.50300 -41.73000 1.000 150.72873 ?  114 TYR B CE2 1 
ATOM   6819 C CZ  . TYR F 2 94  ? 0.08600   33.20100 -40.74700 1.000 144.13028 ?  114 TYR B CZ  1 
ATOM   6820 O OH  . TYR F 2 94  ? 1.35300   32.80900 -40.39400 1.000 141.59329 ?  114 TYR B OH  1 
ATOM   6821 N N   . LEU F 2 95  ? -7.08700  35.40900 -40.67500 1.000 146.01548 ?  115 LEU B N   1 
ATOM   6822 C CA  . LEU F 2 95  ? -8.43900  35.55800 -41.20100 1.000 150.46126 ?  115 LEU B CA  1 
ATOM   6823 C C   . LEU F 2 95  ? -9.31200  36.26800 -40.17800 1.000 144.82280 ?  115 LEU B C   1 
ATOM   6824 O O   . LEU F 2 95  ? -9.31000  35.88700 -39.00600 1.000 137.05570 ?  115 LEU B O   1 
ATOM   6825 C CB  . LEU F 2 95  ? -9.02600  34.17900 -41.53300 1.000 153.16038 ?  115 LEU B CB  1 
ATOM   6826 C CG  . LEU F 2 95  ? -10.48400 34.08400 -41.97600 1.000 155.89193 ?  115 LEU B CG  1 
ATOM   6827 C CD1 . LEU F 2 95  ? -10.64400 34.85500 -43.26100 1.000 158.89732 ?  115 LEU B CD1 1 
ATOM   6828 C CD2 . LEU F 2 95  ? -10.92300 32.63400 -42.14800 1.000 157.39662 ?  115 LEU B CD2 1 
ATOM   6829 N N   . PHE F 2 96  ? -10.03100 37.31200 -40.59800 1.000 157.45591 ?  116 PHE B N   1 
ATOM   6830 C CA  . PHE F 2 96  ? -11.03400 37.91700 -39.72600 1.000 153.11084 ?  116 PHE B CA  1 
ATOM   6831 C C   . PHE F 2 96  ? -12.44100 37.87000 -40.30600 1.000 158.60854 ?  116 PHE B C   1 
ATOM   6832 O O   . PHE F 2 96  ? -13.33000 37.29200 -39.67400 1.000 157.31795 ?  116 PHE B O   1 
ATOM   6833 C CB  . PHE F 2 96  ? -10.61600 39.34200 -39.36200 1.000 148.30617 ?  116 PHE B CB  1 
ATOM   6834 C CG  . PHE F 2 96  ? -9.81500  39.40500 -38.09900 1.000 138.12923 ?  116 PHE B CG  1 
ATOM   6835 C CD1 . PHE F 2 96  ? -8.53400  38.87300 -38.03800 1.000 136.13085 ?  116 PHE B CD1 1 
ATOM   6836 C CD2 . PHE F 2 96  ? -10.36500 39.95300 -36.95400 1.000 130.38303 ?  116 PHE B CD2 1 
ATOM   6837 C CE1 . PHE F 2 96  ? -7.81200  38.91500 -36.85700 1.000 126.39795 ?  116 PHE B CE1 1 
ATOM   6838 C CE2 . PHE F 2 96  ? -9.65400  40.00400 -35.77600 1.000 120.69534 ?  116 PHE B CE2 1 
ATOM   6839 C CZ  . PHE F 2 96  ? -8.37800  39.48300 -35.72000 1.000 118.66654 ?  116 PHE B CZ  1 
ATOM   6840 N N   . THR F 2 97  ? -12.67800 38.45200 -41.48700 1.000 150.36259 ?  117 THR B N   1 
ATOM   6841 C CA  . THR F 2 97  ? -13.98300 38.38500 -42.15300 1.000 153.52222 ?  117 THR B CA  1 
ATOM   6842 C C   . THR F 2 97  ? -15.09700 38.93600 -41.25400 1.000 151.77548 ?  117 THR B C   1 
ATOM   6843 O O   . THR F 2 97  ? -15.91200 38.20100 -40.69000 1.000 152.18913 ?  117 THR B O   1 
ATOM   6844 C CB  . THR F 2 97  ? -14.29800 36.95400 -42.60700 1.000 156.57725 ?  117 THR B CB  1 
ATOM   6845 O OG1 . THR F 2 97  ? -13.25400 36.48200 -43.46400 1.000 157.79014 ?  117 THR B OG1 1 
ATOM   6846 C CG2 . THR F 2 97  ? -15.61200 36.90700 -43.37900 1.000 159.77173 ?  117 THR B CG2 1 
ATOM   6847 N N   . PHE F 2 98  ? -15.07800 40.25300 -41.07400 1.000 153.00618 ?  118 PHE B N   1 
ATOM   6848 C CA  . PHE F 2 98  ? -16.13800 40.84300 -40.27500 1.000 151.12760 ?  118 PHE B CA  1 
ATOM   6849 C C   . PHE F 2 98  ? -17.42400 40.88200 -41.09000 1.000 155.24130 ?  118 PHE B C   1 
ATOM   6850 O O   . PHE F 2 98  ? -17.41100 41.02300 -42.31600 1.000 157.70206 ?  118 PHE B O   1 
ATOM   6851 C CB  . PHE F 2 98  ? -15.76700 42.24700 -39.79700 1.000 146.63664 ?  118 PHE B CB  1 
ATOM   6852 C CG  . PHE F 2 98  ? -15.15700 42.27300 -38.42300 1.000 138.95032 ?  118 PHE B CG  1 
ATOM   6853 C CD1 . PHE F 2 98  ? -15.85500 41.76800 -37.33700 1.000 135.27887 ?  118 PHE B CD1 1 
ATOM   6854 C CD2 . PHE F 2 98  ? -13.90200 42.81900 -38.20900 1.000 133.91529 ?  118 PHE B CD2 1 
ATOM   6855 C CE1 . PHE F 2 98  ? -15.30700 41.78900 -36.06600 1.000 125.64844 ?  118 PHE B CE1 1 
ATOM   6856 C CE2 . PHE F 2 98  ? -13.34900 42.84300 -36.93600 1.000 124.65775 ?  118 PHE B CE2 1 
ATOM   6857 C CZ  . PHE F 2 98  ? -14.05400 42.32800 -35.86500 1.000 120.23454 ?  118 PHE B CZ  1 
ATOM   6858 N N   . GLY F 2 99  ? -18.54600 40.77400 -40.38500 1.000 151.15059 ?  119 GLY B N   1 
ATOM   6859 C CA  . GLY F 2 99  ? -19.82700 40.70200 -41.04500 1.000 154.87117 ?  119 GLY B CA  1 
ATOM   6860 C C   . GLY F 2 99  ? -20.30900 42.03200 -41.57700 1.000 154.38462 ?  119 GLY B C   1 
ATOM   6861 O O   . GLY F 2 99  ? -19.81800 43.10100 -41.21500 1.000 151.16186 ?  119 GLY B O   1 
ATOM   6862 N N   . GLN F 2 100 ? -21.31100 41.93600 -42.45400 1.000 159.70438 ?  120 GLN B N   1 
ATOM   6863 C CA  . GLN F 2 100 ? -21.86600 43.12200 -43.09300 1.000 159.28021 ?  120 GLN B CA  1 
ATOM   6864 C C   . GLN F 2 100 ? -22.38300 44.09600 -42.04700 1.000 156.84751 ?  120 GLN B C   1 
ATOM   6865 O O   . GLN F 2 100 ? -22.29900 45.31800 -42.22100 1.000 154.85084 ?  120 GLN B O   1 
ATOM   6866 C CB  . GLN F 2 100 ? -22.99100 42.72200 -44.05000 1.000 162.47471 ?  120 GLN B CB  1 
ATOM   6867 C CG  . GLN F 2 100 ? -23.53500 43.86000 -44.90100 1.000 161.96748 ?  120 GLN B CG  1 
ATOM   6868 C CD  . GLN F 2 100 ? -24.60100 43.39600 -45.87900 1.000 164.57512 ?  120 GLN B CD  1 
ATOM   6869 O OE1 . GLN F 2 100 ? -24.87000 42.20000 -46.00500 1.000 166.81273 ?  120 GLN B OE1 1 
ATOM   6870 N NE2 . GLN F 2 100 ? -25.21400 44.34500 -46.57500 1.000 164.08978 ?  120 GLN B NE2 1 
ATOM   6871 N N   . GLY F 2 101 ? -22.94100 43.56600 -40.96600 1.000 152.63960 ?  121 GLY B N   1 
ATOM   6872 C CA  . GLY F 2 101 ? -23.51300 44.36900 -39.91200 1.000 150.36570 ?  121 GLY B CA  1 
ATOM   6873 C C   . GLY F 2 101 ? -25.01700 44.34200 -40.01800 1.000 153.34220 ?  121 GLY B C   1 
ATOM   6874 O O   . GLY F 2 101 ? -25.56100 44.35900 -41.12600 1.000 155.81393 ?  121 GLY B O   1 
ATOM   6875 N N   . THR F 2 102 ? -25.70500 44.29000 -38.88300 1.000 156.68303 ?  122 THR B N   1 
ATOM   6876 C CA  . THR F 2 102 ? -27.16200 44.23100 -38.87700 1.000 158.33806 ?  122 THR B CA  1 
ATOM   6877 C C   . THR F 2 102 ? -27.66000 45.29200 -37.90800 1.000 156.08894 ?  122 THR B C   1 
ATOM   6878 O O   . THR F 2 102 ? -27.40600 45.20000 -36.70000 1.000 152.60761 ?  122 THR B O   1 
ATOM   6879 C CB  . THR F 2 102 ? -27.66400 42.84300 -38.47800 1.000 158.72080 ?  122 THR B CB  1 
ATOM   6880 O OG1 . THR F 2 102 ? -27.13500 41.85800 -39.37700 1.000 160.61837 ?  122 THR B OG1 1 
ATOM   6881 C CG2 . THR F 2 102 ? -29.18200 42.79800 -38.52300 1.000 160.59345 ?  122 THR B CG2 1 
ATOM   6882 N N   . LYS F 2 103 ? -28.32900 46.31100 -38.44600 1.000 161.33499 ?  123 LYS B N   1 
ATOM   6883 C CA  . LYS F 2 103 ? -28.94500 47.33300 -37.61200 1.000 159.68739 ?  123 LYS B CA  1 
ATOM   6884 C C   . LYS F 2 103 ? -30.19700 46.76800 -36.96000 1.000 160.37277 ?  123 LYS B C   1 
ATOM   6885 O O   . LYS F 2 103 ? -31.05200 46.19100 -37.63900 1.000 163.37099 ?  123 LYS B O   1 
ATOM   6886 C CB  . LYS F 2 103 ? -29.28700 48.56700 -38.44900 1.000 161.15698 ?  123 LYS B CB  1 
ATOM   6887 N N   . VAL F 2 104 ? -30.29200 46.89600 -35.63700 1.000 162.98618 ?  124 VAL B N   1 
ATOM   6888 C CA  . VAL F 2 104 ? -31.45000 46.40600 -34.90600 1.000 163.20605 ?  124 VAL B CA  1 
ATOM   6889 C C   . VAL F 2 104 ? -32.27600 47.55500 -34.33500 1.000 162.70635 ?  124 VAL B C   1 
ATOM   6890 O O   . VAL F 2 104 ? -32.00400 48.03800 -33.23000 1.000 158.92721 ?  124 VAL B O   1 
ATOM   6891 C CB  . VAL F 2 104 ? -30.99900 45.43300 -33.80500 1.000 159.53981 ?  124 VAL B CB  1 
ATOM   6892 C CG1 . VAL F 2 104 ? -32.19900 44.83200 -33.10600 1.000 159.60199 ?  124 VAL B CG1 1 
ATOM   6893 C CG2 . VAL F 2 104 ? -30.13400 44.35100 -34.41700 1.000 160.14068 ?  124 VAL B CG2 1 
ATOM   6894 N N   . GLU F 2 105 ? -33.27200 48.01200 -35.08600 1.000 171.21661 ?  125 GLU B N   1 
ATOM   6895 C CA  . GLU F 2 105 ? -34.24100 48.97900 -34.59100 1.000 171.44040 ?  125 GLU B CA  1 
ATOM   6896 C C   . GLU F 2 105 ? -35.39000 48.24600 -33.89700 1.000 172.09777 ?  125 GLU B C   1 
ATOM   6897 O O   . GLU F 2 105 ? -35.56900 47.03600 -34.05800 1.000 172.92317 ?  125 GLU B O   1 
ATOM   6898 C CB  . GLU F 2 105 ? -34.76000 49.85900 -35.72700 1.000 174.53660 ?  125 GLU B CB  1 
ATOM   6899 N N   . ILE F 2 106 ? -36.16500 48.98700 -33.09900 1.000 172.89399 ?  126 ILE B N   1 
ATOM   6900 C CA  . ILE F 2 106 ? -37.28900 48.41700 -32.36000 1.000 173.13983 ?  126 ILE B CA  1 
ATOM   6901 C C   . ILE F 2 106 ? -38.52400 49.30900 -32.49200 1.000 176.04949 ?  126 ILE B C   1 
ATOM   6902 O O   . ILE F 2 106 ? -38.43000 50.54000 -32.42800 1.000 175.75071 ?  126 ILE B O   1 
ATOM   6903 C CB  . ILE F 2 106 ? -36.94500 48.15000 -30.87300 1.000 168.26660 ?  126 ILE B CB  1 
ATOM   6904 C CG1 . ILE F 2 106 ? -37.03500 49.39300 -29.99600 1.000 166.08046 ?  126 ILE B CG1 1 
ATOM   6905 C CG2 . ILE F 2 106 ? -35.56300 47.54600 -30.71900 1.000 165.09052 ?  126 ILE B CG2 1 
ATOM   6906 C CD1 . ILE F 2 106 ? -37.00100 49.02700 -28.53000 1.000 161.52951 ?  126 ILE B CD1 1 
ATOM   6907 N N   . LYS F 2 107 ? -39.67900 48.67300 -32.71100 1.000 171.61669 ?  127 LYS B N   1 
ATOM   6908 C CA  . LYS F 2 107 ? -40.95000 49.37800 -32.84600 1.000 174.85025 ?  127 LYS B CA  1 
ATOM   6909 C C   . LYS F 2 107 ? -41.44100 49.86800 -31.48800 1.000 172.51493 ?  127 LYS B C   1 
ATOM   6910 O O   . LYS F 2 107 ? -41.39600 49.14000 -30.49200 1.000 169.25648 ?  127 LYS B O   1 
ATOM   6911 C CB  . LYS F 2 107 ? -41.99800 48.45100 -33.46000 1.000 178.27415 ?  127 LYS B CB  1 
ATOM   6912 C CG  . LYS F 2 107 ? -41.74300 48.06400 -34.90400 1.000 180.91545 ?  127 LYS B CG  1 
ATOM   6913 C CD  . LYS F 2 107 ? -42.82000 47.12200 -35.42000 1.000 183.48108 ?  127 LYS B CD  1 
ATOM   6914 N N   . ARG F 2 108 ? -41.91700 51.11200 -31.45000 1.000 178.46471 ?  128 ARG B N   1 
ATOM   6915 C CA  . ARG F 2 108 ? -42.25000 51.77000 -30.18900 1.000 176.06614 ?  128 ARG B CA  1 
ATOM   6916 C C   . ARG F 2 108 ? -43.60000 52.48000 -30.24700 1.000 179.70724 ?  128 ARG B C   1 
ATOM   6917 O O   . ARG F 2 108 ? -43.71400 53.64200 -29.85200 1.000 179.30090 ?  128 ARG B O   1 
ATOM   6918 C CB  . ARG F 2 108 ? -41.14900 52.75600 -29.80800 1.000 172.68296 ?  128 ARG B CB  1 
ATOM   6919 N N   . THR F 2 109 ? -44.64400 51.79700 -30.73700 1.000 179.28543 ?  129 THR B N   1 
ATOM   6920 C CA  . THR F 2 109 ? -46.01700 52.28300 -30.56700 1.000 182.47297 ?  129 THR B CA  1 
ATOM   6921 C C   . THR F 2 109 ? -46.18900 53.74100 -30.98200 1.000 184.77881 ?  129 THR B C   1 
ATOM   6922 O O   . THR F 2 109 ? -46.27600 54.62500 -30.12400 1.000 183.23690 ?  129 THR B O   1 
ATOM   6923 C CB  . THR F 2 109 ? -46.50100 52.08400 -29.12500 1.000 179.49802 ?  129 THR B CB  1 
ATOM   6924 O OG1 . THR F 2 109 ? -46.07600 53.18000 -28.30400 1.000 177.02341 ?  129 THR B OG1 1 
ATOM   6925 C CG2 . THR F 2 109 ? -45.99300 50.76200 -28.56200 1.000 175.37027 ?  129 THR B CG2 1 
ATOM   6926 N N   . VAL F 2 110 ? -46.24000 53.98300 -32.29200 1.000 183.31103 ?  130 VAL B N   1 
ATOM   6927 C CA  . VAL F 2 110 ? -46.00900 55.26600 -32.95400 1.000 184.45561 ?  130 VAL B CA  1 
ATOM   6928 C C   . VAL F 2 110 ? -46.51200 56.45800 -32.14900 1.000 184.89408 ?  130 VAL B C   1 
ATOM   6929 O O   . VAL F 2 110 ? -47.66400 56.48400 -31.70200 1.000 187.25965 ?  130 VAL B O   1 
ATOM   6930 C CB  . VAL F 2 110 ? -46.69800 55.23300 -34.33200 1.000 188.33700 ?  130 VAL B CB  1 
ATOM   6931 C CG1 . VAL F 2 110 ? -46.43500 56.50100 -35.11600 1.000 189.94617 ?  130 VAL B CG1 1 
ATOM   6932 C CG2 . VAL F 2 110 ? -46.26600 54.00000 -35.11000 1.000 187.71081 ?  130 VAL B CG2 1 
ATOM   6933 N N   . ALA F 2 111 ? -45.64200 57.45000 -31.95500 1.000 187.55596 ?  131 ALA B N   1 
ATOM   6934 C CA  . ALA F 2 111 ? -45.93000 58.60100 -31.11300 1.000 187.38608 ?  131 ALA B CA  1 
ATOM   6935 C C   . ALA F 2 111 ? -45.66100 59.89000 -31.87700 1.000 194.73763 ?  131 ALA B C   1 
ATOM   6936 O O   . ALA F 2 111 ? -44.80900 59.93900 -32.76600 1.000 195.73925 ?  131 ALA B O   1 
ATOM   6937 C CB  . ALA F 2 111 ? -45.09200 58.57100 -29.82300 1.000 181.67868 ?  131 ALA B CB  1 
ATOM   6938 N N   . ALA F 2 112 ? -46.41200 60.94100 -31.51900 1.000 194.45501 ?  132 ALA B N   1 
ATOM   6939 C CA  . ALA F 2 112 ? -46.23400 62.24800 -32.13300 1.000 202.38290 ?  132 ALA B CA  1 
ATOM   6940 C C   . ALA F 2 112 ? -45.03100 62.96200 -31.52000 1.000 200.94827 ?  132 ALA B C   1 
ATOM   6941 O O   . ALA F 2 112 ? -44.79700 62.86500 -30.31300 1.000 196.06356 ?  132 ALA B O   1 
ATOM   6942 C CB  . ALA F 2 112 ? -47.48600 63.10500 -31.95800 1.000 209.37567 ?  132 ALA B CB  1 
ATOM   6943 N N   . PRO F 2 113 ? -44.24600 63.66000 -32.33300 1.000 205.17473 ?  133 PRO B N   1 
ATOM   6944 C CA  . PRO F 2 113 ? -43.09100 64.39100 -31.80600 1.000 204.47321 ?  133 PRO B CA  1 
ATOM   6945 C C   . PRO F 2 113 ? -43.50400 65.58100 -30.95600 1.000 208.73054 ?  133 PRO B C   1 
ATOM   6946 O O   . PRO F 2 113 ? -44.60000 66.13400 -31.07900 1.000 214.56153 ?  133 PRO B O   1 
ATOM   6947 C CB  . PRO F 2 113 ? -42.34800 64.83800 -33.06900 1.000 209.21534 ?  133 PRO B CB  1 
ATOM   6948 C CG  . PRO F 2 113 ? -43.39400 64.91200 -34.11500 1.000 215.41551 ?  133 PRO B CG  1 
ATOM   6949 C CD  . PRO F 2 113 ? -44.42500 63.87000 -33.77900 1.000 211.41060 ?  133 PRO B CD  1 
ATOM   6950 N N   . SER F 2 114 ? -42.58900 65.95700 -30.06400 1.000 171.38468 ?  134 SER B N   1 
ATOM   6951 C CA  . SER F 2 114 ? -42.73000 67.13100 -29.20100 1.000 178.02849 ?  134 SER B CA  1 
ATOM   6952 C C   . SER F 2 114 ? -41.90800 68.27000 -29.80200 1.000 175.30287 ?  134 SER B C   1 
ATOM   6953 O O   . SER F 2 114 ? -40.77600 68.54200 -29.40400 1.000 175.20181 ?  134 SER B O   1 
ATOM   6954 C CB  . SER F 2 114 ? -42.31800 66.79400 -27.77100 1.000 182.46285 ?  134 SER B CB  1 
ATOM   6955 O OG  . SER F 2 114 ? -41.18100 65.95000 -27.75200 1.000 177.88449 ?  134 SER B OG  1 
ATOM   6956 N N   . VAL F 2 115 ? -42.50600 68.94700 -30.78600 1.000 175.09780 ?  135 VAL B N   1 
ATOM   6957 C CA  . VAL F 2 115 ? -41.77700 69.90100 -31.61700 1.000 169.76986 ?  135 VAL B CA  1 
ATOM   6958 C C   . VAL F 2 115 ? -41.47200 71.19000 -30.85400 1.000 175.72243 ?  135 VAL B C   1 
ATOM   6959 O O   . VAL F 2 115 ? -42.24500 71.64200 -29.99800 1.000 182.69735 ?  135 VAL B O   1 
ATOM   6960 C CB  . VAL F 2 115 ? -42.59600 70.19700 -32.88800 1.000 162.89961 ?  135 VAL B CB  1 
ATOM   6961 C CG1 . VAL F 2 115 ? -41.79600 71.03500 -33.86800 1.000 153.99944 ?  135 VAL B CG1 1 
ATOM   6962 C CG2 . VAL F 2 115 ? -43.05100 68.90300 -33.54100 1.000 157.60745 ?  135 VAL B CG2 1 
ATOM   6963 N N   . PHE F 2 116 ? -40.31800 71.78300 -31.17500 1.000 162.08509 ?  136 PHE B N   1 
ATOM   6964 C CA  . PHE F 2 116 ? -39.87200 73.06200 -30.63500 1.000 166.90246 ?  136 PHE B CA  1 
ATOM   6965 C C   . PHE F 2 116 ? -39.20300 73.86700 -31.74000 1.000 160.02783 ?  136 PHE B C   1 
ATOM   6966 O O   . PHE F 2 116 ? -38.77000 73.31600 -32.75500 1.000 151.20776 ?  136 PHE B O   1 
ATOM   6967 C CB  . PHE F 2 116 ? -38.89800 72.87800 -29.46800 1.000 172.58077 ?  136 PHE B CB  1 
ATOM   6968 C CG  . PHE F 2 116 ? -39.52800 72.26600 -28.26400 1.000 178.63552 ?  136 PHE B CG  1 
ATOM   6969 C CD1 . PHE F 2 116 ? -40.64000 72.84500 -27.68400 1.000 183.69745 ?  136 PHE B CD1 1 
ATOM   6970 C CD2 . PHE F 2 116 ? -39.03000 71.09700 -27.72800 1.000 178.31348 ?  136 PHE B CD2 1 
ATOM   6971 C CE1 . PHE F 2 116 ? -41.23600 72.27600 -26.58400 1.000 188.33959 ?  136 PHE B CE1 1 
ATOM   6972 C CE2 . PHE F 2 116 ? -39.61900 70.52300 -26.62600 1.000 182.90555 ?  136 PHE B CE2 1 
ATOM   6973 C CZ  . PHE F 2 116 ? -40.72600 71.11700 -26.05100 1.000 187.93754 ?  136 PHE B CZ  1 
ATOM   6974 N N   . ILE F 2 117 ? -39.05400 75.17200 -31.49800 1.000 176.34050 ?  137 ILE B N   1 
ATOM   6975 C CA  . ILE F 2 117 ? -38.39500 76.08700 -32.42800 1.000 170.52482 ?  137 ILE B CA  1 
ATOM   6976 C C   . ILE F 2 117 ? -37.46800 77.00500 -31.64600 1.000 177.68077 ?  137 ILE B C   1 
ATOM   6977 O O   . ILE F 2 117 ? -37.82800 77.51200 -30.57900 1.000 185.54702 ?  137 ILE B O   1 
ATOM   6978 C CB  . ILE F 2 117 ? -39.40400 76.93300 -33.23900 1.000 164.75655 ?  137 ILE B CB  1 
ATOM   6979 C CG1 . ILE F 2 117 ? -40.44800 76.05300 -33.91800 1.000 158.04111 ?  137 ILE B CG1 1 
ATOM   6980 C CG2 . ILE F 2 117 ? -38.67500 77.76600 -34.27900 1.000 156.81228 ?  137 ILE B CG2 1 
ATOM   6981 C CD1 . ILE F 2 117 ? -39.97200 75.45600 -35.20200 1.000 145.76417 ?  137 ILE B CD1 1 
ATOM   6982 N N   . PHE F 2 118 ? -36.27400 77.23100 -32.19100 1.000 160.81461 ?  138 PHE B N   1 
ATOM   6983 C CA  . PHE F 2 118 ? -35.28600 78.11600 -31.58300 1.000 167.48459 ?  138 PHE B CA  1 
ATOM   6984 C C   . PHE F 2 118 ? -34.81000 79.10100 -32.64000 1.000 162.14630 ?  138 PHE B C   1 
ATOM   6985 O O   . PHE F 2 118 ? -34.21300 78.68100 -33.64800 1.000 154.38852 ?  138 PHE B O   1 
ATOM   6986 C CB  . PHE F 2 118 ? -34.10000 77.32700 -31.02100 1.000 170.73948 ?  138 PHE B CB  1 
ATOM   6987 C CG  . PHE F 2 118 ? -34.40500 76.60900 -29.74400 1.000 176.86119 ?  138 PHE B CG  1 
ATOM   6988 C CD1 . PHE F 2 118 ? -35.25200 75.51300 -29.72700 1.000 174.07974 ?  138 PHE B CD1 1 
ATOM   6989 C CD2 . PHE F 2 118 ? -33.85600 77.04500 -28.55400 1.000 184.93176 ?  138 PHE B CD2 1 
ATOM   6990 C CE1 . PHE F 2 118 ? -35.53700 74.86400 -28.54300 1.000 179.26954 ?  138 PHE B CE1 1 
ATOM   6991 C CE2 . PHE F 2 118 ? -34.13500 76.39800 -27.36900 1.000 189.23436 ?  138 PHE B CE2 1 
ATOM   6992 C CZ  . PHE F 2 118 ? -34.97800 75.30800 -27.36300 1.000 186.43393 ?  138 PHE B CZ  1 
ATOM   6993 N N   . PRO F 2 119 ? -35.00700 80.40000 -32.45400 1.000 171.36069 ?  139 PRO B N   1 
ATOM   6994 C CA  . PRO F 2 119 ? -34.55200 81.36100 -33.45400 1.000 165.96206 ?  139 PRO B CA  1 
ATOM   6995 C C   . PRO F 2 119 ? -33.05100 81.55600 -33.35500 1.000 170.34238 ?  139 PRO B C   1 
ATOM   6996 O O   . PRO F 2 119 ? -32.41300 81.06100 -32.41200 1.000 177.73324 ?  139 PRO B O   1 
ATOM   6997 C CB  . PRO F 2 119 ? -35.31300 82.64400 -33.08300 1.000 168.41118 ?  139 PRO B CB  1 
ATOM   6998 C CG  . PRO F 2 119 ? -36.48100 82.17400 -32.29700 1.000 171.51440 ?  139 PRO B CG  1 
ATOM   6999 C CD  . PRO F 2 119 ? -35.95500 81.00800 -31.51100 1.000 177.19584 ?  139 PRO B CD  1 
ATOM   7000 N N   . PRO F 2 120 ? -32.43800 82.21000 -34.33900 1.000 165.66888 ?  140 PRO B N   1 
ATOM   7001 C CA  . PRO F 2 120 ? -31.02400 82.56800 -34.20300 1.000 170.44966 ?  140 PRO B CA  1 
ATOM   7002 C C   . PRO F 2 120 ? -30.81000 83.49200 -33.01500 1.000 181.10209 ?  140 PRO B C   1 
ATOM   7003 O O   . PRO F 2 120 ? -31.63100 84.36500 -32.72600 1.000 182.44390 ?  140 PRO B O   1 
ATOM   7004 C CB  . PRO F 2 120 ? -30.70000 83.26100 -35.53200 1.000 162.45782 ?  140 PRO B CB  1 
ATOM   7005 C CG  . PRO F 2 120 ? -32.02600 83.59300 -36.13600 1.000 154.73338 ?  140 PRO B CG  1 
ATOM   7006 C CD  . PRO F 2 120 ? -32.94800 82.52000 -35.68300 1.000 154.24713 ?  140 PRO B CD  1 
ATOM   7007 N N   . SER F 2 121 ? -29.70900 83.27000 -32.30900 1.000 170.89090 ?  141 SER B N   1 
ATOM   7008 C CA  . SER F 2 121 ? -29.36100 84.11500 -31.17800 1.000 179.78857 ?  141 SER B CA  1 
ATOM   7009 C C   . SER F 2 121 ? -28.88600 85.48200 -31.65000 1.000 180.15815 ?  141 SER B C   1 
ATOM   7010 O O   . SER F 2 121 ? -28.34300 85.63100 -32.74900 1.000 175.84905 ?  141 SER B O   1 
ATOM   7011 C CB  . SER F 2 121 ? -28.27000 83.46400 -30.33400 1.000 186.13204 ?  141 SER B CB  1 
ATOM   7012 O OG  . SER F 2 121 ? -27.47200 84.46700 -29.73600 1.000 192.53840 ?  141 SER B OG  1 
ATOM   7013 N N   . ASP F 2 122 ? -29.12100 86.49600 -30.81200 1.000 179.98628 ?  142 ASP B N   1 
ATOM   7014 C CA  . ASP F 2 122 ? -28.62800 87.83400 -31.12400 1.000 180.38618 ?  142 ASP B CA  1 
ATOM   7015 C C   . ASP F 2 122 ? -27.12800 87.87100 -31.37100 1.000 184.25503 ?  142 ASP B C   1 
ATOM   7016 O O   . ASP F 2 122 ? -26.65500 88.64900 -32.20600 1.000 181.97830 ?  142 ASP B O   1 
ATOM   7017 C CB  . ASP F 2 122 ? -28.98400 88.80000 -29.99600 1.000 185.30710 ?  142 ASP B CB  1 
ATOM   7018 C CG  . ASP F 2 122 ? -28.29400 88.44600 -28.69400 1.000 192.61131 ?  142 ASP B CG  1 
ATOM   7019 O OD1 . ASP F 2 122 ? -28.16500 87.23400 -28.41800 1.000 194.01222 ?  142 ASP B OD1 1 
ATOM   7020 O OD2 . ASP F 2 122 ? -27.88100 89.36600 -27.95300 1.000 196.44906 -1 142 ASP B OD2 1 
ATOM   7021 N N   . GLU F 2 123 ? -26.37100 87.02700 -30.66500 1.000 183.69336 ?  143 GLU B N   1 
ATOM   7022 C CA  . GLU F 2 123 ? -24.94400 86.89700 -30.93800 1.000 185.73941 ?  143 GLU B CA  1 
ATOM   7023 C C   . GLU F 2 123 ? -24.68200 86.21900 -32.27800 1.000 179.90709 ?  143 GLU B C   1 
ATOM   7024 O O   . GLU F 2 123 ? -23.76400 86.60500 -33.00900 1.000 179.84574 ?  143 GLU B O   1 
ATOM   7025 C CB  . GLU F 2 123 ? -24.26200 86.08800 -29.83300 1.000 186.72483 ?  143 GLU B CB  1 
ATOM   7026 C CG  . GLU F 2 123 ? -22.75600 85.95300 -30.00200 1.000 186.33552 ?  143 GLU B CG  1 
ATOM   7027 C CD  . GLU F 2 123 ? -22.11100 85.18600 -28.86300 1.000 187.01115 ?  143 GLU B CD  1 
ATOM   7028 O OE1 . GLU F 2 123 ? -22.84300 84.72800 -27.96200 1.000 189.00921 ?  143 GLU B OE1 1 
ATOM   7029 O OE2 . GLU F 2 123 ? -20.87000 85.04400 -28.86900 1.000 184.53305 ?  143 GLU B OE2 1 
ATOM   7030 N N   . GLN F 2 124 ? -25.47400 85.19800 -32.61300 1.000 194.27680 ?  144 GLN B N   1 
ATOM   7031 C CA  . GLN F 2 124 ? -25.30800 84.54200 -33.90400 1.000 186.42885 ?  144 GLN B CA  1 
ATOM   7032 C C   . GLN F 2 124 ? -25.68000 85.52000 -35.00900 1.000 180.53386 ?  144 GLN B C   1 
ATOM   7033 O O   . GLN F 2 124 ? -24.95100 85.64900 -36.00000 1.000 177.41301 ?  144 GLN B O   1 
ATOM   7034 C CB  . GLN F 2 124 ? -26.12900 83.25900 -34.01400 1.000 179.81378 ?  144 GLN B CB  1 
ATOM   7035 C CG  . GLN F 2 124 ? -25.56900 82.28600 -35.03500 1.000 171.51192 ?  144 GLN B CG  1 
ATOM   7036 C CD  . GLN F 2 124 ? -26.64300 81.52100 -35.77500 1.000 160.10463 ?  144 GLN B CD  1 
ATOM   7037 O OE1 . GLN F 2 124 ? -27.76900 81.38200 -35.29400 1.000 159.97734 ?  144 GLN B OE1 1 
ATOM   7038 N NE2 . GLN F 2 124 ? -26.30300 81.02600 -36.95900 1.000 149.30086 ?  144 GLN B NE2 1 
ATOM   7039 N N   . LEU F 2 125 ? -26.79100 86.24500 -34.83900 1.000 186.48566 ?  145 LEU B N   1 
ATOM   7040 C CA  . LEU F 2 125 ? -27.14200 87.29700 -35.78800 1.000 179.94729 ?  145 LEU B CA  1 
ATOM   7041 C C   . LEU F 2 125 ? -26.01600 88.31500 -35.89000 1.000 185.16261 ?  145 LEU B C   1 
ATOM   7042 O O   . LEU F 2 125 ? -25.71000 88.81800 -36.97800 1.000 180.01529 ?  145 LEU B O   1 
ATOM   7043 C CB  . LEU F 2 125 ? -28.44500 87.97500 -35.35900 1.000 177.56129 ?  145 LEU B CB  1 
ATOM   7044 C CG  . LEU F 2 125 ? -29.71300 87.11900 -35.35000 1.000 171.79110 ?  145 LEU B CG  1 
ATOM   7045 C CD1 . LEU F 2 125 ? -30.87800 87.87000 -34.72300 1.000 171.83758 ?  145 LEU B CD1 1 
ATOM   7046 C CD2 . LEU F 2 125 ? -30.06700 86.69600 -36.75500 1.000 159.60183 ?  145 LEU B CD2 1 
ATOM   7047 N N   . LYS F 2 126 ? -25.38700 88.62400 -34.75700 1.000 173.97021 ?  146 LYS B N   1 
ATOM   7048 C CA  . LYS F 2 126 ? -24.25500 89.53700 -34.74100 1.000 179.03522 ?  146 LYS B CA  1 
ATOM   7049 C C   . LYS F 2 126 ? -23.06300 88.98000 -35.51200 1.000 180.00101 ?  146 LYS B C   1 
ATOM   7050 O O   . LYS F 2 126 ? -22.26200 89.74900 -36.05600 1.000 180.88445 ?  146 LYS B O   1 
ATOM   7051 C CB  . LYS F 2 126 ? -23.88000 89.81500 -33.28900 1.000 187.63990 ?  146 LYS B CB  1 
ATOM   7052 C CG  . LYS F 2 126 ? -22.86700 90.89900 -33.08500 1.000 191.74720 ?  146 LYS B CG  1 
ATOM   7053 C CD  . LYS F 2 126 ? -22.25300 90.76000 -31.71000 1.000 198.79789 ?  146 LYS B CD  1 
ATOM   7054 N N   . SER F 2 127 ? -22.93500 87.65300 -35.58800 1.000 185.00522 ?  147 SER B N   1 
ATOM   7055 C CA  . SER F 2 127 ? -21.85100 87.05800 -36.36200 1.000 183.90328 ?  147 SER B CA  1 
ATOM   7056 C C   . SER F 2 127 ? -22.05400 87.18600 -37.86400 1.000 174.66056 ?  147 SER B C   1 
ATOM   7057 O O   . SER F 2 127 ? -21.11900 86.90200 -38.61900 1.000 172.80027 ?  147 SER B O   1 
ATOM   7058 C CB  . SER F 2 127 ? -21.68100 85.58000 -36.00000 1.000 181.84373 ?  147 SER B CB  1 
ATOM   7059 O OG  . SER F 2 127 ? -21.60500 85.40400 -34.59800 1.000 188.05347 ?  147 SER B OG  1 
ATOM   7060 N N   . GLY F 2 128 ? -23.23500 87.59800 -38.31400 1.000 189.30004 ?  148 GLY B N   1 
ATOM   7061 C CA  . GLY F 2 128 ? -23.53000 87.65800 -39.72700 1.000 177.95371 ?  148 GLY B CA  1 
ATOM   7062 C C   . GLY F 2 128 ? -24.26100 86.45200 -40.26900 1.000 166.62755 ?  148 GLY B C   1 
ATOM   7063 O O   . GLY F 2 128 ? -24.42500 86.34900 -41.49100 1.000 154.63372 ?  148 GLY B O   1 
ATOM   7064 N N   . THR F 2 129 ? -24.69500 85.53400 -39.40500 1.000 180.11537 ?  149 THR B N   1 
ATOM   7065 C CA  . THR F 2 129 ? -25.38000 84.32100 -39.82600 1.000 175.39721 ?  149 THR B CA  1 
ATOM   7066 C C   . THR F 2 129 ? -26.48200 83.98400 -38.82900 1.000 174.40535 ?  149 THR B C   1 
ATOM   7067 O O   . THR F 2 129 ? -26.29200 84.10100 -37.61700 1.000 175.80359 ?  149 THR B O   1 
ATOM   7068 C CB  . THR F 2 129 ? -24.39600 83.14900 -39.94400 1.000 171.98168 ?  149 THR B CB  1 
ATOM   7069 O OG1 . THR F 2 129 ? -23.21500 83.59000 -40.62400 1.000 173.89168 ?  149 THR B OG1 1 
ATOM   7070 C CG2 . THR F 2 129 ? -25.01500 82.01000 -40.73300 1.000 167.64426 ?  149 THR B CG2 1 
ATOM   7071 N N   . ALA F 2 130 ? -27.62800 83.55500 -39.35000 1.000 175.98182 ?  150 ALA B N   1 
ATOM   7072 C CA  . ALA F 2 130 ? -28.81100 83.22400 -38.57400 1.000 175.47482 ?  150 ALA B CA  1 
ATOM   7073 C C   . ALA F 2 130 ? -29.10300 81.73600 -38.71200 1.000 171.23170 ?  150 ALA B C   1 
ATOM   7074 O O   . ALA F 2 130 ? -29.05900 81.18900 -39.82100 1.000 169.46642 ?  150 ALA B O   1 
ATOM   7075 C CB  . ALA F 2 130 ? -30.01900 84.03700 -39.05200 1.000 178.14817 ?  150 ALA B CB  1 
ATOM   7076 N N   . SER F 2 131 ? -29.37300 81.07500 -37.58700 1.000 167.10993 ?  151 SER B N   1 
ATOM   7077 C CA  . SER F 2 131 ? -29.72600 79.66000 -37.58500 1.000 163.51093 ?  151 SER B CA  1 
ATOM   7078 C C   . SER F 2 131 ? -31.01000 79.46800 -36.79500 1.000 165.22640 ?  151 SER B C   1 
ATOM   7079 O O   . SER F 2 131 ? -31.04400 79.72900 -35.58800 1.000 166.64403 ?  151 SER B O   1 
ATOM   7080 C CB  . SER F 2 131 ? -28.60300 78.80300 -36.99200 1.000 160.69310 ?  151 SER B CB  1 
ATOM   7081 O OG  . SER F 2 131 ? -27.48300 78.77600 -37.85600 1.000 159.52851 ?  151 SER B OG  1 
ATOM   7082 N N   . VAL F 2 132 ? -32.04600 78.98700 -37.46100 1.000 159.34939 ?  152 VAL B N   1 
ATOM   7083 C CA  . VAL F 2 132 ? -33.30300 78.64300 -36.82000 1.000 161.69998 ?  152 VAL B CA  1 
ATOM   7084 C C   . VAL F 2 132 ? -33.27000 77.13300 -36.65400 1.000 159.20123 ?  152 VAL B C   1 
ATOM   7085 O O   . VAL F 2 132 ? -32.80000 76.41500 -37.54100 1.000 157.18858 ?  152 VAL B O   1 
ATOM   7086 C CB  . VAL F 2 132 ? -34.52100 79.10400 -37.64900 1.000 166.16309 ?  152 VAL B CB  1 
ATOM   7087 C CG1 . VAL F 2 132 ? -35.80400 78.91200 -36.85300 1.000 169.57440 ?  152 VAL B CG1 1 
ATOM   7088 C CG2 . VAL F 2 132 ? -34.35800 80.54700 -38.15300 1.000 168.01641 ?  152 VAL B CG2 1 
ATOM   7089 N N   . VAL F 2 133 ? -33.73700 76.65300 -35.51200 1.000 163.21146 ?  153 VAL B N   1 
ATOM   7090 C CA  . VAL F 2 133 ? -33.63200 75.25600 -35.12900 1.000 160.79489 ?  153 VAL B CA  1 
ATOM   7091 C C   . VAL F 2 133 ? -35.03000 74.71500 -34.87900 1.000 164.78671 ?  153 VAL B C   1 
ATOM   7092 O O   . VAL F 2 133 ? -35.92100 75.44200 -34.43200 1.000 168.76719 ?  153 VAL B O   1 
ATOM   7093 C CB  . VAL F 2 133 ? -32.73000 75.13300 -33.87300 1.000 158.24173 ?  153 VAL B CB  1 
ATOM   7094 C CG1 . VAL F 2 133 ? -32.89600 73.79500 -33.16800 1.000 156.61677 ?  153 VAL B CG1 1 
ATOM   7095 C CG2 . VAL F 2 133 ? -31.27600 75.38100 -34.23500 1.000 155.19164 ?  153 VAL B CG2 1 
ATOM   7096 N N   . CYS F 2 134 ? -35.21700 73.42700 -35.16300 1.000 158.58735 ?  154 CYS B N   1 
ATOM   7097 C CA  . CYS F 2 134 ? -36.49600 72.77200 -34.93100 1.000 163.51710 ?  154 CYS B CA  1 
ATOM   7098 C C   . CYS F 2 134 ? -36.20600 71.42300 -34.29500 1.000 160.51924 ?  154 CYS B C   1 
ATOM   7099 O O   . CYS F 2 134 ? -35.45600 70.61500 -34.85900 1.000 157.04996 ?  154 CYS B O   1 
ATOM   7100 C CB  . CYS F 2 134 ? -37.28600 72.61800 -36.23600 1.000 169.39015 ?  154 CYS B CB  1 
ATOM   7101 S SG  . CYS F 2 134 ? -39.02400 72.16600 -36.02800 1.000 178.97375 ?  154 CYS B SG  1 
ATOM   7102 N N   . LEU F 2 135 ? -36.78100 71.20700 -33.11200 1.000 161.89223 ?  155 LEU B N   1 
ATOM   7103 C CA  . LEU F 2 135 ? -36.53100 70.03000 -32.28500 1.000 159.07919 ?  155 LEU B CA  1 
ATOM   7104 C C   . LEU F 2 135 ? -37.74000 69.10700 -32.34800 1.000 164.30070 ?  155 LEU B C   1 
ATOM   7105 O O   . LEU F 2 135 ? -38.87900 69.57200 -32.26700 1.000 170.54793 ?  155 LEU B O   1 
ATOM   7106 C CB  . LEU F 2 135 ? -36.24300 70.42800 -30.83300 1.000 157.79413 ?  155 LEU B CB  1 
ATOM   7107 C CG  . LEU F 2 135 ? -36.08000 69.29900 -29.80800 1.000 155.68798 ?  155 LEU B CG  1 
ATOM   7108 C CD1 . LEU F 2 135 ? -34.93800 68.37600 -30.19100 1.000 149.92059 ?  155 LEU B CD1 1 
ATOM   7109 C CD2 . LEU F 2 135 ? -35.87000 69.85100 -28.40000 1.000 156.36611 ?  155 LEU B CD2 1 
ATOM   7110 N N   . LEU F 2 136 ? -37.49200 67.80800 -32.50200 1.000 160.84429 ?  156 LEU B N   1 
ATOM   7111 C CA  . LEU F 2 136 ? -38.54300 66.79400 -32.52700 1.000 166.15585 ?  156 LEU B CA  1 
ATOM   7112 C C   . LEU F 2 136 ? -38.16600 65.71600 -31.52100 1.000 161.54810 ?  156 LEU B C   1 
ATOM   7113 O O   . LEU F 2 136 ? -37.31800 64.87500 -31.81400 1.000 156.57081 ?  156 LEU B O   1 
ATOM   7114 C CB  . LEU F 2 136 ? -38.67400 66.18600 -33.92000 1.000 169.78507 ?  156 LEU B CB  1 
ATOM   7115 C CG  . LEU F 2 136 ? -39.36000 66.84900 -35.11200 1.000 177.96285 ?  156 LEU B CG  1 
ATOM   7116 C CD1 . LEU F 2 136 ? -38.62800 68.10300 -35.57000 1.000 174.43870 ?  156 LEU B CD1 1 
ATOM   7117 C CD2 . LEU F 2 136 ? -39.39100 65.82800 -36.23200 1.000 182.18526 ?  156 LEU B CD2 1 
ATOM   7118 N N   . ASN F 2 137 ? -38.78600 65.70200 -30.35300 1.000 170.59226 ?  157 ASN B N   1 
ATOM   7119 C CA  . ASN F 2 137 ? -38.36200 64.78000 -29.31400 1.000 166.32226 ?  157 ASN B CA  1 
ATOM   7120 C C   . ASN F 2 137 ? -39.42200 63.70500 -29.09500 1.000 170.66015 ?  157 ASN B C   1 
ATOM   7121 O O   . ASN F 2 137 ? -40.61800 63.95500 -29.27900 1.000 177.87256 ?  157 ASN B O   1 
ATOM   7122 C CB  . ASN F 2 137 ? -38.07600 65.54800 -28.02100 1.000 165.02470 ?  157 ASN B CB  1 
ATOM   7123 C CG  . ASN F 2 137 ? -37.33800 64.71900 -27.00400 1.000 160.51713 ?  157 ASN B CG  1 
ATOM   7124 O OD1 . ASN F 2 137 ? -36.71600 63.71400 -27.34500 1.000 156.49706 ?  157 ASN B OD1 1 
ATOM   7125 N ND2 . ASN F 2 137 ? -37.37600 65.14900 -25.74700 1.000 161.74282 ?  157 ASN B ND2 1 
ATOM   7126 N N   . ASN F 2 138 ? -38.97500 62.50400 -28.70300 1.000 165.45508 ?  158 ASN B N   1 
ATOM   7127 C CA  . ASN F 2 138 ? -39.87500 61.41300 -28.30800 1.000 168.68998 ?  158 ASN B CA  1 
ATOM   7128 C C   . ASN F 2 138 ? -40.95000 61.14100 -29.36000 1.000 176.11623 ?  158 ASN B C   1 
ATOM   7129 O O   . ASN F 2 138 ? -42.15000 61.31500 -29.13300 1.000 182.33585 ?  158 ASN B O   1 
ATOM   7130 C CB  . ASN F 2 138 ? -40.51900 61.69400 -26.94900 1.000 170.94434 ?  158 ASN B CB  1 
ATOM   7131 C CG  . ASN F 2 138 ? -39.52900 62.20000 -25.92900 1.000 165.90042 ?  158 ASN B CG  1 
ATOM   7132 O OD1 . ASN F 2 138 ? -39.74300 63.23400 -25.29400 1.000 168.15459 ?  158 ASN B OD1 1 
ATOM   7133 N ND2 . ASN F 2 138 ? -38.43600 61.46700 -25.76000 1.000 160.02694 ?  158 ASN B ND2 1 
ATOM   7134 N N   . PHE F 2 139 ? -40.49200 60.71900 -30.53300 1.000 169.69922 ?  159 PHE B N   1 
ATOM   7135 C CA  . PHE F 2 139 ? -41.37500 60.40500 -31.64300 1.000 176.99910 ?  159 PHE B CA  1 
ATOM   7136 C C   . PHE F 2 139 ? -40.97100 59.09000 -32.28900 1.000 174.18669 ?  159 PHE B C   1 
ATOM   7137 O O   . PHE F 2 139 ? -39.81300 58.67300 -32.22500 1.000 166.67233 ?  159 PHE B O   1 
ATOM   7138 C CB  . PHE F 2 139 ? -41.38000 61.52700 -32.68200 1.000 181.33830 ?  159 PHE B CB  1 
ATOM   7139 C CG  . PHE F 2 139 ? -40.16000 61.56500 -33.55100 1.000 176.24932 ?  159 PHE B CG  1 
ATOM   7140 C CD1 . PHE F 2 139 ? -38.99700 62.15000 -33.09000 1.000 168.09798 ?  159 PHE B CD1 1 
ATOM   7141 C CD2 . PHE F 2 139 ? -40.18500 61.06100 -34.84000 1.000 179.85888 ?  159 PHE B CD2 1 
ATOM   7142 C CE1 . PHE F 2 139 ? -37.87100 62.20600 -33.88200 1.000 163.05918 ?  159 PHE B CE1 1 
ATOM   7143 C CE2 . PHE F 2 139 ? -39.06000 61.11600 -35.64100 1.000 175.49145 ?  159 PHE B CE2 1 
ATOM   7144 C CZ  . PHE F 2 139 ? -37.90100 61.69000 -35.16000 1.000 166.93037 ?  159 PHE B CZ  1 
ATOM   7145 N N   . TYR F 2 140 ? -41.95100 58.43800 -32.90700 1.000 169.06792 ?  160 TYR B N   1 
ATOM   7146 C CA  . TYR F 2 140 ? -41.72400 57.23400 -33.68900 1.000 174.56798 ?  160 TYR B CA  1 
ATOM   7147 C C   . TYR F 2 140 ? -42.73000 57.25100 -34.82700 1.000 196.67970 ?  160 TYR B C   1 
ATOM   7148 O O   . TYR F 2 140 ? -43.81300 57.82600 -34.67600 1.000 205.41305 ?  160 TYR B O   1 
ATOM   7149 C CB  . TYR F 2 140 ? -41.87900 55.96300 -32.84100 1.000 169.03612 ?  160 TYR B CB  1 
ATOM   7150 N N   . PRO F 2 141 ? -42.37900 56.70000 -35.99400 1.000 181.28404 ?  161 PRO B N   1 
ATOM   7151 C CA  . PRO F 2 141 ? -41.09500 56.08000 -36.30900 1.000 171.54567 ?  161 PRO B CA  1 
ATOM   7152 C C   . PRO F 2 141 ? -40.06500 57.15600 -36.61700 1.000 168.67489 ?  161 PRO B C   1 
ATOM   7153 O O   . PRO F 2 141 ? -40.34500 58.33200 -36.41900 1.000 172.30733 ?  161 PRO B O   1 
ATOM   7154 C CB  . PRO F 2 141 ? -41.44000 55.21900 -37.52500 1.000 183.35012 ?  161 PRO B CB  1 
ATOM   7155 C CG  . PRO F 2 141 ? -42.44000 56.07200 -38.26800 1.000 200.64305 ?  161 PRO B CG  1 
ATOM   7156 C CD  . PRO F 2 141 ? -43.24700 56.77500 -37.18500 1.000 199.32523 ?  161 PRO B CD  1 
ATOM   7157 N N   . ARG F 2 142 ? -38.88300 56.81700 -37.12400 1.000 172.86601 ?  162 ARG B N   1 
ATOM   7158 C CA  . ARG F 2 142 ? -37.87700 57.84500 -37.35900 1.000 169.31718 ?  162 ARG B CA  1 
ATOM   7159 C C   . ARG F 2 142 ? -38.08600 58.60500 -38.66200 1.000 188.50551 ?  162 ARG B C   1 
ATOM   7160 O O   . ARG F 2 142 ? -37.54200 59.70300 -38.81200 1.000 188.15185 ?  162 ARG B O   1 
ATOM   7161 C CB  . ARG F 2 142 ? -36.48100 57.21600 -37.33700 1.000 153.81245 ?  162 ARG B CB  1 
ATOM   7162 N N   . GLU F 2 143 ? -38.87900 58.06600 -39.58500 1.000 172.90668 ?  163 GLU B N   1 
ATOM   7163 C CA  . GLU F 2 143 ? -39.07600 58.65100 -40.91200 1.000 186.05117 ?  163 GLU B CA  1 
ATOM   7164 C C   . GLU F 2 143 ? -40.09600 59.78400 -40.81100 1.000 188.04281 ?  163 GLU B C   1 
ATOM   7165 O O   . GLU F 2 143 ? -41.30700 59.55200 -40.80000 1.000 191.06026 ?  163 GLU B O   1 
ATOM   7166 C CB  . GLU F 2 143 ? -39.50900 57.58200 -41.90900 1.000 189.69842 ?  163 GLU B CB  1 
ATOM   7167 C CG  . GLU F 2 143 ? -39.50200 58.05300 -43.35900 1.000 189.70568 ?  163 GLU B CG  1 
ATOM   7168 C CD  . GLU F 2 143 ? -40.77000 58.78900 -43.73500 1.000 192.08201 ?  163 GLU B CD  1 
ATOM   7169 O OE1 . GLU F 2 143 ? -41.84200 58.41000 -43.21600 1.000 195.03755 ?  163 GLU B OE1 1 
ATOM   7170 O OE2 . GLU F 2 143 ? -40.69300 59.74900 -44.53500 1.000 190.60962 ?  163 GLU B OE2 1 
ATOM   7171 N N   . ALA F 2 144 ? -39.60400 61.01700 -40.69100 1.000 190.91783 ?  164 ALA B N   1 
ATOM   7172 C CA  . ALA F 2 144 ? -40.43800 62.19600 -40.45600 1.000 189.29020 ?  164 ALA B CA  1 
ATOM   7173 C C   . ALA F 2 144 ? -40.02200 63.32700 -41.39400 1.000 189.07190 ?  164 ALA B C   1 
ATOM   7174 O O   . ALA F 2 144 ? -39.05800 64.04300 -41.10800 1.000 183.95385 ?  164 ALA B O   1 
ATOM   7175 C CB  . ALA F 2 144 ? -40.34700 62.63100 -38.99800 1.000 181.76639 ?  164 ALA B CB  1 
ATOM   7176 N N   . LYS F 2 145 ? -40.68800 63.45300 -42.54500 1.000 187.65481 ?  165 LYS B N   1 
ATOM   7177 C CA  . LYS F 2 145 ? -40.30200 64.49500 -43.49900 1.000 189.08538 ?  165 LYS B CA  1 
ATOM   7178 C C   . LYS F 2 145 ? -40.51100 65.86700 -42.85900 1.000 187.86492 ?  165 LYS B C   1 
ATOM   7179 O O   . LYS F 2 145 ? -41.64500 66.33400 -42.70500 1.000 190.25368 ?  165 LYS B O   1 
ATOM   7180 C CB  . LYS F 2 145 ? -41.09500 64.35900 -44.79400 1.000 192.77066 ?  165 LYS B CB  1 
ATOM   7181 N N   . VAL F 2 146 ? -39.41500 66.49800 -42.43300 1.000 197.37038 ?  166 VAL B N   1 
ATOM   7182 C CA  . VAL F 2 146 ? -39.46600 67.83300 -41.84400 1.000 193.58395 ?  166 VAL B CA  1 
ATOM   7183 C C   . VAL F 2 146 ? -39.36500 68.87300 -42.95400 1.000 199.41816 ?  166 VAL B C   1 
ATOM   7184 O O   . VAL F 2 146 ? -38.51400 68.76900 -43.84600 1.000 202.20964 ?  166 VAL B O   1 
ATOM   7185 C CB  . VAL F 2 146 ? -38.35900 68.01700 -40.79400 1.000 182.97689 ?  166 VAL B CB  1 
ATOM   7186 C CG1 . VAL F 2 146 ? -38.45100 69.40300 -40.16200 1.000 176.88962 ?  166 VAL B CG1 1 
ATOM   7187 C CG2 . VAL F 2 146 ? -38.47600 66.94700 -39.72700 1.000 177.44585 ?  166 VAL B CG2 1 
ATOM   7188 N N   . SER F 2 147 ? -40.23200 69.87700 -42.88900 1.000 197.82523 ?  167 SER B N   1 
ATOM   7189 C CA  . SER F 2 147 ? -40.36300 70.94200 -43.87100 1.000 202.87785 ?  167 SER B CA  1 
ATOM   7190 C C   . SER F 2 147 ? -40.22100 72.28900 -43.17000 1.000 197.58927 ?  167 SER B C   1 
ATOM   7191 O O   . SER F 2 147 ? -40.66800 72.45000 -42.02900 1.000 192.05776 ?  167 SER B O   1 
ATOM   7192 C CB  . SER F 2 147 ? -41.71600 70.84700 -44.57700 1.000 210.26434 ?  167 SER B CB  1 
ATOM   7193 O OG  . SER F 2 147 ? -41.68700 69.88200 -45.61600 1.000 214.78246 ?  167 SER B OG  1 
ATOM   7194 N N   . TRP F 2 148 ? -39.60700 73.25800 -43.84600 1.000 213.34734 ?  168 TRP B N   1 
ATOM   7195 C CA  . TRP F 2 148 ? -39.43900 74.60600 -43.31300 1.000 208.34811 ?  168 TRP B CA  1 
ATOM   7196 C C   . TRP F 2 148 ? -40.18400 75.59800 -44.19900 1.000 216.80149 ?  168 TRP B C   1 
ATOM   7197 O O   . TRP F 2 148 ? -40.23400 75.43100 -45.42100 1.000 224.03320 ?  168 TRP B O   1 
ATOM   7198 C CB  . TRP F 2 148 ? -37.96300 75.00700 -43.23900 1.000 199.77789 ?  168 TRP B CB  1 
ATOM   7199 C CG  . TRP F 2 148 ? -37.27000 74.59700 -41.99100 1.000 187.33247 ?  168 TRP B CG  1 
ATOM   7200 C CD1 . TRP F 2 148 ? -36.51500 73.47700 -41.79600 1.000 185.02460 ?  168 TRP B CD1 1 
ATOM   7201 C CD2 . TRP F 2 148 ? -37.26700 75.30500 -40.75000 1.000 174.07684 ?  168 TRP B CD2 1 
ATOM   7202 N NE1 . TRP F 2 148 ? -36.03700 73.44800 -40.50900 1.000 171.62628 ?  168 TRP B NE1 1 
ATOM   7203 C CE2 . TRP F 2 148 ? -36.48600 74.55900 -39.84500 1.000 163.92855 ?  168 TRP B CE2 1 
ATOM   7204 C CE3 . TRP F 2 148 ? -37.84900 76.49700 -40.31600 1.000 168.61982 ?  168 TRP B CE3 1 
ATOM   7205 C CZ2 . TRP F 2 148 ? -36.27200 74.96900 -38.53400 1.000 148.23336 ?  168 TRP B CZ2 1 
ATOM   7206 C CZ3 . TRP F 2 148 ? -37.63700 76.90000 -39.01600 1.000 151.00148 ?  168 TRP B CZ3 1 
ATOM   7207 C CH2 . TRP F 2 148 ? -36.86000 76.13400 -38.13900 1.000 140.58171 ?  168 TRP B CH2 1 
ATOM   7208 N N   . TYR F 2 149 ? -40.76300 76.63100 -43.58100 1.000 195.58117 ?  169 TYR B N   1 
ATOM   7209 C CA  . TYR F 2 149 ? -41.57500 77.61400 -44.30000 1.000 204.11979 ?  169 TYR B CA  1 
ATOM   7210 C C   . TYR F 2 149 ? -41.29500 79.01100 -43.75700 1.000 194.59040 ?  169 TYR B C   1 
ATOM   7211 O O   . TYR F 2 149 ? -41.77400 79.36200 -42.67900 1.000 187.54121 ?  169 TYR B O   1 
ATOM   7212 C CB  . TYR F 2 149 ? -43.06100 77.26600 -44.19400 1.000 210.05195 ?  169 TYR B CB  1 
ATOM   7213 C CG  . TYR F 2 149 ? -43.37200 75.87600 -44.70700 1.000 212.40412 ?  169 TYR B CG  1 
ATOM   7214 C CD1 . TYR F 2 149 ? -43.55900 75.64700 -46.06200 1.000 218.82202 ?  169 TYR B CD1 1 
ATOM   7215 C CD2 . TYR F 2 149 ? -43.47800 74.79500 -43.84000 1.000 207.55671 ?  169 TYR B CD2 1 
ATOM   7216 C CE1 . TYR F 2 149 ? -43.83400 74.37800 -46.54400 1.000 219.92907 ?  169 TYR B CE1 1 
ATOM   7217 C CE2 . TYR F 2 149 ? -43.76100 73.52500 -44.31300 1.000 209.97358 ?  169 TYR B CE2 1 
ATOM   7218 C CZ  . TYR F 2 149 ? -43.93600 73.32200 -45.66900 1.000 216.13245 ?  169 TYR B CZ  1 
ATOM   7219 O OH  . TYR F 2 149 ? -44.21600 72.06700 -46.16600 1.000 218.02055 ?  169 TYR B OH  1 
ATOM   7220 N N   . VAL F 2 150 ? -40.54100 79.81300 -44.50100 1.000 210.97009 ?  170 VAL B N   1 
ATOM   7221 C CA  . VAL F 2 150 ? -40.27900 81.20000 -44.12700 1.000 193.41764 ?  170 VAL B CA  1 
ATOM   7222 C C   . VAL F 2 150 ? -41.36100 82.08000 -44.74800 1.000 200.58837 ?  170 VAL B C   1 
ATOM   7223 O O   . VAL F 2 150 ? -41.39500 82.27400 -45.96500 1.000 209.89972 ?  170 VAL B O   1 
ATOM   7224 C CB  . VAL F 2 150 ? -38.87700 81.63900 -44.55900 1.000 182.16041 ?  170 VAL B CB  1 
ATOM   7225 C CG1 . VAL F 2 150 ? -38.60800 83.05000 -44.10500 1.000 165.39398 ?  170 VAL B CG1 1 
ATOM   7226 C CG2 . VAL F 2 150 ? -37.85200 80.70400 -43.96300 1.000 176.21991 ?  170 VAL B CG2 1 
ATOM   7227 N N   . ASP F 2 151 ? -42.25800 82.60400 -43.91000 1.000 190.81559 ?  171 ASP B N   1 
ATOM   7228 C CA  . ASP F 2 151 ? -43.47500 83.26200 -44.38900 1.000 194.81825 ?  171 ASP B CA  1 
ATOM   7229 C C   . ASP F 2 151 ? -44.22800 82.34700 -45.34800 1.000 202.86268 ?  171 ASP B C   1 
ATOM   7230 O O   . ASP F 2 151 ? -44.60000 82.73500 -46.45900 1.000 208.86010 ?  171 ASP B O   1 
ATOM   7231 C CB  . ASP F 2 151 ? -43.19000 84.62000 -45.03400 1.000 194.99366 ?  171 ASP B CB  1 
ATOM   7232 C CG  . ASP F 2 151 ? -42.75400 85.66700 -44.03100 1.000 194.33102 ?  171 ASP B CG  1 
ATOM   7233 O OD1 . ASP F 2 151 ? -42.63200 85.32900 -42.83400 1.000 199.96088 ?  171 ASP B OD1 1 
ATOM   7234 O OD2 . ASP F 2 151 ? -42.56800 86.83500 -44.43700 1.000 195.10539 -1 171 ASP B OD2 1 
ATOM   7235 N N   . ASN F 2 152 ? -44.44000 81.10900 -44.89800 1.000 204.28152 ?  172 ASN B N   1 
ATOM   7236 C CA  . ASN F 2 152 ? -45.12100 80.08200 -45.68200 1.000 213.26763 ?  172 ASN B CA  1 
ATOM   7237 C C   . ASN F 2 152 ? -44.40400 79.83100 -47.00800 1.000 223.41470 ?  172 ASN B C   1 
ATOM   7238 O O   . ASN F 2 152 ? -45.02100 79.79000 -48.07300 1.000 231.23247 ?  172 ASN B O   1 
ATOM   7239 C CB  . ASN F 2 152 ? -46.58600 80.46100 -45.91200 1.000 214.50006 ?  172 ASN B CB  1 
ATOM   7240 C CG  . ASN F 2 152 ? -47.28100 80.88500 -44.63500 1.000 205.30918 ?  172 ASN B CG  1 
ATOM   7241 O OD1 . ASN F 2 152 ? -46.68100 81.53100 -43.77400 1.000 199.82855 ?  172 ASN B OD1 1 
ATOM   7242 N ND2 . ASN F 2 152 ? -48.55600 80.53500 -44.51100 1.000 205.93492 ?  172 ASN B ND2 1 
ATOM   7243 N N   . ALA F 2 153 ? -43.08100 79.68100 -46.93900 1.000 206.81068 ?  173 ALA B N   1 
ATOM   7244 C CA  . ALA F 2 153 ? -42.28000 79.36400 -48.11600 1.000 216.64686 ?  173 ALA B CA  1 
ATOM   7245 C C   . ALA F 2 153 ? -41.39700 78.15600 -47.84600 1.000 216.58720 ?  173 ALA B C   1 
ATOM   7246 O O   . ALA F 2 153 ? -40.48200 78.22700 -47.01900 1.000 206.05639 ?  173 ALA B O   1 
ATOM   7247 C CB  . ALA F 2 153 ? -41.42000 80.55800 -48.53800 1.000 213.01805 ?  173 ALA B CB  1 
ATOM   7248 N N   . LEU F 2 154 ? -41.64800 77.06900 -48.57800 1.000 218.20476 ?  174 LEU B N   1 
ATOM   7249 C CA  . LEU F 2 154 ? -40.87600 75.84100 -48.42900 1.000 217.26389 ?  174 LEU B CA  1 
ATOM   7250 C C   . LEU F 2 154 ? -39.39100 76.12100 -48.63500 1.000 210.29837 ?  174 LEU B C   1 
ATOM   7251 O O   . LEU F 2 154 ? -39.00300 76.87600 -49.53000 1.000 207.70528 ?  174 LEU B O   1 
ATOM   7252 C CB  . LEU F 2 154 ? -41.36600 74.78200 -49.41800 1.000 222.95301 ?  174 LEU B CB  1 
ATOM   7253 N N   . GLN F 2 155 ? -38.55600 75.50700 -47.80200 1.000 222.14448 ?  175 GLN B N   1 
ATOM   7254 C CA  . GLN F 2 155 ? -37.13100 75.79900 -47.76900 1.000 210.64126 ?  175 GLN B CA  1 
ATOM   7255 C C   . GLN F 2 155 ? -36.35700 74.59500 -48.28700 1.000 204.15157 ?  175 GLN B C   1 
ATOM   7256 O O   . GLN F 2 155 ? -36.56800 73.46900 -47.82200 1.000 207.39935 ?  175 GLN B O   1 
ATOM   7257 C CB  . GLN F 2 155 ? -36.67900 76.12900 -46.34700 1.000 200.73212 ?  175 GLN B CB  1 
ATOM   7258 C CG  . GLN F 2 155 ? -37.36700 77.34600 -45.74700 1.000 198.04469 ?  175 GLN B CG  1 
ATOM   7259 C CD  . GLN F 2 155 ? -37.15500 78.61100 -46.54500 1.000 197.95368 ?  175 GLN B CD  1 
ATOM   7260 O OE1 . GLN F 2 155 ? -36.05400 79.15800 -46.59200 1.000 189.95384 ?  175 GLN B OE1 1 
ATOM   7261 N NE2 . GLN F 2 155 ? -38.22100 79.08800 -47.17900 1.000 206.13762 ?  175 GLN B NE2 1 
ATOM   7262 N N   . SER F 2 156 ? -35.46700 74.83700 -49.24600 1.000 222.32970 ?  176 SER B N   1 
ATOM   7263 C CA  . SER F 2 156 ? -34.61900 73.79900 -49.80700 1.000 202.11353 ?  176 SER B CA  1 
ATOM   7264 C C   . SER F 2 156 ? -33.15300 74.15600 -49.60400 1.000 181.53679 ?  176 SER B C   1 
ATOM   7265 O O   . SER F 2 156 ? -32.79900 75.31500 -49.36700 1.000 177.02981 ?  176 SER B O   1 
ATOM   7266 C CB  . SER F 2 156 ? -34.90300 73.61900 -51.30700 1.000 182.96416 ?  176 SER B CB  1 
ATOM   7267 O OG  . SER F 2 156 ? -33.78400 73.07400 -51.98500 1.000 166.13877 ?  176 SER B OG  1 
ATOM   7268 N N   . GLY F 2 157 ? -32.29900 73.14000 -49.72300 1.000 181.77401 ?  177 GLY B N   1 
ATOM   7269 C CA  . GLY F 2 157 ? -30.85800 73.30600 -49.65400 1.000 170.07064 ?  177 GLY B CA  1 
ATOM   7270 C C   . GLY F 2 157 ? -30.33500 74.09400 -48.46700 1.000 172.24261 ?  177 GLY B C   1 
ATOM   7271 O O   . GLY F 2 157 ? -29.15900 74.46900 -48.45400 1.000 162.61406 ?  177 GLY B O   1 
ATOM   7272 N N   . ASN F 2 158 ? -31.18400 74.35600 -47.46500 1.000 160.74169 ?  178 ASN B N   1 
ATOM   7273 C CA  . ASN F 2 158 ? -30.75600 75.02500 -46.24200 1.000 162.93661 ?  178 ASN B CA  1 
ATOM   7274 C C   . ASN F 2 158 ? -31.07900 74.23200 -44.98500 1.000 176.99274 ?  178 ASN B C   1 
ATOM   7275 O O   . ASN F 2 158 ? -30.86800 74.74500 -43.88000 1.000 176.90810 ?  178 ASN B O   1 
ATOM   7276 C CB  . ASN F 2 158 ? -31.41200 76.40500 -46.11700 1.000 169.43200 ?  178 ASN B CB  1 
ATOM   7277 C CG  . ASN F 2 158 ? -32.89700 76.37300 -46.43400 1.000 188.95939 ?  178 ASN B CG  1 
ATOM   7278 O OD1 . ASN F 2 158 ? -33.54200 75.32700 -46.34400 1.000 198.98502 ?  178 ASN B OD1 1 
ATOM   7279 N ND2 . ASN F 2 158 ? -33.44800 77.52400 -46.80000 1.000 192.54306 ?  178 ASN B ND2 1 
ATOM   7280 N N   . SER F 2 159 ? -31.57100 73.00700 -45.10800 1.000 170.22723 ?  179 SER B N   1 
ATOM   7281 C CA  . SER F 2 159 ? -32.00400 72.23700 -43.95400 1.000 176.40905 ?  179 SER B CA  1 
ATOM   7282 C C   . SER F 2 159 ? -31.02200 71.10300 -43.72500 1.000 171.42512 ?  179 SER B C   1 
ATOM   7283 O O   . SER F 2 159 ? -30.85500 70.23700 -44.59000 1.000 170.26791 ?  179 SER B O   1 
ATOM   7284 C CB  . SER F 2 159 ? -33.41200 71.68200 -44.15500 1.000 186.56387 ?  179 SER B CB  1 
ATOM   7285 O OG  . SER F 2 159 ? -33.60800 71.26100 -45.49400 1.000 190.45274 ?  179 SER B OG  1 
ATOM   7286 N N   . GLN F 2 160 ? -30.38500 71.10900 -42.56100 1.000 174.08282 ?  180 GLN B N   1 
ATOM   7287 C CA  . GLN F 2 160 ? -29.51500 70.01000 -42.15500 1.000 171.41711 ?  180 GLN B CA  1 
ATOM   7288 C C   . GLN F 2 160 ? -30.17400 69.29500 -40.98500 1.000 173.89444 ?  180 GLN B C   1 
ATOM   7289 O O   . GLN F 2 160 ? -30.50700 69.92500 -39.97600 1.000 171.62697 ?  180 GLN B O   1 
ATOM   7290 C CB  . GLN F 2 160 ? -28.11200 70.49700 -41.78800 1.000 162.97319 ?  180 GLN B CB  1 
ATOM   7291 N N   . GLU F 2 161 ? -30.41500 67.99500 -41.14700 1.000 167.37452 ?  181 GLU B N   1 
ATOM   7292 C CA  . GLU F 2 161 ? -31.10700 67.18800 -40.15400 1.000 168.11130 ?  181 GLU B CA  1 
ATOM   7293 C C   . GLU F 2 161 ? -30.12200 66.27200 -39.43500 1.000 164.80688 ?  181 GLU B C   1 
ATOM   7294 O O   . GLU F 2 161 ? -29.15500 65.78900 -40.02700 1.000 164.56343 ?  181 GLU B O   1 
ATOM   7295 C CB  . GLU F 2 161 ? -32.21400 66.35900 -40.81500 1.000 174.66557 ?  181 GLU B CB  1 
ATOM   7296 C CG  . GLU F 2 161 ? -33.59600 66.98800 -40.73800 1.000 177.93449 ?  181 GLU B CG  1 
ATOM   7297 C CD  . GLU F 2 161 ? -34.55600 66.48200 -41.80700 1.000 185.71235 ?  181 GLU B CD  1 
ATOM   7298 O OE1 . GLU F 2 161 ? -34.52000 67.00600 -42.94300 1.000 190.57397 ?  181 GLU B OE1 1 
ATOM   7299 O OE2 . GLU F 2 161 ? -35.36500 65.57700 -41.49800 1.000 184.81865 -1 181 GLU B OE2 1 
ATOM   7300 N N   . SER F 2 162 ? -30.38000 66.03000 -38.14900 1.000 165.04555 ?  182 SER B N   1 
ATOM   7301 C CA  . SER F 2 162 ? -29.57200 65.10000 -37.36500 1.000 162.80250 ?  182 SER B CA  1 
ATOM   7302 C C   . SER F 2 162 ? -30.46500 64.40200 -36.34300 1.000 162.86996 ?  182 SER B C   1 
ATOM   7303 O O   . SER F 2 162 ? -31.29300 65.04700 -35.69700 1.000 162.54823 ?  182 SER B O   1 
ATOM   7304 C CB  . SER F 2 162 ? -28.40900 65.82400 -36.67300 1.000 158.85384 ?  182 SER B CB  1 
ATOM   7305 O OG  . SER F 2 162 ? -27.56700 64.91100 -35.99300 1.000 157.65287 ?  182 SER B OG  1 
ATOM   7306 N N   . VAL F 2 163 ? -30.29500 63.08500 -36.20400 1.000 153.51443 ?  183 VAL B N   1 
ATOM   7307 C CA  . VAL F 2 163 ? -31.17200 62.25200 -35.38200 1.000 153.90411 ?  183 VAL B CA  1 
ATOM   7308 C C   . VAL F 2 163 ? -30.36300 61.42100 -34.39700 1.000 152.33950 ?  183 VAL B C   1 
ATOM   7309 O O   . VAL F 2 163 ? -29.30500 60.88600 -34.74700 1.000 150.76891 ?  183 VAL B O   1 
ATOM   7310 C CB  . VAL F 2 163 ? -32.03900 61.32500 -36.25900 1.000 155.97872 ?  183 VAL B CB  1 
ATOM   7311 C CG1 . VAL F 2 163 ? -33.12800 60.68000 -35.42600 1.000 156.92638 ?  183 VAL B CG1 1 
ATOM   7312 C CG2 . VAL F 2 163 ? -32.63600 62.09800 -37.42100 1.000 158.86212 ?  183 VAL B CG2 1 
ATOM   7313 N N   . THR F 2 164 ? -30.87800 61.28700 -33.17400 1.000 155.11687 ?  184 THR B N   1 
ATOM   7314 C CA  . THR F 2 164 ? -30.24000 60.45200 -32.16300 1.000 156.26252 ?  184 THR B CA  1 
ATOM   7315 C C   . THR F 2 164 ? -30.55200 58.98800 -32.45500 1.000 154.41834 ?  184 THR B C   1 
ATOM   7316 O O   . THR F 2 164 ? -31.15000 58.63900 -33.47600 1.000 152.19914 ?  184 THR B O   1 
ATOM   7317 C CB  . THR F 2 164 ? -30.73100 60.79500 -30.76000 1.000 164.56492 ?  184 THR B CB  1 
ATOM   7318 O OG1 . THR F 2 164 ? -32.04400 60.24900 -30.58600 1.000 169.13590 ?  184 THR B OG1 1 
ATOM   7319 C CG2 . THR F 2 164 ? -30.78200 62.29400 -30.55600 1.000 168.21882 ?  184 THR B CG2 1 
ATOM   7320 N N   . GLU F 2 165 ? -30.17000 58.11600 -31.53400 1.000 161.39998 ?  185 GLU B N   1 
ATOM   7321 C CA  . GLU F 2 165 ? -30.48200 56.70100 -31.58400 1.000 160.93004 ?  185 GLU B CA  1 
ATOM   7322 C C   . GLU F 2 165 ? -31.61800 56.41800 -30.61300 1.000 165.23015 ?  185 GLU B C   1 
ATOM   7323 O O   . GLU F 2 165 ? -31.86000 57.18700 -29.68000 1.000 168.88293 ?  185 GLU B O   1 
ATOM   7324 C CB  . GLU F 2 165 ? -29.25500 55.86600 -31.23000 1.000 158.23307 ?  185 GLU B CB  1 
ATOM   7325 N N   . GLN F 2 166 ? -32.34200 55.32500 -30.86100 1.000 165.35080 ?  186 GLN B N   1 
ATOM   7326 C CA  . GLN F 2 166 ? -33.46900 54.97500 -30.00300 1.000 172.09430 ?  186 GLN B CA  1 
ATOM   7327 C C   . GLN F 2 166 ? -33.06400 55.05100 -28.54500 1.000 176.82649 ?  186 GLN B C   1 
ATOM   7328 O O   . GLN F 2 166 ? -32.14200 54.36000 -28.10800 1.000 174.45608 ?  186 GLN B O   1 
ATOM   7329 C CB  . GLN F 2 166 ? -33.99600 53.57600 -30.31800 1.000 172.48025 ?  186 GLN B CB  1 
ATOM   7330 C CG  . GLN F 2 166 ? -34.43300 53.37900 -31.73600 1.000 169.43311 ?  186 GLN B CG  1 
ATOM   7331 C CD  . GLN F 2 166 ? -35.60100 52.42900 -31.84400 1.000 173.88131 ?  186 GLN B CD  1 
ATOM   7332 O OE1 . GLN F 2 166 ? -35.64700 51.57300 -32.72900 1.000 172.32337 ?  186 GLN B OE1 1 
ATOM   7333 N NE2 . GLN F 2 166 ? -36.56500 52.58500 -30.94600 1.000 181.57611 ?  186 GLN B NE2 1 
ATOM   7334 N N   . ASP F 2 167 ? -33.74100 55.91800 -27.80000 1.000 184.01606 ?  187 ASP B N   1 
ATOM   7335 C CA  . ASP F 2 167 ? -33.43900 56.04500 -26.38700 1.000 190.06581 ?  187 ASP B CA  1 
ATOM   7336 C C   . ASP F 2 167 ? -33.70800 54.72400 -25.68900 1.000 193.34661 ?  187 ASP B C   1 
ATOM   7337 O O   . ASP F 2 167 ? -34.64300 54.00000 -26.03500 1.000 195.08637 ?  187 ASP B O   1 
ATOM   7338 C CB  . ASP F 2 167 ? -34.27200 57.14900 -25.74300 1.000 198.83446 ?  187 ASP B CB  1 
ATOM   7339 C CG  . ASP F 2 167 ? -34.22200 57.09400 -24.22900 1.000 207.41056 ?  187 ASP B CG  1 
ATOM   7340 O OD1 . ASP F 2 167 ? -33.15200 57.38700 -23.65700 1.000 206.60723 ?  187 ASP B OD1 1 
ATOM   7341 O OD2 . ASP F 2 167 ? -35.24500 56.72100 -23.61800 1.000 215.36627 -1 187 ASP B OD2 1 
ATOM   7342 N N   . SER F 2 168 ? -32.86300 54.40800 -24.71000 1.000 194.42829 ?  188 SER B N   1 
ATOM   7343 C CA  . SER F 2 168 ? -32.96400 53.12300 -24.03200 1.000 196.99398 ?  188 SER B CA  1 
ATOM   7344 C C   . SER F 2 168 ? -34.32600 52.93400 -23.37400 1.000 206.84973 ?  188 SER B C   1 
ATOM   7345 O O   . SER F 2 168 ? -34.81400 51.80200 -23.28000 1.000 208.57517 ?  188 SER B O   1 
ATOM   7346 C CB  . SER F 2 168 ? -31.85000 52.99800 -22.99600 1.000 197.52524 ?  188 SER B CB  1 
ATOM   7347 O OG  . SER F 2 168 ? -31.83000 54.12500 -22.13500 1.000 204.12016 ?  188 SER B OG  1 
ATOM   7348 N N   . LYS F 2 169 ? -34.96200 54.01800 -22.93200 1.000 213.94825 ?  189 LYS B N   1 
ATOM   7349 C CA  . LYS F 2 169 ? -36.20500 53.88700 -22.17500 1.000 224.76420 ?  189 LYS B CA  1 
ATOM   7350 C C   . LYS F 2 169 ? -37.43900 53.92600 -23.07700 1.000 225.82310 ?  189 LYS B C   1 
ATOM   7351 O O   . LYS F 2 169 ? -38.18500 52.94600 -23.16000 1.000 228.30687 ?  189 LYS B O   1 
ATOM   7352 C CB  . LYS F 2 169 ? -36.28600 54.98700 -21.11100 1.000 233.85848 ?  189 LYS B CB  1 
ATOM   7353 N N   . ASP F 2 170 ? -37.66100 55.04700 -23.76500 1.000 224.24725 ?  190 ASP B N   1 
ATOM   7354 C CA  . ASP F 2 170 ? -38.85800 55.19100 -24.58200 1.000 225.97213 ?  190 ASP B CA  1 
ATOM   7355 C C   . ASP F 2 170 ? -38.71800 54.51900 -25.94000 1.000 216.65651 ?  190 ASP B C   1 
ATOM   7356 O O   . ASP F 2 170 ? -39.73400 54.21700 -26.57600 1.000 218.51651 ?  190 ASP B O   1 
ATOM   7357 C CB  . ASP F 2 170 ? -39.20600 56.67600 -24.74900 1.000 228.76238 ?  190 ASP B CB  1 
ATOM   7358 C CG  . ASP F 2 170 ? -38.05500 57.49900 -25.30500 1.000 220.33710 ?  190 ASP B CG  1 
ATOM   7359 O OD1 . ASP F 2 170 ? -37.54100 57.17400 -26.39900 1.000 210.74613 ?  190 ASP B OD1 1 
ATOM   7360 O OD2 . ASP F 2 170 ? -37.66300 58.47500 -24.63200 1.000 224.11654 -1 190 ASP B OD2 1 
ATOM   7361 N N   . SER F 2 171 ? -37.48600 54.29600 -26.39600 1.000 207.46761 ?  191 SER B N   1 
ATOM   7362 C CA  . SER F 2 171 ? -37.21000 53.68200 -27.69400 1.000 199.04209 ?  191 SER B CA  1 
ATOM   7363 C C   . SER F 2 171 ? -37.77900 54.51400 -28.83400 1.000 196.84718 ?  191 SER B C   1 
ATOM   7364 O O   . SER F 2 171 ? -38.10200 53.99200 -29.90500 1.000 193.40944 ?  191 SER B O   1 
ATOM   7365 C CB  . SER F 2 171 ? -37.74600 52.25300 -27.74500 1.000 200.99977 ?  191 SER B CB  1 
ATOM   7366 O OG  . SER F 2 171 ? -37.25100 51.50700 -26.64600 1.000 203.42169 ?  191 SER B OG  1 
ATOM   7367 N N   . THR F 2 172 ? -37.90100 55.81200 -28.59900 1.000 199.36513 ?  192 THR B N   1 
ATOM   7368 C CA  . THR F 2 172 ? -38.23800 56.79000 -29.61400 1.000 196.70917 ?  192 THR B CA  1 
ATOM   7369 C C   . THR F 2 172 ? -37.00400 57.62600 -29.91600 1.000 189.93553 ?  192 THR B C   1 
ATOM   7370 O O   . THR F 2 172 ? -36.02900 57.64400 -29.15900 1.000 189.18368 ?  192 THR B O   1 
ATOM   7371 C CB  . THR F 2 172 ? -39.40400 57.67400 -29.15500 1.000 205.64861 ?  192 THR B CB  1 
ATOM   7372 O OG1 . THR F 2 172 ? -38.98500 58.47400 -28.04400 1.000 210.35833 ?  192 THR B OG1 1 
ATOM   7373 C CG2 . THR F 2 172 ? -40.58500 56.80900 -28.74400 1.000 213.39754 ?  192 THR B CG2 1 
ATOM   7374 N N   . TYR F 2 173 ? -37.06200 58.33900 -31.02400 1.000 163.75310 ?  193 TYR B N   1 
ATOM   7375 C CA  . TYR F 2 173 ? -35.91900 59.08900 -31.49700 1.000 161.01543 ?  193 TYR B CA  1 
ATOM   7376 C C   . TYR F 2 173 ? -36.06500 60.57100 -31.13900 1.000 158.61705 ?  193 TYR B C   1 
ATOM   7377 O O   . TYR F 2 173 ? -37.00200 60.99900 -30.43900 1.000 159.19185 ?  193 TYR B O   1 
ATOM   7378 C CB  . TYR F 2 173 ? -35.75200 58.87700 -33.01000 1.000 166.51138 ?  193 TYR B CB  1 
ATOM   7379 C CG  . TYR F 2 173 ? -35.81900 57.42900 -33.47400 1.000 171.58764 ?  193 TYR B CG  1 
ATOM   7380 C CD1 . TYR F 2 173 ? -37.04100 56.79200 -33.66800 1.000 176.97084 ?  193 TYR B CD1 1 
ATOM   7381 C CD2 . TYR F 2 173 ? -34.66000 56.72000 -33.77600 1.000 170.86958 ?  193 TYR B CD2 1 
ATOM   7382 C CE1 . TYR F 2 173 ? -37.10600 55.47600 -34.10000 1.000 181.87554 ?  193 TYR B CE1 1 
ATOM   7383 C CE2 . TYR F 2 173 ? -34.71600 55.41100 -34.22600 1.000 176.50413 ?  193 TYR B CE2 1 
ATOM   7384 C CZ  . TYR F 2 173 ? -35.94200 54.79100 -34.37900 1.000 182.11475 ?  193 TYR B CZ  1 
ATOM   7385 O OH  . TYR F 2 173 ? -36.00200 53.48500 -34.81600 1.000 186.32753 ?  193 TYR B OH  1 
ATOM   7386 N N   . SER F 2 174 ? -35.11800 61.36200 -31.63200 1.000 156.83599 ?  194 SER B N   1 
ATOM   7387 C CA  . SER F 2 174 ? -35.12700 62.81100 -31.52200 1.000 156.16837 ?  194 SER B CA  1 
ATOM   7388 C C   . SER F 2 174 ? -34.42300 63.35000 -32.75400 1.000 157.23603 ?  194 SER B C   1 
ATOM   7389 O O   . SER F 2 174 ? -33.33900 62.88200 -33.11100 1.000 154.05970 ?  194 SER B O   1 
ATOM   7390 C CB  . SER F 2 174 ? -34.42700 63.29200 -30.24500 1.000 150.70716 ?  194 SER B CB  1 
ATOM   7391 O OG  . SER F 2 174 ? -35.18900 62.97700 -29.09400 1.000 151.16030 ?  194 SER B OG  1 
ATOM   7392 N N   . LEU F 2 175 ? -35.04700 64.32600 -33.39500 1.000 155.64013 ?  195 LEU B N   1 
ATOM   7393 C CA  . LEU F 2 175 ? -34.58800 64.89500 -34.64700 1.000 158.23529 ?  195 LEU B CA  1 
ATOM   7394 C C   . LEU F 2 175 ? -34.34000 66.38000 -34.45700 1.000 157.57504 ?  195 LEU B C   1 
ATOM   7395 O O   . LEU F 2 175 ? -34.94800 67.02700 -33.60100 1.000 157.60660 ?  195 LEU B O   1 
ATOM   7396 C CB  . LEU F 2 175 ? -35.61500 64.67200 -35.76300 1.000 165.51060 ?  195 LEU B CB  1 
ATOM   7397 C CG  . LEU F 2 175 ? -35.20100 64.93700 -37.21300 1.000 169.87751 ?  195 LEU B CG  1 
ATOM   7398 C CD1 . LEU F 2 175 ? -35.75500 63.86400 -38.13600 1.000 177.19633 ?  195 LEU B CD1 1 
ATOM   7399 C CD2 . LEU F 2 175 ? -35.66500 66.31300 -37.65400 1.000 172.59195 ?  195 LEU B CD2 1 
ATOM   7400 N N   . SER F 2 176 ? -33.44900 66.92000 -35.27200 1.000 158.77640 ?  196 SER B N   1 
ATOM   7401 C CA  . SER F 2 176 ? -33.09700 68.32800 -35.16500 1.000 159.20383 ?  196 SER B CA  1 
ATOM   7402 C C   . SER F 2 176 ? -32.81100 68.81300 -36.57400 1.000 162.33441 ?  196 SER B C   1 
ATOM   7403 O O   . SER F 2 176 ? -31.83800 68.37500 -37.19700 1.000 160.69335 ?  196 SER B O   1 
ATOM   7404 C CB  . SER F 2 176 ? -31.89600 68.52900 -34.24500 1.000 154.98431 ?  196 SER B CB  1 
ATOM   7405 O OG  . SER F 2 176 ? -30.70300 68.05800 -34.84300 1.000 151.46276 ?  196 SER B OG  1 
ATOM   7406 N N   . SER F 2 177 ? -33.68400 69.67100 -37.08400 1.000 161.39606 ?  197 SER B N   1 
ATOM   7407 C CA  . SER F 2 177 ? -33.48500 70.25900 -38.39700 1.000 164.78970 ?  197 SER B CA  1 
ATOM   7408 C C   . SER F 2 177 ? -33.11400 71.72300 -38.24500 1.000 164.92818 ?  197 SER B C   1 
ATOM   7409 O O   . SER F 2 177 ? -33.71500 72.44800 -37.44300 1.000 164.99304 ?  197 SER B O   1 
ATOM   7410 C CB  . SER F 2 177 ? -34.72900 70.13100 -39.27700 1.000 170.72971 ?  197 SER B CB  1 
ATOM   7411 O OG  . SER F 2 177 ? -34.44800 70.60300 -40.58500 1.000 173.73071 ?  197 SER B OG  1 
ATOM   7412 N N   . THR F 2 178 ? -32.13000 72.16000 -39.02500 1.000 162.33850 ?  198 THR B N   1 
ATOM   7413 C CA  . THR F 2 178 ? -31.62400 73.51800 -38.91700 1.000 163.78731 ?  198 THR B CA  1 
ATOM   7414 C C   . THR F 2 178 ? -31.82500 74.22900 -40.24500 1.000 166.81128 ?  198 THR B C   1 
ATOM   7415 O O   . THR F 2 178 ? -31.35700 73.75100 -41.29200 1.000 165.82806 ?  198 THR B O   1 
ATOM   7416 C CB  . THR F 2 178 ? -30.15400 73.55400 -38.50100 1.000 162.70548 ?  198 THR B CB  1 
ATOM   7417 O OG1 . THR F 2 178 ? -29.93900 72.63900 -37.42200 1.000 159.05519 ?  198 THR B OG1 1 
ATOM   7418 C CG2 . THR F 2 178 ? -29.78900 74.96100 -38.02600 1.000 166.17297 ?  198 THR B CG2 1 
ATOM   7419 N N   . LEU F 2 179 ? -32.59500 75.32000 -40.18500 1.000 164.35888 ?  199 LEU B N   1 
ATOM   7420 C CA  . LEU F 2 179 ? -32.76000 76.31700 -41.23800 1.000 166.83042 ?  199 LEU B CA  1 
ATOM   7421 C C   . LEU F 2 179 ? -31.67200 77.36600 -41.06300 1.000 167.58254 ?  199 LEU B C   1 
ATOM   7422 O O   . LEU F 2 179 ? -31.74000 78.18700 -40.14500 1.000 169.04424 ?  199 LEU B O   1 
ATOM   7423 C CB  . LEU F 2 179 ? -34.13100 76.98000 -41.12600 1.000 169.55797 ?  199 LEU B CB  1 
ATOM   7424 C CG  . LEU F 2 179 ? -34.34400 78.25100 -41.95500 1.000 172.60413 ?  199 LEU B CG  1 
ATOM   7425 C CD1 . LEU F 2 179 ? -34.02500 78.01400 -43.41500 1.000 173.47603 ?  199 LEU B CD1 1 
ATOM   7426 C CD2 . LEU F 2 179 ? -35.73700 78.86100 -41.77200 1.000 176.19235 ?  199 LEU B CD2 1 
ATOM   7427 N N   . THR F 2 180 ? -30.68100 77.36400 -41.93900 1.000 169.21081 ?  200 THR B N   1 
ATOM   7428 C CA  . THR F 2 180 ? -29.55300 78.27200 -41.80700 1.000 170.99402 ?  200 THR B CA  1 
ATOM   7429 C C   . THR F 2 180 ? -29.53000 79.24900 -42.97500 1.000 172.23209 ?  200 THR B C   1 
ATOM   7430 O O   . THR F 2 180 ? -29.77200 78.86900 -44.12400 1.000 170.61688 ?  200 THR B O   1 
ATOM   7431 C CB  . THR F 2 180 ? -28.24400 77.49400 -41.70700 1.000 168.91892 ?  200 THR B CB  1 
ATOM   7432 O OG1 . THR F 2 180 ? -28.26200 76.71300 -40.50500 1.000 168.47216 ?  200 THR B OG1 1 
ATOM   7433 C CG2 . THR F 2 180 ? -27.06500 78.44400 -41.65000 1.000 172.31897 ?  200 THR B CG2 1 
ATOM   7434 N N   . LEU F 2 181 ? -29.29000 80.51800 -42.65700 1.000 174.57985 ?  201 LEU B N   1 
ATOM   7435 C CA  . LEU F 2 181 ? -29.29000 81.60800 -43.62400 1.000 176.68197 ?  201 LEU B CA  1 
ATOM   7436 C C   . LEU F 2 181 ? -28.47600 82.75300 -43.02800 1.000 180.78707 ?  201 LEU B C   1 
ATOM   7437 O O   . LEU F 2 181 ? -27.88800 82.61300 -41.95700 1.000 182.10135 ?  201 LEU B O   1 
ATOM   7438 C CB  . LEU F 2 181 ? -30.73000 81.97200 -44.00900 1.000 177.64267 ?  201 LEU B CB  1 
ATOM   7439 C CG  . LEU F 2 181 ? -31.75800 82.21600 -42.89600 1.000 178.53261 ?  201 LEU B CG  1 
ATOM   7440 C CD1 . LEU F 2 181 ? -31.91100 83.67500 -42.50700 1.000 181.83246 ?  201 LEU B CD1 1 
ATOM   7441 C CD2 . LEU F 2 181 ? -33.10400 81.61500 -43.27500 1.000 178.40308 ?  201 LEU B CD2 1 
ATOM   7442 N N   . SER F 2 182 ? -28.35300 83.84900 -43.77300 1.000 178.93329 ?  202 SER B N   1 
ATOM   7443 C CA  . SER F 2 182 ? -27.64800 85.01800 -43.25900 1.000 183.66254 ?  202 SER B CA  1 
ATOM   7444 C C   . SER F 2 182 ? -28.58600 85.87800 -42.41100 1.000 186.02404 ?  202 SER B C   1 
ATOM   7445 O O   . SER F 2 182 ? -29.81000 85.79600 -42.52400 1.000 184.08900 ?  202 SER B O   1 
ATOM   7446 C CB  . SER F 2 182 ? -27.04900 85.84200 -44.39900 1.000 185.98804 ?  202 SER B CB  1 
ATOM   7447 O OG  . SER F 2 182 ? -27.99000 86.76300 -44.91400 1.000 187.70929 ?  202 SER B OG  1 
ATOM   7448 N N   . LYS F 2 183 ? -27.99700 86.71700 -41.55200 1.000 180.02680 ?  203 LYS B N   1 
ATOM   7449 C CA  . LYS F 2 183 ? -28.80300 87.56200 -40.67300 1.000 181.73431 ?  203 LYS B CA  1 
ATOM   7450 C C   . LYS F 2 183 ? -29.74200 88.49100 -41.44100 1.000 182.38256 ?  203 LYS B C   1 
ATOM   7451 O O   . LYS F 2 183 ? -30.79500 88.87700 -40.90800 1.000 182.12703 ?  203 LYS B O   1 
ATOM   7452 C CB  . LYS F 2 183 ? -27.88600 88.39100 -39.76800 1.000 186.73791 ?  203 LYS B CB  1 
ATOM   7453 N N   . ALA F 2 184 ? -29.42400 88.80000 -42.69900 1.000 185.32779 ?  204 ALA B N   1 
ATOM   7454 C CA  . ALA F 2 184 ? -30.29500 89.65400 -43.49800 1.000 188.12769 ?  204 ALA B CA  1 
ATOM   7455 C C   . ALA F 2 184 ? -31.64800 88.99900 -43.73700 1.000 185.38306 ?  204 ALA B C   1 
ATOM   7456 O O   . ALA F 2 184 ? -32.69700 89.57800 -43.43500 1.000 189.07193 ?  204 ALA B O   1 
ATOM   7457 C CB  . ALA F 2 184 ? -29.61800 89.97600 -44.82800 1.000 194.49228 ?  204 ALA B CB  1 
ATOM   7458 N N   . ASP F 2 185 ? -31.64100 87.77000 -44.24500 1.000 195.52008 ?  205 ASP B N   1 
ATOM   7459 C CA  . ASP F 2 185 ? -32.87800 87.05900 -44.52200 1.000 194.04795 ?  205 ASP B CA  1 
ATOM   7460 C C   . ASP F 2 185 ? -33.64300 86.70500 -43.25600 1.000 192.33333 ?  205 ASP B C   1 
ATOM   7461 O O   . ASP F 2 185 ? -34.81700 86.33000 -43.35000 1.000 192.66582 ?  205 ASP B O   1 
ATOM   7462 C CB  . ASP F 2 185 ? -32.56800 85.80100 -45.32500 1.000 191.28490 ?  205 ASP B CB  1 
ATOM   7463 C CG  . ASP F 2 185 ? -31.50600 86.03900 -46.37600 1.000 192.00526 ?  205 ASP B CG  1 
ATOM   7464 O OD1 . ASP F 2 185 ? -31.85100 86.50900 -47.48000 1.000 194.67244 ?  205 ASP B OD1 1 
ATOM   7465 O OD2 . ASP F 2 185 ? -30.32000 85.76900 -46.08800 1.000 190.51591 -1 205 ASP B OD2 1 
ATOM   7466 N N   . TYR F 2 186 ? -33.01100 86.80100 -42.08500 1.000 188.26934 ?  206 TYR B N   1 
ATOM   7467 C CA  . TYR F 2 186 ? -33.76500 86.65500 -40.84800 1.000 187.05160 ?  206 TYR B CA  1 
ATOM   7468 C C   . TYR F 2 186 ? -34.46700 87.94900 -40.45500 1.000 190.01859 ?  206 TYR B C   1 
ATOM   7469 O O   . TYR F 2 186 ? -35.62100 87.91600 -40.01400 1.000 189.88174 ?  206 TYR B O   1 
ATOM   7470 C CB  . TYR F 2 186 ? -32.86800 86.18400 -39.70700 1.000 185.63132 ?  206 TYR B CB  1 
ATOM   7471 C CG  . TYR F 2 186 ? -33.66200 85.88600 -38.46000 1.000 183.79108 ?  206 TYR B CG  1 
ATOM   7472 C CD1 . TYR F 2 186 ? -34.60200 84.86900 -38.43900 1.000 180.98648 ?  206 TYR B CD1 1 
ATOM   7473 C CD2 . TYR F 2 186 ? -33.49600 86.64700 -37.31200 1.000 185.27863 ?  206 TYR B CD2 1 
ATOM   7474 C CE1 . TYR F 2 186 ? -35.34100 84.60500 -37.30400 1.000 179.35470 ?  206 TYR B CE1 1 
ATOM   7475 C CE2 . TYR F 2 186 ? -34.22800 86.39100 -36.17100 1.000 183.36944 ?  206 TYR B CE2 1 
ATOM   7476 C CZ  . TYR F 2 186 ? -35.14900 85.36900 -36.17000 1.000 180.23907 ?  206 TYR B CZ  1 
ATOM   7477 O OH  . TYR F 2 186 ? -35.87800 85.11900 -35.02900 1.000 178.59667 ?  206 TYR B OH  1 
ATOM   7478 N N   . GLU F 2 187 ? -33.80500 89.09800 -40.59900 1.000 190.62839 ?  207 GLU B N   1 
ATOM   7479 C CA  . GLU F 2 187 ? -34.52900 90.33100 -40.30300 1.000 193.62223 ?  207 GLU B CA  1 
ATOM   7480 C C   . GLU F 2 187 ? -35.46000 90.78400 -41.42500 1.000 196.42295 ?  207 GLU B C   1 
ATOM   7481 O O   . GLU F 2 187 ? -36.22600 91.73200 -41.21700 1.000 200.89921 ?  207 GLU B O   1 
ATOM   7482 C CB  . GLU F 2 187 ? -33.56400 91.45800 -39.93100 1.000 196.81431 ?  207 GLU B CB  1 
ATOM   7483 C CG  . GLU F 2 187 ? -32.42400 91.04000 -39.01600 1.000 196.17634 ?  207 GLU B CG  1 
ATOM   7484 C CD  . GLU F 2 187 ? -32.91000 90.26300 -37.79900 1.000 192.99720 ?  207 GLU B CD  1 
ATOM   7485 O OE1 . GLU F 2 187 ? -33.93500 90.66100 -37.20100 1.000 192.67739 ?  207 GLU B OE1 1 
ATOM   7486 O OE2 . GLU F 2 187 ? -32.25600 89.26800 -37.42600 1.000 191.26611 -1 207 GLU B OE2 1 
ATOM   7487 N N   . LYS F 2 188 ? -35.40400 90.16500 -42.60100 1.000 197.15591 ?  208 LYS B N   1 
ATOM   7488 C CA  . LYS F 2 188 ? -36.31000 90.51200 -43.69400 1.000 196.94839 ?  208 LYS B CA  1 
ATOM   7489 C C   . LYS F 2 188 ? -37.60300 89.70000 -43.71000 1.000 195.18170 ?  208 LYS B C   1 
ATOM   7490 O O   . LYS F 2 188 ? -38.47000 89.97400 -44.54700 1.000 196.24585 ?  208 LYS B O   1 
ATOM   7491 C CB  . LYS F 2 188 ? -35.59300 90.35500 -45.03900 1.000 196.19850 ?  208 LYS B CB  1 
ATOM   7492 N N   . HIS F 2 189 ? -37.76500 88.72300 -42.81600 1.000 192.03955 ?  209 HIS B N   1 
ATOM   7493 C CA  . HIS F 2 189 ? -38.92300 87.83400 -42.83700 1.000 191.20705 ?  209 HIS B CA  1 
ATOM   7494 C C   . HIS F 2 189 ? -39.45100 87.65000 -41.42000 1.000 191.43940 ?  209 HIS B C   1 
ATOM   7495 O O   . HIS F 2 189 ? -38.70500 87.76700 -40.44700 1.000 191.18815 ?  209 HIS B O   1 
ATOM   7496 C CB  . HIS F 2 189 ? -38.55600 86.47300 -43.43100 1.000 188.74763 ?  209 HIS B CB  1 
ATOM   7497 C CG  . HIS F 2 189 ? -38.10100 86.53300 -44.85500 1.000 188.44154 ?  209 HIS B CG  1 
ATOM   7498 N ND1 . HIS F 2 189 ? -37.04000 85.79100 -45.32800 1.000 186.05456 ?  209 HIS B ND1 1 
ATOM   7499 C CD2 . HIS F 2 189 ? -38.56900 87.23600 -45.91300 1.000 190.34540 ?  209 HIS B CD2 1 
ATOM   7500 C CE1 . HIS F 2 189 ? -36.86700 86.04200 -46.61300 1.000 186.20968 ?  209 HIS B CE1 1 
ATOM   7501 N NE2 . HIS F 2 189 ? -37.78300 86.91400 -46.99300 1.000 188.85948 ?  209 HIS B NE2 1 
ATOM   7502 N N   . LYS F 2 190 ? -40.74100 87.31900 -41.30600 1.000 186.95487 ?  210 LYS B N   1 
ATOM   7503 C CA  . LYS F 2 190 ? -41.38700 87.18800 -40.00300 1.000 187.51005 ?  210 LYS B CA  1 
ATOM   7504 C C   . LYS F 2 190 ? -41.77000 85.75700 -39.63800 1.000 186.24847 ?  210 LYS B C   1 
ATOM   7505 O O   . LYS F 2 190 ? -41.34500 85.25800 -38.59300 1.000 184.51069 ?  210 LYS B O   1 
ATOM   7506 C CB  . LYS F 2 190 ? -42.63000 88.08700 -39.95700 1.000 190.90611 ?  210 LYS B CB  1 
ATOM   7507 N N   . VAL F 2 191 ? -42.56300 85.07500 -40.45800 1.000 185.76248 ?  211 VAL B N   1 
ATOM   7508 C CA  . VAL F 2 191 ? -43.05400 83.74900 -40.09400 1.000 184.96690 ?  211 VAL B CA  1 
ATOM   7509 C C   . VAL F 2 191 ? -41.99000 82.70300 -40.39700 1.000 181.86664 ?  211 VAL B C   1 
ATOM   7510 O O   . VAL F 2 191 ? -41.52900 82.58000 -41.53600 1.000 181.49549 ?  211 VAL B O   1 
ATOM   7511 C CB  . VAL F 2 191 ? -44.36600 83.41800 -40.81800 1.000 188.75246 ?  211 VAL B CB  1 
ATOM   7512 C CG1 . VAL F 2 191 ? -44.81900 82.01400 -40.44100 1.000 189.76503 ?  211 VAL B CG1 1 
ATOM   7513 C CG2 . VAL F 2 191 ? -45.43500 84.43700 -40.46700 1.000 191.76353 ?  211 VAL B CG2 1 
ATOM   7514 N N   . TYR F 2 192 ? -41.61000 81.94100 -39.37600 1.000 184.31658 ?  212 TYR B N   1 
ATOM   7515 C CA  . TYR F 2 192 ? -40.69800 80.81000 -39.51800 1.000 181.76439 ?  212 TYR B CA  1 
ATOM   7516 C C   . TYR F 2 192 ? -41.43100 79.59100 -38.98200 1.000 182.80253 ?  212 TYR B C   1 
ATOM   7517 O O   . TYR F 2 192 ? -41.56900 79.43300 -37.76500 1.000 181.73715 ?  212 TYR B O   1 
ATOM   7518 C CB  . TYR F 2 192 ? -39.39100 81.03200 -38.77300 1.000 178.74185 ?  212 TYR B CB  1 
ATOM   7519 C CG  . TYR F 2 192 ? -38.44400 81.97700 -39.45400 1.000 178.54756 ?  212 TYR B CG  1 
ATOM   7520 C CD1 . TYR F 2 192 ? -38.69900 83.33500 -39.49600 1.000 180.31388 ?  212 TYR B CD1 1 
ATOM   7521 C CD2 . TYR F 2 192 ? -37.30200 81.50300 -40.08000 1.000 177.06275 ?  212 TYR B CD2 1 
ATOM   7522 C CE1 . TYR F 2 192 ? -37.83500 84.19800 -40.12500 1.000 180.71711 ?  212 TYR B CE1 1 
ATOM   7523 C CE2 . TYR F 2 192 ? -36.43000 82.35700 -40.71700 1.000 177.51075 ?  212 TYR B CE2 1 
ATOM   7524 C CZ  . TYR F 2 192 ? -36.70300 83.70700 -40.73700 1.000 179.40264 ?  212 TYR B CZ  1 
ATOM   7525 O OH  . TYR F 2 192 ? -35.84500 84.57200 -41.37000 1.000 180.40358 ?  212 TYR B OH  1 
ATOM   7526 N N   . ALA F 2 193 ? -41.93100 78.76900 -39.90000 1.000 185.32454 ?  213 ALA B N   1 
ATOM   7527 C CA  . ALA F 2 193 ? -42.69000 77.56300 -39.61400 1.000 187.94625 ?  213 ALA B CA  1 
ATOM   7528 C C   . ALA F 2 193 ? -41.83400 76.33000 -39.84700 1.000 186.17073 ?  213 ALA B C   1 
ATOM   7529 O O   . ALA F 2 193 ? -40.96800 76.30600 -40.72500 1.000 184.81813 ?  213 ALA B O   1 
ATOM   7530 C CB  . ALA F 2 193 ? -43.94400 77.48500 -40.49100 1.000 194.10207 ?  213 ALA B CB  1 
ATOM   7531 N N   . CYS F 2 194 ? -42.09600 75.29800 -39.05600 1.000 185.40700 ?  214 CYS B N   1 
ATOM   7532 C CA  . CYS F 2 194 ? -41.42500 74.01600 -39.20300 1.000 184.21520 ?  214 CYS B CA  1 
ATOM   7533 C C   . CYS F 2 194 ? -42.50200 72.95200 -39.05900 1.000 189.19570 ?  214 CYS B C   1 
ATOM   7534 O O   . CYS F 2 194 ? -43.04500 72.75200 -37.96600 1.000 188.51918 ?  214 CYS B O   1 
ATOM   7535 C CB  . CYS F 2 194 ? -40.31400 73.84400 -38.17000 1.000 178.01345 ?  214 CYS B CB  1 
ATOM   7536 S SG  . CYS F 2 194 ? -39.75400 72.16100 -37.92300 1.000 176.36513 ?  214 CYS B SG  1 
ATOM   7537 N N   . GLU F 2 195 ? -42.84000 72.31500 -40.17200 1.000 190.12030 ?  215 GLU B N   1 
ATOM   7538 C CA  . GLU F 2 195 ? -43.83300 71.25900 -40.21500 1.000 194.48523 ?  215 GLU B CA  1 
ATOM   7539 C C   . GLU F 2 195 ? -43.10800 69.92200 -40.23300 1.000 194.10665 ?  215 GLU B C   1 
ATOM   7540 O O   . GLU F 2 195 ? -41.99200 69.81000 -40.73300 1.000 191.86506 ?  215 GLU B O   1 
ATOM   7541 C CB  . GLU F 2 195 ? -44.72100 71.40500 -41.45600 1.000 197.12939 ?  215 GLU B CB  1 
ATOM   7542 C CG  . GLU F 2 195 ? -45.84700 70.39000 -41.58900 1.000 195.20601 ?  215 GLU B CG  1 
ATOM   7543 C CD  . GLU F 2 195 ? -46.33700 70.26200 -43.01800 1.000 192.88522 ?  215 GLU B CD  1 
ATOM   7544 O OE1 . GLU F 2 195 ? -46.16300 71.22300 -43.79400 1.000 194.06319 ?  215 GLU B OE1 1 
ATOM   7545 O OE2 . GLU F 2 195 ? -46.90900 69.21200 -43.36700 1.000 189.28659 -1 215 GLU B OE2 1 
ATOM   7546 N N   . VAL F 2 196 ? -43.73000 68.91300 -39.64200 1.000 192.85667 ?  216 VAL B N   1 
ATOM   7547 C CA  . VAL F 2 196 ? -43.22300 67.55600 -39.67300 1.000 190.17699 ?  216 VAL B CA  1 
ATOM   7548 C C   . VAL F 2 196 ? -44.37000 66.67600 -40.13700 1.000 189.33479 ?  216 VAL B C   1 
ATOM   7549 O O   . VAL F 2 196 ? -45.35800 66.50000 -39.40600 1.000 188.69569 ?  216 VAL B O   1 
ATOM   7550 C CB  . VAL F 2 196 ? -42.70000 67.09700 -38.30700 1.000 186.42180 ?  216 VAL B CB  1 
ATOM   7551 C CG1 . VAL F 2 196 ? -42.13900 65.69400 -38.41100 1.000 184.31606 ?  216 VAL B CG1 1 
ATOM   7552 C CG2 . VAL F 2 196 ? -41.65400 68.07600 -37.78100 1.000 181.73512 ?  216 VAL B CG2 1 
ATOM   7553 N N   . THR F 2 197 ? -44.25900 66.16500 -41.36100 1.000 193.64240 ?  217 THR B N   1 
ATOM   7554 C CA  . THR F 2 197 ? -45.15900 65.15300 -41.89700 1.000 191.04727 ?  217 THR B CA  1 
ATOM   7555 C C   . THR F 2 197 ? -44.64500 63.80500 -41.41100 1.000 190.71905 ?  217 THR B C   1 
ATOM   7556 O O   . THR F 2 197 ? -43.62100 63.30500 -41.89000 1.000 190.74171 ?  217 THR B O   1 
ATOM   7557 C CB  . THR F 2 197 ? -45.24500 65.23700 -43.41500 1.000 188.58259 ?  217 THR B CB  1 
ATOM   7558 O OG1 . THR F 2 197 ? -43.92700 65.28600 -43.96800 1.000 189.00633 ?  217 THR B OG1 1 
ATOM   7559 C CG2 . THR F 2 197 ? -46.00600 66.48000 -43.82700 1.000 188.75871 ?  217 THR B CG2 1 
ATOM   7560 N N   . GLN F 2 198 ? -45.31500 63.25700 -40.40000 1.000 190.32058 ?  218 GLN B N   1 
ATOM   7561 C CA  . GLN F 2 198 ? -45.01200 61.96600 -39.79400 1.000 190.75411 ?  218 GLN B CA  1 
ATOM   7562 C C   . GLN F 2 198 ? -46.25000 61.09900 -39.94500 1.000 190.63797 ?  218 GLN B C   1 
ATOM   7563 O O   . GLN F 2 198 ? -47.14100 61.14500 -39.09500 1.000 190.89521 ?  218 GLN B O   1 
ATOM   7564 C CB  . GLN F 2 198 ? -44.67500 62.14300 -38.31900 1.000 190.55094 ?  218 GLN B CB  1 
ATOM   7565 C CG  . GLN F 2 198 ? -44.26200 60.86300 -37.61900 1.000 190.71164 ?  218 GLN B CG  1 
ATOM   7566 C CD  . GLN F 2 198 ? -44.24100 61.01300 -36.10700 1.000 188.23728 ?  218 GLN B CD  1 
ATOM   7567 O OE1 . GLN F 2 198 ? -45.22400 61.44200 -35.50200 1.000 188.55849 ?  218 GLN B OE1 1 
ATOM   7568 N NE2 . GLN F 2 198 ? -43.12800 60.63400 -35.48800 1.000 185.20213 ?  218 GLN B NE2 1 
ATOM   7569 N N   . GLY F 2 199 ? -46.27600 60.27800 -40.98600 1.000 192.52856 ?  219 GLY B N   1 
ATOM   7570 C CA  . GLY F 2 199 ? -47.41700 59.40500 -41.20700 1.000 193.18040 ?  219 GLY B CA  1 
ATOM   7571 C C   . GLY F 2 199 ? -48.71600 60.18600 -41.23500 1.000 194.40526 ?  219 GLY B C   1 
ATOM   7572 O O   . GLY F 2 199 ? -48.90700 61.10600 -42.03900 1.000 198.08979 ?  219 GLY B O   1 
ATOM   7573 N N   . THR F 2 200 ? -49.62500 59.81400 -40.33300 1.000 193.38775 ?  220 THR B N   1 
ATOM   7574 C CA  . THR F 2 200 ? -50.91700 60.46600 -40.16000 1.000 194.34136 ?  220 THR B CA  1 
ATOM   7575 C C   . THR F 2 200 ? -50.86800 61.63900 -39.17600 1.000 191.46452 ?  220 THR B C   1 
ATOM   7576 O O   . THR F 2 200 ? -51.87700 61.92900 -38.51900 1.000 190.28167 ?  220 THR B O   1 
ATOM   7577 C CB  . THR F 2 200 ? -51.95900 59.43000 -39.72600 1.000 193.43970 ?  220 THR B CB  1 
ATOM   7578 O OG1 . THR F 2 200 ? -51.62900 58.89900 -38.43600 1.000 188.81751 ?  220 THR B OG1 1 
ATOM   7579 C CG2 . THR F 2 200 ? -52.04700 58.29800 -40.74700 1.000 197.29960 ?  220 THR B CG2 1 
ATOM   7580 N N   . THR F 2 201 ? -49.72700 62.31800 -39.05000 1.000 192.15329 ?  221 THR B N   1 
ATOM   7581 C CA  . THR F 2 201 ? -49.58000 63.41800 -38.09900 1.000 189.35482 ?  221 THR B CA  1 
ATOM   7582 C C   . THR F 2 201 ? -48.71900 64.52000 -38.71500 1.000 193.64205 ?  221 THR B C   1 
ATOM   7583 O O   . THR F 2 201 ? -47.51600 64.33500 -38.91900 1.000 193.60598 ?  221 THR B O   1 
ATOM   7584 C CB  . THR F 2 201 ? -48.96500 62.88800 -36.79800 1.000 181.64980 ?  221 THR B CB  1 
ATOM   7585 O OG1 . THR F 2 201 ? -49.98400 62.26100 -36.00500 1.000 178.94673 ?  221 THR B OG1 1 
ATOM   7586 C CG2 . THR F 2 201 ? -48.33900 64.00000 -35.98500 1.000 178.70793 ?  221 THR B CG2 1 
ATOM   7587 N N   . SER F 2 202 ? -49.34400 65.63700 -39.08700 1.000 184.99165 ?  222 SER B N   1 
ATOM   7588 C CA  . SER F 2 202 ? -48.63700 66.75100 -39.72500 1.000 190.31257 ?  222 SER B CA  1 
ATOM   7589 C C   . SER F 2 202 ? -48.39900 67.90100 -38.74200 1.000 188.28785 ?  222 SER B C   1 
ATOM   7590 O O   . SER F 2 202 ? -48.93300 69.00000 -38.89200 1.000 191.99414 ?  222 SER B O   1 
ATOM   7591 C CB  . SER F 2 202 ? -49.40000 67.22000 -40.95900 1.000 196.32782 ?  222 SER B CB  1 
ATOM   7592 O OG  . SER F 2 202 ? -48.93900 66.54600 -42.11700 1.000 197.88013 ?  222 SER B OG  1 
ATOM   7593 N N   . VAL F 2 203 ? -47.57200 67.64600 -37.72300 1.000 189.86894 ?  225 VAL B N   1 
ATOM   7594 C CA  . VAL F 2 203 ? -47.41000 68.65700 -36.67200 1.000 186.30993 ?  225 VAL B CA  1 
ATOM   7595 C C   . VAL F 2 203 ? -46.63000 69.85400 -37.20600 1.000 191.48591 ?  225 VAL B C   1 
ATOM   7596 O O   . VAL F 2 203 ? -45.89400 69.74900 -38.18400 1.000 196.75568 ?  225 VAL B O   1 
ATOM   7597 C CB  . VAL F 2 203 ? -46.73100 68.07100 -35.42100 1.000 177.31633 ?  225 VAL B CB  1 
ATOM   7598 C CG1 . VAL F 2 203 ? -47.68300 67.15500 -34.68600 1.000 172.18063 ?  225 VAL B CG1 1 
ATOM   7599 C CG2 . VAL F 2 203 ? -45.47700 67.31700 -35.80600 1.000 176.85525 ?  225 VAL B CG2 1 
ATOM   7600 N N   . THR F 2 204 ? -46.83000 71.02300 -36.59800 1.000 179.89870 ?  226 THR B N   1 
ATOM   7601 C CA  . THR F 2 204 ? -46.09600 72.20400 -37.03700 1.000 183.10598 ?  226 THR B CA  1 
ATOM   7602 C C   . THR F 2 204 ? -45.92300 73.17200 -35.87900 1.000 176.48291 ?  226 THR B C   1 
ATOM   7603 O O   . THR F 2 204 ? -46.83200 73.34800 -35.06400 1.000 173.22385 ?  226 THR B O   1 
ATOM   7604 C CB  . THR F 2 204 ? -46.79100 72.92500 -38.20300 1.000 191.74832 ?  226 THR B CB  1 
ATOM   7605 O OG1 . THR F 2 204 ? -47.17800 71.97500 -39.20300 1.000 197.43181 ?  226 THR B OG1 1 
ATOM   7606 C CG2 . THR F 2 204 ? -45.85900 73.96600 -38.82400 1.000 194.58283 ?  226 THR B CG2 1 
ATOM   7607 N N   . LYS F 2 205 ? -44.76100 73.81700 -35.82600 1.000 179.03728 ?  227 LYS B N   1 
ATOM   7608 C CA  . LYS F 2 205 ? -44.53500 74.86400 -34.84200 1.000 174.23407 ?  227 LYS B CA  1 
ATOM   7609 C C   . LYS F 2 205 ? -43.78600 76.00000 -35.52000 1.000 177.96278 ?  227 LYS B C   1 
ATOM   7610 O O   . LYS F 2 205 ? -42.94400 75.76000 -36.38800 1.000 181.53820 ?  227 LYS B O   1 
ATOM   7611 C CB  . LYS F 2 205 ? -43.77000 74.33800 -33.62600 1.000 167.00257 ?  227 LYS B CB  1 
ATOM   7612 C CG  . LYS F 2 205 ? -43.66900 75.32900 -32.48000 1.000 163.15879 ?  227 LYS B CG  1 
ATOM   7613 C CD  . LYS F 2 205 ? -42.72700 74.81700 -31.41400 1.000 157.81323 ?  227 LYS B CD  1 
ATOM   7614 C CE  . LYS F 2 205 ? -42.68200 75.73800 -30.21100 1.000 155.17751 ?  227 LYS B CE  1 
ATOM   7615 N NZ  . LYS F 2 205 ? -43.97200 75.66300 -29.46600 1.000 152.09036 ?  227 LYS B NZ  1 
ATOM   7616 N N   . SER F 2 206 ? -44.08700 77.23200 -35.12300 1.000 169.68912 ?  228 SER B N   1 
ATOM   7617 C CA  . SER F 2 206 ? -43.56400 78.38400 -35.83300 1.000 173.61108 ?  228 SER B CA  1 
ATOM   7618 C C   . SER F 2 206 ? -43.30900 79.51900 -34.85900 1.000 171.13413 ?  228 SER B C   1 
ATOM   7619 O O   . SER F 2 206 ? -43.57700 79.41900 -33.65900 1.000 166.65314 ?  228 SER B O   1 
ATOM   7620 C CB  . SER F 2 206 ? -44.53300 78.82300 -36.93400 1.000 178.99885 ?  228 SER B CB  1 
ATOM   7621 O OG  . SER F 2 206 ? -44.11000 80.04300 -37.51400 1.000 181.61348 ?  228 SER B OG  1 
ATOM   7622 N N   . PHE F 2 207 ? -42.77300 80.60600 -35.39100 1.000 170.92264 ?  229 PHE B N   1 
ATOM   7623 C CA  . PHE F 2 207 ? -42.60200 81.81500 -34.59800 1.000 170.57719 ?  229 PHE B CA  1 
ATOM   7624 C C   . PHE F 2 207 ? -42.64100 83.01400 -35.53200 1.000 174.91715 ?  229 PHE B C   1 
ATOM   7625 O O   . PHE F 2 207 ? -42.53900 82.88800 -36.75900 1.000 178.08094 ?  229 PHE B O   1 
ATOM   7626 C CB  . PHE F 2 207 ? -41.29900 81.81200 -33.77600 1.000 170.73479 ?  229 PHE B CB  1 
ATOM   7627 C CG  . PHE F 2 207 ? -40.05200 82.05400 -34.58500 1.000 176.17525 ?  229 PHE B CG  1 
ATOM   7628 C CD1 . PHE F 2 207 ? -39.62300 83.34300 -34.85900 1.000 180.68966 ?  229 PHE B CD1 1 
ATOM   7629 C CD2 . PHE F 2 207 ? -39.29200 80.99600 -35.04100 1.000 177.05531 ?  229 PHE B CD2 1 
ATOM   7630 C CE1 . PHE F 2 207 ? -38.48600 83.56300 -35.59400 1.000 185.92684 ?  229 PHE B CE1 1 
ATOM   7631 C CE2 . PHE F 2 207 ? -38.13800 81.21700 -35.76400 1.000 182.41159 ?  229 PHE B CE2 1 
ATOM   7632 C CZ  . PHE F 2 207 ? -37.74100 82.50000 -36.04700 1.000 186.82644 ?  229 PHE B CZ  1 
ATOM   7633 N N   . ASN F 2 208 ? -42.76100 84.18700 -34.93400 1.000 180.01518 ?  230 ASN B N   1 
ATOM   7634 C CA  . ASN F 2 208 ? -42.77000 85.43800 -35.66600 1.000 183.78527 ?  230 ASN B CA  1 
ATOM   7635 C C   . ASN F 2 208 ? -41.50300 86.17800 -35.27500 1.000 186.87582 ?  230 ASN B C   1 
ATOM   7636 O O   . ASN F 2 208 ? -41.25000 86.38500 -34.08500 1.000 186.23266 ?  230 ASN B O   1 
ATOM   7637 C CB  . ASN F 2 208 ? -44.00300 86.26400 -35.34700 1.000 183.24225 ?  230 ASN B CB  1 
ATOM   7638 C CG  . ASN F 2 208 ? -45.28400 85.53800 -35.63800 1.000 182.08816 ?  230 ASN B CG  1 
ATOM   7639 O OD1 . ASN F 2 208 ? -45.37800 84.74400 -36.57400 1.000 183.59729 ?  230 ASN B OD1 1 
ATOM   7640 N ND2 . ASN F 2 208 ? -46.29900 85.82100 -34.83700 1.000 180.47549 ?  230 ASN B ND2 1 
ATOM   7641 N N   . ARG F 2 209 ? -40.66900 86.49200 -36.26900 1.000 176.68954 ?  231 ARG B N   1 
ATOM   7642 C CA  . ARG F 2 209 ? -39.37100 87.14700 -35.96400 1.000 181.75314 ?  231 ARG B CA  1 
ATOM   7643 C C   . ARG F 2 209 ? -39.64000 88.28000 -34.97500 1.000 185.50142 ?  231 ARG B C   1 
ATOM   7644 O O   . ARG F 2 209 ? -38.74500 88.59800 -34.17400 1.000 187.52508 ?  231 ARG B O   1 
ATOM   7645 C CB  . ARG F 2 209 ? -38.70800 87.63200 -37.25500 1.000 186.70205 ?  231 ARG B CB  1 
ATOM   7646 C CG  . ARG F 2 209 ? -38.70400 89.14200 -37.44100 1.000 192.30306 ?  231 ARG B CG  1 
ATOM   7647 C CD  . ARG F 2 209 ? -37.30800 89.65700 -37.72100 1.000 197.52592 ?  231 ARG B CD  1 
ATOM   7648 N NE  . ARG F 2 209 ? -37.34100 90.90300 -38.46900 1.000 205.16889 ?  231 ARG B NE  1 
ATOM   7649 C CZ  . ARG F 2 209 ? -36.80700 92.04300 -38.04700 1.000 212.74205 ?  231 ARG B CZ  1 
ATOM   7650 N NH1 . ARG F 2 209 ? -36.26800 92.11300 -36.84300 1.000 212.76821 ?  231 ARG B NH1 1 
ATOM   7651 N NH2 . ARG F 2 209 ? -36.80600 93.10500 -38.83400 1.000 220.93859 ?  231 ARG B NH2 1 
ATOM   7652 N N   . GLY F 2 210 ? -40.84600 88.84500 -35.02600 1.000 195.51619 ?  232 GLY B N   1 
ATOM   7653 C CA  . GLY F 2 210 ? -41.20700 89.93700 -34.10600 1.000 196.57024 ?  232 GLY B CA  1 
ATOM   7654 C C   . GLY F 2 210 ? -41.33200 89.42200 -32.68700 1.000 193.32609 ?  232 GLY B C   1 
ATOM   7655 O O   . GLY F 2 210 ? -40.68700 90.00100 -31.79600 1.000 196.42972 ?  232 GLY B O   1 
ATOM   7656 N N   . GLU F 2 211 ? -42.11700 88.35900 -32.49000 1.000 198.29716 ?  233 GLU B N   1 
ATOM   7657 C CA  . GLU F 2 211 ? -42.32400 87.79200 -31.13200 1.000 194.72338 ?  233 GLU B CA  1 
ATOM   7658 C C   . GLU F 2 211 ? -41.01200 87.90900 -30.35800 1.000 199.21691 ?  233 GLU B C   1 
ATOM   7659 O O   . GLU F 2 211 ? -41.05400 88.35000 -29.19400 1.000 199.84720 ?  233 GLU B O   1 
ATOM   7660 C CB  . GLU F 2 211 ? -42.77300 86.33400 -31.22700 1.000 188.62043 ?  233 GLU B CB  1 
ATOM   7661 N N   . CYS F 2 212 ? -39.90100 87.52200 -30.98700 1.000 194.97095 ?  234 CYS B N   1 
ATOM   7662 C CA  . CYS F 2 212 ? -38.57200 87.65300 -30.33900 1.000 201.06762 ?  234 CYS B CA  1 
ATOM   7663 C C   . CYS F 2 212 ? -38.51300 88.97700 -29.57100 1.000 205.97942 ?  234 CYS B C   1 
ATOM   7664 O O   . CYS F 2 212 ? -38.11700 88.93100 -28.39000 1.000 206.69627 ?  234 CYS B O   1 
ATOM   7665 C CB  . CYS F 2 212 ? -37.47000 87.61600 -31.38800 1.000 207.02771 ?  234 CYS B CB  1 
ATOM   7666 S SG  . CYS F 2 212 ? -37.69500 86.29900 -32.61200 1.000 203.66286 ?  234 CYS B SG  1 
HETATM 7667 C C1  . NAG G 4 .   ? 14.02700  19.94600 -43.57500 1.000 170.97247 ?  1   NAG G C1  1 
HETATM 7668 C C2  . NAG G 4 .   ? 13.05600  19.91900 -44.77400 1.000 170.97247 ?  1   NAG G C2  1 
HETATM 7669 C C3  . NAG G 4 .   ? 13.82100  19.72100 -46.08000 1.000 170.97247 ?  1   NAG G C3  1 
HETATM 7670 C C4  . NAG G 4 .   ? 14.59100  18.40500 -46.07700 1.000 170.97247 ?  1   NAG G C4  1 
HETATM 7671 C C5  . NAG G 4 .   ? 14.96200  18.01000 -44.65000 1.000 170.97247 ?  1   NAG G C5  1 
HETATM 7672 C C6  . NAG G 4 .   ? 16.19500  17.14300 -44.57100 1.000 170.97247 ?  1   NAG G C6  1 
HETATM 7673 C C7  . NAG G 4 .   ? 10.84500  19.06400 -44.06800 1.000 170.97247 ?  1   NAG G C7  1 
HETATM 7674 C C8  . NAG G 4 .   ? 10.56500  20.43600 -43.54800 1.000 170.97247 ?  1   NAG G C8  1 
HETATM 7675 N N2  . NAG G 4 .   ? 12.04600  18.88000 -44.62600 1.000 170.97247 ?  1   NAG G N2  1 
HETATM 7676 O O3  . NAG G 4 .   ? 14.72400  20.80900 -46.25100 1.000 170.97247 ?  1   NAG G O3  1 
HETATM 7677 O O4  . NAG G 4 .   ? 13.76400  17.38300 -46.62600 1.000 170.97247 ?  1   NAG G O4  1 
HETATM 7678 O O5  . NAG G 4 .   ? 15.23500  19.20200 -43.90200 1.000 170.97247 ?  1   NAG G O5  1 
HETATM 7679 O O6  . NAG G 4 .   ? 17.33300  17.81800 -45.08800 1.000 170.97247 ?  1   NAG G O6  1 
HETATM 7680 O O7  . NAG G 4 .   ? 10.02200  18.15400 -43.97900 1.000 170.97247 ?  1   NAG G O7  1 
HETATM 7681 C C1  . NAG G 4 .   ? 14.19000  16.98400 -47.95100 1.000 170.55724 ?  2   NAG G C1  1 
HETATM 7682 C C2  . NAG G 4 .   ? 14.78000  15.58600 -47.85300 1.000 170.55724 ?  2   NAG G C2  1 
HETATM 7683 C C3  . NAG G 4 .   ? 13.68800  14.57000 -47.55500 1.000 170.55724 ?  2   NAG G C3  1 
HETATM 7684 C C4  . NAG G 4 .   ? 12.60000  14.59900 -48.62100 1.000 170.55724 ?  2   NAG G C4  1 
HETATM 7685 C C5  . NAG G 4 .   ? 12.07900  16.01000 -48.90800 1.000 170.55724 ?  2   NAG G C5  1 
HETATM 7686 C C6  . NAG G 4 .   ? 11.03000  16.47400 -47.92100 1.000 170.55724 ?  2   NAG G C6  1 
HETATM 7687 C C7  . NAG G 4 .   ? 16.74900  15.65500 -49.29800 1.000 170.55724 ?  2   NAG G C7  1 
HETATM 7688 C C8  . NAG G 4 .   ? 17.38000  15.19400 -50.58200 1.000 170.55724 ?  2   NAG G C8  1 
HETATM 7689 N N2  . NAG G 4 .   ? 15.50700  15.22300 -49.05900 1.000 170.55724 ?  2   NAG G N2  1 
HETATM 7690 O O3  . NAG G 4 .   ? 13.13800  14.83300 -46.26800 1.000 170.55724 ?  2   NAG G O3  1 
HETATM 7691 O O4  . NAG G 4 .   ? 13.07500  14.01500 -49.82900 1.000 170.55724 ?  2   NAG G O4  1 
HETATM 7692 O O5  . NAG G 4 .   ? 13.11900  17.01000 -48.95200 1.000 170.55724 ?  2   NAG G O5  1 
HETATM 7693 O O6  . NAG G 4 .   ? 9.76300   15.90100 -48.21600 1.000 170.55724 ?  2   NAG G O6  1 
HETATM 7694 O O7  . NAG G 4 .   ? 17.33900  16.38600 -48.51200 1.000 170.55724 ?  2   NAG G O7  1 
HETATM 7695 C C1  . NAG H 5 .   ? 5.40800   21.53700 -3.03000  1.000 173.17149 ?  1   NAG H C1  1 
HETATM 7696 C C2  . NAG H 5 .   ? 6.57800   21.38700 -1.98600  1.000 173.17149 ?  1   NAG H C2  1 
HETATM 7697 C C3  . NAG H 5 .   ? 6.40900   20.22000 -0.95500  1.000 173.17149 ?  1   NAG H C3  1 
HETATM 7698 C C4  . NAG H 5 .   ? 5.44000   19.10900 -1.35600  1.000 173.17149 ?  1   NAG H C4  1 
HETATM 7699 C C5  . NAG H 5 .   ? 4.96400   19.31900 -2.77000  1.000 173.17149 ?  1   NAG H C5  1 
HETATM 7700 C C6  . NAG H 5 .   ? 3.84900   18.39700 -3.19500  1.000 173.17149 ?  1   NAG H C6  1 
HETATM 7701 C C7  . NAG H 5 .   ? 8.64900   22.36700 -2.85600  1.000 173.17149 ?  1   NAG H C7  1 
HETATM 7702 C C8  . NAG H 5 .   ? 8.17900   23.64800 -2.23900  1.000 173.17149 ?  1   NAG H C8  1 
HETATM 7703 N N2  . NAG H 5 .   ? 7.85600   21.30500 -2.67600  1.000 173.17149 ?  1   NAG H N2  1 
HETATM 7704 O O3  . NAG H 5 .   ? 6.02200   20.76600 0.30200   1.000 173.17149 ?  1   NAG H O3  1 
HETATM 7705 O O4  . NAG H 5 .   ? 5.99100   17.81000 -1.14600  1.000 173.17149 ?  1   NAG H O4  1 
HETATM 7706 O O5  . NAG H 5 .   ? 4.43400   20.63600 -2.78300  1.000 173.17149 ?  1   NAG H O5  1 
HETATM 7707 O O6  . NAG H 5 .   ? 4.34700   17.31700 -3.97200  1.000 173.17149 ?  1   NAG H O6  1 
HETATM 7708 O O7  . NAG H 5 .   ? 9.71300   22.29100 -3.46100  1.000 173.17149 ?  1   NAG H O7  1 
HETATM 7709 C C1  . NAG H 5 .   ? 5.09600   17.05500 -0.27400  1.000 188.65640 ?  2   NAG H C1  1 
HETATM 7710 C C2  . NAG H 5 .   ? 5.86600   16.10400 0.67300   1.000 188.65640 ?  2   NAG H C2  1 
HETATM 7711 C C3  . NAG H 5 .   ? 4.94600   15.45200 1.71800   1.000 188.65640 ?  2   NAG H C3  1 
HETATM 7712 C C4  . NAG H 5 .   ? 4.12000   16.50400 2.45300   1.000 188.65640 ?  2   NAG H C4  1 
HETATM 7713 C C5  . NAG H 5 .   ? 3.40400   17.39100 1.43100   1.000 188.65640 ?  2   NAG H C5  1 
HETATM 7714 C C6  . NAG H 5 .   ? 2.67200   18.54900 2.06200   1.000 188.65640 ?  2   NAG H C6  1 
HETATM 7715 C C7  . NAG H 5 .   ? 6.30400   14.09700 -0.81500  1.000 188.65640 ?  2   NAG H C7  1 
HETATM 7716 C C8  . NAG H 5 .   ? 4.83100   13.94600 -1.09900  1.000 188.65640 ?  2   NAG H C8  1 
HETATM 7717 N N2  . NAG H 5 .   ? 6.69200   15.11200 -0.01300  1.000 188.65640 ?  2   NAG H N2  1 
HETATM 7718 O O3  . NAG H 5 .   ? 5.78200   14.70400 2.59500   1.000 188.65640 ?  2   NAG H O3  1 
HETATM 7719 O O4  . NAG H 5 .   ? 3.13000   15.99100 3.34900   1.000 188.65640 ?  2   NAG H O4  1 
HETATM 7720 O O5  . NAG H 5 .   ? 4.32300   17.96100 0.48500   1.000 188.65640 ?  2   NAG H O5  1 
HETATM 7721 O O6  . NAG H 5 .   ? 1.31000   18.54700 1.66400   1.000 188.65640 ?  2   NAG H O6  1 
HETATM 7722 O O7  . NAG H 5 .   ? 7.12600   13.33300 -1.30900  1.000 188.65640 ?  2   NAG H O7  1 
HETATM 7723 C C1  . BMA H 5 .   ? 3.19800   14.67000 3.96200   1.000 202.26297 ?  3   BMA H C1  1 
HETATM 7724 C C2  . BMA H 5 .   ? 4.13700   14.64700 5.18800   1.000 202.26297 ?  3   BMA H C2  1 
HETATM 7725 C C3  . BMA H 5 .   ? 4.19400   13.21100 5.69500   1.000 202.26297 ?  3   BMA H C3  1 
HETATM 7726 C C4  . BMA H 5 .   ? 2.79600   12.63000 5.99100   1.000 202.26297 ?  3   BMA H C4  1 
HETATM 7727 C C5  . BMA H 5 .   ? 1.81200   12.88000 4.83000   1.000 202.26297 ?  3   BMA H C5  1 
HETATM 7728 C C6  . BMA H 5 .   ? 0.35900   12.59800 5.21900   1.000 202.26297 ?  3   BMA H C6  1 
HETATM 7729 O O2  . BMA H 5 .   ? 3.62400   15.44500 6.24900   1.000 202.26297 ?  3   BMA H O2  1 
HETATM 7730 O O3  . BMA H 5 .   ? 5.01500   13.09900 6.84500   1.000 202.26297 ?  3   BMA H O3  1 
HETATM 7731 O O4  . BMA H 5 .   ? 2.91600   11.23700 6.17600   1.000 202.26297 ?  3   BMA H O4  1 
HETATM 7732 O O5  . BMA H 5 .   ? 1.89600   14.25200 4.39200   1.000 202.26297 ?  3   BMA H O5  1 
HETATM 7733 O O6  . BMA H 5 .   ? 0.24000   11.23600 5.63400   1.000 202.26297 ?  3   BMA H O6  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLU A 1   ? 1.53756 1.37128 2.63465 -0.10215 0.37547  0.59993  1   GLU C N   
2    C CA  . GLU A 1   ? 1.57746 1.39010 2.55441 -0.07225 0.35841  0.58502  1   GLU C CA  
3    C C   . GLU A 1   ? 1.58485 1.34819 2.52597 -0.09006 0.30823  0.55837  1   GLU C C   
4    O O   . GLU A 1   ? 1.60609 1.31965 2.53295 -0.09823 0.31145  0.56401  1   GLU C O   
5    C CB  . GLU A 1   ? 1.57122 1.43647 2.53123 -0.05039 0.34391  0.56668  1   GLU C CB  
6    N N   . VAL A 2   ? 1.50297 1.27701 2.42692 -0.09780 0.26103  0.52816  2   VAL C N   
7    C CA  . VAL A 2   ? 1.52235 1.25226 2.39606 -0.11760 0.21699  0.49771  2   VAL C CA  
8    C C   . VAL A 2   ? 1.49994 1.20253 2.45166 -0.15288 0.19420  0.49815  2   VAL C C   
9    O O   . VAL A 2   ? 1.46137 1.18614 2.50689 -0.17063 0.17976  0.50366  2   VAL C O   
10   C CB  . VAL A 2   ? 1.52818 1.26733 2.35440 -0.12383 0.17437  0.47008  2   VAL C CB  
11   C CG1 . VAL A 2   ? 1.56809 1.26043 2.31958 -0.14664 0.14022  0.43555  2   VAL C CG1 
12   C CG2 . VAL A 2   ? 1.54383 1.31850 2.31678 -0.08850 0.19796  0.47127  2   VAL C CG2 
13   N N   . GLN A 3   ? 1.47658 1.13277 2.39939 -0.16133 0.18876  0.48774  3   GLN C N   
14   C CA  . GLN A 3   ? 1.46360 1.08964 2.45615 -0.19320 0.16396  0.48342  3   GLN C CA  
15   C C   . GLN A 3   ? 1.50782 1.09329 2.43555 -0.20757 0.12580  0.44339  3   GLN C C   
16   O O   . GLN A 3   ? 1.55197 1.12499 2.39589 -0.19014 0.13602  0.42473  3   GLN C O   
17   C CB  . GLN A 3   ? 1.45931 1.06880 2.50224 -0.19064 0.20354  0.51390  3   GLN C CB  
18   N N   . LEU A 4   ? 1.52384 1.09107 2.49473 -0.23961 0.08086  0.42506  4   LEU C N   
19   C CA  . LEU A 4   ? 1.57300 1.10073 2.49790 -0.25947 0.04602  0.38531  4   LEU C CA  
20   C C   . LEU A 4   ? 1.55956 1.06051 2.57503 -0.27598 0.03729  0.38976  4   LEU C C   
21   O O   . LEU A 4   ? 1.51472 1.02563 2.63188 -0.28932 0.03033  0.40923  4   LEU C O   
22   C CB  . LEU A 4   ? 1.60243 1.12042 2.47848 -0.28498 -0.00620 0.35552  4   LEU C CB  
23   C CG  . LEU A 4   ? 1.63997 1.16676 2.39954 -0.27672 -0.00059 0.33892  4   LEU C CG  
24   C CD1 . LEU A 4   ? 1.69615 1.19081 2.38246 -0.31064 -0.05246 0.30705  4   LEU C CD1 
25   C CD2 . LEU A 4   ? 1.67639 1.20186 2.37430 -0.25758 0.03547  0.31944  4   LEU C CD2 
26   N N   . VAL A 5   ? 1.54338 1.01219 2.53057 -0.27469 0.03682  0.36757  5   VAL C N   
27   C CA  . VAL A 5   ? 1.53654 0.97332 2.60495 -0.28789 0.02770  0.36975  5   VAL C CA  
28   C C   . VAL A 5   ? 1.58989 0.99950 2.62202 -0.30692 -0.01570 0.31484  5   VAL C C   
29   O O   . VAL A 5   ? 1.64283 1.05003 2.58503 -0.29855 -0.01399 0.27888  5   VAL C O   
30   C CB  . VAL A 5   ? 1.54174 0.95717 2.61904 -0.26400 0.06931  0.39914  5   VAL C CB  
31   C CG1 . VAL A 5   ? 1.54320 0.93006 2.68361 -0.27495 0.05401  0.39372  5   VAL C CG1 
32   C CG2 . VAL A 5   ? 1.50450 0.95607 2.58938 -0.24418 0.11521  0.44501  5   VAL C CG2 
33   N N   . GLU A 6   ? 1.60032 0.99239 2.70604 -0.33297 -0.05320 0.30344  6   GLU C N   
34   C CA  . GLU A 6   ? 1.65504 1.02263 2.72832 -0.35428 -0.09775 0.24874  6   GLU C CA  
35   C C   . GLU A 6   ? 1.65238 0.98930 2.80180 -0.35691 -0.10611 0.23844  6   GLU C C   
36   O O   . GLU A 6   ? 1.62462 0.96578 2.85003 -0.34669 -0.08695 0.27377  6   GLU C O   
37   C CB  . GLU A 6   ? 1.66234 1.02645 2.74669 -0.38174 -0.14819 0.23533  6   GLU C CB  
38   C CG  . GLU A 6   ? 1.64261 1.03239 2.69928 -0.37736 -0.14518 0.26155  6   GLU C CG  
39   C CD  . GLU A 6   ? 1.69270 1.06223 2.69984 -0.40250 -0.20490 0.23544  6   GLU C CD  
40   O OE1 . GLU A 6   ? 1.70733 1.05171 2.76784 -0.42181 -0.25138 0.21553  6   GLU C OE1 
41   O OE2 . GLU A 6   ? 1.72275 1.09569 2.63573 -0.40282 -0.20865 0.23546  6   GLU C OE2 
42   N N   . SER A 7   ? 1.64756 0.96734 2.75280 -0.36530 -0.13183 0.18209  7   SER C N   
43   C CA  . SER A 7   ? 1.65505 0.94426 2.83297 -0.36901 -0.15149 0.16085  7   SER C CA  
44   C C   . SER A 7   ? 1.71241 0.99486 2.83534 -0.38800 -0.18993 0.08714  7   SER C C   
45   O O   . SER A 7   ? 1.76140 1.05815 2.78128 -0.40060 -0.19508 0.05707  7   SER C O   
46   C CB  . SER A 7   ? 1.65458 0.92626 2.84197 -0.33931 -0.11894 0.17756  7   SER C CB  
47   O OG  . SER A 7   ? 1.71064 0.98527 2.81956 -0.32706 -0.12085 0.12091  7   SER C OG  
48   N N   . GLY A 8   ? 1.65784 0.91579 2.84732 -0.39177 -0.21502 0.05694  8   GLY C N   
49   C CA  . GLY A 8   ? 1.69662 0.94941 2.85078 -0.41056 -0.25144 -0.01792 8   GLY C CA  
50   C C   . GLY A 8   ? 1.73168 0.96900 2.93552 -0.43852 -0.30197 -0.03250 8   GLY C C   
51   O O   . GLY A 8   ? 1.77370 1.00260 2.95768 -0.45475 -0.33533 -0.09581 8   GLY C O   
52   N N   . GLY A 9   ? 1.73602 0.98349 2.98989 -0.43642 -0.30500 0.01864  9   GLY C N   
53   C CA  . GLY A 9   ? 1.75915 1.00560 3.04343 -0.45053 -0.35264 0.00250  9   GLY C CA  
54   C C   . GLY A 9   ? 1.79174 1.03372 3.16174 -0.44378 -0.37483 -0.02125 9   GLY C C   
55   O O   . GLY A 9   ? 1.78397 1.02425 3.21235 -0.42506 -0.35103 -0.00585 9   GLY C O   
56   N N   . GLY A 10  ? 1.83806 1.07233 3.20896 -0.45906 -0.42546 -0.06022 11  GLY C N   
57   C CA  . GLY A 10  ? 1.87268 1.10450 3.32565 -0.45277 -0.45214 -0.08769 11  GLY C CA  
58   C C   . GLY A 10  ? 1.93311 1.15122 3.34391 -0.47229 -0.50925 -0.14588 11  GLY C C   
59   O O   . GLY A 10  ? 1.95521 1.16176 3.29267 -0.48939 -0.53455 -0.15042 11  GLY C O   
60   N N   . LEU A 11  ? 1.96750 1.18297 3.42067 -0.46829 -0.53117 -0.18997 12  LEU C N   
61   C CA  . LEU A 11  ? 2.03447 1.23815 3.45142 -0.48359 -0.58356 -0.25056 12  LEU C CA  
62   C C   . LEU A 11  ? 2.06221 1.26322 3.38952 -0.49678 -0.57916 -0.31948 12  LEU C C   
63   O O   . LEU A 11  ? 2.03402 1.24587 3.39188 -0.48218 -0.54977 -0.32831 12  LEU C O   
64   C CB  . LEU A 11  ? 2.05744 1.26791 3.60257 -0.46737 -0.61353 -0.25461 12  LEU C CB  
65   C CG  . LEU A 11  ? 2.13119 1.33101 3.65566 -0.47698 -0.66965 -0.31810 12  LEU C CG  
66   C CD1 . LEU A 11  ? 2.17475 1.35403 3.62545 -0.49379 -0.71014 -0.32101 12  LEU C CD1 
67   C CD2 . LEU A 11  ? 2.14337 1.35376 3.81160 -0.45634 -0.69107 -0.31943 12  LEU C CD2 
68   N N   . VAL A 12  ? 2.12603 1.31177 3.33923 -0.52453 -0.60884 -0.37118 13  VAL C N   
69   C CA  . VAL A 12  ? 2.16739 1.35847 3.28520 -0.54322 -0.60184 -0.44835 13  VAL C CA  
70   C C   . VAL A 12  ? 2.26143 1.43503 3.31192 -0.56511 -0.65051 -0.50168 13  VAL C C   
71   O O   . VAL A 12  ? 2.30354 1.44648 3.29185 -0.58101 -0.68277 -0.48388 13  VAL C O   
72   C CB  . VAL A 12  ? 2.15383 1.34228 3.14517 -0.56615 -0.56420 -0.45573 13  VAL C CB  
73   C CG1 . VAL A 12  ? 2.22831 1.41930 3.08702 -0.59940 -0.56324 -0.54340 13  VAL C CG1 
74   C CG2 . VAL A 12  ? 2.07216 1.28217 3.12556 -0.54096 -0.51503 -0.42705 13  VAL C CG2 
75   N N   . GLN A 13  ? 2.30142 1.49242 3.36147 -0.56392 -0.65857 -0.56780 14  GLN C N   
76   C CA  . GLN A 13  ? 2.40064 1.57572 3.38566 -0.58569 -0.70086 -0.62357 14  GLN C CA  
77   C C   . GLN A 13  ? 2.47053 1.62344 3.25790 -0.63185 -0.68990 -0.66231 14  GLN C C   
78   O O   . GLN A 13  ? 2.44245 1.61008 3.16511 -0.64508 -0.64262 -0.67473 14  GLN C O   
79   C CB  . GLN A 13  ? 2.42654 1.63164 3.47083 -0.57222 -0.70718 -0.68668 14  GLN C CB  
80   N N   . PRO A 14  ? 2.56841 1.68161 3.25496 -0.65672 -0.73378 -0.67960 15  PRO C N   
81   C CA  . PRO A 14  ? 2.66010 1.74234 3.13997 -0.70617 -0.72415 -0.71812 15  PRO C CA  
82   C C   . PRO A 14  ? 2.67979 1.80021 3.08846 -0.72943 -0.67167 -0.79360 15  PRO C C   
83   O O   . PRO A 14  ? 2.70424 1.85603 3.15605 -0.72162 -0.67272 -0.84792 15  PRO C O   
84   C CB  . PRO A 14  ? 2.77872 1.81819 3.18963 -0.71974 -0.78569 -0.74088 15  PRO C CB  
85   C CG  . PRO A 14  ? 2.72566 1.75825 3.29561 -0.67738 -0.83142 -0.67818 15  PRO C CG  
86   C CD  . PRO A 14  ? 2.60294 1.69072 3.35689 -0.63947 -0.79581 -0.65539 15  PRO C CD  
87   N N   . GLY A 15  ? 2.67077 1.79039 2.97374 -0.75613 -0.62584 -0.79711 16  GLY C N   
88   C CA  . GLY A 15  ? 2.68388 1.84358 2.92238 -0.77549 -0.57047 -0.86441 16  GLY C CA  
89   C C   . GLY A 15  ? 2.55945 1.77145 2.91926 -0.73679 -0.52567 -0.84683 16  GLY C C   
90   O O   . GLY A 15  ? 2.55982 1.80781 2.86284 -0.74541 -0.47611 -0.89198 16  GLY C O   
91   N N   . GLY A 16  ? 2.46104 1.67665 2.97995 -0.69230 -0.54079 -0.77947 17  GLY C N   
92   C CA  . GLY A 16  ? 2.35619 1.61228 2.99210 -0.65298 -0.50412 -0.76090 17  GLY C CA  
93   C C   . GLY A 16  ? 2.29973 1.55011 2.89087 -0.65970 -0.46670 -0.72118 17  GLY C C   
94   O O   . GLY A 16  ? 2.34486 1.56369 2.80283 -0.69861 -0.46393 -0.71683 17  GLY C O   
95   N N   . SER A 17  ? 2.20649 1.48272 2.90874 -0.62032 -0.44002 -0.69137 18  SER C N   
96   C CA  . SER A 17  ? 2.14673 1.42947 2.81881 -0.61887 -0.39655 -0.66210 18  SER C CA  
97   C C   . SER A 17  ? 2.06186 1.33477 2.85398 -0.57615 -0.39701 -0.56819 18  SER C C   
98   O O   . SER A 17  ? 2.04472 1.30752 2.96427 -0.55091 -0.42641 -0.54398 18  SER C O   
99   C CB  . SER A 17  ? 2.13310 1.46905 2.78490 -0.61180 -0.34611 -0.73328 18  SER C CB  
100  O OG  . SER A 17  ? 2.22177 1.57877 2.76088 -0.64503 -0.33673 -0.81317 18  SER C OG  
101  N N   . LEU A 18  ? 2.03175 1.31262 2.76990 -0.56684 -0.35696 -0.51248 19  LEU C N   
102  C CA  . LEU A 18  ? 1.95198 1.22684 2.78150 -0.52999 -0.34676 -0.42383 19  LEU C CA  
103  C C   . LEU A 18  ? 1.95802 1.25150 2.69999 -0.52355 -0.29726 -0.38763 19  LEU C C   
104  O O   . LEU A 18  ? 2.02478 1.31556 2.63723 -0.55452 -0.28775 -0.39667 19  LEU C O   
105  C CB  . LEU A 18  ? 1.94953 1.18959 2.83661 -0.53484 -0.38958 -0.36289 19  LEU C CB  
106  C CG  . LEU A 18  ? 1.88640 1.12010 2.88458 -0.50459 -0.38041 -0.27528 19  LEU C CG  
107  C CD1 . LEU A 18  ? 1.86150 1.09445 2.98380 -0.47476 -0.37481 -0.27675 19  LEU C CD1 
108  C CD2 . LEU A 18  ? 1.90484 1.11151 2.95907 -0.51707 -0.42557 -0.23717 19  LEU C CD2 
109  N N   . ARG A 19  ? 1.85802 1.16432 2.66190 -0.48476 -0.26756 -0.34554 20  ARG C N   
110  C CA  . ARG A 19  ? 1.86788 1.19317 2.59820 -0.47434 -0.22321 -0.31035 20  ARG C CA  
111  C C   . ARG A 19  ? 1.80628 1.11819 2.59367 -0.45222 -0.22066 -0.21395 20  ARG C C   
112  O O   . ARG A 19  ? 1.74621 1.04586 2.64428 -0.42564 -0.22526 -0.17748 20  ARG C O   
113  C CB  . ARG A 19  ? 1.86668 1.22264 2.60126 -0.44656 -0.18663 -0.35197 20  ARG C CB  
114  C CG  . ARG A 19  ? 1.80852 1.15221 2.66227 -0.40148 -0.19117 -0.32597 20  ARG C CG  
115  C CD  . ARG A 19  ? 1.82131 1.19059 2.66887 -0.37341 -0.16540 -0.37924 20  ARG C CD  
116  N NE  . ARG A 19  ? 1.84312 1.23944 2.60118 -0.37003 -0.12273 -0.36456 20  ARG C NE  
117  C CZ  . ARG A 19  ? 1.85610 1.28198 2.59331 -0.34911 -0.09546 -0.41347 20  ARG C CZ  
118  N NH1 . ARG A 19  ? 1.85056 1.28294 2.65029 -0.32736 -0.10829 -0.48274 20  ARG C NH1 
119  N NH2 . ARG A 19  ? 1.86981 1.31905 2.52936 -0.34820 -0.05816 -0.39602 20  ARG C NH2 
120  N N   . LEU A 20  ? 1.78287 1.09424 2.49508 -0.46599 -0.21404 -0.17497 21  LEU C N   
121  C CA  . LEU A 20  ? 1.71897 1.03031 2.48148 -0.44378 -0.20270 -0.09249 21  LEU C CA  
122  C C   . LEU A 20  ? 1.70493 1.04296 2.43764 -0.41324 -0.15292 -0.07267 21  LEU C C   
123  O O   . LEU A 20  ? 1.75551 1.11297 2.39917 -0.41829 -0.12917 -0.11682 21  LEU C O   
124  C CB  . LEU A 20  ? 1.73387 1.03161 2.44498 -0.46701 -0.22623 -0.06046 21  LEU C CB  
125  C CG  . LEU A 20  ? 1.77430 1.03852 2.49057 -0.49769 -0.28412 -0.07786 21  LEU C CG  
126  C CD1 . LEU A 20  ? 1.79461 1.04168 2.43822 -0.51367 -0.30521 -0.04617 21  LEU C CD1 
127  C CD2 . LEU A 20  ? 1.76200 1.01702 2.63148 -0.48523 -0.30883 -0.05358 21  LEU C CD2 
128  N N   . SER A 21  ? 1.68082 1.01973 2.48505 -0.38458 -0.13631 -0.00588 22  SER C N   
129  C CA  . SER A 21  ? 1.66353 1.02168 2.45033 -0.34973 -0.09305 0.02140  22  SER C CA  
130  C C   . SER A 21  ? 1.61225 0.98111 2.40489 -0.34381 -0.07961 0.09011  22  SER C C   
131  O O   . SER A 21  ? 1.56247 0.92059 2.43381 -0.35066 -0.09574 0.13063  22  SER C O   
132  C CB  . SER A 21  ? 1.64011 0.98062 2.50661 -0.31717 -0.08442 0.03352  22  SER C CB  
133  O OG  . SER A 21  ? 1.68125 1.01291 2.55740 -0.31990 -0.10369 -0.03604 22  SER C OG  
134  N N   . CYS A 22  ? 1.69693 1.09033 2.41435 -0.33187 -0.05098 0.09721  23  CYS C N   
135  C CA  . CYS A 22  ? 1.64684 1.05707 2.36696 -0.32238 -0.03691 0.15485  23  CYS C CA  
136  C C   . CYS A 22  ? 1.63588 1.06779 2.33386 -0.28296 0.00730  0.17370  23  CYS C C   
137  O O   . CYS A 22  ? 1.67535 1.12556 2.29191 -0.27804 0.02334  0.14423  23  CYS C O   
138  C CB  . CYS A 22  ? 1.67711 1.08912 2.31589 -0.35114 -0.05766 0.14420  23  CYS C CB  
139  S SG  . CYS A 22  ? 1.61397 1.05122 2.26227 -0.33431 -0.04452 0.20572  23  CYS C SG  
140  N N   . ALA A 23  ? 1.57870 1.00517 2.34529 -0.25674 0.02723  0.22111  24  ALA C N   
141  C CA  . ALA A 23  ? 1.57879 1.01760 2.31924 -0.21699 0.06509  0.24308  24  ALA C CA  
142  C C   . ALA A 23  ? 1.52785 0.99698 2.26761 -0.20872 0.08599  0.29208  24  ALA C C   
143  O O   . ALA A 23  ? 1.47788 0.95219 2.27787 -0.22607 0.07700  0.32465  24  ALA C O   
144  C CB  . ALA A 23  ? 1.57871 0.98288 2.37271 -0.19339 0.07565  0.26803  24  ALA C CB  
145  N N   . ALA A 24  ? 1.59582 1.08762 2.27638 -0.17961 0.11275  0.29226  25  ALA C N   
146  C CA  . ALA A 24  ? 1.55735 1.08451 2.22398 -0.17010 0.12958  0.32441  25  ALA C CA  
147  C C   . ALA A 24  ? 1.55319 1.08839 2.21943 -0.12753 0.16884  0.36061  25  ALA C C   
148  O O   . ALA A 24  ? 1.60286 1.11928 2.23716 -0.09986 0.17910  0.34448  25  ALA C O   
149  C CB  . ALA A 24  ? 1.58935 1.13646 2.17214 -0.17925 0.12166  0.28633  25  ALA C CB  
150  N N   . SER A 25  ? 1.57302 1.13519 2.27384 -0.12168 0.18805  0.40552  26  SER C N   
151  C CA  . SER A 25  ? 1.57488 1.14291 2.27467 -0.08646 0.22857  0.44549  26  SER C CA  
152  C C   . SER A 25  ? 1.55767 1.17562 2.23120 -0.06730 0.24545  0.45489  26  SER C C   
153  O O   . SER A 25  ? 1.51999 1.16712 2.21422 -0.08743 0.22713  0.45072  26  SER C O   
154  C CB  . SER A 25  ? 1.53915 1.09242 2.32064 -0.10048 0.24655  0.49251  26  SER C CB  
155  O OG  . SER A 25  ? 1.54351 1.05482 2.36612 -0.12616 0.22170  0.48087  26  SER C OG  
156  N N   . GLY A 26  ? 1.59709 1.21989 2.22237 -0.02631 0.27428  0.46433  27  GLY C N   
157  C CA  . GLY A 26  ? 1.58648 1.25787 2.19158 -0.00324 0.29216  0.47319  27  GLY C CA  
158  C C   . GLY A 26  ? 1.58916 1.28488 2.15235 -0.01031 0.26707  0.43249  27  GLY C C   
159  O O   . GLY A 26  ? 1.56954 1.30562 2.13067 -0.00131 0.27036  0.43771  27  GLY C O   
160  N N   . PHE A 27  ? 1.54565 1.21590 2.07387 -0.02835 0.24311  0.38988  28  PHE C N   
161  C CA  . PHE A 27  ? 1.55112 1.23195 2.03726 -0.05335 0.21858  0.35282  28  PHE C CA  
162  C C   . PHE A 27  ? 1.60786 1.26264 2.04814 -0.06765 0.20713  0.29881  28  PHE C C   
163  O O   . PHE A 27  ? 1.61541 1.23952 2.08076 -0.08838 0.19262  0.28970  28  PHE C O   
164  C CB  . PHE A 27  ? 1.50050 1.18027 2.03417 -0.09183 0.18968  0.37125  28  PHE C CB  
165  C CG  . PHE A 27  ? 1.52461 1.17759 2.01833 -0.13496 0.15264  0.33567  28  PHE C CG  
166  C CD1 . PHE A 27  ? 1.55614 1.21115 1.97432 -0.14829 0.14170  0.30713  28  PHE C CD1 
167  C CD2 . PHE A 27  ? 1.52603 1.14683 2.05284 -0.16456 0.12981  0.32992  28  PHE C CD2 
168  C CE1 . PHE A 27  ? 1.59641 1.21734 1.96299 -0.19369 0.11048  0.27646  28  PHE C CE1 
169  C CE2 . PHE A 27  ? 1.56472 1.15660 2.04570 -0.20510 0.09571  0.29608  28  PHE C CE2 
170  C CZ  . PHE A 27  ? 1.60473 1.19434 1.99954 -0.22128 0.08710  0.27017  28  PHE C CZ  
171  N N   . ASP A 28  ? 1.58957 1.25946 1.97013 -0.05796 0.21453  0.25773  29  ASP C N   
172  C CA  . ASP A 28  ? 1.64859 1.30369 1.99395 -0.07178 0.21019  0.19606  29  ASP C CA  
173  C C   . ASP A 28  ? 1.65359 1.29528 1.96202 -0.12909 0.18772  0.16794  29  ASP C C   
174  O O   . ASP A 28  ? 1.63621 1.28407 1.90994 -0.15042 0.17878  0.17842  29  ASP C O   
175  C CB  . ASP A 28  ? 1.69691 1.37656 2.00266 -0.03923 0.23077  0.15547  29  ASP C CB  
176  C CG  . ASP A 28  ? 1.71631 1.40009 2.04242 0.02023  0.24736  0.18201  29  ASP C CG  
177  O OD1 . ASP A 28  ? 1.67320 1.35167 2.03267 0.03171  0.25185  0.24167  29  ASP C OD1 
178  O OD2 . ASP A 28  ? 1.78090 1.47084 2.08898 0.05412  0.25546  0.14057  29  ASP C OD2 
179  N N   . LEU A 29  ? 1.65574 1.27404 1.96515 -0.15377 0.17615  0.12935  30  LEU C N   
180  C CA  . LEU A 29  ? 1.68030 1.28024 1.93786 -0.21011 0.15678  0.09648  30  LEU C CA  
181  C C   . LEU A 29  ? 1.70859 1.32416 1.88749 -0.22710 0.17573  0.04579  30  LEU C C   
182  O O   . LEU A 29  ? 1.71946 1.31724 1.83081 -0.27290 0.16392  0.03900  30  LEU C O   
183  C CB  . LEU A 29  ? 1.71360 1.29006 1.99320 -0.23064 0.14247  0.05974  30  LEU C CB  
184  C CG  . LEU A 29  ? 1.68850 1.23825 2.03498 -0.23846 0.11489  0.09961  30  LEU C CG  
185  C CD1 . LEU A 29  ? 1.65240 1.20450 2.07169 -0.19127 0.12847  0.13694  30  LEU C CD1 
186  C CD2 . LEU A 29  ? 1.73495 1.26115 2.07817 -0.27304 0.09472  0.04943  30  LEU C CD2 
187  N N   . TRP A 30  ? 1.71265 1.35626 1.89846 -0.19141 0.20328  0.00951  35  TRP C N   
188  C CA  . TRP A 30  ? 1.73759 1.40124 1.86451 -0.20946 0.22693  -0.05333 35  TRP C CA  
189  C C   . TRP A 30  ? 1.71689 1.37887 1.77969 -0.23546 0.22758  -0.02955 35  TRP C C   
190  O O   . TRP A 30  ? 1.73670 1.38112 1.72361 -0.29029 0.22980  -0.06156 35  TRP C O   
191  C CB  . TRP A 30  ? 1.76351 1.45995 1.92585 -0.15426 0.24979  -0.08728 35  TRP C CB  
192  C CG  . TRP A 30  ? 1.77730 1.50206 1.89656 -0.17053 0.27746  -0.15632 35  TRP C CG  
193  C CD1 . TRP A 30  ? 1.77015 1.52182 1.87112 -0.15083 0.29599  -0.15629 35  TRP C CD1 
194  C CD2 . TRP A 30  ? 1.77992 1.51151 1.87248 -0.21442 0.29303  -0.23981 35  TRP C CD2 
195  N NE1 . TRP A 30  ? 1.74195 1.51540 1.80978 -0.18076 0.32332  -0.23382 35  TRP C NE1 
196  C CE2 . TRP A 30  ? 1.74692 1.51018 1.80781 -0.22166 0.32465  -0.28743 35  TRP C CE2 
197  C CE3 . TRP A 30  ? 1.78748 1.50448 1.88369 -0.24918 0.28513  -0.28302 35  TRP C CE3 
198  C CZ2 . TRP A 30  ? 1.70905 1.49123 1.74247 -0.26609 0.35365  -0.37735 35  TRP C CZ2 
199  C CZ3 . TRP A 30  ? 1.76793 1.50529 1.83366 -0.29094 0.31207  -0.37324 35  TRP C CZ3 
200  C CH2 . TRP A 30  ? 1.72606 1.49640 1.76089 -0.30096 0.34847  -0.42008 35  TRP C CH2 
201  N N   . TYR A 31  ? 1.83070 1.50587 1.91929 -0.19913 0.22404  0.02706  36  TYR C N   
202  C CA  . TYR A 31  ? 1.81160 1.48414 1.85033 -0.21701 0.21823  0.05027  36  TYR C CA  
203  C C   . TYR A 31  ? 1.79684 1.43012 1.82253 -0.25060 0.17749  0.09901  36  TYR C C   
204  O O   . TYR A 31  ? 1.77305 1.40599 1.79335 -0.24534 0.16173  0.13655  36  TYR C O   
205  C CB  . TYR A 31  ? 1.78451 1.49522 1.86176 -0.15969 0.23127  0.07992  36  TYR C CB  
206  C CG  . TYR A 31  ? 1.81036 1.55603 1.91877 -0.10837 0.26047  0.04492  36  TYR C CG  
207  C CD1 . TYR A 31  ? 1.83229 1.59863 1.90816 -0.11261 0.28447  -0.01681 36  TYR C CD1 
208  C CD2 . TYR A 31  ? 1.81308 1.56719 1.98188 -0.05517 0.26242  0.07422  36  TYR C CD2 
209  C CE1 . TYR A 31  ? 1.83589 1.63226 1.94681 -0.06112 0.30315  -0.05418 36  TYR C CE1 
210  C CE2 . TYR A 31  ? 1.84911 1.62296 2.03669 -0.00474 0.27970  0.04344  36  TYR C CE2 
211  C CZ  . TYR A 31  ? 1.84969 1.64595 2.01259 -0.00514 0.29674  -0.02284 36  TYR C CZ  
212  O OH  . TYR A 31  ? 1.83432 1.64835 2.02260 0.04907  0.30637  -0.05995 36  TYR C OH  
213  N N   . TYR A 32  ? 1.68564 1.28506 1.70922 -0.28368 0.15516  0.09488  37  TYR C N   
214  C CA  . TYR A 32  ? 1.67833 1.24146 1.70866 -0.30579 0.10948  0.14033  37  TYR C CA  
215  C C   . TYR A 32  ? 1.73439 1.24835 1.70766 -0.36154 0.08527  0.11204  37  TYR C C   
216  O O   . TYR A 32  ? 1.77911 1.28767 1.68954 -0.39126 0.10756  0.05701  37  TYR C O   
217  C CB  . TYR A 32  ? 1.62831 1.21278 1.76962 -0.26360 0.10267  0.18792  37  TYR C CB  
218  C CG  . TYR A 32  ? 1.57949 1.20192 1.76587 -0.21974 0.11312  0.22729  37  TYR C CG  
219  C CD1 . TYR A 32  ? 1.56251 1.22637 1.77504 -0.17128 0.15282  0.22347  37  TYR C CD1 
220  C CD2 . TYR A 32  ? 1.55016 1.16613 1.75637 -0.22448 0.07949  0.26439  37  TYR C CD2 
221  C CE1 . TYR A 32  ? 1.52401 1.22378 1.77292 -0.13108 0.16368  0.25620  37  TYR C CE1 
222  C CE2 . TYR A 32  ? 1.50016 1.15785 1.75507 -0.18382 0.09047  0.29390  37  TYR C CE2 
223  C CZ  . TYR A 32  ? 1.49018 1.19071 1.76253 -0.13824 0.13517  0.29009  37  TYR C CZ  
224  O OH  . TYR A 32  ? 1.45694 1.20004 1.77114 -0.09752 0.14810  0.31578  37  TYR C OH  
225  N N   . SER A 33  ? 1.53111 1.20047 1.95354 -0.14462 0.07234  0.13249  38  SER C N   
226  C CA  . SER A 33  ? 1.57163 1.19235 1.95550 -0.15651 0.02695  0.13971  38  SER C CA  
227  C C   . SER A 33  ? 1.56133 1.17950 1.98721 -0.16443 0.00335  0.14994  38  SER C C   
228  O O   . SER A 33  ? 1.51109 1.16107 2.02156 -0.16354 0.00276  0.16134  38  SER C O   
229  C CB  . SER A 33  ? 1.56898 1.17610 1.97621 -0.16077 -0.00191 0.15214  38  SER C CB  
230  O OG  . SER A 33  ? 1.56546 1.18010 1.95593 -0.15334 0.02143  0.14502  38  SER C OG  
231  N N   . ILE A 34  ? 1.58658 1.16869 1.95770 -0.17296 -0.01630 0.14431  39  ILE C N   
232  C CA  . ILE A 34  ? 1.58363 1.15520 1.99206 -0.18367 -0.04524 0.15369  39  ILE C CA  
233  C C   . ILE A 34  ? 1.64160 1.16938 2.00995 -0.19980 -0.09282 0.15485  39  ILE C C   
234  O O   . ILE A 34  ? 1.70560 1.20291 1.99006 -0.20408 -0.09792 0.13898  39  ILE C O   
235  C CB  . ILE A 34  ? 1.59160 1.16137 1.98832 -0.18177 -0.02883 0.14593  39  ILE C CB  
236  C CG1 . ILE A 34  ? 1.53115 1.15555 1.98726 -0.17269 0.00994  0.15436  39  ILE C CG1 
237  C CG2 . ILE A 34  ? 1.60519 1.14824 2.02332 -0.19631 -0.06661 0.15197  39  ILE C CG2 
238  C CD1 . ILE A 34  ? 1.46806 1.13474 2.01367 -0.17398 0.00861  0.17050  39  ILE C CD1 
239  N N   . HIS A 35  ? 1.66356 1.19377 2.09240 -0.21024 -0.12716 0.17350  40  HIS C N   
240  C CA  . HIS A 35  ? 1.72547 1.22026 2.12257 -0.22975 -0.17627 0.17779  40  HIS C CA  
241  C C   . HIS A 35  ? 1.73056 1.21303 2.15670 -0.24264 -0.20185 0.18012  40  HIS C C   
242  O O   . HIS A 35  ? 1.67008 1.17868 2.16756 -0.23829 -0.18995 0.18975  40  HIS C O   
243  C CB  . HIS A 35  ? 1.71689 1.22039 2.15846 -0.23560 -0.20605 0.20164  40  HIS C CB  
244  C CG  . HIS A 35  ? 1.69115 1.21102 2.13578 -0.22206 -0.18225 0.20419  40  HIS C CG  
245  N ND1 . HIS A 35  ? 1.74260 1.24208 2.13207 -0.23023 -0.20086 0.20928  40  HIS C ND1 
246  C CD2 . HIS A 35  ? 1.62420 1.17978 2.12117 -0.20319 -0.14242 0.20197  40  HIS C CD2 
247  C CE1 . HIS A 35  ? 1.70212 1.21926 2.11278 -0.21586 -0.17433 0.21077  40  HIS C CE1 
248  N NE2 . HIS A 35  ? 1.63300 1.18419 2.10803 -0.19895 -0.13791 0.20380  40  HIS C NE2 
249  N N   . TRP A 36  ? 1.80403 1.24912 2.17408 -0.26138 -0.23880 0.17162  41  TRP C N   
250  C CA  . TRP A 36  ? 1.82142 1.24888 2.21557 -0.27929 -0.27442 0.17397  41  TRP C CA  
251  C C   . TRP A 36  ? 1.85590 1.28108 2.26195 -0.29832 -0.32219 0.19440  41  TRP C C   
252  O O   . TRP A 36  ? 1.92413 1.33469 2.26356 -0.30778 -0.33815 0.19114  41  TRP C O   
253  C CB  . TRP A 36  ? 1.89048 1.27719 2.20998 -0.28726 -0.27852 0.14195  41  TRP C CB  
254  C CG  . TRP A 36  ? 1.85648 1.24471 2.18492 -0.27021 -0.23949 0.12829  41  TRP C CG  
255  C CD1 . TRP A 36  ? 1.88022 1.26140 2.14956 -0.25544 -0.20498 0.10513  41  TRP C CD1 
256  C CD2 . TRP A 36  ? 1.79592 1.19676 2.19934 -0.26799 -0.23292 0.14088  41  TRP C CD2 
257  N NE1 . TRP A 36  ? 1.84201 1.22991 2.14686 -0.24337 -0.17861 0.10403  41  TRP C NE1 
258  C CE2 . TRP A 36  ? 1.78991 1.18985 2.17558 -0.25189 -0.19539 0.12674  41  TRP C CE2 
259  C CE3 . TRP A 36  ? 1.74718 1.16332 2.23270 -0.27954 -0.25592 0.16509  41  TRP C CE3 
260  C CZ2 . TRP A 36  ? 1.73945 1.15254 2.18550 -0.24857 -0.18208 0.13896  41  TRP C CZ2 
261  C CZ3 . TRP A 36  ? 1.69349 1.12387 2.23691 -0.27666 -0.24070 0.17523  41  TRP C CZ3 
262  C CH2 . TRP A 36  ? 1.69086 1.11928 2.21377 -0.26199 -0.20491 0.16358  41  TRP C CH2 
263  N N   . VAL A 37  ? 1.86538 1.31011 2.35921 -0.30457 -0.34423 0.21817  42  VAL C N   
264  C CA  . VAL A 37  ? 1.89181 1.34012 2.41812 -0.32296 -0.39317 0.24318  42  VAL C CA  
265  C C   . VAL A 37  ? 1.89959 1.33627 2.45457 -0.34341 -0.42697 0.24524  42  VAL C C   
266  O O   . VAL A 37  ? 1.82930 1.28541 2.45573 -0.33775 -0.41399 0.25206  42  VAL C O   
267  C CB  . VAL A 37  ? 1.81846 1.30933 2.44238 -0.30883 -0.38688 0.27164  42  VAL C CB  
268  C CG1 . VAL A 37  ? 1.85589 1.34938 2.51481 -0.32737 -0.44075 0.30015  42  VAL C CG1 
269  C CG2 . VAL A 37  ? 1.79677 1.29860 2.40053 -0.28736 -0.34852 0.26594  42  VAL C CG2 
270  N N   . ARG A 38  ? 1.88375 1.29167 2.38254 -0.36957 -0.47022 0.23935  43  ARG C N   
271  C CA  . ARG A 38  ? 1.89414 1.28757 2.41505 -0.39241 -0.50585 0.23835  43  ARG C CA  
272  C C   . ARG A 38  ? 1.89614 1.31101 2.47892 -0.41055 -0.55399 0.27383  43  ARG C C   
273  O O   . ARG A 38  ? 1.94382 1.36516 2.50684 -0.41745 -0.57662 0.29075  43  ARG C O   
274  C CB  . ARG A 38  ? 1.98301 1.33177 2.40362 -0.41186 -0.52150 0.20146  43  ARG C CB  
275  C CG  . ARG A 38  ? 2.07700 1.41657 2.42819 -0.43864 -0.56350 0.20227  43  ARG C CG  
276  C CD  . ARG A 38  ? 2.15789 1.46394 2.39496 -0.44821 -0.55669 0.15685  43  ARG C CD  
277  N NE  . ARG A 38  ? 2.24333 1.54199 2.41695 -0.48452 -0.60522 0.15293  43  ARG C NE  
278  C CZ  . ARG A 38  ? 2.31038 1.58269 2.39621 -0.50416 -0.61396 0.10997  43  ARG C CZ  
279  N NH1 . ARG A 38  ? 2.30662 1.55165 2.36615 -0.48974 -0.58069 0.06663  43  ARG C NH1 
280  N NH2 . ARG A 38  ? 2.38168 1.65761 2.40849 -0.54025 -0.65822 0.11010  43  ARG C NH2 
281  N N   . GLN A 39  ? 1.94904 1.37744 2.61170 -0.41853 -0.56991 0.28802  44  GLN C N   
282  C CA  . GLN A 39  ? 1.94428 1.39573 2.67687 -0.43704 -0.61742 0.32166  44  GLN C CA  
283  C C   . GLN A 39  ? 1.98858 1.40908 2.68832 -0.46992 -0.65876 0.30824  44  GLN C C   
284  O O   . GLN A 39  ? 1.95038 1.35965 2.67443 -0.47240 -0.64993 0.29572  44  GLN C O   
285  C CB  . GLN A 39  ? 1.84143 1.34139 2.69941 -0.42085 -0.60082 0.34800  44  GLN C CB  
286  C CG  . GLN A 39  ? 1.82905 1.35925 2.77428 -0.43770 -0.64841 0.38386  44  GLN C CG  
287  C CD  . GLN A 39  ? 1.76262 1.34596 2.81314 -0.41400 -0.63134 0.41048  44  GLN C CD  
288  O OE1 . GLN A 39  ? 1.79373 1.38888 2.86746 -0.41407 -0.65735 0.43309  44  GLN C OE1 
289  N NE2 . GLN A 39  ? 1.67377 1.29158 2.79166 -0.39488 -0.58843 0.40782  44  GLN C NE2 
290  N N   . ALA A 40  ? 2.08244 1.48830 2.72109 -0.49659 -0.70289 0.30902  45  ALA C N   
291  C CA  . ALA A 40  ? 2.13039 1.50968 2.73100 -0.53215 -0.74649 0.29356  45  ALA C CA  
292  C C   . ALA A 40  ? 2.07834 1.48243 2.78044 -0.54829 -0.78298 0.32524  45  ALA C C   
293  O O   . ALA A 40  ? 2.02499 1.47125 2.81911 -0.53543 -0.78371 0.36287  45  ALA C O   
294  C CB  . ALA A 40  ? 2.22916 1.59774 2.73553 -0.55895 -0.78296 0.28882  45  ALA C CB  
295  N N   . PRO A 41  ? 2.17460 1.55380 2.86594 -0.57633 -0.81236 0.30812  46  PRO C N   
296  C CA  . PRO A 41  ? 2.12284 1.52550 2.91069 -0.59438 -0.84725 0.33724  46  PRO C CA  
297  C C   . PRO A 41  ? 2.12202 1.56736 2.96614 -0.60523 -0.88840 0.38319  46  PRO C C   
298  O O   . PRO A 41  ? 2.19101 1.63136 2.97834 -0.63161 -0.93098 0.38792  46  PRO C O   
299  C CB  . PRO A 41  ? 2.19301 1.55345 2.92569 -0.63050 -0.88232 0.30520  46  PRO C CB  
300  C CG  . PRO A 41  ? 2.25384 1.57320 2.86129 -0.63010 -0.86520 0.25805  46  PRO C CG  
301  C CD  . PRO A 41  ? 2.22735 1.55568 2.82848 -0.58924 -0.80843 0.25766  46  PRO C CD  
302  N N   . GLY A 42  ? 2.00750 1.49884 2.96611 -0.58497 -0.87506 0.41747  47  GLY C N   
303  C CA  . GLY A 42  ? 2.00004 1.53580 3.03648 -0.59066 -0.91214 0.46273  47  GLY C CA  
304  C C   . GLY A 42  ? 2.03068 1.57290 3.03274 -0.58116 -0.91748 0.47789  47  GLY C C   
305  O O   . GLY A 42  ? 2.03319 1.60843 3.09809 -0.58761 -0.95460 0.51782  47  GLY C O   
306  N N   . LYS A 43  ? 1.94439 1.45798 2.85607 -0.56537 -0.88139 0.44972  48  LYS C N   
307  C CA  . LYS A 43  ? 1.99761 1.51237 2.86436 -0.55896 -0.88477 0.46223  48  LYS C CA  
308  C C   . LYS A 43  ? 1.94229 1.47241 2.85016 -0.51550 -0.82750 0.46156  48  LYS C C   
309  O O   . LYS A 43  ? 1.86094 1.40586 2.82990 -0.49212 -0.78604 0.45205  48  LYS C O   
310  C CB  . LYS A 43  ? 2.09060 1.56426 2.81240 -0.58045 -0.89150 0.42912  48  LYS C CB  
311  N N   . GLY A 44  ? 1.93780 1.46656 2.81062 -0.50735 -0.82628 0.47244  49  GLY C N   
312  C CA  . GLY A 44  ? 1.89105 1.43338 2.80068 -0.46900 -0.77635 0.47144  49  GLY C CA  
313  C C   . GLY A 44  ? 1.88074 1.39581 2.70756 -0.45177 -0.72024 0.42813  49  GLY C C   
314  O O   . GLY A 44  ? 1.91050 1.39494 2.65845 -0.46637 -0.71740 0.39717  49  GLY C O   
315  N N   . LEU A 45  ? 1.84835 1.37590 2.69933 -0.41972 -0.67512 0.42521  50  LEU C N   
316  C CA  . LEU A 45  ? 1.83658 1.34446 2.61653 -0.40143 -0.62082 0.38841  50  LEU C CA  
317  C C   . LEU A 45  ? 1.94507 1.42101 2.60307 -0.41375 -0.62780 0.37556  50  LEU C C   
318  O O   . LEU A 45  ? 2.01926 1.49510 2.65864 -0.43060 -0.66693 0.40057  50  LEU C O   
319  C CB  . LEU A 45  ? 1.73925 1.27685 2.58863 -0.36547 -0.56977 0.38830  50  LEU C CB  
320  C CG  . LEU A 45  ? 1.64022 1.21574 2.59374 -0.35101 -0.54446 0.38953  50  LEU C CG  
321  C CD1 . LEU A 45  ? 1.56562 1.18244 2.61032 -0.32189 -0.51220 0.39828  50  LEU C CD1 
322  C CD2 . LEU A 45  ? 1.61324 1.17599 2.52235 -0.34689 -0.50605 0.35908  50  LEU C CD2 
323  N N   . GLU A 46  ? 1.90338 1.35560 2.48033 -0.40621 -0.58952 0.33766  51  GLU C N   
324  C CA  . GLU A 46  ? 2.00438 1.43007 2.46023 -0.41779 -0.58901 0.31773  51  GLU C CA  
325  C C   . GLU A 46  ? 1.96370 1.38295 2.38329 -0.38989 -0.52793 0.28750  51  GLU C C   
326  O O   . GLU A 46  ? 1.92209 1.33221 2.34038 -0.38080 -0.50056 0.26159  51  GLU C O   
327  C CB  . GLU A 46  ? 2.08444 1.48343 2.46155 -0.44980 -0.62046 0.29460  51  GLU C CB  
328  C CG  . GLU A 46  ? 2.18527 1.56348 2.43520 -0.46283 -0.61558 0.26717  51  GLU C CG  
329  C CD  . GLU A 46  ? 2.24020 1.59272 2.41746 -0.48987 -0.63541 0.23088  51  GLU C CD  
330  O OE1 . GLU A 46  ? 2.20629 1.55425 2.43275 -0.50141 -0.65922 0.23181  51  GLU C OE1 
331  O OE2 . GLU A 46  ? 2.31326 1.65168 2.38644 -0.50028 -0.62675 0.19943  51  GLU C OE2 
332  N N   . TRP A 47  ? 2.04451 1.46907 2.43857 -0.37762 -0.50864 0.29325  52  TRP C N   
333  C CA  . TRP A 47  ? 2.01307 1.43273 2.36168 -0.35463 -0.45346 0.26479  52  TRP C CA  
334  C C   . TRP A 47  ? 2.09933 1.49006 2.33734 -0.36821 -0.44942 0.22777  52  TRP C C   
335  O O   . TRP A 47  ? 2.20585 1.58545 2.36530 -0.39222 -0.47726 0.22574  52  TRP C O   
336  C CB  . TRP A 47  ? 2.00852 1.43822 2.35026 -0.34357 -0.43994 0.27986  52  TRP C CB  
337  C CG  . TRP A 47  ? 1.99105 1.41612 2.27176 -0.32511 -0.38818 0.25155  52  TRP C CG  
338  C CD1 . TRP A 47  ? 1.89121 1.33277 2.21296 -0.29673 -0.33801 0.23982  52  TRP C CD1 
339  C CD2 . TRP A 47  ? 2.08233 1.49033 2.24982 -0.33585 -0.38205 0.23195  52  TRP C CD2 
340  N NE1 . TRP A 47  ? 1.91289 1.34632 2.15524 -0.28859 -0.30265 0.21564  52  TRP C NE1 
341  C CE2 . TRP A 47  ? 2.02598 1.43904 2.17475 -0.31135 -0.32802 0.20989  52  TRP C CE2 
342  C CE3 . TRP A 47  ? 2.21216 1.60653 2.29167 -0.36579 -0.41666 0.23052  52  TRP C CE3 
343  C CZ2 . TRP A 47  ? 2.08768 1.49135 2.13769 -0.31394 -0.30779 0.18706  52  TRP C CZ2 
344  C CZ3 . TRP A 47  ? 2.27623 1.66388 2.25581 -0.36911 -0.39465 0.20605  52  TRP C CZ3 
345  C CH2 . TRP A 47  ? 2.21042 1.60195 2.17791 -0.34239 -0.34071 0.18467  52  TRP C CH2 
346  N N   . VAL A 48  ? 2.03139 1.41296 2.26639 -0.35376 -0.41511 0.19858  53  VAL C N   
347  C CA  . VAL A 48  ? 2.10108 1.45446 2.24542 -0.36236 -0.40811 0.15846  53  VAL C CA  
348  C C   . VAL A 48  ? 2.12046 1.47523 2.19664 -0.34715 -0.36802 0.14047  53  VAL C C   
349  O O   . VAL A 48  ? 2.21443 1.56025 2.20085 -0.36293 -0.37706 0.12537  53  VAL C O   
350  C CB  . VAL A 48  ? 2.05002 1.38970 2.22832 -0.35400 -0.39279 0.13760  53  VAL C CB  
351  C CG1 . VAL A 48  ? 2.12526 1.43220 2.21750 -0.36361 -0.39103 0.09291  53  VAL C CG1 
352  C CG2 . VAL A 48  ? 2.01107 1.35593 2.27151 -0.36709 -0.42794 0.16040  53  VAL C CG2 
353  N N   . ALA A 49  ? 2.06849 1.43936 2.18631 -0.31869 -0.32361 0.14233  54  ALA C N   
354  C CA  . ALA A 49  ? 2.07863 1.45216 2.13443 -0.30396 -0.28346 0.12381  54  ALA C CA  
355  C C   . ALA A 49  ? 1.97228 1.37291 2.09127 -0.27697 -0.24299 0.13687  54  ALA C C   
356  O O   . ALA A 49  ? 1.89376 1.31253 2.10216 -0.26927 -0.24282 0.15570  54  ALA C O   
357  C CB  . ALA A 49  ? 2.11745 1.46957 2.11200 -0.30085 -0.26354 0.08234  54  ALA C CB  
358  N N   . TYR A 50  ? 1.99029 1.39746 2.06067 -0.26409 -0.20718 0.12426  55  TYR C N   
359  C CA  . TYR A 50  ? 1.89908 1.33357 2.01835 -0.23980 -0.16397 0.12912  55  TYR C CA  
360  C C   . TYR A 50  ? 1.91454 1.34897 1.96910 -0.22707 -0.12316 0.10267  55  TYR C C   
361  O O   . TYR A 50  ? 1.99138 1.40854 1.96222 -0.23609 -0.12715 0.08330  55  TYR C O   
362  C CB  . TYR A 50  ? 1.85788 1.31182 2.01834 -0.23629 -0.16585 0.15439  55  TYR C CB  
363  C CG  . TYR A 50  ? 1.90966 1.35675 1.99892 -0.24323 -0.16679 0.15519  55  TYR C CG  
364  C CD1 . TYR A 50  ? 1.91787 1.36894 1.94539 -0.23329 -0.12841 0.13467  55  TYR C CD1 
365  C CD2 . TYR A 50  ? 1.94882 1.38874 2.03757 -0.26117 -0.20758 0.18043  55  TYR C CD2 
366  C CE1 . TYR A 50  ? 1.96146 1.40933 1.92549 -0.24221 -0.12992 0.13756  55  TYR C CE1 
367  C CE2 . TYR A 50  ? 1.99534 1.43109 2.02124 -0.27100 -0.21100 0.18620  55  TYR C CE2 
368  C CZ  . TYR A 50  ? 1.99901 1.43903 1.96208 -0.26175 -0.17128 0.16411  55  TYR C CZ  
369  O OH  . TYR A 50  ? 2.04048 1.47933 1.94147 -0.27386 -0.17480 0.17164  55  TYR C OH  
370  N N   . ILE A 51  ? 1.81159 1.27086 1.90767 -0.20720 -0.08355 0.10211  56  ILE C N   
371  C CA  . ILE A 51  ? 1.81507 1.28360 1.86250 -0.19338 -0.04224 0.08341  56  ILE C CA  
372  C C   . ILE A 51  ? 1.74481 1.24995 1.84032 -0.17902 -0.00939 0.09549  56  ILE C C   
373  O O   . ILE A 51  ? 1.68279 1.21120 1.85901 -0.17425 -0.00601 0.11011  56  ILE C O   
374  C CB  . ILE A 51  ? 1.82328 1.28364 1.86233 -0.18539 -0.02598 0.06395  56  ILE C CB  
375  C CG1 . ILE A 51  ? 1.82236 1.29750 1.81674 -0.17043 0.01616  0.04793  56  ILE C CG1 
376  C CG2 . ILE A 51  ? 1.75986 1.23679 1.88580 -0.18033 -0.02273 0.07944  56  ILE C CG2 
377  C CD1 . ILE A 51  ? 1.83477 1.29932 1.81946 -0.16155 0.02998  0.02898  56  ILE C CD1 
378  N N   . TYR A 52  ? 1.78833 1.30114 1.83385 -0.17406 0.01446  0.08765  57  TYR C N   
379  C CA  . TYR A 52  ? 1.73396 1.27967 1.81338 -0.16241 0.04695  0.09324  57  TYR C CA  
380  C C   . TYR A 52  ? 1.72710 1.28901 1.76231 -0.15102 0.08833  0.07557  57  TYR C C   
381  O O   . TYR A 52  ? 1.75229 1.30984 1.72229 -0.15231 0.09893  0.06611  57  TYR C O   
382  C CB  . TYR A 52  ? 1.74219 1.28177 1.81016 -0.16950 0.03331  0.10424  57  TYR C CB  
383  C CG  . TYR A 52  ? 1.71929 1.25400 1.85624 -0.17651 -0.00212 0.12676  57  TYR C CG  
384  C CD1 . TYR A 52  ? 1.73215 1.25175 1.89312 -0.18606 -0.03703 0.13507  57  TYR C CD1 
385  C CD2 . TYR A 52  ? 1.68325 1.22960 1.86921 -0.17296 -0.00062 0.13912  57  TYR C CD2 
386  C CE1 . TYR A 52  ? 1.71057 1.22923 1.93840 -0.19250 -0.07072 0.15746  57  TYR C CE1 
387  C CE2 . TYR A 52  ? 1.65918 1.20257 1.91815 -0.17730 -0.03389 0.16033  57  TYR C CE2 
388  C CZ  . TYR A 52  ? 1.67157 1.20306 1.95081 -0.18701 -0.06880 0.17056  57  TYR C CZ  
389  O OH  . TYR A 52  ? 1.64668 1.17882 2.00225 -0.19135 -0.10295 0.19336  57  TYR C OH  
390  N N   . PRO A 53  ? 1.70210 1.28570 1.77243 -0.14139 0.11098  0.07345  58  PRO C N   
391  C CA  . PRO A 53  ? 1.70460 1.30132 1.73512 -0.13153 0.14407  0.05947  58  PRO C CA  
392  C C   . PRO A 53  ? 1.69612 1.31271 1.68502 -0.12696 0.17389  0.05218  58  PRO C C   
393  O O   . PRO A 53  ? 1.72516 1.33094 1.64561 -0.12618 0.18124  0.03785  58  PRO C O   
394  C CB  . PRO A 53  ? 1.65788 1.28801 1.75650 -0.12532 0.16217  0.07002  58  PRO C CB  
395  C CG  . PRO A 53  ? 1.65333 1.26765 1.80436 -0.13365 0.12860  0.08229  58  PRO C CG  
396  C CD  . PRO A 53  ? 1.66824 1.26211 1.81441 -0.14225 0.10023  0.08637  58  PRO C CD  
397  N N   . SER A 54  ? 1.72802 1.37489 1.75897 -0.12472 0.19136  0.05961  59  SER C N   
398  C CA  . SER A 54  ? 1.71393 1.38126 1.70954 -0.12153 0.22130  0.05156  59  SER C CA  
399  C C   . SER A 54  ? 1.74519 1.38445 1.68404 -0.13055 0.20401  0.04990  59  SER C C   
400  O O   . SER A 54  ? 1.72530 1.37870 1.63392 -0.13030 0.22591  0.04464  59  SER C O   
401  C CB  . SER A 54  ? 1.66555 1.37339 1.72465 -0.11808 0.24513  0.05493  59  SER C CB  
402  O OG  . SER A 54  ? 1.65467 1.35311 1.77306 -0.12184 0.22090  0.06482  59  SER C OG  
403  N N   . TYR A 55  ? 1.68489 1.28812 1.60769 -0.14110 0.16476  0.05583  62  TYR C N   
404  C CA  . TYR A 55  ? 1.72394 1.30423 1.59251 -0.15467 0.14317  0.05979  62  TYR C CA  
405  C C   . TYR A 55  ? 1.78635 1.34470 1.57597 -0.16330 0.12856  0.04701  62  TYR C C   
406  O O   . TYR A 55  ? 1.81814 1.36950 1.54509 -0.17549 0.12146  0.04646  62  TYR C O   
407  C CB  . TYR A 55  ? 1.72992 1.29183 1.64590 -0.16487 0.10454  0.08093  62  TYR C CB  
408  C CG  . TYR A 55  ? 1.67125 1.25340 1.67280 -0.15672 0.11530  0.09033  62  TYR C CG  
409  C CD1 . TYR A 55  ? 1.62304 1.23226 1.69240 -0.14473 0.13459  0.08655  62  TYR C CD1 
410  C CD2 . TYR A 55  ? 1.66611 1.24184 1.68512 -0.16225 0.10492  0.10260  62  TYR C CD2 
411  C CE1 . TYR A 55  ? 1.57242 1.20663 1.72117 -0.13782 0.14738  0.08928  62  TYR C CE1 
412  C CE2 . TYR A 55  ? 1.61187 1.20599 1.71668 -0.15320 0.11590  0.10517  62  TYR C CE2 
413  C CZ  . TYR A 55  ? 1.56596 1.19160 1.73440 -0.14073 0.13881  0.09591  62  TYR C CZ  
414  O OH  . TYR A 55  ? 1.51749 1.16835 1.77246 -0.13225 0.15305  0.09277  62  TYR C OH  
415  N N   . GLY A 56  ? 1.77921 1.32842 1.57188 -0.15862 0.12413  0.03568  63  GLY C N   
416  C CA  . GLY A 56  ? 1.84374 1.37090 1.56956 -0.16742 0.10789  0.01787  63  GLY C CA  
417  C C   . GLY A 56  ? 1.90679 1.40820 1.61921 -0.18823 0.06216  0.02792  63  GLY C C   
418  O O   . GLY A 56  ? 1.96931 1.46220 1.60900 -0.20386 0.04846  0.01876  63  GLY C O   
419  N N   . TYR A 57  ? 1.91980 1.41351 1.70071 -0.19069 0.03765  0.04730  64  TYR C N   
420  C CA  . TYR A 57  ? 1.96918 1.44233 1.74716 -0.21153 -0.00907 0.06255  64  TYR C CA  
421  C C   . TYR A 57  ? 1.99464 1.44937 1.79380 -0.21470 -0.03138 0.05380  64  TYR C C   
422  O O   . TYR A 57  ? 1.93757 1.39757 1.80978 -0.20329 -0.02633 0.06048  64  TYR C O   
423  C CB  . TYR A 57  ? 1.91838 1.39749 1.76672 -0.21290 -0.02445 0.09362  64  TYR C CB  
424  C CG  . TYR A 57  ? 1.89412 1.38551 1.73198 -0.21232 -0.00897 0.10427  64  TYR C CG  
425  C CD1 . TYR A 57  ? 1.92216 1.41918 1.68021 -0.21604 0.01132  0.09104  64  TYR C CD1 
426  C CD2 . TYR A 57  ? 1.84072 1.33915 1.75442 -0.20781 -0.01395 0.12602  64  TYR C CD2 
427  C CE1 . TYR A 57  ? 1.89611 1.40319 1.64763 -0.21748 0.02413  0.10211  64  TYR C CE1 
428  C CE2 . TYR A 57  ? 1.82036 1.32608 1.73128 -0.20750 -0.00076 0.13397  64  TYR C CE2 
429  C CZ  . TYR A 57  ? 1.84709 1.35599 1.67589 -0.21336 0.01727  0.12343  64  TYR C CZ  
430  O OH  . TYR A 57  ? 1.82366 1.33843 1.65271 -0.21511 0.02860  0.13281  64  TYR C OH  
431  N N   . THR A 58  ? 1.99817 1.43404 1.73403 -0.23284 -0.05696 0.03892  65  THR C N   
432  C CA  . THR A 58  ? 2.03695 1.45089 1.78334 -0.24133 -0.08419 0.02726  65  THR C CA  
433  C C   . THR A 58  ? 2.12516 1.52936 1.82796 -0.27107 -0.12881 0.03750  65  THR C C   
434  O O   . THR A 58  ? 2.20643 1.60826 1.82554 -0.28685 -0.13429 0.01654  65  THR C O   
435  C CB  . THR A 58  ? 2.06591 1.46889 1.77149 -0.23333 -0.06496 -0.01246 65  THR C CB  
436  O OG1 . THR A 58  ? 2.11904 1.52786 1.73426 -0.24144 -0.05478 -0.03489 65  THR C OG1 
437  C CG2 . THR A 58  ? 1.98443 1.40010 1.73673 -0.20610 -0.02454 -0.01581 65  THR C CG2 
438  N N   . TYR A 59  ? 2.11158 1.51511 1.87261 -0.27985 -0.16062 0.07054  66  TYR C N   
439  C CA  . TYR A 59  ? 2.19776 1.59400 1.93075 -0.31006 -0.20950 0.08705  66  TYR C CA  
440  C C   . TYR A 59  ? 2.19731 1.57926 1.98311 -0.31711 -0.24102 0.09000  66  TYR C C   
441  O O   . TYR A 59  ? 2.10486 1.49069 1.97894 -0.30086 -0.23490 0.10408  66  TYR C O   
442  C CB  . TYR A 59  ? 2.16824 1.57633 1.93025 -0.31576 -0.22481 0.12789  66  TYR C CB  
443  C CG  . TYR A 59  ? 2.24889 1.65388 1.99545 -0.34778 -0.27953 0.15675  66  TYR C CG  
444  C CD1 . TYR A 59  ? 2.37073 1.77550 2.01974 -0.37752 -0.30095 0.14500  66  TYR C CD1 
445  C CD2 . TYR A 59  ? 2.19814 1.60550 2.02957 -0.34920 -0.30944 0.19676  66  TYR C CD2 
446  C CE1 . TYR A 59  ? 2.44072 1.84849 2.07350 -0.41049 -0.35292 0.17577  66  TYR C CE1 
447  C CE2 . TYR A 59  ? 2.26912 1.67607 2.09166 -0.37901 -0.36209 0.22842  66  TYR C CE2 
448  C CZ  . TYR A 59  ? 2.39080 1.79846 2.11188 -0.41086 -0.38457 0.21976  66  TYR C CZ  
449  O OH  . TYR A 59  ? 2.45085 1.86340 2.16151 -0.44422 -0.43939 0.25540  66  TYR C OH  
450  N N   . TYR A 60  ? 2.26055 1.62990 1.99142 -0.34336 -0.27409 0.07563  67  TYR C N   
451  C CA  . TYR A 60  ? 2.26556 1.61982 2.03454 -0.35575 -0.30837 0.07516  67  TYR C CA  
452  C C   . TYR A 60  ? 2.34694 1.70568 2.09831 -0.38924 -0.36160 0.10337  67  TYR C C   
453  O O   . TYR A 60  ? 2.41605 1.78666 2.10622 -0.40598 -0.37089 0.11450  67  TYR C O   
454  C CB  . TYR A 60  ? 2.29545 1.62891 2.01791 -0.35969 -0.30295 0.02699  67  TYR C CB  
455  C CG  . TYR A 60  ? 2.26496 1.59611 1.96004 -0.33432 -0.25252 -0.00838 67  TYR C CG  
456  C CD1 . TYR A 60  ? 2.17353 1.50282 1.93778 -0.30552 -0.22147 -0.00769 67  TYR C CD1 
457  C CD2 . TYR A 60  ? 2.32174 1.65674 1.92327 -0.34112 -0.23737 -0.04196 67  TYR C CD2 
458  C CE1 . TYR A 60  ? 2.14935 1.47852 1.89299 -0.28342 -0.17888 -0.03595 67  TYR C CE1 
459  C CE2 . TYR A 60  ? 2.28759 1.62270 1.87075 -0.31699 -0.19266 -0.07366 67  TYR C CE2 
460  C CZ  . TYR A 60  ? 2.20587 1.53671 1.86166 -0.28790 -0.16486 -0.06901 67  TYR C CZ  
461  O OH  . TYR A 60  ? 2.17349 1.50667 1.81585 -0.26467 -0.12338 -0.09591 67  TYR C OH  
462  N N   . ALA A 61  ? 2.29570 1.64781 2.10346 -0.40076 -0.39818 0.11851  68  ALA C N   
463  C CA  . ALA A 61  ? 2.37333 1.73134 2.16134 -0.43595 -0.45286 0.14466  68  ALA C CA  
464  C C   . ALA A 61  ? 2.45486 1.80741 2.13357 -0.46593 -0.46733 0.10804  68  ALA C C   
465  O O   . ALA A 61  ? 2.44711 1.78560 2.08589 -0.45740 -0.43969 0.05997  68  ALA C O   
466  C CB  . ALA A 61  ? 2.32902 1.68482 2.20708 -0.44166 -0.48883 0.16936  68  ALA C CB  
467  N N   . ASP A 62  ? 2.50507 1.87187 2.13767 -0.50220 -0.51143 0.13107  69  ASP C N   
468  C CA  . ASP A 62  ? 2.56235 1.93424 2.08370 -0.53540 -0.52468 0.09616  69  ASP C CA  
469  C C   . ASP A 62  ? 2.55653 1.90957 2.07342 -0.54940 -0.54293 0.05788  69  ASP C C   
470  O O   . ASP A 62  ? 2.57900 1.92839 2.01555 -0.56179 -0.53202 0.00583  69  ASP C O   
471  C CB  . ASP A 62  ? 2.61305 2.01179 2.08594 -0.57439 -0.56865 0.13684  69  ASP C CB  
472  C CG  . ASP A 62  ? 2.60202 2.00542 2.16354 -0.58248 -0.61521 0.19661  69  ASP C CG  
473  O OD1 . ASP A 62  ? 2.55387 1.94256 2.21053 -0.56120 -0.61529 0.20277  69  ASP C OD1 
474  O OD2 . ASP A 62  ? 2.63170 2.05651 2.17013 -0.61086 -0.65216 0.23966  69  ASP C OD2 
475  N N   . SER A 63  ? 2.50794 1.85016 2.11147 -0.54867 -0.57062 0.08029  70  SER C N   
476  C CA  . SER A 63  ? 2.50392 1.82661 2.10553 -0.56560 -0.59208 0.04576  70  SER C CA  
477  C C   . SER A 63  ? 2.47571 1.77081 2.07095 -0.53924 -0.54707 -0.01135 70  SER C C   
478  O O   . SER A 63  ? 2.49820 1.77770 2.04502 -0.55622 -0.55392 -0.06060 70  SER C O   
479  C CB  . SER A 63  ? 2.46003 1.77892 2.16574 -0.56708 -0.62666 0.08404  70  SER C CB  
480  O OG  . SER A 63  ? 2.38552 1.69932 2.18762 -0.52685 -0.59408 0.10263  70  SER C OG  
481  N N   . VAL A 64  ? 2.47337 1.76297 2.12057 -0.49850 -0.50189 -0.00612 71  VAL C N   
482  C CA  . VAL A 64  ? 2.43828 1.70313 2.09199 -0.47216 -0.46147 -0.05201 71  VAL C CA  
483  C C   . VAL A 64  ? 2.45455 1.72761 2.03855 -0.45595 -0.41672 -0.08159 71  VAL C C   
484  O O   . VAL A 64  ? 2.42310 1.67883 2.01457 -0.43092 -0.38029 -0.11709 71  VAL C O   
485  C CB  . VAL A 64  ? 2.34898 1.60525 2.11240 -0.44029 -0.44210 -0.02798 71  VAL C CB  
486  C CG1 . VAL A 64  ? 2.32320 1.57704 2.15984 -0.45690 -0.48566 0.00265  71  VAL C CG1 
487  C CG2 . VAL A 64  ? 2.30780 1.58794 2.10004 -0.41430 -0.41057 0.00633  71  VAL C CG2 
488  N N   . LYS A 65  ? 2.44584 1.74641 1.96722 -0.46974 -0.41922 -0.06477 72  LYS C N   
489  C CA  . LYS A 65  ? 2.45217 1.76588 1.91248 -0.45449 -0.37577 -0.08733 72  LYS C CA  
490  C C   . LYS A 65  ? 2.47954 1.78182 1.87450 -0.45851 -0.35951 -0.15482 72  LYS C C   
491  O O   . LYS A 65  ? 2.53223 1.83472 1.87328 -0.49143 -0.38944 -0.18186 72  LYS C O   
492  C CB  . LYS A 65  ? 2.50345 1.84938 1.90263 -0.47738 -0.38956 -0.05659 72  LYS C CB  
493  N N   . GLY A 66  ? 2.58765 1.88270 1.98932 -0.42550 -0.31207 -0.18315 74  GLY C N   
494  C CA  . GLY A 66  ? 2.59095 1.87104 1.95284 -0.42175 -0.29333 -0.24975 74  GLY C CA  
495  C C   . GLY A 66  ? 2.56763 1.80715 1.99947 -0.41082 -0.30121 -0.27141 74  GLY C C   
496  O O   . GLY A 66  ? 2.53839 1.75896 1.99131 -0.38442 -0.26982 -0.30704 74  GLY C O   
497  N N   . ARG A 67  ? 2.49636 1.72249 1.96807 -0.43183 -0.34461 -0.24903 75  ARG C N   
498  C CA  . ARG A 67  ? 2.46971 1.65718 2.01474 -0.42343 -0.35423 -0.26371 75  ARG C CA  
499  C C   . ARG A 67  ? 2.39628 1.57592 2.03254 -0.38598 -0.32542 -0.23207 75  ARG C C   
500  O O   . ARG A 67  ? 2.36870 1.52106 2.04727 -0.36559 -0.30735 -0.25718 75  ARG C O   
501  C CB  . ARG A 67  ? 2.48772 1.66811 2.05854 -0.45579 -0.40781 -0.24137 75  ARG C CB  
502  C CG  . ARG A 67  ? 2.55249 1.75579 2.03695 -0.49850 -0.44316 -0.24859 75  ARG C CG  
503  C CD  . ARG A 67  ? 2.56909 1.75555 2.07581 -0.53085 -0.49393 -0.25076 75  ARG C CD  
504  N NE  . ARG A 67  ? 2.54996 1.75112 2.11453 -0.54152 -0.52856 -0.18421 75  ARG C NE  
505  C CZ  . ARG A 67  ? 2.50637 1.68917 2.16202 -0.53831 -0.54867 -0.15992 75  ARG C CZ  
506  N NH1 . ARG A 67  ? 2.47990 1.62582 2.18092 -0.52621 -0.53996 -0.19202 75  ARG C NH1 
507  N NH2 . ARG A 67  ? 2.48609 1.68931 2.19294 -0.54797 -0.57906 -0.10095 75  ARG C NH2 
508  N N   . PHE A 68  ? 2.43264 1.63790 2.10151 -0.37740 -0.32065 -0.17775 76  PHE C N   
509  C CA  . PHE A 68  ? 2.33808 1.54514 2.09240 -0.34667 -0.29461 -0.14613 76  PHE C CA  
510  C C   . PHE A 68  ? 2.31619 1.54666 2.04561 -0.32115 -0.24846 -0.14336 76  PHE C C   
511  O O   . PHE A 68  ? 2.36208 1.61199 2.01674 -0.32896 -0.24118 -0.15133 76  PHE C O   
512  C CB  . PHE A 68  ? 2.27478 1.49751 2.09986 -0.35251 -0.31829 -0.08989 76  PHE C CB  
513  C CG  . PHE A 68  ? 2.27648 1.48008 2.14500 -0.37516 -0.36246 -0.08447 76  PHE C CG  
514  C CD1 . PHE A 68  ? 2.33876 1.51084 2.17671 -0.39255 -0.38228 -0.12898 76  PHE C CD1 
515  C CD2 . PHE A 68  ? 2.20968 1.42864 2.15540 -0.37874 -0.38315 -0.03650 76  PHE C CD2 
516  C CE1 . PHE A 68  ? 2.33862 1.49331 2.21772 -0.41533 -0.42396 -0.12363 76  PHE C CE1 
517  C CE2 . PHE A 68  ? 2.20787 1.41281 2.19679 -0.40049 -0.42417 -0.02925 76  PHE C CE2 
518  C CZ  . PHE A 68  ? 2.27381 1.44560 2.22776 -0.41974 -0.44545 -0.07187 76  PHE C CZ  
519  N N   . THR A 69  ? 2.23025 1.46193 2.02405 -0.29290 -0.21829 -0.12963 77  THR C N   
520  C CA  . THR A 69  ? 2.19589 1.45410 1.97754 -0.26934 -0.17550 -0.12029 77  THR C CA  
521  C C   . THR A 69  ? 2.10073 1.37382 1.97162 -0.25066 -0.15954 -0.08069 77  THR C C   
522  O O   . THR A 69  ? 2.06633 1.32392 1.99947 -0.24403 -0.16147 -0.07875 77  THR C O   
523  C CB  . THR A 69  ? 2.22428 1.47445 1.96423 -0.25257 -0.14307 -0.16496 77  THR C CB  
524  O OG1 . THR A 69  ? 2.30500 1.55575 1.95364 -0.27113 -0.15173 -0.20131 77  THR C OG1 
525  C CG2 . THR A 69  ? 2.17178 1.45115 1.91604 -0.22715 -0.09911 -0.14946 77  THR C CG2 
526  N N   . ILE A 70  ? 2.06374 1.36857 1.94214 -0.24475 -0.14536 -0.04935 78  ILE C N   
527  C CA  . ILE A 70  ? 1.97225 1.30163 1.92799 -0.22775 -0.12407 -0.01631 78  ILE C CA  
528  C C   . ILE A 70  ? 1.95530 1.30132 1.89526 -0.20426 -0.07761 -0.02647 78  ILE C C   
529  O O   . ILE A 70  ? 1.99788 1.34562 1.86716 -0.20135 -0.06155 -0.04916 78  ILE C O   
530  C CB  . ILE A 70  ? 1.92492 1.28013 1.90886 -0.23391 -0.13472 0.01979  78  ILE C CB  
531  C CG1 . ILE A 70  ? 1.82926 1.20988 1.90772 -0.22235 -0.12186 0.04944  78  ILE C CG1 
532  C CG2 . ILE A 70  ? 1.93422 1.30871 1.86387 -0.22889 -0.11297 0.02058  78  ILE C CG2 
533  C CD1 . ILE A 70  ? 1.77662 1.17953 1.90170 -0.22843 -0.13780 0.08075  78  ILE C CD1 
534  N N   . SER A 71  ? 1.80662 1.16963 1.81314 -0.18942 -0.05639 -0.00813 79  SER C N   
535  C CA  . SER A 71  ? 1.78885 1.16989 1.78948 -0.16859 -0.01505 -0.01437 79  SER C CA  
536  C C   . SER A 71  ? 1.71380 1.12848 1.79291 -0.16014 0.00285  0.01853  79  SER C C   
537  O O   . SER A 71  ? 1.67207 1.09313 1.80994 -0.16956 -0.01634 0.04141  79  SER C O   
538  C CB  . SER A 71  ? 1.83528 1.18591 1.81768 -0.16152 -0.01254 -0.04682 79  SER C CB  
539  O OG  . SER A 71  ? 1.82143 1.15215 1.87017 -0.16450 -0.03077 -0.03842 79  SER C OG  
540  N N   . ALA A 72  ? 1.77204 1.21240 1.85230 -0.14389 0.03968  0.02035  80  ALA C N   
541  C CA  . ALA A 72  ? 1.70101 1.18257 1.84844 -0.13871 0.06001  0.05035  80  ALA C CA  
542  C C   . ALA A 72  ? 1.69025 1.18626 1.83902 -0.12397 0.08989  0.04869  80  ALA C C   
543  O O   . ALA A 72  ? 1.71131 1.20446 1.80417 -0.11370 0.10824  0.02774  80  ALA C O   
544  C CB  . ALA A 72  ? 1.65403 1.17600 1.80688 -0.13858 0.07709  0.06518  80  ALA C CB  
545  N N   . ASP A 73  ? 1.61841 1.13363 1.83317 -0.12443 0.09364  0.07334  81  ASP C N   
546  C CA  . ASP A 73  ? 1.60279 1.14139 1.83214 -0.11305 0.12010  0.08260  81  ASP C CA  
547  C C   . ASP A 73  ? 1.54476 1.14860 1.80852 -0.11577 0.14692  0.11110  81  ASP C C   
548  O O   . ASP A 73  ? 1.50745 1.13474 1.83007 -0.12726 0.13882  0.13521  81  ASP C O   
549  C CB  . ASP A 73  ? 1.61243 1.12333 1.89174 -0.11455 0.10105  0.09108  81  ASP C CB  
550  C CG  . ASP A 73  ? 1.58268 1.13103 1.90208 -0.10836 0.12373  0.11806  81  ASP C CG  
551  O OD1 . ASP A 73  ? 1.57736 1.15726 1.86565 -0.09728 0.15439  0.11577  81  ASP C OD1 
552  O OD2 . ASP A 73  ? 1.56282 1.11063 1.94613 -0.11670 0.10898  0.14412  81  ASP C OD2 
553  N N   . THR A 74  ? 1.59731 1.23225 1.82156 -0.10663 0.17889  0.10463  82  THR C N   
554  C CA  . THR A 74  ? 1.54903 1.24741 1.79410 -0.10960 0.20795  0.12221  82  THR C CA  
555  C C   . THR A 74  ? 1.52006 1.26323 1.82625 -0.11562 0.21865  0.15410  82  THR C C   
556  O O   . THR A 74  ? 1.48039 1.27260 1.83086 -0.12618 0.22837  0.17258  82  THR C O   
557  C CB  . THR A 74  ? 1.53809 1.25534 1.72413 -0.09961 0.23818  0.10639  82  THR C CB  
558  O OG1 . THR A 74  ? 1.48708 1.26864 1.69466 -0.10351 0.26851  0.12055  82  THR C OG1 
559  C CG2 . THR A 74  ? 1.55847 1.26344 1.71780 -0.08764 0.24690  0.09915  82  THR C CG2 
560  N N   . SER A 75  ? 1.52782 1.25750 1.84033 -0.10995 0.21651  0.16132  83  SER C N   
561  C CA  . SER A 75  ? 1.49871 1.27468 1.86615 -0.11763 0.22595  0.19739  83  SER C CA  
562  C C   . SER A 75  ? 1.47286 1.25557 1.90682 -0.13467 0.20403  0.22214  83  SER C C   
563  O O   . SER A 75  ? 1.42899 1.27535 1.90611 -0.14820 0.21846  0.25076  83  SER C O   
564  C CB  . SER A 75  ? 1.52743 1.27717 1.89592 -0.10686 0.22122  0.20093  83  SER C CB  
565  O OG  . SER A 75  ? 1.54715 1.24462 1.95500 -0.11009 0.18676  0.20505  83  SER C OG  
566  N N   . LYS A 76  ? 1.53752 1.25986 1.97963 -0.13639 0.16957  0.21070  84  LYS C N   
567  C CA  . LYS A 76  ? 1.50852 1.23185 2.01408 -0.15342 0.14478  0.23327  84  LYS C CA  
568  C C   . LYS A 76  ? 1.48064 1.22311 1.99517 -0.16120 0.14225  0.22761  84  LYS C C   
569  O O   . LYS A 76  ? 1.45413 1.19872 2.02111 -0.17533 0.12057  0.24371  84  LYS C O   
570  C CB  . LYS A 76  ? 1.54168 1.19013 2.05637 -0.15343 0.10653  0.22306  84  LYS C CB  
571  N N   . ASN A 77  ? 1.58708 1.34360 2.05691 -0.15250 0.16265  0.20629  85  ASN C N   
572  C CA  . ASN A 77  ? 1.55694 1.32980 2.04137 -0.15729 0.15993  0.20027  85  ASN C CA  
573  C C   . ASN A 77  ? 1.56781 1.28501 2.06213 -0.16334 0.11775  0.19392  85  ASN C C   
574  O O   . ASN A 77  ? 1.53096 1.26588 2.07871 -0.17444 0.10350  0.20706  85  ASN C O   
575  C CB  . ASN A 77  ? 1.50000 1.34979 2.04914 -0.16948 0.17947  0.22424  85  ASN C CB  
576  C CG  . ASN A 77  ? 1.47518 1.36942 2.01796 -0.16509 0.20793  0.20955  85  ASN C CG  
577  O OD1 . ASN A 77  ? 1.49827 1.37548 1.98456 -0.15319 0.22063  0.18747  85  ASN C OD1 
578  N ND2 . ASN A 77  ? 1.42722 1.37990 2.03189 -0.17537 0.21805  0.22042  85  ASN C ND2 
579  N N   . THR A 78  ? 1.54448 1.19771 1.98863 -0.15737 0.09746  0.17266  86  THR C N   
580  C CA  . THR A 78  ? 1.55935 1.16324 2.01739 -0.16748 0.05564  0.16887  86  THR C CA  
581  C C   . THR A 78  ? 1.61753 1.16943 2.00539 -0.16336 0.03816  0.13716  86  THR C C   
582  O O   . THR A 78  ? 1.66474 1.19730 1.99322 -0.15216 0.05124  0.11543  86  THR C O   
583  C CB  . THR A 78  ? 1.57082 1.14784 2.06099 -0.17283 0.03852  0.17953  86  THR C CB  
584  O OG1 . THR A 78  ? 1.51842 1.15047 2.07522 -0.18156 0.05212  0.21512  86  THR C OG1 
585  C CG2 . THR A 78  ? 1.58778 1.11488 2.09376 -0.18587 -0.00532 0.17349  86  THR C CG2 
586  N N   . ALA A 79  ? 1.58900 1.12362 1.98522 -0.17417 0.00812  0.13620  87  ALA C N   
587  C CA  . ALA A 79  ? 1.65171 1.13963 1.98377 -0.17690 -0.01555 0.11050  87  ALA C CA  
588  C C   . ALA A 79  ? 1.69217 1.13023 2.02744 -0.18809 -0.05136 0.09990  87  ALA C C   
589  O O   . ALA A 79  ? 1.65828 1.09826 2.05709 -0.19722 -0.06618 0.11873  87  ALA C O   
590  C CB  . ALA A 79  ? 1.63253 1.13157 1.97110 -0.18418 -0.03111 0.11794  87  ALA C CB  
591  N N   . TYR A 80  ? 1.69905 1.09479 1.96583 -0.18899 -0.06459 0.06822  88  TYR C N   
592  C CA  . TYR A 80  ? 1.74807 1.09454 2.01095 -0.20090 -0.09865 0.04943  88  TYR C CA  
593  C C   . TYR A 80  ? 1.81274 1.13383 2.01189 -0.21428 -0.12590 0.02692  88  TYR C C   
594  O O   . TYR A 80  ? 1.84849 1.17568 1.98211 -0.20928 -0.11191 0.01224  88  TYR C O   
595  C CB  . TYR A 80  ? 1.78861 1.10709 2.03646 -0.18900 -0.08592 0.02532  88  TYR C CB  
596  C CG  . TYR A 80  ? 1.73522 1.08382 2.03422 -0.17550 -0.05626 0.04986  88  TYR C CG  
597  C CD1 . TYR A 80  ? 1.69188 1.04054 2.06750 -0.18302 -0.06882 0.07569  88  TYR C CD1 
598  C CD2 . TYR A 80  ? 1.73067 1.10982 2.00081 -0.15807 -0.01754 0.04907  88  TYR C CD2 
599  C CE1 . TYR A 80  ? 1.64770 1.02905 2.06893 -0.17470 -0.04409 0.10268  88  TYR C CE1 
600  C CE2 . TYR A 80  ? 1.68576 1.09738 2.00083 -0.14898 0.00747  0.07391  88  TYR C CE2 
601  C CZ  . TYR A 80  ? 1.64638 1.06019 2.03632 -0.15791 -0.00622 0.10175  88  TYR C CZ  
602  O OH  . TYR A 80  ? 1.60717 1.05869 2.04065 -0.15268 0.01661  0.13106  88  TYR C OH  
603  N N   . LEU A 81  ? 1.86046 1.15670 2.07964 -0.23390 -0.16593 0.02684  89  LEU C N   
604  C CA  . LEU A 81  ? 1.93335 1.20553 2.09226 -0.25227 -0.19793 0.00562  89  LEU C CA  
605  C C   . LEU A 81  ? 1.99603 1.22110 2.13723 -0.26028 -0.21655 -0.03103 89  LEU C C   
606  O O   . LEU A 81  ? 1.98337 1.18900 2.17706 -0.27305 -0.24371 -0.02451 89  LEU C O   
607  C CB  . LEU A 81  ? 1.90757 1.19324 2.10397 -0.27105 -0.23225 0.03488  89  LEU C CB  
608  C CG  . LEU A 81  ? 1.99047 1.25689 2.12371 -0.29427 -0.26936 0.01881  89  LEU C CG  
609  C CD1 . LEU A 81  ? 2.04997 1.31865 2.09188 -0.28905 -0.24987 -0.00469 89  LEU C CD1 
610  C CD2 . LEU A 81  ? 1.96238 1.25061 2.13610 -0.30923 -0.30004 0.05479  89  LEU C CD2 
611  N N   . GLN A 82  ? 2.10512 1.31360 2.17836 -0.25193 -0.19977 -0.07081 90  GLN C N   
612  C CA  . GLN A 82  ? 2.16783 1.33181 2.22264 -0.25714 -0.21350 -0.11504 90  GLN C CA  
613  C C   . GLN A 82  ? 2.24425 1.39311 2.23797 -0.28510 -0.24961 -0.13998 90  GLN C C   
614  O O   . GLN A 82  ? 2.29323 1.45764 2.21004 -0.29032 -0.24415 -0.15403 90  GLN C O   
615  C CB  . GLN A 82  ? 2.19627 1.35464 2.21518 -0.23407 -0.17717 -0.14873 90  GLN C CB  
616  C CG  . GLN A 82  ? 2.26401 1.37725 2.26237 -0.23736 -0.18869 -0.20352 90  GLN C CG  
617  C CD  . GLN A 82  ? 2.23648 1.31421 2.31969 -0.23672 -0.20521 -0.19887 90  GLN C CD  
618  O OE1 . GLN A 82  ? 2.18724 1.26920 2.32876 -0.21704 -0.18433 -0.17725 90  GLN C OE1 
619  N NE2 . GLN A 82  ? 2.27094 1.31474 2.36099 -0.26059 -0.24435 -0.21800 90  GLN C NE2 
620  N N   . MET A 83  ? 2.26829 1.39217 2.29848 -0.30604 -0.28814 -0.13989 91  MET C N   
621  C CA  . MET A 83  ? 2.34517 1.45310 2.32443 -0.33683 -0.32725 -0.16524 91  MET C CA  
622  C C   . MET A 83  ? 2.41089 1.47695 2.36080 -0.33969 -0.33001 -0.22667 91  MET C C   
623  O O   . MET A 83  ? 2.38412 1.41939 2.39554 -0.32931 -0.32788 -0.23504 91  MET C O   
624  C CB  . MET A 83  ? 2.31354 1.41947 2.35537 -0.35895 -0.36839 -0.13151 91  MET C CB  
625  C CG  . MET A 83  ? 2.21794 1.36049 2.33115 -0.34800 -0.35925 -0.07258 91  MET C CG  
626  S SD  . MET A 83  ? 2.20387 1.35937 2.36333 -0.37846 -0.41081 -0.03487 91  MET C SD  
627  C CE  . MET A 83  ? 2.07652 1.26985 2.34388 -0.35938 -0.38983 0.02060  91  MET C CE  
628  N N   . ASN A 84  ? 2.44480 1.51124 2.30482 -0.35496 -0.33541 -0.26968 92  ASN C N   
629  C CA  . ASN A 84  ? 2.51500 1.54819 2.34194 -0.35500 -0.33091 -0.33717 92  ASN C CA  
630  C C   . ASN A 84  ? 2.60488 1.61969 2.38982 -0.39219 -0.37224 -0.37560 92  ASN C C   
631  O O   . ASN A 84  ? 2.64524 1.62185 2.43688 -0.39422 -0.37711 -0.42898 92  ASN C O   
632  C CB  . ASN A 84  ? 2.55081 1.60507 2.30268 -0.33868 -0.29184 -0.37090 92  ASN C CB  
633  C CG  . ASN A 84  ? 2.47524 1.53700 2.27077 -0.29985 -0.24836 -0.35288 92  ASN C CG  
634  O OD1 . ASN A 84  ? 2.45829 1.49004 2.30396 -0.28019 -0.23560 -0.37454 92  ASN C OD1 
635  N ND2 . ASN A 84  ? 2.43185 1.53412 2.21025 -0.28965 -0.22658 -0.31299 92  ASN C ND2 
636  N N   . SER A 85  ? 2.56584 1.60701 2.31090 -0.42231 -0.40308 -0.35087 93  SER C N   
637  C CA  . SER A 85  ? 2.65629 1.68858 2.35241 -0.46255 -0.44427 -0.38512 93  SER C CA  
638  C C   . SER A 85  ? 2.63523 1.67373 2.37769 -0.48794 -0.48991 -0.33325 93  SER C C   
639  O O   . SER A 85  ? 2.68551 1.75210 2.37811 -0.51839 -0.51958 -0.31683 93  SER C O   
640  C CB  . SER A 85  ? 2.74159 1.80871 2.32304 -0.48240 -0.44069 -0.41328 93  SER C CB  
641  O OG  . SER A 85  ? 2.82825 1.89255 2.35872 -0.52488 -0.48080 -0.44765 93  SER C OG  
642  N N   . LEU A 86  ? 2.58995 1.60502 2.43126 -0.47679 -0.49685 -0.30556 94  LEU C N   
643  C CA  . LEU A 86  ? 2.55359 1.58150 2.45179 -0.49591 -0.53470 -0.25101 94  LEU C CA  
644  C C   . LEU A 86  ? 2.64083 1.66162 2.50014 -0.54055 -0.58499 -0.27395 94  LEU C C   
645  O O   . LEU A 86  ? 2.68060 1.66291 2.54322 -0.55398 -0.59999 -0.32163 94  LEU C O   
646  C CB  . LEU A 86  ? 2.46076 1.46719 2.47008 -0.47911 -0.53185 -0.22288 94  LEU C CB  
647  C CG  . LEU A 86  ? 2.35496 1.38681 2.42052 -0.44403 -0.49356 -0.17507 94  LEU C CG  
648  C CD1 . LEU A 86  ? 2.29880 1.30344 2.44873 -0.42456 -0.47827 -0.17063 94  LEU C CD1 
649  C CD2 . LEU A 86  ? 2.30292 1.37510 2.41009 -0.45223 -0.51168 -0.11341 94  LEU C CD2 
650  N N   . ARG A 87  ? 2.64351 1.70232 2.46788 -0.56438 -0.61202 -0.23944 95  ARG C N   
651  C CA  . ARG A 87  ? 2.71695 1.78128 2.50868 -0.61042 -0.66490 -0.24543 95  ARG C CA  
652  C C   . ARG A 87  ? 2.65838 1.73367 2.54002 -0.62057 -0.70028 -0.18387 95  ARG C C   
653  O O   . ARG A 87  ? 2.56418 1.64933 2.52477 -0.59257 -0.68133 -0.13761 95  ARG C O   
654  C CB  . ARG A 87  ? 2.79745 1.90175 2.48579 -0.63408 -0.67449 -0.24653 95  ARG C CB  
655  C CG  . ARG A 87  ? 2.86670 1.96758 2.45735 -0.63303 -0.64451 -0.31462 95  ARG C CG  
656  C CD  . ARG A 87  ? 2.89543 1.94988 2.48990 -0.63659 -0.64313 -0.38628 95  ARG C CD  
657  N N   . ALA A 88  ? 2.66066 1.73816 2.53022 -0.66265 -0.75191 -0.18582 96  ALA C N   
658  C CA  . ALA A 88  ? 2.61069 1.69808 2.56907 -0.67619 -0.78981 -0.13331 96  ALA C CA  
659  C C   . ALA A 88  ? 2.54375 1.67376 2.55207 -0.65709 -0.78286 -0.06302 96  ALA C C   
660  O O   . ALA A 88  ? 2.45028 1.58516 2.55720 -0.63729 -0.77508 -0.02397 96  ALA C O   
661  C CB  . ALA A 88  ? 2.69244 1.78759 2.61150 -0.72814 -0.84819 -0.14265 96  ALA C CB  
662  N N   . GLU A 89  ? 2.55842 1.72151 2.50145 -0.66396 -0.78545 -0.04716 97  GLU C N   
663  C CA  . GLU A 89  ? 2.50467 1.70641 2.49401 -0.64774 -0.78228 0.01635  97  GLU C CA  
664  C C   . GLU A 89  ? 2.39911 1.59972 2.45194 -0.59990 -0.72921 0.03139  97  GLU C C   
665  O O   . GLU A 89  ? 2.32891 1.55816 2.45458 -0.58415 -0.72659 0.08237  97  GLU C O   
666  C CB  . GLU A 89  ? 2.57999 1.81019 2.47843 -0.66308 -0.78998 0.02353  97  GLU C CB  
667  C CG  . GLU A 89  ? 2.69336 1.92553 2.50000 -0.71190 -0.83167 -0.00853 97  GLU C CG  
668  C CD  . GLU A 89  ? 2.75308 1.96174 2.46502 -0.71308 -0.80229 -0.08258 97  GLU C CD  
669  O OE1 . GLU A 89  ? 2.70507 1.89099 2.43077 -0.67486 -0.75202 -0.10775 97  GLU C OE1 
670  O OE2 . GLU A 89  ? 2.84549 2.06168 2.47183 -0.75312 -0.82979 -0.11645 97  GLU C OE2 
671  N N   . ASP A 90  ? 2.50895 1.68041 2.53750 -0.57705 -0.68706 -0.01246 98  ASP C N   
672  C CA  . ASP A 90  ? 2.40795 1.58195 2.49279 -0.53478 -0.63748 0.00192  98  ASP C CA  
673  C C   . ASP A 90  ? 2.31462 1.49198 2.51514 -0.52637 -0.64209 0.03583  98  ASP C C   
674  O O   . ASP A 90  ? 2.22340 1.41932 2.48133 -0.49629 -0.60702 0.06165  98  ASP C O   
675  C CB  . ASP A 90  ? 2.41992 1.56181 2.45865 -0.51542 -0.59732 -0.05161 98  ASP C CB  
676  C CG  . ASP A 90  ? 2.51540 1.65870 2.43915 -0.52556 -0.59063 -0.09061 98  ASP C CG  
677  O OD1 . ASP A 90  ? 2.59398 1.75188 2.46503 -0.55941 -0.62859 -0.08850 98  ASP C OD1 
678  O OD2 . ASP A 90  ? 2.51279 1.64709 2.39915 -0.50156 -0.54821 -0.12176 98  ASP C OD2 
679  N N   . THR A 91  ? 2.35700 1.52045 2.59163 -0.55415 -0.68367 0.03534  99  THR C N   
680  C CA  . THR A 91  ? 2.27381 1.44667 2.61921 -0.55136 -0.69202 0.07085  99  THR C CA  
681  C C   . THR A 91  ? 2.20489 1.42821 2.61477 -0.53606 -0.68500 0.12610  99  THR C C   
682  O O   . THR A 91  ? 2.24099 1.48974 2.64117 -0.55131 -0.71490 0.15082  99  THR C O   
683  C CB  . THR A 91  ? 2.31818 1.47826 2.68289 -0.59054 -0.74727 0.06916  99  THR C CB  
684  O OG1 . THR A 91  ? 2.40640 1.58000 2.70323 -0.61940 -0.78451 0.06825  99  THR C OG1 
685  C CG2 . THR A 91  ? 2.35161 1.45939 2.69570 -0.60031 -0.74950 0.01819  99  THR C CG2 
686  N N   . ALA A 92  ? 2.16740 1.40735 2.64709 -0.50726 -0.64678 0.14550  100 ALA C N   
687  C CA  . ALA A 92  ? 2.09603 1.38636 2.64042 -0.49018 -0.63421 0.19055  100 ALA C CA  
688  C C   . ALA A 92  ? 1.99885 1.30767 2.61651 -0.46384 -0.59118 0.20362  100 ALA C C   
689  O O   . ALA A 92  ? 1.99030 1.27145 2.59708 -0.45604 -0.56863 0.18021  100 ALA C O   
690  C CB  . ALA A 92  ? 2.11749 1.42159 2.60097 -0.47654 -0.61723 0.19147  100 ALA C CB  
691  N N   . VAL A 93  ? 1.93069 1.28957 2.62566 -0.45091 -0.58018 0.24127  101 VAL C N   
692  C CA  . VAL A 93  ? 1.85362 1.24228 2.60160 -0.42401 -0.53096 0.25191  101 VAL C CA  
693  C C   . VAL A 93  ? 1.84628 1.24262 2.54075 -0.39826 -0.49190 0.24143  101 VAL C C   
694  O O   . VAL A 93  ? 1.85938 1.26932 2.53752 -0.39665 -0.50185 0.25141  101 VAL C O   
695  C CB  . VAL A 93  ? 1.78803 1.23303 2.65058 -0.42356 -0.53384 0.29172  101 VAL C CB  
696  C CG1 . VAL A 93  ? 1.78242 1.26146 2.66973 -0.41865 -0.54609 0.31348  101 VAL C CG1 
697  C CG2 . VAL A 93  ? 1.71990 1.19934 2.63141 -0.40163 -0.48290 0.29925  101 VAL C CG2 
698  N N   . TYR A 94  ? 1.88303 1.27011 2.55166 -0.37946 -0.44955 0.22306  102 TYR C N   
699  C CA  . TYR A 94  ? 1.87963 1.27008 2.49017 -0.35685 -0.41175 0.20907  102 TYR C CA  
700  C C   . TYR A 94  ? 1.79793 1.23861 2.47543 -0.33451 -0.36840 0.22883  102 TYR C C   
701  O O   . TYR A 94  ? 1.76138 1.21656 2.49047 -0.33295 -0.35273 0.23712  102 TYR C O   
702  C CB  . TYR A 94  ? 1.92596 1.27132 2.45257 -0.35280 -0.39633 0.17037  102 TYR C CB  
703  C CG  . TYR A 94  ? 2.02443 1.32913 2.46692 -0.37318 -0.43112 0.14288  102 TYR C CG  
704  C CD1 . TYR A 94  ? 2.07186 1.35141 2.52224 -0.40072 -0.47599 0.13729  102 TYR C CD1 
705  C CD2 . TYR A 94  ? 2.07540 1.37085 2.42914 -0.36757 -0.41878 0.12159  102 TYR C CD2 
706  C CE1 . TYR A 94  ? 2.17016 1.41893 2.54071 -0.42273 -0.50710 0.10917  102 TYR C CE1 
707  C CE2 . TYR A 94  ? 2.17468 1.44160 2.44816 -0.38982 -0.44931 0.09553  102 TYR C CE2 
708  C CZ  . TYR A 94  ? 2.22265 1.46741 2.50384 -0.41758 -0.49300 0.08820  102 TYR C CZ  
709  O OH  . TYR A 94  ? 2.32706 1.54951 2.52585 -0.44280 -0.52265 0.05947  102 TYR C OH  
710  N N   . TYR A 95  ? 1.78686 1.25719 2.47021 -0.32076 -0.35318 0.23848  103 TYR C N   
711  C CA  . TYR A 95  ? 1.72433 1.24634 2.46527 -0.30000 -0.31115 0.25127  103 TYR C CA  
712  C C   . TYR A 95  ? 1.72652 1.24323 2.39977 -0.28029 -0.27136 0.23141  103 TYR C C   
713  O O   . TYR A 95  ? 1.77156 1.25673 2.36809 -0.28187 -0.28159 0.21666  103 TYR C O   
714  C CB  . TYR A 95  ? 1.70213 1.26238 2.51299 -0.29833 -0.32490 0.27472  103 TYR C CB  
715  C CG  . TYR A 95  ? 1.68879 1.27322 2.58845 -0.31380 -0.35474 0.29840  103 TYR C CG  
716  C CD1 . TYR A 95  ? 1.64037 1.27244 2.62002 -0.31031 -0.33025 0.31082  103 TYR C CD1 
717  C CD2 . TYR A 95  ? 1.73429 1.29809 2.63629 -0.33482 -0.40839 0.30954  103 TYR C CD2 
718  C CE1 . TYR A 95  ? 1.62771 1.28627 2.69009 -0.32596 -0.35696 0.33329  103 TYR C CE1 
719  C CE2 . TYR A 95  ? 1.72252 1.31054 2.70746 -0.35008 -0.43678 0.33204  103 TYR C CE2 
720  C CZ  . TYR A 95  ? 1.66606 1.30114 2.73211 -0.34502 -0.41031 0.34356  103 TYR C CZ  
721  O OH  . TYR A 95  ? 1.65306 1.31698 2.80405 -0.36160 -0.43784 0.36692  103 TYR C OH  
722  N N   . CYS A 96  ? 1.56842 1.12085 2.26994 -0.26419 -0.22655 0.23232  104 CYS C N   
723  C CA  . CYS A 96  ? 1.56029 1.11933 2.21196 -0.24535 -0.18657 0.21720  104 CYS C CA  
724  C C   . CYS A 96  ? 1.51042 1.12671 2.23096 -0.23244 -0.15946 0.22952  104 CYS C C   
725  O O   . CYS A 96  ? 1.47806 1.13744 2.28241 -0.23504 -0.15503 0.24569  104 CYS C O   
726  C CB  . CYS A 96  ? 1.55994 1.11110 2.17600 -0.23823 -0.15563 0.20349  104 CYS C CB  
727  S SG  . CYS A 96  ? 1.50292 1.11402 2.20394 -0.23524 -0.12236 0.22356  104 CYS C SG  
728  N N   . ALA A 97  ? 1.47652 1.09491 2.16391 -0.21968 -0.14133 0.22023  105 ALA C N   
729  C CA  . ALA A 97  ? 1.43841 1.10636 2.19537 -0.20746 -0.11906 0.22688  105 ALA C CA  
730  C C   . ALA A 97  ? 1.43048 1.10438 2.14013 -0.19172 -0.08009 0.20979  105 ALA C C   
731  O O   . ALA A 97  ? 1.45982 1.09492 2.08161 -0.19152 -0.08070 0.19696  105 ALA C O   
732  C CB  . ALA A 97  ? 1.44717 1.11155 2.25103 -0.21228 -0.15757 0.24241  105 ALA C CB  
733  N N   . ARG A 98  ? 1.33985 1.06520 2.11123 -0.17968 -0.04721 0.20805  106 ARG C N   
734  C CA  . ARG A 98  ? 1.33049 1.06685 2.06742 -0.16595 -0.00934 0.19100  106 ARG C CA  
735  C C   . ARG A 98  ? 1.33255 1.05984 2.09308 -0.16014 -0.02402 0.19282  106 ARG C C   
736  O O   . ARG A 98  ? 1.32574 1.07004 2.16875 -0.16030 -0.04411 0.20513  106 ARG C O   
737  C CB  . ARG A 98  ? 1.30070 1.10204 2.08424 -0.15821 0.03992  0.18306  106 ARG C CB  
738  C CG  . ARG A 98  ? 1.29106 1.11596 2.07536 -0.14470 0.07512  0.16505  106 ARG C CG  
739  C CD  . ARG A 98  ? 1.27547 1.17235 2.10506 -0.14057 0.12409  0.15413  106 ARG C CD  
740  N NE  . ARG A 98  ? 1.26912 1.21529 2.19887 -0.13512 0.13369  0.14891  106 ARG C NE  
741  C CZ  . ARG A 98  ? 1.25890 1.27287 2.23298 -0.13125 0.17807  0.13200  106 ARG C CZ  
742  N NH1 . ARG A 98  ? 1.24703 1.29026 2.17412 -0.13413 0.21529  0.12328  106 ARG C NH1 
743  N NH2 . ARG A 98  ? 1.25275 1.31011 2.32323 -0.12529 0.18506  0.12300  106 ARG C NH2 
744  N N   . HIS A 99  ? 1.43626 1.13645 2.12722 -0.15579 -0.01608 0.18253  107 HIS C N   
745  C CA  . HIS A 99  ? 1.43587 1.12694 2.14669 -0.15026 -0.02557 0.18509  107 HIS C CA  
746  C C   . HIS A 99  ? 1.41676 1.13702 2.12536 -0.13668 0.02391  0.16403  107 HIS C C   
747  O O   . HIS A 99  ? 1.42627 1.13086 2.05195 -0.13624 0.04298  0.15244  107 HIS C O   
748  C CB  . HIS A 99  ? 1.47275 1.10883 2.10358 -0.16164 -0.06266 0.19439  107 HIS C CB  
749  C CG  . HIS A 99  ? 1.47305 1.09802 2.10116 -0.15687 -0.06307 0.19621  107 HIS C CG  
750  N ND1 . HIS A 99  ? 1.50483 1.09579 2.03962 -0.16434 -0.06931 0.19516  107 HIS C ND1 
751  C CD2 . HIS A 99  ? 1.44937 1.09306 2.16133 -0.14611 -0.05861 0.19888  107 HIS C CD2 
752  C CE1 . HIS A 99  ? 1.49638 1.08384 2.05626 -0.15995 -0.07040 0.20076  107 HIS C CE1 
753  N NE2 . HIS A 99  ? 1.46180 1.07844 2.13092 -0.14780 -0.06414 0.20184  107 HIS C NE2 
754  N N   . ALA A 100 ? 1.37397 1.13920 2.17479 -0.12639 0.04487  0.15700  108 ALA C N   
755  C CA  . ALA A 100 ? 1.36100 1.15854 2.16985 -0.11516 0.09130  0.13332  108 ALA C CA  
756  C C   . ALA A 100 ? 1.35638 1.13143 2.19342 -0.10860 0.07817  0.13291  108 ALA C C   
757  O O   . ALA A 100 ? 1.35774 1.11975 2.25943 -0.10830 0.04211  0.14960  108 ALA C O   
758  C CB  . ALA A 100 ? 1.35065 1.21863 2.24415 -0.10962 0.12692  0.11996  108 ALA C CB  
759  N N   . TRP A 101 ? 1.42460 1.19519 2.21663 -0.10426 0.10556  0.11602  109 TRP C N   
760  C CA  . TRP A 101 ? 1.42015 1.16364 2.23633 -0.10003 0.09080  0.11816  109 TRP C CA  
761  C C   . TRP A 101 ? 1.40429 1.18389 2.34569 -0.08652 0.10279  0.10467  109 TRP C C   
762  O O   . TRP A 101 ? 1.40130 1.15583 2.39824 -0.08238 0.07498  0.11542  109 TRP C O   
763  C CB  . TRP A 101 ? 1.41746 1.14862 2.15665 -0.10043 0.11769  0.10292  109 TRP C CB  
764  C CG  . TRP A 101 ? 1.44157 1.13174 2.06253 -0.11299 0.10090  0.11589  109 TRP C CG  
765  C CD1 . TRP A 101 ? 1.44945 1.14756 1.98546 -0.11578 0.12843  0.10415  109 TRP C CD1 
766  C CD2 . TRP A 101 ? 1.46632 1.10605 2.04303 -0.12528 0.05370  0.14172  109 TRP C CD2 
767  N NE1 . TRP A 101 ? 1.48214 1.13804 1.92709 -0.12713 0.10313  0.11695  109 TRP C NE1 
768  C CE2 . TRP A 101 ? 1.49538 1.11699 1.95919 -0.13483 0.05774  0.13979  109 TRP C CE2 
769  C CE3 . TRP A 101 ? 1.47041 1.08230 2.09386 -0.13042 0.00743  0.16751  109 TRP C CE3 
770  C CZ2 . TRP A 101 ? 1.53552 1.11627 1.92811 -0.15070 0.01994  0.15893  109 TRP C CZ2 
771  C CZ3 . TRP A 101 ? 1.50453 1.07540 2.05528 -0.14794 -0.03262 0.19156  109 TRP C CZ3 
772  C CH2 . TRP A 101 ? 1.54008 1.09749 1.97433 -0.15867 -0.02501 0.18543  109 TRP C CH2 
773  N N   . TYR A 102 ? 1.22379 1.06480 2.21412 -0.08040 0.14339  0.08140  110 TYR C N   
774  C CA  . TYR A 102 ? 1.21209 1.09586 2.32577 -0.06741 0.15904  0.06200  110 TYR C CA  
775  C C   . TYR A 102 ? 1.22152 1.09369 2.42303 -0.06470 0.11350  0.08635  110 TYR C C   
776  O O   . TYR A 102 ? 1.21061 1.09368 2.51618 -0.05198 0.11016  0.07716  110 TYR C O   
777  C CB  . TYR A 102 ? 1.20474 1.16611 2.35016 -0.06629 0.20910  0.03509  110 TYR C CB  
778  C CG  . TYR A 102 ? 1.18642 1.19780 2.46302 -0.05350 0.22557  0.01119  110 TYR C CG  
779  C CD1 . TYR A 102 ? 1.16888 1.19455 2.48642 -0.04288 0.25556  -0.02385 110 TYR C CD1 
780  C CD2 . TYR A 102 ? 1.18950 1.23377 2.55319 -0.05208 0.21058  0.02159  110 TYR C CD2 
781  C CE1 . TYR A 102 ? 1.15173 1.22273 2.59534 -0.02959 0.27162  -0.05144 110 TYR C CE1 
782  C CE2 . TYR A 102 ? 1.16028 1.25375 2.64967 -0.03899 0.22675  -0.00322 110 TYR C CE2 
783  C CZ  . TYR A 102 ? 1.14152 1.24818 2.67149 -0.02699 0.25802  -0.04148 110 TYR C CZ  
784  O OH  . TYR A 102 ? 1.09788 1.25499 2.75923 -0.01258 0.27592  -0.07196 110 TYR C OH  
785  N N   . TYR A 103 ? 1.26855 1.11892 2.43419 -0.07652 0.07738  0.11635  111 TYR C N   
786  C CA  . TYR A 103 ? 1.27893 1.11553 2.51697 -0.07759 0.02844  0.14417  111 TYR C CA  
787  C C   . TYR A 103 ? 1.28160 1.04965 2.46730 -0.08711 -0.02390 0.17580  111 TYR C C   
788  O O   . TYR A 103 ? 1.28825 1.03858 2.50583 -0.09434 -0.07195 0.20572  111 TYR C O   
789  C CB  . TYR A 103 ? 1.29223 1.15359 2.53316 -0.08780 0.01944  0.15718  111 TYR C CB  
790  C CG  . TYR A 103 ? 1.29040 1.22694 2.58646 -0.08268 0.06819  0.13172  111 TYR C CG  
791  C CD1 . TYR A 103 ? 1.28347 1.27250 2.70307 -0.06927 0.08559  0.11382  111 TYR C CD1 
792  C CD2 . TYR A 103 ? 1.29044 1.24900 2.51763 -0.09242 0.09647  0.12600  111 TYR C CD2 
793  C CE1 . TYR A 103 ? 1.26108 1.32777 2.72767 -0.06812 0.13184  0.08939  111 TYR C CE1 
794  C CE2 . TYR A 103 ? 1.28281 1.31620 2.55753 -0.09216 0.13942  0.10740  111 TYR C CE2 
795  C CZ  . TYR A 103 ? 1.25376 1.34358 2.64483 -0.08126 0.15784  0.08849  111 TYR C CZ  
796  O OH  . TYR A 103 ? 1.19161 1.36457 2.62759 -0.08431 0.20197  0.06886  111 TYR C OH  
797  N N   . GLY A 104 ? 1.46265 1.19654 2.56852 -0.08962 -0.01594 0.17096  112 GLY C N   
798  C CA  . GLY A 104 ? 1.46998 1.14599 2.52202 -0.10201 -0.06308 0.20150  112 GLY C CA  
799  C C   . GLY A 104 ? 1.49107 1.14211 2.44784 -0.12151 -0.09211 0.22156  112 GLY C C   
800  O O   . GLY A 104 ? 1.49500 1.16341 2.40434 -0.12423 -0.06863 0.20785  112 GLY C O   
801  N N   . TRP A 105 ? 1.68094 1.29151 2.61175 -0.13661 -0.14513 0.25455  113 TRP C N   
802  C CA  . TRP A 105 ? 1.71332 1.30105 2.56277 -0.15748 -0.17865 0.27189  113 TRP C CA  
803  C C   . TRP A 105 ? 1.71074 1.32044 2.62892 -0.15916 -0.19866 0.28153  113 TRP C C   
804  O O   . TRP A 105 ? 1.72168 1.32623 2.70470 -0.16484 -0.24392 0.30991  113 TRP C O   
805  C CB  . TRP A 105 ? 1.75212 1.29820 2.55222 -0.17703 -0.22910 0.30444  113 TRP C CB  
806  C CG  . TRP A 105 ? 1.76926 1.29400 2.46670 -0.18304 -0.21055 0.29503  113 TRP C CG  
807  C CD1 . TRP A 105 ? 1.75158 1.28911 2.40355 -0.17162 -0.15663 0.26195  113 TRP C CD1 
808  C CD2 . TRP A 105 ? 1.81124 1.30338 2.44250 -0.20344 -0.24577 0.32102  113 TRP C CD2 
809  N NE1 . TRP A 105 ? 1.78012 1.29370 2.34071 -0.18277 -0.15593 0.26436  113 TRP C NE1 
810  C CE2 . TRP A 105 ? 1.81780 1.30422 2.36333 -0.20293 -0.20944 0.30028  113 TRP C CE2 
811  C CE3 . TRP A 105 ? 1.84868 1.32014 2.48388 -0.22462 -0.30581 0.36235  113 TRP C CE3 
812  C CZ2 . TRP A 105 ? 1.86078 1.32269 2.32516 -0.22285 -0.22951 0.31828  113 TRP C CZ2 
813  C CZ3 . TRP A 105 ? 1.89298 1.34088 2.44589 -0.24579 -0.32665 0.38195  113 TRP C CZ3 
814  C CH2 . TRP A 105 ? 1.89838 1.34209 2.36670 -0.24485 -0.28786 0.35935  113 TRP C CH2 
815  N N   . GLY A 106 ? 1.42415 1.05933 2.33007 -0.15605 -0.16767 0.26129  114 GLY C N   
816  C CA  . GLY A 106 ? 1.41649 1.08017 2.39906 -0.15700 -0.18020 0.26890  114 GLY C CA  
817  C C   . GLY A 106 ? 1.40466 1.09058 2.35507 -0.15798 -0.14738 0.25016  114 GLY C C   
818  O O   . GLY A 106 ? 1.39067 1.08741 2.29438 -0.15039 -0.10258 0.22677  114 GLY C O   
819  N N   . LEU A 107 ? 1.35569 1.04945 2.33466 -0.16873 -0.17164 0.26292  115 LEU C N   
820  C CA  . LEU A 107 ? 1.34822 1.05642 2.29911 -0.17389 -0.15059 0.25220  115 LEU C CA  
821  C C   . LEU A 107 ? 1.31990 1.09088 2.37927 -0.16498 -0.12518 0.24891  115 LEU C C   
822  O O   . LEU A 107 ? 1.32231 1.11105 2.45707 -0.17103 -0.15277 0.26614  115 LEU C O   
823  C CB  . LEU A 107 ? 1.38191 1.05263 2.28275 -0.19538 -0.19565 0.26667  115 LEU C CB  
824  C CG  . LEU A 107 ? 1.41913 1.03987 2.19287 -0.20526 -0.20214 0.25673  115 LEU C CG  
825  C CD1 . LEU A 107 ? 1.44268 1.03682 2.17446 -0.20609 -0.21752 0.26266  115 LEU C CD1 
826  C CD2 . LEU A 107 ? 1.45948 1.05003 2.19617 -0.22711 -0.24384 0.26452  115 LEU C CD2 
827  N N   . ASP A 108 ? 1.35005 1.15939 2.41556 -0.15246 -0.07193 0.22640  116 ASP C N   
828  C CA  . ASP A 108 ? 1.34521 1.22403 2.49466 -0.14738 -0.03750 0.21813  116 ASP C CA  
829  C C   . ASP A 108 ? 1.34316 1.22366 2.45456 -0.16229 -0.03769 0.22594  116 ASP C C   
830  O O   . ASP A 108 ? 1.34810 1.17936 2.41050 -0.17543 -0.07725 0.24020  116 ASP C O   
831  C CB  . ASP A 108 ? 1.34416 1.26434 2.50365 -0.13267 0.01787  0.19022  116 ASP C CB  
832  C CG  . ASP A 108 ? 1.34030 1.23741 2.39137 -0.13375 0.04341  0.17774  116 ASP C CG  
833  O OD1 . ASP A 108 ? 1.33724 1.25873 2.36256 -0.14064 0.06586  0.17649  116 ASP C OD1 
834  O OD2 . ASP A 108 ? 1.34021 1.19594 2.33422 -0.12881 0.03917  0.17183  116 ASP C OD2 
835  N N   . TYR A 109 ? 1.38932 1.32702 2.52710 -0.16248 0.00314  0.21779  117 TYR C N   
836  C CA  . TYR A 109 ? 1.38361 1.33711 2.52525 -0.17825 -0.00109 0.23246  117 TYR C CA  
837  C C   . TYR A 109 ? 1.38899 1.27100 2.45760 -0.19099 -0.04389 0.24508  117 TYR C C   
838  O O   . TYR A 109 ? 1.39842 1.23170 2.37426 -0.18863 -0.04338 0.23505  117 TYR C O   
839  C CB  . TYR A 109 ? 1.37885 1.37108 2.48890 -0.17885 0.04695  0.22236  117 TYR C CB  
840  C CG  . TYR A 109 ? 1.36593 1.44052 2.53929 -0.17191 0.09524  0.20660  117 TYR C CG  
841  C CD1 . TYR A 109 ? 1.36328 1.44591 2.51971 -0.15679 0.12634  0.18103  117 TYR C CD1 
842  C CD2 . TYR A 109 ? 1.33817 1.48538 2.58302 -0.18308 0.11166  0.21574  117 TYR C CD2 
843  C CE1 . TYR A 109 ? 1.31883 1.47891 2.53061 -0.15213 0.17224  0.16079  117 TYR C CE1 
844  C CE2 . TYR A 109 ? 1.28443 1.51430 2.58263 -0.17953 0.15833  0.19740  117 TYR C CE2 
845  C CZ  . TYR A 109 ? 1.27039 1.50626 2.55169 -0.16374 0.18903  0.16778  117 TYR C CZ  
846  O OH  . TYR A 109 ? 1.19895 1.52030 2.53354 -0.16197 0.23672  0.14429  117 TYR C OH  
847  N N   . TRP A 110 ? 1.37156 1.24978 2.48467 -0.20512 -0.08122 0.26475  118 TRP C N   
848  C CA  . TRP A 110 ? 1.38331 1.19751 2.44089 -0.21998 -0.12698 0.27422  118 TRP C CA  
849  C C   . TRP A 110 ? 1.38057 1.19314 2.42224 -0.23339 -0.12334 0.28029  118 TRP C C   
850  O O   . TRP A 110 ? 1.36624 1.23244 2.44831 -0.23393 -0.09032 0.28431  118 TRP C O   
851  C CB  . TRP A 110 ? 1.38515 1.19391 2.50274 -0.22983 -0.17541 0.29313  118 TRP C CB  
852  C CG  . TRP A 110 ? 1.39953 1.17298 2.49262 -0.22443 -0.20124 0.29291  118 TRP C CG  
853  C CD1 . TRP A 110 ? 1.39516 1.18789 2.52144 -0.20709 -0.18452 0.28697  118 TRP C CD1 
854  C CD2 . TRP A 110 ? 1.42609 1.14036 2.45691 -0.23878 -0.24976 0.29994  118 TRP C CD2 
855  N NE1 . TRP A 110 ? 1.41192 1.15986 2.50292 -0.21000 -0.22159 0.29489  118 TRP C NE1 
856  C CE2 . TRP A 110 ? 1.43416 1.13687 2.46315 -0.23051 -0.26167 0.30318  118 TRP C CE2 
857  C CE3 . TRP A 110 ? 1.45216 1.12354 2.42927 -0.25952 -0.28468 0.30261  118 TRP C CE3 
858  C CZ2 . TRP A 110 ? 1.47522 1.13056 2.44714 -0.24448 -0.30760 0.31311  118 TRP C CZ2 
859  C CZ3 . TRP A 110 ? 1.50052 1.12564 2.41921 -0.27274 -0.32816 0.30649  118 TRP C CZ3 
860  C CH2 . TRP A 110 ? 1.51240 1.13248 2.42706 -0.26623 -0.33945 0.31373  118 TRP C CH2 
861  N N   . GLY A 111 ? 1.50838 1.26021 2.49275 -0.24600 -0.15884 0.28108  119 GLY C N   
862  C CA  . GLY A 111 ? 1.50906 1.24873 2.48552 -0.25957 -0.16328 0.28733  119 GLY C CA  
863  C C   . GLY A 111 ? 1.49177 1.26225 2.55605 -0.27687 -0.18736 0.31125  119 GLY C C   
864  O O   . GLY A 111 ? 1.47459 1.29252 2.61576 -0.27530 -0.18886 0.32206  119 GLY C O   
865  N N   . GLN A 112 ? 1.61628 1.35953 2.67328 -0.29366 -0.20682 0.31896  120 GLN C N   
866  C CA  . GLN A 112 ? 1.59834 1.36548 2.73380 -0.31412 -0.23326 0.34325  120 GLN C CA  
867  C C   . GLN A 112 ? 1.62407 1.33349 2.74126 -0.33174 -0.28934 0.34373  120 GLN C C   
868  O O   . GLN A 112 ? 1.61257 1.34394 2.79655 -0.34542 -0.31887 0.36218  120 GLN C O   
869  C CB  . GLN A 112 ? 1.58131 1.36906 2.73887 -0.32477 -0.21534 0.35760  120 GLN C CB  
870  C CG  . GLN A 112 ? 1.56867 1.39972 2.71116 -0.30906 -0.16045 0.35235  120 GLN C CG  
871  C CD  . GLN A 112 ? 1.54611 1.45332 2.74295 -0.29707 -0.12799 0.35153  120 GLN C CD  
872  O OE1 . GLN A 112 ? 1.52194 1.48666 2.80376 -0.30658 -0.13065 0.36830  120 GLN C OE1 
873  N NE2 . GLN A 112 ? 1.55489 1.46316 2.70541 -0.27627 -0.09709 0.32966  120 GLN C NE2 
874  N N   . GLY A 113 ? 1.69875 1.33896 2.72713 -0.33257 -0.30387 0.32208  121 GLY C N   
875  C CA  . GLY A 113 ? 1.74128 1.32605 2.73855 -0.35153 -0.35510 0.31582  121 GLY C CA  
876  C C   . GLY A 113 ? 1.76635 1.30060 2.73229 -0.36465 -0.36791 0.30483  121 GLY C C   
877  O O   . GLY A 113 ? 1.73988 1.29203 2.76469 -0.37590 -0.36751 0.32358  121 GLY C O   
878  N N   . THR A 114 ? 1.84036 1.31348 2.71781 -0.36395 -0.37861 0.27424  122 THR C N   
879  C CA  . THR A 114 ? 1.87471 1.29359 2.72625 -0.37554 -0.39374 0.25724  122 THR C CA  
880  C C   . THR A 114 ? 1.94114 1.30809 2.74398 -0.39576 -0.44148 0.23532  122 THR C C   
881  O O   . THR A 114 ? 1.98059 1.33439 2.71716 -0.39241 -0.44757 0.21765  122 THR C O   
882  C CB  . THR A 114 ? 1.88561 1.28244 2.68000 -0.35519 -0.35608 0.23442  122 THR C CB  
883  O OG1 . THR A 114 ? 1.92292 1.26457 2.70312 -0.36489 -0.37258 0.21619  122 THR C OG1 
884  C CG2 . THR A 114 ? 1.92193 1.30310 2.62928 -0.34054 -0.34419 0.20728  122 THR C CG2 
885  N N   . LEU A 115 ? 1.92426 1.26567 2.76120 -0.41959 -0.47650 0.23806  123 LEU C N   
886  C CA  . LEU A 115 ? 1.98686 1.28894 2.78965 -0.44476 -0.52602 0.22038  123 LEU C CA  
887  C C   . LEU A 115 ? 2.05768 1.29395 2.78065 -0.44660 -0.52989 0.17308  123 LEU C C   
888  O O   . LEU A 115 ? 2.05447 1.26343 2.79141 -0.44153 -0.51626 0.16260  123 LEU C O   
889  C CB  . LEU A 115 ? 1.96960 1.27938 2.85246 -0.47219 -0.56409 0.24541  123 LEU C CB  
890  C CG  . LEU A 115 ? 2.02257 1.31313 2.88728 -0.50152 -0.61875 0.23884  123 LEU C CG  
891  C CD1 . LEU A 115 ? 2.04410 1.35517 2.86205 -0.49553 -0.62318 0.23976  123 LEU C CD1 
892  C CD2 . LEU A 115 ? 1.98469 1.30637 2.94614 -0.52424 -0.64940 0.27557  123 LEU C CD2 
893  N N   . VAL A 116 ? 2.03431 1.24796 2.67741 -0.45507 -0.54947 0.14499  124 VAL C N   
894  C CA  . VAL A 116 ? 2.11349 1.27103 2.67658 -0.45946 -0.55440 0.09347  124 VAL C CA  
895  C C   . VAL A 116 ? 2.18159 1.31513 2.71677 -0.49450 -0.60745 0.07631  124 VAL C C   
896  O O   . VAL A 116 ? 2.20149 1.35947 2.71144 -0.50725 -0.63007 0.08927  124 VAL C O   
897  C CB  . VAL A 116 ? 2.14293 1.30245 2.62031 -0.43785 -0.52118 0.06939  124 VAL C CB  
898  C CG1 . VAL A 116 ? 2.23622 1.34599 2.62847 -0.44708 -0.53078 0.01260  124 VAL C CG1 
899  C CG2 . VAL A 116 ? 2.08276 1.26176 2.58451 -0.40560 -0.46976 0.08117  124 VAL C CG2 
900  N N   . THR A 117 ? 2.15993 1.24594 2.70160 -0.51109 -0.62840 0.04758  125 THR C N   
901  C CA  . THR A 117 ? 2.22606 1.28591 2.74349 -0.54769 -0.67917 0.02524  125 THR C CA  
902  C C   . THR A 117 ? 2.31446 1.32346 2.74619 -0.55117 -0.67706 -0.04128 125 THR C C   
903  O O   . THR A 117 ? 2.31729 1.28809 2.76233 -0.53676 -0.65676 -0.06836 125 THR C O   
904  C CB  . THR A 117 ? 2.19599 1.24375 2.80249 -0.56913 -0.70999 0.04514  125 THR C CB  
905  O OG1 . THR A 117 ? 2.11514 1.21837 2.80384 -0.56658 -0.71011 0.10500  125 THR C OG1 
906  C CG2 . THR A 117 ? 2.27190 1.29288 2.84871 -0.60920 -0.76331 0.01853  125 THR C CG2 
907  N N   . VAL A 118 ? 2.34523 1.35658 2.69379 -0.57184 -0.69941 -0.06697 126 VAL C N   
908  C CA  . VAL A 118 ? 2.43671 1.41033 2.69609 -0.57950 -0.69805 -0.13496 126 VAL C CA  
909  C C   . VAL A 118 ? 2.49219 1.43657 2.75151 -0.62057 -0.74895 -0.16204 126 VAL C C   
910  O O   . VAL A 118 ? 2.53604 1.50113 2.75370 -0.65260 -0.78615 -0.15881 126 VAL C O   
911  C CB  . VAL A 118 ? 2.48521 1.48787 2.64536 -0.57866 -0.68676 -0.14658 126 VAL C CB  
912  C CG1 . VAL A 118 ? 2.57683 1.54791 2.64616 -0.58584 -0.67962 -0.22073 126 VAL C CG1 
913  C CG2 . VAL A 118 ? 2.42188 1.45677 2.59246 -0.54087 -0.64053 -0.11278 126 VAL C CG2 
914  N N   . SER A 119 ? 2.53170 1.42750 2.84055 -0.62139 -0.75259 -0.18785 127 SER C N   
915  C CA  . SER A 119 ? 2.58265 1.44470 2.89576 -0.66052 -0.79971 -0.21938 127 SER C CA  
916  C C   . SER A 119 ? 2.61364 1.41111 2.93822 -0.65234 -0.78821 -0.27898 127 SER C C   
917  O O   . SER A 119 ? 2.56174 1.34136 2.94209 -0.62044 -0.75587 -0.26800 127 SER C O   
918  C CB  . SER A 119 ? 2.53407 1.41174 2.94170 -0.68072 -0.83555 -0.16245 127 SER C CB  
919  O OG  . SER A 119 ? 2.59906 1.45447 3.02076 -0.70249 -0.86107 -0.19066 127 SER C OG  
920  N N   . SER A 120 ? 2.66363 1.43383 2.93807 -0.67967 -0.81212 -0.34042 128 SER C N   
921  C CA  . SER A 120 ? 2.72372 1.44451 3.00909 -0.66691 -0.79398 -0.40140 128 SER C CA  
922  C C   . SER A 120 ? 2.73968 1.44524 3.11833 -0.66985 -0.80604 -0.38002 128 SER C C   
923  O O   . SER A 120 ? 2.78770 1.45051 3.19245 -0.65800 -0.79198 -0.42136 128 SER C O   
924  C CB  . SER A 120 ? 2.82807 1.53584 3.01640 -0.69258 -0.80572 -0.48283 128 SER C CB  
925  O OG  . SER A 120 ? 2.89592 1.61140 3.08656 -0.73085 -0.84516 -0.48908 128 SER C OG  
926  N N   . ALA A 121 ? 2.70298 1.44416 3.13375 -0.68506 -0.83160 -0.31581 129 ALA C N   
927  C CA  . ALA A 121 ? 2.71061 1.44456 3.23127 -0.68771 -0.84281 -0.28660 129 ALA C CA  
928  C C   . ALA A 121 ? 2.64337 1.36929 3.23877 -0.64949 -0.80643 -0.25254 129 ALA C C   
929  O O   . ALA A 121 ? 2.57874 1.31339 3.16264 -0.62213 -0.77434 -0.24106 129 ALA C O   
930  C CB  . ALA A 121 ? 2.68352 1.46667 3.24014 -0.71182 -0.87713 -0.22502 129 ALA C CB  
931  N N   . SER A 122 ? 2.66241 1.37400 3.33368 -0.64956 -0.81276 -0.23480 130 SER C N   
932  C CA  . SER A 122 ? 2.61407 1.31916 3.35605 -0.61784 -0.78268 -0.20314 130 SER C CA  
933  C C   . SER A 122 ? 2.53562 1.29628 3.35160 -0.61709 -0.78581 -0.12034 130 SER C C   
934  O O   . SER A 122 ? 2.54287 1.33275 3.37742 -0.64273 -0.81692 -0.09296 130 SER C O   
935  C CB  . SER A 122 ? 2.69287 1.34418 3.47198 -0.61645 -0.78563 -0.23894 130 SER C CB  
936  O OG  . SER A 122 ? 2.65749 1.29458 3.47985 -0.58184 -0.75213 -0.22592 130 SER C OG  
937  N N   . THR A 123 ? 2.46196 1.24173 3.31961 -0.58778 -0.75223 -0.08182 131 THR C N   
938  C CA  . THR A 123 ? 2.38486 1.22508 3.31201 -0.58477 -0.74769 -0.00670 131 THR C CA  
939  C C   . THR A 123 ? 2.42427 1.26599 3.42013 -0.60357 -0.77493 0.01834  131 THR C C   
940  O O   . THR A 123 ? 2.48499 1.28030 3.50418 -0.60250 -0.77931 -0.00521 131 THR C O   
941  C CB  . THR A 123 ? 2.31439 1.17098 3.26975 -0.55211 -0.70567 0.02146  131 THR C CB  
942  O OG1 . THR A 123 ? 2.30646 1.13802 3.19439 -0.53345 -0.68112 -0.02005 131 THR C OG1 
943  C CG2 . THR A 123 ? 2.22180 1.15428 3.22087 -0.54847 -0.69284 0.08934  131 THR C CG2 
944  N N   . LYS A 124 ? 2.39301 1.28840 3.42393 -0.62089 -0.79414 0.06569  132 LYS C N   
945  C CA  . LYS A 124 ? 2.42243 1.32983 3.52149 -0.63998 -0.82025 0.09715  132 LYS C CA  
946  C C   . LYS A 124 ? 2.33832 1.31832 3.50652 -0.63229 -0.80535 0.16898  132 LYS C C   
947  O O   . LYS A 124 ? 2.27346 1.30836 3.43856 -0.63009 -0.79772 0.19703  132 LYS C O   
948  C CB  . LYS A 124 ? 2.47808 1.38579 3.55749 -0.67340 -0.86280 0.08353  132 LYS C CB  
949  N N   . GLY A 125 ? 2.34354 1.32619 3.57575 -0.62954 -0.80198 0.19797  133 GLY C N   
950  C CA  . GLY A 125 ? 2.27611 1.33130 3.57604 -0.62755 -0.79035 0.26432  133 GLY C CA  
951  C C   . GLY A 125 ? 2.27901 1.38029 3.61749 -0.65309 -0.82055 0.29681  133 GLY C C   
952  O O   . GLY A 125 ? 2.34996 1.41910 3.68011 -0.67614 -0.85671 0.27427  133 GLY C O   
953  N N   . PRO A 126 ? 2.20419 1.38428 3.58774 -0.64989 -0.80539 0.34941  134 PRO C N   
954  C CA  . PRO A 126 ? 2.19890 1.43236 3.62536 -0.67119 -0.83056 0.38314  134 PRO C CA  
955  C C   . PRO A 126 ? 2.23060 1.47960 3.72796 -0.68832 -0.84828 0.41927  134 PRO C C   
956  O O   . PRO A 126 ? 2.25144 1.47545 3.77017 -0.68332 -0.84050 0.42426  134 PRO C O   
957  C CB  . PRO A 126 ? 2.10238 1.41443 3.54706 -0.65583 -0.79876 0.41821  134 PRO C CB  
958  C CG  . PRO A 126 ? 2.06311 1.37972 3.51438 -0.63446 -0.75990 0.42886  134 PRO C CG  
959  C CD  . PRO A 126 ? 2.12178 1.34965 3.52073 -0.62658 -0.76225 0.37912  134 PRO C CD  
960  N N   . SER A 127 ? 2.23819 1.52871 3.77345 -0.70955 -0.87472 0.44553  135 SER C N   
961  C CA  . SER A 127 ? 2.25391 1.57985 3.86284 -0.72680 -0.88882 0.49032  135 SER C CA  
962  C C   . SER A 127 ? 2.19059 1.61019 3.84819 -0.73067 -0.88215 0.53692  135 SER C C   
963  O O   . SER A 127 ? 2.16780 1.60957 3.80743 -0.73042 -0.88808 0.52951  135 SER C O   
964  C CB  . SER A 127 ? 2.35058 1.62474 3.96569 -0.75415 -0.93428 0.47249  135 SER C CB  
965  O OG  . SER A 127 ? 2.37285 1.64618 3.95976 -0.76913 -0.96176 0.45376  135 SER C OG  
966  N N   . VAL A 128 ? 2.16503 1.64158 3.88618 -0.73454 -0.86975 0.58504  136 VAL C N   
967  C CA  . VAL A 128 ? 2.10465 1.67690 3.87853 -0.73691 -0.85649 0.62874  136 VAL C CA  
968  C C   . VAL A 128 ? 2.14810 1.74803 3.98465 -0.76422 -0.88564 0.66463  136 VAL C C   
969  O O   . VAL A 128 ? 2.17584 1.77056 4.04298 -0.77279 -0.88721 0.68707  136 VAL C O   
970  C CB  . VAL A 128 ? 2.02895 1.65989 3.81952 -0.71789 -0.80812 0.65476  136 VAL C CB  
971  C CG1 . VAL A 128 ? 1.97502 1.70831 3.82509 -0.72241 -0.79275 0.69629  136 VAL C CG1 
972  C CG2 . VAL A 128 ? 1.98715 1.59114 3.71620 -0.69176 -0.77994 0.61967  136 VAL C CG2 
973  N N   . PHE A 129 ? 2.15514 1.78654 4.01310 -0.77813 -0.90941 0.67265  137 PHE C N   
974  C CA  . PHE A 129 ? 2.18969 1.85876 4.11137 -0.80382 -0.93365 0.71085  137 PHE C CA  
975  C C   . PHE A 129 ? 2.12470 1.89942 4.10437 -0.80194 -0.91081 0.75260  137 PHE C C   
976  O O   . PHE A 129 ? 2.06978 1.88014 4.04176 -0.78600 -0.89365 0.74467  137 PHE C O   
977  C CB  . PHE A 129 ? 2.26236 1.89119 4.17645 -0.82722 -0.98321 0.69340  137 PHE C CB  
978  C CG  . PHE A 129 ? 2.32310 1.85336 4.16838 -0.82781 -1.00351 0.63937  137 PHE C CG  
979  C CD1 . PHE A 129 ? 2.37977 1.84416 4.21532 -0.83213 -1.01009 0.62377  137 PHE C CD1 
980  C CD2 . PHE A 129 ? 2.32923 1.83434 4.12178 -0.82549 -1.01712 0.60391  137 PHE C CD2 
981  C CE1 . PHE A 129 ? 2.44045 1.81590 4.21494 -0.83269 -1.02603 0.56881  137 PHE C CE1 
982  C CE2 . PHE A 129 ? 2.39032 1.80915 4.11578 -0.82864 -1.03403 0.55106  137 PHE C CE2 
983  C CZ  . PHE A 129 ? 2.44616 1.80001 4.16282 -0.83176 -1.03690 0.53100  137 PHE C CZ  
984  N N   . PRO A 130 ? 2.13305 1.95976 4.17239 -0.81821 -0.90956 0.79612  138 PRO C N   
985  C CA  . PRO A 130 ? 2.07872 2.01030 4.17545 -0.81847 -0.88579 0.83282  138 PRO C CA  
986  C C   . PRO A 130 ? 2.09173 2.04651 4.21351 -0.82882 -0.91449 0.83332  138 PRO C C   
987  O O   . PRO A 130 ? 2.15804 2.06051 4.26947 -0.84714 -0.95869 0.82158  138 PRO C O   
988  C CB  . PRO A 130 ? 2.10550 2.07345 4.25154 -0.83911 -0.88539 0.87668  138 PRO C CB  
989  C CG  . PRO A 130 ? 2.19180 2.07308 4.32325 -0.85756 -0.92935 0.86529  138 PRO C CG  
990  C CD  . PRO A 130 ? 2.20095 1.99294 4.26088 -0.83950 -0.93312 0.81297  138 PRO C CD  
991  N N   . LEU A 131 ? 2.03076 2.06709 4.18867 -0.81740 -0.88880 0.84683  139 LEU C N   
992  C CA  . LEU A 131 ? 2.03634 2.11513 4.23654 -0.82592 -0.91118 0.85704  139 LEU C CA  
993  C C   . LEU A 131 ? 2.01180 2.19210 4.28647 -0.83443 -0.88679 0.89868  139 LEU C C   
994  O O   . LEU A 131 ? 1.94737 2.20168 4.24990 -0.81700 -0.84624 0.90376  139 LEU C O   
995  C CB  . LEU A 131 ? 1.99084 2.07324 4.17075 -0.80268 -0.90324 0.83197  139 LEU C CB  
996  C CG  . LEU A 131 ? 2.00635 1.99488 4.10238 -0.79188 -0.91476 0.78893  139 LEU C CG  
997  C CD1 . LEU A 131 ? 1.96042 1.95912 4.03952 -0.76990 -0.90627 0.76940  139 LEU C CD1 
998  C CD2 . LEU A 131 ? 2.09349 2.00529 4.15730 -0.81615 -0.96714 0.77345  139 LEU C CD2 
999  N N   . ALA A 132 ? 2.06770 2.25017 4.37255 -0.86216 -0.91063 0.92587  140 ALA C N   
1000 C CA  . ALA A 132 ? 2.05649 2.32897 4.42272 -0.87512 -0.88729 0.96652  140 ALA C CA  
1001 C C   . ALA A 132 ? 2.02813 2.38830 4.45558 -0.87360 -0.87963 0.97887  140 ALA C C   
1002 O O   . ALA A 132 ? 2.05591 2.39905 4.49500 -0.87971 -0.91627 0.97311  140 ALA C O   
1003 C CB  . ALA A 132 ? 2.13209 2.37799 4.51567 -0.90716 -0.92179 0.99259  140 ALA C CB  
1004 N N   . PRO A 133 ? 1.97758 2.43557 4.44692 -0.86665 -0.83250 0.99528  141 PRO C N   
1005 C CA  . PRO A 133 ? 1.95547 2.50374 4.49273 -0.86522 -0.82229 1.00560  141 PRO C CA  
1006 C C   . PRO A 133 ? 2.01262 2.59460 4.60244 -0.89785 -0.85080 1.04014  141 PRO C C   
1007 O O   . PRO A 133 ? 2.06232 2.60548 4.63622 -0.92041 -0.87040 1.05803  141 PRO C O   
1008 C CB  . PRO A 133 ? 1.89137 2.52927 4.44746 -0.84957 -0.75881 1.00586  141 PRO C CB  
1009 C CG  . PRO A 133 ? 1.90403 2.51896 4.42129 -0.86002 -0.74507 1.01865  141 PRO C CG  
1010 C CD  . PRO A 133 ? 1.94232 2.43481 4.39743 -0.86036 -0.78549 1.00279  141 PRO C CD  
1011 N N   . SER A 135 ? 2.14946 2.84453 4.93595 -0.96225 -0.96788 1.10476  143 SER C N   
1012 C CA  . SER A 135 ? 2.14491 2.93587 5.01438 -0.96597 -0.96328 1.12234  143 SER C CA  
1013 C C   . SER A 135 ? 2.10011 2.90831 4.98856 -0.93464 -0.95758 1.09970  143 SER C C   
1014 O O   . SER A 135 ? 2.06866 2.97031 5.02738 -0.92308 -0.93065 1.10357  143 SER C O   
1015 C CB  . SER A 135 ? 2.22138 2.99855 5.11811 -1.00064 -1.01645 1.14828  143 SER C CB  
1016 O OG  . SER A 135 ? 2.26164 2.94225 5.10998 -1.00409 -1.06813 1.13217  143 SER C OG  
1017 N N   . LYS A 136 ? 2.18307 2.90207 5.01069 -0.92126 -0.98360 1.07526  144 LYS C N   
1018 C CA  . LYS A 136 ? 2.14126 2.87018 4.98179 -0.89073 -0.97881 1.05551  144 LYS C CA  
1019 C C   . LYS A 136 ? 2.06400 2.84114 4.90972 -0.85865 -0.91655 1.03602  144 LYS C C   
1020 O O   . LYS A 136 ? 2.02380 2.86621 4.92610 -0.83543 -0.89341 1.02910  144 LYS C O   
1021 C CB  . LYS A 136 ? 2.16807 2.79090 4.93532 -0.88851 -1.02313 1.03486  144 LYS C CB  
1022 N N   . SER A 137 ? 2.10326 2.84825 4.89170 -0.85653 -0.88943 1.02570  145 SER C N   
1023 C CA  . SER A 137 ? 2.04538 2.84308 4.83699 -0.83065 -0.82782 1.00860  145 SER C CA  
1024 C C   . SER A 137 ? 2.03015 2.94497 4.89026 -0.83829 -0.78522 1.02472  145 SER C C   
1025 O O   . SER A 137 ? 1.98452 2.96498 4.86303 -0.81688 -0.73190 1.00748  145 SER C O   
1026 C CB  . SER A 137 ? 2.03362 2.76272 4.74274 -0.82806 -0.81391 0.99514  145 SER C CB  
1027 O OG  . SER A 137 ? 2.05365 2.79256 4.75633 -0.85447 -0.80875 1.01862  145 SER C OG  
1028 N N   . THR A 138 ? 1.95463 2.89994 4.85212 -0.86947 -0.80702 1.05517  146 THR C N   
1029 C CA  . THR A 138 ? 1.94847 3.01148 4.91405 -0.88038 -0.77001 1.07065  146 THR C CA  
1030 C C   . THR A 138 ? 1.92126 3.06883 4.96909 -0.86021 -0.75437 1.05964  146 THR C C   
1031 O O   . THR A 138 ? 1.91674 3.17139 5.02977 -0.86694 -0.72262 1.06623  146 THR C O   
1032 C CB  . THR A 138 ? 2.01635 3.07946 4.99672 -0.92108 -0.80368 1.10795  146 THR C CB  
1033 O OG1 . THR A 138 ? 2.04639 3.01748 4.95299 -0.93599 -0.82436 1.11498  146 THR C OG1 
1034 C CG2 . THR A 138 ? 2.01507 3.19584 5.04974 -0.93786 -0.76260 1.12570  146 THR C CG2 
1035 N N   . SER A 139 ? 1.93844 3.04237 4.98560 -0.83488 -0.77476 1.04157  147 SER C N   
1036 C CA  . SER A 139 ? 1.91186 3.08783 5.03895 -0.81041 -0.76058 1.02946  147 SER C CA  
1037 C C   . SER A 139 ? 1.84398 3.05784 4.97176 -0.77477 -0.70316 0.99391  147 SER C C   
1038 O O   . SER A 139 ? 1.81696 2.96671 4.90514 -0.75019 -0.70845 0.97369  147 SER C O   
1039 C CB  . SER A 139 ? 1.93730 3.04789 5.06832 -0.80361 -0.81760 1.03348  147 SER C CB  
1040 O OG  . SER A 139 ? 1.90878 2.93984 4.97712 -0.77980 -0.82195 1.00993  147 SER C OG  
1041 N N   . THR A 142 ? 1.68284 2.98340 4.70262 -0.74904 -0.53993 0.93329  150 THR C N   
1042 C CA  . THR A 142 ? 1.65583 2.86440 4.59517 -0.73216 -0.54092 0.91705  150 THR C CA  
1043 C C   . THR A 142 ? 1.69706 2.78408 4.58102 -0.74631 -0.60446 0.93713  150 THR C C   
1044 O O   . THR A 142 ? 1.72702 2.78405 4.63922 -0.74906 -0.65092 0.94789  150 THR C O   
1045 C CB  . THR A 142 ? 1.60669 2.81892 4.56636 -0.69156 -0.52088 0.88123  150 THR C CB  
1046 O OG1 . THR A 142 ? 1.57910 2.91122 4.60776 -0.67834 -0.46770 0.85896  150 THR C OG1 
1047 C CG2 . THR A 142 ? 1.57134 2.71571 4.44931 -0.67533 -0.50399 0.86068  150 THR C CG2 
1048 N N   . ALA A 143 ? 1.69926 2.71873 4.50418 -0.75559 -0.60605 0.94016  151 ALA C N   
1049 C CA  . ALA A 143 ? 1.74391 2.64980 4.49152 -0.77059 -0.66226 0.95297  151 ALA C CA  
1050 C C   . ALA A 143 ? 1.71831 2.53559 4.40180 -0.74651 -0.67063 0.92578  151 ALA C C   
1051 O O   . ALA A 143 ? 1.66655 2.50019 4.33111 -0.72322 -0.62784 0.90235  151 ALA C O   
1052 C CB  . ALA A 143 ? 1.77930 2.66590 4.48865 -0.79970 -0.66474 0.97673  151 ALA C CB  
1053 N N   . LEU A 145 ? 1.76071 2.29740 4.21418 -0.76220 -0.72554 0.90758  153 LEU C N   
1054 C CA  . LEU A 145 ? 1.79645 2.23931 4.18009 -0.77179 -0.74710 0.90237  153 LEU C CA  
1055 C C   . LEU A 145 ? 1.76701 2.14283 4.08431 -0.74756 -0.73953 0.86752  153 LEU C C   
1056 O O   . LEU A 145 ? 1.70877 2.12078 4.03133 -0.72302 -0.70433 0.85138  153 LEU C O   
1057 C CB  . LEU A 145 ? 1.80265 2.27266 4.18355 -0.78601 -0.72121 0.92483  153 LEU C CB  
1058 C CG  . LEU A 145 ? 1.74546 2.29281 4.13267 -0.77360 -0.65956 0.92623  153 LEU C CG  
1059 C CD1 . LEU A 145 ? 1.70510 2.20505 4.02921 -0.74930 -0.63506 0.89783  153 LEU C CD1 
1060 C CD2 . LEU A 145 ? 1.77499 2.36060 4.17542 -0.79910 -0.65008 0.96088  153 LEU C CD2 
1061 N N   . GLY A 146 ? 2.01957 1.99665 3.70742 -0.27186 -0.72381 0.40214  154 GLY C N   
1062 C CA  . GLY A 146 ? 2.05487 1.95529 3.64252 -0.25947 -0.72135 0.38191  154 GLY C CA  
1063 C C   . GLY A 146 ? 2.03490 1.87424 3.54626 -0.28363 -0.73248 0.37098  154 GLY C C   
1064 O O   . GLY A 146 ? 2.00451 1.85302 3.53035 -0.30798 -0.73818 0.37999  154 GLY C O   
1065 N N   . CYS A 147 ? 1.98300 1.75669 3.41097 -0.27683 -0.73239 0.34949  155 CYS C N   
1066 C CA  . CYS A 147 ? 1.96530 1.67804 3.31743 -0.29344 -0.74154 0.33189  155 CYS C CA  
1067 C C   . CYS A 147 ? 2.00090 1.64675 3.28722 -0.29901 -0.77094 0.32376  155 CYS C C   
1068 O O   . CYS A 147 ? 2.04911 1.67969 3.32185 -0.28355 -0.76817 0.32250  155 CYS C O   
1069 C CB  . CYS A 147 ? 1.95404 1.65528 3.26685 -0.27857 -0.70049 0.30359  155 CYS C CB  
1070 S SG  . CYS A 147 ? 1.93538 1.66351 3.26639 -0.28149 -0.68216 0.30704  155 CYS C SG  
1071 N N   . LEU A 148 ? 2.02343 1.61934 3.25807 -0.32059 -0.79720 0.31736  156 LEU C N   
1072 C CA  . LEU A 148 ? 2.06533 1.58547 3.22066 -0.32859 -0.82194 0.30725  156 LEU C CA  
1073 C C   . LEU A 148 ? 2.05204 1.52146 3.13344 -0.33347 -0.80128 0.27369  156 LEU C C   
1074 O O   . LEU A 148 ? 2.02474 1.48994 3.10131 -0.34438 -0.80967 0.26893  156 LEU C O   
1075 C CB  . LEU A 148 ? 2.08021 1.58283 3.24014 -0.34988 -0.87956 0.32822  156 LEU C CB  
1076 C CG  . LEU A 148 ? 2.12374 1.53322 3.18230 -0.36407 -0.90760 0.31513  156 LEU C CG  
1077 C CD1 . LEU A 148 ? 2.19646 1.55015 3.18856 -0.35055 -0.89990 0.30709  156 LEU C CD1 
1078 C CD2 . LEU A 148 ? 2.13849 1.53814 3.21098 -0.38566 -0.96818 0.33525  156 LEU C CD2 
1079 N N   . VAL A 149 ? 2.06345 1.49452 3.08969 -0.32528 -0.77275 0.24851  157 VAL C N   
1080 C CA  . VAL A 149 ? 2.06471 1.45430 3.02906 -0.32967 -0.74957 0.20963  157 VAL C CA  
1081 C C   . VAL A 149 ? 2.12381 1.42879 3.00055 -0.34706 -0.77007 0.20347  157 VAL C C   
1082 O O   . VAL A 149 ? 2.17797 1.44012 3.00852 -0.34704 -0.76015 0.20228  157 VAL C O   
1083 C CB  . VAL A 149 ? 2.05944 1.46841 3.02710 -0.31402 -0.69694 0.17883  157 VAL C CB  
1084 C CG1 . VAL A 149 ? 2.07419 1.44326 2.98416 -0.32092 -0.67350 0.13300  157 VAL C CG1 
1085 C CG2 . VAL A 149 ? 2.01311 1.49526 3.05272 -0.29576 -0.67973 0.18157  157 VAL C CG2 
1086 N N   . LYS A 150 ? 2.16983 1.44113 3.01383 -0.36177 -0.79778 0.19912  158 LYS C N   
1087 C CA  . LYS A 150 ? 2.23093 1.41838 2.98936 -0.37971 -0.82676 0.19794  158 LYS C CA  
1088 C C   . LYS A 150 ? 2.25278 1.39385 2.94639 -0.38601 -0.80416 0.15595  158 LYS C C   
1089 O O   . LYS A 150 ? 2.21635 1.39199 2.94127 -0.37747 -0.78985 0.13522  158 LYS C O   
1090 C CB  . LYS A 150 ? 2.23127 1.41519 3.00808 -0.39375 -0.88712 0.22998  158 LYS C CB  
1091 N N   . ASP A 151 ? 2.37498 1.43339 2.97393 -0.39916 -0.80119 0.14208  159 ASP C N   
1092 C CA  . ASP A 151 ? 2.40877 1.41379 2.93806 -0.40811 -0.78268 0.10166  159 ASP C CA  
1093 C C   . ASP A 151 ? 2.38049 1.43313 2.94436 -0.39524 -0.72585 0.05621  159 ASP C C   
1094 O O   . ASP A 151 ? 2.34915 1.42958 2.94090 -0.38507 -0.72559 0.03293  159 ASP C O   
1095 C CB  . ASP A 151 ? 2.39451 1.38019 2.91520 -0.41503 -0.82871 0.10803  159 ASP C CB  
1096 C CG  . ASP A 151 ? 2.45159 1.36159 2.90315 -0.43368 -0.88022 0.13368  159 ASP C CG  
1097 O OD1 . ASP A 151 ? 2.52712 1.37500 2.90488 -0.44064 -0.87399 0.13466  159 ASP C OD1 
1098 O OD2 . ASP A 151 ? 2.43277 1.33920 2.89835 -0.44216 -0.92832 0.15211  159 ASP C OD2 
1099 N N   . TYR A 152 ? 2.30290 1.36195 2.86415 -0.39485 -0.68033 0.04235  160 TYR C N   
1100 C CA  . TYR A 152 ? 2.28705 1.38949 2.88038 -0.38701 -0.62470 -0.00678 160 TYR C CA  
1101 C C   . TYR A 152 ? 2.37103 1.41308 2.88957 -0.40756 -0.57456 -0.03754 160 TYR C C   
1102 O O   . TYR A 152 ? 2.43744 1.41193 2.88798 -0.42176 -0.57822 -0.01202 160 TYR C O   
1103 C CB  . TYR A 152 ? 2.22112 1.40909 2.90675 -0.36689 -0.61180 0.00251  160 TYR C CB  
1104 C CG  . TYR A 152 ? 2.24880 1.42996 2.92962 -0.37053 -0.58684 0.01732  160 TYR C CG  
1105 C CD1 . TYR A 152 ? 2.28527 1.45587 2.94628 -0.38017 -0.52996 -0.02121 160 TYR C CD1 
1106 C CD2 . TYR A 152 ? 2.24594 1.43036 2.94416 -0.36448 -0.62018 0.06787  160 TYR C CD2 
1107 C CE1 . TYR A 152 ? 2.32118 1.47276 2.96819 -0.38390 -0.50796 -0.00665 160 TYR C CE1 
1108 C CE2 . TYR A 152 ? 2.28267 1.45385 2.97229 -0.36269 -0.60117 0.08106  160 TYR C CE2 
1109 C CZ  . TYR A 152 ? 2.32155 1.47035 2.97967 -0.37250 -0.54544 0.04519  160 TYR C CZ  
1110 O OH  . TYR A 152 ? 2.36804 1.49074 3.00748 -0.37140 -0.52652 0.05861  160 TYR C OH  
1111 N N   . PHE A 153 ? 2.24319 1.30777 2.77363 -0.40888 -0.52744 -0.09485 161 PHE C N   
1112 C CA  . PHE A 153 ? 2.32718 1.34360 2.79649 -0.43353 -0.46694 -0.13419 161 PHE C CA  
1113 C C   . PHE A 153 ? 2.29010 1.38474 2.83429 -0.42549 -0.41953 -0.19758 161 PHE C C   
1114 O O   . PHE A 153 ? 2.23531 1.38187 2.83354 -0.40291 -0.44032 -0.21900 161 PHE C O   
1115 C CB  . PHE A 153 ? 2.42279 1.33934 2.77989 -0.45534 -0.46910 -0.14194 161 PHE C CB  
1116 C CG  . PHE A 153 ? 2.52159 1.38879 2.81411 -0.48408 -0.39677 -0.19060 161 PHE C CG  
1117 C CD1 . PHE A 153 ? 2.61345 1.39477 2.81485 -0.50969 -0.36939 -0.17334 161 PHE C CD1 
1118 C CD2 . PHE A 153 ? 2.53180 1.43385 2.85158 -0.48574 -0.35545 -0.25507 161 PHE C CD2 
1119 C CE1 . PHE A 153 ? 2.71208 1.43904 2.84575 -0.54226 -0.29612 -0.21774 161 PHE C CE1 
1120 C CE2 . PHE A 153 ? 2.62978 1.49209 2.89725 -0.51692 -0.28195 -0.30325 161 PHE C CE2 
1121 C CZ  . PHE A 153 ? 2.71797 1.48986 2.88900 -0.54824 -0.24945 -0.28361 161 PHE C CZ  
1122 N N   . PRO A 154 ? 2.28366 1.38739 2.83418 -0.44229 -0.35932 -0.22990 162 PRO C N   
1123 C CA  . PRO A 154 ? 2.35636 1.39398 2.84146 -0.46675 -0.33170 -0.20649 162 PRO C CA  
1124 C C   . PRO A 154 ? 2.28863 1.38080 2.84166 -0.44780 -0.34557 -0.17499 162 PRO C C   
1125 O O   . PRO A 154 ? 2.19274 1.36862 2.83517 -0.41856 -0.37518 -0.17012 162 PRO C O   
1126 C CB  . PRO A 154 ? 2.42095 1.44916 2.88910 -0.49696 -0.25252 -0.27060 162 PRO C CB  
1127 C CG  . PRO A 154 ? 2.31355 1.46111 2.90448 -0.47436 -0.24283 -0.32437 162 PRO C CG  
1128 C CD  . PRO A 154 ? 2.25345 1.42928 2.87369 -0.44030 -0.31067 -0.30174 162 PRO C CD  
1129 N N   . GLU A 155 ? 2.29681 1.33602 2.80220 -0.46239 -0.32471 -0.15329 163 GLU C N   
1130 C CA  . GLU A 155 ? 2.24070 1.33240 2.81175 -0.44358 -0.32980 -0.13161 163 GLU C CA  
1131 C C   . GLU A 155 ? 2.18013 1.36268 2.84260 -0.43984 -0.28689 -0.18749 163 GLU C C   
1132 O O   . GLU A 155 ? 2.20306 1.39062 2.86393 -0.46075 -0.24031 -0.24405 163 GLU C O   
1133 C CB  . GLU A 155 ? 2.33347 1.33605 2.82309 -0.45956 -0.31282 -0.10360 163 GLU C CB  
1134 C CG  . GLU A 155 ? 2.36296 1.30821 2.80258 -0.44509 -0.37362 -0.03878 163 GLU C CG  
1135 C CD  . GLU A 155 ? 2.32333 1.31082 2.82254 -0.41796 -0.39459 -0.00319 163 GLU C CD  
1136 O OE1 . GLU A 155 ? 2.23063 1.31822 2.83298 -0.39872 -0.39080 -0.01486 163 GLU C OE1 
1137 O OE2 . GLU A 155 ? 2.39352 1.30987 2.83208 -0.41359 -0.41552 0.03490  163 GLU C OE2 
1138 N N   . PRO A 156 ? 2.17396 1.43057 2.91858 -0.41325 -0.30128 -0.17605 164 PRO C N   
1139 C CA  . PRO A 156 ? 2.14557 1.41378 2.91113 -0.38794 -0.34553 -0.11722 164 PRO C CA  
1140 C C   . PRO A 156 ? 2.06134 1.40079 2.89648 -0.35663 -0.39434 -0.09889 164 PRO C C   
1141 O O   . PRO A 156 ? 2.02033 1.40251 2.89047 -0.34822 -0.39893 -0.13197 164 PRO C O   
1142 C CB  . PRO A 156 ? 2.13859 1.43386 2.94003 -0.38561 -0.30981 -0.13014 164 PRO C CB  
1143 C CG  . PRO A 156 ? 2.09072 1.45269 2.95237 -0.39012 -0.27318 -0.19831 164 PRO C CG  
1144 C CD  . PRO A 156 ? 2.12126 1.45355 2.94303 -0.41108 -0.26151 -0.23047 164 PRO C CD  
1145 N N   . VAL A 157 ? 2.12788 1.47581 2.98052 -0.33892 -0.43137 -0.04569 165 VAL C N   
1146 C CA  . VAL A 157 ? 2.06086 1.47361 2.97894 -0.31267 -0.46890 -0.02428 165 VAL C CA  
1147 C C   . VAL A 157 ? 2.04429 1.49786 3.01104 -0.29308 -0.46582 0.00050  165 VAL C C   
1148 O O   . VAL A 157 ? 2.08548 1.50413 3.02845 -0.29550 -0.46535 0.02960  165 VAL C O   
1149 C CB  . VAL A 157 ? 2.06242 1.44689 2.95709 -0.31503 -0.51985 0.01679  165 VAL C CB  
1150 C CG1 . VAL A 157 ? 2.01682 1.45555 2.97385 -0.29427 -0.55195 0.05592  165 VAL C CG1 
1151 C CG2 . VAL A 157 ? 2.05575 1.42788 2.92911 -0.32166 -0.52897 -0.01256 165 VAL C CG2 
1152 N N   . THR A 158 ? 2.00558 1.52661 3.03379 -0.27125 -0.46431 -0.01287 166 THR C N   
1153 C CA  . THR A 158 ? 2.00327 1.56482 3.07632 -0.25051 -0.45941 0.00789  166 THR C CA  
1154 C C   . THR A 158 ? 1.98628 1.58183 3.09478 -0.23436 -0.49575 0.04801  166 THR C C   
1155 O O   . THR A 158 ? 1.96852 1.57854 3.08367 -0.22992 -0.51434 0.03948  166 THR C O   
1156 C CB  . THR A 158 ? 1.99232 1.59828 3.10029 -0.23847 -0.42829 -0.03844 166 THR C CB  
1157 O OG1 . THR A 158 ? 1.97101 1.62053 3.11050 -0.21882 -0.44859 -0.05094 166 THR C OG1 
1158 C CG2 . THR A 158 ? 1.99695 1.57931 3.07961 -0.26143 -0.39249 -0.09115 166 THR C CG2 
1159 N N   . VAL A 159 ? 2.02570 1.63122 3.15617 -0.22620 -0.50495 0.09012  167 VAL C N   
1160 C CA  . VAL A 159 ? 2.01480 1.65668 3.18568 -0.21655 -0.53176 0.12734  167 VAL C CA  
1161 C C   . VAL A 159 ? 2.03531 1.72114 3.25130 -0.19471 -0.51184 0.14017  167 VAL C C   
1162 O O   . VAL A 159 ? 2.05726 1.74334 3.28873 -0.18964 -0.51169 0.16577  167 VAL C O   
1163 C CB  . VAL A 159 ? 2.01453 1.63342 3.17956 -0.23066 -0.56847 0.16679  167 VAL C CB  
1164 C CG1 . VAL A 159 ? 1.99836 1.65843 3.21032 -0.22846 -0.59125 0.19818  167 VAL C CG1 
1165 C CG2 . VAL A 159 ? 2.01317 1.57422 3.11816 -0.25237 -0.58459 0.15203  167 VAL C CG2 
1166 N N   . SER A 160 ? 2.01950 1.73869 3.25287 -0.17885 -0.49773 0.12172  168 SER C N   
1167 C CA  . SER A 160 ? 2.05199 1.81045 3.32154 -0.15762 -0.47970 0.13479  168 SER C CA  
1168 C C   . SER A 160 ? 2.05629 1.84075 3.35649 -0.15798 -0.49736 0.17490  168 SER C C   
1169 O O   . SER A 160 ? 2.03184 1.80247 3.32403 -0.17493 -0.52510 0.18930  168 SER C O   
1170 C CB  . SER A 160 ? 2.07512 1.84927 3.33897 -0.14021 -0.46012 0.09590  168 SER C CB  
1171 O OG  . SER A 160 ? 2.08609 1.86504 3.34108 -0.13499 -0.47835 0.09434  168 SER C OG  
1172 N N   . TRP A 161 ? 1.99700 1.81750 3.33168 -0.14141 -0.47819 0.19145  169 TRP C N   
1173 C CA  . TRP A 161 ? 2.00766 1.85701 3.37567 -0.14536 -0.48420 0.22644  169 TRP C CA  
1174 C C   . TRP A 161 ? 2.06537 1.92938 3.42518 -0.12701 -0.45926 0.21912  169 TRP C C   
1175 O O   . TRP A 161 ? 2.09639 1.97324 3.46009 -0.10607 -0.43213 0.20530  169 TRP C O   
1176 C CB  . TRP A 161 ? 2.00303 1.88485 3.42822 -0.14528 -0.48496 0.25849  169 TRP C CB  
1177 C CG  . TRP A 161 ? 1.96304 1.82913 3.39514 -0.16612 -0.52221 0.27560  169 TRP C CG  
1178 C CD1 . TRP A 161 ? 1.96108 1.79158 3.36898 -0.16812 -0.53708 0.26918  169 TRP C CD1 
1179 C CD2 . TRP A 161 ? 1.93219 1.80939 3.38934 -0.18924 -0.55027 0.30109  169 TRP C CD2 
1180 N NE1 . TRP A 161 ? 1.93712 1.75539 3.35054 -0.18777 -0.57613 0.28898  169 TRP C NE1 
1181 C CE2 . TRP A 161 ? 1.91180 1.76239 3.36086 -0.20180 -0.58569 0.30769  169 TRP C CE2 
1182 C CE3 . TRP A 161 ? 1.93133 1.83118 3.41053 -0.20283 -0.54802 0.31852  169 TRP C CE3 
1183 C CZ2 . TRP A 161 ? 1.88157 1.73425 3.35109 -0.22626 -0.62253 0.32890  169 TRP C CZ2 
1184 C CZ3 . TRP A 161 ? 1.89648 1.79833 3.39849 -0.23073 -0.58025 0.34007  169 TRP C CZ3 
1185 C CH2 . TRP A 161 ? 1.86698 1.74889 3.36786 -0.24162 -0.61894 0.34407  169 TRP C CH2 
1186 N N   . ASN A 162 ? 2.04921 1.90074 3.38715 -0.13483 -0.46987 0.22771  170 ASN C N   
1187 C CA  . ASN A 162 ? 2.12941 1.97821 3.44123 -0.11900 -0.45032 0.22570  170 ASN C CA  
1188 C C   . ASN A 162 ? 2.15587 1.99015 3.42915 -0.09241 -0.44167 0.18230  170 ASN C C   
1189 O O   . ASN A 162 ? 2.19122 2.03569 3.45843 -0.07164 -0.41591 0.17605  170 ASN C O   
1190 C CB  . ASN A 162 ? 2.16346 2.05285 3.52031 -0.11587 -0.41868 0.25513  170 ASN C CB  
1191 C CG  . ASN A 162 ? 2.14422 2.05250 3.54175 -0.14448 -0.42608 0.29344  170 ASN C CG  
1192 O OD1 . ASN A 162 ? 2.11099 1.99265 3.49158 -0.16684 -0.45627 0.29996  170 ASN C OD1 
1193 N ND2 . ASN A 162 ? 2.15878 2.11549 3.61476 -0.14455 -0.39804 0.31605  170 ASN C ND2 
1194 N N   . SER A 163 ? 2.15704 1.96894 3.40655 -0.09380 -0.46335 0.14913  171 SER C N   
1195 C CA  . SER A 163 ? 2.17060 1.97570 3.39464 -0.07199 -0.46088 0.09987  171 SER C CA  
1196 C C   . SER A 163 ? 2.16313 1.99167 3.40976 -0.05975 -0.43040 0.08561  171 SER C C   
1197 O O   . SER A 163 ? 2.19095 2.02196 3.42074 -0.03690 -0.41770 0.06404  171 SER C O   
1198 C CB  . SER A 163 ? 2.22635 2.00720 3.40148 -0.05067 -0.47141 0.08939  171 SER C CB  
1199 O OG  . SER A 163 ? 2.23427 1.98171 3.37835 -0.05729 -0.50416 0.08748  171 SER C OG  
1200 N N   . GLY A 164 ? 2.11320 1.95092 3.39101 -0.07403 -0.42117 0.09785  172 GLY C N   
1201 C CA  . GLY A 164 ? 2.11637 1.96354 3.40885 -0.06445 -0.39404 0.08514  172 GLY C CA  
1202 C C   . GLY A 164 ? 2.13226 2.00176 3.44984 -0.05087 -0.37163 0.11740  172 GLY C C   
1203 O O   . GLY A 164 ? 2.12889 2.00184 3.46426 -0.04498 -0.35329 0.11843  172 GLY C O   
1204 N N   . ALA A 165 ? 2.09513 1.97542 3.41111 -0.04582 -0.37022 0.14219  173 ALA C N   
1205 C CA  . ALA A 165 ? 2.12233 2.02836 3.46357 -0.03233 -0.34127 0.16728  173 ALA C CA  
1206 C C   . ALA A 165 ? 2.09382 2.02743 3.49396 -0.04187 -0.34076 0.19993  173 ALA C C   
1207 O O   . ALA A 165 ? 2.08994 2.04003 3.51782 -0.02573 -0.31958 0.20317  173 ALA C O   
1208 C CB  . ALA A 165 ? 2.18635 2.08931 3.50397 -0.03114 -0.33556 0.18585  173 ALA C CB  
1209 N N   . LEU A 166 ? 2.08440 2.02092 3.50330 -0.06556 -0.36749 0.22246  174 LEU C N   
1210 C CA  . LEU A 166 ? 2.05269 2.01749 3.53073 -0.07322 -0.37642 0.25167  174 LEU C CA  
1211 C C   . LEU A 166 ? 2.03113 1.96926 3.49969 -0.07062 -0.38836 0.23781  174 LEU C C   
1212 O O   . LEU A 166 ? 2.01358 1.91866 3.45377 -0.08884 -0.41421 0.23000  174 LEU C O   
1213 C CB  . LEU A 166 ? 2.02612 1.99692 3.52154 -0.10152 -0.40484 0.27649  174 LEU C CB  
1214 C CG  . LEU A 166 ? 1.98391 1.99510 3.55207 -0.11158 -0.41996 0.30706  174 LEU C CG  
1215 C CD1 . LEU A 166 ? 1.99933 2.06473 3.62881 -0.09128 -0.38636 0.31886  174 LEU C CD1 
1216 C CD2 . LEU A 166 ? 1.95794 1.97412 3.53942 -0.14346 -0.44347 0.32798  174 LEU C CD2 
1217 N N   . THR A 167 ? 1.98995 1.93439 3.47468 -0.04825 -0.36758 0.23453  175 THR C N   
1218 C CA  . THR A 167 ? 1.99564 1.90009 3.45841 -0.04499 -0.37406 0.22277  175 THR C CA  
1219 C C   . THR A 167 ? 1.98958 1.90918 3.49709 -0.02573 -0.37681 0.24491  175 THR C C   
1220 O O   . THR A 167 ? 1.99845 1.88026 3.48958 -0.02891 -0.40001 0.24981  175 THR C O   
1221 C CB  . THR A 167 ? 2.01784 1.89189 3.43500 -0.03509 -0.34714 0.18482  175 THR C CB  
1222 O OG1 . THR A 167 ? 2.02122 1.92544 3.45081 -0.01364 -0.31858 0.18066  175 THR C OG1 
1223 C CG2 . THR A 167 ? 2.02088 1.86870 3.39373 -0.05573 -0.35655 0.15501  175 THR C CG2 
1224 N N   . SER A 168 ? 1.94383 1.91326 3.50289 -0.00358 -0.35368 0.25642  176 SER C N   
1225 C CA  . SER A 168 ? 1.93214 1.92363 3.54394 0.02125  -0.35735 0.27298  176 SER C CA  
1226 C C   . SER A 168 ? 1.90054 1.91307 3.55803 0.00818  -0.40031 0.29857  176 SER C C   
1227 O O   . SER A 168 ? 1.87380 1.92983 3.57046 -0.01258 -0.40898 0.31339  176 SER C O   
1228 C CB  . SER A 168 ? 1.93072 1.98199 3.59762 0.04517  -0.32021 0.27800  176 SER C CB  
1229 O OG  . SER A 168 ? 1.96064 1.98760 3.57756 0.05711  -0.28423 0.25317  176 SER C OG  
1230 N N   . GLY A 169 ? 1.98786 1.96229 3.63413 0.01992  -0.42907 0.30309  177 GLY C N   
1231 C CA  . GLY A 169 ? 1.96287 1.95248 3.64854 0.01141  -0.47706 0.32478  177 GLY C CA  
1232 C C   . GLY A 169 ? 1.97014 1.91849 3.60361 -0.02597 -0.50683 0.32546  177 GLY C C   
1233 O O   . GLY A 169 ? 1.93775 1.91540 3.61279 -0.04214 -0.54188 0.34296  177 GLY C O   
1234 N N   . VAL A 170 ? 2.02717 1.91141 3.57489 -0.04093 -0.49288 0.30385  178 VAL C N   
1235 C CA  . VAL A 170 ? 2.04057 1.87988 3.53300 -0.07359 -0.51746 0.29945  178 VAL C CA  
1236 C C   . VAL A 170 ? 2.07717 1.83550 3.50464 -0.07353 -0.54405 0.29941  178 VAL C C   
1237 O O   . VAL A 170 ? 2.10673 1.81365 3.48732 -0.05925 -0.52460 0.28642  178 VAL C O   
1238 C CB  . VAL A 170 ? 2.04605 1.86723 3.48896 -0.08899 -0.48721 0.27097  178 VAL C CB  
1239 C CG1 . VAL A 170 ? 2.02447 1.78118 3.39555 -0.11613 -0.50486 0.25647  178 VAL C CG1 
1240 C CG2 . VAL A 170 ? 2.01478 1.89474 3.49936 -0.09541 -0.47616 0.27604  178 VAL C CG2 
1241 N N   . HIS A 171 ? 2.13400 1.87204 3.54988 -0.09096 -0.58846 0.31377  179 HIS C N   
1242 C CA  . HIS A 171 ? 2.17047 1.82159 3.51303 -0.09200 -0.62108 0.31782  179 HIS C CA  
1243 C C   . HIS A 171 ? 2.15658 1.75700 3.43179 -0.12794 -0.63672 0.30960  179 HIS C C   
1244 O O   . HIS A 171 ? 2.16531 1.74772 3.43208 -0.13832 -0.68318 0.32521  179 HIS C O   
1245 C CB  . HIS A 171 ? 2.18017 1.84991 3.57283 -0.06951 -0.67092 0.34376  179 HIS C CB  
1246 C CG  . HIS A 171 ? 2.16230 1.88853 3.63096 -0.03040 -0.65739 0.34964  179 HIS C CG  
1247 N ND1 . HIS A 171 ? 2.09677 1.93220 3.67947 -0.02276 -0.64629 0.35775  179 HIS C ND1 
1248 C CD2 . HIS A 171 ? 2.19710 1.88068 3.64039 0.00356  -0.65166 0.34756  179 HIS C CD2 
1249 C CE1 . HIS A 171 ? 2.08871 1.95313 3.71826 0.01565  -0.63246 0.35845  179 HIS C CE1 
1250 N NE2 . HIS A 171 ? 2.15152 1.92387 3.69793 0.03404  -0.63801 0.35260  179 HIS C NE2 
1251 N N   . THR A 172 ? 2.16930 1.74734 3.39781 -0.14565 -0.59851 0.28153  180 THR C N   
1252 C CA  . THR A 172 ? 2.14582 1.67367 3.30789 -0.17686 -0.60548 0.26655  180 THR C CA  
1253 C C   . THR A 172 ? 2.20250 1.62819 3.27003 -0.18543 -0.62672 0.26950  180 THR C C   
1254 O O   . THR A 172 ? 2.24503 1.60493 3.24716 -0.18440 -0.59896 0.25491  180 THR C O   
1255 C CB  . THR A 172 ? 2.11255 1.63987 3.25034 -0.18854 -0.55828 0.22878  180 THR C CB  
1256 O OG1 . THR A 172 ? 2.08218 1.68912 3.29157 -0.17397 -0.53767 0.22579  180 THR C OG1 
1257 C CG2 . THR A 172 ? 2.07923 1.57914 3.17338 -0.21658 -0.56623 0.21118  180 THR C CG2 
1258 N N   . PHE A 173 ? 2.27557 1.67979 3.32766 -0.19598 -0.67553 0.28761  181 PHE C N   
1259 C CA  . PHE A 173 ? 2.34547 1.64352 3.29707 -0.20164 -0.70301 0.29377  181 PHE C CA  
1260 C C   . PHE A 173 ? 2.35731 1.57538 3.20603 -0.23189 -0.66801 0.26338  181 PHE C C   
1261 O O   . PHE A 173 ? 2.29949 1.55417 3.16644 -0.24961 -0.64224 0.23991  181 PHE C O   
1262 C CB  . PHE A 173 ? 2.35711 1.65614 3.32114 -0.20534 -0.76856 0.31806  181 PHE C CB  
1263 N N   . PRO A 174 ? 2.49207 1.59763 3.22991 -0.23760 -0.66534 0.26147  182 PRO C N   
1264 C CA  . PRO A 174 ? 2.52067 1.54556 3.15683 -0.27138 -0.62900 0.23138  182 PRO C CA  
1265 C C   . PRO A 174 ? 2.50467 1.52023 3.11759 -0.29276 -0.65794 0.22944  182 PRO C C   
1266 O O   . PRO A 174 ? 2.48049 1.53654 3.14264 -0.28439 -0.71116 0.25386  182 PRO C O   
1267 C CB  . PRO A 174 ? 2.63145 1.52497 3.14487 -0.27090 -0.62924 0.23972  182 PRO C CB  
1268 C CG  . PRO A 174 ? 2.64305 1.56380 3.20959 -0.23205 -0.64809 0.26403  182 PRO C CG  
1269 C CD  . PRO A 174 ? 2.57029 1.61185 3.26626 -0.21206 -0.69099 0.28439  182 PRO C CD  
1270 N N   . ALA A 175 ? 2.52898 1.48988 3.06701 -0.32233 -0.62019 0.19704  183 ALA C N   
1271 C CA  . ALA A 175 ? 2.52260 1.46611 3.02924 -0.34197 -0.64234 0.19009  183 ALA C CA  
1272 C C   . ALA A 175 ? 2.62173 1.44834 3.01209 -0.34871 -0.68495 0.21119  183 ALA C C   
1273 O O   . ALA A 175 ? 2.70668 1.44386 3.01364 -0.34421 -0.68298 0.22196  183 ALA C O   
1274 C CB  . ALA A 175 ? 2.51104 1.44936 2.99109 -0.36789 -0.58463 0.14201  183 ALA C CB  
1275 N N   . VAL A 176 ? 2.68212 1.50127 3.05921 -0.35865 -0.72656 0.21677  184 VAL C N   
1276 C CA  . VAL A 176 ? 2.77896 1.48371 3.03794 -0.36692 -0.77149 0.23222  184 VAL C CA  
1277 C C   . VAL A 176 ? 2.80398 1.45540 2.98487 -0.39739 -0.74847 0.20172  184 VAL C C   
1278 O O   . VAL A 176 ? 2.72694 1.45320 2.97695 -0.40399 -0.73542 0.18164  184 VAL C O   
1279 C CB  . VAL A 176 ? 2.76699 1.50645 3.08117 -0.34894 -0.85530 0.26870  184 VAL C CB  
1280 C CG1 . VAL A 176 ? 2.73025 1.55189 3.15247 -0.31709 -0.87110 0.29236  184 VAL C CG1 
1281 C CG2 . VAL A 176 ? 2.69104 1.50140 3.07479 -0.36134 -0.87685 0.26384  184 VAL C CG2 
1282 N N   . LEU A 177 ? 2.96481 1.48060 2.99513 -0.41458 -0.74006 0.19627  185 LEU C N   
1283 C CA  . LEU A 177 ? 3.01099 1.46242 2.95275 -0.44276 -0.72132 0.16809  185 LEU C CA  
1284 C C   . LEU A 177 ? 3.02315 1.45449 2.94840 -0.43925 -0.80061 0.19136  185 LEU C C   
1285 O O   . LEU A 177 ? 3.11993 1.44526 2.93764 -0.43780 -0.84749 0.21309  185 LEU C O   
1286 C CB  . LEU A 177 ? 3.14004 1.44650 2.91777 -0.46628 -0.67451 0.15230  185 LEU C CB  
1287 N N   . GLN A 178 ? 2.87506 1.40432 2.90464 -0.43755 -0.81880 0.18640  186 GLN C N   
1288 C CA  . GLN A 178 ? 2.88468 1.40001 2.90716 -0.43948 -0.89112 0.20455  186 GLN C CA  
1289 C C   . GLN A 178 ? 2.99964 1.38040 2.86299 -0.46153 -0.89211 0.18793  186 GLN C C   
1290 O O   . GLN A 178 ? 3.03062 1.37109 2.83098 -0.47926 -0.82649 0.15116  186 GLN C O   
1291 C CB  . GLN A 178 ? 2.76666 1.39385 2.91138 -0.43902 -0.89752 0.19706  186 GLN C CB  
1292 N N   . SER A 179 ? 3.08745 1.39887 2.88636 -0.46031 -0.96694 0.21286  187 SER C N   
1293 C CA  . SER A 179 ? 3.22311 1.39269 2.85534 -0.47947 -0.97650 0.20051  187 SER C CA  
1294 C C   . SER A 179 ? 3.20672 1.38036 2.82495 -0.49959 -0.93137 0.16036  187 SER C C   
1295 O O   . SER A 179 ? 3.31932 1.38140 2.79839 -0.51847 -0.89825 0.13582  187 SER C O   
1296 C CB  . SER A 179 ? 3.27827 1.40316 2.87874 -0.47338 -1.07631 0.23014  187 SER C CB  
1297 O OG  . SER A 179 ? 3.16470 1.40327 2.90373 -0.47157 -1.11773 0.23804  187 SER C OG  
1298 N N   . SER A 180 ? 3.16436 1.45948 2.91952 -0.49449 -0.92950 0.15216  188 SER C N   
1299 C CA  . SER A 180 ? 3.14202 1.45149 2.89812 -0.50567 -0.88464 0.11018  188 SER C CA  
1300 C C   . SER A 180 ? 3.16657 1.46761 2.89290 -0.51393 -0.79177 0.06973  188 SER C C   
1301 O O   . SER A 180 ? 3.21870 1.47831 2.88397 -0.52787 -0.74922 0.02890  188 SER C O   
1302 C CB  . SER A 180 ? 3.00304 1.44041 2.91016 -0.49385 -0.90014 0.11196  188 SER C CB  
1303 O OG  . SER A 180 ? 2.91504 1.45543 2.93718 -0.47802 -0.87210 0.12017  188 SER C OG  
1304 N N   . GLY A 181 ? 3.02574 1.36827 2.79908 -0.50633 -0.75808 0.07716  189 GLY C N   
1305 C CA  . GLY A 181 ? 3.03224 1.38684 2.80379 -0.51658 -0.66971 0.03672  189 GLY C CA  
1306 C C   . GLY A 181 ? 2.90423 1.40087 2.83188 -0.50042 -0.63990 0.02167  189 GLY C C   
1307 O O   . GLY A 181 ? 2.90151 1.42457 2.84680 -0.50870 -0.56869 -0.01877 189 GLY C O   
1308 N N   . LEU A 182 ? 2.85549 1.44158 2.89419 -0.47928 -0.69137 0.05113  190 LEU C N   
1309 C CA  . LEU A 182 ? 2.74165 1.45329 2.91830 -0.46104 -0.67119 0.04347  190 LEU C CA  
1310 C C   . LEU A 182 ? 2.71197 1.45767 2.93824 -0.44702 -0.68409 0.08072  190 LEU C C   
1311 O O   . LEU A 182 ? 2.75527 1.45049 2.93959 -0.44460 -0.73131 0.11899  190 LEU C O   
1312 C CB  . LEU A 182 ? 2.65737 1.43796 2.91598 -0.44838 -0.71372 0.04964  190 LEU C CB  
1313 N N   . TYR A 183 ? 2.61076 1.44102 2.92591 -0.43525 -0.64410 0.06663  191 TYR C N   
1314 C CA  . TYR A 183 ? 2.58505 1.45163 2.95141 -0.41935 -0.64933 0.09676  191 TYR C CA  
1315 C C   . TYR A 183 ? 2.49838 1.45299 2.97207 -0.39903 -0.69952 0.13071  191 TYR C C   
1316 O O   . TYR A 183 ? 2.43907 1.44333 2.96386 -0.39673 -0.71413 0.12360  191 TYR C O   
1317 C CB  . TYR A 183 ? 2.56154 1.47266 2.96855 -0.41782 -0.58272 0.06461  191 TYR C CB  
1318 N N   . SER A 184 ? 2.47419 1.44354 2.97897 -0.38437 -0.72431 0.16671  192 SER C N   
1319 C CA  . SER A 184 ? 2.40394 1.46013 3.01547 -0.36798 -0.76442 0.19804  192 SER C CA  
1320 C C   . SER A 184 ? 2.40238 1.49612 3.06518 -0.34676 -0.75671 0.21828  192 SER C C   
1321 O O   . SER A 184 ? 2.47612 1.50215 3.07355 -0.34342 -0.75641 0.22646  192 SER C O   
1322 C CB  . SER A 184 ? 2.42697 1.45487 3.02307 -0.37476 -0.83366 0.22703  192 SER C CB  
1323 O OG  . SER A 184 ? 2.41960 1.42216 2.98128 -0.39210 -0.84353 0.20957  192 SER C OG  
1324 N N   . LEU A 185 ? 2.21798 1.41135 2.98962 -0.33141 -0.75079 0.22633  193 LEU C N   
1325 C CA  . LEU A 185 ? 2.21618 1.45544 3.04715 -0.30842 -0.74105 0.24332  193 LEU C CA  
1326 C C   . LEU A 185 ? 2.15673 1.49260 3.10017 -0.29754 -0.76538 0.26752  193 LEU C C   
1327 O O   . LEU A 185 ? 2.11263 1.47414 3.08196 -0.31023 -0.78475 0.26963  193 LEU C O   
1328 C CB  . LEU A 185 ? 2.20286 1.45743 3.03697 -0.30269 -0.67804 0.21340  193 LEU C CB  
1329 C CG  . LEU A 185 ? 2.12654 1.45647 3.02463 -0.30073 -0.65164 0.19050  193 LEU C CG  
1330 C CD1 . LEU A 185 ? 2.09018 1.50397 3.08021 -0.27729 -0.64031 0.20412  193 LEU C CD1 
1331 C CD2 . LEU A 185 ? 2.13088 1.43653 2.98594 -0.31186 -0.60238 0.14336  193 LEU C CD2 
1332 N N   . SER A 186 ? 2.05315 1.43959 3.06062 -0.27483 -0.75805 0.28324  194 SER C N   
1333 C CA  . SER A 186 ? 2.01341 1.49180 3.12964 -0.26519 -0.77455 0.30654  194 SER C CA  
1334 C C   . SER A 186 ? 2.00623 1.53922 3.17708 -0.24078 -0.73240 0.30365  194 SER C C   
1335 O O   . SER A 186 ? 2.05758 1.56612 3.21227 -0.22216 -0.72618 0.30680  194 SER C O   
1336 C CB  . SER A 186 ? 2.06322 1.54477 3.20889 -0.26119 -0.83292 0.33572  194 SER C CB  
1337 O OG  . SER A 186 ? 2.14235 1.56689 3.23894 -0.24223 -0.84443 0.34074  194 SER C OG  
1338 N N   . SER A 187 ? 1.96390 1.56164 3.19073 -0.23950 -0.70543 0.29799  195 SER C N   
1339 C CA  . SER A 187 ? 1.95699 1.60634 3.23304 -0.21631 -0.66600 0.29459  195 SER C CA  
1340 C C   . SER A 187 ? 1.94643 1.67481 3.31971 -0.20868 -0.67895 0.32225  195 SER C C   
1341 O O   . SER A 187 ? 1.90129 1.66206 3.30725 -0.22553 -0.68875 0.33090  195 SER C O   
1342 C CB  . SER A 187 ? 1.91452 1.57592 3.17765 -0.21742 -0.62587 0.26580  195 SER C CB  
1343 O OG  . SER A 187 ? 1.92427 1.61332 3.20979 -0.19517 -0.58697 0.25541  195 SER C OG  
1344 N N   . VAL A 188 ? 1.94916 1.70793 3.36908 -0.18373 -0.67486 0.33388  196 VAL C N   
1345 C CA  . VAL A 188 ? 1.92380 1.76564 3.44691 -0.17679 -0.68376 0.35632  196 VAL C CA  
1346 C C   . VAL A 188 ? 1.92616 1.81576 3.49329 -0.14917 -0.63796 0.35218  196 VAL C C   
1347 O O   . VAL A 188 ? 1.98052 1.83343 3.50087 -0.13168 -0.61123 0.33552  196 VAL C O   
1348 C CB  . VAL A 188 ? 1.93914 1.78481 3.49731 -0.17006 -0.73674 0.37513  196 VAL C CB  
1349 C CG1 . VAL A 188 ? 1.95044 1.74023 3.45422 -0.19791 -0.78423 0.37791  196 VAL C CG1 
1350 C CG2 . VAL A 188 ? 2.00965 1.80988 3.53133 -0.13823 -0.73887 0.37175  196 VAL C CG2 
1351 N N   . VAL A 189 ? 1.98499 1.95459 3.64116 -0.14795 -0.62664 0.36620  197 VAL C N   
1352 C CA  . VAL A 189 ? 1.98022 1.99892 3.68205 -0.12145 -0.58212 0.36340  197 VAL C CA  
1353 C C   . VAL A 189 ? 1.92156 2.02882 3.73808 -0.11817 -0.58745 0.38254  197 VAL C C   
1354 O O   . VAL A 189 ? 1.88389 2.02906 3.74345 -0.14699 -0.59475 0.39420  197 VAL C O   
1355 C CB  . VAL A 189 ? 1.98901 2.00342 3.65341 -0.12676 -0.53737 0.34861  197 VAL C CB  
1356 C CG1 . VAL A 189 ? 1.96076 1.98551 3.62757 -0.15894 -0.54412 0.35718  197 VAL C CG1 
1357 C CG2 . VAL A 189 ? 1.98154 2.04533 3.69049 -0.10034 -0.49182 0.34704  197 VAL C CG2 
1358 N N   . THR A 190 ? 1.99626 2.13470 3.86387 -0.08370 -0.58481 0.38375  198 THR C N   
1359 C CA  . THR A 190 ? 1.93803 2.17207 3.92945 -0.07455 -0.58652 0.39548  198 THR C CA  
1360 C C   . THR A 190 ? 1.92047 2.21244 3.95294 -0.07817 -0.52533 0.39455  198 THR C C   
1361 O O   . THR A 190 ? 1.94611 2.22681 3.94979 -0.05259 -0.48331 0.38322  198 THR C O   
1362 C CB  . THR A 190 ? 1.94383 2.18405 3.96794 -0.02912 -0.60381 0.39288  198 THR C CB  
1363 O OG1 . THR A 190 ? 1.95760 2.20437 3.97580 0.00098  -0.55074 0.38183  198 THR C OG1 
1364 C CG2 . THR A 190 ? 2.00740 2.14565 3.93171 -0.02195 -0.64690 0.38982  198 THR C CG2 
1365 N N   . VAL A 191 ? 1.95858 2.30358 4.04883 -0.11201 -0.51911 0.40585  199 VAL C N   
1366 C CA  . VAL A 191 ? 1.97139 2.35628 4.08290 -0.12141 -0.45858 0.40711  199 VAL C CA  
1367 C C   . VAL A 191 ? 1.92277 2.41493 4.17240 -0.12756 -0.44518 0.41534  199 VAL C C   
1368 O O   . VAL A 191 ? 1.87724 2.40787 4.19629 -0.14900 -0.48720 0.42303  199 VAL C O   
1369 C CB  . VAL A 191 ? 2.00920 2.34327 4.04364 -0.16047 -0.45156 0.41107  199 VAL C CB  
1370 C CG1 . VAL A 191 ? 1.97498 2.30872 4.03180 -0.19926 -0.50073 0.42310  199 VAL C CG1 
1371 C CG2 . VAL A 191 ? 2.05433 2.41433 4.09490 -0.17136 -0.39112 0.41486  199 VAL C CG2 
1372 N N   . PRO A 192 ? 1.90922 2.45374 4.20449 -0.11094 -0.38677 0.41125  200 PRO C N   
1373 C CA  . PRO A 192 ? 1.86166 2.51848 4.30010 -0.11797 -0.36616 0.41419  200 PRO C CA  
1374 C C   . PRO A 192 ? 1.86002 2.54848 4.33804 -0.17677 -0.35771 0.42695  200 PRO C C   
1375 O O   . PRO A 192 ? 1.92355 2.55029 4.31062 -0.20771 -0.33562 0.43445  200 PRO C O   
1376 C CB  . PRO A 192 ? 1.89595 2.57856 4.34098 -0.08797 -0.29593 0.40475  200 PRO C CB  
1377 C CG  . PRO A 192 ? 1.93160 2.52877 4.26797 -0.04877 -0.30444 0.39405  200 PRO C CG  
1378 C CD  . PRO A 192 ? 1.95843 2.46588 4.18661 -0.07561 -0.34307 0.39870  200 PRO C CD  
1379 N N   . SER A 193 ? 1.84431 2.62822 4.46080 -0.19127 -0.37823 0.42740  201 SER C N   
1380 C CA  . SER A 193 ? 1.83811 2.66214 4.51045 -0.25186 -0.36673 0.43714  201 SER C CA  
1381 C C   . SER A 193 ? 1.89798 2.74524 4.57319 -0.27432 -0.27898 0.44004  201 SER C C   
1382 O O   . SER A 193 ? 1.95416 2.76121 4.57766 -0.32468 -0.25673 0.45245  201 SER C O   
1383 C CB  . SER A 193 ? 1.74791 2.68214 4.58451 -0.25971 -0.40755 0.43074  201 SER C CB  
1384 O OG  . SER A 193 ? 1.71351 2.61632 4.53599 -0.23580 -0.49139 0.42842  201 SER C OG  
1385 N N   . SER A 194 ? 1.74573 2.64971 4.47339 -0.23742 -0.22761 0.42858  202 SER C N   
1386 C CA  . SER A 194 ? 1.82112 2.73526 4.53395 -0.25509 -0.13913 0.43031  202 SER C CA  
1387 C C   . SER A 194 ? 1.93965 2.72579 4.47326 -0.26721 -0.11807 0.44123  202 SER C C   
1388 O O   . SER A 194 ? 2.02315 2.78597 4.51472 -0.30450 -0.06189 0.45050  202 SER C O   
1389 C CB  . SER A 194 ? 1.81011 2.78714 4.58419 -0.20300 -0.09263 0.41335  202 SER C CB  
1390 O OG  . SER A 194 ? 1.84056 2.74044 4.50927 -0.15045 -0.10795 0.40720  202 SER C OG  
1391 N N   . SER A 195 ? 1.92285 2.62356 4.34881 -0.23533 -0.16155 0.43823  203 SER C N   
1392 C CA  . SER A 195 ? 2.03137 2.61658 4.29567 -0.23943 -0.15117 0.44232  203 SER C CA  
1393 C C   . SER A 195 ? 2.07818 2.60956 4.28756 -0.29522 -0.16285 0.45851  203 SER C C   
1394 O O   . SER A 195 ? 2.19478 2.64886 4.29234 -0.30791 -0.13085 0.46420  203 SER C O   
1395 C CB  . SER A 195 ? 2.01741 2.53743 4.20249 -0.19994 -0.20069 0.43123  203 SER C CB  
1396 O OG  . SER A 195 ? 1.97455 2.46114 4.14248 -0.22137 -0.26566 0.43675  203 SER C OG  
1397 N N   . LEU A 196 ? 1.99027 2.55264 4.26827 -0.32686 -0.21146 0.46516  204 LEU C N   
1398 C CA  . LEU A 196 ? 2.02766 2.53896 4.26076 -0.38241 -0.22477 0.47993  204 LEU C CA  
1399 C C   . LEU A 196 ? 2.11651 2.49893 4.18214 -0.37872 -0.24014 0.48200  204 LEU C C   
1400 O O   . LEU A 196 ? 2.08144 2.41825 4.09698 -0.35847 -0.29512 0.47431  204 LEU C O   
1401 C CB  . LEU A 196 ? 2.08078 2.63058 4.36093 -0.42901 -0.15759 0.49028  204 LEU C CB  
1402 N N   . GLY A 197 ? 2.13167 2.45243 4.10886 -0.39810 -0.19281 0.49070  205 GLY C N   
1403 C CA  . GLY A 197 ? 2.23236 2.43189 4.05209 -0.38941 -0.20714 0.48969  205 GLY C CA  
1404 C C   . GLY A 197 ? 2.34478 2.50206 4.07622 -0.34930 -0.16596 0.47963  205 GLY C C   
1405 O O   . GLY A 197 ? 2.45740 2.51535 4.05762 -0.34324 -0.16805 0.47824  205 GLY C O   
1406 N N   . THR A 198 ? 2.23259 2.46225 4.03376 -0.31919 -0.13158 0.47058  206 THR C N   
1407 C CA  . THR A 198 ? 2.34824 2.54061 4.06939 -0.28354 -0.08779 0.46029  206 THR C CA  
1408 C C   . THR A 198 ? 2.38546 2.50317 4.00228 -0.24400 -0.12834 0.44102  206 THR C C   
1409 O O   . THR A 198 ? 2.52062 2.55964 4.02005 -0.22928 -0.11289 0.43492  206 THR C O   
1410 C CB  . THR A 198 ? 2.29309 2.58148 4.11963 -0.25761 -0.04780 0.45202  206 THR C CB  
1411 O OG1 . THR A 198 ? 2.14944 2.49685 4.06489 -0.23464 -0.09606 0.44214  206 THR C OG1 
1412 C CG2 . THR A 198 ? 2.28709 2.64662 4.20812 -0.29857 0.00595  0.46619  206 THR C CG2 
1413 N N   . GLN A 199 ? 2.33421 2.47396 3.99048 -0.22609 -0.17918 0.42891  207 GLN C N   
1414 C CA  . GLN A 199 ? 2.35394 2.42468 3.91953 -0.20085 -0.21988 0.40877  207 GLN C CA  
1415 C C   . GLN A 199 ? 2.32971 2.35171 3.85916 -0.23111 -0.26752 0.41569  207 GLN C C   
1416 O O   . GLN A 199 ? 2.34062 2.36172 3.88687 -0.27140 -0.26272 0.43695  207 GLN C O   
1417 C CB  . GLN A 199 ? 2.25853 2.36327 3.86711 -0.16666 -0.24206 0.38933  207 GLN C CB  
1418 C CG  . GLN A 199 ? 2.13120 2.30922 3.85495 -0.17477 -0.26295 0.39868  207 GLN C CG  
1419 C CD  . GLN A 199 ? 2.10452 2.36422 3.92505 -0.16648 -0.21991 0.40587  207 GLN C CD  
1420 O OE1 . GLN A 199 ? 2.18504 2.44874 3.98976 -0.16552 -0.16677 0.40883  207 GLN C OE1 
1421 N NE2 . GLN A 199 ? 1.99842 2.32078 3.91682 -0.15795 -0.24318 0.40694  207 GLN C NE2 
1422 N N   . THR A 200 ? 2.37771 2.35604 3.85504 -0.21332 -0.31071 0.39551  208 THR C N   
1423 C CA  . THR A 200 ? 2.34070 2.27387 3.78536 -0.23477 -0.35919 0.39601  208 THR C CA  
1424 C C   . THR A 200 ? 2.21872 2.18198 3.71490 -0.22864 -0.39804 0.38545  208 THR C C   
1425 O O   . THR A 200 ? 2.18025 2.17979 3.71233 -0.20224 -0.38985 0.37353  208 THR C O   
1426 C CB  . THR A 200 ? 2.42845 2.27451 3.75548 -0.21799 -0.37539 0.37687  208 THR C CB  
1427 O OG1 . THR A 200 ? 2.39234 2.19462 3.69052 -0.23803 -0.42071 0.37662  208 THR C OG1 
1428 C CG2 . THR A 200 ? 2.42097 2.26631 3.72503 -0.17615 -0.37952 0.34307  208 THR C CG2 
1429 N N   . TYR A 201 ? 2.28508 2.22444 3.77681 -0.25384 -0.44008 0.39034  209 TYR C N   
1430 C CA  . TYR A 201 ? 2.18741 2.14090 3.71227 -0.25176 -0.47826 0.38232  209 TYR C CA  
1431 C C   . TYR A 201 ? 2.18534 2.06961 3.63435 -0.25681 -0.51637 0.36595  209 TYR C C   
1432 O O   . TYR A 201 ? 2.17555 2.03239 3.61314 -0.28634 -0.54287 0.37785  209 TYR C O   
1433 C CB  . TYR A 201 ? 2.11701 2.12560 3.73429 -0.27901 -0.49396 0.40533  209 TYR C CB  
1434 C CG  . TYR A 201 ? 2.12405 2.20547 3.82287 -0.27798 -0.45197 0.41963  209 TYR C CG  
1435 C CD1 . TYR A 201 ? 2.09928 2.22922 3.84712 -0.24486 -0.43446 0.41201  209 TYR C CD1 
1436 C CD2 . TYR A 201 ? 2.16228 2.25904 3.88454 -0.31039 -0.42563 0.43877  209 TYR C CD2 
1437 C CE1 . TYR A 201 ? 2.10247 2.30178 3.92799 -0.24022 -0.39365 0.42132  209 TYR C CE1 
1438 C CE2 . TYR A 201 ? 2.16954 2.33717 3.97004 -0.31080 -0.38004 0.44813  209 TYR C CE2 
1439 C CZ  . TYR A 201 ? 2.13560 2.35800 3.99088 -0.27353 -0.36470 0.43838  209 TYR C CZ  
1440 O OH  . TYR A 201 ? 2.13825 2.43481 4.07591 -0.27047 -0.31734 0.44427  209 TYR C OH  
1441 N N   . ILE A 202 ? 2.07565 1.93404 3.47709 -0.22846 -0.51740 0.33584  210 ILE C N   
1442 C CA  . ILE A 202 ? 2.07033 1.87208 3.40714 -0.22699 -0.54766 0.31134  210 ILE C CA  
1443 C C   . ILE A 202 ? 2.02365 1.83088 3.36153 -0.20860 -0.54935 0.28455  210 ILE C C   
1444 O O   . ILE A 202 ? 2.03903 1.86718 3.38423 -0.18463 -0.52188 0.27035  210 ILE C O   
1445 C CB  . ILE A 202 ? 2.15411 1.90814 3.41701 -0.21078 -0.54224 0.29347  210 ILE C CB  
1446 C CG1 . ILE A 202 ? 2.20994 1.92800 3.44467 -0.23519 -0.54838 0.31917  210 ILE C CG1 
1447 C CG2 . ILE A 202 ? 2.13668 1.85105 3.35033 -0.19744 -0.56766 0.25573  210 ILE C CG2 
1448 C CD1 . ILE A 202 ? 2.32079 1.99410 3.48492 -0.21691 -0.53245 0.31361  210 ILE C CD1 
1449 N N   . CYS A 203 ? 2.04809 1.83046 3.37298 -0.22185 -0.57900 0.27745  211 CYS C N   
1450 C CA  . CYS A 203 ? 2.02118 1.79107 3.32813 -0.21033 -0.57710 0.24899  211 CYS C CA  
1451 C C   . CYS A 203 ? 2.04066 1.77053 3.28976 -0.20315 -0.58320 0.21044  211 CYS C C   
1452 O O   . CYS A 203 ? 2.04345 1.73922 3.26109 -0.21498 -0.60827 0.20978  211 CYS C O   
1453 C CB  . CYS A 203 ? 1.96993 1.72957 3.28826 -0.22748 -0.60218 0.26215  211 CYS C CB  
1454 S SG  . CYS A 203 ? 1.94271 1.64646 3.21318 -0.25395 -0.64427 0.25928  211 CYS C SG  
1455 N N   . ASN A 204 ? 2.04591 1.78182 3.28516 -0.18300 -0.56054 0.17580  212 ASN C N   
1456 C CA  . ASN A 204 ? 2.05949 1.77303 3.26108 -0.17242 -0.56327 0.13007  212 ASN C CA  
1457 C C   . ASN A 204 ? 2.01925 1.71435 3.20863 -0.18540 -0.56086 0.10701  212 ASN C C   
1458 O O   . ASN A 204 ? 2.00818 1.71386 3.20791 -0.18220 -0.53587 0.09373  212 ASN C O   
1459 C CB  . ASN A 204 ? 2.09636 1.83172 3.29974 -0.14458 -0.54012 0.10082  212 ASN C CB  
1460 C CG  . ASN A 204 ? 2.15128 1.89978 3.35921 -0.13211 -0.53235 0.12790  212 ASN C CG  
1461 O OD1 . ASN A 204 ? 2.14880 1.92516 3.38958 -0.13218 -0.51173 0.15397  212 ASN C OD1 
1462 N ND2 . ASN A 204 ? 2.21127 1.93490 3.38108 -0.11937 -0.54722 0.11977  212 ASN C ND2 
1463 N N   . VAL A 205 ? 2.02991 1.68982 3.18928 -0.20062 -0.58400 0.10069  213 VAL C N   
1464 C CA  . VAL A 205 ? 2.00645 1.63680 3.13895 -0.21561 -0.57941 0.07647  213 VAL C CA  
1465 C C   . VAL A 205 ? 2.01908 1.64849 3.13704 -0.20459 -0.56982 0.02013  213 VAL C C   
1466 O O   . VAL A 205 ? 2.04411 1.67522 3.15715 -0.18863 -0.58708 0.00703  213 VAL C O   
1467 C CB  . VAL A 205 ? 1.98998 1.57880 3.09455 -0.23916 -0.61135 0.10199  213 VAL C CB  
1468 C CG1 . VAL A 205 ? 1.98506 1.53373 3.05092 -0.25610 -0.60220 0.08544  213 VAL C CG1 
1469 C CG2 . VAL A 205 ? 1.97372 1.57842 3.11028 -0.24681 -0.62946 0.15452  213 VAL C CG2 
1470 N N   . ASN A 206 ? 1.97250 1.59811 3.08412 -0.21250 -0.54168 -0.01525 214 ASN C N   
1471 C CA  . ASN A 206 ? 1.97341 1.60730 3.08407 -0.20629 -0.52852 -0.07589 214 ASN C CA  
1472 C C   . ASN A 206 ? 1.97032 1.56624 3.04683 -0.23418 -0.50840 -0.09622 214 ASN C C   
1473 O O   . ASN A 206 ? 1.97289 1.54677 3.03325 -0.25190 -0.48759 -0.08011 214 ASN C O   
1474 C CB  . ASN A 206 ? 1.96914 1.65036 3.11833 -0.18705 -0.50330 -0.11152 214 ASN C CB  
1475 C CG  . ASN A 206 ? 1.95520 1.65777 3.11968 -0.18083 -0.49066 -0.18097 214 ASN C CG  
1476 O OD1 . ASN A 206 ? 1.96275 1.68178 3.13710 -0.15523 -0.51480 -0.20626 214 ASN C OD1 
1477 N ND2 . ASN A 206 ? 1.93849 1.63867 3.10444 -0.20400 -0.45261 -0.21423 214 ASN C ND2 
1478 N N   . HIS A 207 ? 1.94245 1.52360 3.00095 -0.23632 -0.51500 -0.13144 215 HIS C N   
1479 C CA  . HIS A 207 ? 1.95756 1.49752 2.97499 -0.26254 -0.49369 -0.15787 215 HIS C CA  
1480 C C   . HIS A 207 ? 1.94923 1.52458 2.99569 -0.25336 -0.47160 -0.23092 215 HIS C C   
1481 O O   . HIS A 207 ? 1.96004 1.52393 2.99375 -0.24703 -0.48718 -0.25577 215 HIS C O   
1482 C CB  . HIS A 207 ? 1.97822 1.46069 2.94247 -0.27499 -0.52746 -0.12671 215 HIS C CB  
1483 C CG  . HIS A 207 ? 2.01399 1.43747 2.91704 -0.30452 -0.50543 -0.14254 215 HIS C CG  
1484 N ND1 . HIS A 207 ? 2.04123 1.40345 2.88490 -0.31800 -0.53340 -0.12234 215 HIS C ND1 
1485 C CD2 . HIS A 207 ? 2.03860 1.44703 2.92226 -0.32550 -0.45622 -0.17693 215 HIS C CD2 
1486 C CE1 . HIS A 207 ? 2.08884 1.39800 2.87345 -0.34360 -0.50283 -0.14301 215 HIS C CE1 
1487 N NE2 . HIS A 207 ? 2.09138 1.42615 2.89815 -0.35019 -0.45337 -0.17579 215 HIS C NE2 
1488 N N   . LYS A 208 ? 1.87381 1.49733 2.96652 -0.24872 -0.43985 -0.26681 216 LYS C N   
1489 C CA  . LYS A 208 ? 1.84746 1.51970 2.98613 -0.24084 -0.41707 -0.34289 216 LYS C CA  
1490 C C   . LYS A 208 ? 1.86592 1.50996 2.97682 -0.26799 -0.38650 -0.38327 216 LYS C C   
1491 O O   . LYS A 208 ? 1.84949 1.53095 2.99695 -0.25365 -0.38445 -0.44289 216 LYS C O   
1492 C CB  . LYS A 208 ? 1.81552 1.53409 3.00197 -0.24390 -0.38162 -0.37154 216 LYS C CB  
1493 N N   . PRO A 209 ? 1.84306 1.42014 2.88805 -0.30513 -0.36149 -0.35691 217 PRO C N   
1494 C CA  . PRO A 209 ? 1.88816 1.42522 2.88994 -0.32987 -0.33476 -0.39142 217 PRO C CA  
1495 C C   . PRO A 209 ? 1.90156 1.42555 2.88805 -0.30870 -0.37710 -0.39251 217 PRO C C   
1496 O O   . PRO A 209 ? 1.91582 1.44625 2.90658 -0.31053 -0.35832 -0.44717 217 PRO C O   
1497 C CB  . PRO A 209 ? 1.95359 1.40166 2.86615 -0.36617 -0.31779 -0.34441 217 PRO C CB  
1498 C CG  . PRO A 209 ? 1.93013 1.39378 2.86467 -0.36727 -0.30608 -0.31971 217 PRO C CG  
1499 C CD  . PRO A 209 ? 1.86281 1.40125 2.87342 -0.32690 -0.34364 -0.31229 217 PRO C CD  
1500 N N   . SER A 210 ? 1.93790 1.44223 2.90717 -0.28976 -0.43182 -0.33518 218 SER C N   
1501 C CA  . SER A 210 ? 1.94765 1.43492 2.90164 -0.26788 -0.47678 -0.33307 218 SER C CA  
1502 C C   . SER A 210 ? 1.90686 1.44782 2.91725 -0.22484 -0.51328 -0.34002 218 SER C C   
1503 O O   . SER A 210 ? 1.92258 1.44274 2.91623 -0.20302 -0.55429 -0.33583 218 SER C O   
1504 C CB  . SER A 210 ? 1.97909 1.39289 2.86322 -0.28341 -0.51295 -0.26560 218 SER C CB  
1505 O OG  . SER A 210 ? 1.94426 1.37446 2.85046 -0.27211 -0.54373 -0.21106 218 SER C OG  
1506 N N   . ASN A 211 ? 1.93462 1.53390 3.00125 -0.21227 -0.50016 -0.34998 219 ASN C N   
1507 C CA  . ASN A 211 ? 1.91615 1.56099 3.02731 -0.16993 -0.53224 -0.36082 219 ASN C CA  
1508 C C   . ASN A 211 ? 1.94855 1.55410 3.02338 -0.15657 -0.58124 -0.29690 219 ASN C C   
1509 O O   . ASN A 211 ? 1.96721 1.56973 3.04022 -0.12339 -0.61835 -0.30529 219 ASN C O   
1510 C CB  . ASN A 211 ? 1.90034 1.58112 3.04839 -0.14025 -0.53867 -0.43536 219 ASN C CB  
1511 C CG  . ASN A 211 ? 1.87463 1.61249 3.07681 -0.09705 -0.56128 -0.46514 219 ASN C CG  
1512 O OD1 . ASN A 211 ? 1.89006 1.62459 3.08451 -0.08451 -0.58175 -0.42171 219 ASN C OD1 
1513 N ND2 . ASN A 211 ? 1.83643 1.62860 3.09511 -0.07399 -0.55621 -0.54331 219 ASN C ND2 
1514 N N   . THR A 212 ? 2.01105 1.58288 3.05532 -0.18317 -0.58159 -0.23425 220 THR C N   
1515 C CA  . THR A 212 ? 2.03344 1.57454 3.05295 -0.17975 -0.62053 -0.17310 220 THR C CA  
1516 C C   . THR A 212 ? 2.02443 1.59864 3.07385 -0.17377 -0.61418 -0.13790 220 THR C C   
1517 O O   . THR A 212 ? 1.99976 1.59833 3.07095 -0.18580 -0.58164 -0.13843 220 THR C O   
1518 C CB  . THR A 212 ? 2.04154 1.52542 3.01287 -0.21272 -0.63214 -0.12994 220 THR C CB  
1519 O OG1 . THR A 212 ? 2.05746 1.50829 2.99509 -0.22260 -0.62543 -0.16779 220 THR C OG1 
1520 C CG2 . THR A 212 ? 2.06270 1.51430 3.01253 -0.21154 -0.67537 -0.08035 220 THR C CG2 
1521 N N   . LYS A 213 ? 2.05126 1.62118 3.09656 -0.15449 -0.64234 -0.11029 221 LYS C N   
1522 C CA  . LYS A 213 ? 2.05673 1.65371 3.12480 -0.14908 -0.63378 -0.07531 221 LYS C CA  
1523 C C   . LYS A 213 ? 2.08518 1.64956 3.12979 -0.15700 -0.66106 -0.01846 221 LYS C C   
1524 O O   . LYS A 213 ? 2.12820 1.66060 3.14200 -0.14172 -0.68889 -0.01968 221 LYS C O   
1525 C CB  . LYS A 213 ? 2.07484 1.70842 3.16522 -0.11372 -0.62939 -0.11268 221 LYS C CB  
1526 C CG  . LYS A 213 ? 2.06683 1.73885 3.18854 -0.11276 -0.60097 -0.09876 221 LYS C CG  
1527 N N   . VAL A 214 ? 2.10398 1.67505 3.16388 -0.18038 -0.65331 0.02911  222 VAL C N   
1528 C CA  . VAL A 214 ? 2.11180 1.66046 3.16286 -0.19686 -0.67522 0.08104  222 VAL C CA  
1529 C C   . VAL A 214 ? 2.11399 1.70210 3.20332 -0.19648 -0.65544 0.11604  222 VAL C C   
1530 O O   . VAL A 214 ? 2.07839 1.69528 3.20025 -0.20528 -0.63707 0.12763  222 VAL C O   
1531 C CB  . VAL A 214 ? 2.07062 1.59034 3.11001 -0.22896 -0.69255 0.10344  222 VAL C CB  
1532 C CG1 . VAL A 214 ? 2.06240 1.57234 3.10982 -0.24984 -0.71335 0.15458  222 VAL C CG1 
1533 C CG2 . VAL A 214 ? 2.08042 1.55484 3.07493 -0.22974 -0.70971 0.06887  222 VAL C CG2 
1534 N N   . ASP A 215 ? 2.07760 1.65960 3.15689 -0.18678 -0.65894 0.13406  223 ASP C N   
1535 C CA  . ASP A 215 ? 2.09241 1.70987 3.20505 -0.18697 -0.63576 0.16645  223 ASP C CA  
1536 C C   . ASP A 215 ? 2.09076 1.69128 3.20633 -0.21595 -0.65011 0.21240  223 ASP C C   
1537 O O   . ASP A 215 ? 2.15059 1.71707 3.23078 -0.21581 -0.65635 0.22493  223 ASP C O   
1538 C CB  . ASP A 215 ? 2.16567 1.78475 3.25714 -0.15524 -0.62239 0.14880  223 ASP C CB  
1539 C CG  . ASP A 215 ? 2.16049 1.79879 3.25506 -0.12890 -0.61349 0.09624  223 ASP C CG  
1540 O OD1 . ASP A 215 ? 2.11582 1.75081 3.21248 -0.13440 -0.62095 0.06713  223 ASP C OD1 
1541 O OD2 . ASP A 215 ? 2.20194 1.85781 3.29622 -0.10447 -0.59752 0.08193  223 ASP C OD2 
1542 N N   . LYS A 216 ? 2.15347 1.77419 3.30913 -0.24166 -0.65621 0.23623  224 LYS C N   
1543 C CA  . LYS A 216 ? 2.13664 1.74842 3.30754 -0.27437 -0.67449 0.27405  224 LYS C CA  
1544 C C   . LYS A 216 ? 2.14065 1.80830 3.37542 -0.28291 -0.64936 0.30687  224 LYS C C   
1545 O O   . LYS A 216 ? 2.11676 1.83296 3.39795 -0.27109 -0.63054 0.30678  224 LYS C O   
1546 C CB  . LYS A 216 ? 2.06903 1.66734 3.24547 -0.29700 -0.70473 0.27756  224 LYS C CB  
1547 C CG  . LYS A 216 ? 2.03233 1.65919 3.26533 -0.32842 -0.71816 0.31659  224 LYS C CG  
1548 C CD  . LYS A 216 ? 1.99492 1.58224 3.20846 -0.35512 -0.76078 0.32108  224 LYS C CD  
1549 N N   . LYS A 217 ? 2.12202 1.77995 3.35902 -0.30530 -0.64780 0.33403  225 LYS C N   
1550 C CA  . LYS A 217 ? 2.13391 1.84913 3.43787 -0.31761 -0.61886 0.36282  225 LYS C CA  
1551 C C   . LYS A 217 ? 2.06257 1.81638 3.43857 -0.34887 -0.64088 0.38453  225 LYS C C   
1552 O O   . LYS A 217 ? 2.05280 1.76999 3.41129 -0.37619 -0.67534 0.39049  225 LYS C O   
1553 C CB  . LYS A 217 ? 2.22474 1.90898 3.49400 -0.33045 -0.59803 0.38010  225 LYS C CB  
1554 N N   . VAL A 218 ? 2.16572 1.99119 3.62152 -0.34209 -0.62453 0.39378  226 VAL C N   
1555 C CA  . VAL A 218 ? 2.10307 1.97617 3.63957 -0.36484 -0.64875 0.41145  226 VAL C CA  
1556 C C   . VAL A 218 ? 2.11957 2.05292 3.73358 -0.38671 -0.61894 0.43466  226 VAL C C   
1557 O O   . VAL A 218 ? 2.14122 2.12187 3.79162 -0.36707 -0.57689 0.43605  226 VAL C O   
1558 C CB  . VAL A 218 ? 2.06086 1.96731 3.63219 -0.33824 -0.65744 0.40267  226 VAL C CB  
1559 C CG1 . VAL A 218 ? 2.01140 1.95077 3.64960 -0.35724 -0.69764 0.41682  226 VAL C CG1 
1560 C CG2 . VAL A 218 ? 2.05914 1.90399 3.54669 -0.31807 -0.66923 0.37584  226 VAL C CG2 
1561 N N   . GLU A 219 ? 2.02287 1.95309 3.66144 -0.42937 -0.63780 0.45068  227 GLU C N   
1562 C CA  . GLU A 219 ? 2.03486 2.02310 3.75299 -0.46048 -0.60720 0.47039  227 GLU C CA  
1563 C C   . GLU A 219 ? 1.97565 1.99651 3.76896 -0.50041 -0.64898 0.48025  227 GLU C C   
1564 O O   . GLU A 219 ? 1.95757 1.92318 3.70376 -0.51180 -0.69844 0.47551  227 GLU C O   
1565 C CB  . GLU A 219 ? 2.12974 2.05822 3.77456 -0.48019 -0.57180 0.47913  227 GLU C CB  
1566 C CG  . GLU A 219 ? 2.14706 2.00683 3.74441 -0.52402 -0.60122 0.48799  227 GLU C CG  
1567 C CD  . GLU A 219 ? 2.25623 2.01954 3.73521 -0.52551 -0.57890 0.49033  227 GLU C CD  
1568 O OE1 . GLU A 219 ? 2.32825 2.09113 3.77876 -0.50262 -0.53358 0.49006  227 GLU C OE1 
1569 O OE2 . GLU A 219 ? 2.27734 1.95883 3.68562 -0.54731 -0.60937 0.49164  227 GLU C OE2 
1570 N N   . PRO A 220 ? 1.90166 2.01459 3.81552 -0.52167 -0.63092 0.49081  228 PRO C N   
1571 C CA  . PRO A 220 ? 1.85159 2.01477 3.86047 -0.55882 -0.67264 0.49590  228 PRO C CA  
1572 C C   . PRO A 220 ? 1.88348 1.97623 3.84049 -0.61008 -0.69827 0.50309  228 PRO C C   
1573 O O   . PRO A 220 ? 1.94804 1.98591 3.84123 -0.63304 -0.66195 0.51173  228 PRO C O   
1574 C CB  . PRO A 220 ? 1.83617 2.11041 3.97776 -0.57338 -0.62698 0.50205  228 PRO C CB  
1575 C CG  . PRO A 220 ? 1.84492 2.14193 3.97633 -0.52237 -0.58165 0.49618  228 PRO C CG  
1576 C CD  . PRO A 220 ? 1.90848 2.09705 3.88819 -0.49771 -0.57599 0.49124  228 PRO C CD  
1577 N N   . THR B 5   ? 2.50454 1.77190 2.98605 -0.01909 -0.74141 0.00227  5   THR D N   
1578 C CA  . THR B 5   ? 2.49040 1.75173 3.08813 -0.00825 -0.77021 -0.00458 5   THR D CA  
1579 C C   . THR B 5   ? 2.50491 1.70920 3.14515 -0.02416 -0.73074 0.05675  5   THR D C   
1580 O O   . THR B 5   ? 2.54229 1.70819 3.09710 -0.03744 -0.68611 0.10438  5   THR D O   
1581 C CB  . THR B 5   ? 2.51013 1.80471 3.07818 0.01406  -0.80368 -0.02485 5   THR D CB  
1582 O OG1 . THR B 5   ? 2.56232 1.82455 3.06168 0.00843  -0.77221 0.02829  5   THR D OG1 
1583 C CG2 . THR B 5   ? 2.53324 1.87814 3.00234 0.02934  -0.82380 -0.06803 5   THR D CG2 
1584 N N   . GLN B 6   ? 2.45244 1.65215 3.22533 -0.02219 -0.74797 0.05538  6   GLN D N   
1585 C CA  . GLN B 6   ? 2.52811 1.68706 3.35526 -0.03243 -0.71116 0.11140  6   GLN D CA  
1586 C C   . GLN B 6   ? 2.58799 1.77348 3.48426 -0.01798 -0.73434 0.11079  6   GLN D C   
1587 O O   . GLN B 6   ? 2.55065 1.77981 3.49289 -0.00258 -0.78756 0.06147  6   GLN D O   
1588 C CB  . GLN B 6   ? 2.49391 1.62225 3.43029 -0.04853 -0.70082 0.12094  6   GLN D CB  
1589 N N   . SER B 7   ? 2.45332 1.61213 3.35458 -0.01940 -0.69555 0.16458  7   SER D N   
1590 C CA  . SER B 7   ? 2.51722 1.70240 3.49046 -0.00438 -0.71021 0.17104  7   SER D CA  
1591 C C   . SER B 7   ? 2.57835 1.73233 3.59372 -0.01022 -0.65668 0.23316  7   SER D C   
1592 O O   . SER B 7   ? 2.60240 1.70698 3.51297 -0.01311 -0.61014 0.27574  7   SER D O   
1593 C CB  . SER B 7   ? 2.56941 1.76732 3.42663 0.01782  -0.72886 0.16093  7   SER D CB  
1594 O OG  . SER B 7   ? 2.60770 1.75950 3.31355 0.01350  -0.68759 0.19967  7   SER D OG  
1595 N N   . PRO B 8   ? 2.48281 1.66547 3.64866 -0.01082 -0.66124 0.24102  8   PRO D N   
1596 C CA  . PRO B 8   ? 2.45103 1.69182 3.75404 -0.00588 -0.71876 0.19656  8   PRO D CA  
1597 C C   . PRO B 8   ? 2.34661 1.59429 3.75291 -0.02522 -0.75369 0.15857  8   PRO D C   
1598 O O   . PRO B 8   ? 2.32096 1.52896 3.72422 -0.04510 -0.72598 0.17523  8   PRO D O   
1599 C CB  . PRO B 8   ? 2.50771 1.77032 3.92513 -0.00381 -0.69198 0.23744  8   PRO D CB  
1600 C CG  . PRO B 8   ? 2.49768 1.70942 3.89630 -0.02062 -0.62290 0.29586  8   PRO D CG  
1601 C CD  . PRO B 8   ? 2.50600 1.66305 3.71962 -0.01748 -0.60313 0.30164  8   PRO D CD  
1602 N N   . SER B 9   ? 2.44595 1.73815 3.94068 -0.01688 -0.82014 0.10449  9   SER D N   
1603 C CA  . SER B 9   ? 2.34148 1.63468 3.94625 -0.03344 -0.86091 0.06743  9   SER D CA  
1604 C C   . SER B 9   ? 2.34655 1.63005 4.10348 -0.06278 -0.83272 0.10922  9   SER D C   
1605 O O   . SER B 9   ? 2.31135 1.55844 4.10771 -0.08514 -0.82755 0.11208  9   SER D O   
1606 C CB  . SER B 9   ? 2.25021 1.58902 3.91637 -0.01413 -0.94324 0.00031  9   SER D CB  
1607 O OG  . SER B 9   ? 2.25332 1.63218 4.05150 -0.01283 -0.95967 0.00907  9   SER D OG  
1608 N N   . SER B 10  ? 2.26773 1.58418 4.10915 -0.06197 -0.81359 0.14276  10  SER D N   
1609 C CA  . SER B 10  ? 2.26985 1.58915 4.25821 -0.08961 -0.77810 0.19019  10  SER D CA  
1610 C C   . SER B 10  ? 2.32360 1.68166 4.33268 -0.07456 -0.73982 0.23206  10  SER D C   
1611 O O   . SER B 10  ? 2.33285 1.72605 4.30020 -0.04543 -0.76877 0.20759  10  SER D O   
1612 C CB  . SER B 10  ? 2.18482 1.53107 4.35729 -0.11135 -0.83844 0.15576  10  SER D CB  
1613 O OG  . SER B 10  ? 2.19647 1.59863 4.41944 -0.08993 -0.90637 0.10437  10  SER D OG  
1614 N N   . LEU B 11  ? 2.22743 1.57778 4.29694 -0.09124 -0.67522 0.29472  11  LEU D N   
1615 C CA  . LEU B 11  ? 2.24906 1.63566 4.32926 -0.07184 -0.63115 0.33770  11  LEU D CA  
1616 C C   . LEU B 11  ? 2.22195 1.62864 4.45531 -0.09871 -0.58202 0.39174  11  LEU D C   
1617 O O   . LEU B 11  ? 2.22410 1.58201 4.47231 -0.12717 -0.55248 0.41791  11  LEU D O   
1618 C CB  . LEU B 11  ? 2.31230 1.64765 4.19570 -0.04639 -0.57950 0.37020  11  LEU D CB  
1619 N N   . SER B 12  ? 2.16857 1.64794 4.51285 -0.08835 -0.57203 0.40958  12  SER D N   
1620 C CA  . SER B 12  ? 2.16566 1.67937 4.65822 -0.11161 -0.51656 0.46703  12  SER D CA  
1621 C C   . SER B 12  ? 2.17003 1.71573 4.61772 -0.07527 -0.45738 0.51141  12  SER D C   
1622 O O   . SER B 12  ? 2.16824 1.78415 4.66728 -0.04917 -0.48364 0.49228  12  SER D O   
1623 C CB  . SER B 12  ? 2.16590 1.75484 4.88655 -0.14062 -0.56737 0.44350  12  SER D CB  
1624 O OG  . SER B 12  ? 2.16132 1.82172 4.92465 -0.11148 -0.61997 0.40195  12  SER D OG  
1625 N N   . ALA B 13  ? 2.19679 1.68695 4.54444 -0.06984 -0.38153 0.56787  13  ALA D N   
1626 C CA  . ALA B 13  ? 2.20916 1.72091 4.52530 -0.03737 -0.31282 0.62112  13  ALA D CA  
1627 C C   . ALA B 13  ? 2.21237 1.73963 4.65131 -0.06582 -0.24447 0.68369  13  ALA D C   
1628 O O   . ALA B 13  ? 2.21161 1.73828 4.77295 -0.11257 -0.25883 0.68261  13  ALA D O   
1629 C CB  . ALA B 13  ? 2.26581 1.69138 4.34733 -0.00251 -0.28410 0.63458  13  ALA D CB  
1630 N N   . SER B 14  ? 2.23447 1.77226 4.63690 -0.03643 -0.17048 0.73924  14  SER D N   
1631 C CA  . SER B 14  ? 2.25981 1.81189 4.75854 -0.05729 -0.09444 0.80598  14  SER D CA  
1632 C C   . SER B 14  ? 2.29336 1.74579 4.60821 -0.03463 -0.02638 0.85389  14  SER D C   
1633 O O   . SER B 14  ? 2.29311 1.66543 4.41985 -0.00996 -0.04329 0.83329  14  SER D O   
1634 C CB  . SER B 14  ? 2.26514 1.93871 4.91733 -0.04091 -0.06191 0.83278  14  SER D CB  
1635 O OG  . SER B 14  ? 2.23587 1.99189 5.00145 -0.04097 -0.13742 0.77578  14  SER D OG  
1636 N N   . VAL B 15  ? 2.32828 1.78465 4.70051 -0.04472 0.05026  0.91928  15  VAL D N   
1637 C CA  . VAL B 15  ? 2.37116 1.72901 4.57639 -0.02211 0.11570  0.96739  15  VAL D CA  
1638 C C   . VAL B 15  ? 2.38734 1.73692 4.44138 0.04415  0.13825  0.97397  15  VAL D C   
1639 O O   . VAL B 15  ? 2.38903 1.83025 4.51388 0.07469  0.15349  0.98153  15  VAL D O   
1640 C CB  . VAL B 15  ? 2.41590 1.78707 4.72041 -0.04382 0.19545  1.03873  15  VAL D CB  
1641 C CG1 . VAL B 15  ? 2.46537 1.71109 4.59481 -0.02982 0.24730  1.07946  15  VAL D CG1 
1642 C CG2 . VAL B 15  ? 2.40322 1.81031 4.90278 -0.11112 0.16469  1.03089  15  VAL D CG2 
1643 N N   . GLY B 16  ? 2.40351 1.64208 4.24976 0.06745  0.13638  0.96936  16  GLY D N   
1644 C CA  . GLY B 16  ? 2.42823 1.63667 4.11226 0.12772  0.14860  0.97344  16  GLY D CA  
1645 C C   . GLY B 16  ? 2.40570 1.61848 4.02057 0.14193  0.07331  0.91261  16  GLY D C   
1646 O O   . GLY B 16  ? 2.45412 1.59718 3.88811 0.17950  0.06737  0.90846  16  GLY D O   
1647 N N   . ASP B 17  ? 2.38091 1.66923 4.13182 0.11303  0.01399  0.86628  17  ASP D N   
1648 C CA  . ASP B 17  ? 2.39002 1.68282 4.07447 0.12715  -0.05813 0.80863  17  ASP D CA  
1649 C C   . ASP B 17  ? 2.43399 1.61829 3.93943 0.11859  -0.08508 0.78729  17  ASP D C   
1650 O O   . ASP B 17  ? 2.42551 1.57374 3.94973 0.07816  -0.09686 0.77685  17  ASP D O   
1651 C CB  . ASP B 17  ? 2.33918 1.71915 4.19837 0.09434  -0.12028 0.76065  17  ASP D CB  
1652 C CG  . ASP B 17  ? 2.29413 1.79187 4.34869 0.09833  -0.10054 0.77781  17  ASP D CG  
1653 O OD1 . ASP B 17  ? 2.31285 1.82957 4.39993 0.11211  -0.02700 0.83458  17  ASP D OD1 
1654 O OD2 . ASP B 17  ? 2.26115 1.83470 4.43695 0.08900  -0.15974 0.73341  17  ASP D OD2 
1655 N N   . ARG B 18  ? 2.53579 1.66793 3.86944 0.15654  -0.09589 0.78129  18  ARG D N   
1656 C CA  . ARG B 18  ? 2.56937 1.60975 3.73998 0.14613  -0.12496 0.75957  18  ARG D CA  
1657 C C   . ARG B 18  ? 2.54700 1.62124 3.77064 0.11309  -0.19531 0.69928  18  ARG D C   
1658 O O   . ARG B 18  ? 2.54191 1.68583 3.83692 0.12115  -0.23740 0.66635  18  ARG D O   
1659 C CB  . ARG B 18  ? 2.63159 1.61348 3.61853 0.19101  -0.12747 0.76638  18  ARG D CB  
1660 C CG  . ARG B 18  ? 2.68343 1.57539 3.49944 0.17960  -0.15742 0.74729  18  ARG D CG  
1661 C CD  . ARG B 18  ? 2.74753 1.54691 3.38692 0.21748  -0.12661 0.78431  18  ARG D CD  
1662 N NE  . ARG B 18  ? 2.80338 1.53020 3.27822 0.21247  -0.16524 0.76418  18  ARG D NE  
1663 C CZ  . ARG B 18  ? 2.85611 1.48308 3.18033 0.21981  -0.14926 0.78754  18  ARG D CZ  
1664 N NH1 . ARG B 18  ? 2.86713 1.46835 3.14769 0.23265  -0.09508 0.80809  18  ARG D NH1 
1665 N NH2 . ARG B 18  ? 2.90168 1.47565 3.09087 0.20953  -0.18714 0.76761  18  ARG D NH2 
1666 N N   . VAL B 19  ? 2.50219 1.52628 3.68655 0.08028  -0.20977 0.68290  19  VAL D N   
1667 C CA  . VAL B 19  ? 2.47489 1.52976 3.71370 0.05031  -0.27247 0.62593  19  VAL D CA  
1668 C C   . VAL B 19  ? 2.46103 1.44376 3.54033 0.04205  -0.29222 0.60567  19  VAL D C   
1669 O O   . VAL B 19  ? 2.45515 1.36708 3.45494 0.03647  -0.25784 0.63312  19  VAL D O   
1670 C CB  . VAL B 19  ? 2.45918 1.54741 3.86896 0.01260  -0.27250 0.62305  19  VAL D CB  
1671 C CG1 . VAL B 19  ? 2.47273 1.65393 4.06195 0.01400  -0.27206 0.62884  19  VAL D CG1 
1672 C CG2 . VAL B 19  ? 2.46004 1.48300 3.84474 0.00217  -0.21306 0.67234  19  VAL D CG2 
1673 N N   . THR B 20  ? 2.50497 1.50775 3.54013 0.04115  -0.34784 0.55736  20  THR D N   
1674 C CA  . THR B 20  ? 2.49908 1.44535 3.38130 0.03388  -0.36401 0.54033  20  THR D CA  
1675 C C   . THR B 20  ? 2.48754 1.47400 3.40596 0.01372  -0.42181 0.48031  20  THR D C   
1676 O O   . THR B 20  ? 2.50170 1.54439 3.46711 0.02271  -0.46447 0.44596  20  THR D O   
1677 C CB  . THR B 20  ? 2.53024 1.44027 3.25742 0.06191  -0.36415 0.55352  20  THR D CB  
1678 O OG1 . THR B 20  ? 2.54616 1.39723 3.20745 0.08196  -0.31097 0.60754  20  THR D OG1 
1679 C CG2 . THR B 20  ? 2.53003 1.40295 3.12037 0.04781  -0.39138 0.52861  20  THR D CG2 
1680 N N   . ILE B 21  ? 2.51168 1.46776 3.40388 -0.00906 -0.42442 0.46640  21  ILE D N   
1681 C CA  . ILE B 21  ? 2.50726 1.49265 3.40656 -0.02375 -0.47496 0.40937  21  ILE D CA  
1682 C C   . ILE B 21  ? 2.51883 1.47631 3.25093 -0.02043 -0.48305 0.39989  21  ILE D C   
1683 O O   . ILE B 21  ? 2.51728 1.41484 3.13845 -0.01809 -0.44801 0.43716  21  ILE D O   
1684 C CB  . ILE B 21  ? 2.48202 1.45109 3.45302 -0.04771 -0.47311 0.39960  21  ILE D CB  
1685 C CG1 . ILE B 21  ? 2.47665 1.44904 3.58656 -0.05471 -0.44408 0.43392  21  ILE D CG1 
1686 C CG2 . ILE B 21  ? 2.48737 1.50015 3.50260 -0.05627 -0.53172 0.33517  21  ILE D CG2 
1687 C CD1 . ILE B 21  ? 2.45937 1.40654 3.64353 -0.07873 -0.44440 0.42855  21  ILE D CD1 
1688 N N   . THR B 22  ? 2.56351 1.56349 3.27551 -0.02011 -0.53017 0.35077  22  THR D N   
1689 C CA  . THR B 22  ? 2.58323 1.56727 3.14407 -0.02141 -0.53821 0.34138  22  THR D CA  
1690 C C   . THR B 22  ? 2.58113 1.59971 3.14717 -0.03429 -0.57070 0.28944  22  THR D C   
1691 O O   . THR B 22  ? 2.58285 1.64939 3.25342 -0.03176 -0.60800 0.24688  22  THR D O   
1692 C CB  . THR B 22  ? 2.62503 1.62433 3.11939 -0.00112 -0.55981 0.33831  22  THR D CB  
1693 O OG1 . THR B 22  ? 2.63101 1.60352 3.13146 0.01689  -0.53256 0.38226  22  THR D OG1 
1694 C CG2 . THR B 22  ? 2.65368 1.62529 2.98213 -0.00770 -0.56036 0.34133  22  THR D CG2 
1695 N N   . CYS B 23  ? 2.61667 1.61136 3.07115 -0.04659 -0.55791 0.29246  23  CYS D N   
1696 C CA  . CYS B 23  ? 2.61875 1.64609 3.06115 -0.05675 -0.57963 0.24791  23  CYS D CA  
1697 C C   . CYS B 23  ? 2.65721 1.69974 2.96430 -0.05916 -0.58619 0.24064  23  CYS D C   
1698 O O   . CYS B 23  ? 2.66528 1.66247 2.86653 -0.06563 -0.55995 0.28217  23  CYS D O   
1699 C CB  . CYS B 23  ? 2.57920 1.56609 3.02486 -0.07209 -0.55277 0.26183  23  CYS D CB  
1700 S SG  . CYS B 23  ? 2.57423 1.60277 3.06474 -0.07749 -0.58329 0.20159  23  CYS D SG  
1701 N N   . ARG B 24  ? 2.61462 1.71847 2.92608 -0.05329 -0.62233 0.18831  24  ARG D N   
1702 C CA  . ARG B 24  ? 2.66031 1.78822 2.84481 -0.05658 -0.62731 0.18024  24  ARG D CA  
1703 C C   . ARG B 24  ? 2.65643 1.80032 2.79650 -0.07484 -0.61328 0.16859  24  ARG D C   
1704 O O   . ARG B 24  ? 2.62969 1.78441 2.85112 -0.07492 -0.61856 0.14357  24  ARG D O   
1705 C CB  . ARG B 24  ? 2.69544 1.88417 2.89502 -0.03480 -0.67280 0.12984  24  ARG D CB  
1706 C CG  . ARG B 24  ? 2.75362 1.94617 2.82252 -0.03131 -0.67672 0.14006  24  ARG D CG  
1707 C CD  . ARG B 24  ? 2.77127 2.01855 2.76462 -0.03567 -0.68335 0.10758  24  ARG D CD  
1708 N NE  . ARG B 24  ? 2.77961 2.08744 2.82598 -0.00768 -0.72874 0.04553  24  ARG D NE  
1709 C CZ  . ARG B 24  ? 2.80972 2.12619 2.85805 0.01827  -0.76437 0.02704  24  ARG D CZ  
1710 N NH1 . ARG B 24  ? 2.86303 2.17163 2.78924 0.02202  -0.76436 0.04337  24  ARG D NH1 
1711 N NH2 . ARG B 24  ? 2.79104 2.12045 2.96337 0.03967  -0.80248 -0.00716 24  ARG D NH2 
1712 N N   . ALA B 25  ? 2.78777 1.93273 2.80574 -0.09011 -0.59787 0.18646  25  ALA D N   
1713 C CA  . ALA B 25  ? 2.78873 1.96168 2.76175 -0.10923 -0.58394 0.17622  25  ALA D CA  
1714 C C   . ALA B 25  ? 2.85072 2.07763 2.72288 -0.11482 -0.58935 0.16384  25  ALA D C   
1715 O O   . ALA B 25  ? 2.87464 2.07469 2.64208 -0.13754 -0.56795 0.20393  25  ALA D O   
1716 C CB  . ALA B 25  ? 2.75200 1.85722 2.68174 -0.13203 -0.54871 0.22592  25  ALA D CB  
1717 N N   . SER B 26  ? 2.67373 1.97289 2.57465 -0.09357 -0.61901 0.10938  26  SER D N   
1718 C CA  . SER B 26  ? 2.90467 2.26302 2.71138 -0.09308 -0.62378 0.09333  26  SER D CA  
1719 C C   . SER B 26  ? 3.05759 2.43601 2.78029 -0.12672 -0.58985 0.11697  26  SER D C   
1720 O O   . SER B 26  ? 3.13107 2.49960 2.74520 -0.14647 -0.57489 0.15137  26  SER D O   
1721 C CB  . SER B 26  ? 3.01437 2.45106 2.87477 -0.06093 -0.65924 0.02361  26  SER D CB  
1722 O OG  . SER B 26  ? 3.07655 2.56082 2.97407 -0.06400 -0.65269 -0.00660 26  SER D OG  
1723 N N   . ALA B 28  ? 2.80201 2.06288 2.36558 -0.24126 -0.49678 0.25532  28  ALA D N   
1724 C CA  . ALA B 28  ? 2.63607 1.85448 2.29662 -0.22389 -0.50040 0.24524  28  ALA D CA  
1725 C C   . ALA B 28  ? 2.68246 1.90695 2.35643 -0.24438 -0.48548 0.24613  28  ALA D C   
1726 O O   . ALA B 28  ? 2.83920 2.10451 2.45307 -0.27385 -0.47252 0.25633  28  ALA D O   
1727 C CB  . ALA B 28  ? 2.40021 1.51433 2.05033 -0.21739 -0.49724 0.28943  28  ALA D CB  
1728 N N   . ALA B 29  ? 2.60560 1.79090 2.35657 -0.22975 -0.48800 0.23659  29  ALA D N   
1729 C CA  . ALA B 29  ? 2.63097 1.81210 2.39354 -0.24414 -0.47863 0.23566  29  ALA D CA  
1730 C C   . ALA B 29  ? 2.42865 1.49425 2.15453 -0.25492 -0.46478 0.28909  29  ALA D C   
1731 O O   . ALA B 29  ? 2.28919 1.29540 2.06535 -0.23811 -0.46455 0.29111  29  ALA D O   
1732 C CB  . ALA B 29  ? 2.61929 1.83768 2.48269 -0.21772 -0.49483 0.18234  29  ALA D CB  
1733 N N   . TYR B 30  ? 2.40786 1.43755 2.03832 -0.28200 -0.45447 0.33351  36  TYR D N   
1734 C CA  . TYR B 30  ? 2.38260 1.30987 1.95464 -0.29725 -0.44493 0.38249  36  TYR D CA  
1735 C C   . TYR B 30  ? 2.37152 1.20135 1.97331 -0.26800 -0.44135 0.40187  36  TYR D C   
1736 O O   . TYR B 30  ? 2.37833 1.13523 1.96734 -0.26728 -0.43587 0.42216  36  TYR D O   
1737 C CB  . TYR B 30  ? 2.48844 1.43886 2.06515 -0.31882 -0.44341 0.37293  36  TYR D CB  
1738 C CG  . TYR B 30  ? 2.69096 1.73491 2.23157 -0.35425 -0.44038 0.36556  36  TYR D CG  
1739 C CD1 . TYR B 30  ? 2.68507 1.72235 2.13861 -0.38046 -0.43581 0.40052  36  TYR D CD1 
1740 C CD2 . TYR B 30  ? 2.86758 2.00720 2.46009 -0.36062 -0.44146 0.32470  36  TYR D CD2 
1741 C CE1 . TYR B 30  ? 2.83262 1.95676 2.25211 -0.41618 -0.42863 0.39906  36  TYR D CE1 
1742 C CE2 . TYR B 30  ? 3.00808 2.24452 2.57269 -0.39342 -0.43334 0.32022  36  TYR D CE2 
1743 C CZ  . TYR B 30  ? 2.98294 2.21148 2.46119 -0.42315 -0.42504 0.35959  36  TYR D CZ  
1744 O OH  . TYR B 30  ? 3.03361 2.35937 2.48276 -0.45914 -0.41276 0.36038  36  TYR D OH  
1745 N N   . GLY B 31  ? 2.50373 1.33474 2.14576 -0.24286 -0.44445 0.39574  37  GLY D N   
1746 C CA  . GLY B 31  ? 2.48090 1.23080 2.15317 -0.21634 -0.43607 0.41911  37  GLY D CA  
1747 C C   . GLY B 31  ? 2.43233 1.15506 2.17284 -0.20281 -0.43142 0.40649  37  GLY D C   
1748 O O   . GLY B 31  ? 2.42827 1.06062 2.15217 -0.18998 -0.41733 0.44075  37  GLY D O   
1749 N N   . ARG B 32  ? 2.47966 1.27408 2.28731 -0.20309 -0.44379 0.35828  38  ARG D N   
1750 C CA  . ARG B 32  ? 2.43913 1.20897 2.31745 -0.18727 -0.44531 0.33997  38  ARG D CA  
1751 C C   . ARG B 32  ? 2.42956 1.22599 2.40761 -0.16617 -0.45489 0.31453  38  ARG D C   
1752 O O   . ARG B 32  ? 2.43105 1.30735 2.46592 -0.16213 -0.47633 0.26516  38  ARG D O   
1753 C CB  . ARG B 32  ? 2.42337 1.24906 2.31251 -0.19746 -0.45789 0.30101  38  ARG D CB  
1754 N N   . VAL B 33  ? 2.48681 1.21713 2.48817 -0.15171 -0.44004 0.34817  39  VAL D N   
1755 C CA  . VAL B 33  ? 2.48310 1.23724 2.58286 -0.13672 -0.44864 0.33232  39  VAL D CA  
1756 C C   . VAL B 33  ? 2.46241 1.14133 2.61310 -0.12417 -0.43146 0.35663  39  VAL D C   
1757 O O   . VAL B 33  ? 2.46347 1.06323 2.55585 -0.12149 -0.40841 0.39530  39  VAL D O   
1758 C CB  . VAL B 33  ? 2.51303 1.28311 2.60042 -0.13255 -0.44711 0.35053  39  VAL D CB  
1759 C CG1 . VAL B 33  ? 2.51350 1.32782 2.71391 -0.11982 -0.46554 0.32319  39  VAL D CG1 
1760 C CG2 . VAL B 33  ? 2.54722 1.36814 2.55358 -0.14666 -0.45794 0.34032  39  VAL D CG2 
1761 N N   . ALA B 34  ? 2.39503 1.09606 2.65330 -0.11631 -0.44447 0.33391  40  ALA D N   
1762 C CA  . ALA B 34  ? 2.38549 1.01996 2.70141 -0.10775 -0.42634 0.36041  40  ALA D CA  
1763 C C   . ALA B 34  ? 2.39154 1.05471 2.81142 -0.10362 -0.43057 0.36120  40  ALA D C   
1764 O O   . ALA B 34  ? 2.40135 1.13679 2.85977 -0.10465 -0.45801 0.32749  40  ALA D O   
1765 C CB  . ALA B 34  ? 2.36791 0.98368 2.71975 -0.10668 -0.44248 0.33021  40  ALA D CB  
1766 N N   . TRP B 35  ? 2.35427 0.96039 2.81863 -0.09829 -0.40279 0.40123  41  TRP D N   
1767 C CA  . TRP B 35  ? 2.36057 0.99030 2.94122 -0.09798 -0.40301 0.40776  41  TRP D CA  
1768 C C   . TRP B 35  ? 2.35025 0.97374 2.98386 -0.09850 -0.38295 0.40264  41  TRP D C   
1769 O O   . TRP B 35  ? 2.35002 0.94246 2.90560 -0.08953 -0.33647 0.42199  41  TRP D O   
1770 C CB  . TRP B 35  ? 2.37769 1.00860 2.93211 -0.08655 -0.36179 0.45364  41  TRP D CB  
1771 C CG  . TRP B 35  ? 2.39244 1.06233 2.91078 -0.08397 -0.38297 0.44618  41  TRP D CG  
1772 C CD1 . TRP B 35  ? 2.40632 1.05420 2.79972 -0.07875 -0.37196 0.46520  41  TRP D CD1 
1773 C CD2 . TRP B 35  ? 2.40229 1.15043 2.99405 -0.08464 -0.41736 0.41042  41  TRP D CD2 
1774 N NE1 . TRP B 35  ? 2.42438 1.12977 2.80549 -0.07686 -0.39476 0.44620  41  TRP D NE1 
1775 C CE2 . TRP B 35  ? 2.42332 1.19168 2.92323 -0.07832 -0.42281 0.41136  41  TRP D CE2 
1776 C CE3 . TRP B 35  ? 2.40265 1.19984 3.12652 -0.08938 -0.44776 0.37755  41  TRP D CE3 
1777 C CZ2 . TRP B 35  ? 2.44602 1.28120 2.97644 -0.07362 -0.45562 0.38051  41  TRP D CZ2 
1778 C CZ3 . TRP B 35  ? 2.42478 1.29044 3.18349 -0.08421 -0.48285 0.34466  41  TRP D CZ3 
1779 C CH2 . TRP B 35  ? 2.44645 1.33052 3.10629 -0.07492 -0.48558 0.34625  41  TRP D CH2 
1780 N N   . TYR B 36  ? 2.22679 0.87542 2.98770 -0.10795 -0.41940 0.37671  42  TYR D N   
1781 C CA  . TYR B 36  ? 2.24425 0.88679 3.06607 -0.11307 -0.41328 0.36835  42  TYR D CA  
1782 C C   . TYR B 36  ? 2.24677 0.91877 3.19522 -0.12297 -0.41123 0.38410  42  TYR D C   
1783 O O   . TYR B 36  ? 2.22704 0.93130 3.24867 -0.12608 -0.44093 0.37814  42  TYR D O   
1784 C CB  . TYR B 36  ? 2.24170 0.88425 3.10492 -0.11656 -0.47297 0.31098  42  TYR D CB  
1785 C CG  . TYR B 36  ? 2.24340 0.85949 3.00570 -0.10830 -0.48032 0.29084  42  TYR D CG  
1786 C CD1 . TYR B 36  ? 2.22582 0.85339 2.92301 -0.10644 -0.49739 0.28060  42  TYR D CD1 
1787 C CD2 . TYR B 36  ? 2.26729 0.85330 2.99548 -0.10268 -0.46949 0.28166  42  TYR D CD2 
1788 C CE1 . TYR B 36  ? 2.22742 0.84671 2.83852 -0.10165 -0.50243 0.26111  42  TYR D CE1 
1789 C CE2 . TYR B 36  ? 2.26896 0.83417 2.91628 -0.09433 -0.48011 0.26163  42  TYR D CE2 
1790 C CZ  . TYR B 36  ? 2.24946 0.82282 2.84843 -0.09582 -0.50047 0.25353  42  TYR D CZ  
1791 O OH  . TYR B 36  ? 2.25469 0.80892 2.78286 -0.09085 -0.51367 0.23464  42  TYR D OH  
1792 N N   . GLN B 37  ? 2.27716 0.93466 3.25443 -0.12884 -0.38143 0.40170  43  GLN D N   
1793 C CA  . GLN B 37  ? 2.28978 0.97231 3.39179 -0.14315 -0.37310 0.42353  43  GLN D CA  
1794 C C   . GLN B 37  ? 2.31046 0.98859 3.49474 -0.15785 -0.41272 0.39062  43  GLN D C   
1795 O O   . GLN B 37  ? 2.34410 0.98083 3.46759 -0.15560 -0.39700 0.38959  43  GLN D O   
1796 C CB  . GLN B 37  ? 2.32467 0.98627 3.37888 -0.13795 -0.29891 0.48093  43  GLN D CB  
1797 C CG  . GLN B 37  ? 2.34554 1.03299 3.53236 -0.15569 -0.28348 0.51071  43  GLN D CG  
1798 C CD  . GLN B 37  ? 2.37826 1.05316 3.51798 -0.14521 -0.21110 0.56923  43  GLN D CD  
1799 O OE1 . GLN B 37  ? 2.37566 1.09071 3.61666 -0.15088 -0.19320 0.60182  43  GLN D OE1 
1800 N NE2 . GLN B 37  ? 2.41356 1.03190 3.40091 -0.12749 -0.17165 0.58095  43  GLN D NE2 
1801 N N   . GLN B 38  ? 2.29784 1.01351 3.61536 -0.17073 -0.46691 0.36232  44  GLN D N   
1802 C CA  . GLN B 38  ? 2.32260 1.03552 3.72416 -0.18305 -0.51658 0.32490  44  GLN D CA  
1803 C C   . GLN B 38  ? 2.34880 1.08168 3.87620 -0.20613 -0.50071 0.35918  44  GLN D C   
1804 O O   . GLN B 38  ? 2.33117 1.10889 3.97882 -0.21643 -0.53048 0.35336  44  GLN D O   
1805 C CB  . GLN B 38  ? 2.29874 1.03602 3.75075 -0.17716 -0.59787 0.25923  44  GLN D CB  
1806 C CG  . GLN B 38  ? 2.32813 1.06707 3.87331 -0.18471 -0.66240 0.21153  44  GLN D CG  
1807 C CD  . GLN B 38  ? 2.36962 1.06204 3.85759 -0.18250 -0.65527 0.20645  44  GLN D CD  
1808 O OE1 . GLN B 38  ? 2.36667 1.02831 3.73569 -0.16732 -0.63058 0.20725  44  GLN D OE1 
1809 N NE2 . GLN B 38  ? 2.41414 1.09848 3.98793 -0.19737 -0.68171 0.19959  44  GLN D NE2 
1810 N N   . LYS B 39  ? 1.92927 1.28030 3.66348 -0.02763 -0.73849 0.14352  45  LYS D N   
1811 C CA  . LYS B 39  ? 1.91298 1.31828 3.73592 -0.05280 -0.75965 0.10504  45  LYS D CA  
1812 C C   . LYS B 39  ? 1.92433 1.29359 3.72223 -0.05417 -0.76523 0.12490  45  LYS D C   
1813 O O   . LYS B 39  ? 1.92974 1.26987 3.62821 -0.04400 -0.73959 0.16974  45  LYS D O   
1814 C CB  . LYS B 39  ? 1.82216 1.33235 3.69332 -0.11859 -0.72691 0.10556  45  LYS D CB  
1815 N N   . PRO B 40  ? 1.94195 1.37748 3.78958 -0.06672 -0.77872 0.07796  46  PRO D N   
1816 C CA  . PRO B 40  ? 1.95240 1.35719 3.78555 -0.07084 -0.78223 0.08820  46  PRO D CA  
1817 C C   . PRO B 40  ? 1.91655 1.29110 3.70248 -0.10548 -0.74277 0.15739  46  PRO D C   
1818 O O   . PRO B 40  ? 1.86195 1.28498 3.67847 -0.15973 -0.71410 0.17556  46  PRO D O   
1819 C CB  . PRO B 40  ? 1.91790 1.43403 3.82542 -0.10509 -0.78306 0.02625  46  PRO D CB  
1820 C CG  . PRO B 40  ? 1.93299 1.51395 3.88345 -0.08225 -0.80414 -0.03267 46  PRO D CG  
1821 C CD  . PRO B 40  ? 1.93979 1.48064 3.85926 -0.07007 -0.79386 0.00319  46  PRO D CD  
1822 N N   . GLY B 41  ? 1.99251 1.32321 3.67926 -0.07346 -0.73109 0.18877  47  GLY D N   
1823 C CA  . GLY B 41  ? 1.96428 1.29208 3.58283 -0.09416 -0.68804 0.24119  47  GLY D CA  
1824 C C   . GLY B 41  ? 1.90525 1.26731 3.51994 -0.12712 -0.65416 0.28038  47  GLY D C   
1825 O O   . GLY B 41  ? 1.87552 1.25859 3.49424 -0.16120 -0.62857 0.30893  47  GLY D O   
1826 N N   . LYS B 42  ? 1.84488 1.21180 3.44984 -0.11650 -0.65298 0.28113  48  LYS D N   
1827 C CA  . LYS B 42  ? 1.79428 1.19771 3.40472 -0.14715 -0.62574 0.31348  48  LYS D CA  
1828 C C   . LYS B 42  ? 1.79593 1.18018 3.33385 -0.12458 -0.60680 0.32866  48  LYS D C   
1829 O O   . LYS B 42  ? 1.83771 1.17834 3.30318 -0.09138 -0.60507 0.32043  48  LYS D O   
1830 C CB  . LYS B 42  ? 1.76878 1.22029 3.47748 -0.17993 -0.63923 0.28664  48  LYS D CB  
1831 C CG  . LYS B 42  ? 1.75864 1.25095 3.52805 -0.22243 -0.64009 0.27040  48  LYS D CG  
1832 C CD  . LYS B 42  ? 1.73049 1.30734 3.58647 -0.26431 -0.64533 0.22489  48  LYS D CD  
1833 C CE  . LYS B 42  ? 1.69588 1.32748 3.54386 -0.29744 -0.61594 0.25561  48  LYS D CE  
1834 N NZ  . LYS B 42  ? 1.67055 1.41560 3.58405 -0.33881 -0.61070 0.20587  48  LYS D NZ  
1835 N N   . ALA B 43  ? 1.61701 1.03337 3.17158 -0.14622 -0.58983 0.34777  49  ALA D N   
1836 C CA  . ALA B 43  ? 1.61346 1.01386 3.10368 -0.13151 -0.56624 0.36091  49  ALA D CA  
1837 C C   . ALA B 43  ? 1.62905 1.00670 3.12809 -0.10869 -0.57809 0.32761  49  ALA D C   
1838 O O   . ALA B 43  ? 1.61563 1.01939 3.19760 -0.12125 -0.59617 0.30484  49  ALA D O   
1839 C CB  . ALA B 43  ? 1.57923 1.02404 3.08756 -0.16290 -0.54496 0.39431  49  ALA D CB  
1840 N N   . PRO B 44  ? 1.56038 0.88707 2.97392 -0.07718 -0.56552 0.32079  50  PRO D N   
1841 C CA  . PRO B 44  ? 1.58557 0.88212 2.99475 -0.05423 -0.57005 0.29291  50  PRO D CA  
1842 C C   . PRO B 44  ? 1.54808 0.87659 3.00895 -0.07707 -0.55541 0.29546  50  PRO D C   
1843 O O   . PRO B 44  ? 1.53233 0.86715 2.95933 -0.09004 -0.52566 0.31910  50  PRO D O   
1844 C CB  . PRO B 44  ? 1.63517 0.86800 2.92336 -0.02617 -0.54533 0.29761  50  PRO D CB  
1845 C CG  . PRO B 44  ? 1.64323 0.87210 2.88799 -0.02782 -0.54113 0.31464  50  PRO D CG  
1846 C CD  . PRO B 44  ? 1.58642 0.87650 2.90025 -0.06317 -0.54245 0.33663  50  PRO D CD  
1847 N N   . LYS B 45  ? 1.49960 0.85026 3.04979 -0.08273 -0.57704 0.26577  51  LYS D N   
1848 C CA  . LYS B 45  ? 1.47599 0.85582 3.08393 -0.10572 -0.56309 0.25687  51  LYS D CA  
1849 C C   . LYS B 45  ? 1.52176 0.84805 3.09946 -0.07208 -0.55737 0.22700  51  LYS D C   
1850 O O   . LYS B 45  ? 1.56451 0.85055 3.11939 -0.03552 -0.57909 0.20331  51  LYS D O   
1851 C CB  . LYS B 45  ? 1.43597 0.88237 3.16335 -0.14441 -0.58257 0.23326  51  LYS D CB  
1852 N N   . LEU B 46  ? 1.59814 0.92270 3.17358 -0.08425 -0.52727 0.22746  52  LEU D N   
1853 C CA  . LEU B 46  ? 1.64470 0.90993 3.18337 -0.05463 -0.51456 0.20121  52  LEU D CA  
1854 C C   . LEU B 46  ? 1.63379 0.92606 3.28135 -0.06022 -0.53029 0.15486  52  LEU D C   
1855 O O   . LEU B 46  ? 1.58335 0.94888 3.33182 -0.10354 -0.53405 0.14255  52  LEU D O   
1856 C CB  . LEU B 46  ? 1.65721 0.89439 3.13637 -0.06309 -0.46967 0.21575  52  LEU D CB  
1857 C CG  . LEU B 46  ? 1.62450 0.90356 3.17567 -0.09988 -0.44434 0.20488  52  LEU D CG  
1858 C CD1 . LEU B 46  ? 1.65469 0.90126 3.23581 -0.08782 -0.43421 0.16174  52  LEU D CD1 
1859 C CD2 . LEU B 46  ? 1.63905 0.90137 3.12211 -0.10993 -0.40737 0.23141  52  LEU D CD2 
1860 N N   . LEU B 47  ? 1.72766 0.96383 3.34873 -0.01949 -0.53702 0.12591  53  LEU D N   
1861 C CA  . LEU B 47  ? 1.72768 0.98076 3.44542 -0.01569 -0.54906 0.07327  53  LEU D CA  
1862 C C   . LEU B 47  ? 1.76013 0.96263 3.44623 -0.00512 -0.51252 0.05805  53  LEU D C   
1863 O O   . LEU B 47  ? 1.72821 0.96828 3.50858 -0.02869 -0.50106 0.01872  53  LEU D O   
1864 C CB  . LEU B 47  ? 1.78436 1.02127 3.51617 0.02891  -0.59403 0.04269  53  LEU D CB  
1865 C CG  . LEU B 47  ? 1.78492 1.04496 3.51308 0.03042  -0.62757 0.05942  53  LEU D CG  
1866 C CD1 . LEU B 47  ? 1.86369 1.10516 3.59864 0.08053  -0.67071 0.02289  53  LEU D CD1 
1867 C CD2 . LEU B 47  ? 1.70416 1.04776 3.54192 -0.02655 -0.63518 0.05560  53  LEU D CD2 
1868 N N   . ILE B 48  ? 1.75530 0.87402 3.30977 0.02320  -0.48870 0.08438  54  ILE D N   
1869 C CA  . ILE B 48  ? 1.81486 0.86738 3.32512 0.03498  -0.45091 0.07069  54  ILE D CA  
1870 C C   . ILE B 48  ? 1.83687 0.84558 3.24393 0.02050  -0.40640 0.10734  54  ILE D C   
1871 O O   . ILE B 48  ? 1.86565 0.83648 3.16977 0.03590  -0.40653 0.14013  54  ILE D O   
1872 C CB  . ILE B 48  ? 1.91482 0.88518 3.35456 0.09109  -0.46454 0.05801  54  ILE D CB  
1873 C CG1 . ILE B 48  ? 1.89940 0.91473 3.45541 0.10826  -0.50492 0.00801  54  ILE D CG1 
1874 C CG2 . ILE B 48  ? 2.00690 0.88294 3.35953 0.10317  -0.41695 0.05971  54  ILE D CG2 
1875 C CD1 . ILE B 48  ? 1.84664 0.92317 3.53657 0.07345  -0.48997 -0.03696 54  ILE D CD1 
1876 N N   . TYR B 49  ? 1.82732 0.84313 3.26564 -0.00986 -0.36695 0.09536  55  TYR D N   
1877 C CA  . TYR B 49  ? 1.85806 0.82695 3.20397 -0.02213 -0.32293 0.11997  55  TYR D CA  
1878 C C   . TYR B 49  ? 1.94370 0.83154 3.24835 -0.01435 -0.28160 0.09748  55  TYR D C   
1879 O O   . TYR B 49  ? 1.95503 0.84890 3.33310 -0.01185 -0.28142 0.05956  55  TYR D O   
1880 C CB  . TYR B 49  ? 1.77105 0.82481 3.18548 -0.07130 -0.30878 0.12915  55  TYR D CB  
1881 C CG  . TYR B 49  ? 1.71176 0.84700 3.26683 -0.10929 -0.30371 0.09062  55  TYR D CG  
1882 C CD1 . TYR B 49  ? 1.64976 0.86429 3.31131 -0.12213 -0.34094 0.07325  55  TYR D CD1 
1883 C CD2 . TYR B 49  ? 1.72152 0.85832 3.30273 -0.13764 -0.25781 0.06453  55  TYR D CD2 
1884 C CE1 . TYR B 49  ? 1.59740 0.89876 3.38118 -0.16599 -0.33134 0.02981  55  TYR D CE1 
1885 C CE2 . TYR B 49  ? 1.66714 0.89243 3.37445 -0.17900 -0.24766 0.02051  55  TYR D CE2 
1886 C CZ  . TYR B 49  ? 1.60485 0.91646 3.40950 -0.19434 -0.28420 0.00256  55  TYR D CZ  
1887 O OH  . TYR B 49  ? 1.55045 0.97335 3.46933 -0.24358 -0.27010 -0.04868 55  TYR D OH  
1888 N N   . LYS B 50  ? 2.00903 0.81815 3.19492 -0.01211 -0.24436 0.11835  56  LYS D N   
1889 C CA  . LYS B 50  ? 2.11442 0.82200 3.23042 -0.00359 -0.20169 0.10372  56  LYS D CA  
1890 C C   . LYS B 50  ? 2.20575 0.83714 3.28070 0.04442  -0.21821 0.09345  56  LYS D C   
1891 O O   . LYS B 50  ? 2.28447 0.84936 3.34532 0.05173  -0.19096 0.07133  56  LYS D O   
1892 C CB  . LYS B 50  ? 2.07792 0.83321 3.29499 -0.04709 -0.16618 0.06813  56  LYS D CB  
1893 C CG  . LYS B 50  ? 2.03791 0.82475 3.24794 -0.08762 -0.13382 0.07948  56  LYS D CG  
1894 C CD  . LYS B 50  ? 1.94611 0.84575 3.30222 -0.13752 -0.11747 0.04605  56  LYS D CD  
1895 C CE  . LYS B 50  ? 1.95342 0.87136 3.40280 -0.14267 -0.10891 -0.00390 56  LYS D CE  
1896 N NZ  . LYS B 50  ? 1.87319 0.90472 3.45247 -0.19825 -0.08254 -0.04497 56  LYS D NZ  
1897 N N   . ALA B 51  ? 2.19574 0.84139 3.25818 0.07681  -0.26358 0.10759  57  ALA D N   
1898 C CA  . ALA B 51  ? 2.28327 0.86229 3.29682 0.12982  -0.28689 0.10393  57  ALA D CA  
1899 C C   . ALA B 51  ? 2.27917 0.88819 3.40418 0.14123  -0.30642 0.06104  57  ALA D C   
1900 O O   . ALA B 51  ? 2.34074 0.91300 3.44637 0.18783  -0.33484 0.05395  57  ALA D O   
1901 C CB  . ALA B 51  ? 2.42894 0.86231 3.28230 0.15726  -0.24637 0.12335  57  ALA D CB  
1902 N N   . SER B 52  ? 2.20960 0.88868 3.45565 0.10062  -0.29088 0.02835  65  SER D N   
1903 C CA  . SER B 52  ? 2.18740 0.91613 3.56091 0.10686  -0.31116 -0.02113 65  SER D CA  
1904 C C   . SER B 52  ? 2.05285 0.91758 3.59046 0.05784  -0.32173 -0.05279 65  SER D C   
1905 O O   . SER B 52  ? 2.01406 0.94107 3.66442 0.06387  -0.35351 -0.09427 65  SER D O   
1906 C CB  . SER B 52  ? 2.28354 0.93274 3.63838 0.11467  -0.26857 -0.04752 65  SER D CB  
1907 O OG  . SER B 52  ? 2.27354 0.91865 3.62407 0.06842  -0.21456 -0.04920 65  SER D OG  
1908 N N   . GLU B 53  ? 1.98685 0.89964 3.54148 0.00962  -0.29516 -0.03838 66  GLU D N   
1909 C CA  . GLU B 53  ? 1.86969 0.90930 3.56772 -0.04130 -0.30085 -0.06505 66  GLU D CA  
1910 C C   . GLU B 53  ? 1.80000 0.90592 3.53975 -0.03894 -0.35520 -0.04976 66  GLU D C   
1911 O O   . GLU B 53  ? 1.83551 0.90032 3.48392 -0.00869 -0.37950 -0.00832 66  GLU D O   
1912 C CB  . GLU B 53  ? 1.83078 0.90023 3.51931 -0.08937 -0.25917 -0.04833 66  GLU D CB  
1913 C CG  . GLU B 53  ? 1.90542 0.90410 3.54459 -0.09521 -0.20189 -0.06375 66  GLU D CG  
1914 C CD  . GLU B 53  ? 1.85056 0.93868 3.60963 -0.15003 -0.16436 -0.11666 66  GLU D CD  
1915 O OE1 . GLU B 53  ? 1.75836 0.96717 3.63373 -0.18420 -0.18439 -0.14342 66  GLU D OE1 
1916 O OE2 . GLU B 53  ? 1.90362 0.94755 3.63487 -0.16340 -0.11262 -0.13461 66  GLU D OE2 
1917 N N   . LEU B 54  ? 1.71506 0.92961 3.59085 -0.07873 -0.36965 -0.08741 67  LEU D N   
1918 C CA  . LEU B 54  ? 1.67708 0.95797 3.60869 -0.08457 -0.41883 -0.08522 67  LEU D CA  
1919 C C   . LEU B 54  ? 1.61893 1.02017 3.58336 -0.14779 -0.40864 -0.06629 67  LEU D C   
1920 O O   . LEU B 54  ? 1.58447 1.08379 3.59461 -0.19448 -0.37368 -0.09328 67  LEU D O   
1921 C CB  . LEU B 54  ? 1.66761 1.01156 3.69411 -0.07552 -0.44166 -0.15128 67  LEU D CB  
1922 C CG  . LEU B 54  ? 1.63805 1.11668 3.71373 -0.09349 -0.47569 -0.16636 67  LEU D CG  
1923 C CD1 . LEU B 54  ? 1.68365 1.13775 3.78788 -0.04006 -0.51692 -0.20580 67  LEU D CD1 
1924 C CD2 . LEU B 54  ? 1.57994 1.23215 3.73462 -0.15881 -0.44888 -0.20778 67  LEU D CD2 
1925 N N   . TYR B 55  ? 1.61473 1.02052 3.54305 -0.14600 -0.43666 -0.01950 68  TYR D N   
1926 C CA  . TYR B 55  ? 1.57130 1.08815 3.50680 -0.19668 -0.42774 0.00919  68  TYR D CA  
1927 C C   . TYR B 55  ? 1.52649 1.21304 3.54054 -0.23958 -0.42750 -0.03391 68  TYR D C   
1928 O O   . TYR B 55  ? 1.52677 1.24823 3.58856 -0.22689 -0.44627 -0.08016 68  TYR D O   
1929 C CB  . TYR B 55  ? 1.57811 1.05176 3.46101 -0.18204 -0.45769 0.06576  68  TYR D CB  
1930 C CG  . TYR B 55  ? 1.55908 1.08106 3.41987 -0.21977 -0.44150 0.11330  68  TYR D CG  
1931 C CD1 . TYR B 55  ? 1.57963 1.07423 3.40496 -0.22794 -0.40600 0.12882  68  TYR D CD1 
1932 C CD2 . TYR B 55  ? 1.53147 1.13458 3.39977 -0.24400 -0.45827 0.13954  68  TYR D CD2 
1933 C CE1 . TYR B 55  ? 1.57591 1.12065 3.38322 -0.25624 -0.39404 0.16875  68  TYR D CE1 
1934 C CE2 . TYR B 55  ? 1.52659 1.16952 3.37370 -0.27301 -0.44535 0.18533  68  TYR D CE2 
1935 C CZ  . TYR B 55  ? 1.54978 1.16419 3.37172 -0.27810 -0.41620 0.19949  68  TYR D CZ  
1936 O OH  . TYR B 55  ? 1.55782 1.21896 3.35904 -0.30053 -0.40627 0.24225  68  TYR D OH  
1937 N N   . ALA B 56  ? 1.48524 1.28118 3.51089 -0.29054 -0.40636 -0.01884 69  ALA D N   
1938 C CA  . ALA B 56  ? 1.44942 1.41108 3.53823 -0.33742 -0.40279 -0.05327 69  ALA D CA  
1939 C C   . ALA B 56  ? 1.44159 1.43724 3.53886 -0.33468 -0.43757 -0.04801 69  ALA D C   
1940 O O   . ALA B 56  ? 1.45348 1.38758 3.50158 -0.31856 -0.45821 0.00323  69  ALA D O   
1941 C CB  . ALA B 56  ? 1.43947 1.50184 3.52226 -0.38641 -0.37839 -0.02619 69  ALA D CB  
1942 N N   . GLY B 57  ? 1.48000 1.57623 3.64419 -0.35244 -0.44152 -0.10671 70  GLY D N   
1943 C CA  . GLY B 57  ? 1.47478 1.61295 3.65177 -0.35174 -0.46835 -0.11685 70  GLY D CA  
1944 C C   . GLY B 57  ? 1.50873 1.55598 3.69920 -0.29593 -0.50272 -0.14460 70  GLY D C   
1945 O O   . GLY B 57  ? 1.50057 1.61180 3.73861 -0.29806 -0.52216 -0.18720 70  GLY D O   
1946 N N   . VAL B 58  ? 1.54174 1.44352 3.68376 -0.24429 -0.50910 -0.12246 71  VAL D N   
1947 C CA  . VAL B 58  ? 1.59728 1.40163 3.73063 -0.18166 -0.54491 -0.13944 71  VAL D CA  
1948 C C   . VAL B 58  ? 1.61152 1.47427 3.82392 -0.17027 -0.55090 -0.21902 71  VAL D C   
1949 O O   . VAL B 58  ? 1.59247 1.48944 3.84287 -0.18751 -0.52131 -0.25364 71  VAL D O   
1950 C CB  . VAL B 58  ? 1.63835 1.27428 3.69792 -0.13209 -0.54405 -0.10044 71  VAL D CB  
1951 C CG1 . VAL B 58  ? 1.70652 1.24270 3.74794 -0.06352 -0.58433 -0.11414 71  VAL D CG1 
1952 C CG2 . VAL B 58  ? 1.62264 1.21126 3.61258 -0.14569 -0.53711 -0.02797 71  VAL D CG2 
1953 N N   . PRO B 59  ? 1.54647 1.42803 3.79097 -0.14239 -0.58730 -0.25468 72  PRO D N   
1954 C CA  . PRO B 59  ? 1.55316 1.50944 3.88416 -0.13412 -0.59462 -0.33664 72  PRO D CA  
1955 C C   . PRO B 59  ? 1.60790 1.46709 3.94334 -0.08432 -0.59016 -0.36243 72  PRO D C   
1956 O O   . PRO B 59  ? 1.65367 1.36279 3.91783 -0.03590 -0.59670 -0.32067 72  PRO D O   
1957 C CB  . PRO B 59  ? 1.59082 1.56090 3.93921 -0.10283 -0.63971 -0.35999 72  PRO D CB  
1958 C CG  . PRO B 59  ? 1.56033 1.53759 3.85816 -0.13385 -0.64097 -0.30109 72  PRO D CG  
1959 C CD  . PRO B 59  ? 1.56027 1.43615 3.77773 -0.13481 -0.61802 -0.22795 72  PRO D CD  
1960 N N   . SER B 60  ? 1.47294 1.41952 3.89343 -0.09920 -0.57605 -0.43359 74  SER D N   
1961 C CA  . SER B 60  ? 1.52529 1.38730 3.96455 -0.05287 -0.56980 -0.46852 74  SER D CA  
1962 C C   . SER B 60  ? 1.61197 1.35076 4.02203 0.03373  -0.61722 -0.46876 74  SER D C   
1963 O O   . SER B 60  ? 1.68990 1.29662 4.06929 0.08530  -0.61463 -0.46381 74  SER D O   
1964 C CB  . SER B 60  ? 1.49195 1.48723 4.04116 -0.08390 -0.55159 -0.55444 74  SER D CB  
1965 O OG  . SER B 60  ? 1.42220 1.53707 3.99558 -0.16290 -0.50795 -0.55697 74  SER D OG  
1966 N N   . ARG B 61  ? 1.63829 1.41820 4.05521 0.05049  -0.65970 -0.47519 75  ARG D N   
1967 C CA  . ARG B 61  ? 1.72114 1.40210 4.10995 0.13371  -0.71042 -0.47756 75  ARG D CA  
1968 C C   . ARG B 61  ? 1.74003 1.24513 4.01084 0.17689  -0.71664 -0.39893 75  ARG D C   
1969 O O   . ARG B 61  ? 1.82752 1.22068 4.05986 0.25328  -0.75220 -0.39555 75  ARG D O   
1970 C CB  . ARG B 61  ? 1.71673 1.50321 4.14387 0.12799  -0.74794 -0.50566 75  ARG D CB  
1971 C CG  . ARG B 61  ? 1.72024 1.48584 4.07566 0.10721  -0.75449 -0.43978 75  ARG D CG  
1972 C CD  . ARG B 61  ? 1.69465 1.56798 4.09816 0.09819  -0.78622 -0.47870 75  ARG D CD  
1973 N NE  . ARG B 61  ? 1.64062 1.57112 4.01998 0.03263  -0.76698 -0.43645 75  ARG D NE  
1974 C CZ  . ARG B 61  ? 1.52467 1.59543 3.95974 -0.04161 -0.73971 -0.46065 75  ARG D CZ  
1975 N NH1 . ARG B 61  ? 1.46566 1.64378 3.98661 -0.06563 -0.72615 -0.52945 75  ARG D NH1 
1976 N NH2 . ARG B 61  ? 1.46049 1.56221 3.86225 -0.09324 -0.72431 -0.41422 75  ARG D NH2 
1977 N N   . PHE B 62  ? 1.83367 1.41234 4.15873 0.02594  -0.53465 0.07130  76  PHE D N   
1978 C CA  . PHE B 62  ? 1.86347 1.38529 4.07602 0.02148  -0.56528 0.12546  76  PHE D CA  
1979 C C   . PHE B 62  ? 1.89432 1.36322 4.15049 0.02689  -0.53392 0.11856  76  PHE D C   
1980 O O   . PHE B 62  ? 1.87737 1.35917 4.19273 0.02339  -0.48077 0.05458  76  PHE D O   
1981 C CB  . PHE B 62  ? 1.83278 1.36495 3.87538 -0.00363 -0.56783 0.11106  76  PHE D CB  
1982 C CG  . PHE B 62  ? 1.81547 1.38269 3.79261 -0.01050 -0.60681 0.13490  76  PHE D CG  
1983 C CD1 . PHE B 62  ? 1.84701 1.38952 3.77282 -0.00786 -0.66279 0.20657  76  PHE D CD1 
1984 C CD2 . PHE B 62  ? 1.77297 1.39627 3.73652 -0.02179 -0.58609 0.08479  76  PHE D CD2 
1985 C CE1 . PHE B 62  ? 1.84765 1.42370 3.71516 -0.01642 -0.69692 0.22508  76  PHE D CE1 
1986 C CE2 . PHE B 62  ? 1.79604 1.44909 3.70107 -0.02970 -0.61834 0.10488  76  PHE D CE2 
1987 C CZ  . PHE B 62  ? 1.84183 1.47267 3.70146 -0.02704 -0.67356 0.17374  76  PHE D CZ  
1988 N N   . SER B 63  ? 1.94529 1.35329 4.17292 0.03394  -0.56623 0.18473  77  SER D N   
1989 C CA  . SER B 63  ? 1.98661 1.33484 4.26015 0.03998  -0.53998 0.18922  77  SER D CA  
1990 C C   . SER B 63  ? 2.03906 1.32128 4.20920 0.03565  -0.57834 0.26137  77  SER D C   
1991 O O   . SER B 63  ? 2.05251 1.33526 4.15140 0.03426  -0.63057 0.31556  77  SER D O   
1992 C CB  . SER B 63  ? 2.01710 1.35667 4.47282 0.06700  -0.52957 0.19535  77  SER D CB  
1993 O OG  . SER B 63  ? 1.97351 1.37593 4.52969 0.06992  -0.49611 0.13131  77  SER D OG  
1994 N N   . GLY B 64  ? 2.07153 1.29702 4.23052 0.03064  -0.54976 0.25889  78  GLY D N   
1995 C CA  . GLY B 64  ? 2.13088 1.28654 4.19694 0.02423  -0.57818 0.32435  78  GLY D CA  
1996 C C   . GLY B 64  ? 2.19803 1.28445 4.35399 0.03855  -0.56166 0.35182  78  GLY D C   
1997 O O   . GLY B 64  ? 2.19098 1.28040 4.46511 0.04771  -0.51523 0.30519  78  GLY D O   
1998 N N   . SER B 65  ? 2.26908 1.28951 4.36252 0.03830  -0.59842 0.42804  79  SER D N   
1999 C CA  . SER B 65  ? 2.34578 1.28854 4.50663 0.05005  -0.58481 0.46337  79  SER D CA  
2000 C C   . SER B 65  ? 2.41374 1.28204 4.43872 0.03223  -0.60686 0.52412  79  SER D C   
2001 O O   . SER B 65  ? 2.40796 1.28579 4.30048 0.01500  -0.64246 0.54963  79  SER D O   
2002 C CB  . SER B 65  ? 2.38720 1.32877 4.68419 0.08299  -0.61451 0.50893  79  SER D CB  
2003 O OG  . SER B 65  ? 2.40703 1.36384 4.64421 0.08710  -0.68274 0.57281  79  SER D OG  
2004 N N   . ARG B 66  ? 2.48351 1.29166 4.53055 0.03441  -0.57890 0.54195  80  ARG D N   
2005 C CA  . ARG B 66  ? 2.55506 1.29562 4.47076 0.01346  -0.58008 0.58453  80  ARG D CA  
2006 C C   . ARG B 66  ? 2.65866 1.35491 4.60938 0.03016  -0.58315 0.64071  80  ARG D C   
2007 O O   . ARG B 66  ? 2.67837 1.36069 4.72903 0.04150  -0.53675 0.61353  80  ARG D O   
2008 C CB  . ARG B 66  ? 2.52617 1.24306 4.41002 -0.01075 -0.52095 0.52189  80  ARG D CB  
2009 C CG  . ARG B 66  ? 2.60561 1.24805 4.39334 -0.03077 -0.50002 0.54986  80  ARG D CG  
2010 C CD  . ARG B 66  ? 2.56416 1.20048 4.35519 -0.05173 -0.43719 0.47333  80  ARG D CD  
2011 N NE  . ARG B 66  ? 2.60116 1.18402 4.25986 -0.08278 -0.42604 0.48477  80  ARG D NE  
2012 C CZ  . ARG B 66  ? 2.69777 1.21080 4.30438 -0.09064 -0.41299 0.52799  80  ARG D CZ  
2013 N NH1 . ARG B 66  ? 2.77110 1.25613 4.44320 -0.06889 -0.41095 0.56627  80  ARG D NH1 
2014 N NH2 . ARG B 66  ? 2.72547 1.19386 4.21293 -0.12190 -0.39943 0.53090  80  ARG D NH2 
2015 N N   . SER B 67  ? 2.72923 1.40363 4.59518 0.03042  -0.63715 0.71715  83  SER D N   
2016 C CA  . SER B 67  ? 2.84316 1.46865 4.71729 0.04411  -0.64870 0.77970  83  SER D CA  
2017 C C   . SER B 67  ? 2.92837 1.47159 4.66494 0.01867  -0.63331 0.81209  83  SER D C   
2018 O O   . SER B 67  ? 3.01877 1.52605 4.66649 0.01553  -0.67274 0.88103  83  SER D O   
2019 C CB  . SER B 67  ? 2.87729 1.53465 4.75192 0.06093  -0.71937 0.84177  83  SER D CB  
2020 O OG  . SER B 67  ? 3.00146 1.60120 4.82759 0.06524  -0.74004 0.91150  83  SER D OG  
2021 N N   . GLY B 68  ? 2.90774 1.41963 4.62609 -0.00087 -0.57434 0.76164  84  GLY D N   
2022 C CA  . GLY B 68  ? 2.98556 1.42042 4.57196 -0.02839 -0.55674 0.78768  84  GLY D CA  
2023 C C   . GLY B 68  ? 2.94730 1.39061 4.39393 -0.05852 -0.57985 0.78738  84  GLY D C   
2024 O O   . GLY B 68  ? 2.87427 1.33103 4.30290 -0.07802 -0.54716 0.72818  84  GLY D O   
2025 N N   . THR B 69  ? 2.99774 1.43696 4.34597 -0.06317 -0.63695 0.85110  85  THR D N   
2026 C CA  . THR B 69  ? 2.96491 1.41752 4.18095 -0.09158 -0.66311 0.85346  85  THR D CA  
2027 C C   . THR B 69  ? 2.90537 1.43222 4.13520 -0.07975 -0.72178 0.86442  85  THR D C   
2028 O O   . THR B 69  ? 2.89010 1.42933 4.00572 -0.10228 -0.75071 0.87508  85  THR D O   
2029 C CB  . THR B 69  ? 3.07598 1.46067 4.13823 -0.11713 -0.67507 0.91110  85  THR D CB  
2030 O OG1 . THR B 69  ? 3.15229 1.54069 4.20272 -0.10065 -0.73051 0.97944  85  THR D OG1 
2031 C CG2 . THR B 69  ? 3.15013 1.45478 4.20331 -0.12758 -0.61666 0.90615  85  THR D CG2 
2032 N N   . ASP B 70  ? 2.87484 1.45106 4.24128 -0.04665 -0.73822 0.86077  86  ASP D N   
2033 C CA  . ASP B 70  ? 2.82785 1.47384 4.21654 -0.03467 -0.79396 0.87370  86  ASP D CA  
2034 C C   . ASP B 70  ? 2.71570 1.42215 4.23503 -0.01809 -0.77245 0.80708  86  ASP D C   
2035 O O   . ASP B 70  ? 2.70823 1.43415 4.37083 0.00956  -0.75691 0.79162  86  ASP D O   
2036 C CB  . ASP B 70  ? 2.90750 1.55993 4.33673 -0.01150 -0.84074 0.93649  86  ASP D CB  
2037 C CG  . ASP B 70  ? 3.00611 1.62092 4.28253 -0.03208 -0.88098 1.00228  86  ASP D CG  
2038 O OD1 . ASP B 70  ? 3.10225 1.64580 4.32451 -0.03943 -0.86140 1.03288  86  ASP D OD1 
2039 O OD2 . ASP B 70  ? 2.99219 1.64766 4.20206 -0.04211 -0.93002 1.02167  86  ASP D OD2 
2040 N N   . PHE B 71  ? 2.63388 1.36863 4.10240 -0.03583 -0.77049 0.76681  87  PHE D N   
2041 C CA  . PHE B 71  ? 2.53105 1.32143 4.10235 -0.02493 -0.74600 0.69744  87  PHE D CA  
2042 C C   . PHE B 71  ? 2.48605 1.35174 4.09926 -0.00953 -0.79072 0.70285  87  PHE D C   
2043 O O   . PHE B 71  ? 2.49505 1.37487 4.00989 -0.02193 -0.83708 0.73840  87  PHE D O   
2044 C CB  . PHE B 71  ? 2.46676 1.28163 3.93981 -0.05309 -0.70621 0.63240  87  PHE D CB  
2045 C CG  . PHE B 71  ? 2.51537 1.25810 3.91433 -0.07561 -0.67078 0.63300  87  PHE D CG  
2046 C CD1 . PHE B 71  ? 2.51093 1.23167 3.98899 -0.07257 -0.61302 0.58684  87  PHE D CD1 
2047 C CD2 . PHE B 71  ? 2.56807 1.26541 3.82011 -0.10211 -0.69239 0.67644  87  PHE D CD2 
2048 C CE1 . PHE B 71  ? 2.55676 1.21222 3.97156 -0.09486 -0.57787 0.58442  87  PHE D CE1 
2049 C CE2 . PHE B 71  ? 2.61529 1.24593 3.80224 -0.12489 -0.65585 0.67401  87  PHE D CE2 
2050 C CZ  . PHE B 71  ? 2.60902 1.21897 3.87874 -0.12095 -0.59875 0.62824  87  PHE D CZ  
2051 N N   . THR B 72  ? 2.43542 1.35233 4.19375 0.01450  -0.77227 0.66087  88  THR D N   
2052 C CA  . THR B 72  ? 2.39701 1.38472 4.21640 0.03048  -0.81028 0.66367  88  THR D CA  
2053 C C   . THR B 72  ? 2.29684 1.36356 4.16101 0.02889  -0.77108 0.57792  88  THR D C   
2054 O O   . THR B 72  ? 2.26352 1.33280 4.17288 0.02704  -0.71404 0.51673  88  THR D O   
2055 C CB  . THR B 72  ? 2.44646 1.42661 4.41419 0.06439  -0.83530 0.70571  88  THR D CB  
2056 O OG1 . THR B 72  ? 2.40952 1.40546 4.52948 0.08293  -0.78411 0.64852  88  THR D OG1 
2057 C CG2 . THR B 72  ? 2.55403 1.47629 4.46425 0.06234  -0.84547 0.76688  88  THR D CG2 
2058 N N   . LEU B 73  ? 2.25423 1.38433 4.09698 0.02695  -0.80260 0.57435  89  LEU D N   
2059 C CA  . LEU B 73  ? 2.16939 1.37673 4.05598 0.02646  -0.77442 0.50291  89  LEU D CA  
2060 C C   . LEU B 73  ? 2.16320 1.41563 4.19992 0.05306  -0.79423 0.50843  89  LEU D C   
2061 O O   . LEU B 73  ? 2.20118 1.45520 4.24805 0.06301  -0.85086 0.56836  89  LEU D O   
2062 C CB  . LEU B 73  ? 2.12659 1.37017 3.87222 0.00153  -0.78923 0.49011  89  LEU D CB  
2063 C CG  . LEU B 73  ? 2.04664 1.36642 3.80560 -0.00356 -0.76563 0.42359  89  LEU D CG  
2064 C CD1 . LEU B 73  ? 2.00704 1.34304 3.84108 -0.00025 -0.70289 0.35019  89  LEU D CD1 
2065 C CD2 . LEU B 73  ? 2.01920 1.35110 3.61977 -0.03015 -0.77373 0.41589  89  LEU D CD2 
2066 N N   . THR B 74  ? 2.11872 1.40872 4.27379 0.06344  -0.74718 0.44427  90  THR D N   
2067 C CA  . THR B 74  ? 2.11491 1.44277 4.43847 0.08972  -0.75147 0.43848  90  THR D CA  
2068 C C   . THR B 74  ? 2.04006 1.44784 4.39025 0.08207  -0.72581 0.36996  90  THR D C   
2069 O O   . THR B 74  ? 1.99542 1.41987 4.31198 0.06628  -0.67471 0.30379  90  THR D O   
2070 C CB  . THR B 74  ? 2.14212 1.43331 4.60048 0.10847  -0.70918 0.42094  90  THR D CB  
2071 O OG1 . THR B 74  ? 2.22469 1.44290 4.68955 0.12224  -0.74198 0.49677  90  THR D OG1 
2072 C CG2 . THR B 74  ? 2.11845 1.46112 4.75710 0.13057  -0.69138 0.38468  90  THR D CG2 
2073 N N   . ILE B 75  ? 2.03010 1.48737 4.43678 0.09167  -0.76120 0.38511  91  ILE D N   
2074 C CA  . ILE B 75  ? 1.96900 1.50026 4.42618 0.08646  -0.73466 0.32202  91  ILE D CA  
2075 C C   . ILE B 75  ? 1.97990 1.53894 4.63352 0.11459  -0.73501 0.31911  91  ILE D C   
2076 O O   . ILE B 75  ? 2.01468 1.57739 4.72277 0.13229  -0.78983 0.37694  91  ILE D O   
2077 C CB  . ILE B 75  ? 1.94300 1.51393 4.28704 0.06804  -0.77093 0.33415  91  ILE D CB  
2078 C CG1 . ILE B 75  ? 1.94841 1.48015 4.10425 0.04406  -0.78150 0.35453  91  ILE D CG1 
2079 C CG2 . ILE B 75  ? 1.88282 1.52206 4.25538 0.05716  -0.73397 0.26358  91  ILE D CG2 
2080 C CD1 . ILE B 75  ? 2.00188 1.49902 4.08238 0.04362  -0.84679 0.43632  91  ILE D CD1 
2081 N N   . SER B 76  ? 1.95306 1.53363 4.71540 0.11820  -0.67470 0.25084  92  SER D N   
2082 C CA  . SER B 76  ? 1.96829 1.56864 4.93065 0.14599  -0.66838 0.24517  92  SER D CA  
2083 C C   . SER B 76  ? 1.93589 1.61086 4.96271 0.14687  -0.68290 0.22682  92  SER D C   
2084 O O   . SER B 76  ? 1.96272 1.65155 5.06866 0.16725  -0.73460 0.27684  92  SER D O   
2085 C CB  . SER B 76  ? 1.95802 1.55133 5.01972 0.14766  -0.59507 0.17672  92  SER D CB  
2086 O OG  . SER B 76  ? 1.90328 1.53765 4.89950 0.12026  -0.54510 0.09948  92  SER D OG  
2087 N N   . SER B 77  ? 1.88234 1.60614 4.87426 0.12399  -0.63897 0.15606  93  SER D N   
2088 C CA  . SER B 77  ? 1.85290 1.64594 4.89588 0.12018  -0.64675 0.13419  93  SER D CA  
2089 C C   . SER B 77  ? 1.83119 1.63528 4.68990 0.09434  -0.67619 0.15071  93  SER D C   
2090 O O   . SER B 77  ? 1.79515 1.61371 4.55006 0.06855  -0.63892 0.10108  93  SER D O   
2091 C CB  . SER B 77  ? 1.81784 1.65551 4.95207 0.11075  -0.57558 0.04487  93  SER D CB  
2092 O OG  . SER B 77  ? 1.79494 1.61862 4.81679 0.08605  -0.52570 -0.00650 93  SER D OG  
2093 N N   . LEU B 78  ? 1.85815 1.65482 4.67799 0.10134  -0.74446 0.22167  94  LEU D N   
2094 C CA  . LEU B 78  ? 1.84465 1.64856 4.49621 0.07734  -0.77643 0.24302  94  LEU D CA  
2095 C C   . LEU B 78  ? 1.79839 1.66686 4.44514 0.05828  -0.75135 0.18833  94  LEU D C   
2096 O O   . LEU B 78  ? 1.79457 1.71211 4.55934 0.06743  -0.76324 0.18280  94  LEU D O   
2097 C CB  . LEU B 78  ? 1.88845 1.68041 4.52481 0.08843  -0.85442 0.32546  94  LEU D CB  
2098 C CG  . LEU B 78  ? 1.88303 1.68016 4.35139 0.06322  -0.89215 0.35288  94  LEU D CG  
2099 C CD1 . LEU B 78  ? 1.87501 1.62448 4.17607 0.04190  -0.86803 0.34456  94  LEU D CD1 
2100 C CD2 . LEU B 78  ? 1.93649 1.72083 4.40146 0.07431  -0.96944 0.43388  94  LEU D CD2 
2101 N N   . GLN B 79  ? 1.76707 1.63484 4.28190 0.03208  -0.71589 0.14771  95  GLN D N   
2102 C CA  . GLN B 79  ? 1.73087 1.65167 4.22072 0.01120  -0.69060 0.09891  95  GLN D CA  
2103 C C   . GLN B 79  ? 1.72707 1.64886 4.06391 -0.00860 -0.72996 0.13222  95  GLN D C   
2104 O O   . GLN B 79  ? 1.74502 1.62210 3.96581 -0.01218 -0.76050 0.17691  95  GLN D O   
2105 C CB  . GLN B 79  ? 1.70376 1.62676 4.15399 -0.00558 -0.62124 0.02620  95  GLN D CB  
2106 C CG  . GLN B 79  ? 1.70766 1.63261 4.30737 0.00901  -0.57383 -0.01751 95  GLN D CG  
2107 C CD  . GLN B 79  ? 1.71237 1.68097 4.49822 0.02598  -0.57487 -0.02620 95  GLN D CD  
2108 O OE1 . GLN B 79  ? 1.73939 1.69347 4.64873 0.05342  -0.59917 0.00910  95  GLN D OE1 
2109 N NE2 . GLN B 79  ? 1.68973 1.71093 4.49836 0.00970  -0.54793 -0.07301 95  GLN D NE2 
2110 N N   . PRO B 80  ? 1.77602 1.74727 4.11284 -0.02308 -0.72845 0.11070  96  PRO D N   
2111 C CA  . PRO B 80  ? 1.75639 1.73053 3.96459 -0.04131 -0.76923 0.14529  96  PRO D CA  
2112 C C   . PRO B 80  ? 1.76540 1.70101 3.78735 -0.06220 -0.75759 0.14361  96  PRO D C   
2113 O O   . PRO B 80  ? 1.78986 1.70659 3.70120 -0.07247 -0.79838 0.18747  96  PRO D O   
2114 C CB  . PRO B 80  ? 1.68709 1.72248 3.94678 -0.05467 -0.75138 0.10545  96  PRO D CB  
2115 C CG  . PRO B 80  ? 1.66941 1.72377 4.02534 -0.05235 -0.68655 0.03855  96  PRO D CG  
2116 C CD  . PRO B 80  ? 1.69092 1.71730 4.15144 -0.02482 -0.68889 0.05412  96  PRO D CD  
2117 N N   . GLU B 81  ? 1.85295 1.77774 3.83865 -0.06937 -0.70360 0.09314  97  GLU D N   
2118 C CA  . GLU B 81  ? 1.83212 1.72400 3.64941 -0.08724 -0.69292 0.08908  97  GLU D CA  
2119 C C   . GLU B 81  ? 1.93322 1.77157 3.67504 -0.08169 -0.73032 0.14427  97  GLU D C   
2120 O O   . GLU B 81  ? 1.92080 1.73510 3.52000 -0.09756 -0.74076 0.15898  97  GLU D O   
2121 C CB  . GLU B 81  ? 1.77255 1.66253 3.58008 -0.09231 -0.63327 0.02763  97  GLU D CB  
2122 C CG  . GLU B 81  ? 1.69865 1.63505 3.60762 -0.09558 -0.58772 -0.03163 97  GLU D CG  
2123 C CD  . GLU B 81  ? 1.66421 1.59474 3.58194 -0.09807 -0.53264 -0.08845 97  GLU D CD  
2124 O OE1 . GLU B 81  ? 1.71637 1.62262 3.69866 -0.08215 -0.52757 -0.08490 97  GLU D OE1 
2125 O OE2 . GLU B 81  ? 1.62409 1.57325 3.48194 -0.11708 -0.49446 -0.13650 97  GLU D OE2 
2126 N N   . ASP B 82  ? 1.82360 1.64072 3.65889 -0.06016 -0.75006 0.17615  98  ASP D N   
2127 C CA  . ASP B 82  ? 1.87409 1.63353 3.64194 -0.05606 -0.77421 0.22175  98  ASP D CA  
2128 C C   . ASP B 82  ? 1.91059 1.65553 3.61732 -0.06018 -0.83587 0.28834  98  ASP D C   
2129 O O   . ASP B 82  ? 1.90120 1.60446 3.60870 -0.05019 -0.86683 0.33817  98  ASP D O   
2130 C CB  . ASP B 82  ? 1.85578 1.59111 3.74593 -0.03227 -0.76424 0.22711  98  ASP D CB  
2131 C CG  . ASP B 82  ? 1.82576 1.58224 3.79867 -0.02880 -0.70349 0.15826  98  ASP D CG  
2132 O OD1 . ASP B 82  ? 1.77699 1.54530 3.66879 -0.04653 -0.66707 0.11071  98  ASP D OD1 
2133 O OD2 . ASP B 82  ? 1.81774 1.57832 3.93651 -0.00875 -0.69232 0.15172  98  ASP D OD2 
2134 N N   . PHE B 83  ? 2.07661 1.85315 3.72483 -0.07699 -0.85266 0.28923  99  PHE D N   
2135 C CA  . PHE B 83  ? 2.07855 1.84342 3.65009 -0.08693 -0.90839 0.34625  99  PHE D CA  
2136 C C   . PHE B 83  ? 2.10846 1.82991 3.51177 -0.10742 -0.90323 0.35337  99  PHE D C   
2137 O O   . PHE B 83  ? 2.05407 1.78498 3.38078 -0.12284 -0.87025 0.31345  99  PHE D O   
2138 C CB  . PHE B 83  ? 2.01152 1.83010 3.59741 -0.09825 -0.92711 0.34144  99  PHE D CB  
2139 C CG  . PHE B 83  ? 2.00891 1.81497 3.45481 -0.12219 -0.96008 0.37304  99  PHE D CG  
2140 C CD1 . PHE B 83  ? 2.04545 1.83052 3.46491 -0.12249 -1.01691 0.43482  99  PHE D CD1 
2141 C CD2 . PHE B 83  ? 1.95523 1.76620 3.29102 -0.14528 -0.93302 0.34142  99  PHE D CD2 
2142 C CE1 . PHE B 83  ? 2.05128 1.82362 3.33924 -0.14763 -1.04425 0.46064  99  PHE D CE1 
2143 C CE2 . PHE B 83  ? 1.95548 1.75192 3.16581 -0.16799 -0.95967 0.36828  99  PHE D CE2 
2144 C CZ  . PHE B 83  ? 2.01167 1.78987 3.19833 -0.17033 -1.01413 0.42596  99  PHE D CZ  
2145 N N   . ALA B 84  ? 2.06024 1.73268 3.40861 -0.10748 -0.93420 0.40356  100 ALA D N   
2146 C CA  . ALA B 84  ? 2.05752 1.68376 3.25868 -0.12574 -0.92638 0.41008  100 ALA D CA  
2147 C C   . ALA B 84  ? 2.07945 1.65634 3.23952 -0.12677 -0.96911 0.47402  100 ALA D C   
2148 O O   . ALA B 84  ? 2.09013 1.67257 3.32247 -0.11485 -1.01044 0.51590  100 ALA D O   
2149 C CB  . ALA B 84  ? 1.99601 1.60444 3.19062 -0.12161 -0.87319 0.36345  100 ALA D CB  
2150 N N   . THR B 85  ? 2.16190 1.69085 3.20195 -0.14242 -0.96029 0.48208  101 THR D N   
2151 C CA  . THR B 85  ? 2.17473 1.64550 3.17033 -0.14501 -0.98621 0.53460  101 THR D CA  
2152 C C   . THR B 85  ? 2.12592 1.55709 3.13321 -0.13669 -0.94400 0.51184  101 THR D C   
2153 O O   . THR B 85  ? 2.08951 1.52148 3.04409 -0.14513 -0.90404 0.46650  101 THR D O   
2154 C CB  . THR B 85  ? 2.22092 1.66655 3.06580 -0.17451 -1.00814 0.56114  101 THR D CB  
2155 O OG1 . THR B 85  ? 2.25435 1.74774 3.08171 -0.18613 -1.02854 0.55662  101 THR D OG1 
2156 C CG2 . THR B 85  ? 2.26370 1.66049 3.07314 -0.17944 -1.05044 0.62666  101 THR D CG2 
2157 N N   . TYR B 86  ? 2.10885 1.50559 3.18644 -0.12024 -0.95275 0.54253  102 TYR D N   
2158 C CA  . TYR B 86  ? 2.06583 1.42974 3.17740 -0.11108 -0.90926 0.51592  102 TYR D CA  
2159 C C   . TYR B 86  ? 2.09833 1.39158 3.11649 -0.12501 -0.91516 0.55409  102 TYR D C   
2160 O O   . TYR B 86  ? 2.15358 1.41463 3.14922 -0.12757 -0.95759 0.61505  102 TYR D O   
2161 C CB  . TYR B 86  ? 2.04286 1.41586 3.31473 -0.08208 -0.90251 0.51345  102 TYR D CB  
2162 C CG  . TYR B 86  ? 2.01395 1.45207 3.38573 -0.07015 -0.87604 0.45756  102 TYR D CG  
2163 C CD1 . TYR B 86  ? 2.02795 1.51607 3.35520 -0.08278 -0.87656 0.43055  102 TYR D CD1 
2164 C CD2 . TYR B 86  ? 1.98173 1.42796 3.49097 -0.04826 -0.84686 0.43031  102 TYR D CD2 
2165 C CE1 . TYR B 86  ? 2.01630 1.55976 3.42919 -0.07479 -0.84911 0.37935  102 TYR D CE1 
2166 C CE2 . TYR B 86  ? 1.96788 1.47154 3.56535 -0.04067 -0.81886 0.37670  102 TYR D CE2 
2167 C CZ  . TYR B 86  ? 1.98806 1.53978 3.53433 -0.05454 -0.82010 0.35185  102 TYR D CZ  
2168 O OH  . TYR B 86  ? 1.98534 1.59099 3.61279 -0.05000 -0.78946 0.29830  102 TYR D OH  
2169 N N   . TYR B 87  ? 2.19598 1.46575 3.16136 -0.13473 -0.87251 0.51748  103 TYR D N   
2170 C CA  . TYR B 87  ? 2.22425 1.42857 3.09452 -0.15220 -0.86926 0.54380  103 TYR D CA  
2171 C C   . TYR B 87  ? 2.19167 1.36171 3.11940 -0.14254 -0.82693 0.51992  103 TYR D C   
2172 O O   . TYR B 87  ? 2.13794 1.34087 3.14325 -0.12960 -0.79083 0.46596  103 TYR D O   
2173 C CB  . TYR B 87  ? 2.22691 1.43177 2.96373 -0.17848 -0.85771 0.52210  103 TYR D CB  
2174 C CG  . TYR B 87  ? 2.27254 1.49900 2.93251 -0.19440 -0.89676 0.54819  103 TYR D CG  
2175 C CD1 . TYR B 87  ? 2.25935 1.54797 2.96162 -0.18694 -0.90748 0.52892  103 TYR D CD1 
2176 C CD2 . TYR B 87  ? 2.33736 1.52154 2.88096 -0.21969 -0.91927 0.58853  103 TYR D CD2 
2177 C CE1 . TYR B 87  ? 2.30695 1.61549 2.94151 -0.20337 -0.94045 0.54954  103 TYR D CE1 
2178 C CE2 . TYR B 87  ? 2.38562 1.59007 2.85901 -0.23682 -0.95261 0.60853  103 TYR D CE2 
2179 C CZ  . TYR B 87  ? 2.36866 1.63564 2.88934 -0.22824 -0.96343 0.58893  103 TYR D CZ  
2180 O OH  . TYR B 87  ? 2.42251 1.70925 2.87498 -0.24723 -0.99466 0.60673  103 TYR D OH  
2181 N N   . CYS B 88  ? 2.19068 1.29329 3.07794 -0.15108 -0.82988 0.55913  104 CYS D N   
2182 C CA  . CYS B 88  ? 2.20407 1.26640 3.13482 -0.14650 -0.78748 0.53804  104 CYS D CA  
2183 C C   . CYS B 88  ? 2.21972 1.24119 3.03180 -0.17355 -0.76436 0.52793  104 CYS D C   
2184 O O   . CYS B 88  ? 2.26668 1.25525 2.97215 -0.19455 -0.78950 0.56904  104 CYS D O   
2185 C CB  . CYS B 88  ? 2.27888 1.28791 3.27966 -0.13214 -0.80259 0.59124  104 CYS D CB  
2186 S SG  . CYS B 88  ? 2.35637 1.34528 3.32708 -0.13129 -0.87512 0.68083  104 CYS D SG  
2187 N N   . GLN B 89  ? 2.19769 1.22132 3.03205 -0.17410 -0.71592 0.47216  105 GLN D N   
2188 C CA  . GLN B 89  ? 2.21256 1.20723 2.95102 -0.19797 -0.68878 0.45094  105 GLN D CA  
2189 C C   . GLN B 89  ? 2.24851 1.17692 3.01580 -0.20053 -0.66281 0.46377  105 GLN D C   
2190 O O   . GLN B 89  ? 2.22990 1.16379 3.09452 -0.18626 -0.62929 0.42756  105 GLN D O   
2191 C CB  . GLN B 89  ? 2.14952 1.19807 2.89038 -0.19755 -0.65514 0.37712  105 GLN D CB  
2192 C CG  . GLN B 89  ? 2.16233 1.19451 2.79927 -0.22135 -0.63489 0.35412  105 GLN D CG  
2193 C CD  . GLN B 89  ? 2.13304 1.16919 2.81140 -0.22058 -0.58670 0.29430  105 GLN D CD  
2194 O OE1 . GLN B 89  ? 2.12248 1.14810 2.89420 -0.20834 -0.56526 0.28189  105 GLN D OE1 
2195 N NE2 . GLN B 89  ? 2.12116 1.17466 2.73480 -0.23341 -0.56971 0.25526  105 GLN D NE2 
2196 N N   . GLN B 90  ? 2.38379 1.24792 3.06370 -0.22087 -0.67683 0.51487  106 GLN D N   
2197 C CA  . GLN B 90  ? 2.42953 1.22002 3.12055 -0.22755 -0.65260 0.53477  106 GLN D CA  
2198 C C   . GLN B 90  ? 2.41587 1.19878 3.09085 -0.24224 -0.59872 0.47523  106 GLN D C   
2199 O O   . GLN B 90  ? 2.43342 1.16962 3.15218 -0.24358 -0.56530 0.46969  106 GLN D O   
2200 C CB  . GLN B 90  ? 2.53152 1.25463 3.12091 -0.24864 -0.68393 0.60772  106 GLN D CB  
2201 N N   . ARG B 91  ? 2.30988 1.13751 2.92562 -0.25309 -0.59041 0.43133  107 ARG D N   
2202 C CA  . ARG B 91  ? 2.27870 1.11173 2.88291 -0.26524 -0.54412 0.37037  107 ARG D CA  
2203 C C   . ARG B 91  ? 2.35772 1.11429 2.89465 -0.29260 -0.52170 0.39020  107 ARG D C   
2204 O O   . ARG B 91  ? 2.43530 1.13825 2.90012 -0.30761 -0.54614 0.45148  107 ARG D O   
2205 C CB  . ARG B 91  ? 2.23357 1.09891 2.95946 -0.24528 -0.50981 0.31525  107 ARG D CB  
2206 N N   . GLY B 92  ? 2.34197 1.09467 2.90094 -0.30092 -0.47464 0.33661  108 GLY D N   
2207 C CA  . GLY B 92  ? 2.41509 1.10385 2.91264 -0.32991 -0.44386 0.33938  108 GLY D CA  
2208 C C   . GLY B 92  ? 2.38829 1.11545 2.85313 -0.34249 -0.41646 0.27518  108 GLY D C   
2209 O O   . GLY B 92  ? 2.35872 1.13087 2.77045 -0.34275 -0.43750 0.26487  108 GLY D O   
2210 N N   . TRP B 93  ? 2.35056 1.05993 2.85122 -0.35265 -0.36926 0.23146  109 TRP D N   
2211 C CA  . TRP B 93  ? 2.32428 1.06918 2.80483 -0.36427 -0.34189 0.16834  109 TRP D CA  
2212 C C   . TRP B 93  ? 2.36174 1.09209 2.72467 -0.38744 -0.35489 0.18703  109 TRP D C   
2213 O O   . TRP B 93  ? 2.31881 1.10387 2.65429 -0.38368 -0.36481 0.15586  109 TRP D O   
2214 C CB  . TRP B 93  ? 2.35668 1.06653 2.88420 -0.37843 -0.28937 0.13129  109 TRP D CB  
2215 C CG  . TRP B 93  ? 2.31880 1.07828 2.86719 -0.38328 -0.25906 0.05490  109 TRP D CG  
2216 C CD1 . TRP B 93  ? 2.34561 1.07597 2.87402 -0.40907 -0.21939 0.02469  109 TRP D CD1 
2217 C CD2 . TRP B 93  ? 2.23656 1.08428 2.83145 -0.36227 -0.26645 -0.00162 109 TRP D CD2 
2218 N NE1 . TRP B 93  ? 2.27766 1.07595 2.84329 -0.40358 -0.20435 -0.04712 109 TRP D NE1 
2219 C CE2 . TRP B 93  ? 2.21453 1.08421 2.81684 -0.37498 -0.23403 -0.06268 109 TRP D CE2 
2220 C CE3 . TRP B 93  ? 2.17738 1.08698 2.80729 -0.33509 -0.29678 -0.00677 109 TRP D CE3 
2221 C CZ2 . TRP B 93  ? 2.14284 1.09368 2.78316 -0.36004 -0.23539 -0.12479 109 TRP D CZ2 
2222 C CZ3 . TRP B 93  ? 2.11368 1.09990 2.77450 -0.32268 -0.29443 -0.06888 109 TRP D CZ3 
2223 C CH2 . TRP B 93  ? 2.09891 1.10523 2.76315 -0.33439 -0.26618 -0.12544 109 TRP D CH2 
2224 N N   . TYR B 94  ? 2.46018 1.11438 2.75067 -0.41235 -0.35473 0.23915  114 TYR D N   
2225 C CA  . TYR B 94  ? 2.51105 1.14190 2.68688 -0.44025 -0.36052 0.25604  114 TYR D CA  
2226 C C   . TYR B 94  ? 2.55915 1.15792 2.66132 -0.44570 -0.40600 0.33095  114 TYR D C   
2227 O O   . TYR B 94  ? 2.62832 1.19023 2.62653 -0.47459 -0.41048 0.35674  114 TYR D O   
2228 C CB  . TYR B 94  ? 2.58365 1.15198 2.72952 -0.47282 -0.31217 0.24160  114 TYR D CB  
2229 C CG  . TYR B 94  ? 2.53793 1.15136 2.72938 -0.47357 -0.27353 0.16197  114 TYR D CG  
2230 C CD1 . TYR B 94  ? 2.44537 1.14443 2.69937 -0.44506 -0.28501 0.11377  114 TYR D CD1 
2231 C CD2 . TYR B 94  ? 2.58661 1.15714 2.76945 -0.50157 -0.22474 0.13413  114 TYR D CD2 
2232 C CE1 . TYR B 94  ? 2.40420 1.14773 2.70236 -0.44399 -0.25515 0.04303  114 TYR D CE1 
2233 C CE2 . TYR B 94  ? 2.53925 1.15607 2.77375 -0.50092 -0.19215 0.06000  114 TYR D CE2 
2234 C CZ  . TYR B 94  ? 2.44523 1.14994 2.73784 -0.47104 -0.20982 0.01547  114 TYR D CZ  
2235 O OH  . TYR B 94  ? 2.38925 1.14354 2.73405 -0.46914 -0.18242 -0.05705 114 TYR D OH  
2236 N N   . LEU B 95  ? 2.58772 1.20015 2.74499 -0.41980 -0.43877 0.36452  115 LEU D N   
2237 C CA  . LEU B 95  ? 2.63524 1.22095 2.73870 -0.42181 -0.48606 0.43707  115 LEU D CA  
2238 C C   . LEU B 95  ? 2.55795 1.20653 2.73049 -0.38726 -0.52573 0.44465  115 LEU D C   
2239 O O   . LEU B 95  ? 2.57173 1.20237 2.78190 -0.37294 -0.55346 0.49263  115 LEU D O   
2240 C CB  . LEU B 95  ? 2.72291 1.22255 2.81531 -0.43424 -0.48102 0.49149  115 LEU D CB  
2241 C CG  . LEU B 95  ? 2.83749 1.26595 2.80152 -0.47676 -0.47206 0.52354  115 LEU D CG  
2242 C CD1 . LEU B 95  ? 2.92759 1.26535 2.88036 -0.49014 -0.46018 0.57347  115 LEU D CD1 
2243 C CD2 . LEU B 95  ? 2.87708 1.31629 2.74278 -0.48904 -0.51916 0.56416  115 LEU D CD2 
2244 N N   . PHE B 96  ? 2.43439 1.15716 2.62928 -0.37291 -0.52770 0.39646  116 PHE D N   
2245 C CA  . PHE B 96  ? 2.36817 1.15036 2.61629 -0.34493 -0.56329 0.40227  116 PHE D CA  
2246 C C   . PHE B 96  ? 2.42006 1.18873 2.60084 -0.35244 -0.61258 0.46633  116 PHE D C   
2247 O O   . PHE B 96  ? 2.46877 1.22228 2.54599 -0.37761 -0.62137 0.47986  116 PHE D O   
2248 C CB  . PHE B 96  ? 2.28504 1.14128 2.54376 -0.33418 -0.55618 0.34290  116 PHE D CB  
2249 C CG  . PHE B 96  ? 2.22594 1.11709 2.57541 -0.31788 -0.51978 0.27932  116 PHE D CG  
2250 C CD1 . PHE B 96  ? 2.17921 1.09971 2.63330 -0.29184 -0.52112 0.26900  116 PHE D CD1 
2251 C CD2 . PHE B 96  ? 2.22033 1.12051 2.55292 -0.32884 -0.48555 0.22700  116 PHE D CD2 
2252 C CE1 . PHE B 96  ? 2.13462 1.08929 2.66839 -0.27972 -0.48797 0.20847  116 PHE D CE1 
2253 C CE2 . PHE B 96  ? 2.17593 1.11369 2.59104 -0.31483 -0.45599 0.16740  116 PHE D CE2 
2254 C CZ  . PHE B 96  ? 2.13508 1.09970 2.64719 -0.29140 -0.45708 0.15803  116 PHE D CZ  
2255 N N   . THR B 97  ? 2.45255 1.22953 2.69706 -0.33089 -0.64453 0.50318  117 THR D N   
2256 C CA  . THR B 97  ? 2.50225 1.27359 2.70009 -0.33464 -0.69645 0.56437  117 THR D CA  
2257 C C   . THR B 97  ? 2.44160 1.26926 2.73642 -0.30252 -0.72642 0.56908  117 THR D C   
2258 O O   . THR B 97  ? 2.40837 1.23671 2.80937 -0.27905 -0.71740 0.56553  117 THR D O   
2259 C CB  . THR B 97  ? 2.60262 1.29397 2.75961 -0.34982 -0.71016 0.62972  117 THR D CB  
2260 O OG1 . THR B 97  ? 2.59018 1.25453 2.84635 -0.33040 -0.69075 0.63199  117 THR D OG1 
2261 C CG2 . THR B 97  ? 2.68758 1.32057 2.72493 -0.38911 -0.68638 0.63344  117 THR D CG2 
2262 N N   . PHE B 98  ? 2.39501 1.26793 2.65532 -0.30320 -0.75948 0.57587  118 PHE D N   
2263 C CA  . PHE B 98  ? 2.34525 1.27690 2.69006 -0.27672 -0.78725 0.57666  118 PHE D CA  
2264 C C   . PHE B 98  ? 2.39799 1.30929 2.77561 -0.26759 -0.83303 0.64286  118 PHE D C   
2265 O O   . PHE B 98  ? 2.49394 1.35235 2.79484 -0.28712 -0.85629 0.69597  118 PHE D O   
2266 C CB  . PHE B 98  ? 2.32504 1.31011 2.61672 -0.28376 -0.80273 0.55790  118 PHE D CB  
2267 C CG  . PHE B 98  ? 2.24544 1.27277 2.54728 -0.27867 -0.76571 0.49015  118 PHE D CG  
2268 C CD1 . PHE B 98  ? 2.17050 1.24604 2.57580 -0.25256 -0.74997 0.44981  118 PHE D CD1 
2269 C CD2 . PHE B 98  ? 2.25089 1.26908 2.45854 -0.30057 -0.74682 0.46674  118 PHE D CD2 
2270 C CE1 . PHE B 98  ? 2.10629 1.22041 2.51287 -0.24886 -0.71939 0.38981  118 PHE D CE1 
2271 C CE2 . PHE B 98  ? 2.17953 1.23640 2.39625 -0.29408 -0.71731 0.40798  118 PHE D CE2 
2272 C CZ  . PHE B 98  ? 2.10925 1.21420 2.42150 -0.26842 -0.70515 0.37060  118 PHE D CZ  
2273 N N   . GLY B 99  ? 2.36915 1.32415 2.86467 -0.23758 -0.84610 0.63859  119 GLY D N   
2274 C CA  . GLY B 99  ? 2.40493 1.35196 2.95415 -0.22296 -0.89205 0.69720  119 GLY D CA  
2275 C C   . GLY B 99  ? 2.44803 1.42649 2.94215 -0.23283 -0.94364 0.73021  119 GLY D C   
2276 O O   . GLY B 99  ? 2.43987 1.45532 2.87201 -0.24704 -0.94112 0.70160  119 GLY D O   
2277 N N   . GLN B 100 ? 2.59084 1.55336 3.11099 -0.22490 -0.99191 0.79222  120 GLN D N   
2278 C CA  . GLN B 100 ? 2.64640 1.63506 3.11216 -0.23693 -1.04611 0.82933  120 GLN D CA  
2279 C C   . GLN B 100 ? 2.59412 1.66627 3.11872 -0.22464 -1.05244 0.79068  120 GLN D C   
2280 O O   . GLN B 100 ? 2.62608 1.72635 3.07345 -0.24480 -1.06998 0.78732  120 GLN D O   
2281 C CB  . GLN B 100 ? 2.69717 1.65743 3.19743 -0.22592 -1.09935 0.90257  120 GLN D CB  
2282 N N   . GLY B 101 ? 2.53681 1.64743 3.19650 -0.19387 -1.03550 0.75968  121 GLY D N   
2283 C CA  . GLY B 101 ? 2.49841 1.68552 3.21915 -0.18305 -1.03976 0.72440  121 GLY D CA  
2284 C C   . GLY B 101 ? 2.50556 1.72426 3.33206 -0.16110 -1.08706 0.76106  121 GLY D C   
2285 O O   . GLY B 101 ? 2.56009 1.75168 3.35979 -0.16525 -1.13576 0.82327  121 GLY D O   
2286 N N   . THR B 102 ? 2.40480 1.68134 3.35255 -0.13830 -1.07363 0.72269  122 THR D N   
2287 C CA  . THR B 102 ? 2.39769 1.71067 3.47019 -0.11404 -1.11279 0.74893  122 THR D CA  
2288 C C   . THR B 102 ? 2.37948 1.77049 3.49654 -0.11300 -1.11118 0.70742  122 THR D C   
2289 O O   . THR B 102 ? 2.34044 1.76181 3.50419 -0.10650 -1.06393 0.64722  122 THR D O   
2290 C CB  . THR B 102 ? 2.35410 1.65045 3.56566 -0.08256 -1.09185 0.74530  122 THR D CB  
2291 O OG1 . THR B 102 ? 2.38430 1.60524 3.55935 -0.08312 -1.10465 0.79803  122 THR D OG1 
2292 C CG2 . THR B 102 ? 2.33324 1.68078 3.69496 -0.05502 -1.12296 0.75634  122 THR D CG2 
2293 N N   . LYS B 103 ? 2.59528 1.49578 3.52769 0.50472  0.17705  -0.43245 123 LYS D N   
2294 C CA  . LYS B 103 ? 2.51260 1.57222 3.47819 0.48159  0.09916  -0.42342 123 LYS D CA  
2295 C C   . LYS B 103 ? 2.44653 1.64159 3.55998 0.50011  0.09720  -0.44462 123 LYS D C   
2296 O O   . LYS B 103 ? 2.51591 1.65221 3.64569 0.53707  0.10398  -0.41967 123 LYS D O   
2297 C CB  . LYS B 103 ? 2.58376 1.57602 3.41791 0.48325  0.01359  -0.35158 123 LYS D CB  
2298 N N   . VAL B 104 ? 2.33678 1.71783 3.55644 0.47781  0.08783  -0.48695 124 VAL D N   
2299 C CA  . VAL B 104 ? 2.26721 1.79667 3.63309 0.49416  0.08569  -0.51322 124 VAL D CA  
2300 C C   . VAL B 104 ? 2.23992 1.86331 3.59359 0.48676  -0.00637 -0.46081 124 VAL D C   
2301 O O   . VAL B 104 ? 2.16814 1.93414 3.55916 0.46265  -0.03561 -0.46948 124 VAL D O   
2302 C CB  . VAL B 104 ? 2.17569 1.86146 3.67469 0.48276  0.13901  -0.59871 124 VAL D CB  
2303 C CG1 . VAL B 104 ? 2.11080 1.94990 3.75948 0.50340  0.13577  -0.62736 124 VAL D CG1 
2304 C CG2 . VAL B 104 ? 2.19596 1.78139 3.70853 0.48621  0.22883  -0.65408 124 VAL D CG2 
2305 N N   . GLU B 105 ? 2.36718 1.91241 3.67369 0.51111  -0.04973 -0.40433 125 GLU D N   
2306 C CA  . GLU B 105 ? 2.34011 1.96659 3.64921 0.50895  -0.13648 -0.35611 125 GLU D CA  
2307 C C   . GLU B 105 ? 2.26185 2.04225 3.72106 0.52585  -0.13646 -0.37707 125 GLU D C   
2308 O O   . GLU B 105 ? 2.25161 2.04183 3.79799 0.54635  -0.07350 -0.42064 125 GLU D O   
2309 C CB  . GLU B 105 ? 2.43973 1.91813 3.62866 0.53183  -0.18416 -0.29087 125 GLU D CB  
2310 C CG  . GLU B 105 ? 2.41974 1.96525 3.60826 0.53259  -0.27767 -0.24162 125 GLU D CG  
2311 C CD  . GLU B 105 ? 2.41358 1.96320 3.52700 0.49755  -0.33872 -0.21830 125 GLU D CD  
2312 O OE1 . GLU B 105 ? 2.50413 1.91234 3.48391 0.49782  -0.35400 -0.19468 125 GLU D OE1 
2313 O OE2 . GLU B 105 ? 2.31734 2.01429 3.51073 0.47224  -0.36888 -0.22284 125 GLU D OE2 
2314 N N   . ILE B 106 ? 2.20926 2.11431 3.70801 0.51720  -0.20543 -0.34778 126 ILE D N   
2315 C CA  . ILE B 106 ? 2.13108 2.18859 3.77014 0.53533  -0.21191 -0.36130 126 ILE D CA  
2316 C C   . ILE B 106 ? 2.11174 2.20787 3.74265 0.53862  -0.30046 -0.29771 126 ILE D C   
2317 O O   . ILE B 106 ? 2.06246 2.22361 3.67896 0.51286  -0.35000 -0.27429 126 ILE D O   
2318 C CB  . ILE B 106 ? 2.02488 2.26955 3.77671 0.52118  -0.18128 -0.41832 126 ILE D CB  
2319 N N   . LYS B 107 ? 2.14939 2.20861 3.79643 0.57002  -0.31709 -0.27055 127 LYS D N   
2320 C CA  . LYS B 107 ? 2.15806 2.26716 3.81250 0.57544  -0.40223 -0.21463 127 LYS D CA  
2321 C C   . LYS B 107 ? 2.02659 2.34299 3.82095 0.56777  -0.41676 -0.22925 127 LYS D C   
2322 O O   . LYS B 107 ? 1.96285 2.36709 3.85949 0.57991  -0.36076 -0.27862 127 LYS D O   
2323 C CB  . LYS B 107 ? 2.25528 2.28010 3.89454 0.61548  -0.40963 -0.18288 127 LYS D CB  
2324 N N   . ARG B 108 ? 1.98931 2.38412 3.79465 0.55081  -0.48682 -0.18966 128 ARG D N   
2325 C CA  . ARG B 108 ? 1.86249 2.46155 3.80103 0.54687  -0.49724 -0.19594 128 ARG D CA  
2326 C C   . ARG B 108 ? 1.86262 2.52618 3.87719 0.57140  -0.54114 -0.16365 128 ARG D C   
2327 O O   . ARG B 108 ? 1.96177 2.51299 3.91178 0.58501  -0.57914 -0.12748 128 ARG D O   
2328 C CB  . ARG B 108 ? 1.81345 2.47168 3.74192 0.51553  -0.53828 -0.16823 128 ARG D CB  
2329 N N   . THR B 109 ? 1.75678 2.60048 3.90184 0.58003  -0.53573 -0.17552 129 THR D N   
2330 C CA  . THR B 109 ? 1.74690 2.66596 3.97421 0.60278  -0.57723 -0.14345 129 THR D CA  
2331 C C   . THR B 109 ? 1.80578 2.66972 3.98163 0.59292  -0.66274 -0.07839 129 THR D C   
2332 O O   . THR B 109 ? 1.74307 2.70626 3.96650 0.57530  -0.70173 -0.05179 129 THR D O   
2333 C CB  . THR B 109 ? 1.61732 2.75282 3.98617 0.61095  -0.56729 -0.15751 129 THR D CB  
2334 O OG1 . THR B 109 ? 1.55454 2.77248 3.93301 0.58787  -0.59121 -0.13425 129 THR D OG1 
2335 C CG2 . THR B 109 ? 1.55861 2.76219 3.97956 0.62139  -0.48585 -0.23311 129 THR D CG2 
2336 N N   . ALA B 112 ? 1.63839 2.89290 4.08520 0.43423  -0.90037 0.14466  132 ALA D N   
2337 C CA  . ALA B 112 ? 1.66208 2.89015 4.14220 0.40734  -0.95946 0.17908  132 ALA D CA  
2338 C C   . ALA B 112 ? 1.70465 2.82420 4.09241 0.37346  -0.94845 0.16498  132 ALA D C   
2339 O O   . ALA B 112 ? 1.66126 2.80339 4.02316 0.36822  -0.88514 0.14876  132 ALA D O   
2340 C CB  . ALA B 112 ? 1.59983 2.96585 4.16457 0.40012  -0.92894 0.21869  132 ALA D CB  
2341 N N   . PRO B 113 ? 1.77289 2.77943 4.11248 0.35210  -1.01136 0.16840  133 PRO D N   
2342 C CA  . PRO B 113 ? 1.81901 2.71574 4.06829 0.31984  -1.00474 0.15286  133 PRO D CA  
2343 C C   . PRO B 113 ? 1.73447 2.72617 4.08694 0.29617  -0.97593 0.17968  133 PRO D C   
2344 O O   . PRO B 113 ? 1.73464 2.67387 4.01802 0.27690  -0.93394 0.16488  133 PRO D O   
2345 C CB  . PRO B 113 ? 1.93315 2.71280 4.12782 0.30997  -1.08793 0.14802  133 PRO D CB  
2346 C CG  . PRO B 113 ? 1.91158 2.78810 4.23100 0.32674  -1.14005 0.17604  133 PRO D CG  
2347 C CD  . PRO B 113 ? 1.84021 2.81489 4.20020 0.35907  -1.09181 0.18103  133 PRO D CD  
2348 N N   . SER B 114 ? 1.68004 2.80744 4.19789 0.29883  -0.99444 0.22196  134 SER D N   
2349 C CA  . SER B 114 ? 1.59365 2.83330 4.23270 0.28482  -0.95708 0.25934  134 SER D CA  
2350 C C   . SER B 114 ? 1.63480 2.77265 4.22342 0.24618  -0.95704 0.25035  134 SER D C   
2351 O O   . SER B 114 ? 1.60074 2.73985 4.14575 0.23797  -0.89542 0.24504  134 SER D O   
2352 C CB  . SER B 114 ? 1.50944 2.86683 4.14113 0.30694  -0.86198 0.26228  134 SER D CB  
2353 O OG  . SER B 114 ? 1.51403 2.82208 4.05247 0.32322  -0.84146 0.21773  134 SER D OG  
2354 N N   . VAL B 115 ? 1.68239 2.73493 4.27847 0.22327  -1.02804 0.24563  135 VAL D N   
2355 C CA  . VAL B 115 ? 1.75577 2.69134 4.29203 0.18601  -1.04129 0.22698  135 VAL D CA  
2356 C C   . VAL B 115 ? 1.65846 2.69029 4.35243 0.16457  -1.01100 0.26863  135 VAL D C   
2357 O O   . VAL B 115 ? 1.59268 2.75096 4.43708 0.17386  -1.00302 0.31079  135 VAL D O   
2358 C CB  . VAL B 115 ? 1.87594 2.69503 4.36181 0.17602  -1.13274 0.19762  135 VAL D CB  
2359 C CG1 . VAL B 115 ? 1.93207 2.67132 4.42231 0.13651  -1.15836 0.18275  135 VAL D CG1 
2360 C CG2 . VAL B 115 ? 1.99324 2.68748 4.28823 0.19701  -1.14581 0.15782  135 VAL D CG2 
2361 N N   . PHE B 116 ? 1.78803 2.74811 4.42670 0.13580  -0.98026 0.25806  136 PHE D N   
2362 C CA  . PHE B 116 ? 1.70641 2.74022 4.49095 0.11368  -0.94755 0.29806  136 PHE D CA  
2363 C C   . PHE B 116 ? 1.80688 2.70131 4.53454 0.07188  -0.97332 0.26771  136 PHE D C   
2364 O O   . PHE B 116 ? 1.93589 2.68231 4.49097 0.06386  -1.00377 0.21767  136 PHE D O   
2365 C CB  . PHE B 116 ? 1.60265 2.74808 4.40955 0.12981  -0.85175 0.33103  136 PHE D CB  
2366 C CG  . PHE B 116 ? 1.51601 2.81666 4.39058 0.16873  -0.81060 0.36531  136 PHE D CG  
2367 C CD1 . PHE B 116 ? 1.48903 2.86315 4.44287 0.16904  -0.77639 0.40704  136 PHE D CD1 
2368 C CD2 . PHE B 116 ? 1.50453 2.84312 4.29868 0.20193  -0.78584 0.34452  136 PHE D CD2 
2369 C CE1 . PHE B 116 ? 1.45346 2.93478 4.39204 0.20303  -0.72396 0.42690  136 PHE D CE1 
2370 C CE2 . PHE B 116 ? 1.46608 2.91791 4.25188 0.23385  -0.73171 0.36104  136 PHE D CE2 
2371 C CZ  . PHE B 116 ? 1.44119 2.96377 4.29231 0.23516  -0.70296 0.40199  136 PHE D CZ  
2372 N N   . ILE B 117 ? 1.63172 2.57708 4.51462 0.04761  -0.95988 0.29959  137 ILE D N   
2373 C CA  . ILE B 117 ? 1.71425 2.54531 4.57413 0.00613  -0.97656 0.27271  137 ILE D CA  
2374 C C   . ILE B 117 ? 1.61835 2.53126 4.60815 -0.00887 -0.90011 0.32272  137 ILE D C   
2375 O O   . ILE B 117 ? 1.50387 2.56890 4.67640 0.00729  -0.86556 0.38213  137 ILE D O   
2376 C CB  . ILE B 117 ? 1.78193 2.56659 4.72334 -0.01332 -1.06895 0.24409  137 ILE D CB  
2377 N N   . PHE B 118 ? 1.69589 2.51053 4.59164 -0.03622 -0.87000 0.30286  138 PHE D N   
2378 C CA  . PHE B 118 ? 1.61752 2.49598 4.62886 -0.05194 -0.79597 0.34992  138 PHE D CA  
2379 C C   . PHE B 118 ? 1.71358 2.46490 4.72185 -0.09864 -0.82283 0.31542  138 PHE D C   
2380 O O   . PHE B 118 ? 1.83830 2.43812 4.65759 -0.11414 -0.85083 0.25815  138 PHE D O   
2381 C CB  . PHE B 118 ? 1.56265 2.48062 4.47107 -0.03284 -0.70758 0.36984  138 PHE D CB  
2382 C CG  . PHE B 118 ? 1.43700 2.52825 4.41091 0.01473  -0.66239 0.41532  138 PHE D CG  
2383 C CD1 . PHE B 118 ? 1.44905 2.55488 4.36029 0.04365  -0.70135 0.39208  138 PHE D CD1 
2384 C CD2 . PHE B 118 ? 1.31855 2.56278 4.41673 0.03414  -0.57883 0.48145  138 PHE D CD2 
2385 C CE1 . PHE B 118 ? 1.34554 2.61383 4.31877 0.08822  -0.66063 0.42822  138 PHE D CE1 
2386 C CE2 . PHE B 118 ? 1.25535 2.63065 4.33977 0.08034  -0.52641 0.50959  138 PHE D CE2 
2387 C CZ  . PHE B 118 ? 1.26894 2.65674 4.29269 0.10565  -0.56758 0.48032  138 PHE D CZ  
2388 N N   . PRO B 119 ? 1.61189 2.41920 4.82966 -0.12014 -0.81489 0.34684  139 PRO D N   
2389 C CA  . PRO B 119 ? 1.68717 2.38023 4.92538 -0.16585 -0.84336 0.30713  139 PRO D CA  
2390 C C   . PRO B 119 ? 1.67520 2.31750 4.83652 -0.18453 -0.76834 0.31788  139 PRO D C   
2391 O O   . PRO B 119 ? 1.59282 2.31815 4.73411 -0.16169 -0.68643 0.36795  139 PRO D O   
2392 C CB  . PRO B 119 ? 1.64479 2.44110 5.16781 -0.17712 -0.84713 0.34565  139 PRO D CB  
2393 C CG  . PRO B 119 ? 1.52057 2.49150 5.16087 -0.13938 -0.76641 0.43355  139 PRO D CG  
2394 C CD  . PRO B 119 ? 1.50578 2.49129 4.96003 -0.10064 -0.76646 0.42523  139 PRO D CD  
2395 N N   . PRO B 120 ? 1.75607 2.26918 4.87646 -0.22423 -0.79353 0.27036  140 PRO D N   
2396 C CA  . PRO B 120 ? 1.74296 2.20977 4.80947 -0.24474 -0.71946 0.28495  140 PRO D CA  
2397 C C   . PRO B 120 ? 1.63582 2.24489 4.92158 -0.24277 -0.63053 0.36884  140 PRO D C   
2398 O O   . PRO B 120 ? 1.60713 2.29874 5.12221 -0.24810 -0.63908 0.39771  140 PRO D O   
2399 C CB  . PRO B 120 ? 1.85431 2.17029 4.88272 -0.28756 -0.77748 0.21523  140 PRO D CB  
2400 C CG  . PRO B 120 ? 1.90084 2.22990 5.05106 -0.29165 -0.86871 0.17927  140 PRO D CG  
2401 C CD  . PRO B 120 ? 1.86690 2.27325 4.98103 -0.24943 -0.89211 0.19688  140 PRO D CD  
2402 N N   . SER B 121 ? 1.57786 2.21943 4.79656 -0.23192 -0.54191 0.40979  141 SER D N   
2403 C CA  . SER B 121 ? 1.48247 2.25829 4.89714 -0.22506 -0.44954 0.49428  141 SER D CA  
2404 C C   . SER B 121 ? 1.52388 2.22540 5.05597 -0.27258 -0.44266 0.48552  141 SER D C   
2405 O O   . SER B 121 ? 1.61183 2.15608 5.00670 -0.30734 -0.47709 0.42060  141 SER D O   
2406 C CB  . SER B 121 ? 1.41429 2.25008 4.71926 -0.19776 -0.35812 0.53572  141 SER D CB  
2407 O OG  . SER B 121 ? 1.47177 2.16452 4.61005 -0.22835 -0.34439 0.49569  141 SER D OG  
2408 N N   . ASP B 122 ? 1.45916 2.27940 5.25379 -0.27114 -0.39224 0.55400  142 ASP D N   
2409 C CA  . ASP B 122 ? 1.50689 2.25791 5.41945 -0.30857 -0.37170 0.54904  142 ASP D CA  
2410 C C   . ASP B 122 ? 1.50791 2.18373 5.32232 -0.33714 -0.31845 0.54608  142 ASP D C   
2411 O O   . ASP B 122 ? 1.57616 2.13728 5.41235 -0.38173 -0.33555 0.50215  142 ASP D O   
2412 C CB  . ASP B 122 ? 1.50520 2.33473 5.54798 -0.26803 -0.29254 0.62591  142 ASP D CB  
2413 C CG  . ASP B 122 ? 1.44065 2.38019 5.40651 -0.21215 -0.19007 0.71131  142 ASP D CG  
2414 O OD1 . ASP B 122 ? 1.40056 2.41804 5.28913 -0.17804 -0.20257 0.72091  142 ASP D OD1 
2415 O OD2 . ASP B 122 ? 1.43945 2.38446 5.40641 -0.19938 -0.10046 0.76311  142 ASP D OD2 
2416 N N   . GLU B 123 ? 1.45284 2.17726 5.12221 -0.30507 -0.25459 0.58356  143 GLU D N   
2417 C CA  . GLU B 123 ? 1.47306 2.10503 4.99138 -0.32467 -0.20271 0.57471  143 GLU D CA  
2418 C C   . GLU B 123 ? 1.59212 2.02446 4.88483 -0.35722 -0.28941 0.47074  143 GLU D C   
2419 O O   . GLU B 123 ? 1.65564 1.96850 4.93215 -0.39887 -0.29402 0.43523  143 GLU D O   
2420 C CB  . GLU B 123 ? 1.39297 2.12498 4.79593 -0.27976 -0.12624 0.62496  143 GLU D CB  
2421 C CG  . GLU B 123 ? 1.41724 2.04911 4.63803 -0.29727 -0.08070 0.60792  143 GLU D CG  
2422 C CD  . GLU B 123 ? 1.34661 2.07184 4.43827 -0.25312 -0.01505 0.64024  143 GLU D CD  
2423 O OE1 . GLU B 123 ? 1.26887 2.15813 4.43522 -0.20546 0.00672  0.68577  143 GLU D OE1 
2424 O OE2 . GLU B 123 ? 1.37075 2.00766 4.29077 -0.26538 0.01351  0.61670  143 GLU D OE2 
2425 N N   . GLN B 124 ? 1.62242 2.02507 4.75327 -0.33531 -0.35332 0.42614  144 GLN D N   
2426 C CA  . GLN B 124 ? 1.73920 1.95903 4.64407 -0.35544 -0.43258 0.33394  144 GLN D CA  
2427 C C   . GLN B 124 ? 1.82554 1.95936 4.82980 -0.39444 -0.50705 0.27813  144 GLN D C   
2428 O O   . GLN B 124 ? 1.91286 1.90161 4.80367 -0.42546 -0.53232 0.22129  144 GLN D O   
2429 C CB  . GLN B 124 ? 1.75148 1.97945 4.52334 -0.32021 -0.48775 0.30620  144 GLN D CB  
2430 C CG  . GLN B 124 ? 1.86693 1.92767 4.36857 -0.32421 -0.53365 0.23438  144 GLN D CG  
2431 C CD  . GLN B 124 ? 1.99889 1.98324 4.45774 -0.32484 -0.64291 0.16886  144 GLN D CD  
2432 O OE1 . GLN B 124 ? 1.95306 2.02633 4.54568 -0.31094 -0.68372 0.17848  144 GLN D OE1 
2433 N NE2 . GLN B 124 ? 2.14323 1.96510 4.41457 -0.33798 -0.69021 0.10314  144 GLN D NE2 
2434 N N   . LEU B 125 ? 1.80151 2.02850 5.01587 -0.39063 -0.54079 0.29199  145 LEU D N   
2435 C CA  . LEU B 125 ? 1.87817 2.04296 5.22248 -0.42746 -0.61100 0.23428  145 LEU D CA  
2436 C C   . LEU B 125 ? 1.89079 1.99868 5.30753 -0.46772 -0.55679 0.23755  145 LEU D C   
2437 O O   . LEU B 125 ? 1.99260 1.95865 5.30683 -0.49830 -0.60819 0.16012  145 LEU D O   
2438 C CB  . LEU B 125 ? 1.81957 2.12540 5.43086 -0.41635 -0.62216 0.27328  145 LEU D CB  
2439 C CG  . LEU B 125 ? 1.87027 2.17202 5.45216 -0.40073 -0.72776 0.22032  145 LEU D CG  
2440 C CD1 . LEU B 125 ? 1.77444 2.24360 5.52511 -0.36572 -0.70774 0.29017  145 LEU D CD1 
2441 C CD2 . LEU B 125 ? 1.96545 2.19210 5.64459 -0.43676 -0.81351 0.13885  145 LEU D CD2 
2442 N N   . LYS B 126 ? 1.79264 2.01153 5.37704 -0.46365 -0.45418 0.32605  146 LYS D N   
2443 C CA  . LYS B 126 ? 1.80458 1.97823 5.46647 -0.49453 -0.38980 0.33848  146 LYS D CA  
2444 C C   . LYS B 126 ? 1.86081 1.88779 5.27511 -0.51645 -0.38671 0.29557  146 LYS D C   
2445 O O   . LYS B 126 ? 1.93769 1.85992 5.33017 -0.54498 -0.39124 0.24902  146 LYS D O   
2446 C CB  . LYS B 126 ? 1.71586 2.02662 5.48859 -0.45168 -0.26606 0.44694  146 LYS D CB  
2447 N N   . SER B 127 ? 1.84213 1.86324 5.03238 -0.48474 -0.37300 0.30607  147 SER D N   
2448 C CA  . SER B 127 ? 1.90199 1.78029 4.83270 -0.49586 -0.36563 0.26676  147 SER D CA  
2449 C C   . SER B 127 ? 2.03497 1.74883 4.87792 -0.52943 -0.45746 0.16691  147 SER D C   
2450 O O   . SER B 127 ? 2.08411 1.68925 4.85108 -0.55868 -0.43590 0.14273  147 SER D O   
2451 C CB  . SER B 127 ? 1.88421 1.76748 4.59764 -0.45692 -0.36537 0.26899  147 SER D CB  
2452 O OG  . SER B 127 ? 1.99667 1.77885 4.55479 -0.45124 -0.46599 0.19158  147 SER D OG  
2453 N N   . GLY B 128 ? 2.09228 1.79463 4.94345 -0.52212 -0.55594 0.11098  148 GLY D N   
2454 C CA  . GLY B 128 ? 2.22246 1.78855 5.00316 -0.54717 -0.64858 0.01220  148 GLY D CA  
2455 C C   . GLY B 128 ? 2.29280 1.82351 4.93009 -0.51819 -0.74818 -0.04466 148 GLY D C   
2456 O O   . GLY B 128 ? 2.39640 1.85306 5.01862 -0.52999 -0.83724 -0.12587 148 GLY D O   
2457 N N   . THR B 129 ? 2.77839 1.44941 4.47710 -0.38745 -0.84913 -0.04470 149 THR D N   
2458 C CA  . THR B 129 ? 2.73158 1.48024 4.44094 -0.39787 -0.85780 -0.06075 149 THR D CA  
2459 C C   . THR B 129 ? 2.66885 1.57718 4.51286 -0.40453 -0.88769 -0.00555 149 THR D C   
2460 O O   . THR B 129 ? 2.64424 1.63235 4.54446 -0.36482 -0.86952 0.02353  149 THR D O   
2461 C CB  . THR B 129 ? 2.69735 1.43340 4.34710 -0.33714 -0.80784 -0.13755 149 THR D CB  
2462 O OG1 . THR B 129 ? 2.74383 1.39643 4.25692 -0.36990 -0.79460 -0.17121 149 THR D OG1 
2463 C CG2 . THR B 129 ? 2.61024 1.45703 4.33689 -0.30487 -0.81041 -0.14873 149 THR D CG2 
2464 N N   . ALA B 130 ? 2.59599 1.59043 4.45070 -0.43879 -0.91519 0.01173  150 ALA D N   
2465 C CA  . ALA B 130 ? 2.54505 1.74776 4.48710 -0.42750 -0.92230 0.06389  150 ALA D CA  
2466 C C   . ALA B 130 ? 2.49092 1.78497 4.44386 -0.36982 -0.90546 0.02725  150 ALA D C   
2467 O O   . ALA B 130 ? 2.51017 1.73180 4.40237 -0.38140 -0.91818 -0.01432 150 ALA D O   
2468 C CB  . ALA B 130 ? 2.57376 1.83172 4.53404 -0.51069 -0.97132 0.12042  150 ALA D CB  
2469 N N   . SER B 131 ? 2.36954 1.81458 4.39084 -0.31090 -0.87834 0.04377  151 SER D N   
2470 C CA  . SER B 131 ? 2.32756 1.86031 4.35548 -0.25051 -0.85959 0.01253  151 SER D CA  
2471 C C   . SER B 131 ? 2.25716 1.99787 4.37473 -0.23831 -0.86886 0.06474  151 SER D C   
2472 O O   . SER B 131 ? 2.19199 2.03354 4.37343 -0.22506 -0.85092 0.10467  151 SER D O   
2473 C CB  . SER B 131 ? 2.30134 1.80614 4.31325 -0.18119 -0.80804 -0.03209 151 SER D CB  
2474 O OG  . SER B 131 ? 2.33369 1.66216 4.27662 -0.19129 -0.79630 -0.08015 151 SER D OG  
2475 N N   . VAL B 132 ? 2.16304 1.96634 4.28280 -0.24140 -0.89728 0.06217  152 VAL D N   
2476 C CA  . VAL B 132 ? 2.07276 2.07903 4.27747 -0.22185 -0.90790 0.10088  152 VAL D CA  
2477 C C   . VAL B 132 ? 2.03903 2.09322 4.23063 -0.13930 -0.88004 0.06207  152 VAL D C   
2478 O O   . VAL B 132 ? 2.12285 2.05473 4.22857 -0.12112 -0.87802 0.00811  152 VAL D O   
2479 C CB  . VAL B 132 ? 2.10417 2.14750 4.32047 -0.27838 -0.96492 0.12330  152 VAL D CB  
2480 C CG1 . VAL B 132 ? 1.99398 2.26483 4.31183 -0.25860 -0.97674 0.16290  152 VAL D CG1 
2481 C CG2 . VAL B 132 ? 2.17509 2.12771 4.37368 -0.36900 -0.99266 0.15274  152 VAL D CG2 
2482 N N   . VAL B 133 ? 2.07000 2.29069 4.33518 -0.09187 -0.85568 0.08650  153 VAL D N   
2483 C CA  . VAL B 133 ? 2.04519 2.29589 4.28460 -0.01431 -0.82778 0.04852  153 VAL D CA  
2484 C C   . VAL B 133 ? 1.94349 2.37620 4.25325 0.01726  -0.84431 0.07336  153 VAL D C   
2485 O O   . VAL B 133 ? 1.84117 2.42185 4.24409 -0.00864 -0.85544 0.12408  153 VAL D O   
2486 C CB  . VAL B 133 ? 1.98073 2.23355 4.21912 0.03099  -0.77116 0.03685  153 VAL D CB  
2487 C CG1 . VAL B 133 ? 1.81335 2.24687 4.14964 0.04449  -0.75252 0.08849  153 VAL D CG1 
2488 C CG2 . VAL B 133 ? 2.02463 2.22600 4.18818 0.09350  -0.74374 -0.02026 153 VAL D CG2 
2489 N N   . CYS B 134 ? 1.97193 2.39198 4.23231 0.07468  -0.84451 0.03479  154 CYS D N   
2490 C CA  . CYS B 134 ? 1.89417 2.46820 4.20829 0.12050  -0.86201 0.04726  154 CYS D CA  
2491 C C   . CYS B 134 ? 1.87522 2.45160 4.14351 0.20279  -0.82203 0.01136  154 CYS D C   
2492 O O   . CYS B 134 ? 1.99713 2.42127 4.15477 0.22079  -0.81371 -0.03831 154 CYS D O   
2493 C CB  . CYS B 134 ? 1.99779 2.53214 4.28227 0.10009  -0.92455 0.03872  154 CYS D CB  
2494 S SG  . CYS B 134 ? 1.89023 2.65070 4.28203 0.13563  -0.96483 0.07042  154 CYS D SG  
2495 N N   . LEU B 135 ? 1.86467 2.61320 4.21304 0.24691  -0.79592 0.03594  155 LEU D N   
2496 C CA  . LEU B 135 ? 1.82526 2.60168 4.14359 0.32097  -0.75024 0.01164  155 LEU D CA  
2497 C C   . LEU B 135 ? 1.82402 2.68587 4.14851 0.38657  -0.76992 0.00117  155 LEU D C   
2498 O O   . LEU B 135 ? 1.75254 2.76711 4.17364 0.38627  -0.79877 0.03314  155 LEU D O   
2499 C CB  . LEU B 135 ? 1.67725 2.58662 4.07809 0.32381  -0.70369 0.04754  155 LEU D CB  
2500 C CG  . LEU B 135 ? 1.61838 2.61124 4.01537 0.39840  -0.65853 0.03481  155 LEU D CG  
2501 C CD1 . LEU B 135 ? 1.70668 2.54597 3.98137 0.43035  -0.62667 -0.01639 155 LEU D CD1 
2502 C CD2 . LEU B 135 ? 1.50723 2.64191 3.96234 0.38564  -0.61162 0.07766  155 LEU D CD2 
2503 N N   . LEU B 136 ? 1.73789 2.50449 3.95807 0.44357  -0.75371 -0.04451 156 LEU D N   
2504 C CA  . LEU B 136 ? 1.75510 2.58090 3.96188 0.51911  -0.76764 -0.05930 156 LEU D CA  
2505 C C   . LEU B 136 ? 1.74023 2.56427 3.89430 0.57968  -0.70960 -0.08286 156 LEU D C   
2506 O O   . LEU B 136 ? 1.84946 2.51390 3.87556 0.58906  -0.69233 -0.12570 156 LEU D O   
2507 C CB  . LEU B 136 ? 1.91374 2.59025 4.01403 0.52474  -0.82093 -0.09395 156 LEU D CB  
2508 N N   . ASN B 137 ? 1.69312 2.67422 3.88205 0.60185  -0.66162 -0.05362 157 ASN D N   
2509 C CA  . ASN B 137 ? 1.69301 2.67185 3.81218 0.64319  -0.59529 -0.06842 157 ASN D CA  
2510 C C   . ASN B 137 ? 1.75362 2.76144 3.80625 0.71824  -0.58372 -0.08456 157 ASN D C   
2511 O O   . ASN B 137 ? 1.73720 2.84901 3.83560 0.73929  -0.60852 -0.06651 157 ASN D O   
2512 C CB  . ASN B 137 ? 1.56147 2.67626 3.74939 0.61570  -0.54340 -0.02668 157 ASN D CB  
2513 C CG  . ASN B 137 ? 1.56169 2.61905 3.68869 0.62123  -0.48807 -0.04120 157 ASN D CG  
2514 O OD1 . ASN B 137 ? 1.65544 2.63332 3.68442 0.66628  -0.46775 -0.07765 157 ASN D OD1 
2515 N ND2 . ASN B 137 ? 1.46558 2.55985 3.64620 0.57434  -0.46596 -0.01257 157 ASN D ND2 
2516 N N   . ASN B 138 ? 1.74265 2.66098 3.69031 0.75628  -0.54696 -0.11758 158 ASN D N   
2517 C CA  . ASN B 138 ? 1.81207 2.73886 3.68397 0.82777  -0.52814 -0.13281 158 ASN D CA  
2518 C C   . ASN B 138 ? 1.89112 2.77924 3.73658 0.86484  -0.59004 -0.14721 158 ASN D C   
2519 O O   . ASN B 138 ? 1.86821 2.87678 3.75634 0.90203  -0.59384 -0.12575 158 ASN D O   
2520 C CB  . ASN B 138 ? 1.72167 2.83111 3.65590 0.84532  -0.47392 -0.09326 158 ASN D CB  
2521 C CG  . ASN B 138 ? 1.63570 2.78823 3.60162 0.80195  -0.42372 -0.07338 158 ASN D CG  
2522 O OD1 . ASN B 138 ? 1.52184 2.79707 3.58741 0.75950  -0.41915 -0.03464 158 ASN D OD1 
2523 N ND2 . ASN B 138 ? 1.69462 2.74093 3.57021 0.80970  -0.38951 -0.10190 158 ASN D ND2 
2524 N N   . PHE B 139 ? 1.88955 2.60293 3.66018 0.85470  -0.64016 -0.18527 159 PHE D N   
2525 C CA  . PHE B 139 ? 1.97960 2.62454 3.70774 0.88390  -0.70951 -0.20138 159 PHE D CA  
2526 C C   . PHE B 139 ? 2.13721 2.55869 3.69491 0.91194  -0.73111 -0.25766 159 PHE D C   
2527 O O   . PHE B 139 ? 2.17824 2.48415 3.66980 0.88784  -0.70616 -0.28720 159 PHE D O   
2528 C CB  . PHE B 139 ? 1.95106 2.60744 3.76885 0.82770  -0.77228 -0.18340 159 PHE D CB  
2529 N N   . TYR B 140 ? 2.05970 2.42050 3.54034 0.96269  -0.77725 -0.27253 160 TYR D N   
2530 C CA  . TYR B 140 ? 2.21791 2.35004 3.51618 0.98807  -0.81280 -0.32328 160 TYR D CA  
2531 C C   . TYR B 140 ? 2.28711 2.38656 3.56348 1.01661  -0.89252 -0.32091 160 TYR D C   
2532 O O   . TYR B 140 ? 2.21614 2.48786 3.60087 1.04092  -0.89880 -0.28516 160 TYR D O   
2533 C CB  . TYR B 140 ? 2.27528 2.35139 3.44579 1.03954  -0.75881 -0.34791 160 TYR D CB  
2534 N N   . PRO B 141 ? 2.34518 2.22551 3.47806 1.01235  -0.95408 -0.35760 161 PRO D N   
2535 C CA  . PRO B 141 ? 2.45419 2.10735 3.40602 0.94915  -0.93367 -0.39832 161 PRO D CA  
2536 C C   . PRO B 141 ? 2.45471 2.06120 3.43143 0.84518  -0.94000 -0.39369 161 PRO D C   
2537 O O   . PRO B 141 ? 2.35526 2.11063 3.49720 0.81265  -0.94509 -0.35572 161 PRO D O   
2538 C CB  . PRO B 141 ? 2.60950 2.06861 3.37591 0.98982  -0.99414 -0.42988 161 PRO D CB  
2539 C CG  . PRO B 141 ? 2.59497 2.15999 3.47532 1.02520  -1.07333 -0.39804 161 PRO D CG  
2540 C CD  . PRO B 141 ? 2.41841 2.26917 3.52815 1.03911  -1.03568 -0.35170 161 PRO D CD  
2541 N N   . ARG B 142 ? 2.72131 2.11161 3.52207 0.78920  -0.93645 -0.43577 162 ARG D N   
2542 C CA  . ARG B 142 ? 2.75139 2.06323 3.54424 0.69207  -0.94192 -0.44254 162 ARG D CA  
2543 C C   . ARG B 142 ? 2.85388 2.10020 3.62520 0.67466  -1.02879 -0.43350 162 ARG D C   
2544 O O   . ARG B 142 ? 2.86875 2.17549 3.67428 0.74033  -1.08374 -0.41380 162 ARG D O   
2545 C CB  . ARG B 142 ? 2.77223 1.89624 3.38991 0.63887  -0.89648 -0.49590 162 ARG D CB  
2546 N N   . GLU B 143 ? 2.97545 2.09765 3.68809 0.58647  -1.04267 -0.44966 163 GLU D N   
2547 C CA  . GLU B 143 ? 3.08724 2.14244 3.77971 0.55125  -1.12257 -0.43977 163 GLU D CA  
2548 C C   . GLU B 143 ? 3.02609 2.29955 3.92777 0.57178  -1.15972 -0.38237 163 GLU D C   
2549 O O   . GLU B 143 ? 3.02467 2.36578 3.96425 0.63131  -1.21973 -0.36153 163 GLU D O   
2550 C CB  . GLU B 143 ? 3.21097 2.09478 3.72185 0.58856  -1.18286 -0.46581 163 GLU D CB  
2551 N N   . ALA B 144 ? 3.08354 2.46545 4.11793 0.51869  -1.12226 -0.35871 164 ALA D N   
2552 C CA  . ALA B 144 ? 2.94595 2.54637 4.18327 0.52119  -1.14029 -0.30397 164 ALA D CA  
2553 C C   . ALA B 144 ? 2.98362 2.55728 4.26367 0.42221  -1.14810 -0.29060 164 ALA D C   
2554 O O   . ALA B 144 ? 2.87303 2.54780 4.26432 0.39094  -1.10351 -0.26837 164 ALA D O   
2555 C CB  . ALA B 144 ? 2.75503 2.54620 4.12498 0.56858  -1.07669 -0.28104 164 ALA D CB  
2556 N N   . LYS B 145 ? 3.10134 2.52611 4.28216 0.37120  -1.20571 -0.30484 165 LYS D N   
2557 C CA  . LYS B 145 ? 3.15019 2.51679 4.34384 0.27377  -1.21260 -0.29927 165 LYS D CA  
2558 C C   . LYS B 145 ? 2.97967 2.55200 4.36797 0.25510  -1.21747 -0.24275 165 LYS D C   
2559 O O   . LYS B 145 ? 2.91534 2.60796 4.38973 0.27023  -1.27577 -0.20708 165 LYS D O   
2560 C CB  . LYS B 145 ? 3.27956 2.48258 4.35004 0.22777  -1.28604 -0.31477 165 LYS D CB  
2561 N N   . VAL B 146 ? 2.93647 2.54630 4.38907 0.21924  -1.15758 -0.23564 166 VAL D N   
2562 C CA  . VAL B 146 ? 2.76615 2.55948 4.38950 0.19655  -1.15134 -0.18295 166 VAL D CA  
2563 C C   . VAL B 146 ? 2.80453 2.55304 4.43861 0.10942  -1.20127 -0.16358 166 VAL D C   
2564 O O   . VAL B 146 ? 2.90564 2.46749 4.42672 0.04896  -1.20464 -0.19537 166 VAL D O   
2565 C CB  . VAL B 146 ? 2.67937 2.50212 4.34694 0.18983  -1.07323 -0.18366 166 VAL D CB  
2566 C CG1 . VAL B 146 ? 2.48235 2.51749 4.32270 0.18680  -1.06285 -0.12673 166 VAL D CG1 
2567 C CG2 . VAL B 146 ? 2.68802 2.47878 4.28600 0.25722  -1.02183 -0.21967 166 VAL D CG2 
2568 N N   . SER B 147 ? 2.69508 2.61775 4.46285 0.09889  -1.23847 -0.11292 167 SER D N   
2569 C CA  . SER B 147 ? 2.71759 2.62203 4.50351 0.01579  -1.29233 -0.08823 167 SER D CA  
2570 C C   . SER B 147 ? 2.58383 2.61078 4.49509 -0.03325 -1.26353 -0.04509 167 SER D C   
2571 O O   . SER B 147 ? 2.43960 2.64527 4.46571 0.00810  -1.23168 -0.01768 167 SER D O   
2572 C CB  . SER B 147 ? 2.70856 2.71982 4.53981 0.03933  -1.37057 -0.06458 167 SER D CB  
2573 O OG  . SER B 147 ? 2.82697 2.73164 4.54223 0.09863  -1.39895 -0.10124 167 SER D OG  
2574 N N   . TRP B 148 ? 2.58173 2.50065 4.45987 -0.12300 -1.27265 -0.04083 168 TRP D N   
2575 C CA  . TRP B 148 ? 2.48287 2.48141 4.45493 -0.18010 -1.25172 -0.00015 168 TRP D CA  
2576 C C   . TRP B 148 ? 2.49271 2.50864 4.48799 -0.26314 -1.31638 0.03308  168 TRP D C   
2577 O O   . TRP B 148 ? 2.59371 2.47857 4.49424 -0.29666 -1.36380 0.01251  168 TRP D O   
2578 C CB  . TRP B 148 ? 2.50651 2.34451 4.41028 -0.21005 -1.19531 -0.02800 168 TRP D CB  
2579 C CG  . TRP B 148 ? 2.45821 2.32948 4.37873 -0.14258 -1.12600 -0.04459 168 TRP D CG  
2580 C CD1 . TRP B 148 ? 2.51878 2.30180 4.35158 -0.08524 -1.09499 -0.09442 168 TRP D CD1 
2581 C CD2 . TRP B 148 ? 2.34474 2.32231 4.35855 -0.13681 -1.07936 -0.01369 168 TRP D CD2 
2582 N NE1 . TRP B 148 ? 2.44702 2.28996 4.32102 -0.04077 -1.03310 -0.09560 168 TRP D NE1 
2583 C CE2 . TRP B 148 ? 2.33506 2.29526 4.31998 -0.06991 -1.02341 -0.04605 168 TRP D CE2 
2584 C CE3 . TRP B 148 ? 2.25151 2.33584 4.36342 -0.18506 -1.08152 0.03933  168 TRP D CE3 
2585 C CZ2 . TRP B 148 ? 2.22555 2.27335 4.28021 -0.04716 -0.97217 -0.02626 168 TRP D CZ2 
2586 C CZ3 . TRP B 148 ? 2.15073 2.31386 4.32564 -0.16299 -1.03033 0.05884  168 TRP D CZ3 
2587 C CH2 . TRP B 148 ? 2.13374 2.27908 4.28176 -0.09327 -0.97750 0.02652  168 TRP D CH2 
2588 N N   . TYR B 149 ? 2.39349 2.57080 4.50836 -0.30144 -1.31948 0.08476  169 TYR D N   
2589 C CA  . TYR B 149 ? 2.41963 2.64182 4.56731 -0.38599 -1.38008 0.12145  169 TYR D CA  
2590 C C   . TYR B 149 ? 2.38557 2.62722 4.58027 -0.46279 -1.35499 0.15868  169 TYR D C   
2591 O O   . TYR B 149 ? 2.27937 2.70559 4.58832 -0.45399 -1.33382 0.19641  169 TYR D O   
2592 C CB  . TYR B 149 ? 2.34942 2.80264 4.60981 -0.35153 -1.42767 0.15166  169 TYR D CB  
2593 C CG  . TYR B 149 ? 2.40399 2.82830 4.61119 -0.28360 -1.47122 0.12080  169 TYR D CG  
2594 C CD1 . TYR B 149 ? 2.37048 2.81481 4.56775 -0.17779 -1.43926 0.09176  169 TYR D CD1 
2595 C CD2 . TYR B 149 ? 2.49364 2.86602 4.65381 -0.32654 -1.54723 0.12227  169 TYR D CD2 
2596 C CE1 . TYR B 149 ? 2.43387 2.83585 4.56911 -0.11462 -1.48206 0.06433  169 TYR D CE1 
2597 C CE2 . TYR B 149 ? 2.55392 2.88911 4.65660 -0.26301 -1.59283 0.09608  169 TYR D CE2 
2598 C CZ  . TYR B 149 ? 2.52755 2.87340 4.61542 -0.15586 -1.56021 0.06701  169 TYR D CZ  
2599 O OH  . TYR B 149 ? 2.60445 2.89583 4.62088 -0.09163 -1.60838 0.04127  169 TYR D OH  
2600 N N   . VAL B 150 ? 2.45766 2.50504 4.55830 -0.54031 -1.35872 0.14788  170 VAL D N   
2601 C CA  . VAL B 150 ? 2.45143 2.49038 4.57708 -0.62239 -1.34745 0.18482  170 VAL D CA  
2602 C C   . VAL B 150 ? 2.47433 2.59417 4.63368 -0.70761 -1.41396 0.22518  170 VAL D C   
2603 O O   . VAL B 150 ? 2.56948 2.55482 4.64132 -0.76189 -1.45782 0.21057  170 VAL D O   
2604 C CB  . VAL B 150 ? 2.52815 2.31732 4.53645 -0.65926 -1.31670 0.15140  170 VAL D CB  
2605 C CG1 . VAL B 150 ? 2.54035 2.30617 4.56253 -0.74645 -1.31507 0.19225  170 VAL D CG1 
2606 C CG2 . VAL B 150 ? 2.49294 2.23180 4.48265 -0.57608 -1.25115 0.11336  170 VAL D CG2 
2607 N N   . ASP B 151 ? 2.87497 2.62819 4.09194 -0.90280 -1.33661 0.45470  171 ASP D N   
2608 C CA  . ASP B 151 ? 2.88575 2.74225 4.09658 -0.96880 -1.38145 0.46393  171 ASP D CA  
2609 C C   . ASP B 151 ? 2.90436 2.86710 4.14750 -0.90644 -1.36663 0.44397  171 ASP D C   
2610 O O   . ASP B 151 ? 2.98157 2.92377 4.17693 -0.91829 -1.40015 0.43560  171 ASP D O   
2611 C CB  . ASP B 151 ? 2.98656 2.68345 4.09196 -1.02981 -1.43754 0.46610  171 ASP D CB  
2612 C CG  . ASP B 151 ? 2.98589 2.60673 4.05667 -1.11297 -1.46900 0.49279  171 ASP D CG  
2613 O OD1 . ASP B 151 ? 2.90680 2.61909 4.04039 -1.13139 -1.44825 0.51199  171 ASP D OD1 
2614 O OD2 . ASP B 151 ? 3.11018 2.57296 4.08534 -1.16035 -1.51608 0.49446  171 ASP D OD2 
2615 N N   . ASN B 152 ? 2.72031 2.79053 4.04029 -0.83933 -1.31813 0.43674  172 ASN D N   
2616 C CA  . ASN B 152 ? 2.73935 2.90510 4.09164 -0.76882 -1.30272 0.41835  172 ASN D CA  
2617 C C   . ASN B 152 ? 2.87675 2.88996 4.14714 -0.71728 -1.30748 0.39609  172 ASN D C   
2618 O O   . ASN B 152 ? 2.93428 2.99049 4.18946 -0.70368 -1.33088 0.38744  172 ASN D O   
2619 C CB  . ASN B 152 ? 2.68498 3.05158 4.08839 -0.81381 -1.33600 0.42605  172 ASN D CB  
2620 C CG  . ASN B 152 ? 2.54267 3.08352 4.03162 -0.86296 -1.32568 0.44300  172 ASN D CG  
2621 O OD1 . ASN B 152 ? 2.50612 3.00938 3.98209 -0.93581 -1.33484 0.46340  172 ASN D OD1 
2622 N ND2 . ASN B 152 ? 2.46570 3.19552 4.03908 -0.82177 -1.30768 0.43316  172 ASN D ND2 
2623 N N   . ALA B 153 ? 2.85350 2.69358 4.07159 -0.68736 -1.28448 0.38519  173 ALA D N   
2624 C CA  . ALA B 153 ? 2.97500 2.66652 4.11406 -0.63649 -1.27916 0.35953  173 ALA D CA  
2625 C C   . ALA B 153 ? 2.97279 2.61191 4.12258 -0.55894 -1.22020 0.34416  173 ALA D C   
2626 O O   . ALA B 153 ? 2.91601 2.50256 4.07794 -0.56121 -1.19718 0.34785  173 ALA D O   
2627 C CB  . ALA B 153 ? 3.03593 2.56045 4.08787 -0.68263 -1.31330 0.35455  173 ALA D CB  
2628 N N   . LEU B 154 ? 2.90711 2.55755 4.04678 -0.49379 -1.19870 0.32795  174 LEU D N   
2629 C CA  . LEU B 154 ? 2.89586 2.51497 4.04382 -0.42552 -1.14254 0.31522  174 LEU D CA  
2630 C C   . LEU B 154 ? 2.90848 2.37543 4.00804 -0.41617 -1.11871 0.29976  174 LEU D C   
2631 O O   . LEU B 154 ? 2.97764 2.32326 4.00284 -0.42417 -1.13744 0.28233  174 LEU D O   
2632 C CB  . LEU B 154 ? 2.98343 2.59566 4.09401 -0.36698 -1.13508 0.29922  174 LEU D CB  
2633 C CG  . LEU B 154 ? 2.94761 2.69783 4.11941 -0.32587 -1.12321 0.30606  174 LEU D CG  
2634 C CD1 . LEU B 154 ? 3.07493 2.79058 4.18870 -0.27573 -1.13193 0.29230  174 LEU D CD1 
2635 C CD2 . LEU B 154 ? 2.87637 2.64529 4.09245 -0.29252 -1.06920 0.30720  174 LEU D CD2 
2636 N N   . GLN B 155 ? 2.99821 2.47814 4.14182 -0.39813 -1.07771 0.30410  175 GLN D N   
2637 C CA  . GLN B 155 ? 2.96887 2.32809 4.08169 -0.38361 -1.05290 0.28892  175 GLN D CA  
2638 C C   . GLN B 155 ? 2.96284 2.31736 4.07787 -0.32113 -0.99446 0.27385  175 GLN D C   
2639 O O   . GLN B 155 ? 2.91665 2.36718 4.09142 -0.30659 -0.96633 0.28770  175 GLN D O   
2640 C CB  . GLN B 155 ? 2.86938 2.23835 4.02585 -0.42834 -1.06277 0.31015  175 GLN D CB  
2641 C CG  . GLN B 155 ? 2.87920 2.21934 4.01324 -0.49896 -1.12252 0.32484  175 GLN D CG  
2642 C CD  . GLN B 155 ? 2.97022 2.17104 4.01382 -0.49911 -1.15145 0.30000  175 GLN D CD  
2643 O OE1 . GLN B 155 ? 2.98166 2.06724 3.98119 -0.45968 -1.13101 0.27230  175 GLN D OE1 
2644 N NE2 . GLN B 155 ? 3.02577 2.24284 4.04127 -0.54560 -1.19909 0.30773  175 GLN D NE2 
2645 N N   . SER B 156 ? 3.03135 2.27534 4.07692 -0.28852 -0.97630 0.24404  176 SER D N   
2646 C CA  . SER B 156 ? 3.01046 2.22833 4.03774 -0.23850 -0.92166 0.22543  176 SER D CA  
2647 C C   . SER B 156 ? 2.94620 2.06052 3.94087 -0.23022 -0.90578 0.19984  176 SER D C   
2648 O O   . SER B 156 ? 2.94061 1.99531 3.92301 -0.25761 -0.94029 0.19656  176 SER D O   
2649 C CB  . SER B 156 ? 3.11494 2.31078 4.07869 -0.20733 -0.91531 0.21009  176 SER D CB  
2650 O OG  . SER B 156 ? 3.08114 2.20676 3.99316 -0.17375 -0.87031 0.18323  176 SER D OG  
2651 N N   . GLY B 157 ? 3.05480 2.15098 4.03663 -0.19287 -0.85464 0.18121  177 GLY D N   
2652 C CA  . GLY B 157 ? 3.00511 2.01682 3.95561 -0.17627 -0.83601 0.14908  177 GLY D CA  
2653 C C   . GLY B 157 ? 2.94737 1.93448 3.93782 -0.19601 -0.85950 0.15652  177 GLY D C   
2654 O O   . GLY B 157 ? 2.92874 1.83931 3.89444 -0.17966 -0.85654 0.12754  177 GLY D O   
2655 N N   . ASN B 158 ? 2.92821 1.98190 3.97822 -0.23172 -0.88537 0.19469  178 ASN D N   
2656 C CA  . ASN B 158 ? 2.86991 1.91472 3.96252 -0.25778 -0.90687 0.21271  178 ASN D CA  
2657 C C   . ASN B 158 ? 2.79943 1.95391 3.96857 -0.26541 -0.87984 0.24401  178 ASN D C   
2658 O O   . ASN B 158 ? 2.75124 1.92013 3.96231 -0.29538 -0.89733 0.26751  178 ASN D O   
2659 C CB  . ASN B 158 ? 2.91879 1.93174 3.99703 -0.31084 -0.97134 0.23025  178 ASN D CB  
2660 C CG  . ASN B 158 ? 2.97303 2.07097 4.06060 -0.33932 -0.99118 0.25100  178 ASN D CG  
2661 O OD1 . ASN B 158 ? 2.96055 2.16205 4.09050 -0.32621 -0.96257 0.26392  178 ASN D OD1 
2662 N ND2 . ASN B 158 ? 3.03733 2.09388 4.08554 -0.37883 -1.04309 0.25381  178 ASN D ND2 
2663 N N   . SER B 159 ? 2.76594 1.99044 3.94629 -0.24014 -0.83938 0.24414  179 SER D N   
2664 C CA  . SER B 159 ? 2.71495 2.04623 3.96067 -0.24294 -0.80987 0.26923  179 SER D CA  
2665 C C   . SER B 159 ? 2.66171 1.98458 3.90159 -0.20238 -0.75205 0.25155  179 SER D C   
2666 O O   . SER B 159 ? 2.69369 1.98386 3.88033 -0.17006 -0.72567 0.22711  179 SER D O   
2667 C CB  . SER B 159 ? 2.77941 2.19450 4.03619 -0.24332 -0.81379 0.28116  179 SER D CB  
2668 O OG  . SER B 159 ? 2.83902 2.25053 4.08147 -0.27568 -0.86668 0.28775  179 SER D OG  
2669 N N   . GLN B 160 ? 2.62408 1.97678 3.91313 -0.20904 -0.73384 0.26466  180 GLN D N   
2670 C CA  . GLN B 160 ? 2.56774 1.93220 3.85930 -0.17842 -0.67825 0.25217  180 GLN D CA  
2671 C C   . GLN B 160 ? 2.53643 2.00409 3.88278 -0.18872 -0.65107 0.27941  180 GLN D C   
2672 O O   . GLN B 160 ? 2.50050 2.02212 3.90452 -0.22247 -0.66803 0.30739  180 GLN D O   
2673 C CB  . GLN B 160 ? 2.51428 1.83182 3.81696 -0.17211 -0.67706 0.24139  180 GLN D CB  
2674 N N   . GLU B 161 ? 2.47465 1.96437 3.79635 -0.16232 -0.61036 0.27046  181 GLU D N   
2675 C CA  . GLU B 161 ? 2.46542 2.04434 3.82835 -0.16551 -0.58364 0.29056  181 GLU D CA  
2676 C C   . GLU B 161 ? 2.39621 1.98457 3.76163 -0.15362 -0.53065 0.28598  181 GLU D C   
2677 O O   . GLU B 161 ? 2.37955 1.91055 3.69587 -0.13282 -0.50519 0.26105  181 GLU D O   
2678 C CB  . GLU B 161 ? 2.55422 2.14790 3.88303 -0.14354 -0.58204 0.28607  181 GLU D CB  
2679 N N   . SER B 162 ? 2.30435 1.97375 3.72683 -0.17086 -0.51391 0.30914  182 SER D N   
2680 C CA  . SER B 162 ? 2.24762 1.94126 3.67647 -0.16605 -0.46349 0.30954  182 SER D CA  
2681 C C   . SER B 162 ? 2.23953 2.01736 3.70268 -0.17315 -0.44387 0.32753  182 SER D C   
2682 O O   . SER B 162 ? 2.19352 2.03922 3.71153 -0.19705 -0.47013 0.34714  182 SER D O   
2683 C CB  . SER B 162 ? 2.17452 1.87263 3.64606 -0.18530 -0.46503 0.31840  182 SER D CB  
2684 O OG  . SER B 162 ? 2.16812 1.79039 3.60139 -0.16543 -0.46846 0.29214  182 SER D OG  
2685 N N   . VAL B 163 ? 2.16489 1.93912 3.59160 -0.15483 -0.39755 0.31881  183 VAL D N   
2686 C CA  . VAL B 163 ? 2.15931 1.99825 3.60400 -0.15282 -0.37579 0.32900  183 VAL D CA  
2687 C C   . VAL B 163 ? 2.10560 1.97016 3.56021 -0.16597 -0.32865 0.33482  183 VAL D C   
2688 O O   . VAL B 163 ? 2.10821 1.92280 3.51786 -0.16013 -0.30048 0.32145  183 VAL D O   
2689 C CB  . VAL B 163 ? 2.25179 2.04728 3.62586 -0.11586 -0.37031 0.31304  183 VAL D CB  
2690 C CG1 . VAL B 163 ? 2.25892 2.13042 3.66701 -0.10710 -0.36856 0.32137  183 VAL D CG1 
2691 C CG2 . VAL B 163 ? 2.31724 2.05723 3.65622 -0.10147 -0.41198 0.30178  183 VAL D CG2 
2692 N N   . THR B 164 ? 2.08590 2.03598 3.59799 -0.18612 -0.31914 0.35302  184 THR D N   
2693 C CA  . THR B 164 ? 2.03574 2.01850 3.55935 -0.20339 -0.27543 0.36091  184 THR D CA  
2694 C C   . THR B 164 ? 2.12444 2.07114 3.57617 -0.17803 -0.23509 0.34582  184 THR D C   
2695 O O   . THR B 164 ? 2.20515 2.08953 3.59284 -0.14668 -0.24273 0.32960  184 THR D O   
2696 C CB  . THR B 164 ? 1.93113 2.01722 3.53489 -0.23834 -0.27965 0.38439  184 THR D CB  
2697 O OG1 . THR B 164 ? 1.96397 2.10070 3.57908 -0.22394 -0.28657 0.38066  184 THR D OG1 
2698 C CG2 . THR B 164 ? 1.84660 1.95347 3.50674 -0.27178 -0.32343 0.40260  184 THR D CG2 
2699 N N   . GLU B 165 ? 1.98412 1.96125 3.43726 -0.19428 -0.19377 0.35192  185 GLU D N   
2700 C CA  . GLU B 165 ? 2.06230 2.00014 3.44101 -0.17703 -0.15645 0.33993  185 GLU D CA  
2701 C C   . GLU B 165 ? 2.06263 2.06681 3.47443 -0.17413 -0.14986 0.34559  185 GLU D C   
2702 O O   . GLU B 165 ? 1.97166 2.06904 3.46799 -0.19916 -0.16009 0.36114  185 GLU D O   
2703 C CB  . GLU B 165 ? 2.05059 1.97035 3.39311 -0.19877 -0.11156 0.33867  185 GLU D CB  
2704 N N   . GLN B 166 ? 2.02921 1.98155 3.36803 -0.14360 -0.13439 0.33109  186 GLN D N   
2705 C CA  . GLN B 166 ? 2.04992 2.05556 3.40934 -0.12837 -0.12823 0.32810  186 GLN D CA  
2706 C C   . GLN B 166 ? 1.97269 2.07068 3.39708 -0.16972 -0.09959 0.34279  186 GLN D C   
2707 O O   . GLN B 166 ? 1.97657 2.05269 3.36909 -0.19543 -0.06189 0.34759  186 GLN D O   
2708 C CB  . GLN B 166 ? 2.15541 2.06492 3.40555 -0.09463 -0.10800 0.31094  186 GLN D CB  
2709 C CG  . GLN B 166 ? 2.23332 2.07063 3.42673 -0.04436 -0.14418 0.29613  186 GLN D CG  
2710 C CD  . GLN B 166 ? 2.26902 2.15174 3.48654 -0.00170 -0.16135 0.28459  186 GLN D CD  
2711 O OE1 . GLN B 166 ? 2.31716 2.17338 3.48871 0.01512  -0.13751 0.27481  186 GLN D OE1 
2712 N NE2 . GLN B 166 ? 2.24478 2.19461 3.52969 0.01788  -0.20429 0.28295  186 GLN D NE2 
2713 N N   . ASP B 167 ? 2.03581 2.24318 3.55017 -0.18131 -0.11819 0.35020  187 ASP D N   
2714 C CA  . ASP B 167 ? 1.94051 2.24006 3.51414 -0.22521 -0.09292 0.36458  187 ASP D CA  
2715 C C   . ASP B 167 ? 2.02210 2.30398 3.54272 -0.21204 -0.05033 0.35106  187 ASP D C   
2716 O O   . ASP B 167 ? 2.11696 2.35988 3.59021 -0.16422 -0.05343 0.32973  187 ASP D O   
2717 C CB  . ASP B 167 ? 1.81895 2.24261 3.48968 -0.24416 -0.12217 0.37224  187 ASP D CB  
2718 C CG  . ASP B 167 ? 1.67957 2.20099 3.41211 -0.30051 -0.10134 0.39078  187 ASP D CG  
2719 O OD1 . ASP B 167 ? 1.70125 2.21788 3.40572 -0.31031 -0.05875 0.38897  187 ASP D OD1 
2720 O OD2 . ASP B 167 ? 1.54648 2.14534 3.35010 -0.34021 -0.12994 0.40872  187 ASP D OD2 
2721 N N   . SER B 168 ? 1.96506 2.26927 3.48858 -0.25397 -0.01309 0.36341  188 SER D N   
2722 C CA  . SER B 168 ? 2.06190 2.33442 3.52160 -0.24862 0.02971  0.35130  188 SER D CA  
2723 C C   . SER B 168 ? 2.06661 2.40698 3.55523 -0.22353 0.03017  0.33366  188 SER D C   
2724 O O   . SER B 168 ? 2.18483 2.46540 3.60075 -0.19131 0.05058  0.31334  188 SER D O   
2725 C CB  . SER B 168 ? 1.99060 2.29268 3.45872 -0.30499 0.06702  0.36981  188 SER D CB  
2726 O OG  . SER B 168 ? 1.80616 2.22855 3.37530 -0.34670 0.05798  0.38875  188 SER D OG  
2727 N N   . LYS B 169 ? 1.86659 2.33136 3.45597 -0.23893 0.00750  0.33911  189 LYS D N   
2728 C CA  . LYS B 169 ? 1.84265 2.40021 3.47131 -0.21973 0.01190  0.31837  189 LYS D CA  
2729 C C   . LYS B 169 ? 1.88757 2.44684 3.52008 -0.15552 -0.02618 0.29448  189 LYS D C   
2730 O O   . LYS B 169 ? 1.99614 2.51088 3.57559 -0.09908 -0.02057 0.26657  189 LYS D O   
2731 C CB  . LYS B 169 ? 1.64873 2.35762 3.38159 -0.28047 0.01159  0.33536  189 LYS D CB  
2732 N N   . ASP B 170 ? 1.86479 2.47073 3.55546 -0.16285 -0.06799 0.30501  190 ASP D N   
2733 C CA  . ASP B 170 ? 1.88500 2.51651 3.59195 -0.10838 -0.10734 0.28413  190 ASP D CA  
2734 C C   . ASP B 170 ? 2.02927 2.51235 3.64465 -0.05515 -0.12749 0.27624  190 ASP D C   
2735 O O   . ASP B 170 ? 2.07711 2.55704 3.68164 0.00373  -0.15540 0.25425  190 ASP D O   
2736 C CB  . ASP B 170 ? 1.73974 2.48637 3.54126 -0.14642 -0.14512 0.29916  190 ASP D CB  
2737 C CG  . ASP B 170 ? 1.71799 2.39794 3.51189 -0.18728 -0.16270 0.32917  190 ASP D CG  
2738 O OD1 . ASP B 170 ? 1.83224 2.38305 3.55370 -0.15858 -0.16942 0.32835  190 ASP D OD1 
2739 O OD2 . ASP B 170 ? 1.58233 2.33811 3.43951 -0.24930 -0.17101 0.35252  190 ASP D OD2 
2740 N N   . SER B 171 ? 1.97426 2.34230 3.52479 -0.07553 -0.11563 0.29254  191 SER D N   
2741 C CA  . SER B 171 ? 2.08940 2.31739 3.54707 -0.03731 -0.13327 0.28657  191 SER D CA  
2742 C C   . SER B 171 ? 2.06733 2.31541 3.56085 -0.02014 -0.18498 0.28730  191 SER D C   
2743 O O   . SER B 171 ? 2.15592 2.32131 3.58695 0.02790  -0.21014 0.27452  191 SER D O   
2744 C CB  . SER B 171 ? 2.21208 2.34658 3.57418 0.02027  -0.12398 0.26247  191 SER D CB  
2745 O OG  . SER B 171 ? 2.24299 2.35247 3.56366 -0.00016 -0.07644 0.26146  191 SER D OG  
2746 N N   . THR B 172 ? 2.06741 2.41997 3.65457 -0.06282 -0.20353 0.30338  192 THR D N   
2747 C CA  . THR B 172 ? 2.04773 2.41368 3.66466 -0.06141 -0.25168 0.30811  192 THR D CA  
2748 C C   . THR B 172 ? 2.03628 2.34009 3.64201 -0.10250 -0.25585 0.32843  192 THR D C   
2749 O O   . THR B 172 ? 2.00413 2.28890 3.60354 -0.13696 -0.22409 0.34081  192 THR D O   
2750 C CB  . THR B 172 ? 1.91460 2.44105 3.63734 -0.08375 -0.27613 0.31015  192 THR D CB  
2751 O OG1 . THR B 172 ? 1.78973 2.38534 3.57076 -0.15210 -0.26025 0.33297  192 THR D OG1 
2752 C CG2 . THR B 172 ? 1.90980 2.51866 3.65410 -0.04003 -0.26850 0.28398  192 THR D CG2 
2753 N N   . TYR B 173 ? 2.06734 2.34033 3.66935 -0.09577 -0.29681 0.32953  193 TYR D N   
2754 C CA  . TYR B 173 ? 2.05846 2.25980 3.64082 -0.12217 -0.30618 0.34128  193 TYR D CA  
2755 C C   . TYR B 173 ? 1.94603 2.22335 3.60818 -0.17075 -0.33865 0.36049  193 TYR D C   
2756 O O   . TYR B 173 ? 1.85481 2.24826 3.58734 -0.19401 -0.34897 0.36719  193 TYR D O   
2757 C CB  . TYR B 173 ? 2.16534 2.25756 3.66900 -0.08311 -0.32750 0.32705  193 TYR D CB  
2758 C CG  . TYR B 173 ? 2.23969 2.22218 3.64514 -0.06140 -0.29148 0.31590  193 TYR D CG  
2759 C CD1 . TYR B 173 ? 2.20477 2.14884 3.58845 -0.09049 -0.25744 0.32155  193 TYR D CD1 
2760 C CD2 . TYR B 173 ? 2.33937 2.25853 3.67039 -0.01416 -0.29334 0.29982  193 TYR D CD2 
2761 C CE1 . TYR B 173 ? 2.25852 2.11199 3.54856 -0.07998 -0.22346 0.31113  193 TYR D CE1 
2762 C CE2 . TYR B 173 ? 2.39632 2.20760 3.62474 -0.00390 -0.26236 0.29161  193 TYR D CE2 
2763 C CZ  . TYR B 173 ? 2.34931 2.13250 3.55753 -0.04050 -0.22574 0.29716  193 TYR D CZ  
2764 O OH  . TYR B 173 ? 2.38627 2.07111 3.48820 -0.03920 -0.19362 0.28865  193 TYR D OH  
2765 N N   . SER B 174 ? 2.07581 2.28549 3.72207 -0.18891 -0.35539 0.36819  194 SER D N   
2766 C CA  . SER B 174 ? 1.98839 2.23808 3.68956 -0.23300 -0.39510 0.38599  194 SER D CA  
2767 C C   . SER B 174 ? 2.04616 2.19070 3.70143 -0.22421 -0.42226 0.38046  194 SER D C   
2768 O O   . SER B 174 ? 2.08126 2.14099 3.68673 -0.20947 -0.39942 0.37186  194 SER D O   
2769 C CB  . SER B 174 ? 1.86658 2.16310 3.61600 -0.28387 -0.38061 0.40851  194 SER D CB  
2770 O OG  . SER B 174 ? 1.78574 2.20410 3.59311 -0.30819 -0.37124 0.41598  194 SER D OG  
2771 N N   . LEU B 175 ? 2.00652 2.16240 3.67705 -0.23550 -0.46991 0.38318  195 LEU D N   
2772 C CA  . LEU B 175 ? 2.08622 2.14485 3.70981 -0.22547 -0.50009 0.37425  195 LEU D CA  
2773 C C   . LEU B 175 ? 2.04684 2.10821 3.70365 -0.27375 -0.54383 0.39186  195 LEU D C   
2774 O O   . LEU B 175 ? 1.96780 2.12019 3.68172 -0.31700 -0.56257 0.41110  195 LEU D O   
2775 C CB  . LEU B 175 ? 2.17030 2.21645 3.75892 -0.18933 -0.52184 0.35818  195 LEU D CB  
2776 N N   . SER B 176 ? 2.18573 2.14338 3.79932 -0.26729 -0.56168 0.38309  196 SER D N   
2777 C CA  . SER B 176 ? 2.16081 2.08637 3.78684 -0.30748 -0.60675 0.39673  196 SER D CA  
2778 C C   . SER B 176 ? 2.26400 2.08505 3.82973 -0.28515 -0.63388 0.37605  196 SER D C   
2779 O O   . SER B 176 ? 2.31139 2.05369 3.83068 -0.24988 -0.61049 0.35421  196 SER D O   
2780 C CB  . SER B 176 ? 2.09574 1.99746 3.73958 -0.32551 -0.59459 0.40870  196 SER D CB  
2781 O OG  . SER B 176 ? 2.10974 1.97859 3.72697 -0.28616 -0.54545 0.39114  196 SER D OG  
2782 N N   . SER B 177 ? 2.32906 2.15693 3.89308 -0.30809 -0.68106 0.38095  197 SER D N   
2783 C CA  . SER B 177 ? 2.42529 2.15523 3.93119 -0.29569 -0.71261 0.36288  197 SER D CA  
2784 C C   . SER B 177 ? 2.41042 2.08606 3.91550 -0.33950 -0.76075 0.37550  197 SER D C   
2785 O O   . SER B 177 ? 2.35319 2.08996 3.89863 -0.39233 -0.78838 0.40240  197 SER D O   
2786 C CB  . SER B 177 ? 2.49476 2.26153 3.98658 -0.28719 -0.73373 0.35711  197 SER D CB  
2787 O OG  . SER B 177 ? 2.59330 2.26079 4.02024 -0.27210 -0.75783 0.33714  197 SER D OG  
2788 N N   . THR B 178 ? 2.53283 2.09105 3.98634 -0.31896 -0.77185 0.35444  198 THR D N   
2789 C CA  . THR B 178 ? 2.53277 2.01052 3.97248 -0.34962 -0.81789 0.36136  198 THR D CA  
2790 C C   . THR B 178 ? 2.61294 2.00026 3.99075 -0.34722 -0.85733 0.34173  198 THR D C   
2791 O O   . THR B 178 ? 2.64920 1.97432 3.97985 -0.30199 -0.83857 0.30896  198 THR D O   
2792 C CB  . THR B 178 ? 2.49888 1.91490 3.93719 -0.32267 -0.79768 0.35033  198 THR D CB  
2793 O OG1 . THR B 178 ? 2.43023 1.93298 3.92147 -0.32472 -0.75691 0.36750  198 THR D OG1 
2794 C CG2 . THR B 178 ? 2.52148 1.85236 3.94727 -0.35319 -0.85164 0.36132  198 THR D CG2 
2795 N N   . LEU B 179 ? 2.57335 1.95685 3.94710 -0.40157 -0.91127 0.36176  199 LEU D N   
2796 C CA  . LEU B 179 ? 2.65480 1.94218 3.96625 -0.41371 -0.95828 0.34807  199 LEU D CA  
2797 C C   . LEU B 179 ? 2.68963 1.84818 3.96705 -0.41835 -0.99006 0.34222  199 LEU D C   
2798 O O   . LEU B 179 ? 2.68811 1.83788 3.97879 -0.46870 -1.02574 0.37129  199 LEU D O   
2799 C CB  . LEU B 179 ? 2.66731 2.02017 3.98767 -0.47733 -1.00256 0.37382  199 LEU D CB  
2800 C CG  . LEU B 179 ? 2.75215 2.04610 4.01144 -0.48781 -1.04174 0.35913  199 LEU D CG  
2801 C CD1 . LEU B 179 ? 2.77179 2.09853 4.01963 -0.43483 -1.00809 0.33530  199 LEU D CD1 
2802 C CD2 . LEU B 179 ? 2.75646 2.11649 4.02565 -0.56467 -1.09129 0.38832  199 LEU D CD2 
2803 N N   . THR B 180 ? 2.80139 1.85803 4.03041 -0.36738 -0.98068 0.30360  200 THR D N   
2804 C CA  . THR B 180 ? 2.83214 1.76366 4.02877 -0.35714 -1.01060 0.29002  200 THR D CA  
2805 C C   . THR B 180 ? 2.92083 1.73683 4.04101 -0.36296 -1.05561 0.26674  200 THR D C   
2806 O O   . THR B 180 ? 2.94858 1.75764 4.03386 -0.33600 -1.03805 0.23811  200 THR D O   
2807 C CB  . THR B 180 ? 2.80028 1.71359 4.00626 -0.28983 -0.96283 0.25741  200 THR D CB  
2808 O OG1 . THR B 180 ? 2.72032 1.75202 3.98864 -0.28370 -0.91181 0.27534  200 THR D OG1 
2809 C CG2 . THR B 180 ? 2.83400 1.64564 4.02921 -0.27792 -0.99555 0.25084  200 THR D CG2 
2810 N N   . LEU B 181 ? 2.96976 1.68751 4.05621 -0.40059 -1.11539 0.27922  201 LEU D N   
2811 C CA  . LEU B 181 ? 3.06362 1.66238 4.07008 -0.41402 -1.16328 0.25908  201 LEU D CA  
2812 C C   . LEU B 181 ? 3.13328 1.59142 4.09926 -0.42790 -1.21952 0.26217  201 LEU D C   
2813 O O   . LEU B 181 ? 3.10821 1.57120 4.11076 -0.43077 -1.22291 0.28378  201 LEU D O   
2814 C CB  . LEU B 181 ? 3.08607 1.74395 4.08098 -0.48033 -1.19189 0.28568  201 LEU D CB  
2815 C CG  . LEU B 181 ? 3.08305 1.78266 4.09717 -0.56532 -1.23571 0.33654  201 LEU D CG  
2816 C CD1 . LEU B 181 ? 3.15318 1.82850 4.11202 -0.63142 -1.28891 0.34729  201 LEU D CD1 
2817 C CD2 . LEU B 181 ? 2.98435 1.85983 4.08691 -0.57953 -1.19516 0.36670  201 LEU D CD2 
2818 N N   . SER B 182 ? 3.21156 1.53700 4.09603 -0.43658 -1.26660 0.24052  202 SER D N   
2819 C CA  . SER B 182 ? 3.30011 1.47113 4.13124 -0.45128 -1.32909 0.24344  202 SER D CA  
2820 C C   . SER B 182 ? 3.33173 1.50641 4.14744 -0.55192 -1.38492 0.29909  202 SER D C   
2821 O O   . SER B 182 ? 3.30815 1.57778 4.13191 -0.60879 -1.38570 0.32191  202 SER D O   
2822 C CB  . SER B 182 ? 3.41058 1.42485 4.15130 -0.41989 -1.35925 0.19424  202 SER D CB  
2823 O OG  . SER B 182 ? 3.47081 1.46616 4.15498 -0.48194 -1.39331 0.20426  202 SER D OG  
2824 N N   . LYS B 183 ? 3.38711 1.49388 4.16869 -0.56430 -1.41998 0.31797  203 LYS D N   
2825 C CA  . LYS B 183 ? 3.44444 1.57275 4.18535 -0.65476 -1.46288 0.36773  203 LYS D CA  
2826 C C   . LYS B 183 ? 3.56764 1.62617 4.21629 -0.70183 -1.50524 0.36270  203 LYS D C   
2827 O O   . LYS B 183 ? 3.59370 1.70586 4.21648 -0.78715 -1.53232 0.40261  203 LYS D O   
2828 C CB  . LYS B 183 ? 3.53319 1.58661 4.23478 -0.65152 -1.49385 0.38493  203 LYS D CB  
2829 N N   . ALA B 184 ? 3.64666 1.59300 4.24284 -0.64876 -1.50911 0.31282  204 ALA D N   
2830 C CA  . ALA B 184 ? 3.76119 1.64136 4.26939 -0.69121 -1.54570 0.30439  204 ALA D CA  
2831 C C   . ALA B 184 ? 3.65934 1.67288 4.21631 -0.74488 -1.53186 0.32202  204 ALA D C   
2832 O O   . ALA B 184 ? 3.70540 1.75641 4.22444 -0.82702 -1.56460 0.35357  204 ALA D O   
2833 C CB  . ALA B 184 ? 3.85561 1.59986 4.30469 -0.61628 -1.54442 0.24178  204 ALA D CB  
2834 N N   . ASP B 185 ? 3.52650 1.61608 4.16568 -0.69925 -1.48479 0.30107  205 ASP D N   
2835 C CA  . ASP B 185 ? 3.45502 1.71118 4.13930 -0.73020 -1.45915 0.31661  205 ASP D CA  
2836 C C   . ASP B 185 ? 3.37610 1.78635 4.13500 -0.79069 -1.45453 0.36778  205 ASP D C   
2837 O O   . ASP B 185 ? 3.34214 1.89055 4.13174 -0.83558 -1.45098 0.38703  205 ASP D O   
2838 C CB  . ASP B 185 ? 3.39267 1.72711 4.12177 -0.64487 -1.38949 0.28054  205 ASP D CB  
2839 C CG  . ASP B 185 ? 3.45818 1.65294 4.11927 -0.58127 -1.38555 0.22508  205 ASP D CG  
2840 O OD1 . ASP B 185 ? 3.49125 1.56420 4.12737 -0.54423 -1.39717 0.20429  205 ASP D OD1 
2841 O OD2 . ASP B 185 ? 3.48081 1.69075 4.11315 -0.56762 -1.37204 0.20100  205 ASP D OD2 
2842 N N   . TYR B 186 ? 3.37457 1.76837 4.16346 -0.79105 -1.45503 0.38785  206 TYR D N   
2843 C CA  . TYR B 186 ? 3.31164 1.83647 4.15149 -0.85508 -1.45448 0.43624  206 TYR D CA  
2844 C C   . TYR B 186 ? 3.39789 1.87672 4.14041 -0.93137 -1.50585 0.46537  206 TYR D C   
2845 O O   . TYR B 186 ? 3.52703 1.85810 4.16917 -0.93081 -1.54427 0.44827  206 TYR D O   
2846 C CB  . TYR B 186 ? 3.25215 1.79154 4.14786 -0.81209 -1.42217 0.44361  206 TYR D CB  
2847 C CG  . TYR B 186 ? 3.16118 1.86963 4.12644 -0.86248 -1.40109 0.48621  206 TYR D CG  
2848 C CD1 . TYR B 186 ? 3.05507 1.93563 4.11711 -0.85594 -1.35437 0.48840  206 TYR D CD1 
2849 C CD2 . TYR B 186 ? 3.18490 1.88824 4.10669 -0.91072 -1.42356 0.52145  206 TYR D CD2 
2850 C CE1 . TYR B 186 ? 2.96526 2.00226 4.09189 -0.90213 -1.33535 0.52264  206 TYR D CE1 
2851 C CE2 . TYR B 186 ? 3.10005 1.96115 4.07532 -0.95620 -1.39940 0.55657  206 TYR D CE2 
2852 C CZ  . TYR B 186 ? 2.98571 2.01654 4.06369 -0.94956 -1.35279 0.55518  206 TYR D CZ  
2853 O OH  . TYR B 186 ? 2.89485 2.08695 4.02089 -0.98832 -1.32351 0.58409  206 TYR D OH  
2854 N N   . GLU B 187 ? 3.35571 1.96720 4.12321 -0.99912 -1.50397 0.50786  207 GLU D N   
2855 C CA  . GLU B 187 ? 3.46913 2.05316 4.14330 -1.07940 -1.54673 0.54075  207 GLU D CA  
2856 C C   . GLU B 187 ? 3.55598 2.13060 4.16519 -1.13139 -1.57923 0.53705  207 GLU D C   
2857 O O   . GLU B 187 ? 3.65594 2.23947 4.19266 -1.20947 -1.60978 0.56592  207 GLU D O   
2858 C CB  . GLU B 187 ? 3.61881 2.01437 4.19983 -1.05943 -1.58321 0.53975  207 GLU D CB  
2859 C CG  . GLU B 187 ? 3.56143 1.94579 4.19097 -1.00810 -1.56099 0.54297  207 GLU D CG  
2860 C CD  . GLU B 187 ? 3.67854 2.00407 4.23232 -1.05541 -1.59857 0.57897  207 GLU D CD  
2861 O OE1 . GLU B 187 ? 3.83414 1.98334 4.29578 -1.03397 -1.64294 0.56686  207 GLU D OE1 
2862 O OE2 . GLU B 187 ? 3.62431 2.07748 4.20516 -1.11277 -1.58458 0.61715  207 GLU D OE2 
2863 N N   . LYS B 188 ? 3.52183 2.08277 4.15343 -1.09199 -1.57216 0.50252  208 LYS D N   
2864 C CA  . LYS B 188 ? 3.58930 2.15705 4.16921 -1.13826 -1.60056 0.49719  208 LYS D CA  
2865 C C   . LYS B 188 ? 3.46252 2.25470 4.12943 -1.17915 -1.57992 0.51295  208 LYS D C   
2866 O O   . LYS B 188 ? 3.50438 2.34200 4.14062 -1.22431 -1.60221 0.51287  208 LYS D O   
2867 C CB  . LYS B 188 ? 3.62879 2.06607 4.17917 -1.07534 -1.60550 0.44959  208 LYS D CB  
2868 N N   . HIS B 189 ? 3.31413 2.25131 4.08813 -1.16052 -1.53751 0.52443  209 HIS D N   
2869 C CA  . HIS B 189 ? 3.18899 2.35161 4.05885 -1.18022 -1.51205 0.53266  209 HIS D CA  
2870 C C   . HIS B 189 ? 3.10905 2.40880 4.02781 -1.20760 -1.47978 0.56268  209 HIS D C   
2871 O O   . HIS B 189 ? 3.12008 2.34557 4.02709 -1.19151 -1.46966 0.57321  209 HIS D O   
2872 C CB  . HIS B 189 ? 3.13205 2.34216 4.09520 -1.10491 -1.48369 0.50233  209 HIS D CB  
2873 C CG  . HIS B 189 ? 3.22626 2.27695 4.11894 -1.04094 -1.48614 0.46490  209 HIS D CG  
2874 N ND1 . HIS B 189 ? 3.29485 2.14482 4.12419 -1.00353 -1.49520 0.44692  209 HIS D ND1 
2875 C CD2 . HIS B 189 ? 3.26380 2.32962 4.13653 -1.01049 -1.48303 0.44059  209 HIS D CD2 
2876 C CE1 . HIS B 189 ? 3.36102 2.11588 4.13670 -0.95305 -1.49319 0.41047  209 HIS D CE1 
2877 N NE2 . HIS B 189 ? 3.34787 2.22653 4.14545 -0.95931 -1.48642 0.40795  209 HIS D NE2 
2878 N N   . LYS B 190 ? 3.04484 2.55109 4.01681 -1.24644 -1.46282 0.57335  210 LYS D N   
2879 C CA  . LYS B 190 ? 2.97490 2.63551 3.99034 -1.27625 -1.42649 0.59562  210 LYS D CA  
2880 C C   . LYS B 190 ? 2.79717 2.62970 3.94328 -1.22198 -1.37708 0.58258  210 LYS D C   
2881 O O   . LYS B 190 ? 2.72523 2.58976 3.91650 -1.19789 -1.33995 0.58954  210 LYS D O   
2882 C CB  . LYS B 190 ? 3.04598 2.82191 4.01559 -1.36313 -1.43873 0.61269  210 LYS D CB  
2883 N N   . VAL B 191 ? 2.06154 3.17878 5.00975 -1.03825 -0.84623 0.38964  211 VAL D N   
2884 C CA  . VAL B 191 ? 2.04149 3.14798 5.03176 -0.96037 -0.94353 0.46127  211 VAL D CA  
2885 C C   . VAL B 191 ? 2.02573 3.17024 4.86754 -0.92994 -1.03363 0.60915  211 VAL D C   
2886 O O   . VAL B 191 ? 2.07884 3.31883 4.81832 -0.96842 -1.10157 0.65852  211 VAL D O   
2887 C CB  . VAL B 191 ? 2.11528 3.29254 5.21204 -0.97091 -1.02635 0.41390  211 VAL D CB  
2888 C CG1 . VAL B 191 ? 2.11511 3.27691 5.21944 -0.90179 -1.12828 0.51058  211 VAL D CG1 
2889 C CG2 . VAL B 191 ? 2.13115 3.25262 5.37777 -0.98739 -0.93454 0.27717  211 VAL D CG2 
2890 N N   . TYR B 192 ? 1.96114 3.02493 4.78765 -0.85970 -1.02935 0.67765  212 TYR D N   
2891 C CA  . TYR B 192 ? 1.95527 3.03047 4.65365 -0.82491 -1.10335 0.81276  212 TYR D CA  
2892 C C   . TYR B 192 ? 1.95478 2.95851 4.72848 -0.76065 -1.15220 0.84602  212 TYR D C   
2893 O O   . TYR B 192 ? 1.88935 2.80122 4.71849 -0.70741 -1.10331 0.83289  212 TYR D O   
2894 C CB  . TYR B 192 ? 1.87979 2.92670 4.47445 -0.80903 -1.03818 0.86172  212 TYR D CB  
2895 C CG  . TYR B 192 ? 1.88534 2.99398 4.37704 -0.87907 -0.98182 0.84992  212 TYR D CG  
2896 C CD1 . TYR B 192 ? 1.94609 3.15214 4.29261 -0.92435 -1.04931 0.92042  212 TYR D CD1 
2897 C CD2 . TYR B 192 ? 1.89097 2.94085 4.42013 -0.90230 -0.84563 0.77203  212 TYR D CD2 
2898 C CE1 . TYR B 192 ? 2.00919 3.26988 4.24098 -0.99467 -0.99536 0.91540  212 TYR D CE1 
2899 C CE2 . TYR B 192 ? 1.96299 3.04484 4.38040 -0.97767 -0.77137 0.76655  212 TYR D CE2 
2900 C CZ  . TYR B 192 ? 2.01834 3.21666 4.28238 -1.02708 -0.85328 0.83890  212 TYR D CZ  
2901 O OH  . TYR B 192 ? 2.20477 3.37994 4.23833 -1.06266 -0.74523 0.81125  212 TYR D OH  
2902 N N   . ALA B 193 ? 2.03240 3.07248 4.80862 -0.76639 -1.24343 0.88955  213 ALA D N   
2903 C CA  . ALA B 193 ? 2.04949 3.02025 4.89634 -0.72075 -1.28692 0.92254  213 ALA D CA  
2904 C C   . ALA B 193 ? 2.06798 3.01075 4.80579 -0.70429 -1.32985 1.04603  213 ALA D C   
2905 O O   . ALA B 193 ? 2.10440 3.10834 4.72113 -0.73577 -1.35655 1.11111  213 ALA D O   
2906 C CB  . ALA B 193 ? 2.13133 3.15625 5.07700 -0.74217 -1.34864 0.88038  213 ALA D CB  
2907 N N   . CYS B 194 ? 2.10095 2.94606 4.88384 -0.65933 -1.32962 1.07524  214 CYS D N   
2908 C CA  . CYS B 194 ? 2.12109 2.92898 4.82425 -0.65271 -1.35526 1.17849  214 CYS D CA  
2909 C C   . CYS B 194 ? 2.16614 2.90955 4.96184 -0.63623 -1.39801 1.20095  214 CYS D C   
2910 O O   . CYS B 194 ? 2.12366 2.77894 5.00217 -0.59645 -1.37079 1.16426  214 CYS D O   
2911 C CB  . CYS B 194 ? 2.03623 2.78864 4.67621 -0.62058 -1.29239 1.19382  214 CYS D CB  
2912 S SG  . CYS B 194 ? 2.02782 2.67847 4.67179 -0.59031 -1.29256 1.25585  214 CYS D SG  
2913 N N   . GLU B 195 ? 2.20104 2.98878 4.97444 -0.66806 -1.46290 1.26796  215 GLU D N   
2914 C CA  . GLU B 195 ? 2.25912 3.00109 5.12375 -0.66179 -1.51140 1.29700  215 GLU D CA  
2915 C C   . GLU B 195 ? 2.27399 2.96130 5.09834 -0.66680 -1.51593 1.39139  215 GLU D C   
2916 O O   . GLU B 195 ? 2.26800 2.98659 4.98563 -0.68696 -1.50055 1.44475  215 GLU D O   
2917 C CB  . GLU B 195 ? 2.35724 3.19682 5.24674 -0.69407 -1.58443 1.30199  215 GLU D CB  
2918 C CG  . GLU B 195 ? 2.42402 3.23510 5.42577 -0.68769 -1.63995 1.31754  215 GLU D CG  
2919 C CD  . GLU B 195 ? 2.49030 3.40044 5.56115 -0.69988 -1.69472 1.25852  215 GLU D CD  
2920 O OE1 . GLU B 195 ? 2.47979 3.47350 5.52607 -0.71575 -1.68451 1.19510  215 GLU D OE1 
2921 O OE2 . GLU B 195 ? 2.56986 3.46901 5.74076 -0.70068 -1.75766 1.28625  215 GLU D OE2 
2922 N N   . VAL B 196 ? 2.31469 2.91617 5.25077 -0.66049 -1.54714 1.42782  216 VAL D N   
2923 C CA  . VAL B 196 ? 2.34942 2.89031 5.29919 -0.67805 -1.56167 1.52436  216 VAL D CA  
2924 C C   . VAL B 196 ? 2.46018 3.00406 5.50400 -0.70529 -1.63989 1.58700  216 VAL D C   
2925 O O   . VAL B 196 ? 2.49088 3.00766 5.64220 -0.69122 -1.67213 1.55128  216 VAL D O   
2926 C CB  . VAL B 196 ? 2.28785 2.70938 5.29335 -0.64491 -1.51824 1.50837  216 VAL D CB  
2927 C CG1 . VAL B 196 ? 2.18503 2.61932 5.08341 -0.62004 -1.44316 1.46084  216 VAL D CG1 
2928 C CG2 . VAL B 196 ? 2.28209 2.63308 5.40895 -0.61133 -1.52452 1.44441  216 VAL D CG2 
2929 N N   . THR B 197 ? 2.52040 3.10333 5.52735 -0.74332 -1.66878 1.67830  217 THR D N   
2930 C CA  . THR B 197 ? 2.62729 3.22520 5.71901 -0.76857 -1.74191 1.74218  217 THR D CA  
2931 C C   . THR B 197 ? 2.64363 3.12612 5.86733 -0.76580 -1.75320 1.77709  217 THR D C   
2932 O O   . THR B 197 ? 2.64449 3.08500 5.88179 -0.78592 -1.74054 1.84476  217 THR D O   
2933 C CB  . THR B 197 ? 2.68398 3.36077 5.70071 -0.80812 -1.76276 1.83009  217 THR D CB  
2934 O OG1 . THR B 197 ? 2.67019 3.44773 5.55665 -0.80960 -1.75075 1.79666  217 THR D OG1 
2935 C CG2 . THR B 197 ? 2.79857 3.50981 5.89758 -0.82797 -1.84036 1.89029  217 THR D CG2 
2936 N N   . GLN B 198 ? 2.65703 3.09152 5.98484 -0.74168 -1.77641 1.72680  218 GLN D N   
2937 C CA  . GLN B 198 ? 2.67995 3.00136 6.14151 -0.73633 -1.79292 1.75036  218 GLN D CA  
2938 C C   . GLN B 198 ? 2.77340 3.12590 6.33273 -0.74243 -1.86679 1.75661  218 GLN D C   
2939 O O   . GLN B 198 ? 2.77078 3.14098 6.36713 -0.71665 -1.87856 1.67952  218 GLN D O   
2940 C CB  . GLN B 198 ? 2.59677 2.81283 6.09460 -0.69217 -1.74080 1.67508  218 GLN D CB  
2941 C CG  . GLN B 198 ? 2.49804 2.71955 5.88223 -0.67322 -1.66815 1.63575  218 GLN D CG  
2942 C CD  . GLN B 198 ? 2.48522 2.68411 5.83310 -0.69549 -1.64511 1.70432  218 GLN D CD  
2943 O OE1 . GLN B 198 ? 2.45248 2.71960 5.68604 -0.70741 -1.61514 1.71711  218 GLN D OE1 
2944 N NE2 . GLN B 198 ? 2.51176 2.61809 5.96385 -0.70202 -1.65870 1.74570  218 GLN D NE2 
2945 N N   . GLY B 199 ? 2.85561 3.22656 6.46051 -0.77547 -1.91551 1.84386  219 GLY D N   
2946 C CA  . GLY B 199 ? 2.95131 3.35981 6.64963 -0.77871 -1.98970 1.85528  219 GLY D CA  
2947 C C   . GLY B 199 ? 2.94890 3.27287 6.76890 -0.74948 -2.00091 1.79617  219 GLY D C   
2948 O O   . GLY B 199 ? 3.01813 3.39237 6.90690 -0.74242 -2.05959 1.77548  219 GLY D O   
2949 N N   . THR B 200 ? 2.87269 3.07294 6.72083 -0.72826 -1.94627 1.76494  220 THR D N   
2950 C CA  . THR B 200 ? 2.86359 2.97412 6.82291 -0.69544 -1.94860 1.70422  220 THR D CA  
2951 C C   . THR B 200 ? 2.81093 2.96409 6.74255 -0.65910 -1.92299 1.59603  220 THR D C   
2952 O O   . THR B 200 ? 2.85321 3.05310 6.85493 -0.64751 -1.96290 1.54664  220 THR D O   
2953 C CB  . THR B 200 ? 2.81330 2.77228 6.82136 -0.68488 -1.90452 1.71754  220 THR D CB  
2954 O OG1 . THR B 200 ? 2.80111 2.66621 6.91133 -0.64850 -1.90178 1.65506  220 THR D OG1 
2955 C CG2 . THR B 200 ? 2.71968 2.66199 6.61763 -0.67388 -1.83246 1.70107  220 THR D CG2 
2956 N N   . THR B 201 ? 2.71827 2.86480 6.55546 -0.64133 -1.85528 1.55385  221 THR D N   
2957 C CA  . THR B 201 ? 2.65730 2.85322 6.46528 -0.61084 -1.81928 1.45010  221 THR D CA  
2958 C C   . THR B 201 ? 2.59739 2.86446 6.25417 -0.62047 -1.77311 1.44925  221 THR D C   
2959 O O   . THR B 201 ? 2.53405 2.73649 6.13526 -0.61193 -1.72105 1.46652  221 THR D O   
2960 C CB  . THR B 201 ? 2.58890 2.66798 6.46783 -0.56373 -1.76939 1.38015  221 THR D CB  
2961 O OG1 . THR B 201 ? 2.49870 2.52673 6.29178 -0.54613 -1.69886 1.37241  221 THR D OG1 
2962 C CG2 . THR B 201 ? 2.63668 2.59293 6.64808 -0.55711 -1.80116 1.41301  221 THR D CG2 
2963 N N   . SER B 202 ? 2.61727 3.02043 6.20953 -0.63701 -1.79180 1.42268  222 SER D N   
2964 C CA  . SER B 202 ? 2.57423 3.05434 6.01817 -0.65224 -1.75651 1.43059  222 SER D CA  
2965 C C   . SER B 202 ? 2.47542 2.97388 5.87825 -0.62409 -1.68774 1.32654  222 SER D C   
2966 O O   . SER B 202 ? 2.46792 3.07749 5.83012 -0.63308 -1.68451 1.26403  222 SER D O   
2967 C CB  . SER B 202 ? 2.65498 3.27044 6.04738 -0.68584 -1.81511 1.46157  222 SER D CB  
2968 O OG  . SER B 202 ? 2.61274 3.31016 5.86558 -0.69722 -1.78054 1.44915  222 SER D OG  
2969 N N   . VAL B 203 ? 2.39951 2.78743 5.81920 -0.59006 -1.63008 1.30532  225 VAL D N   
2970 C CA  . VAL B 203 ? 2.30335 2.68729 5.71203 -0.55513 -1.55894 1.20435  225 VAL D CA  
2971 C C   . VAL B 203 ? 2.24095 2.71752 5.50399 -0.56671 -1.51070 1.18027  225 VAL D C   
2972 O O   . VAL B 203 ? 2.25638 2.77005 5.41631 -0.59256 -1.52058 1.24923  225 VAL D O   
2973 C CB  . VAL B 203 ? 2.24388 2.48591 5.70206 -0.51116 -1.51258 1.19276  225 VAL D CB  
2974 C CG1 . VAL B 203 ? 2.28924 2.44703 5.90276 -0.49163 -1.54604 1.17745  225 VAL D CG1 
2975 C CG2 . VAL B 203 ? 2.24555 2.42768 5.64921 -0.52236 -1.51102 1.27875  225 VAL D CG2 
2976 N N   . THR B 204 ? 2.22144 2.73456 5.48280 -0.54925 -1.45307 1.07848  226 THR D N   
2977 C CA  . THR B 204 ? 2.17532 2.77419 5.33690 -0.56675 -1.41229 1.04633  226 THR D CA  
2978 C C   . THR B 204 ? 2.08728 2.64052 5.28833 -0.53295 -1.33334 0.96436  226 THR D C   
2979 O O   . THR B 204 ? 2.07153 2.56474 5.38487 -0.50260 -1.31327 0.90529  226 THR D O   
2980 C CB  . THR B 204 ? 2.24128 2.96903 5.41139 -0.61215 -1.45660 1.01688  226 THR D CB  
2981 O OG1 . THR B 204 ? 2.33279 3.09409 5.50251 -0.63263 -1.53506 1.08498  226 THR D OG1 
2982 C CG2 . THR B 204 ? 2.22206 3.03204 5.28323 -0.64378 -1.43385 1.01601  226 THR D CG2 
2983 N N   . LYS B 205 ? 2.04020 2.61866 5.15224 -0.53648 -1.28637 0.96446  227 LYS D N   
2984 C CA  . LYS B 205 ? 1.95946 2.50484 5.11026 -0.50777 -1.20509 0.88856  227 LYS D CA  
2985 C C   . LYS B 205 ? 1.94444 2.58629 5.03072 -0.54983 -1.17166 0.85942  227 LYS D C   
2986 O O   . LYS B 205 ? 1.96937 2.67893 4.93780 -0.58357 -1.20284 0.92268  227 LYS D O   
2987 C CB  . LYS B 205 ? 1.89087 2.33912 5.01000 -0.45604 -1.16398 0.91581  227 LYS D CB  
2988 N N   . SER B 206 ? 1.84847 2.48750 5.01381 -0.55101 -1.09920 0.76261  228 SER D N   
2989 C CA  . SER B 206 ? 1.84645 2.56791 4.96704 -0.60622 -1.05426 0.71857  228 SER D CA  
2990 C C   . SER B 206 ? 1.77718 2.43482 4.95425 -0.58626 -0.93343 0.63901  228 SER D C   
2991 O O   . SER B 206 ? 1.73272 2.29045 4.99610 -0.52301 -0.89210 0.61331  228 SER D O   
2992 C CB  . SER B 206 ? 1.92498 2.73348 5.09746 -0.66663 -1.08743 0.66025  228 SER D CB  
2993 O OG  . SER B 206 ? 1.93228 2.81148 5.05712 -0.72948 -1.03904 0.61216  228 SER D OG  
2994 N N   . PHE B 207 ? 1.77772 2.48332 4.90619 -0.64250 -0.86773 0.59847  229 PHE D N   
2995 C CA  . PHE B 207 ? 1.73682 2.36455 4.90428 -0.63871 -0.72201 0.51828  229 PHE D CA  
2996 C C   . PHE B 207 ? 1.79406 2.46467 4.92949 -0.72974 -0.65357 0.44618  229 PHE D C   
2997 O O   . PHE B 207 ? 1.84630 2.63051 4.92360 -0.79002 -0.73586 0.47042  229 PHE D O   
2998 C CB  . PHE B 207 ? 1.65900 2.25413 4.74956 -0.59442 -0.67991 0.58176  229 PHE D CB  
2999 N N   . ASN B 208 ? 1.79931 2.35853 4.96815 -0.73550 -0.48838 0.35133  230 ASN D N   
3000 C CA  . ASN B 208 ? 1.87173 2.42382 5.00256 -0.82044 -0.38353 0.26583  230 ASN D CA  
3001 C C   . ASN B 208 ? 1.86211 2.31271 4.87641 -0.82263 -0.22249 0.27032  230 ASN D C   
3002 O O   . ASN B 208 ? 1.85073 2.13942 4.85829 -0.74583 -0.08279 0.23829  230 ASN D O   
3003 C CB  . ASN B 208 ? 1.93758 2.40426 5.19158 -0.82415 -0.29078 0.12919  230 ASN D CB  
3004 C CG  . ASN B 208 ? 2.00631 2.60289 5.31339 -0.89481 -0.39179 0.09037  230 ASN D CG  
3005 O OD1 . ASN B 208 ? 2.01768 2.75551 5.25445 -0.94623 -0.50681 0.15094  230 ASN D OD1 
3006 N ND2 . ASN B 208 ? 2.05798 2.60913 5.48963 -0.88998 -0.34926 -0.00906 230 ASN D ND2 
3007 N N   . ARG B 209 ? 1.90483 2.42765 4.74693 -0.88202 -0.22693 0.30801  231 ARG D N   
3008 C CA  . ARG B 209 ? 2.00177 2.38824 4.49145 -0.81963 -0.04757 0.29703  231 ARG D CA  
3009 C C   . ARG B 209 ? 2.10051 2.26816 4.53399 -0.78119 0.19583  0.15638  231 ARG D C   
3010 O O   . ARG B 209 ? 2.20096 2.19983 4.42586 -0.67561 0.35530  0.14405  231 ARG D O   
3011 C CB  . ARG B 209 ? 2.15338 2.63981 4.44012 -0.89032 -0.07726 0.32785  231 ARG D CB  
3012 C CG  . ARG B 209 ? 2.11426 2.76144 4.30567 -0.89867 -0.24828 0.47709  231 ARG D CG  
3013 C CD  . ARG B 209 ? 2.32693 2.97945 4.20336 -0.92404 -0.17945 0.48822  231 ARG D CD  
3014 N NE  . ARG B 209 ? 2.45892 3.05618 4.32234 -0.98789 -0.06233 0.35967  231 ARG D NE  
3015 C CZ  . ARG B 209 ? 2.65191 3.07711 4.29351 -0.95506 0.15833  0.27292  231 ARG D CZ  
3016 N NH1 . ARG B 209 ? 2.74333 3.02956 4.14440 -0.85006 0.28968  0.29773  231 ARG D NH1 
3017 N NH2 . ARG B 209 ? 2.70238 3.09330 4.36708 -1.02576 0.25240  0.15362  231 ARG D NH2 
3018 N N   . GLY B 210 ? 2.18447 2.35148 4.80814 -0.86168 0.22921  0.04605  232 GLY D N   
3019 C CA  . GLY B 210 ? 2.25665 2.21503 4.85723 -0.83842 0.46714  -0.09503 232 GLY D CA  
3020 C C   . GLY B 210 ? 2.21479 2.00716 4.89460 -0.73146 0.56316  -0.11962 232 GLY D C   
3021 O O   . GLY B 210 ? 2.32040 1.89570 4.88670 -0.67100 0.79290  -0.21220 232 GLY D O   
3022 N N   . GLU B 211 ? 2.24020 2.12616 5.12790 -0.70882 0.39489  -0.04459 233 GLU D N   
3023 C CA  . GLU B 211 ? 2.16369 1.91349 5.13288 -0.60159 0.45550  -0.05373 233 GLU D CA  
3024 C C   . GLU B 211 ? 2.17096 1.89320 4.91502 -0.48576 0.44260  0.04681  233 GLU D C   
3025 O O   . GLU B 211 ? 2.20719 2.06462 4.81742 -0.50412 0.32529  0.14639  233 GLU D O   
3026 C CB  . GLU B 211 ? 2.02381 1.89957 5.23151 -0.59499 0.27006  -0.04173 233 GLU D CB  
3027 N N   . CYS B 212 ? 2.37879 1.92164 5.07944 -0.36198 0.57100  0.01376  234 CYS D N   
3028 C CA  . CYS B 212 ? 2.38968 1.89099 4.88704 -0.23368 0.57642  0.08552  234 CYS D CA  
3029 C C   . CYS B 212 ? 2.30755 1.67051 4.92052 -0.11882 0.63430  0.05126  234 CYS D C   
3030 O O   . CYS B 212 ? 2.39200 1.54007 4.82629 -0.00647 0.84062  -0.01612 234 CYS D O   
3031 C CB  . CYS B 212 ? 2.61912 1.99491 4.72115 -0.16611 0.75832  0.06798  234 CYS D CB  
3032 S SG  . CYS B 212 ? 2.72788 1.83094 4.68570 -0.13518 1.06921  -0.08141 234 CYS D SG  
3033 N N   . HIS C 11  ? 2.24780 3.42526 1.73816 0.06716  0.12414  0.03216  11  HIS E N   
3034 C CA  . HIS C 11  ? 2.29648 3.33619 1.76951 0.11618  0.20180  0.03054  11  HIS E CA  
3035 C C   . HIS C 11  ? 2.29358 3.28195 1.61165 0.07711  0.17803  0.07943  11  HIS E C   
3036 O O   . HIS C 11  ? 2.34085 3.32503 1.61185 0.02160  0.09227  0.12531  11  HIS E O   
3037 C CB  . HIS C 11  ? 2.43750 3.34850 2.06472 0.16111  0.23158  0.02279  11  HIS E CB  
3038 C CG  . HIS C 11  ? 2.43437 3.24012 2.07807 0.21214  0.33235  -0.00515 11  HIS E CG  
3039 N ND1 . HIS C 11  ? 2.37956 3.14502 1.88948 0.20963  0.37688  0.00220  11  HIS E ND1 
3040 C CD2 . HIS C 11  ? 2.47107 3.20403 2.24239 0.25600  0.39530  -0.04131 11  HIS E CD2 
3041 C CE1 . HIS C 11  ? 2.40026 3.06422 1.95121 0.24431  0.46045  -0.02603 11  HIS E CE1 
3042 N NE2 . HIS C 11  ? 2.45069 3.10119 2.15721 0.27017  0.47429  -0.05501 11  HIS E NE2 
3043 N N   . HIS C 12  ? 2.46694 3.40686 1.69845 0.10174  0.24675  0.07188  12  HIS E N   
3044 C CA  . HIS C 12  ? 2.45878 3.32973 1.53993 0.07462  0.23924  0.12108  12  HIS E CA  
3045 C C   . HIS C 12  ? 2.42642 3.19667 1.47223 0.11878  0.33730  0.10227  12  HIS E C   
3046 O O   . HIS C 12  ? 2.37726 3.17132 1.47208 0.15249  0.38915  0.04983  12  HIS E O   
3047 C CB  . HIS C 12  ? 2.33182 3.34647 1.26003 0.00510  0.17168  0.14270  12  HIS E CB  
3048 C CG  . HIS C 12  ? 2.28001 3.24318 1.03340 -0.01772 0.17869  0.18606  12  HIS E CG  
3049 N ND1 . HIS C 12  ? 2.14453 3.06244 0.90341 -0.01763 0.19636  0.14658  12  HIS E ND1 
3050 C CD2 . HIS C 12  ? 2.35222 3.18576 1.02599 -0.03790 0.14801  0.24918  12  HIS E CD2 
3051 C CE1 . HIS C 12  ? 2.14848 2.91390 0.83322 -0.03543 0.18558  0.18277  12  HIS E CE1 
3052 N NE2 . HIS C 12  ? 2.24853 2.95478 0.88153 -0.04670 0.15806  0.24248  12  HIS E NE2 
3053 N N   . GLU C 13  ? 2.37153 3.01875 1.32590 0.11329  0.35416  0.14708  13  GLU E N   
3054 C CA  . GLU C 13  ? 2.34916 2.87635 1.26146 0.14222  0.44522  0.13723  13  GLU E CA  
3055 C C   . GLU C 13  ? 2.28103 2.77133 1.00471 0.11191  0.43779  0.19038  13  GLU E C   
3056 O O   . GLU C 13  ? 2.30710 2.78643 0.95850 0.07393  0.36784  0.24493  13  GLU E O   
3057 C CB  . GLU C 13  ? 2.47024 2.85198 1.49157 0.17407  0.49982  0.12938  13  GLU E CB  
3058 N N   . VAL C 14  ? 2.36630 2.75816 1.08648 0.09864  0.47195  0.15496  14  VAL E N   
3059 C CA  . VAL C 14  ? 2.28378 2.54638 0.93220 0.04028  0.44322  0.17102  14  VAL E CA  
3060 C C   . VAL C 14  ? 2.25505 2.42531 0.93991 0.03213  0.50098  0.15653  14  VAL E C   
3061 O O   . VAL C 14  ? 2.28423 2.45615 1.03160 0.07056  0.55680  0.11741  14  VAL E O   
3062 C CB  . VAL C 14  ? 2.23515 2.52938 0.86718 0.02109  0.39371  0.13852  14  VAL E CB  
3063 C CG1 . VAL C 14  ? 2.23195 2.63492 0.84911 0.00492  0.31202  0.16125  14  VAL E CG1 
3064 C CG2 . VAL C 14  ? 2.19279 2.57980 0.89918 0.05566  0.41930  0.07476  14  VAL E CG2 
3065 N N   . VAL C 15  ? 2.22711 2.33993 0.89373 -0.01366 0.47322  0.19079  15  VAL E N   
3066 C CA  . VAL C 15  ? 2.16874 2.23438 0.89740 -0.00463 0.49886  0.19034  15  VAL E CA  
3067 C C   . VAL C 15  ? 2.07931 2.19967 0.81669 -0.06322 0.43873  0.18443  15  VAL E C   
3068 O O   . VAL C 15  ? 2.07849 2.19920 0.80197 -0.11059 0.37787  0.20744  15  VAL E O   
3069 C CB  . VAL C 15  ? 2.20751 2.15694 0.93981 0.01898  0.52482  0.23610  15  VAL E CB  
3070 C CG1 . VAL C 15  ? 2.18452 2.02136 0.96384 0.02934  0.56688  0.22281  15  VAL E CG1 
3071 C CG2 . VAL C 15  ? 2.33983 2.24426 1.05372 0.07051  0.58180  0.24238  15  VAL E CG2 
3072 N N   . LYS C 16  ? 2.18119 2.31213 0.95353 -0.04837 0.45250  0.14970  16  LYS E N   
3073 C CA  . LYS C 16  ? 2.15572 2.30161 0.93008 -0.06324 0.41353  0.14690  16  LYS E CA  
3074 C C   . LYS C 16  ? 2.18804 2.23247 0.94294 -0.04547 0.41463  0.20741  16  LYS E C   
3075 O O   . LYS C 16  ? 2.21738 2.13525 0.98668 -0.02216 0.44836  0.22915  16  LYS E O   
3076 C CB  . LYS C 16  ? 2.13034 2.27473 0.92213 -0.03771 0.43072  0.10072  16  LYS E CB  
3077 N N   . PHE C 17  ? 1.56130 1.70828 1.64088 -0.54108 0.41855  -0.22352 17  PHE E N   
3078 C CA  . PHE C 17  ? 1.63630 1.72090 1.74361 -0.52098 0.39546  -0.22924 17  PHE E CA  
3079 C C   . PHE C 17  ? 1.73914 1.73474 1.82833 -0.43413 0.33472  -0.23826 17  PHE E C   
3080 O O   . PHE C 17  ? 1.78730 1.70309 1.83487 -0.40212 0.31300  -0.19576 17  PHE E O   
3081 C CB  . PHE C 17  ? 1.63445 1.78798 1.86110 -0.56300 0.41269  -0.31712 17  PHE E CB  
3082 C CG  . PHE C 17  ? 1.68884 1.79106 1.96024 -0.55249 0.39532  -0.33392 17  PHE E CG  
3083 C CD1 . PHE C 17  ? 1.71151 1.77574 2.03262 -0.47960 0.33329  -0.39286 17  PHE E CD1 
3084 C CD2 . PHE C 17  ? 1.66560 1.74842 1.92121 -0.61204 0.43954  -0.29154 17  PHE E CD2 
3085 C CE1 . PHE C 17  ? 1.71788 1.74340 2.08727 -0.46777 0.31449  -0.41651 17  PHE E CE1 
3086 C CE2 . PHE C 17  ? 1.71572 1.74939 2.02037 -0.60531 0.42593  -0.31238 17  PHE E CE2 
3087 C CZ  . PHE C 17  ? 1.74510 1.75859 2.11424 -0.53346 0.36245  -0.37859 17  PHE E CZ  
3088 N N   . MET C 18  ? 1.83549 1.83567 1.94938 -0.39270 0.30620  -0.29595 18  MET E N   
3089 C CA  . MET C 18  ? 1.84949 1.74500 1.91637 -0.30681 0.25143  -0.29858 18  MET E CA  
3090 C C   . MET C 18  ? 1.93251 1.75052 1.88363 -0.28757 0.25762  -0.20673 18  MET E C   
3091 O O   . MET C 18  ? 1.96710 1.69385 1.86840 -0.23509 0.22611  -0.18184 18  MET E O   
3092 C CB  . MET C 18  ? 1.74548 1.63907 1.83053 -0.26576 0.22452  -0.36463 18  MET E CB  
3093 C CG  . MET C 18  ? 1.62315 1.61769 1.83545 -0.28723 0.22073  -0.46710 18  MET E CG  
3094 S SD  . MET C 18  ? 1.52842 1.50111 1.82371 -0.22865 0.15840  -0.55205 18  MET E SD  
3095 C CE  . MET C 18  ? 1.55210 1.35553 1.71638 -0.11568 0.09318  -0.51721 18  MET E CE  
3096 N N   . ASP C 19  ? 1.92223 1.78550 1.83542 -0.33054 0.29872  -0.16224 19  ASP E N   
3097 C CA  . ASP C 19  ? 1.87680 1.68984 1.69765 -0.31745 0.30824  -0.08775 19  ASP E CA  
3098 C C   . ASP C 19  ? 1.83634 1.62288 1.63104 -0.32246 0.30728  -0.03198 19  ASP E C   
3099 O O   . ASP C 19  ? 1.85869 1.56947 1.59357 -0.28062 0.28989  0.00687  19  ASP E O   
3100 C CB  . ASP C 19  ? 1.74436 1.63215 1.54855 -0.36202 0.34854  -0.06917 19  ASP E CB  
3101 C CG  . ASP C 19  ? 1.78656 1.66464 1.59035 -0.34530 0.34931  -0.10952 19  ASP E CG  
3102 O OD1 . ASP C 19  ? 1.90107 1.69224 1.69195 -0.29115 0.31688  -0.13921 19  ASP E OD1 
3103 O OD2 . ASP C 19  ? 1.69473 1.64663 1.50573 -0.38406 0.38107  -0.11308 19  ASP E OD2 
3104 N N   . VAL C 20  ? 1.76147 1.60340 1.59367 -0.37506 0.32985  -0.02696 20  VAL E N   
3105 C CA  . VAL C 20  ? 1.74474 1.54443 1.54871 -0.37966 0.32875  0.02489  20  VAL E CA  
3106 C C   . VAL C 20  ? 1.86990 1.58904 1.69134 -0.32620 0.28646  0.00437  20  VAL E C   
3107 O O   . VAL C 20  ? 1.88115 1.53246 1.64980 -0.28986 0.26771  0.04863  20  VAL E O   
3108 C CB  . VAL C 20  ? 1.70206 1.55232 1.53879 -0.44854 0.36583  0.02515  20  VAL E CB  
3109 C CG1 . VAL C 20  ? 1.71719 1.50088 1.51204 -0.45143 0.36540  0.08315  20  VAL E CG1 
3110 C CG2 . VAL C 20  ? 1.61490 1.54800 1.42664 -0.49803 0.40564  0.03891  20  VAL E CG2 
3111 N N   . TYR C 21  ? 1.75391 1.48686 1.65376 -0.31695 0.26785  -0.07126 21  TYR E N   
3112 C CA  . TYR C 21  ? 1.83086 1.49937 1.75597 -0.26146 0.22131  -0.10680 21  TYR E CA  
3113 C C   . TYR C 21  ? 1.86673 1.44574 1.70455 -0.18743 0.18706  -0.08007 21  TYR E C   
3114 O O   . TYR C 21  ? 1.88857 1.40005 1.69456 -0.14913 0.16230  -0.05722 21  TYR E O   
3115 C CB  . TYR C 21  ? 1.78258 1.49890 1.80951 -0.25589 0.20170  -0.20725 21  TYR E CB  
3116 C CG  . TYR C 21  ? 1.73351 1.41618 1.82007 -0.21470 0.15759  -0.26324 21  TYR E CG  
3117 C CD1 . TYR C 21  ? 1.72348 1.31335 1.74937 -0.13249 0.10584  -0.25648 21  TYR E CD1 
3118 C CD2 . TYR C 21  ? 1.68628 1.43170 1.88951 -0.26086 0.17167  -0.32676 21  TYR E CD2 
3119 C CE1 . TYR C 21  ? 1.65757 1.22277 1.73772 -0.08976 0.06069  -0.31362 21  TYR E CE1 
3120 C CE2 . TYR C 21  ? 1.61971 1.34449 1.89123 -0.22372 0.13037  -0.38898 21  TYR E CE2 
3121 C CZ  . TYR C 21  ? 1.60013 1.23704 1.80966 -0.13457 0.07081  -0.38273 21  TYR E CZ  
3122 O OH  . TYR C 21  ? 1.51402 1.13574 1.79044 -0.09186 0.02450  -0.45042 21  TYR E OH  
3123 N N   . GLN C 22  ? 1.94077 1.51332 1.73517 -0.16978 0.19037  -0.08344 22  GLN E N   
3124 C CA  . GLN C 22  ? 1.96327 1.43668 1.66473 -0.10470 0.16770  -0.06262 22  GLN E CA  
3125 C C   . GLN C 22  ? 1.95389 1.40243 1.58418 -0.11115 0.19026  0.01339  22  GLN E C   
3126 O O   . GLN C 22  ? 1.97269 1.34322 1.54770 -0.06334 0.16880  0.03371  22  GLN E O   
3127 C CB  . GLN C 22  ? 1.94447 1.40166 1.61502 -0.08932 0.17199  -0.08864 22  GLN E CB  
3128 C CG  . GLN C 22  ? 1.93553 1.26485 1.51270 -0.01145 0.13906  -0.09226 22  GLN E CG  
3129 C CD  . GLN C 22  ? 1.85881 1.15272 1.46658 0.04829  0.08082  -0.16640 22  GLN E CD  
3130 O OE1 . GLN C 22  ? 1.79968 1.17768 1.51848 0.02663  0.06705  -0.22120 22  GLN E OE1 
3131 N NE2 . GLN C 22  ? 1.86144 1.02900 1.36770 0.12563  0.04641  -0.17226 22  GLN E NE2 
3132 N N   . ARG C 23  ? 2.07894 1.59812 1.71031 -0.16585 0.23077  0.04978  23  ARG E N   
3133 C CA  . ARG C 23  ? 1.97136 1.48061 1.54370 -0.16604 0.24728  0.10973  23  ARG E CA  
3134 C C   . ARG C 23  ? 1.96832 1.45333 1.54378 -0.15765 0.22964  0.14058  23  ARG E C   
3135 O O   . ARG C 23  ? 1.92917 1.38065 1.45548 -0.13318 0.22654  0.17839  23  ARG E O   
3136 C CB  . ARG C 23  ? 1.82980 1.42838 1.40482 -0.21849 0.28631  0.13077  23  ARG E CB  
3137 C CG  . ARG C 23  ? 1.82519 1.44892 1.40217 -0.23048 0.30732  0.09815  23  ARG E CG  
3138 C CD  . ARG C 23  ? 1.71696 1.43088 1.29259 -0.27476 0.34334  0.11597  23  ARG E CD  
3139 N NE  . ARG C 23  ? 1.68760 1.41011 1.22582 -0.26842 0.34663  0.16259  23  ARG E NE  
3140 C CZ  . ARG C 23  ? 1.65737 1.45395 1.19615 -0.29671 0.35517  0.18916  23  ARG E CZ  
3141 N NH1 . ARG C 23  ? 1.62718 1.49841 1.20008 -0.33480 0.36432  0.17718  23  ARG E NH1 
3142 N NH2 . ARG C 23  ? 1.66615 1.46532 1.17454 -0.27587 0.34649  0.22322  23  ARG E NH2 
3143 N N   . SER C 24  ? 1.90746 1.24367 1.46954 -0.32774 0.75827  0.13329  24  SER E N   
3144 C CA  . SER C 24  ? 1.91956 1.23258 1.60611 -0.34780 0.77110  0.14911  24  SER E CA  
3145 C C   . SER C 24  ? 1.99653 1.27355 1.79155 -0.33696 0.81967  0.10274  24  SER E C   
3146 O O   . SER C 24  ? 1.99127 1.28189 1.94668 -0.33173 0.78288  0.09594  24  SER E O   
3147 C CB  . SER C 24  ? 1.90033 1.24296 1.66974 -0.38058 0.75880  0.20349  24  SER E CB  
3148 O OG  . SER C 24  ? 1.94938 1.30287 1.74496 -0.38233 0.78689  0.19704  24  SER E OG  
3149 N N   . TYR C 25  ? 1.98448 1.26530 1.72331 -0.29799 0.83565  0.04852  25  TYR E N   
3150 C CA  . TYR C 25  ? 1.95878 1.27066 1.82945 -0.24218 0.79602  -0.02346 25  TYR E CA  
3151 C C   . TYR C 25  ? 1.93315 1.25625 1.81797 -0.19667 0.73193  -0.06537 25  TYR E C   
3152 O O   . TYR C 25  ? 1.93894 1.24442 1.70322 -0.20006 0.72659  -0.04834 25  TYR E O   
3153 C CB  . TYR C 25  ? 1.92696 1.24559 1.74121 -0.20846 0.82796  -0.06931 25  TYR E CB  
3154 C CG  . TYR C 25  ? 1.83600 1.19230 1.79125 -0.15118 0.78873  -0.14386 25  TYR E CG  
3155 C CD1 . TYR C 25  ? 1.79324 1.16999 1.89990 -0.16129 0.79754  -0.15050 25  TYR E CD1 
3156 C CD2 . TYR C 25  ? 1.78925 1.16268 1.72778 -0.08660 0.74299  -0.20826 25  TYR E CD2 
3157 C CE1 . TYR C 25  ? 1.69774 1.11341 1.93826 -0.10904 0.75917  -0.22228 25  TYR E CE1 
3158 C CE2 . TYR C 25  ? 1.70538 1.11755 1.77023 -0.03260 0.70422  -0.27856 25  TYR E CE2 
3159 C CZ  . TYR C 25  ? 1.65557 1.09003 1.87281 -0.04408 0.71091  -0.28700 25  TYR E CZ  
3160 O OH  . TYR C 25  ? 1.61451 1.09179 1.95930 0.01095  0.66920  -0.36160 25  TYR E OH  
3161 N N   . CYS C 26  ? 1.92524 1.27946 1.96629 -0.15555 0.68291  -0.12074 26  CYS E N   
3162 C CA  . CYS C 26  ? 1.89196 1.26293 1.97893 -0.10864 0.61776  -0.16827 26  CYS E CA  
3163 C C   . CYS C 26  ? 1.89220 1.25387 1.81314 -0.07009 0.61690  -0.19610 26  CYS E C   
3164 O O   . CYS C 26  ? 1.86010 1.22997 1.72539 -0.03062 0.63184  -0.23965 26  CYS E O   
3165 C CB  . CYS C 26  ? 1.80818 1.21871 2.07274 -0.06391 0.57627  -0.23713 26  CYS E CB  
3166 S SG  . CYS C 26  ? 1.74916 1.19072 2.08448 0.00768  0.49569  -0.31737 26  CYS E SG  
3167 N N   . HIS C 27  ? 2.01393 1.35907 1.85966 -0.07950 0.59973  -0.17142 27  HIS E N   
3168 C CA  . HIS C 27  ? 2.00041 1.33167 1.68147 -0.05116 0.60676  -0.18817 27  HIS E CA  
3169 C C   . HIS C 27  ? 1.98752 1.31136 1.64813 -0.05539 0.56972  -0.17164 27  HIS E C   
3170 O O   . HIS C 27  ? 1.98727 1.30626 1.71580 -0.09800 0.55786  -0.12440 27  HIS E O   
3171 C CB  . HIS C 27  ? 2.02818 1.32967 1.54821 -0.08711 0.67577  -0.14676 27  HIS E CB  
3172 C CG  . HIS C 27  ? 1.99635 1.27251 1.45320 -0.15364 0.70077  -0.07118 27  HIS E CG  
3173 N ND1 . HIS C 27  ? 2.01171 1.28094 1.51069 -0.20949 0.73375  -0.01695 27  HIS E ND1 
3174 C CD2 . HIS C 27  ? 1.92411 1.18209 1.27508 -0.17230 0.69872  -0.04090 27  HIS E CD2 
3175 C CE1 . HIS C 27  ? 1.95287 1.20488 1.37544 -0.25630 0.74392  0.04256  27  HIS E CE1 
3176 N NE2 . HIS C 27  ? 1.89911 1.15008 1.24145 -0.23254 0.71361  0.02657  27  HIS E NE2 
3177 N N   . PRO C 28  ? 1.98468 1.30860 1.56007 -0.00979 0.55034  -0.20969 28  PRO E N   
3178 C CA  . PRO C 28  ? 1.95209 1.27018 1.50848 -0.01220 0.51573  -0.19614 28  PRO E CA  
3179 C C   . PRO C 28  ? 1.92428 1.21274 1.36989 -0.07467 0.55216  -0.12279 28  PRO E C   
3180 O O   . PRO C 28  ? 1.90968 1.17718 1.20930 -0.08872 0.60043  -0.10657 28  PRO E O   
3181 C CB  . PRO C 28  ? 1.91275 1.23524 1.38147 0.05139  0.50128  -0.25313 28  PRO E CB  
3182 C CG  . PRO C 28  ? 1.91853 1.26073 1.42146 0.09732  0.50619  -0.30754 28  PRO E CG  
3183 C CD  . PRO C 28  ? 1.95616 1.28843 1.46308 0.05122  0.55553  -0.26968 28  PRO E CD  
3184 N N   . ILE C 29  ? 1.99258 1.28038 1.50948 -0.11106 0.52815  -0.07948 29  ILE E N   
3185 C CA  . ILE C 29  ? 2.01272 1.27851 1.44036 -0.17034 0.55472  -0.00808 29  ILE E CA  
3186 C C   . ILE C 29  ? 2.02804 1.29526 1.45843 -0.16615 0.51144  0.00011  29  ILE E C   
3187 O O   . ILE C 29  ? 2.05606 1.34115 1.60896 -0.13519 0.45927  -0.03075 29  ILE E O   
3188 C CB  . ILE C 29  ? 2.03448 1.29712 1.54003 -0.22584 0.57531  0.05070  29  ILE E CB  
3189 C CG1 . ILE C 29  ? 2.06129 1.30570 1.47674 -0.28476 0.59741  0.12551  29  ILE E CG1 
3190 C CG2 . ILE C 29  ? 2.02152 1.30375 1.72173 -0.21469 0.52808  0.03916  29  ILE E CG2 
3191 C CD1 . ILE C 29  ? 2.04819 1.32453 1.33659 -0.27573 0.59565  0.11841  29  ILE E CD1 
3192 N N   . GLU C 30  ? 2.04903 1.29871 1.34232 -0.19464 0.53355  0.03641  30  GLU E N   
3193 C CA  . GLU C 30  ? 2.10729 1.35759 1.39598 -0.20301 0.49918  0.05794  30  GLU E CA  
3194 C C   . GLU C 30  ? 2.15358 1.41156 1.57818 -0.23452 0.46983  0.10297  30  GLU E C   
3195 O O   . GLU C 30  ? 2.14387 1.39384 1.56838 -0.28517 0.49831  0.16139  30  GLU E O   
3196 C CB  . GLU C 30  ? 2.10425 1.35293 1.25226 -0.23326 0.52042  0.09229  30  GLU E CB  
3197 C CG  . GLU C 30  ? 2.15380 1.41027 1.29416 -0.24515 0.48630  0.11774  30  GLU E CG  
3198 C CD  . GLU C 30  ? 2.09121 1.39892 1.18702 -0.21547 0.45188  0.08833  30  GLU E CD  
3199 O OE1 . GLU C 30  ? 2.07800 1.36895 1.13852 -0.17574 0.44996  0.04402  30  GLU E OE1 
3200 O OE2 . GLU C 30  ? 2.04038 1.41251 1.15631 -0.22842 0.42532  0.11074  30  GLU E OE2 
3201 N N   . THR C 31  ? 1.94864 1.22156 1.48943 -0.20326 0.41458  0.07583  31  THR E N   
3202 C CA  . THR C 31  ? 1.98361 1.26280 1.66486 -0.22571 0.38157  0.11321  31  THR E CA  
3203 C C   . THR C 31  ? 2.04110 1.32418 1.72251 -0.21558 0.33977  0.11644  31  THR E C   
3204 O O   . THR C 31  ? 2.07650 1.36858 1.75317 -0.16646 0.31161  0.05836  31  THR E O   
3205 C CB  . THR C 31  ? 1.99462 1.29047 1.85133 -0.19497 0.35243  0.06966  31  THR E CB  
3206 O OG1 . THR C 31  ? 1.93333 1.22753 1.79455 -0.20494 0.39227  0.06675  31  THR E OG1 
3207 C CG2 . THR C 31  ? 2.02012 1.31928 2.02822 -0.21757 0.31994  0.10852  31  THR E CG2 
3208 N N   . LEU C 32  ? 1.99111 1.26850 1.67399 -0.26026 0.33660  0.18436  32  LEU E N   
3209 C CA  . LEU C 32  ? 2.02464 1.30732 1.71757 -0.25308 0.29615  0.19198  32  LEU E CA  
3210 C C   . LEU C 32  ? 2.04581 1.34055 1.92640 -0.23115 0.24457  0.17595  32  LEU E C   
3211 O O   . LEU C 32  ? 2.02137 1.31437 2.01372 -0.25716 0.24381  0.21405  32  LEU E O   
3212 C CB  . LEU C 32  ? 2.00052 1.27516 1.60932 -0.30775 0.31331  0.27027  32  LEU E CB  
3213 C CG  . LEU C 32  ? 1.97488 1.23740 1.41229 -0.33669 0.36987  0.28853  32  LEU E CG  
3214 C CD1 . LEU C 32  ? 1.93274 1.23818 1.35206 -0.37478 0.36855  0.35601  32  LEU E CD1 
3215 C CD2 . LEU C 32  ? 1.99031 1.25163 1.30526 -0.30779 0.37266  0.24331  32  LEU E CD2 
3216 N N   . VAL C 33  ? 1.87433 1.18061 1.79034 -0.18318 0.20319  0.11947  33  VAL E N   
3217 C CA  . VAL C 33  ? 1.88991 1.20975 1.98309 -0.15181 0.15333  0.08404  33  VAL E CA  
3218 C C   . VAL C 33  ? 1.87918 1.20375 1.99280 -0.14233 0.11253  0.09039  33  VAL E C   
3219 O O   . VAL C 33  ? 1.89682 1.22342 1.90531 -0.12024 0.10950  0.06472  33  VAL E O   
3220 C CB  . VAL C 33  ? 1.94237 1.27677 2.07173 -0.09311 0.13984  -0.00538 33  VAL E CB  
3221 C CG1 . VAL C 33  ? 1.95354 1.30516 2.25806 -0.05636 0.08426  -0.05185 33  VAL E CG1 
3222 C CG2 . VAL C 33  ? 1.92663 1.25874 2.05075 -0.10226 0.17853  -0.01112 33  VAL E CG2 
3223 N N   . ASP C 34  ? 2.00863 1.33444 2.26080 -0.15777 0.08270  0.12409  34  ASP E N   
3224 C CA  . ASP C 34  ? 1.97326 1.30490 2.26341 -0.14568 0.04108  0.12728  34  ASP E CA  
3225 C C   . ASP C 34  ? 1.99416 1.34153 2.33521 -0.08223 0.00350  0.03785  34  ASP E C   
3226 O O   . ASP C 34  ? 2.01448 1.37139 2.46111 -0.05234 -0.01075 -0.01538 34  ASP E O   
3227 C CB  . ASP C 34  ? 1.90555 1.23364 2.34549 -0.17296 0.01849  0.18176  34  ASP E CB  
3228 C CG  . ASP C 34  ? 1.84663 1.17990 2.32359 -0.16495 -0.02220 0.19455  34  ASP E CG  
3229 O OD1 . ASP C 34  ? 1.85950 1.20175 2.27300 -0.13126 -0.03912 0.14863  34  ASP E OD1 
3230 O OD2 . ASP C 34  ? 1.77523 1.10326 2.34848 -0.19179 -0.03614 0.25245  34  ASP E OD2 
3231 N N   . ILE C 35  ? 1.93480 1.28680 2.20318 -0.06144 -0.01300 0.02099  35  ILE E N   
3232 C CA  . ILE C 35  ? 1.91718 1.28424 2.20660 0.00063  -0.04411 -0.06264 35  ILE E CA  
3233 C C   . ILE C 35  ? 1.86552 1.24518 2.34965 0.02720  -0.09248 -0.09871 35  ILE E C   
3234 O O   . ILE C 35  ? 1.83595 1.23148 2.36881 0.07978  -0.11632 -0.17713 35  ILE E O   
3235 C CB  . ILE C 35  ? 1.86737 1.23543 2.04981 0.01101  -0.05022 -0.06241 35  ILE E CB  
3236 C CG1 . ILE C 35  ? 1.91453 1.26912 1.91500 -0.02392 -0.00091 -0.01981 35  ILE E CG1 
3237 C CG2 . ILE C 35  ? 1.79002 1.17252 1.96877 0.07695  -0.07446 -0.14788 35  ILE E CG2 
3238 C CD1 . ILE C 35  ? 1.86605 1.22205 1.76006 -0.01580 -0.00229 -0.02129 35  ILE E CD1 
3239 N N   . PHE C 36  ? 1.88530 1.25874 2.48405 -0.00699 -0.10765 -0.04353 36  PHE E N   
3240 C CA  . PHE C 36  ? 1.83094 1.21360 2.62614 0.01464  -0.15026 -0.07615 36  PHE E CA  
3241 C C   . PHE C 36  ? 1.87598 1.26790 2.75346 0.03608  -0.14802 -0.13101 36  PHE E C   
3242 O O   . PHE C 36  ? 1.83689 1.24641 2.82586 0.08111  -0.18487 -0.20373 36  PHE E O   
3243 C CB  . PHE C 36  ? 1.77605 1.14599 2.68023 -0.03046 -0.15689 0.00121  36  PHE E CB  
3244 C CG  . PHE C 36  ? 1.69425 1.07141 2.79189 -0.00692 -0.20453 -0.02921 36  PHE E CG  
3245 C CD1 . PHE C 36  ? 1.63206 1.02287 2.75239 0.03694  -0.24373 -0.08437 36  PHE E CD1 
3246 C CD2 . PHE C 36  ? 1.67678 1.04736 2.93798 -0.02600 -0.20815 -0.00931 36  PHE E CD2 
3247 C CE1 . PHE C 36  ? 1.55598 0.95350 2.85686 0.05925  -0.28707 -0.11655 36  PHE E CE1 
3248 C CE2 . PHE C 36  ? 1.60575 0.98182 3.05113 -0.00433 -0.25058 -0.04101 36  PHE E CE2 
3249 C CZ  . PHE C 36  ? 1.54774 0.93763 3.01267 0.03858  -0.29081 -0.09616 36  PHE E CZ  
3250 N N   . GLN C 37  ? 1.87188 1.25432 2.69670 0.00494  -0.10536 -0.09933 37  GLN E N   
3251 C CA  . GLN C 37  ? 1.90986 1.30197 2.82558 0.01930  -0.10129 -0.14382 37  GLN E CA  
3252 C C   . GLN C 37  ? 1.92518 1.33999 2.81534 0.08252  -0.11930 -0.24131 37  GLN E C   
3253 O O   . GLN C 37  ? 1.91877 1.35165 2.93591 0.11146  -0.14151 -0.30087 37  GLN E O   
3254 C CB  . GLN C 37  ? 1.95851 1.33641 2.79550 -0.02404 -0.04731 -0.09218 37  GLN E CB  
3255 C CG  . GLN C 37  ? 1.91862 1.27455 2.71561 -0.08523 -0.02178 0.00954  37  GLN E CG  
3256 C CD  . GLN C 37  ? 1.84282 1.19317 2.81840 -0.10643 -0.04572 0.04837  37  GLN E CD  
3257 O OE1 . GLN C 37  ? 1.78302 1.13188 2.79788 -0.10527 -0.07608 0.06748  37  GLN E OE1 
3258 N NE2 . GLN C 37  ? 1.83114 1.17808 2.92120 -0.12486 -0.03105 0.05969  37  GLN E NE2 
3259 N N   . GLU C 38  ? 1.94128 1.35678 2.67173 0.10586  -0.11010 -0.25970 38  GLU E N   
3260 C CA  . GLU C 38  ? 1.89108 1.32768 2.58615 0.16857  -0.12381 -0.34825 38  GLU E CA  
3261 C C   . GLU C 38  ? 1.75893 1.21236 2.51478 0.21642  -0.17398 -0.40441 38  GLU E C   
3262 O O   . GLU C 38  ? 1.68829 1.16613 2.53529 0.26516  -0.20675 -0.48185 38  GLU E O   
3263 C CB  . GLU C 38  ? 1.89184 1.31907 2.38094 0.17325  -0.08151 -0.34298 38  GLU E CB  
3264 C CG  . GLU C 38  ? 2.02257 1.42966 2.43165 0.11966  -0.02836 -0.27798 38  GLU E CG  
3265 C CD  . GLU C 38  ? 2.09197 1.50702 2.60229 0.11486  -0.02005 -0.29314 38  GLU E CD  
3266 O OE1 . GLU C 38  ? 2.10220 1.51414 2.74932 0.08210  -0.02892 -0.25933 38  GLU E OE1 
3267 O OE2 . GLU C 38  ? 2.07372 1.49818 2.52869 0.14441  -0.00334 -0.33794 38  GLU E OE2 
3268 N N   . TYR C 39  ? 1.94627 1.91735 1.40076 0.72091  -0.41974 0.33792  39  TYR E N   
3269 C CA  . TYR C 39  ? 2.06128 1.95103 1.49098 0.65201  -0.35698 0.35103  39  TYR E CA  
3270 C C   . TYR C 39  ? 1.95389 1.92092 1.48212 0.59742  -0.34582 0.31179  39  TYR E C   
3271 O O   . TYR C 39  ? 2.07893 1.98905 1.70032 0.56734  -0.31447 0.28195  39  TYR E O   
3272 C CB  . TYR C 39  ? 2.35200 2.07708 1.79263 0.63908  -0.30934 0.36305  39  TYR E CB  
3273 C CG  . TYR C 39  ? 2.48091 2.10894 1.81189 0.67141  -0.31271 0.41678  39  TYR E CG  
3274 C CD1 . TYR C 39  ? 2.34811 2.03385 1.58687 0.72081  -0.36232 0.44125  39  TYR E CD1 
3275 C CD2 . TYR C 39  ? 2.71587 2.19552 2.04000 0.65077  -0.26974 0.44578  39  TYR E CD2 
3276 C CE1 . TYR C 39  ? 2.48507 2.07834 1.62581 0.74992  -0.37205 0.49163  39  TYR E CE1 
3277 C CE2 . TYR C 39  ? 2.82697 2.21721 2.05437 0.67590  -0.27910 0.50336  39  TYR E CE2 
3278 C CZ  . TYR C 39  ? 2.71266 2.15730 1.84776 0.72624  -0.33193 0.52536  39  TYR E CZ  
3279 O OH  . TYR C 39  ? 2.82804 2.17938 1.86791 0.75104  -0.34757 0.58410  39  TYR E OH  
3280 N N   . PRO C 40  ? 2.16872 2.26286 1.68717 0.58254  -0.37548 0.31115  40  PRO E N   
3281 C CA  . PRO C 40  ? 2.02827 2.19787 1.65477 0.53065  -0.37839 0.27681  40  PRO E CA  
3282 C C   . PRO C 40  ? 2.17602 2.27709 1.81778 0.46251  -0.32627 0.26200  40  PRO E C   
3283 O O   . PRO C 40  ? 2.01991 2.19425 1.71578 0.41794  -0.33958 0.24261  40  PRO E O   
3284 C CB  . PRO C 40  ? 1.73886 2.06736 1.34891 0.54032  -0.43621 0.29022  40  PRO E CB  
3285 C CG  . PRO C 40  ? 1.78810 2.09090 1.26788 0.56595  -0.43581 0.32518  40  PRO E CG  
3286 C CD  . PRO C 40  ? 2.03673 2.20805 1.45421 0.61060  -0.41200 0.34238  40  PRO E CD  
3287 N N   . ASP C 41  ? 1.92210 1.88804 1.52494 0.45330  -0.27042 0.26970  41  ASP E N   
3288 C CA  . ASP C 41  ? 2.09073 1.99263 1.70437 0.39184  -0.21354 0.25157  41  ASP E CA  
3289 C C   . ASP C 41  ? 2.22553 2.06265 1.96056 0.36164  -0.18235 0.21052  41  ASP E C   
3290 O O   . ASP C 41  ? 2.23880 2.05260 2.02867 0.39490  -0.19685 0.20439  41  ASP E O   
3291 C CB  . ASP C 41  ? 2.28930 2.09642 1.78013 0.39458  -0.16822 0.29157  41  ASP E CB  
3292 N N   . GLU C 42  ? 2.02788 1.83988 1.80870 0.30084  -0.14156 0.17649  42  GLU E N   
3293 C CA  . GLU C 42  ? 2.14686 1.88345 2.03681 0.26568  -0.10249 0.13446  42  GLU E CA  
3294 C C   . GLU C 42  ? 1.96515 1.75372 1.97707 0.27583  -0.14643 0.10231  42  GLU E C   
3295 O O   . GLU C 42  ? 1.96637 1.70485 2.02511 0.30591  -0.14605 0.09765  42  GLU E O   
3296 C CB  . GLU C 42  ? 2.32062 1.92434 2.17437 0.27925  -0.05214 0.16078  42  GLU E CB  
3297 N N   . ILE C 43  ? 2.06128 1.95744 2.12788 0.24965  -0.18892 0.08085  43  ILE E N   
3298 C CA  . ILE C 43  ? 1.76759 1.73506 1.94483 0.25273  -0.23613 0.05800  43  ILE E CA  
3299 C C   . ILE C 43  ? 1.75537 1.64129 2.04876 0.22083  -0.20311 0.00798  43  ILE E C   
3300 O O   . ILE C 43  ? 1.67499 1.55786 2.03462 0.24728  -0.21798 -0.00496 43  ILE E O   
3301 C CB  . ILE C 43  ? 1.40491 1.50312 1.61916 0.22291  -0.29314 0.05577  43  ILE E CB  
3302 N N   . GLU C 44  ? 1.94092 1.76632 2.26380 0.16608  -0.15928 -0.02600 44  GLU E N   
3303 C CA  . GLU C 44  ? 1.78200 1.52686 2.21752 0.13105  -0.12478 -0.07916 44  GLU E CA  
3304 C C   . GLU C 44  ? 1.98938 1.60560 2.39522 0.15273  -0.06522 -0.06820 44  GLU E C   
3305 O O   . GLU C 44  ? 2.01452 1.54626 2.42720 0.11616  -0.00532 -0.08774 44  GLU E O   
3306 C CB  . GLU C 44  ? 1.64482 1.38959 2.13018 0.06522  -0.10656 -0.12661 44  GLU E CB  
3307 N N   . TYR C 45  ? 1.84469 1.45438 2.22326 0.21352  -0.08686 -0.03663 45  TYR E N   
3308 C CA  . TYR C 45  ? 1.98941 1.48041 2.34252 0.24288  -0.04740 -0.01634 45  TYR E CA  
3309 C C   . TYR C 45  ? 1.94405 1.46120 2.32555 0.31078  -0.09581 -0.01030 45  TYR E C   
3310 O O   . TYR C 45  ? 2.00782 1.61600 2.32553 0.35314  -0.14361 0.01951  45  TYR E O   
3311 C CB  . TYR C 45  ? 2.25534 1.71038 2.46861 0.24946  -0.01898 0.03988  45  TYR E CB  
3312 C CG  . TYR C 45  ? 2.29168 1.65250 2.48984 0.19796  0.05511  0.03789  45  TYR E CG  
3313 C CD1 . TYR C 45  ? 2.23064 1.47206 2.47780 0.19445  0.09747  0.03731  45  TYR E CD1 
3314 C CD2 . TYR C 45  ? 2.36547 1.76712 2.50656 0.15271  0.08084  0.03409  45  TYR E CD2 
3315 C CE1 . TYR C 45  ? 2.24770 1.41754 2.48153 0.14278  0.16768  0.03955  45  TYR E CE1 
3316 C CE2 . TYR C 45  ? 2.38960 1.72764 2.51508 0.10522  0.15030  0.02894  45  TYR E CE2 
3317 C CZ  . TYR C 45  ? 2.33224 1.55677 2.50215 0.09799  0.19571  0.03452  45  TYR E CZ  
3318 O OH  . TYR C 45  ? 2.35397 1.52846 2.50939 0.04642  0.26727  0.03331  45  TYR E OH  
3319 N N   . ILE C 46  ? 1.56836 1.50389 2.48328 0.11023  0.02681  0.01767  46  ILE E N   
3320 C CA  . ILE C 46  ? 1.62861 1.64299 2.53536 0.04332  0.01850  0.03433  46  ILE E CA  
3321 C C   . ILE C 46  ? 1.62336 1.64508 2.47966 0.04537  0.11149  0.01467  46  ILE E C   
3322 O O   . ILE C 46  ? 1.54539 1.54246 2.42009 0.08531  0.19129  -0.01327 46  ILE E O   
3323 C CB  . ILE C 46  ? 1.61436 1.71226 2.63982 0.00951  -0.01007 0.03678  46  ILE E CB  
3324 C CG1 . ILE C 46  ? 1.60882 1.68595 2.68111 0.01534  -0.10882 0.05808  46  ILE E CG1 
3325 C CG2 . ILE C 46  ? 1.63892 1.81400 2.64676 -0.06227 -0.01905 0.05066  46  ILE E CG2 
3326 C CD1 . ILE C 46  ? 1.66393 1.69627 2.64021 -0.01676 -0.19395 0.09621  46  ILE E CD1 
3327 N N   . PHE C 47  ? 1.62628 1.67639 2.41321 0.00379  0.10195  0.02900  47  PHE E N   
3328 C CA  . PHE C 47  ? 1.61947 1.67979 2.36270 0.00265  0.18028  0.01157  47  PHE E CA  
3329 C C   . PHE C 47  ? 1.57100 1.72197 2.35180 -0.06018 0.17476  0.01424  47  PHE E C   
3330 O O   . PHE C 47  ? 1.54649 1.74288 2.31407 -0.10896 0.10734  0.03775  47  PHE E O   
3331 C CB  . PHE C 47  ? 1.67921 1.69765 2.30804 0.01607  0.18040  0.01857  47  PHE E CB  
3332 C CG  . PHE C 47  ? 1.64934 1.57071 2.21932 0.07559  0.18634  0.01400  47  PHE E CG  
3333 C CD1 . PHE C 47  ? 1.55444 1.42286 2.15987 0.12311  0.22524  -0.00511 47  PHE E CD1 
3334 C CD2 . PHE C 47  ? 1.71737 1.60458 2.19427 0.08226  0.15440  0.02618  47  PHE E CD2 
3335 C CE1 . PHE C 47  ? 1.53152 1.30526 2.06795 0.17641  0.23144  -0.01212 47  PHE E CE1 
3336 C CE2 . PHE C 47  ? 1.70126 1.49529 2.11287 0.13343  0.15493  0.02081  47  PHE E CE2 
3337 C CZ  . PHE C 47  ? 1.60947 1.34172 2.04431 0.18090  0.19386  0.00138  47  PHE E CZ  
3338 N N   . LYS C 48  ? 1.47135 1.64360 2.29054 -0.06280 0.24649  -0.01024 48  LYS E N   
3339 C CA  . LYS C 48  ? 1.37380 1.61980 2.21348 -0.11963 0.25324  -0.01524 48  LYS E CA  
3340 C C   . LYS C 48  ? 1.34121 1.55979 2.11891 -0.10633 0.33452  -0.03692 48  LYS E C   
3341 O O   . LYS C 48  ? 1.31042 1.47962 2.09604 -0.07146 0.40606  -0.05665 48  LYS E O   
3342 C CB  . LYS C 48  ? 1.29634 1.59589 2.25145 -0.14414 0.25300  -0.02569 48  LYS E CB  
3343 N N   . PRO C 49  ? 1.25198 1.49775 1.96681 -0.13184 0.32925  -0.03524 49  PRO E N   
3344 C CA  . PRO C 49  ? 1.24737 1.55628 1.94080 -0.17996 0.25803  -0.01430 49  PRO E CA  
3345 C C   . PRO C 49  ? 1.34068 1.62019 1.98751 -0.16119 0.20107  0.01124  49  PRO E C   
3346 O O   . PRO C 49  ? 1.42920 1.63634 2.04130 -0.10628 0.22111  0.00896  49  PRO E O   
3347 C CB  . PRO C 49  ? 1.19829 1.53356 1.83730 -0.19517 0.29891  -0.03238 49  PRO E CB  
3348 C CG  . PRO C 49  ? 1.22864 1.48173 1.82037 -0.13191 0.36647  -0.04867 49  PRO E CG  
3349 C CD  . PRO C 49  ? 1.22793 1.42990 1.87352 -0.10408 0.39889  -0.05457 49  PRO E CD  
3350 N N   . SER C 50  ? 1.26706 1.59765 1.90663 -0.21127 0.12750  0.03648  50  SER E N   
3351 C CA  . SER C 50  ? 1.33461 1.63703 1.92722 -0.20469 0.06899  0.06202  50  SER E CA  
3352 C C   . SER C 50  ? 1.37233 1.67842 1.88929 -0.19127 0.08963  0.05638  50  SER E C   
3353 O O   . SER C 50  ? 1.46013 1.71995 1.93335 -0.16366 0.06404  0.06744  50  SER E O   
3354 C CB  . SER C 50  ? 1.26587 1.61474 1.86863 -0.26954 -0.01670 0.09428  50  SER E CB  
3355 O OG  . SER C 50  ? 1.16472 1.59591 1.74065 -0.32949 -0.01833 0.09492  50  SER E OG  
3356 N N   . CYS C 51  ? 1.26864 1.62952 1.77143 -0.20909 0.13210  0.03731  51  CYS E N   
3357 C CA  . CYS C 51  ? 1.29866 1.67518 1.74297 -0.19133 0.15208  0.02767  51  CYS E CA  
3358 C C   . CYS C 51  ? 1.30615 1.64260 1.73622 -0.14088 0.23341  -0.00421 51  CYS E C   
3359 O O   . CYS C 51  ? 1.25425 1.56506 1.71931 -0.13491 0.27746  -0.01945 51  CYS E O   
3360 C CB  . CYS C 51  ? 1.17246 1.65361 1.60454 -0.25436 0.12919  0.03053  51  CYS E CB  
3361 S SG  . CYS C 51  ? 1.03443 1.58466 1.50501 -0.33934 0.08880  0.04499  51  CYS E SG  
3362 N N   . VAL C 52  ? 1.35144 1.67992 1.72908 -0.10512 0.24942  -0.01300 52  VAL E N   
3363 C CA  . VAL C 52  ? 1.30960 1.59160 1.65672 -0.05438 0.31859  -0.04006 52  VAL E CA  
3364 C C   . VAL C 52  ? 1.25886 1.61571 1.58369 -0.06096 0.32141  -0.05474 52  VAL E C   
3365 O O   . VAL C 52  ? 1.27848 1.70323 1.59817 -0.08617 0.27153  -0.04120 52  VAL E O   
3366 C CB  . VAL C 52  ? 1.37328 1.54643 1.67108 0.01537  0.33590  -0.03724 52  VAL E CB  
3367 C CG1 . VAL C 52  ? 1.39848 1.50775 1.72510 0.02290  0.34073  -0.02887 52  VAL E CG1 
3368 C CG2 . VAL C 52  ? 1.48248 1.66413 1.73939 0.02977  0.28192  -0.02158 52  VAL E CG2 
3369 N N   . PRO C 53  ? 1.39491 1.74513 1.70993 -0.04188 0.37865  -0.08393 53  PRO E N   
3370 C CA  . PRO C 53  ? 1.33285 1.75343 1.63190 -0.03611 0.38566  -0.10431 53  PRO E CA  
3371 C C   . PRO C 53  ? 1.37585 1.74236 1.62604 0.03741  0.39092  -0.10728 53  PRO E C   
3372 O O   . PRO C 53  ? 1.35155 1.60907 1.56474 0.09159  0.43198  -0.11364 53  PRO E O   
3373 C CB  . PRO C 53  ? 1.21651 1.63425 1.52468 -0.04510 0.44333  -0.13643 53  PRO E CB  
3374 C CG  . PRO C 53  ? 1.22131 1.52827 1.52775 -0.02281 0.48040  -0.13380 53  PRO E CG  
3375 C CD  . PRO C 53  ? 1.31889 1.60833 1.64670 -0.03579 0.43749  -0.10175 53  PRO E CD  
3376 N N   . LEU C 54  ? 1.29974 1.73915 1.54661 0.03768  0.34803  -0.10141 54  LEU E N   
3377 C CA  . LEU C 54  ? 1.34273 1.73886 1.54655 0.10462  0.33765  -0.10101 54  LEU E CA  
3378 C C   . LEU C 54  ? 1.27278 1.77209 1.49110 0.11685  0.33423  -0.12409 54  LEU E C   
3379 O O   . LEU C 54  ? 1.23365 1.85998 1.49335 0.05990  0.31053  -0.12609 54  LEU E O   
3380 C CB  . LEU C 54  ? 1.46919 1.84627 1.65788 0.09943  0.27769  -0.07004 54  LEU E CB  
3381 C CG  . LEU C 54  ? 1.55141 1.83663 1.73319 0.09071  0.27340  -0.04908 54  LEU E CG  
3382 C CD1 . LEU C 54  ? 1.68801 1.97176 1.85957 0.07412  0.20561  -0.02214 54  LEU E CD1 
3383 C CD2 . LEU C 54  ? 1.50951 1.66008 1.64016 0.15653  0.32423  -0.05649 54  LEU E CD2 
3384 N N   . MET C 55  ? 1.36320 1.80797 1.54669 0.19137  0.35784  -0.14159 55  MET E N   
3385 C CA  . MET C 55  ? 1.32281 1.86416 1.52684 0.21902  0.34913  -0.16539 55  MET E CA  
3386 C C   . MET C 55  ? 1.39932 2.00848 1.61410 0.20756  0.28277  -0.14448 55  MET E C   
3387 O O   . MET C 55  ? 1.47074 2.00763 1.64217 0.26130  0.25712  -0.13262 55  MET E O   
3388 C CB  . MET C 55  ? 1.30848 1.75115 1.46498 0.30959  0.38071  -0.18394 55  MET E CB  
3389 C CG  . MET C 55  ? 1.25310 1.64632 1.40265 0.32345  0.44537  -0.21343 55  MET E CG  
3390 S SD  . MET C 55  ? 1.20029 1.75308 1.42063 0.26517  0.46690  -0.25078 55  MET E SD  
3391 C CE  . MET C 55  ? 1.23858 1.87205 1.48018 0.33857  0.45778  -0.28464 55  MET E CE  
3392 N N   . ARG C 56  ? 1.26584 2.00831 1.53102 0.13353  0.25299  -0.13892 56  ARG E N   
3393 C CA  . ARG C 56  ? 1.33469 2.14863 1.61328 0.11352  0.19002  -0.12053 56  ARG E CA  
3394 C C   . ARG C 56  ? 1.25429 2.22693 1.58854 0.11302  0.18798  -0.14891 56  ARG E C   
3395 O O   . ARG C 56  ? 1.15382 2.19339 1.51883 0.10940  0.23340  -0.18076 56  ARG E O   
3396 C CB  . ARG C 56  ? 1.36788 2.20857 1.65681 0.02543  0.14999  -0.08773 56  ARG E CB  
3397 N N   . CYS C 57  ? 1.98183 1.58528 1.34367 -0.55990 0.06573  0.21910  57  CYS E N   
3398 C CA  . CYS C 57  ? 2.03206 1.67456 1.35580 -0.54560 0.06881  0.21103  57  CYS E CA  
3399 C C   . CYS C 57  ? 2.11597 1.78932 1.43254 -0.51496 0.08947  0.26597  57  CYS E C   
3400 O O   . CYS C 57  ? 2.14519 1.81297 1.48886 -0.49912 0.10931  0.31253  57  CYS E O   
3401 C CB  . CYS C 57  ? 2.01944 1.66860 1.39955 -0.56701 0.10102  0.17235  57  CYS E CB  
3402 S SG  . CYS C 57  ? 1.88677 1.51062 1.20948 -0.56305 0.06775  0.09887  57  CYS E SG  
3403 N N   . GLY C 58  ? 2.12454 1.82377 1.39483 -0.49858 0.08883  0.26137  58  GLY E N   
3404 C CA  . GLY C 58  ? 2.16429 1.87670 1.40447 -0.45732 0.11577  0.31476  58  GLY E CA  
3405 C C   . GLY C 58  ? 2.13216 1.87030 1.29755 -0.44079 0.09035  0.30044  58  GLY E C   
3406 O O   . GLY C 58  ? 2.04220 1.79850 1.16085 -0.45083 0.03584  0.25873  58  GLY E O   
3407 N N   . GLY C 59  ? 2.02081 1.75074 1.17499 -0.41361 0.14023  0.33682  59  GLY E N   
3408 C CA  . GLY C 59  ? 2.00104 1.74828 1.08897 -0.40090 0.12214  0.32634  59  GLY E CA  
3409 C C   . GLY C 59  ? 2.10872 1.82960 1.26020 -0.42066 0.19418  0.30772  59  GLY E C   
3410 O O   . GLY C 59  ? 2.16357 1.87190 1.42279 -0.45322 0.24346  0.27743  59  GLY E O   
3411 N N   . CYS C 60  ? 1.99867 1.71502 1.09965 -0.40263 0.20397  0.31469  60  CYS E N   
3412 C CA  . CYS C 60  ? 2.10360 1.78819 1.28352 -0.42067 0.28381  0.28586  60  CYS E CA  
3413 C C   . CYS C 60  ? 2.12878 1.85385 1.36956 -0.47087 0.24781  0.18602  60  CYS E C   
3414 O O   . CYS C 60  ? 2.05212 1.81435 1.21862 -0.47813 0.16479  0.15529  60  CYS E O   
3415 C CB  . CYS C 60  ? 2.12330 1.77917 1.22721 -0.38554 0.30724  0.32091  60  CYS E CB  
3416 S SG  . CYS C 60  ? 2.07190 1.73268 1.01598 -0.30387 0.26556  0.41243  60  CYS E SG  
3417 N N   . CYS C 61  ? 1.90050 1.62196 1.28124 -0.49720 0.31678  0.12902  61  CYS E N   
3418 C CA  . CYS C 61  ? 1.94362 1.71363 1.39013 -0.52565 0.29150  0.01768  61  CYS E CA  
3419 C C   . CYS C 61  ? 2.00737 1.76567 1.47838 -0.52823 0.32846  -0.01938 61  CYS E C   
3420 O O   . CYS C 61  ? 2.02951 1.83568 1.52905 -0.54193 0.29040  -0.11501 61  CYS E O   
3421 C CB  . CYS C 61  ? 1.90785 1.70450 1.51589 -0.54890 0.34031  -0.05205 61  CYS E CB  
3422 S SG  . CYS C 61  ? 1.81197 1.65871 1.38359 -0.55195 0.24618  -0.09860 61  CYS E SG  
3423 N N   . ASN C 62  ? 2.17060 1.86074 1.62063 -0.50646 0.40281  0.05531  62  ASN E N   
3424 C CA  . ASN C 62  ? 2.21441 1.86599 1.66784 -0.50398 0.44933  0.04149  62  ASN E CA  
3425 C C   . ASN C 62  ? 2.24496 1.91201 1.88279 -0.53802 0.51609  -0.08311 62  ASN E C   
3426 O O   . ASN C 62  ? 2.28531 1.96344 1.93424 -0.55118 0.50116  -0.14793 62  ASN E O   
3427 C CB  . ASN C 62  ? 2.18257 1.86503 1.48754 -0.49943 0.34386  0.05189  62  ASN E CB  
3428 C CG  . ASN C 62  ? 2.08587 1.75368 1.24012 -0.45802 0.30385  0.16170  62  ASN E CG  
3429 O OD1 . ASN C 62  ? 2.10606 1.71589 1.24255 -0.41731 0.37291  0.23990  62  ASN E OD1 
3430 N ND2 . ASN C 62  ? 1.95396 1.67785 1.00563 -0.45995 0.19821  0.16112  62  ASN E ND2 
3431 N N   . ASP C 63  ? 2.17734 1.85483 1.97396 -0.55256 0.58893  -0.12754 63  ASP E N   
3432 C CA  . ASP C 63  ? 2.11805 1.80667 2.13822 -0.57923 0.69089  -0.25017 63  ASP E CA  
3433 C C   . ASP C 63  ? 1.99395 1.68147 2.16007 -0.58780 0.78124  -0.25114 63  ASP E C   
3434 O O   . ASP C 63  ? 1.95235 1.69876 2.09476 -0.59225 0.70845  -0.24810 63  ASP E O   
3435 C CB  . ASP C 63  ? 2.12003 1.91754 2.20240 -0.59829 0.60324  -0.40385 63  ASP E CB  
3436 C CG  . ASP C 63  ? 1.99628 1.83577 2.34566 -0.62201 0.70194  -0.56095 63  ASP E CG  
3437 O OD1 . ASP C 63  ? 1.96465 1.71905 2.43558 -0.63078 0.84877  -0.55709 63  ASP E OD1 
3438 O OD2 . ASP C 63  ? 1.88586 1.84231 2.32837 -0.62458 0.64043  -0.69433 63  ASP E OD2 
3439 N N   . GLU C 64  ? 2.10428 1.71443 2.42164 -0.58890 0.95061  -0.25179 64  GLU E N   
3440 C CA  . GLU C 64  ? 1.97586 1.57197 2.43271 -0.59064 1.05375  -0.23910 64  GLU E CA  
3441 C C   . GLU C 64  ? 1.85908 1.58798 2.47867 -0.63089 1.00730  -0.37505 64  GLU E C   
3442 O O   . GLU C 64  ? 1.80988 1.55901 2.43263 -0.62260 0.98602  -0.33687 64  GLU E O   
3443 C CB  . GLU C 64  ? 2.04682 1.53851 2.62706 -0.53829 1.19119  -0.25396 64  GLU E CB  
3444 N N   . GLY C 65  ? 1.73698 1.55953 2.47552 -0.65165 0.96995  -0.53827 65  GLY E N   
3445 C CA  . GLY C 65  ? 1.62948 1.59008 2.53197 -0.66946 0.92892  -0.68748 65  GLY E CA  
3446 C C   . GLY C 65  ? 1.58929 1.60148 2.33698 -0.65717 0.79037  -0.63524 65  GLY E C   
3447 O O   . GLY C 65  ? 1.52369 1.60396 2.39129 -0.66911 0.79835  -0.69007 65  GLY E O   
3448 N N   . LEU C 66  ? 1.56694 1.54302 2.28526 -0.75483 0.45664  -0.12112 66  LEU E N   
3449 C CA  . LEU C 66  ? 1.55839 1.55433 2.23715 -0.73483 0.43379  -0.15004 66  LEU E CA  
3450 C C   . LEU C 66  ? 1.59031 1.44998 2.15637 -0.69574 0.45141  -0.20785 66  LEU E C   
3451 O O   . LEU C 66  ? 1.61573 1.37433 2.14676 -0.67594 0.49249  -0.21611 66  LEU E O   
3452 C CB  . LEU C 66  ? 1.48800 1.60261 2.26936 -0.70543 0.45698  -0.08881 66  LEU E CB  
3453 C CG  . LEU C 66  ? 1.44154 1.53351 2.26203 -0.65081 0.52924  -0.05286 66  LEU E CG  
3454 C CD1 . LEU C 66  ? 1.35784 1.58810 2.27887 -0.63105 0.53488  0.00767  66  LEU E CD1 
3455 C CD2 . LEU C 66  ? 1.44985 1.50392 2.29331 -0.63806 0.56742  -0.01497 66  LEU E CD2 
3456 N N   . GLU C 67  ? 1.67407 1.53640 2.18367 -0.68155 0.41782  -0.24268 67  GLU E N   
3457 C CA  . GLU C 67  ? 1.69614 1.44506 2.10191 -0.65024 0.42101  -0.29556 67  GLU E CA  
3458 C C   . GLU C 67  ? 1.66950 1.46472 2.08613 -0.61127 0.41966  -0.28876 67  GLU E C   
3459 O O   . GLU C 67  ? 1.64500 1.55704 2.12601 -0.61402 0.40166  -0.25770 67  GLU E O   
3460 C CB  . GLU C 67  ? 1.72648 1.40921 2.03133 -0.67603 0.37622  -0.35365 67  GLU E CB  
3461 C CG  . GLU C 67  ? 1.74031 1.50744 2.05700 -0.71788 0.32373  -0.35220 67  GLU E CG  
3462 C CD  . GLU C 67  ? 1.76831 1.45376 1.96864 -0.73597 0.28557  -0.41154 67  GLU E CD  
3463 O OE1 . GLU C 67  ? 1.75761 1.34567 1.87437 -0.69173 0.29451  -0.43784 67  GLU E OE1 
3464 O OE2 . GLU C 67  ? 1.79790 1.52553 1.98211 -0.77429 0.24090  -0.41821 67  GLU E OE2 
3465 N N   . CYS C 68  ? 1.68465 1.38702 2.04207 -0.57557 0.44045  -0.31352 68  CYS E N   
3466 C CA  . CYS C 68  ? 1.66334 1.38336 2.01775 -0.53765 0.43979  -0.31309 68  CYS E CA  
3467 C C   . CYS C 68  ? 1.67050 1.41019 1.97323 -0.54164 0.39013  -0.34628 68  CYS E C   
3468 O O   . CYS C 68  ? 1.67557 1.32603 1.89014 -0.54167 0.37428  -0.39032 68  CYS E O   
3469 C CB  . CYS C 68  ? 1.67486 1.27608 1.97145 -0.50795 0.46978  -0.33144 68  CYS E CB  
3470 S SG  . CYS C 68  ? 1.64754 1.26605 1.96724 -0.46333 0.48590  -0.31216 68  CYS E SG  
3471 N N   . VAL C 69  ? 1.56338 1.41785 1.91807 -0.54333 0.36788  -0.32255 69  VAL E N   
3472 C CA  . VAL C 69  ? 1.59719 1.47275 1.90044 -0.54203 0.32526  -0.34868 69  VAL E CA  
3473 C C   . VAL C 69  ? 1.58764 1.53279 1.93054 -0.50309 0.32782  -0.32588 69  VAL E C   
3474 O O   . VAL C 69  ? 1.53878 1.55737 1.96874 -0.48976 0.35294  -0.28137 69  VAL E O   
3475 C CB  . VAL C 69  ? 1.63949 1.57672 1.94406 -0.58652 0.28636  -0.34816 69  VAL E CB  
3476 C CG1 . VAL C 69  ? 1.65270 1.49716 1.88854 -0.62326 0.27576  -0.38472 69  VAL E CG1 
3477 C CG2 . VAL C 69  ? 1.61049 1.66807 2.02893 -0.60328 0.29437  -0.29096 69  VAL E CG2 
3478 N N   . PRO C 70  ? 1.52438 1.44861 1.80860 -0.48187 0.30617  -0.35135 70  PRO E N   
3479 C CA  . PRO C 70  ? 1.52764 1.52555 1.85348 -0.44562 0.30669  -0.32685 70  PRO E CA  
3480 C C   . PRO C 70  ? 1.54655 1.67084 1.92666 -0.45639 0.28667  -0.29631 70  PRO E C   
3481 O O   . PRO C 70  ? 1.60001 1.74575 1.95624 -0.49317 0.25724  -0.30537 70  PRO E O   
3482 C CB  . PRO C 70  ? 1.57141 1.50649 1.81354 -0.42357 0.28824  -0.36154 70  PRO E CB  
3483 C CG  . PRO C 70  ? 1.58946 1.45402 1.74634 -0.45562 0.26684  -0.40144 70  PRO E CG  
3484 C CD  . PRO C 70  ? 1.54411 1.37508 1.72279 -0.48737 0.28426  -0.39980 70  PRO E CD  
3485 N N   . THR C 71  ? 1.51841 1.72508 1.97090 -0.42538 0.30166  -0.25821 71  THR E N   
3486 C CA  . THR C 71  ? 1.49499 1.83078 2.00789 -0.42909 0.28588  -0.22168 71  THR E CA  
3487 C C   . THR C 71  ? 1.48953 1.87125 2.00488 -0.38774 0.28045  -0.21262 71  THR E C   
3488 O O   . THR C 71  ? 1.52504 1.98730 2.04286 -0.38965 0.25423  -0.20018 71  THR E O   
3489 C CB  . THR C 71  ? 1.36513 1.77827 1.98869 -0.43206 0.31812  -0.16847 71  THR E CB  
3490 O OG1 . THR C 71  ? 1.27603 1.64687 1.92988 -0.39683 0.36267  -0.15596 71  THR E OG1 
3491 C CG2 . THR C 71  ? 1.38204 1.77538 2.01324 -0.47610 0.31830  -0.16794 71  THR E CG2 
3492 N N   . GLU C 72  ? 1.42094 1.75262 1.93656 -0.35127 0.30431  -0.21567 72  GLU E N   
3493 C CA  . GLU C 72  ? 1.40088 1.76742 1.92302 -0.30982 0.30236  -0.20506 72  GLU E CA  
3494 C C   . GLU C 72  ? 1.48752 1.74808 1.93268 -0.29282 0.29784  -0.24147 72  GLU E C   
3495 O O   . GLU C 72  ? 1.46648 1.64603 1.90347 -0.29247 0.31574  -0.25242 72  GLU E O   
3496 C CB  . GLU C 72  ? 1.23252 1.65869 1.85199 -0.28108 0.33703  -0.15959 72  GLU E CB  
3497 N N   . GLU C 73  ? 1.44537 1.70374 1.83107 -0.27814 0.27496  -0.25740 73  GLU E N   
3498 C CA  . GLU C 73  ? 1.53917 1.70455 1.85360 -0.25990 0.27118  -0.28577 73  GLU E CA  
3499 C C   . GLU C 73  ? 1.54174 1.74762 1.85757 -0.21551 0.26837  -0.26864 73  GLU E C   
3500 O O   . GLU C 73  ? 1.53693 1.82466 1.86674 -0.20597 0.25956  -0.25069 73  GLU E O   
3501 C CB  . GLU C 73  ? 1.69495 1.78145 1.90801 -0.28886 0.25099  -0.32935 73  GLU E CB  
3502 N N   . SER C 74  ? 1.64149 1.79325 1.94775 -0.18786 0.27618  -0.26938 74  SER E N   
3503 C CA  . SER C 74  ? 1.64278 1.82322 1.94685 -0.14302 0.27578  -0.25104 74  SER E CA  
3504 C C   . SER C 74  ? 1.69924 1.78990 1.95869 -0.12660 0.27664  -0.26383 74  SER E C   
3505 O O   . SER C 74  ? 1.73874 1.74606 1.95838 -0.15163 0.27449  -0.29091 74  SER E O   
3506 C CB  . SER C 74  ? 1.47501 1.75019 1.88091 -0.11566 0.29044  -0.20521 74  SER E CB  
3507 O OG  . SER C 74  ? 1.37472 1.62216 1.83614 -0.11471 0.30503  -0.19183 74  SER E OG  
3508 N N   . ASN C 75  ? 1.70779 1.81808 1.97737 -0.08303 0.28083  -0.23996 75  ASN E N   
3509 C CA  . ASN C 75  ? 1.75497 1.79178 1.98455 -0.06313 0.28122  -0.24369 75  ASN E CA  
3510 C C   . ASN C 75  ? 1.66150 1.71591 1.97325 -0.04135 0.28688  -0.20640 75  ASN E C   
3511 O O   . ASN C 75  ? 1.55219 1.68619 1.93977 -0.01926 0.29425  -0.17082 75  ASN E O   
3512 C CB  . ASN C 75  ? 1.83294 1.86347 1.99480 -0.02719 0.28367  -0.24278 75  ASN E CB  
3513 C CG  . ASN C 75  ? 1.92390 1.88252 1.97061 -0.05132 0.27576  -0.28801 75  ASN E CG  
3514 O OD1 . ASN C 75  ? 1.91700 1.84375 1.94384 -0.09655 0.26636  -0.31810 75  ASN E OD1 
3515 N ND2 . ASN C 75  ? 1.98766 1.91411 1.95519 -0.01966 0.28224  -0.29088 75  ASN E ND2 
3516 N N   . ILE C 76  ? 1.70992 1.68806 2.00408 -0.04913 0.28159  -0.21333 76  ILE E N   
3517 C CA  . ILE C 76  ? 1.65908 1.63731 2.01787 -0.03520 0.27889  -0.17902 76  ILE E CA  
3518 C C   . ILE C 76  ? 1.71812 1.65477 2.04205 -0.00803 0.27564  -0.16823 76  ILE E C   
3519 O O   . ILE C 76  ? 1.76716 1.62816 2.01368 -0.02041 0.27252  -0.19831 76  ILE E O   
3520 C CB  . ILE C 76  ? 1.64736 1.56987 2.02008 -0.07376 0.27252  -0.19089 76  ILE E CB  
3521 C CG1 . ILE C 76  ? 1.62168 1.53652 2.05133 -0.06459 0.26259  -0.15513 76  ILE E CG1 
3522 C CG2 . ILE C 76  ? 1.63505 1.46123 1.92357 -0.10324 0.26600  -0.23262 76  ILE E CG2 
3523 C CD1 . ILE C 76  ? 1.49634 1.49810 2.01823 -0.04070 0.26978  -0.11190 76  ILE E CD1 
3524 N N   . THR C 77  ? 1.64357 1.63204 2.02656 0.03161  0.27958  -0.12169 77  THR E N   
3525 C CA  . THR C 77  ? 1.68746 1.64576 2.05789 0.06109  0.27932  -0.09763 77  THR E CA  
3526 C C   . THR C 77  ? 1.67231 1.60589 2.09842 0.04355  0.25971  -0.07359 77  THR E C   
3527 O O   . THR C 77  ? 1.58911 1.56587 2.09505 0.03688  0.25285  -0.04734 77  THR E O   
3528 C CB  . THR C 77  ? 1.63453 1.66200 2.03844 0.11689  0.29680  -0.05409 77  THR E CB  
3529 O OG1 . THR C 77  ? 1.48585 1.59460 1.99219 0.12487  0.29631  -0.01679 77  THR E OG1 
3530 C CG2 . THR C 77  ? 1.69245 1.72685 2.01856 0.13113  0.31245  -0.08144 77  THR E CG2 
3531 N N   . MET C 78  ? 1.73674 1.59679 2.11609 0.03419  0.24979  -0.08232 78  MET E N   
3532 C CA  . MET C 78  ? 1.72499 1.55127 2.14134 0.01284  0.22505  -0.06102 78  MET E CA  
3533 C C   . MET C 78  ? 1.76529 1.58029 2.18422 0.04377  0.22275  -0.02317 78  MET E C   
3534 O O   . MET C 78  ? 1.80985 1.60838 2.17129 0.07403  0.24357  -0.02968 78  MET E O   
3535 C CB  . MET C 78  ? 1.68148 1.42029 2.03626 -0.03729 0.21199  -0.10841 78  MET E CB  
3536 C CG  . MET C 78  ? 1.63460 1.36950 1.95554 -0.06220 0.22501  -0.15409 78  MET E CG  
3537 S SD  . MET C 78  ? 1.54547 1.17190 1.78652 -0.11225 0.21770  -0.20584 78  MET E SD  
3538 C CE  . MET C 78  ? 1.53082 1.10797 1.79717 -0.12791 0.18754  -0.17607 78  MET E CE  
3539 N N   . GLN C 79  ? 1.61534 1.43423 2.09848 0.03418  0.19710  0.01839  79  GLN E N   
3540 C CA  . GLN C 79  ? 1.63682 1.45855 2.14522 0.06190  0.19144  0.06827  79  GLN E CA  
3541 C C   . GLN C 79  ? 1.68878 1.42142 2.12568 0.03671  0.17739  0.04422  79  GLN E C   
3542 O O   . GLN C 79  ? 1.66657 1.34640 2.08547 -0.01109 0.15064  0.02024  79  GLN E O   
3543 C CB  . GLN C 79  ? 1.57013 1.44619 2.19071 0.05975  0.16482  0.13200  79  GLN E CB  
3544 C CG  . GLN C 79  ? 1.46080 1.42727 2.16201 0.08772  0.17967  0.16394  79  GLN E CG  
3545 C CD  . GLN C 79  ? 1.37199 1.38344 2.18342 0.07763  0.14996  0.22519  79  GLN E CD  
3546 O OE1 . GLN C 79  ? 1.41190 1.38958 2.23841 0.05116  0.11561  0.24811  79  GLN E OE1 
3547 N NE2 . GLN C 79  ? 1.23215 1.31970 2.12125 0.09656  0.16087  0.25397  79  GLN E NE2 
3548 N N   . ILE C 80  ? 1.76206 1.47285 2.15298 0.07128  0.19874  0.05171  80  ILE E N   
3549 C CA  . ILE C 80  ? 1.80807 1.43910 2.13380 0.05652  0.19118  0.03642  80  ILE E CA  
3550 C C   . ILE C 80  ? 1.82702 1.48469 2.19727 0.09975  0.19670  0.10517  80  ILE E C   
3551 O O   . ILE C 80  ? 1.81044 1.51380 2.19952 0.15281  0.22914  0.13722  80  ILE E O   
3552 C CB  . ILE C 80  ? 1.83061 1.39396 2.04063 0.05561  0.21935  -0.02771 80  ILE E CB  
3553 C CG1 . ILE C 80  ? 1.77106 1.33046 1.95427 0.02064  0.21906  -0.08414 80  ILE E CG1 
3554 C CG2 . ILE C 80  ? 1.85934 1.33709 2.00505 0.03571  0.21079  -0.04538 80  ILE E CG2 
3555 C CD1 . ILE C 80  ? 1.71138 1.23164 1.89918 -0.03259 0.18907  -0.10547 80  ILE E CD1 
3556 N N   . MET C 81  ? 1.87216 1.49970 2.25599 0.07937  0.16723  0.13087  81  MET E N   
3557 C CA  . MET C 81  ? 1.86697 1.52260 2.29974 0.11883  0.17156  0.20352  81  MET E CA  
3558 C C   . MET C 81  ? 1.91845 1.51399 2.25730 0.15380  0.21368  0.18398  81  MET E C   
3559 O O   . MET C 81  ? 1.97238 1.48984 2.23595 0.12798  0.20764  0.14654  81  MET E O   
3560 C CB  . MET C 81  ? 1.87732 1.52525 2.35865 0.07977  0.11951  0.24093  81  MET E CB  
3561 C CG  . MET C 81  ? 1.83096 1.53304 2.39428 0.11814  0.11788  0.33195  81  MET E CG  
3562 S SD  . MET C 81  ? 1.81580 1.54905 2.47873 0.06697  0.04339  0.39415  81  MET E SD  
3563 C CE  . MET C 81  ? 1.66412 1.52011 2.47443 0.12473  0.05547  0.50625  81  MET E CE  
3564 N N   . ARG C 82  ? 2.09452 1.72022 2.43206 0.21390  0.25904  0.20933  82  ARG E N   
3565 C CA  . ARG C 82  ? 2.14145 1.70697 2.39013 0.25663  0.30588  0.20220  82  ARG E CA  
3566 C C   . ARG C 82  ? 2.11776 1.69356 2.41698 0.28549  0.30678  0.27861  82  ARG E C   
3567 O O   . ARG C 82  ? 2.03327 1.68597 2.43089 0.32566  0.31321  0.35886  82  ARG E O   
3568 C CB  . ARG C 82  ? 2.13413 1.71957 2.35318 0.31048  0.35449  0.20240  82  ARG E CB  
3569 C CG  . ARG C 82  ? 2.19981 1.70537 2.28261 0.30149  0.38043  0.11916  82  ARG E CG  
3570 C CD  . ARG C 82  ? 2.19316 1.72705 2.25098 0.34281  0.41521  0.11640  82  ARG E CD  
3571 N NE  . ARG C 82  ? 2.21999 1.70361 2.17503 0.31183  0.41800  0.03447  82  ARG E NE  
3572 C CZ  . ARG C 82  ? 2.22922 1.71265 2.12597 0.33831  0.44534  0.01594  82  ARG E CZ  
3573 N NH1 . ARG C 82  ? 2.22240 1.74353 2.14150 0.40197  0.47922  0.06996  82  ARG E NH1 
3574 N NH2 . ARG C 82  ? 2.23398 1.67844 2.04764 0.29972  0.43796  -0.05554 82  ARG E NH2 
3575 N N   . ILE C 83  ? 2.22444 1.72686 2.46202 0.26496  0.30035  0.25786  83  ILE E N   
3576 C CA  . ILE C 83  ? 2.20560 1.70987 2.47951 0.28972  0.30204  0.32701  83  ILE E CA  
3577 C C   . ILE C 83  ? 2.23569 1.68397 2.42393 0.35234  0.37065  0.32829  83  ILE E C   
3578 O O   . ILE C 83  ? 2.30942 1.66362 2.37641 0.34139  0.39243  0.25905  83  ILE E O   
3579 C CB  . ILE C 83  ? 2.25686 1.70652 2.50246 0.23363  0.25872  0.30293  83  ILE E CB  
3580 C CG1 . ILE C 83  ? 2.25626 1.73778 2.56067 0.16885  0.19368  0.29179  83  ILE E CG1 
3581 C CG2 . ILE C 83  ? 2.23160 1.68863 2.51635 0.26044  0.26015  0.37939  83  ILE E CG2 
3582 C CD1 . ILE C 83  ? 2.16918 1.75557 2.61065 0.17676  0.16604  0.36991  83  ILE E CD1 
3583 N N   . LYS C 84  ? 2.47983 1.50276 3.04301 -0.00784 0.04018  -0.65033 84  LYS E N   
3584 C CA  . LYS C 84  ? 2.40332 1.59391 3.10254 0.11236  -0.07797 -0.71206 84  LYS E CA  
3585 C C   . LYS C 84  ? 2.18606 1.70086 3.20869 0.14039  -0.15218 -0.72639 84  LYS E C   
3586 O O   . LYS C 84  ? 2.19970 1.87033 3.27574 0.02827  -0.07659 -0.71667 84  LYS E O   
3587 C CB  . LYS C 84  ? 2.68730 1.93694 3.14360 0.04492  0.00284  -0.80175 84  LYS E CB  
3588 N N   . PRO C 85  ? 2.13894 1.75729 3.38193 0.29121  -0.30189 -0.74881 85  PRO E N   
3589 C CA  . PRO C 85  ? 1.88843 1.79142 3.44808 0.33363  -0.38970 -0.75618 85  PRO E CA  
3590 C C   . PRO C 85  ? 2.04834 2.24024 3.60595 0.20345  -0.30170 -0.81292 85  PRO E C   
3591 O O   . PRO C 85  ? 1.84585 2.21669 3.59705 0.17518  -0.32042 -0.79095 85  PRO E O   
3592 C CB  . PRO C 85  ? 1.64955 1.62114 3.36037 0.49776  -0.53266 -0.80080 85  PRO E CB  
3593 C CG  . PRO C 85  ? 1.83040 1.48869 3.35260 0.56224  -0.54023 -0.77980 85  PRO E CG  
3594 C CD  . PRO C 85  ? 2.11176 1.65351 3.30497 0.40945  -0.38154 -0.79175 85  PRO E CD  
3595 N N   . HIS C 86  ? 2.07821 2.31874 3.41601 0.12309  -0.20722 -0.89231 86  HIS E N   
3596 C CA  . HIS C 86  ? 2.11776 2.60302 3.39803 -0.01772 -0.09585 -0.96052 86  HIS E CA  
3597 C C   . HIS C 86  ? 2.38227 2.69066 3.29665 -0.14662 0.06892  -0.98504 86  HIS E C   
3598 O O   . HIS C 86  ? 2.50898 2.50980 3.25722 -0.13419 0.09212  -0.92265 86  HIS E O   
3599 C CB  . HIS C 86  ? 1.93448 2.73461 3.38705 0.03211  -0.17558 -1.06318 86  HIS E CB  
3600 C CG  . HIS C 86  ? 1.49576 2.53652 3.26683 0.07595  -0.27050 -1.04370 86  HIS E CG  
3601 N ND1 . HIS C 86  ? 1.36566 2.43462 3.19713 -0.00291 -0.22161 -0.97615 86  HIS E ND1 
3602 C CD2 . HIS C 86  ? 1.28275 2.54208 3.32485 0.18662  -0.41141 -1.08234 86  HIS E CD2 
3603 C CE1 . HIS C 86  ? 1.16880 2.45367 3.28189 0.05697  -0.33062 -0.97207 86  HIS E CE1 
3604 N NE2 . HIS C 86  ? 1.11862 2.51679 3.36076 0.17489  -0.44713 -1.03422 86  HIS E NE2 
3605 N N   . GLN C 87  ? 2.26134 2.75430 3.04451 -0.27165 0.18501  -1.07881 87  GLN E N   
3606 C CA  . GLN C 87  ? 2.42516 2.77413 2.86745 -0.42443 0.36910  -1.09670 87  GLN E CA  
3607 C C   . GLN C 87  ? 2.63587 2.62195 2.81966 -0.39536 0.38474  -1.05904 87  GLN E C   
3608 O O   . GLN C 87  ? 2.70829 2.63742 2.81339 -0.32778 0.32760  -1.11215 87  GLN E O   
3609 C CB  . GLN C 87  ? 2.38857 2.97021 2.70843 -0.52874 0.46482  -1.23733 87  GLN E CB  
3610 N N   . GLY C 88  ? 2.66628 2.40802 2.73153 -0.44453 0.45545  -0.96605 88  GLY E N   
3611 C CA  . GLY C 88  ? 2.88185 2.25683 2.68557 -0.43250 0.48390  -0.92022 88  GLY E CA  
3612 C C   . GLY C 88  ? 2.87669 2.04214 2.68542 -0.45962 0.51828  -0.80858 88  GLY E C   
3613 O O   . GLY C 88  ? 2.67499 1.89345 2.75752 -0.39324 0.42602  -0.74609 88  GLY E O   
3614 N N   . GLN C 89  ? 3.10730 2.01892 2.61026 -0.55643 0.64718  -0.78592 89  GLN E N   
3615 C CA  . GLN C 89  ? 3.12228 1.83086 2.60618 -0.60461 0.70005  -0.69052 89  GLN E CA  
3616 C C   . GLN C 89  ? 3.39732 1.71242 2.59498 -0.59052 0.72418  -0.65215 89  GLN E C   
3617 O O   . GLN C 89  ? 3.50592 1.64728 2.54926 -0.69274 0.83959  -0.60562 89  GLN E O   
3618 C CB  . GLN C 89  ? 3.08632 1.94401 2.51448 -0.78763 0.87727  -0.69728 89  GLN E CB  
3619 C CG  . GLN C 89  ? 2.80767 1.87721 2.55411 -0.80300 0.84668  -0.65098 89  GLN E CG  
3620 C CD  . GLN C 89  ? 2.58920 1.95857 2.61918 -0.70888 0.71546  -0.69368 89  GLN E CD  
3621 O OE1 . GLN C 89  ? 2.40787 1.80699 2.71060 -0.60785 0.58078  -0.64197 89  GLN E OE1 
3622 N NE2 . GLN C 89  ? 2.61003 2.19934 2.57660 -0.74239 0.75294  -0.79458 89  GLN E NE2 
3623 N N   . HIS C 90  ? 3.51671 1.68736 2.63853 -0.46770 0.61816  -0.67167 90  HIS E N   
3624 C CA  . HIS C 90  ? 3.80590 1.59925 2.62666 -0.45577 0.63971  -0.64160 90  HIS E CA  
3625 C C   . HIS C 90  ? 3.78352 1.33096 2.69634 -0.39664 0.58231  -0.54491 90  HIS E C   
3626 O O   . HIS C 90  ? 3.57029 1.18221 2.78614 -0.28499 0.45197  -0.51128 90  HIS E O   
3627 C CB  . HIS C 90  ? 3.92604 1.63406 2.66349 -0.33285 0.52927  -0.68500 90  HIS E CB  
3628 C CG  . HIS C 90  ? 3.70694 1.51909 2.77515 -0.15471 0.34088  -0.67304 90  HIS E CG  
3629 N ND1 . HIS C 90  ? 3.42490 1.58047 2.80947 -0.12660 0.28333  -0.70184 90  HIS E ND1 
3630 C CD2 . HIS C 90  ? 3.73252 1.34759 2.86156 0.00605  0.19874  -0.63822 90  HIS E CD2 
3631 C CE1 . HIS C 90  ? 3.28687 1.44894 2.91045 0.04119  0.11778  -0.68361 90  HIS E CE1 
3632 N NE2 . HIS C 90  ? 3.46366 1.30725 2.94155 0.12445  0.06624  -0.64779 90  HIS E NE2 
3633 N N   . ILE C 91  ? 1.98813 2.21811 1.62525 0.56876  0.09275  -0.25348 91  ILE E N   
3634 C CA  . ILE C 91  ? 1.98351 2.11199 1.73958 0.50948  0.16651  -0.23126 91  ILE E CA  
3635 C C   . ILE C 91  ? 1.93736 2.09460 1.80595 0.53102  0.16943  -0.12235 91  ILE E C   
3636 O O   . ILE C 91  ? 1.84526 2.11255 1.87845 0.53894  0.19829  -0.06486 91  ILE E O   
3637 C CB  . ILE C 91  ? 1.91291 2.05619 1.85600 0.43950  0.26534  -0.27137 91  ILE E CB  
3638 C CG1 . ILE C 91  ? 1.81359 2.10966 1.89030 0.44843  0.28433  -0.25767 91  ILE E CG1 
3639 C CG2 . ILE C 91  ? 1.97523 2.04458 1.79520 0.40807  0.26910  -0.38056 91  ILE E CG2 
3640 C CD1 . ILE C 91  ? 1.72925 2.04324 2.01390 0.37794  0.38694  -0.28666 91  ILE E CD1 
3641 N N   . GLY C 92  ? 1.91167 1.97093 1.69103 0.54001  0.14050  -0.09404 92  GLY E N   
3642 C CA  . GLY C 92  ? 1.87457 1.96055 1.72871 0.56879  0.12896  0.00343  92  GLY E CA  
3643 C C   . GLY C 92  ? 1.84940 1.86581 1.85938 0.51669  0.20509  0.03771  92  GLY E C   
3644 O O   . GLY C 92  ? 1.89101 1.80351 1.88921 0.46236  0.24839  -0.01745 92  GLY E O   
3645 N N   . GLU C 93  ? 1.72054 1.79817 1.87258 0.53702  0.21892  0.12943  93  GLU E N   
3646 C CA  . GLU C 93  ? 1.68249 1.72083 2.01423 0.49628  0.29374  0.17247  93  GLU E CA  
3647 C C   . GLU C 93  ? 1.73289 1.68899 1.96935 0.50635  0.25645  0.19578  93  GLU E C   
3648 O O   . GLU C 93  ? 1.69490 1.69459 1.98270 0.54204  0.23576  0.27301  93  GLU E O   
3649 C CB  . GLU C 93  ? 1.58479 1.73610 2.12602 0.51444  0.33227  0.25849  93  GLU E CB  
3650 N N   . MET C 94  ? 1.80975 1.64488 1.90641 0.47189  0.25038  0.12614  94  MET E N   
3651 C CA  . MET C 94  ? 1.85879 1.60509 1.85455 0.47180  0.21909  0.13835  94  MET E CA  
3652 C C   . MET C 94  ? 1.80956 1.53437 1.99622 0.43015  0.29509  0.17616  94  MET E C   
3653 O O   . MET C 94  ? 1.79138 1.49171 2.10679 0.37653  0.37484  0.14536  94  MET E O   
3654 C CB  . MET C 94  ? 1.96684 1.58547 1.75184 0.44437  0.19445  0.05203  94  MET E CB  
3655 C CG  . MET C 94  ? 2.03532 1.65601 1.59055 0.49880  0.09977  0.02288  94  MET E CG  
3656 S SD  . MET C 94  ? 2.17265 1.62410 1.44570 0.48595  0.04746  -0.04426 94  MET E SD  
3657 C CE  . MET C 94  ? 2.18724 1.63842 1.37299 0.53915  -0.02983 0.02691  94  MET E CE  
3658 N N   . SER C 95  ? 1.84746 1.58384 2.05356 0.45576  0.27031  0.23948  95  SER E N   
3659 C CA  . SER C 95  ? 1.80209 1.52322 2.18096 0.42241  0.33591  0.27453  95  SER E CA  
3660 C C   . SER C 95  ? 1.87184 1.46786 2.14313 0.37806  0.33812  0.22827  95  SER E C   
3661 O O   . SER C 95  ? 1.95501 1.48309 2.01249 0.38776  0.27392  0.19416  95  SER E O   
3662 C CB  . SER C 95  ? 1.72780 1.54429 2.20927 0.47498  0.31372  0.37082  95  SER E CB  
3663 O OG  . SER C 95  ? 1.71540 1.49191 2.25807 0.45401  0.33727  0.39211  95  SER E OG  
3664 N N   . PHE C 96  ? 1.79094 1.35562 2.21319 0.32873  0.41468  0.22708  96  PHE E N   
3665 C CA  . PHE C 96  ? 1.84991 1.30708 2.20457 0.28003  0.43018  0.18779  96  PHE E CA  
3666 C C   . PHE C 96  ? 1.78318 1.27184 2.34236 0.26427  0.48852  0.23541  96  PHE E C   
3667 O O   . PHE C 96  ? 1.69712 1.26817 2.45454 0.27886  0.53313  0.28322  96  PHE E O   
3668 C CB  . PHE C 96  ? 1.90521 1.26277 2.19338 0.21746  0.47359  0.09651  96  PHE E CB  
3669 C CG  . PHE C 96  ? 1.95553 1.29848 2.07718 0.23454  0.42814  0.04619  96  PHE E CG  
3670 C CD1 . PHE C 96  ? 1.91040 1.32303 2.12478 0.24155  0.45463  0.03691  96  PHE E CD1 
3671 C CD2 . PHE C 96  ? 2.05416 1.31426 1.92528 0.24474  0.35845  0.00732  96  PHE E CD2 
3672 C CE1 . PHE C 96  ? 1.95723 1.36707 2.02191 0.25876  0.41193  -0.01359 96  PHE E CE1 
3673 C CE2 . PHE C 96  ? 2.10094 1.35114 1.81695 0.26631  0.31420  -0.04035 96  PHE E CE2 
3674 C CZ  . PHE C 96  ? 2.05027 1.38096 1.86549 0.27387  0.34042  -0.05216 96  PHE E CZ  
3675 N N   . LEU C 97  ? 1.84311 1.26512 2.35013 0.23506  0.48775  0.22160  97  LEU E N   
3676 C CA  . LEU C 97  ? 1.79352 1.24250 2.47977 0.21830  0.54015  0.25693  97  LEU E CA  
3677 C C   . LEU C 97  ? 1.80321 1.18718 2.58180 0.14723  0.62829  0.19825  97  LEU E C   
3678 O O   . LEU C 97  ? 1.87896 1.16625 2.52183 0.10168  0.63414  0.12424  97  LEU E O   
3679 C CB  . LEU C 97  ? 1.85432 1.27492 2.43865 0.22198  0.49266  0.26943  97  LEU E CB  
3680 C CG  . LEU C 97  ? 1.83659 1.27060 2.56397 0.19642  0.53905  0.28837  97  LEU E CG  
3681 C CD1 . LEU C 97  ? 1.70549 1.26297 2.65528 0.24358  0.56205  0.36864  97  LEU E CD1 
3682 C CD2 . LEU C 97  ? 1.93070 1.32308 2.50843 0.19404  0.48226  0.28469  97  LEU E CD2 
3683 N N   . GLN C 98  ? 1.64062 1.07626 2.64685 0.13974  0.69675  0.23019  98  GLN E N   
3684 C CA  . GLN C 98  ? 1.64853 1.02578 2.75023 0.07375  0.78057  0.17490  98  GLN E CA  
3685 C C   . GLN C 98  ? 1.61656 1.02770 2.88050 0.06783  0.82074  0.20968  98  GLN E C   
3686 O O   . GLN C 98  ? 1.55254 1.05129 2.91473 0.11990  0.80065  0.28510  98  GLN E O   
3687 C CB  . GLN C 98  ? 1.58810 0.98134 2.82110 0.05938  0.84301  0.15594  98  GLN E CB  
3688 C CG  . GLN C 98  ? 1.49090 0.97859 2.95444 0.09521  0.88231  0.22764  98  GLN E CG  
3689 C CD  . GLN C 98  ? 1.45723 1.02990 2.90468 0.16195  0.82618  0.29340  98  GLN E CD  
3690 O OE1 . GLN C 98  ? 1.50258 1.06987 2.76621 0.18551  0.75323  0.28544  98  GLN E OE1 
3691 N NE2 . GLN C 98  ? 1.38491 1.04031 3.01673 0.18947  0.85854  0.35720  98  GLN E NE2 
3692 N N   . HIS C 99  ? 1.46729 0.82528 2.75358 0.00618  0.87490  0.14770  99  HIS E N   
3693 C CA  . HIS C 99  ? 1.45102 0.85897 2.85130 -0.00367 0.90407  0.14986  99  HIS E CA  
3694 C C   . HIS C 99  ? 1.41701 0.89798 3.00358 0.00913  0.96081  0.13796  99  HIS E C   
3695 O O   . HIS C 99  ? 1.45441 0.90656 3.02734 -0.02461 0.99598  0.06675  99  HIS E O   
3696 C CB  . HIS C 99  ? 1.52649 0.85297 2.78922 -0.06474 0.90699  0.07684  99  HIS E CB  
3697 C CG  . HIS C 99  ? 1.60436 0.84368 2.68301 -0.07198 0.85087  0.08662  99  HIS E CG  
3698 N ND1 . HIS C 99  ? 1.72931 0.86802 2.62286 -0.12656 0.84071  0.01970  99  HIS E ND1 
3699 C CD2 . HIS C 99  ? 1.59752 0.87681 2.61570 -0.01674 0.78013  0.14705  99  HIS E CD2 
3700 C CE1 . HIS C 99  ? 1.80525 0.90479 2.53799 -0.10919 0.77302  0.03911  99  HIS E CE1 
3701 N NE2 . HIS C 99  ? 1.72578 0.92407 2.52631 -0.03962 0.72925  0.11322  99  HIS E NE2 
3702 N N   . ASN C 100 ? 1.44780 1.46544 1.97045 0.01641  0.47400  0.08348  100 ASN E N   
3703 C CA  . ASN C 100 ? 1.46135 1.41865 1.98387 0.01599  0.46696  0.09299  100 ASN E CA  
3704 C C   . ASN C 100 ? 1.46150 1.39774 2.00498 0.02104  0.45847  0.03125  100 ASN E C   
3705 O O   . ASN C 100 ? 1.46287 1.34841 2.01464 -0.00402 0.45615  0.02240  100 ASN E O   
3706 C CB  . ASN C 100 ? 1.49096 1.44232 1.98595 0.06388  0.45882  0.13040  100 ASN E CB  
3707 C CG  . ASN C 100 ? 1.49778 1.48440 1.97213 0.06047  0.46846  0.19108  100 ASN E CG  
3708 O OD1 . ASN C 100 ? 1.47818 1.52637 1.95309 0.06415  0.47392  0.18903  100 ASN E OD1 
3709 N ND2 . ASN C 100 ? 1.53710 1.48410 1.98959 0.05287  0.47049  0.24564  100 ASN E ND2 
3710 N N   . LYS C 101 ? 1.43829 1.41907 1.99124 0.05304  0.45313  -0.01501 101 LYS E N   
3711 C CA  . LYS C 101 ? 1.44263 1.42367 2.01630 0.06503  0.44440  -0.07590 101 LYS E CA  
3712 C C   . LYS C 101 ? 1.44070 1.47941 2.03584 0.05204  0.45111  -0.12878 101 LYS E C   
3713 O O   . LYS C 101 ? 1.44903 1.52746 2.03670 0.06534  0.45311  -0.12659 101 LYS E O   
3714 C CB  . LYS C 101 ? 1.46398 1.44125 2.02351 0.12910  0.42638  -0.08207 101 LYS E CB  
3715 C CG  . LYS C 101 ? 1.48999 1.38825 2.03236 0.13788  0.41559  -0.06384 101 LYS E CG  
3716 C CD  . LYS C 101 ? 1.52597 1.40806 2.03804 0.20737  0.39763  -0.05559 101 LYS E CD  
3717 C CE  . LYS C 101 ? 1.57522 1.35368 2.05278 0.20858  0.38944  -0.01352 101 LYS E CE  
3718 N NZ  . LYS C 101 ? 1.58379 1.31575 2.07620 0.18669  0.38269  -0.05236 101 LYS E NZ  
3719 N N   . CYS C 102 ? 1.40523 1.44693 2.02416 0.02543  0.45434  -0.17680 102 CYS E N   
3720 C CA  . CYS C 102 ? 1.41710 1.50988 2.05534 0.00591  0.46250  -0.22960 102 CYS E CA  
3721 C C   . CYS C 102 ? 1.41600 1.55133 2.07792 0.03604  0.45124  -0.29081 102 CYS E C   
3722 O O   . CYS C 102 ? 1.41060 1.52915 2.06894 0.07733  0.43551  -0.29173 102 CYS E O   
3723 C CB  . CYS C 102 ? 1.41494 1.49123 2.05913 -0.05471 0.47937  -0.23586 102 CYS E CB  
3724 S SG  . CYS C 102 ? 1.41079 1.44768 2.02708 -0.08618 0.49052  -0.16947 102 CYS E SG  
3725 N N   . GLU C 103 ? 1.39330 1.58393 2.07638 0.01464  0.45918  -0.34322 103 GLU E N   
3726 C CA  . GLU C 103 ? 1.38593 1.64120 2.09672 0.03995  0.44990  -0.40863 103 GLU E CA  
3727 C C   . GLU C 103 ? 1.39765 1.70443 2.13107 -0.01174 0.46692  -0.45832 103 GLU E C   
3728 O O   . GLU C 103 ? 1.42743 1.71056 2.14661 -0.05625 0.48277  -0.43891 103 GLU E O   
3729 C CB  . GLU C 103 ? 1.39445 1.68764 2.10021 0.10342  0.43213  -0.41546 103 GLU E CB  
3730 C CG  . GLU C 103 ? 1.38096 1.71093 2.09849 0.15997  0.41234  -0.45706 103 GLU E CG  
3731 C CD  . GLU C 103 ? 1.39222 1.73129 2.08774 0.23167  0.39314  -0.43938 103 GLU E CD  
3732 O OE1 . GLU C 103 ? 1.39923 1.67110 2.05975 0.24956  0.39004  -0.37346 103 GLU E OE1 
3733 O OE2 . GLU C 103 ? 1.39205 1.81137 2.10481 0.26867  0.38193  -0.49167 103 GLU E OE2 
3734 N N   . CYS C 104 ? 1.25856 1.63642 2.02354 -0.00466 0.46335  -0.52280 104 CYS E N   
3735 C CA  . CYS C 104 ? 1.26246 1.70145 2.05196 -0.05741 0.48079  -0.57557 104 CYS E CA  
3736 C C   . CYS C 104 ? 1.27381 1.79217 2.08226 -0.03165 0.47144  -0.62181 104 CYS E C   
3737 O O   . CYS C 104 ? 1.24277 1.82661 2.07318 0.01716  0.45466  -0.66380 104 CYS E O   
3738 C CB  . CYS C 104 ? 1.21693 1.69449 2.03208 -0.07469 0.48578  -0.61837 104 CYS E CB  
3739 S SG  . CYS C 104 ? 1.20523 1.61518 2.00389 -0.13732 0.50719  -0.58434 104 CYS E SG  
3740 N N   . ARG C 105 ? 1.28888 1.80008 2.08554 -0.05958 0.47975  -0.61592 105 ARG E N   
3741 C CA  . ARG C 105 ? 1.30679 1.88641 2.11862 -0.03716 0.46926  -0.65786 105 ARG E CA  
3742 C C   . ARG C 105 ? 1.35384 1.95361 2.17229 -0.10761 0.48815  -0.69281 105 ARG E C   
3743 O O   . ARG C 105 ? 1.39247 1.92552 2.18559 -0.16377 0.50756  -0.66381 105 ARG E O   
3744 C CB  . ARG C 105 ? 1.33443 1.87649 2.11574 0.01724  0.45257  -0.61207 105 ARG E CB  
3745 C CG  . ARG C 105 ? 1.29421 1.82368 2.06573 0.09073  0.43257  -0.58226 105 ARG E CG  
3746 C CD  . ARG C 105 ? 1.30765 1.85372 2.06187 0.15466  0.41349  -0.56769 105 ARG E CD  
3747 N NE  . ARG C 105 ? 1.28150 1.80822 2.01726 0.22455  0.39558  -0.53544 105 ARG E NE  
3748 C CZ  . ARG C 105 ? 1.28985 1.79794 1.99450 0.27677  0.38350  -0.49153 105 ARG E CZ  
3749 N NH1 . ARG C 105 ? 1.31009 1.82684 2.00226 0.27496  0.38437  -0.48034 105 ARG E NH1 
3750 N NH2 . ARG C 105 ? 1.28117 1.75751 1.96191 0.33269  0.37004  -0.45715 105 ARG E NH2 
3751 N N   . PRO C 106 ? 1.34978 2.03802 2.19817 -0.10637 0.48232  -0.75533 106 PRO E N   
3752 C CA  . PRO C 106 ? 1.39345 2.10260 2.25013 -0.18370 0.50180  -0.79547 106 PRO E CA  
3753 C C   . PRO C 106 ? 1.49045 2.09960 2.29833 -0.21511 0.50867  -0.75386 106 PRO E C   
3754 O O   . PRO C 106 ? 1.52402 2.07871 2.30026 -0.16743 0.49379  -0.70799 106 PRO E O   
3755 C CB  . PRO C 106 ? 1.36946 2.19800 2.26861 -0.16105 0.48742  -0.86876 106 PRO E CB  
3756 C CG  . PRO C 106 ? 1.30017 2.16974 2.20393 -0.08835 0.45373  -0.86465 106 PRO E CG  
3757 C CD  . PRO C 106 ? 1.30153 2.08087 2.17638 -0.03919 0.45547  -0.79653 106 PRO E CD  
3758 N N   . LYS C 107 ? 1.60642 2.19255 2.40433 -0.29592 0.53171  -0.77110 107 LYS E N   
3759 C CA  . LYS C 107 ? 1.64494 2.12550 2.38757 -0.33276 0.53975  -0.73735 107 LYS E CA  
3760 C C   . LYS C 107 ? 1.70870 2.20429 2.44871 -0.32639 0.52519  -0.77272 107 LYS E C   
3761 O O   . LYS C 107 ? 1.72127 2.31714 2.50578 -0.29564 0.51001  -0.82435 107 LYS E O   
3762 C CB  . LYS C 107 ? 1.54179 1.98252 2.26621 -0.42193 0.57071  -0.74070 107 LYS E CB  
3763 C CG  . LYS C 107 ? 1.52226 1.82786 2.17373 -0.44795 0.57990  -0.68482 107 LYS E CG  
3764 C CD  . LYS C 107 ? 1.39297 1.65842 2.02178 -0.52256 0.61062  -0.67620 107 LYS E CD  
3765 C CE  . LYS C 107 ? 1.32955 1.65748 1.99764 -0.51495 0.61848  -0.67621 107 LYS E CE  
3766 N NZ  . LYS C 107 ? 1.24256 1.54668 1.88575 -0.58456 0.64584  -0.67454 107 LYS E NZ  
3767 N N   . LYS C 108 ? 1.67239 2.06629 2.35623 -0.35281 0.52807  -0.74735 108 LYS E N   
3768 C CA  . LYS C 108 ? 1.72589 2.11089 2.39587 -0.35231 0.51346  -0.77964 108 LYS E CA  
3769 C C   . LYS C 108 ? 1.69730 1.95703 2.30043 -0.41411 0.52649  -0.76272 108 LYS E C   
3770 O O   . LYS C 108 ? 1.76122 1.95096 2.31739 -0.38795 0.50976  -0.74841 108 LYS E O   
3771 C CB  . LYS C 108 ? 1.81801 2.20723 2.47715 -0.25994 0.48354  -0.75442 108 LYS E CB  
3772 N N   . HIS D 11  ? 2.94628 2.22730 2.17670 0.41216  -0.09598 0.67457  11  HIS F N   
3773 C CA  . HIS D 11  ? 2.89172 2.33409 2.33966 0.40218  -0.12620 0.79148  11  HIS F CA  
3774 C C   . HIS D 11  ? 2.79195 2.28493 2.35719 0.35525  -0.14080 0.78037  11  HIS F C   
3775 O O   . HIS D 11  ? 2.74649 2.38080 2.49937 0.33693  -0.19253 0.88003  11  HIS F O   
3776 C CB  . HIS D 11  ? 2.99258 2.48603 2.47848 0.36989  -0.27562 0.87198  11  HIS F CB  
3777 N N   . HIS D 12  ? 2.75248 2.13756 2.21615 0.33565  -0.09443 0.66741  12  HIS F N   
3778 C CA  . HIS D 12  ? 2.65663 2.07522 2.21405 0.27948  -0.11694 0.63776  12  HIS F CA  
3779 C C   . HIS D 12  ? 2.55268 1.92465 2.09948 0.30653  0.03798  0.58352  12  HIS F C   
3780 O O   . HIS D 12  ? 2.57545 1.85032 2.00044 0.35888  0.14167  0.54873  12  HIS F O   
3781 C CB  . HIS D 12  ? 2.83617 2.15334 2.27515 0.21157  -0.23446 0.54767  12  HIS F CB  
3782 C CG  . HIS D 12  ? 2.76161 1.93730 2.05353 0.20434  -0.14993 0.42589  12  HIS F CG  
3783 N ND1 . HIS D 12  ? 2.76815 1.80394 1.85625 0.24395  -0.09525 0.36415  12  HIS F ND1 
3784 C CD2 . HIS D 12  ? 2.63986 1.79623 1.96581 0.15880  -0.11483 0.36307  12  HIS F CD2 
3785 C CE1 . HIS D 12  ? 2.71656 1.65116 1.72134 0.22562  -0.02546 0.27737  12  HIS F CE1 
3786 N NE2 . HIS D 12  ? 2.60526 1.60517 1.74790 0.17011  -0.03678 0.27027  12  HIS F NE2 
3787 N N   . GLU D 13  ? 2.49074 1.93107 2.16982 0.26879  0.04592  0.58194  13  GLU F N   
3788 C CA  . GLU D 13  ? 2.33913 1.74132 2.02936 0.28886  0.18374  0.54221  13  GLU F CA  
3789 C C   . GLU D 13  ? 2.25802 1.61578 1.94944 0.20916  0.16085  0.45279  13  GLU F C   
3790 O O   . GLU D 13  ? 2.35563 1.77967 2.12288 0.14279  0.03624  0.45342  13  GLU F O   
3791 C CB  . GLU D 13  ? 2.26712 1.81793 2.14275 0.34041  0.24706  0.64747  13  GLU F CB  
3792 N N   . VAL D 14  ? 2.42064 1.65848 2.02607 0.21333  0.27633  0.37947  14  VAL F N   
3793 C CA  . VAL D 14  ? 2.31775 1.50090 1.92154 0.13810  0.28101  0.29366  14  VAL F CA  
3794 C C   . VAL D 14  ? 2.10763 1.28539 1.78111 0.15643  0.40972  0.29423  14  VAL F C   
3795 O O   . VAL D 14  ? 2.05255 1.18127 1.68089 0.23220  0.51193  0.32555  14  VAL F O   
3796 C CB  . VAL D 14  ? 2.30486 1.30478 1.69285 0.11330  0.28363  0.19570  14  VAL F CB  
3797 C CG1 . VAL D 14  ? 2.14339 1.07451 1.52577 0.03802  0.31172  0.11171  14  VAL F CG1 
3798 C CG2 . VAL D 14  ? 2.55265 1.54879 1.86111 0.09676  0.14756  0.18876  14  VAL F CG2 
3799 N N   . VAL D 15  ? 2.18563 1.40542 1.96307 0.08634  0.39935  0.25751  15  VAL F N   
3800 C CA  . VAL D 15  ? 2.00290 1.20601 1.84227 0.08994  0.51194  0.24669  15  VAL F CA  
3801 C C   . VAL D 15  ? 1.88537 0.93096 1.61785 0.01719  0.55011  0.14055  15  VAL F C   
3802 O O   . VAL D 15  ? 1.86931 0.92551 1.61316 -0.06629 0.46660  0.08513  15  VAL F O   
3803 C CB  . VAL D 15  ? 1.95431 1.36075 2.03284 0.06979  0.47586  0.30618  15  VAL F CB  
3804 C CG1 . VAL D 15  ? 1.77160 1.15163 1.89932 0.08556  0.59897  0.29644  15  VAL F CG1 
3805 C CG2 . VAL D 15  ? 2.05086 1.62191 2.24353 0.13902  0.42981  0.42929  15  VAL F CG2 
3806 N N   . LYS D 16  ? 2.25783 1.15100 1.88464 0.04890  0.67128  0.11864  16  LYS F N   
3807 C CA  . LYS D 16  ? 2.10214 0.99486 1.65925 -0.01037 0.67149  0.02416  16  LYS F CA  
3808 C C   . LYS D 16  ? 1.93505 0.97644 1.64262 -0.07548 0.63605  -0.01606 16  LYS F C   
3809 O O   . LYS D 16  ? 1.90282 1.01051 1.75591 -0.06351 0.65951  0.02025  16  LYS F O   
3810 C CB  . LYS D 16  ? 2.06320 0.98947 1.53559 0.03435  0.73444  0.02604  16  LYS F CB  
3811 N N   . PHE D 17  ? 1.20781 1.35860 1.81355 0.01741  0.28425  0.26271  17  PHE F N   
3812 C CA  . PHE D 17  ? 1.35520 1.40642 1.87244 0.02016  0.33307  0.23374  17  PHE F CA  
3813 C C   . PHE D 17  ? 1.62086 1.52843 2.06445 0.03441  0.29207  0.22382  17  PHE F C   
3814 O O   . PHE D 17  ? 1.72121 1.55208 2.07910 0.03795  0.33894  0.17428  17  PHE F O   
3815 C CB  . PHE D 17  ? 1.28584 1.35827 1.82707 0.02215  0.34647  0.28615  17  PHE F CB  
3816 C CG  . PHE D 17  ? 1.42828 1.39094 1.89355 0.02802  0.38084  0.27607  17  PHE F CG  
3817 C CD1 . PHE D 17  ? 1.47738 1.38239 1.86196 0.02122  0.44666  0.20653  17  PHE F CD1 
3818 C CD2 . PHE D 17  ? 1.48066 1.40581 1.96424 0.03768  0.34390  0.34614  17  PHE F CD2 
3819 C CE1 . PHE D 17  ? 1.57106 1.37903 1.89216 0.02546  0.47594  0.20371  17  PHE F CE1 
3820 C CE2 . PHE D 17  ? 1.57904 1.40964 2.00021 0.04230  0.37333  0.34471  17  PHE F CE2 
3821 C CZ  . PHE D 17  ? 1.62545 1.39520 1.96376 0.03692  0.44012  0.27142  17  PHE F CZ  
3822 N N   . MET D 18  ? 1.47287 1.33755 1.94196 0.04023  0.20169  0.27379  18  MET F N   
3823 C CA  . MET D 18  ? 1.59779 1.30857 1.97555 0.05169  0.15401  0.26096  18  MET F CA  
3824 C C   . MET D 18  ? 1.66829 1.33205 1.97187 0.07107  0.19408  0.18405  18  MET F C   
3825 O O   . MET D 18  ? 1.73674 1.29839 1.93502 0.08224  0.22267  0.14555  18  MET F O   
3826 C CB  . MET D 18  ? 1.58285 1.25492 2.00150 0.04859  0.04015  0.32145  18  MET F CB  
3827 C CG  . MET D 18  ? 1.57382 1.20158 2.00356 0.03220  -0.02166 0.39961  18  MET F CG  
3828 S SD  . MET D 18  ? 1.69056 1.15663 1.98200 0.03183  -0.01691 0.38121  18  MET F SD  
3829 C CE  . MET D 18  ? 1.81648 1.14996 1.97265 0.05754  -0.01251 0.28516  18  MET F CE  
3830 N N   . ASP D 19  ? 1.58712 1.34373 1.95173 0.07574  0.20675  0.16695  19  ASP F N   
3831 C CA  . ASP D 19  ? 1.63904 1.38050 1.95620 0.09866  0.25191  0.10713  19  ASP F CA  
3832 C C   . ASP D 19  ? 1.62161 1.39581 1.89854 0.08793  0.34834  0.06463  19  ASP F C   
3833 O O   . ASP D 19  ? 1.65101 1.36018 1.84585 0.10855  0.38686  0.02384  19  ASP F O   
3834 C CB  . ASP D 19  ? 1.57212 1.42504 1.98584 0.10249  0.23968  0.11485  19  ASP F CB  
3835 C CG  . ASP D 19  ? 1.53145 1.35745 1.99834 0.10771  0.14062  0.16425  19  ASP F CG  
3836 O OD1 . ASP D 19  ? 1.60412 1.28776 2.00216 0.11724  0.07849  0.17504  19  ASP F OD1 
3837 O OD2 . ASP D 19  ? 1.37785 1.32399 1.95397 0.09766  0.12027  0.19628  19  ASP F OD2 
3838 N N   . VAL D 20  ? 1.70109 1.57511 2.03190 0.05654  0.38866  0.07467  20  VAL F N   
3839 C CA  . VAL D 20  ? 1.60981 1.50406 1.90270 0.03828  0.47231  0.03610  20  VAL F CA  
3840 C C   . VAL D 20  ? 1.73075 1.49881 1.92468 0.04736  0.49081  0.02351  20  VAL F C   
3841 O O   . VAL D 20  ? 1.71831 1.45582 1.85212 0.05298  0.54004  -0.01217 20  VAL F O   
3842 C CB  . VAL D 20  ? 1.37899 1.36790 1.72402 0.00484  0.50359  0.04721  20  VAL F CB  
3843 C CG1 . VAL D 20  ? 1.34976 1.34100 1.64927 -0.02041 0.58089  0.00534  20  VAL F CG1 
3844 C CG2 . VAL D 20  ? 1.15735 1.27789 1.59532 -0.00641 0.48043  0.06531  20  VAL F CG2 
3845 N N   . TYR D 21  ? 1.56085 1.26448 1.74307 0.04788  0.45091  0.06167  21  TYR F N   
3846 C CA  . TYR D 21  ? 1.64425 1.23025 1.73562 0.05418  0.45915  0.05937  21  TYR F CA  
3847 C C   . TYR D 21  ? 1.70668 1.19823 1.70883 0.08280  0.43986  0.03056  21  TYR F C   
3848 O O   . TYR D 21  ? 1.72316 1.15418 1.64137 0.08982  0.48312  0.00392  21  TYR F O   
3849 C CB  . TYR D 21  ? 1.67229 1.21641 1.78070 0.05002  0.40571  0.12029  21  TYR F CB  
3850 C CG  . TYR D 21  ? 1.69947 1.14658 1.73369 0.04830  0.42214  0.13051  21  TYR F CG  
3851 C CD1 . TYR D 21  ? 1.76445 1.09755 1.69440 0.06091  0.39949  0.11374  21  TYR F CD1 
3852 C CD2 . TYR D 21  ? 1.66338 1.13018 1.72797 0.03743  0.46042  0.15990  21  TYR F CD2 
3853 C CE1 . TYR D 21  ? 1.79070 1.04363 1.65455 0.05607  0.41141  0.12915  21  TYR F CE1 
3854 C CE2 . TYR D 21  ? 1.68221 1.06560 1.69008 0.03623  0.47401  0.17743  21  TYR F CE2 
3855 C CZ  . TYR D 21  ? 1.74595 1.02820 1.65692 0.04217  0.44704  0.16421  21  TYR F CZ  
3856 O OH  . TYR D 21  ? 1.77384 0.98086 1.62935 0.03769  0.45788  0.18726  21  TYR F OH  
3857 N N   . GLN D 22  ? 1.77659 1.24954 1.79045 0.10253  0.37613  0.03676  22  GLN F N   
3858 C CA  . GLN D 22  ? 1.84256 1.19772 1.75050 0.13846  0.35314  0.00743  22  GLN F CA  
3859 C C   . GLN D 22  ? 1.80097 1.19315 1.67764 0.16300  0.43201  -0.04167 22  GLN F C   
3860 O O   . GLN D 22  ? 1.82159 1.13403 1.59084 0.18559  0.46473  -0.06815 22  GLN F O   
3861 C CB  . GLN D 22  ? 1.87826 1.19585 1.80991 0.15385  0.26468  0.02566  22  GLN F CB  
3862 C CG  . GLN D 22  ? 1.98862 1.13095 1.78796 0.18155  0.20653  0.01062  22  GLN F CG  
3863 C CD  . GLN D 22  ? 2.05303 1.10518 1.80362 0.15338  0.14969  0.05112  22  GLN F CD  
3864 O OE1 . GLN D 22  ? 2.13310 1.05656 1.75014 0.16425  0.14086  0.03248  22  GLN F OE1 
3865 N NE2 . GLN D 22  ? 1.99674 1.12761 1.85790 0.11770  0.11615  0.11278  22  GLN F NE2 
3866 N N   . ARG D 23  ? 1.85793 1.38076 1.83093 0.15772  0.46293  -0.04643 23  ARG F N   
3867 C CA  . ARG D 23  ? 1.79887 1.37688 1.76478 0.18173  0.52975  -0.07735 23  ARG F CA  
3868 C C   . ARG D 23  ? 1.69938 1.31970 1.64619 0.15703  0.61036  -0.09020 23  ARG F C   
3869 O O   . ARG D 23  ? 1.69198 1.31901 1.59511 0.18263  0.66496  -0.10873 23  ARG F O   
3870 C CB  . ARG D 23  ? 1.71856 1.43318 1.80474 0.17571  0.52871  -0.06630 23  ARG F CB  
3871 C CG  . ARG D 23  ? 1.79654 1.47091 1.90655 0.20609  0.45380  -0.05246 23  ARG F CG  
3872 C CD  . ARG D 23  ? 1.64158 1.47047 1.88516 0.18929  0.45295  -0.03101 23  ARG F CD  
3873 N NE  . ARG D 23  ? 1.47617 1.40044 1.74513 0.20157  0.52556  -0.04595 23  ARG F NE  
3874 C CZ  . ARG D 23  ? 1.24729 1.32890 1.62834 0.17668  0.54343  -0.02706 23  ARG F CZ  
3875 N NH1 . ARG D 23  ? 1.13401 1.29427 1.60522 0.14308  0.49732  0.00232  23  ARG F NH1 
3876 N NH2 . ARG D 23  ? 1.14382 1.31352 1.54870 0.18442  0.60760  -0.03082 23  ARG F NH2 
3877 N N   . SER D 24  ? 1.95874 1.04839 1.28520 -0.17121 0.00942  -0.35147 24  SER F N   
3878 C CA  . SER D 24  ? 1.99706 1.07081 1.41858 -0.19988 -0.01075 -0.34436 24  SER F CA  
3879 C C   . SER D 24  ? 1.97753 0.98119 1.48251 -0.22281 -0.06502 -0.27961 24  SER F C   
3880 O O   . SER D 24  ? 1.96296 0.94152 1.62209 -0.23001 -0.07859 -0.28512 24  SER F O   
3881 C CB  . SER D 24  ? 1.99260 1.10207 1.53232 -0.19326 0.02046  -0.41897 24  SER F CB  
3882 O OG  . SER D 24  ? 1.91944 1.01471 1.54792 -0.17387 0.02594  -0.44841 24  SER F OG  
3883 N N   . TYR D 25  ? 2.10215 1.07957 1.50918 -0.23603 -0.09278 -0.21831 25  TYR F N   
3884 C CA  . TYR D 25  ? 2.08242 1.00733 1.56284 -0.26639 -0.15048 -0.14478 25  TYR F CA  
3885 C C   . TYR D 25  ? 2.10003 1.01853 1.50950 -0.30702 -0.17564 -0.08915 25  TYR F C   
3886 O O   . TYR D 25  ? 2.12587 1.07595 1.44091 -0.30740 -0.14557 -0.11409 25  TYR F O   
3887 C CB  . TYR D 25  ? 2.05381 0.95593 1.49807 -0.26330 -0.17178 -0.11112 25  TYR F CB  
3888 C CG  . TYR D 25  ? 2.03540 0.89739 1.60416 -0.28635 -0.22893 -0.04512 25  TYR F CG  
3889 C CD1 . TYR D 25  ? 2.03538 0.88090 1.78737 -0.26969 -0.23324 -0.06326 25  TYR F CD1 
3890 C CD2 . TYR D 25  ? 2.04352 0.88984 1.55411 -0.32878 -0.27722 0.03760  25  TYR F CD2 
3891 C CE1 . TYR D 25  ? 2.03647 0.84939 1.92108 -0.28879 -0.28542 0.00575  25  TYR F CE1 
3892 C CE2 . TYR D 25  ? 2.05191 0.87392 1.68276 -0.35273 -0.33393 0.10942  25  TYR F CE2 
3893 C CZ  . TYR D 25  ? 2.04600 0.85052 1.86984 -0.32977 -0.33879 0.09689  25  TYR F CZ  
3894 O OH  . TYR D 25  ? 2.06774 0.85206 2.02718 -0.35111 -0.39458 0.17600  25  TYR F OH  
3895 N N   . CYS D 26  ? 2.19780 1.08134 1.66921 -0.34146 -0.22964 -0.01493 26  CYS F N   
3896 C CA  . CYS D 26  ? 2.20139 1.07885 1.60636 -0.38803 -0.26084 0.04869  26  CYS F CA  
3897 C C   . CYS D 26  ? 2.20181 1.09190 1.41527 -0.40484 -0.25067 0.06262  26  CYS F C   
3898 O O   . CYS D 26  ? 2.19032 1.06978 1.35872 -0.41527 -0.26879 0.09261  26  CYS F O   
3899 C CB  . CYS D 26  ? 2.21787 1.06385 1.73755 -0.42281 -0.32528 0.13562  26  CYS F CB  
3900 S SG  . CYS D 26  ? 2.24778 1.09091 1.73102 -0.48272 -0.36567 0.21437  26  CYS F SG  
3901 N N   . HIS D 27  ? 2.22076 1.13481 1.32702 -0.40954 -0.21802 0.03871  27  HIS F N   
3902 C CA  . HIS D 27  ? 2.20603 1.13265 1.14105 -0.42197 -0.19300 0.03961  27  HIS F CA  
3903 C C   . HIS D 27  ? 2.21232 1.16370 1.06576 -0.43200 -0.16351 0.02325  27  HIS F C   
3904 O O   . HIS D 27  ? 2.21401 1.18665 1.12769 -0.41102 -0.14472 -0.01506 27  HIS F O   
3905 C CB  . HIS D 27  ? 2.22020 1.16131 1.11101 -0.37626 -0.14818 -0.01318 27  HIS F CB  
3906 C CG  . HIS D 27  ? 2.23166 1.21311 1.13158 -0.33033 -0.09636 -0.08228 27  HIS F CG  
3907 N ND1 . HIS D 27  ? 2.27701 1.27048 1.29712 -0.29673 -0.08859 -0.12649 27  HIS F ND1 
3908 C CD2 . HIS D 27  ? 2.14384 1.16388 0.95085 -0.31644 -0.04919 -0.11273 27  HIS F CD2 
3909 C CE1 . HIS D 27  ? 2.26138 1.30509 1.25402 -0.26820 -0.04143 -0.18087 27  HIS F CE1 
3910 N NE2 . HIS D 27  ? 2.13378 1.19549 1.00126 -0.27704 -0.01852 -0.16969 27  HIS F NE2 
3911 N N   . PRO D 28  ? 2.38810 1.34039 1.10741 -0.46701 -0.15572 0.04806  28  PRO F N   
3912 C CA  . PRO D 28  ? 2.38848 1.36589 1.03093 -0.47420 -0.12249 0.03031  28  PRO F CA  
3913 C C   . PRO D 28  ? 2.33696 1.35505 0.95402 -0.41956 -0.06082 -0.03569 28  PRO F C   
3914 O O   . PRO D 28  ? 2.31489 1.33918 0.88004 -0.39399 -0.02843 -0.05617 28  PRO F O   
3915 C CB  . PRO D 28  ? 2.40083 1.36734 0.90854 -0.52542 -0.12192 0.06715  28  PRO F CB  
3916 C CG  . PRO D 28  ? 2.42215 1.36068 0.95934 -0.56197 -0.17664 0.12203  28  PRO F CG  
3917 C CD  . PRO D 28  ? 2.39874 1.33080 1.04007 -0.51269 -0.18106 0.09791  28  PRO F CD  
3918 N N   . ILE D 29  ? 2.39629 1.44709 1.05299 -0.40469 -0.04477 -0.06569 29  ILE F N   
3919 C CA  . ILE D 29  ? 2.33772 1.44470 0.97823 -0.35978 0.00866  -0.12097 29  ILE F CA  
3920 C C   . ILE D 29  ? 2.34452 1.48640 0.92264 -0.37391 0.03302  -0.11922 29  ILE F C   
3921 O O   . ILE D 29  ? 2.38733 1.50876 0.96761 -0.41349 0.00545  -0.09513 29  ILE F O   
3922 C CB  . ILE D 29  ? 2.28908 1.42237 1.05351 -0.33109 0.00840  -0.16539 29  ILE F CB  
3923 C CG1 . ILE D 29  ? 2.23520 1.44512 0.97785 -0.29749 0.05919  -0.21652 29  ILE F CG1 
3924 C CG2 . ILE D 29  ? 2.32041 1.43072 1.17891 -0.36247 -0.02919 -0.14955 29  ILE F CG2 
3925 C CD1 . ILE D 29  ? 2.17869 1.45057 0.91600 -0.25008 0.09566  -0.21676 29  ILE F CD1 
3926 N N   . GLU D 30  ? 2.35873 1.60281 1.00104 -0.32200 0.07858  -0.12640 30  GLU F N   
3927 C CA  . GLU D 30  ? 2.33214 1.64578 0.99906 -0.31439 0.09906  -0.12557 30  GLU F CA  
3928 C C   . GLU D 30  ? 2.34440 1.65718 1.00975 -0.32831 0.09229  -0.15763 30  GLU F C   
3929 O O   . GLU D 30  ? 2.30490 1.65753 1.01550 -0.29911 0.10539  -0.19696 30  GLU F O   
3930 C CB  . GLU D 30  ? 2.25367 1.67579 0.99377 -0.25332 0.13685  -0.13158 30  GLU F CB  
3931 C CG  . GLU D 30  ? 2.22432 1.72467 0.99391 -0.23810 0.15345  -0.13597 30  GLU F CG  
3932 C CD  . GLU D 30  ? 2.17771 1.76220 0.99725 -0.19317 0.18094  -0.12347 30  GLU F CD  
3933 O OE1 . GLU D 30  ? 2.19910 1.76086 1.00733 -0.20377 0.18729  -0.10376 30  GLU F OE1 
3934 O OE2 . GLU D 30  ? 2.12706 1.80062 0.99486 -0.15040 0.19538  -0.13393 30  GLU F OE2 
3935 N N   . THR D 31  ? 2.35316 1.62507 0.97267 -0.37696 0.07231  -0.14397 31  THR F N   
3936 C CA  . THR D 31  ? 2.39310 1.65646 1.01812 -0.40159 0.06330  -0.17703 31  THR F CA  
3937 C C   . THR D 31  ? 2.39008 1.71293 1.01438 -0.40629 0.08133  -0.16619 31  THR F C   
3938 O O   . THR D 31  ? 2.42264 1.72541 1.01390 -0.43060 0.07241  -0.12542 31  THR F O   
3939 C CB  . THR D 31  ? 2.44405 1.64187 1.15288 -0.43523 0.00996  -0.14557 31  THR F CB  
3940 O OG1 . THR D 31  ? 2.42311 1.58668 1.18843 -0.41885 -0.00942 -0.14140 31  THR F OG1 
3941 C CG2 . THR D 31  ? 2.45778 1.67513 1.27007 -0.44344 0.00574  -0.17529 31  THR F CG2 
3942 N N   . LEU D 32  ? 2.32349 1.72886 0.99929 -0.38226 0.10599  -0.20271 32  LEU F N   
3943 C CA  . LEU D 32  ? 2.31936 1.78603 1.00597 -0.38312 0.12021  -0.19432 32  LEU F CA  
3944 C C   . LEU D 32  ? 2.43220 1.83284 1.07201 -0.44815 0.09786  -0.20502 32  LEU F C   
3945 O O   . LEU D 32  ? 2.44612 1.83803 1.14918 -0.45841 0.08846  -0.24245 32  LEU F O   
3946 C CB  . LEU D 32  ? 2.22800 1.81625 0.98560 -0.33277 0.14879  -0.22208 32  LEU F CB  
3947 C CG  . LEU D 32  ? 2.14755 1.79620 0.94509 -0.27085 0.16440  -0.20235 32  LEU F CG  
3948 C CD1 . LEU D 32  ? 2.08544 1.83840 0.94105 -0.22368 0.18127  -0.22500 32  LEU F CD1 
3949 C CD2 . LEU D 32  ? 2.13989 1.80446 0.93413 -0.25807 0.17310  -0.16402 32  LEU F CD2 
3950 N N   . VAL D 33  ? 2.40226 1.77573 0.99960 -0.48011 0.08649  -0.16576 33  VAL F N   
3951 C CA  . VAL D 33  ? 2.51086 1.82525 1.10086 -0.53665 0.05447  -0.15442 33  VAL F CA  
3952 C C   . VAL D 33  ? 2.53950 1.90002 1.09288 -0.55185 0.07563  -0.15683 33  VAL F C   
3953 O O   . VAL D 33  ? 2.50326 1.90004 1.06679 -0.53157 0.08918  -0.12485 33  VAL F O   
3954 C CB  . VAL D 33  ? 2.57603 1.80801 1.14566 -0.57307 0.01052  -0.09206 33  VAL F CB  
3955 C CG1 . VAL D 33  ? 2.66991 1.86497 1.30961 -0.61497 -0.02705 -0.06410 33  VAL F CG1 
3956 C CG2 . VAL D 33  ? 2.53023 1.72768 1.13935 -0.55255 -0.00840 -0.08340 33  VAL F CG2 
3957 N N   . ASP D 34  ? 2.44257 1.82606 1.05058 -0.56762 0.07612  -0.18830 34  ASP F N   
3958 C CA  . ASP D 34  ? 2.47581 1.89664 1.04179 -0.58947 0.09292  -0.19046 34  ASP F CA  
3959 C C   . ASP D 34  ? 2.58402 1.93531 1.09795 -0.63691 0.06373  -0.13454 34  ASP F C   
3960 O O   . ASP D 34  ? 2.64912 1.93410 1.21607 -0.66150 0.02189  -0.09972 34  ASP F O   
3961 C CB  . ASP D 34  ? 2.47019 1.93335 1.12439 -0.59877 0.09991  -0.23750 34  ASP F CB  
3962 C CG  . ASP D 34  ? 2.51717 1.91722 1.29283 -0.61609 0.06659  -0.23497 34  ASP F CG  
3963 O OD1 . ASP D 34  ? 2.53723 1.87308 1.33352 -0.61243 0.03718  -0.19968 34  ASP F OD1 
3964 O OD2 . ASP D 34  ? 2.53124 1.94713 1.38824 -0.63467 0.07189  -0.26713 34  ASP F OD2 
3965 N N   . ILE D 35  ? 2.45029 1.84793 0.96405 -0.62424 0.08323  -0.11281 35  ILE F N   
3966 C CA  . ILE D 35  ? 2.55114 1.89525 1.01694 -0.67159 0.06086  -0.06545 35  ILE F CA  
3967 C C   . ILE D 35  ? 2.67533 1.96431 1.09801 -0.73925 0.03205  -0.05791 35  ILE F C   
3968 O O   . ILE D 35  ? 2.77638 2.00697 1.19096 -0.78327 -0.00588 -0.00525 35  ILE F O   
3969 C CB  . ILE D 35  ? 2.49496 1.90572 0.99843 -0.63996 0.09039  -0.06052 35  ILE F CB  
3970 C CG1 . ILE D 35  ? 2.36860 1.83325 0.92425 -0.57142 0.11643  -0.06821 35  ILE F CG1 
3971 C CG2 . ILE D 35  ? 2.58422 1.94549 1.04672 -0.69095 0.06939  -0.02134 35  ILE F CG2 
3972 C CD1 . ILE D 35  ? 2.32788 1.84112 0.91141 -0.54474 0.14227  -0.06259 35  ILE F CD1 
3973 N N   . PHE D 36  ? 2.61402 1.95024 1.11023 -0.72623 0.04782  -0.10384 36  PHE F N   
3974 C CA  . PHE D 36  ? 2.68039 1.99148 1.25862 -0.76057 0.02483  -0.09726 36  PHE F CA  
3975 C C   . PHE D 36  ? 2.75109 1.98849 1.42323 -0.77444 -0.02216 -0.05652 36  PHE F C   
3976 O O   . PHE D 36  ? 2.83745 2.02737 1.53976 -0.81636 -0.05506 -0.00864 36  PHE F O   
3977 C CB  . PHE D 36  ? 2.60510 1.98361 1.25772 -0.74349 0.05514  -0.16452 36  PHE F CB  
3978 N N   . GLN D 37  ? 2.64916 1.87967 1.37507 -0.74002 -0.02603 -0.07081 37  GLN F N   
3979 C CA  . GLN D 37  ? 2.71248 1.87775 1.54073 -0.74964 -0.06948 -0.02939 37  GLN F CA  
3980 C C   . GLN D 37  ? 2.80427 1.91732 1.56298 -0.78782 -0.11150 0.05258  37  GLN F C   
3981 O O   . GLN D 37  ? 2.85453 1.91836 1.69399 -0.81664 -0.15540 0.10925  37  GLN F O   
3982 C CB  . GLN D 37  ? 2.61633 1.78862 1.50227 -0.70474 -0.06160 -0.06299 37  GLN F CB  
3983 N N   . GLU D 38  ? 2.92257 2.05036 1.53720 -0.79259 -0.09650 0.06129  38  GLU F N   
3984 C CA  . GLU D 38  ? 2.92052 2.00967 1.45255 -0.83483 -0.12919 0.12912  38  GLU F CA  
3985 C C   . GLU D 38  ? 2.98339 2.06566 1.44588 -0.89258 -0.13883 0.16710  38  GLU F C   
3986 O O   . GLU D 38  ? 3.01242 2.05881 1.47362 -0.94256 -0.18480 0.23698  38  GLU F O   
3987 C CB  . GLU D 38  ? 2.83640 1.94079 1.25710 -0.81395 -0.10086 0.11274  38  GLU F CB  
3988 C CG  . GLU D 38  ? 2.74420 1.86154 1.22346 -0.75527 -0.08649 0.07201  38  GLU F CG  
3989 C CD  . GLU D 38  ? 2.73664 1.81131 1.33285 -0.75465 -0.13365 0.10483  38  GLU F CD  
3990 O OE1 . GLU D 38  ? 2.76251 1.83387 1.48858 -0.74236 -0.14179 0.08822  38  GLU F OE1 
3991 O OE2 . GLU D 38  ? 2.71298 1.75934 1.27644 -0.76897 -0.15991 0.14665  38  GLU F OE2 
3992 N N   . TYR D 39  ? 2.02636 1.96193 2.12689 -0.18190 0.02982  -0.07855 39  TYR F N   
3993 C CA  . TYR D 39  ? 2.00598 1.96242 2.17611 -0.23320 0.05134  -0.02395 39  TYR F CA  
3994 C C   . TYR D 39  ? 2.08158 1.95156 2.34149 -0.24722 -0.00450 -0.01064 39  TYR F C   
3995 O O   . TYR D 39  ? 2.04203 1.90996 2.38945 -0.26747 -0.01691 -0.02706 39  TYR F O   
3996 C CB  . TYR D 39  ? 1.89561 1.93364 2.10339 -0.26272 0.10001  -0.03020 39  TYR F CB  
3997 C CG  . TYR D 39  ? 1.78018 1.90914 1.92296 -0.26382 0.15872  -0.02459 39  TYR F CG  
3998 C CD1 . TYR D 39  ? 1.75643 1.91888 1.86958 -0.27571 0.19076  0.02907  39  TYR F CD1 
3999 C CD2 . TYR D 39  ? 1.68523 1.86047 1.79596 -0.24966 0.17919  -0.07338 39  TYR F CD2 
4000 C CE1 . TYR D 39  ? 1.64126 1.88220 1.69258 -0.26815 0.23400  0.02624  39  TYR F CE1 
4001 C CE2 . TYR D 39  ? 1.55363 1.80569 1.61484 -0.24961 0.22282  -0.07434 39  TYR F CE2 
4002 C CZ  . TYR D 39  ? 1.53339 1.81940 1.56490 -0.25666 0.24664  -0.02828 39  TYR F CZ  
4003 O OH  . TYR D 39  ? 1.41623 1.77407 1.39436 -0.24760 0.27985  -0.03760 39  TYR F OH  
4004 N N   . PRO D 40  ? 2.01791 1.81237 2.26620 -0.23534 -0.04529 0.01487  40  PRO F N   
4005 C CA  . PRO D 40  ? 2.06072 1.75954 2.40212 -0.24555 -0.11112 0.01994  40  PRO F CA  
4006 C C   . PRO D 40  ? 2.02817 1.73580 2.48976 -0.31050 -0.08869 0.08510  40  PRO F C   
4007 O O   . PRO D 40  ? 2.01669 1.66162 2.59405 -0.32996 -0.14027 0.08209  40  PRO F O   
4008 C CB  . PRO D 40  ? 2.16020 1.77667 2.43534 -0.20715 -0.15873 0.02767  40  PRO F CB  
4009 C CG  . PRO D 40  ? 2.16108 1.83760 2.31283 -0.16852 -0.12192 0.00914  40  PRO F CG  
4010 C CD  . PRO D 40  ? 2.06684 1.85189 2.21935 -0.20552 -0.04419 0.03116  40  PRO F CD  
4011 N N   . ASP D 41  ? 2.02712 1.81404 2.47119 -0.34167 -0.01270 0.14178  41  ASP F N   
4012 C CA  . ASP D 41  ? 1.99073 1.78575 2.54347 -0.39902 0.01998  0.21746  41  ASP F CA  
4013 C C   . ASP D 41  ? 1.90020 1.76606 2.57114 -0.43671 0.04827  0.20685  41  ASP F C   
4014 O O   . ASP D 41  ? 1.86662 1.71916 2.68208 -0.48412 0.04748  0.24883  41  ASP F O   
4015 C CB  . ASP D 41  ? 1.98426 1.82739 2.45342 -0.40447 0.09062  0.28805  41  ASP F CB  
4016 N N   . GLU D 42  ? 1.82202 1.76047 2.44459 -0.41652 0.07045  0.15065  42  GLU F N   
4017 C CA  . GLU D 42  ? 1.74070 1.74160 2.47099 -0.44368 0.08741  0.12964  42  GLU F CA  
4018 C C   . GLU D 42  ? 1.73756 1.66180 2.56218 -0.43461 0.00160  0.07078  42  GLU F C   
4019 O O   . GLU D 42  ? 1.70452 1.63595 2.50196 -0.40220 -0.02271 -0.00132 42  GLU F O   
4020 C CB  . GLU D 42  ? 1.68630 1.77654 2.32652 -0.42026 0.13243  0.08626  42  GLU F CB  
4021 N N   . ILE D 43  ? 1.81315 1.65608 2.74451 -0.45837 -0.04851 0.10007  43  ILE F N   
4022 C CA  . ILE D 43  ? 1.79662 1.55230 2.81752 -0.44181 -0.14587 0.03905  43  ILE F CA  
4023 C C   . ILE D 43  ? 1.69588 1.50708 2.86611 -0.46999 -0.14924 0.00978  43  ILE F C   
4024 O O   . ILE D 43  ? 1.65966 1.44182 2.83425 -0.43094 -0.20999 -0.07156 43  ILE F O   
4025 C CB  . ILE D 43  ? 1.84152 1.48817 2.94302 -0.46020 -0.20524 0.07786  43  ILE F CB  
4026 N N   . GLU D 44  ? 1.67422 1.56551 2.96856 -0.53268 -0.08448 0.07557  44  GLU F N   
4027 C CA  . GLU D 44  ? 1.58023 1.53211 3.04227 -0.56209 -0.08898 0.04986  44  GLU F CA  
4028 C C   . GLU D 44  ? 1.54051 1.59246 2.91987 -0.53717 -0.03961 0.00546  44  GLU F C   
4029 O O   . GLU D 44  ? 1.48094 1.64076 2.94207 -0.57209 0.02576  0.03343  44  GLU F O   
4030 C CB  . GLU D 44  ? 1.56838 1.57488 3.20960 -0.63785 -0.03181 0.14207  44  GLU F CB  
4031 N N   . TYR D 45  ? 1.58169 1.59555 2.80300 -0.47447 -0.07086 -0.06292 45  TYR F N   
4032 C CA  . TYR D 45  ? 1.54756 1.63242 2.67351 -0.44443 -0.03331 -0.10938 45  TYR F CA  
4033 C C   . TYR D 45  ? 1.56448 1.56477 2.55912 -0.37360 -0.09536 -0.18685 45  TYR F C   
4034 O O   . TYR D 45  ? 1.63041 1.58029 2.49931 -0.34437 -0.09848 -0.17909 45  TYR F O   
4035 C CB  . TYR D 45  ? 1.56793 1.73668 2.57806 -0.45354 0.06232  -0.05738 45  TYR F CB  
4036 C CG  . TYR D 45  ? 1.51463 1.80169 2.60811 -0.49964 0.14382  -0.00186 45  TYR F CG  
4037 C CD1 . TYR D 45  ? 1.44230 1.81382 2.57541 -0.49790 0.16791  -0.03890 45  TYR F CD1 
4038 C CD2 . TYR D 45  ? 1.53266 1.84594 2.64852 -0.53657 0.20046  0.08925  45  TYR F CD2 
4039 C CE1 . TYR D 45  ? 1.39330 1.87988 2.59474 -0.53166 0.24659  0.01208  45  TYR F CE1 
4040 C CE2 . TYR D 45  ? 1.47599 1.89889 2.65286 -0.56868 0.28282  0.14512  45  TYR F CE2 
4041 C CZ  . TYR D 45  ? 1.40872 1.92216 2.63038 -0.56572 0.30643  0.10574  45  TYR F CZ  
4042 O OH  . TYR D 45  ? 1.35380 1.98201 2.63256 -0.59056 0.39155  0.16207  45  TYR F OH  
4043 N N   . ILE D 46  ? 1.64774 1.63147 2.66714 -0.34044 -0.14339 -0.26010 46  ILE F N   
4044 C CA  . ILE D 46  ? 1.66658 1.57737 2.54151 -0.26505 -0.18579 -0.32804 46  ILE F CA  
4045 C C   . ILE D 46  ? 1.64202 1.62316 2.38908 -0.25115 -0.11152 -0.33270 46  ILE F C   
4046 O O   . ILE D 46  ? 1.59068 1.66890 2.38153 -0.28686 -0.05415 -0.31375 46  ILE F O   
4047 C CB  . ILE D 46  ? 1.62449 1.47029 2.56228 -0.22261 -0.27647 -0.40668 46  ILE F CB  
4048 C CG1 . ILE D 46  ? 1.64293 1.37448 2.43632 -0.13753 -0.33733 -0.46012 46  ILE F CG1 
4049 C CG2 . ILE D 46  ? 1.56142 1.47638 2.51957 -0.21733 -0.25443 -0.44668 46  ILE F CG2 
4050 C CD1 . ILE D 46  ? 1.70379 1.35455 2.48707 -0.13080 -0.37962 -0.43493 46  ILE F CD1 
4051 N N   . PHE D 47  ? 1.65723 1.59399 2.25007 -0.20098 -0.10762 -0.35217 47  PHE F N   
4052 C CA  . PHE D 47  ? 1.61569 1.61010 2.09695 -0.19086 -0.04074 -0.35452 47  PHE F CA  
4053 C C   . PHE D 47  ? 1.54414 1.48642 1.93353 -0.12622 -0.06438 -0.41960 47  PHE F C   
4054 O O   . PHE D 47  ? 1.54629 1.39584 1.88003 -0.07062 -0.11739 -0.45172 47  PHE F O   
4055 C CB  . PHE D 47  ? 1.65296 1.65613 2.04129 -0.19328 -0.00018 -0.31305 47  PHE F CB  
4056 C CG  . PHE D 47  ? 1.68838 1.73763 2.14082 -0.24798 0.02865  -0.24567 47  PHE F CG  
4057 C CD1 . PHE D 47  ? 1.62896 1.77079 2.14807 -0.29445 0.07999  -0.21272 47  PHE F CD1 
4058 C CD2 . PHE D 47  ? 1.76162 1.75845 2.20040 -0.24658 0.00571  -0.21365 47  PHE F CD2 
4059 C CE1 . PHE D 47  ? 1.63620 1.81552 2.20103 -0.33705 0.11351  -0.14401 47  PHE F CE1 
4060 C CE2 . PHE D 47  ? 1.78171 1.81048 2.26768 -0.29196 0.03422  -0.14691 47  PHE F CE2 
4061 C CZ  . PHE D 47  ? 1.71497 1.83389 2.26117 -0.33643 0.09077  -0.10968 47  PHE F CZ  
4062 N N   . LYS D 48  ? 1.76489 1.76239 2.13154 -0.12794 -0.02499 -0.43794 48  LYS F N   
4063 C CA  . LYS D 48  ? 1.64354 1.59223 1.90879 -0.06777 -0.03374 -0.49064 48  LYS F CA  
4064 C C   . LYS D 48  ? 1.53477 1.52836 1.70214 -0.07201 0.03812  -0.47415 48  LYS F C   
4065 O O   . LYS D 48  ? 1.49867 1.57912 1.69936 -0.11428 0.08385  -0.45541 48  LYS F O   
4066 C CB  . LYS D 48  ? 1.58054 1.53969 1.91221 -0.05898 -0.06417 -0.53719 48  LYS F CB  
4067 N N   . PRO D 49  ? 1.65975 1.60060 1.71330 -0.02890 0.05101  -0.47910 49  PRO F N   
4068 C CA  . PRO D 49  ? 1.69822 1.54214 1.69093 0.03080  0.00726  -0.49615 49  PRO F CA  
4069 C C   . PRO D 49  ? 1.84453 1.68570 1.88101 0.00849  -0.01242 -0.46087 49  PRO F C   
4070 O O   . PRO D 49  ? 1.90979 1.82189 1.99876 -0.04919 0.02044  -0.41788 49  PRO F O   
4071 C CB  . PRO D 49  ? 1.57477 1.39758 1.44481 0.06961  0.05587  -0.49648 49  PRO F CB  
4072 C CG  . PRO D 49  ? 1.50711 1.42299 1.39549 0.01246  0.11978  -0.46528 49  PRO F CG  
4073 C CD  . PRO D 49  ? 1.51782 1.49507 1.49645 -0.03266 0.11402  -0.46965 49  PRO F CD  
4074 N N   . SER D 50  ? 1.68047 1.43470 1.69073 0.05907  -0.06994 -0.47937 50  SER F N   
4075 C CA  . SER D 50  ? 1.80546 1.54608 1.85374 0.04186  -0.09507 -0.44792 50  SER F CA  
4076 C C   . SER D 50  ? 1.80432 1.57098 1.77748 0.04467  -0.04493 -0.41472 50  SER F C   
4077 O O   . SER D 50  ? 1.89687 1.68824 1.90595 0.00973  -0.04185 -0.37611 50  SER F O   
4078 C CB  . SER D 50  ? 1.84177 1.47582 1.88772 0.10094  -0.18290 -0.48510 50  SER F CB  
4079 O OG  . SER D 50  ? 1.75516 1.32065 1.67772 0.18734  -0.19345 -0.52600 50  SER F OG  
4080 N N   . CYS D 51  ? 2.10180 1.51718 1.61392 -0.26513 0.20746  -0.15094 51  CYS F N   
4081 C CA  . CYS D 51  ? 2.10011 1.46076 1.58110 -0.26847 0.18270  -0.13554 51  CYS F CA  
4082 C C   . CYS D 51  ? 2.09721 1.41384 1.50499 -0.24941 0.16431  -0.12418 51  CYS F C   
4083 O O   . CYS D 51  ? 2.07590 1.40629 1.46265 -0.23127 0.16564  -0.13095 51  CYS F O   
4084 C CB  . CYS D 51  ? 2.01613 1.40830 1.54619 -0.28086 0.16532  -0.14884 51  CYS F CB  
4085 S SG  . CYS D 51  ? 1.91067 1.36269 1.45560 -0.27314 0.15091  -0.16669 51  CYS F SG  
4086 N N   . VAL D 52  ? 2.12617 1.38859 1.49635 -0.25298 0.14582  -0.10806 52  VAL F N   
4087 C CA  . VAL D 52  ? 2.12315 1.33539 1.42256 -0.23957 0.12609  -0.09773 52  VAL F CA  
4088 C C   . VAL D 52  ? 2.07595 1.26875 1.36790 -0.24977 0.09584  -0.09275 52  VAL F C   
4089 O O   . VAL D 52  ? 2.06995 1.27104 1.39827 -0.26461 0.09128  -0.09170 52  VAL F O   
4090 C CB  . VAL D 52  ? 2.21015 1.37453 1.45583 -0.23320 0.13619  -0.08241 52  VAL F CB  
4091 C CG1 . VAL D 52  ? 2.26831 1.45985 1.51979 -0.22513 0.16767  -0.08813 52  VAL F CG1 
4092 C CG2 . VAL D 52  ? 2.25480 1.39413 1.50935 -0.24910 0.13425  -0.06667 52  VAL F CG2 
4093 N N   . PRO D 53  ? 2.10047 1.26787 1.34731 -0.24267 0.07419  -0.09057 53  PRO F N   
4094 C CA  . PRO D 53  ? 2.07649 1.22853 1.31324 -0.25627 0.04603  -0.08529 53  PRO F CA  
4095 C C   . PRO D 53  ? 2.11726 1.21304 1.30449 -0.25728 0.03459  -0.07099 53  PRO F C   
4096 O O   . PRO D 53  ? 2.15971 1.21128 1.28789 -0.24462 0.03267  -0.06587 53  PRO F O   
4097 C CB  . PRO D 53  ? 2.06580 1.21262 1.27428 -0.25062 0.02940  -0.08751 53  PRO F CB  
4098 C CG  . PRO D 53  ? 2.10404 1.23105 1.27955 -0.22657 0.04335  -0.09000 53  PRO F CG  
4099 C CD  . PRO D 53  ? 2.11303 1.26901 1.32211 -0.22241 0.07414  -0.09481 53  PRO F CD  
4100 N N   . LEU D 54  ? 2.17188 1.27106 1.38298 -0.27026 0.02626  -0.06637 54  LEU F N   
4101 C CA  . LEU D 54  ? 2.21146 1.26460 1.38046 -0.27057 0.01417  -0.05206 54  LEU F CA  
4102 C C   . LEU D 54  ? 2.18012 1.24304 1.36198 -0.28520 -0.01296 -0.05296 54  LEU F C   
4103 O O   . LEU D 54  ? 2.14230 1.25080 1.38388 -0.29475 -0.01397 -0.06267 54  LEU F O   
4104 C CB  . LEU D 54  ? 2.25776 1.30394 1.44307 -0.26849 0.03260  -0.04213 54  LEU F CB  
4105 C CG  . LEU D 54  ? 2.30402 1.35153 1.48121 -0.25824 0.06258  -0.04195 54  LEU F CG  
4106 C CD1 . LEU D 54  ? 2.36003 1.40525 1.56197 -0.26305 0.08194  -0.03034 54  LEU F CD1 
4107 C CD2 . LEU D 54  ? 2.33561 1.34389 1.43833 -0.24404 0.06179  -0.03776 54  LEU F CD2 
4108 N N   . MET D 55  ? 2.33407 1.35955 1.46213 -0.28755 -0.03469 -0.04577 55  MET F N   
4109 C CA  . MET D 55  ? 2.31840 1.35824 1.45806 -0.30273 -0.06040 -0.04686 55  MET F CA  
4110 C C   . MET D 55  ? 2.33316 1.37748 1.50115 -0.30013 -0.06099 -0.04081 55  MET F C   
4111 O O   . MET D 55  ? 2.37590 1.38131 1.50301 -0.29306 -0.06638 -0.02719 55  MET F O   
4112 C CB  . MET D 55  ? 2.35209 1.35065 1.42645 -0.30821 -0.08356 -0.04202 55  MET F CB  
4113 C CG  . MET D 55  ? 2.36469 1.33989 1.40283 -0.30543 -0.08250 -0.04540 55  MET F CG  
4114 S SD  . MET D 55  ? 2.32580 1.34169 1.39264 -0.32755 -0.09754 -0.05229 55  MET F SD  
4115 C CE  . MET D 55  ? 2.35000 1.34716 1.39699 -0.31131 -0.08404 -0.05431 55  MET F CE  
4116 N N   . ARG D 56  ? 2.19003 1.28164 1.42768 -0.30473 -0.05622 -0.05160 56  ARG F N   
4117 C CA  . ARG D 56  ? 2.21094 1.30276 1.48188 -0.29972 -0.05901 -0.04693 56  ARG F CA  
4118 C C   . ARG D 56  ? 2.18687 1.31760 1.49125 -0.30859 -0.08412 -0.05832 56  ARG F C   
4119 O O   . ARG D 56  ? 2.14765 1.31377 1.45765 -0.32246 -0.09342 -0.07054 56  ARG F O   
4120 C CB  . ARG D 56  ? 2.21392 1.32372 1.54197 -0.29588 -0.03407 -0.05287 56  ARG F CB  
4121 C CG  . ARG D 56  ? 2.26713 1.33063 1.57381 -0.28608 -0.01790 -0.03258 56  ARG F CG  
4122 C CD  . ARG D 56  ? 2.31103 1.32746 1.53540 -0.27997 -0.02001 -0.01477 56  ARG F CD  
4123 N NE  . ARG D 56  ? 2.36957 1.34761 1.56854 -0.27289 -0.00482 0.00679  56  ARG F NE  
4124 C CZ  . ARG D 56  ? 2.39044 1.37191 1.62032 -0.27412 0.02197  0.00973  56  ARG F CZ  
4125 N NH1 . ARG D 56  ? 2.39402 1.39110 1.62166 -0.27457 0.04559  0.00118  56  ARG F NH1 
4126 N NH2 . ARG D 56  ? 2.41581 1.38454 1.67961 -0.27497 0.02413  0.02103  56  ARG F NH2 
4127 N N   . CYS D 57  ? 2.09054 1.21672 1.41642 -0.30062 -0.09480 -0.05382 57  CYS F N   
4128 C CA  . CYS D 57  ? 2.09195 1.26016 1.45373 -0.30474 -0.11905 -0.06679 57  CYS F CA  
4129 C C   . CYS D 57  ? 2.02977 1.26489 1.46622 -0.31202 -0.11294 -0.09363 57  CYS F C   
4130 O O   . CYS D 57  ? 1.99146 1.23753 1.45681 -0.31238 -0.09042 -0.10149 57  CYS F O   
4131 C CB  . CYS D 57  ? 2.16135 1.30642 1.53276 -0.28850 -0.13160 -0.05552 57  CYS F CB  
4132 S SG  . CYS D 57  ? 2.23517 1.33506 1.52720 -0.28413 -0.15502 -0.03264 57  CYS F SG  
4133 N N   . GLY D 58  ? 2.01227 1.29908 1.48008 -0.31855 -0.13365 -0.10985 58  GLY F N   
4134 C CA  . GLY D 58  ? 1.95475 1.31530 1.49284 -0.32568 -0.13036 -0.13888 58  GLY F CA  
4135 C C   . GLY D 58  ? 1.92838 1.35298 1.47991 -0.34083 -0.15237 -0.15468 58  GLY F C   
4136 O O   . GLY D 58  ? 1.93033 1.34342 1.42930 -0.35449 -0.16627 -0.14278 58  GLY F O   
4137 N N   . GLY D 59  ? 1.83580 1.33006 1.45847 -0.33958 -0.15560 -0.18336 59  GLY F N   
4138 C CA  . GLY D 59  ? 1.80120 1.37272 1.44455 -0.35607 -0.17349 -0.20235 59  GLY F CA  
4139 C C   . GLY D 59  ? 1.83217 1.44891 1.53260 -0.34047 -0.19131 -0.22413 59  GLY F C   
4140 O O   . GLY D 59  ? 1.90959 1.47988 1.61858 -0.31482 -0.19726 -0.21634 59  GLY F O   
4141 N N   . CYS D 60  ? 1.73938 1.44897 1.47828 -0.35557 -0.20065 -0.25101 60  CYS F N   
4142 C CA  . CYS D 60  ? 1.75984 1.52772 1.56004 -0.33913 -0.21819 -0.27834 60  CYS F CA  
4143 C C   . CYS D 60  ? 1.80967 1.56168 1.57573 -0.33522 -0.24468 -0.26345 60  CYS F C   
4144 O O   . CYS D 60  ? 1.78519 1.53700 1.49730 -0.36087 -0.25252 -0.24815 60  CYS F O   
4145 C CB  . CYS D 60  ? 1.67504 1.56028 1.52769 -0.35813 -0.21798 -0.31496 60  CYS F CB  
4146 S SG  . CYS D 60  ? 1.58343 1.50775 1.43010 -0.38850 -0.19301 -0.31981 60  CYS F SG  
4147 N N   . CYS D 61  ? 1.71424 1.45138 1.51161 -0.30311 -0.25985 -0.26800 61  CYS F N   
4148 C CA  . CYS D 61  ? 1.75334 1.50578 1.53774 -0.29655 -0.28894 -0.26423 61  CYS F CA  
4149 C C   . CYS D 61  ? 1.70711 1.57543 1.55872 -0.29750 -0.30422 -0.30421 61  CYS F C   
4150 O O   . CYS D 61  ? 1.70915 1.61567 1.55114 -0.30205 -0.32770 -0.30585 61  CYS F O   
4151 C CB  . CYS D 61  ? 1.87448 1.55008 1.65208 -0.25901 -0.30115 -0.24426 61  CYS F CB  
4152 S SG  . CYS D 61  ? 1.92950 1.48243 1.60948 -0.26096 -0.29243 -0.19364 61  CYS F SG  
4153 N N   . ASN D 62  ? 1.74620 1.67709 1.66557 -0.29450 -0.29099 -0.33871 62  ASN F N   
4154 C CA  . ASN D 62  ? 1.68167 1.73494 1.66937 -0.29577 -0.30173 -0.38248 62  ASN F CA  
4155 C C   . ASN D 62  ? 1.74551 1.81428 1.76613 -0.26121 -0.33151 -0.39319 62  ASN F C   
4156 O O   . ASN D 62  ? 1.70291 1.86506 1.74907 -0.26796 -0.34932 -0.41594 62  ASN F O   
4157 C CB  . ASN D 62  ? 1.59030 1.72144 1.55159 -0.34253 -0.30079 -0.38528 62  ASN F CB  
4158 C CG  . ASN D 62  ? 1.52499 1.65202 1.46266 -0.37291 -0.27378 -0.37801 62  ASN F CG  
4159 O OD1 . ASN D 62  ? 1.49519 1.63694 1.47603 -0.36295 -0.25608 -0.39811 62  ASN F OD1 
4160 N ND2 . ASN D 62  ? 1.50621 1.61088 1.37503 -0.40918 -0.27199 -0.34962 62  ASN F ND2 
4161 N N   . ASP D 63  ? 1.71908 1.69719 1.73949 -0.22386 -0.33732 -0.37578 63  ASP F N   
4162 C CA  . ASP D 63  ? 1.80300 1.78332 1.85663 -0.18366 -0.36707 -0.38293 63  ASP F CA  
4163 C C   . ASP D 63  ? 1.91911 1.79429 1.98142 -0.14636 -0.36492 -0.36527 63  ASP F C   
4164 O O   . ASP D 63  ? 1.96754 1.74303 1.96747 -0.15217 -0.35289 -0.32414 63  ASP F O   
4165 C CB  . ASP D 63  ? 1.82946 1.79937 1.82242 -0.19203 -0.39046 -0.35557 63  ASP F CB  
4166 C CG  . ASP D 63  ? 1.91499 1.88527 1.93568 -0.14883 -0.42363 -0.35847 63  ASP F CG  
4167 O OD1 . ASP D 63  ? 1.87136 1.94475 1.95472 -0.13732 -0.44114 -0.39730 63  ASP F OD1 
4168 O OD2 . ASP D 63  ? 2.01253 1.88382 1.99242 -0.12582 -0.43247 -0.32201 63  ASP F OD2 
4169 N N   . GLU D 64  ? 1.87253 1.77089 2.01282 -0.10898 -0.37634 -0.39734 64  GLU F N   
4170 C CA  . GLU D 64  ? 1.97009 1.76775 2.12643 -0.07557 -0.37465 -0.38286 64  GLU F CA  
4171 C C   . GLU D 64  ? 2.08094 1.77806 2.17216 -0.05894 -0.39158 -0.33064 64  GLU F C   
4172 O O   . GLU D 64  ? 2.12899 1.72232 2.18531 -0.05622 -0.37773 -0.29598 64  GLU F O   
4173 C CB  . GLU D 64  ? 1.97846 1.81985 2.23067 -0.03534 -0.39055 -0.42891 64  GLU F CB  
4174 C CG  . GLU D 64  ? 1.90470 1.77101 2.21279 -0.04327 -0.36431 -0.46597 64  GLU F CG  
4175 C CD  . GLU D 64  ? 1.93291 1.68998 2.19850 -0.05765 -0.33762 -0.43008 64  GLU F CD  
4176 O OE1 . GLU D 64  ? 2.02732 1.67937 2.27976 -0.03315 -0.34513 -0.39918 64  GLU F OE1 
4177 O OE2 . GLU D 64  ? 1.85298 1.63013 2.09491 -0.09435 -0.30973 -0.43013 64  GLU F OE2 
4178 N N   . GLY D 65  ? 1.92303 1.65501 1.99886 -0.04773 -0.42195 -0.32555 65  GLY F N   
4179 C CA  . GLY D 65  ? 2.01137 1.65727 2.02621 -0.02952 -0.44123 -0.27805 65  GLY F CA  
4180 C C   . GLY D 65  ? 2.01657 1.57981 1.94018 -0.05971 -0.41883 -0.23223 65  GLY F C   
4181 O O   . GLY D 65  ? 2.09036 1.55547 1.97085 -0.04475 -0.42018 -0.19151 65  GLY F O   
4182 N N   . LEU D 66  ? 2.08247 1.68319 1.97716 -0.10172 -0.39712 -0.23859 66  LEU F N   
4183 C CA  . LEU D 66  ? 2.07518 1.61038 1.88278 -0.13013 -0.37859 -0.20089 66  LEU F CA  
4184 C C   . LEU D 66  ? 2.03215 1.53422 1.84199 -0.14874 -0.34133 -0.20094 66  LEU F C   
4185 O O   . LEU D 66  ? 1.98329 1.53410 1.85827 -0.15056 -0.32844 -0.23525 66  LEU F O   
4186 C CB  . LEU D 66  ? 2.00338 1.59768 1.76928 -0.16439 -0.38484 -0.20520 66  LEU F CB  
4187 C CG  . LEU D 66  ? 2.01346 1.66766 1.78531 -0.15380 -0.42113 -0.21432 66  LEU F CG  
4188 C CD1 . LEU D 66  ? 1.90425 1.65215 1.67578 -0.19312 -0.42198 -0.23834 66  LEU F CD1 
4189 C CD2 . LEU D 66  ? 2.08873 1.67209 1.78591 -0.14321 -0.43908 -0.17392 66  LEU F CD2 
4190 N N   . GLU D 67  ? 2.18476 1.60845 1.92232 -0.16197 -0.32461 -0.16392 67  GLU F N   
4191 C CA  . GLU D 67  ? 2.14592 1.52977 1.87505 -0.17775 -0.28998 -0.15762 67  GLU F CA  
4192 C C   . GLU D 67  ? 2.11549 1.46695 1.76055 -0.20482 -0.27687 -0.13217 67  GLU F C   
4193 O O   . GLU D 67  ? 2.15421 1.47950 1.73886 -0.20472 -0.29315 -0.10928 67  GLU F O   
4194 C CB  . GLU D 67  ? 2.20420 1.50576 1.94467 -0.15498 -0.28091 -0.13706 67  GLU F CB  
4195 C CG  . GLU D 67  ? 2.26016 1.47327 1.92108 -0.15034 -0.28157 -0.08843 67  GLU F CG  
4196 C CD  . GLU D 67  ? 2.32277 1.46469 1.99979 -0.12245 -0.28716 -0.06591 67  GLU F CD  
4197 O OE1 . GLU D 67  ? 2.37859 1.53312 2.09675 -0.09455 -0.31531 -0.07444 67  GLU F OE1 
4198 O OE2 . GLU D 67  ? 2.30935 1.38284 1.95774 -0.12858 -0.26402 -0.03897 67  GLU F OE2 
4199 N N   . CYS D 68  ? 2.27388 1.63040 1.91704 -0.22667 -0.24885 -0.13900 68  CYS F N   
4200 C CA  . CYS D 68  ? 2.23969 1.56190 1.81044 -0.24907 -0.23346 -0.11864 68  CYS F CA  
4201 C C   . CYS D 68  ? 2.29139 1.52373 1.81212 -0.23768 -0.22097 -0.08343 68  CYS F C   
4202 O O   . CYS D 68  ? 2.27412 1.47727 1.81335 -0.23524 -0.19683 -0.08002 68  CYS F O   
4203 C CB  . CYS D 68  ? 2.14969 1.50883 1.74278 -0.27033 -0.20912 -0.13775 68  CYS F CB  
4204 S SG  . CYS D 68  ? 2.07752 1.45050 1.60885 -0.30324 -0.20524 -0.13322 68  CYS F SG  
4205 N N   . VAL D 69  ? 2.29926 1.49209 1.75513 -0.23306 -0.23649 -0.05795 69  VAL F N   
4206 C CA  . VAL D 69  ? 2.33644 1.45080 1.73682 -0.22456 -0.22440 -0.02345 69  VAL F CA  
4207 C C   . VAL D 69  ? 2.32195 1.41207 1.64154 -0.24095 -0.21873 -0.01063 69  VAL F C   
4208 O O   . VAL D 69  ? 2.31848 1.43752 1.61400 -0.25305 -0.23700 -0.01988 69  VAL F O   
4209 C CB  . VAL D 69  ? 2.41960 1.50061 1.81007 -0.19974 -0.24791 -0.00121 69  VAL F CB  
4210 C CG1 . VAL D 69  ? 2.43480 1.50432 1.89365 -0.18069 -0.24516 -0.00438 69  VAL F CG1 
4211 C CG2 . VAL D 69  ? 2.45689 1.58497 1.84573 -0.19631 -0.28288 -0.01242 69  VAL F CG2 
4212 N N   . PRO D 70  ? 2.40849 1.44705 1.68568 -0.24227 -0.19416 0.00878  70  PRO F N   
4213 C CA  . PRO D 70  ? 2.40827 1.41783 1.60526 -0.25205 -0.19119 0.01989  70  PRO F CA  
4214 C C   . PRO D 70  ? 2.47236 1.45505 1.61264 -0.24224 -0.21541 0.03990  70  PRO F C   
4215 O O   . PRO D 70  ? 2.51541 1.48172 1.66526 -0.22457 -0.22675 0.05689  70  PRO F O   
4216 C CB  . PRO D 70  ? 2.38045 1.35089 1.55886 -0.25166 -0.15724 0.03289  70  PRO F CB  
4217 C CG  . PRO D 70  ? 2.38704 1.34773 1.61902 -0.24015 -0.14801 0.04073  70  PRO F CG  
4218 C CD  . PRO D 70  ? 2.38468 1.39711 1.69078 -0.23771 -0.16595 0.01586  70  PRO F CD  
4219 N N   . THR D 71  ? 2.48056 1.45744 1.56048 -0.25375 -0.22483 0.03757  71  THR F N   
4220 C CA  . THR D 71  ? 2.52996 1.48842 1.55186 -0.24719 -0.24934 0.05208  71  THR F CA  
4221 C C   . THR D 71  ? 2.51659 1.42988 1.45497 -0.25154 -0.23790 0.06241  71  THR F C   
4222 O O   . THR D 71  ? 2.53891 1.42375 1.42227 -0.24141 -0.24681 0.08215  71  THR F O   
4223 C CB  . THR D 71  ? 2.53376 1.54093 1.56808 -0.25817 -0.28086 0.03235  71  THR F CB  
4224 O OG1 . THR D 71  ? 2.47081 1.50096 1.51274 -0.28216 -0.27358 0.01029  71  THR F OG1 
4225 C CG2 . THR D 71  ? 2.56105 1.61384 1.66956 -0.24554 -0.29771 0.02448  71  THR F CG2 
4226 N N   . GLU D 72  ? 2.69889 1.60724 1.62681 -0.26490 -0.21916 0.04837  72  GLU F N   
4227 C CA  . GLU D 72  ? 2.68221 1.54962 1.53702 -0.26624 -0.20652 0.05199  72  GLU F CA  
4228 C C   . GLU D 72  ? 2.65271 1.50820 1.52328 -0.26369 -0.17064 0.05223  72  GLU F C   
4229 O O   . GLU D 72  ? 2.62027 1.50061 1.53865 -0.27223 -0.16111 0.03634  72  GLU F O   
4230 C CB  . GLU D 72  ? 2.65902 1.52793 1.48034 -0.28368 -0.22311 0.03198  72  GLU F CB  
4231 N N   . GLU D 73  ? 2.67667 1.50031 1.50728 -0.25302 -0.15070 0.06981  73  GLU F N   
4232 C CA  . GLU D 73  ? 2.65884 1.47832 1.50681 -0.25094 -0.11576 0.06973  73  GLU F CA  
4233 C C   . GLU D 73  ? 2.67011 1.46062 1.44717 -0.24572 -0.09950 0.07083  73  GLU F C   
4234 O O   . GLU D 73  ? 2.69665 1.46525 1.41155 -0.24032 -0.10825 0.08252  73  GLU F O   
4235 C CB  . GLU D 73  ? 2.66721 1.48652 1.55688 -0.24495 -0.10030 0.08961  73  GLU F CB  
4236 C CG  . GLU D 73  ? 2.64198 1.49562 1.61758 -0.24950 -0.10194 0.07646  73  GLU F CG  
4237 C CD  . GLU D 73  ? 2.64663 1.49319 1.66692 -0.24443 -0.08827 0.09309  73  GLU F CD  
4238 O OE1 . GLU D 73  ? 2.66879 1.48381 1.65218 -0.24062 -0.07257 0.11731  73  GLU F OE1 
4239 O OE2 . GLU D 73  ? 2.62923 1.50171 1.72071 -0.24537 -0.09324 0.08137  73  GLU F OE2 
4240 N N   . SER D 74  ? 2.71151 1.50673 1.49970 -0.24578 -0.07587 0.05696  74  SER F N   
4241 C CA  . SER D 74  ? 2.73426 1.50894 1.46406 -0.23739 -0.05760 0.05254  74  SER F CA  
4242 C C   . SER D 74  ? 2.73201 1.52487 1.49954 -0.23432 -0.02409 0.04680  74  SER F C   
4243 O O   . SER D 74  ? 2.70797 1.52598 1.54251 -0.24011 -0.01571 0.04797  74  SER F O   
4244 C CB  . SER D 74  ? 2.72927 1.48499 1.41339 -0.23861 -0.07705 0.03130  74  SER F CB  
4245 O OG  . SER D 74  ? 2.69277 1.46156 1.41749 -0.24554 -0.07995 0.01356  74  SER F OG  
4246 N N   . ASN D 75  ? 2.73653 1.52066 1.46185 -0.22432 -0.00472 0.03861  75  ASN F N   
4247 C CA  . ASN D 75  ? 2.74862 1.55679 1.50657 -0.22005 0.02845  0.03312  75  ASN F CA  
4248 C C   . ASN D 75  ? 2.76160 1.56975 1.50616 -0.20910 0.03230  0.00705  75  ASN F C   
4249 O O   . ASN D 75  ? 2.78841 1.56816 1.47465 -0.20061 0.01943  -0.00444 75  ASN F O   
4250 C CB  . ASN D 75  ? 2.79267 1.60212 1.52265 -0.21718 0.05559  0.05115  75  ASN F CB  
4251 C CG  . ASN D 75  ? 2.77941 1.58914 1.54101 -0.22844 0.05699  0.07945  75  ASN F CG  
4252 O OD1 . ASN D 75  ? 2.74080 1.55651 1.55635 -0.23557 0.04146  0.08044  75  ASN F OD1 
4253 N ND2 . ASN D 75  ? 2.81433 1.61753 1.54278 -0.23000 0.07498  0.10256  75  ASN F ND2 
4254 N N   . ILE D 76  ? 2.56229 1.40160 1.36156 -0.20835 0.04898  -0.00292 76  ILE F N   
4255 C CA  . ILE D 76  ? 2.58499 1.42889 1.37938 -0.19428 0.05485  -0.02540 76  ILE F CA  
4256 C C   . ILE D 76  ? 2.62332 1.50337 1.43951 -0.18575 0.09120  -0.02882 76  ILE F C   
4257 O O   . ILE D 76  ? 2.60358 1.51711 1.47667 -0.19683 0.10789  -0.02082 76  ILE F O   
4258 C CB  . ILE D 76  ? 2.53102 1.38616 1.36992 -0.20086 0.03758  -0.03559 76  ILE F CB  
4259 C CG1 . ILE D 76  ? 2.53910 1.39719 1.37283 -0.18308 0.04364  -0.05524 76  ILE F CG1 
4260 C CG2 . ILE D 76  ? 2.48557 1.38292 1.40013 -0.21520 0.04622  -0.02890 76  ILE F CG2 
4261 C CD1 . ILE D 76  ? 2.57977 1.38979 1.34273 -0.16753 0.03029  -0.06715 76  ILE F CD1 
4262 N N   . THR D 77  ? 2.49845 1.37389 1.27021 -0.16668 0.10354  -0.04267 77  THR F N   
4263 C CA  . THR D 77  ? 2.53250 1.45105 1.32498 -0.15659 0.13770  -0.05143 77  THR F CA  
4264 C C   . THR D 77  ? 2.50915 1.44655 1.33449 -0.14190 0.13506  -0.07370 77  THR F C   
4265 O O   . THR D 77  ? 2.50400 1.40791 1.29855 -0.12798 0.11280  -0.08743 77  THR F O   
4266 C CB  . THR D 77  ? 2.59117 1.50547 1.32031 -0.14153 0.15405  -0.05743 77  THR F CB  
4267 O OG1 . THR D 77  ? 2.59555 1.48807 1.28795 -0.11652 0.14149  -0.08415 77  THR F OG1 
4268 C CG2 . THR D 77  ? 2.60362 1.48539 1.28099 -0.15266 0.14370  -0.03663 77  THR F CG2 
4269 N N   . MET D 78  ? 2.42448 1.41367 1.31220 -0.14616 0.15606  -0.07632 78  MET F N   
4270 C CA  . MET D 78  ? 2.40674 1.42355 1.33134 -0.13259 0.15400  -0.09497 78  MET F CA  
4271 C C   . MET D 78  ? 2.46638 1.54093 1.41630 -0.12056 0.18808  -0.10809 78  MET F C   
4272 O O   . MET D 78  ? 2.49120 1.59139 1.44863 -0.13298 0.21490  -0.09870 78  MET F O   
4273 C CB  . MET D 78  ? 2.29773 1.33373 1.28387 -0.15205 0.14186  -0.08895 78  MET F CB  
4274 C CG  . MET D 78  ? 2.23020 1.22784 1.20602 -0.17198 0.11627  -0.07246 78  MET F CG  
4275 S SD  . MET D 78  ? 2.10911 1.14161 1.16113 -0.19463 0.10603  -0.06960 78  MET F SD  
4276 C CE  . MET D 78  ? 2.07636 1.12805 1.14197 -0.18085 0.09374  -0.08683 78  MET F CE  
4277 N N   . GLN D 79  ? 2.43333 1.52985 1.39668 -0.09685 0.18635  -0.12902 79  GLN F N   
4278 C CA  . GLN D 79  ? 2.45427 1.61388 1.44380 -0.08143 0.21650  -0.14616 79  GLN F CA  
4279 C C   . GLN D 79  ? 2.41836 1.63834 1.48654 -0.09956 0.22946  -0.14522 79  GLN F C   
4280 O O   . GLN D 79  ? 2.36848 1.59342 1.46880 -0.10014 0.21023  -0.14791 79  GLN F O   
4281 C CB  . GLN D 79  ? 2.45408 1.60925 1.42134 -0.04254 0.20599  -0.17079 79  GLN F CB  
4282 C CG  . GLN D 79  ? 2.48170 1.59029 1.37522 -0.02160 0.20131  -0.18016 79  GLN F CG  
4283 C CD  . GLN D 79  ? 2.46132 1.51356 1.32130 0.00514  0.16809  -0.19332 79  GLN F CD  
4284 O OE1 . GLN D 79  ? 2.44436 1.51669 1.32426 0.03259  0.16416  -0.21068 79  GLN F OE1 
4285 N NE2 . GLN D 79  ? 2.46089 1.44098 1.27042 -0.00358 0.14235  -0.18424 79  GLN F NE2 
4286 N N   . ILE D 80  ? 2.38150 1.64836 1.47912 -0.11624 0.26212  -0.14173 80  ILE F N   
4287 C CA  . ILE D 80  ? 2.31700 1.64077 1.49008 -0.13799 0.27751  -0.14266 80  ILE F CA  
4288 C C   . ILE D 80  ? 2.30624 1.70370 1.50706 -0.13272 0.31257  -0.15893 80  ILE F C   
4289 O O   . ILE D 80  ? 2.33417 1.73671 1.50112 -0.13190 0.33459  -0.15636 80  ILE F O   
4290 C CB  . ILE D 80  ? 2.26300 1.56405 1.45267 -0.17382 0.28132  -0.11835 80  ILE F CB  
4291 C CG1 . ILE D 80  ? 2.26737 1.49393 1.41053 -0.17661 0.25065  -0.10069 80  ILE F CG1 
4292 C CG2 . ILE D 80  ? 2.15828 1.50345 1.42682 -0.19468 0.28568  -0.12351 80  ILE F CG2 
4293 C CD1 . ILE D 80  ? 2.20545 1.41898 1.36774 -0.17447 0.21921  -0.10566 80  ILE F CD1 
4294 N N   . MET D 81  ? 2.24211 1.70334 1.50554 -0.13159 0.31869  -0.17585 81  MET F N   
4295 C CA  . MET D 81  ? 2.21299 1.75630 1.51457 -0.13159 0.35252  -0.19293 81  MET F CA  
4296 C C   . MET D 81  ? 2.16600 1.72740 1.50518 -0.17467 0.37841  -0.17786 81  MET F C   
4297 O O   . MET D 81  ? 2.11215 1.68662 1.50656 -0.19743 0.37439  -0.17669 81  MET F O   
4298 C CB  . MET D 81  ? 2.16765 1.77423 1.52285 -0.11432 0.34595  -0.21691 81  MET F CB  
4299 C CG  . MET D 81  ? 2.14886 1.84357 1.53233 -0.09792 0.37321  -0.24219 81  MET F CG  
4300 S SD  . MET D 81  ? 2.15168 1.88133 1.54608 -0.04819 0.34894  -0.26864 81  MET F SD  
4301 C CE  . MET D 81  ? 2.07743 1.81295 1.52551 -0.06994 0.32570  -0.26242 81  MET F CE  
4302 N N   . ARG D 82  ? 2.20183 1.76079 1.50960 -0.18695 0.40387  -0.16578 82  ARG F N   
4303 C CA  . ARG D 82  ? 2.18608 1.76865 1.53097 -0.22826 0.43257  -0.15169 82  ARG F CA  
4304 C C   . ARG D 82  ? 2.15240 1.83463 1.55406 -0.22972 0.46077  -0.17814 82  ARG F C   
4305 O O   . ARG D 82  ? 2.17176 1.90078 1.55291 -0.21303 0.48140  -0.19171 82  ARG F O   
4306 C CB  . ARG D 82  ? 2.23435 1.78284 1.52126 -0.24281 0.45018  -0.12598 82  ARG F CB  
4307 C CG  . ARG D 82  ? 2.28003 1.75476 1.48660 -0.22074 0.42574  -0.11344 82  ARG F CG  
4308 C CD  . ARG D 82  ? 2.31333 1.74254 1.47222 -0.24559 0.43605  -0.07882 82  ARG F CD  
4309 N NE  . ARG D 82  ? 2.34633 1.70256 1.43640 -0.22825 0.40677  -0.06680 82  ARG F NE  
4310 C CZ  . ARG D 82  ? 2.38673 1.71313 1.40863 -0.23035 0.41216  -0.04776 82  ARG F CZ  
4311 N NH1 . ARG D 82  ? 2.40248 1.76196 1.41189 -0.25116 0.44637  -0.03392 82  ARG F NH1 
4312 N NH2 . ARG D 82  ? 2.40952 1.67458 1.37332 -0.21323 0.38250  -0.04234 82  ARG F NH2 
4313 N N   . ILE D 83  ? 2.09469 1.81556 1.56828 -0.24691 0.46029  -0.18943 83  ILE F N   
4314 C CA  . ILE D 83  ? 2.05207 1.87299 1.58799 -0.25339 0.48569  -0.21554 83  ILE F CA  
4315 C C   . ILE D 83  ? 2.03417 1.87004 1.61021 -0.30437 0.51505  -0.20236 83  ILE F C   
4316 O O   . ILE D 83  ? 2.00600 1.80631 1.61574 -0.33093 0.50495  -0.19216 83  ILE F O   
4317 C CB  . ILE D 83  ? 1.99402 1.85503 1.58434 -0.23915 0.46460  -0.23976 83  ILE F CB  
4318 C CG1 . ILE D 83  ? 2.00926 1.83016 1.55467 -0.19481 0.42926  -0.24342 83  ILE F CG1 
4319 C CG2 . ILE D 83  ? 1.94714 1.92107 1.59781 -0.23888 0.48849  -0.27047 83  ILE F CG2 
4320 C CD1 . ILE D 83  ? 1.95180 1.82845 1.54100 -0.17341 0.41225  -0.26787 83  ILE F CD1 
4321 N N   . LYS D 84  ? 2.04977 1.93814 1.62415 -0.31949 0.55116  -0.20320 84  LYS F N   
4322 C CA  . LYS D 84  ? 2.02032 1.93422 1.64407 -0.37101 0.57991  -0.19455 84  LYS F CA  
4323 C C   . LYS D 84  ? 1.95128 1.94042 1.66129 -0.37913 0.58051  -0.22692 84  LYS F C   
4324 O O   . LYS D 84  ? 1.92531 1.98186 1.65277 -0.34522 0.57427  -0.25749 84  LYS F O   
4325 C CB  . LYS D 84  ? 2.04600 2.00859 1.64751 -0.38832 0.62006  -0.18817 84  LYS F CB  
4326 C CG  . LYS D 84  ? 2.03449 2.01676 1.68060 -0.44793 0.65197  -0.17381 84  LYS F CG  
4327 C CD  . LYS D 84  ? 2.07949 2.07354 1.67940 -0.47099 0.68626  -0.15051 84  LYS F CD  
4328 C CE  . LYS D 84  ? 2.13222 2.04733 1.64041 -0.44366 0.66883  -0.12508 84  LYS F CE  
4329 N NZ  . LYS D 84  ? 2.19020 2.12383 1.64365 -0.46075 0.70102  -0.10427 84  LYS F NZ  
4330 N N   . PRO D 85  ? 2.09178 1.66029 2.14116 -0.04743 0.27291  -0.05582 85  PRO F N   
4331 C CA  . PRO D 85  ? 2.06507 1.57651 2.10662 -0.06195 0.21295  -0.00423 85  PRO F CA  
4332 C C   . PRO D 85  ? 2.05066 1.53723 2.22933 -0.06022 0.17277  0.01488  85  PRO F C   
4333 O O   . PRO D 85  ? 2.03738 1.47084 2.23081 -0.07644 0.11684  0.04833  85  PRO F O   
4334 C CB  . PRO D 85  ? 2.02221 1.54879 1.97712 -0.06399 0.22764  0.01634  85  PRO F CB  
4335 C CG  . PRO D 85  ? 1.95904 1.53703 1.83526 -0.05582 0.28160  -0.01050 85  PRO F CG  
4336 C CD  . PRO D 85  ? 1.98530 1.59909 1.92852 -0.04536 0.31215  -0.05892 85  PRO F CD  
4337 N N   . HIS D 86  ? 1.99559 1.52016 2.28124 -0.04194 0.19974  -0.00231 86  HIS F N   
4338 C CA  . HIS D 86  ? 1.95534 1.46305 2.39389 -0.03854 0.16286  0.02067  86  HIS F CA  
4339 C C   . HIS D 86  ? 1.93380 1.47808 2.51567 -0.01338 0.21366  -0.02143 86  HIS F C   
4340 O O   . HIS D 86  ? 1.88680 1.42776 2.61815 -0.00560 0.19378  -0.00186 86  HIS F O   
4341 C CB  . HIS D 86  ? 1.93234 1.43466 2.37207 -0.04972 0.12665  0.06522  86  HIS F CB  
4342 C CG  . HIS D 86  ? 1.92245 1.36510 2.27402 -0.08238 0.05827  0.11663  86  HIS F CG  
4343 N ND1 . HIS D 86  ? 1.92920 1.35491 2.13624 -0.10116 0.05673  0.13353  86  HIS F ND1 
4344 C CD2 . HIS D 86  ? 1.89117 1.28269 2.27358 -0.10244 -0.00744 0.15484  86  HIS F CD2 
4345 C CE1 . HIS D 86  ? 1.90013 1.26288 2.04536 -0.13388 -0.00416 0.17583  86  HIS F CE1 
4346 N NE2 . HIS D 86  ? 1.87774 1.22071 2.12464 -0.13606 -0.04718 0.19134  86  HIS F NE2 
4347 N N   . GLN D 87  ? 1.88773 1.46625 2.43025 -0.00316 0.28003  -0.07683 87  GLN F N   
4348 C CA  . GLN D 87  ? 1.84490 1.45544 2.50065 0.01635  0.34134  -0.12227 87  GLN F CA  
4349 C C   . GLN D 87  ? 1.81960 1.41085 2.54515 0.01972  0.36902  -0.16387 87  GLN F C   
4350 O O   . GLN D 87  ? 1.76711 1.36018 2.63781 0.03498  0.40361  -0.18623 87  GLN F O   
4351 C CB  . GLN D 87  ? 1.81126 1.47532 2.37664 0.02089  0.40535  -0.15895 87  GLN F CB  
4352 C CG  . GLN D 87  ? 1.79821 1.48903 2.36405 0.02679  0.40462  -0.13172 87  GLN F CG  
4353 C CD  . GLN D 87  ? 1.74460 1.47115 2.15629 0.02183  0.43211  -0.13590 87  GLN F CD  
4354 O OE1 . GLN D 87  ? 1.62710 1.39571 2.00433 0.02669  0.49246  -0.17653 87  GLN F OE1 
4355 N NE2 . GLN D 87  ? 1.80496 1.51294 2.12471 0.01008  0.38999  -0.09189 87  GLN F NE2 
4356 N N   . GLY D 88  ? 1.87364 1.44434 2.50603 0.00534  0.35966  -0.17583 88  GLY F N   
4357 C CA  . GLY D 88  ? 1.85114 1.40088 2.54291 0.00513  0.39135  -0.22035 88  GLY F CA  
4358 C C   . GLY D 88  ? 1.88711 1.42972 2.44135 -0.01472 0.38901  -0.23830 88  GLY F C   
4359 O O   . GLY D 88  ? 1.91039 1.48059 2.32566 -0.02445 0.38530  -0.22914 88  GLY F O   
4360 N N   . GLN D 89  ? 1.83321 1.33900 2.42992 -0.02116 0.39091  -0.26002 89  GLN F N   
4361 C CA  . GLN D 89  ? 1.86541 1.36338 2.34122 -0.04221 0.38415  -0.27353 89  GLN F CA  
4362 C C   . GLN D 89  ? 1.84034 1.33320 2.33943 -0.05157 0.44227  -0.34212 89  GLN F C   
4363 O O   . GLN D 89  ? 1.80118 1.28166 2.42229 -0.04068 0.48583  -0.37636 89  GLN F O   
4364 C CB  . GLN D 89  ? 1.88901 1.33449 2.36390 -0.04993 0.31456  -0.22223 89  GLN F CB  
4365 C CG  . GLN D 89  ? 1.86183 1.25718 2.45045 -0.04975 0.31141  -0.23475 89  GLN F CG  
4366 C CD  . GLN D 89  ? 1.85432 1.19802 2.46203 -0.05554 0.23616  -0.17121 89  GLN F CD  
4367 O OE1 . GLN D 89  ? 1.86309 1.20438 2.41669 -0.05967 0.18723  -0.11838 89  GLN F OE1 
4368 N NE2 . GLN D 89  ? 1.83188 1.13017 2.50868 -0.05950 0.22836  -0.17649 89  GLN F NE2 
4369 N N   . HIS D 90  ? 1.85342 1.35479 2.23284 -0.07461 0.44549  -0.36217 90  HIS F N   
4370 C CA  . HIS D 90  ? 1.83460 1.33305 2.20222 -0.09402 0.49842  -0.42964 90  HIS F CA  
4371 C C   . HIS D 90  ? 1.86812 1.36556 2.12067 -0.11955 0.47162  -0.42519 90  HIS F C   
4372 O O   . HIS D 90  ? 1.87647 1.40709 2.02097 -0.12438 0.44275  -0.38927 90  HIS F O   
4373 C CB  . HIS D 90  ? 1.78628 1.33653 2.10341 -0.10155 0.56331  -0.47950 90  HIS F CB  
4374 N N   . ILE D 91  ? 1.95084 1.41006 2.23077 -0.13628 0.48538  -0.46152 91  ILE F N   
4375 C CA  . ILE D 91  ? 1.98315 1.44031 2.16544 -0.16209 0.45993  -0.45712 91  ILE F CA  
4376 C C   . ILE D 91  ? 1.95628 1.46235 2.03329 -0.19439 0.50442  -0.51143 91  ILE F C   
4377 O O   . ILE D 91  ? 1.94564 1.43485 2.04835 -0.21331 0.55402  -0.57522 91  ILE F O   
4378 C CB  . ILE D 91  ? 2.00197 1.38937 2.26653 -0.16583 0.44345  -0.45979 91  ILE F CB  
4379 C CG1 . ILE D 91  ? 1.97213 1.32327 2.35987 -0.16255 0.50058  -0.51735 91  ILE F CG1 
4380 C CG2 . ILE D 91  ? 2.00786 1.35602 2.32888 -0.14445 0.37897  -0.38743 91  ILE F CG2 
4381 C CD1 . ILE D 91  ? 1.96942 1.24834 2.46113 -0.16193 0.48873  -0.51619 91  ILE F CD1 
4382 N N   . GLY D 92  ? 2.02962 1.59476 1.98727 -0.20368 0.48687  -0.48372 92  GLY F N   
4383 C CA  . GLY D 92  ? 1.97141 1.59704 1.82107 -0.23610 0.51676  -0.51800 92  GLY F CA  
4384 C C   . GLY D 92  ? 1.98758 1.63143 1.74946 -0.26452 0.48674  -0.50249 92  GLY F C   
4385 O O   . GLY D 92  ? 2.02988 1.65130 1.79175 -0.25338 0.44129  -0.45203 92  GLY F O   
4386 N N   . GLU D 93  ? 2.05260 1.73672 1.73760 -0.30485 0.51230  -0.54477 93  GLU F N   
4387 C CA  . GLU D 93  ? 2.07243 1.77805 1.68424 -0.33890 0.48719  -0.53669 93  GLU F CA  
4388 C C   . GLU D 93  ? 1.98143 1.77101 1.49894 -0.34367 0.46700  -0.48682 93  GLU F C   
4389 O O   . GLU D 93  ? 1.92702 1.78019 1.36720 -0.37790 0.48186  -0.50468 93  GLU F O   
4390 C CB  . GLU D 93  ? 2.10008 1.79836 1.68543 -0.38709 0.52292  -0.61013 93  GLU F CB  
4391 N N   . MET D 94  ? 2.02788 1.81545 1.55302 -0.31103 0.43368  -0.42121 94  MET F N   
4392 C CA  . MET D 94  ? 1.91890 1.77792 1.36979 -0.31187 0.41790  -0.36763 94  MET F CA  
4393 C C   . MET D 94  ? 1.93998 1.82219 1.34526 -0.34325 0.39428  -0.35198 94  MET F C   
4394 O O   . MET D 94  ? 2.03658 1.86309 1.47268 -0.34544 0.37432  -0.35026 94  MET F O   
4395 C CB  . MET D 94  ? 1.87650 1.71578 1.34627 -0.27099 0.39740  -0.30635 94  MET F CB  
4396 C CG  . MET D 94  ? 1.80903 1.66192 1.29752 -0.24381 0.41820  -0.30290 94  MET F CG  
4397 S SD  . MET D 94  ? 1.87606 1.65128 1.43070 -0.20449 0.39176  -0.26355 94  MET F SD  
4398 C CE  . MET D 94  ? 1.85296 1.61589 1.35358 -0.20952 0.35687  -0.20481 94  MET F CE  
4399 N N   . SER D 95  ? 2.00275 1.96994 1.33894 -0.36857 0.39521  -0.33632 95  SER F N   
4400 C CA  . SER D 95  ? 2.03569 2.04034 1.33419 -0.40050 0.37144  -0.31399 95  SER F CA  
4401 C C   . SER D 95  ? 1.94616 1.97530 1.23745 -0.37530 0.35038  -0.23447 95  SER F C   
4402 O O   . SER D 95  ? 1.83830 1.87628 1.13188 -0.34166 0.35786  -0.19868 95  SER F O   
4403 C CB  . SER D 95  ? 2.02569 2.11358 1.25714 -0.44951 0.37974  -0.33644 95  SER F CB  
4404 O OG  . SER D 95  ? 1.90519 2.07734 1.09829 -0.44217 0.37644  -0.28137 95  SER F OG  
4405 N N   . PHE D 96  ? 1.97957 2.01521 1.26471 -0.39322 0.32825  -0.20839 96  PHE F N   
4406 C CA  . PHE D 96  ? 1.89351 1.94884 1.17507 -0.37410 0.31597  -0.13486 96  PHE F CA  
4407 C C   . PHE D 96  ? 1.92759 2.05016 1.18891 -0.41155 0.29953  -0.11118 96  PHE F C   
4408 O O   . PHE D 96  ? 2.04971 2.17908 1.30192 -0.45235 0.29099  -0.15381 96  PHE F O   
4409 C CB  . PHE D 96  ? 1.91453 1.87369 1.22964 -0.34582 0.30612  -0.11598 96  PHE F CB  
4410 C CG  . PHE D 96  ? 1.92813 1.81586 1.27443 -0.31671 0.31287  -0.14107 96  PHE F CG  
4411 C CD1 . PHE D 96  ? 2.05950 1.88824 1.44517 -0.32418 0.31161  -0.19656 96  PHE F CD1 
4412 C CD2 . PHE D 96  ? 1.82810 1.70826 1.17160 -0.28315 0.32143  -0.10688 96  PHE F CD2 
4413 C CE1 . PHE D 96  ? 2.08539 1.85492 1.51566 -0.29730 0.31554  -0.21231 96  PHE F CE1 
4414 C CE2 . PHE D 96  ? 1.86136 1.68165 1.23955 -0.25985 0.32298  -0.12566 96  PHE F CE2 
4415 C CZ  . PHE D 96  ? 1.98778 1.75568 1.41381 -0.26624 0.31839  -0.17591 96  PHE F CZ  
4416 N N   . LEU D 97  ? 1.94072 2.11207 1.20015 -0.39868 0.29712  -0.04126 97  LEU F N   
4417 C CA  . LEU D 97  ? 1.97285 2.21626 1.22960 -0.43005 0.28049  -0.00389 97  LEU F CA  
4418 C C   . LEU D 97  ? 2.01655 2.19894 1.30271 -0.42518 0.27125  0.01747  97  LEU F C   
4419 O O   . LEU D 97  ? 1.95756 2.06221 1.25737 -0.38980 0.28093  0.03459  97  LEU F O   
4420 C CB  . LEU D 97  ? 1.85256 2.18696 1.10692 -0.41789 0.28745  0.06637  97  LEU F CB  
4421 C CG  . LEU D 97  ? 1.87869 2.30472 1.14739 -0.44621 0.26997  0.12279  97  LEU F CG  
4422 C CD1 . LEU D 97  ? 1.84014 2.36418 1.11128 -0.45230 0.25536  0.14267  97  LEU F CD1 
4423 C CD2 . LEU D 97  ? 1.80213 2.20348 1.12487 -0.40513 0.27897  0.19065  97  LEU F CD2 
4424 N N   . GLN D 98  ? 1.84889 2.06368 1.13991 -0.46525 0.25210  0.01458  98  GLN F N   
4425 C CA  . GLN D 98  ? 1.88314 2.05360 1.20261 -0.46675 0.24429  0.03918  98  GLN F CA  
4426 C C   . GLN D 98  ? 1.89792 2.16584 1.23265 -0.49771 0.23006  0.08873  98  GLN F C   
4427 O O   . GLN D 98  ? 1.94203 2.30386 1.25908 -0.53341 0.21557  0.08581  98  GLN F O   
4428 C CB  . GLN D 98  ? 2.02973 2.12144 1.35558 -0.48806 0.23317  -0.02246 98  GLN F CB  
4429 C CG  . GLN D 98  ? 2.17373 2.31844 1.48328 -0.54419 0.21754  -0.06815 98  GLN F CG  
4430 C CD  . GLN D 98  ? 2.31711 2.37721 1.63080 -0.55917 0.21949  -0.14500 98  GLN F CD  
4431 O OE1 . GLN D 98  ? 2.37254 2.43766 1.66325 -0.57902 0.22857  -0.20346 98  GLN F OE1 
4432 N NE2 . GLN D 98  ? 2.35821 2.33652 1.70366 -0.55053 0.21466  -0.14410 98  GLN F NE2 
4433 N N   . HIS D 99  ? 2.01416 2.25530 1.38233 -0.48775 0.23344  0.13397  99  HIS F N   
4434 C CA  . HIS D 99  ? 2.01983 2.34441 1.42366 -0.51124 0.22321  0.19145  99  HIS F CA  
4435 C C   . HIS D 99  ? 2.14315 2.44349 1.55646 -0.55265 0.20106  0.15676  99  HIS F C   
4436 O O   . HIS D 99  ? 2.13860 2.34795 1.56545 -0.54060 0.20832  0.15039  99  HIS F O   
4437 C CB  . HIS D 99  ? 1.89673 2.20111 1.33693 -0.47239 0.25169  0.26389  99  HIS F CB  
4438 C CG  . HIS D 99  ? 1.78297 2.12434 1.22201 -0.43695 0.27598  0.30594  99  HIS F CG  
4439 N ND1 . HIS D 99  ? 1.68845 1.98915 1.16942 -0.38505 0.30500  0.35496  99  HIS F ND1 
4440 C CD2 . HIS D 99  ? 1.75832 2.15405 1.17121 -0.43383 0.27364  0.29437  99  HIS F CD2 
4441 C CE1 . HIS D 99  ? 1.63263 1.94884 1.12692 -0.34282 0.31381  0.36407  99  HIS F CE1 
4442 N NE2 . HIS D 99  ? 1.65461 2.03231 1.11191 -0.37018 0.29274  0.33190  99  HIS F NE2 
4443 N N   . ASN D 100 ? 2.02164 1.92508 2.03847 -0.36691 -0.25117 0.58513  100 ASN F N   
4444 C CA  . ASN D 100 ? 1.91656 1.80862 1.94074 -0.34098 -0.33452 0.61238  100 ASN F CA  
4445 C C   . ASN D 100 ? 1.81388 1.73509 1.84009 -0.37593 -0.37913 0.61075  100 ASN F C   
4446 O O   . ASN D 100 ? 1.69225 1.70421 1.78515 -0.40382 -0.43494 0.64238  100 ASN F O   
4447 C CB  . ASN D 100 ? 1.95269 1.68703 1.89296 -0.25311 -0.34647 0.60824  100 ASN F CB  
4448 C CG  . ASN D 100 ? 2.07721 1.77569 2.00064 -0.21123 -0.28841 0.60789  100 ASN F CG  
4449 O OD1 . ASN D 100 ? 2.17466 1.89129 2.09992 -0.23375 -0.20946 0.59592  100 ASN F OD1 
4450 N ND2 . ASN D 100 ? 2.06721 1.71486 1.98298 -0.14837 -0.32640 0.61967  100 ASN F ND2 
4451 N N   . LYS D 101 ? 1.92399 1.77179 1.88086 -0.37440 -0.35143 0.57671  101 LYS F N   
4452 C CA  . LYS D 101 ? 1.85489 1.71635 1.80955 -0.39898 -0.38980 0.56845  101 LYS F CA  
4453 C C   . LYS D 101 ? 1.92384 1.79219 1.84744 -0.43461 -0.33775 0.52800  101 LYS F C   
4454 O O   . LYS D 101 ? 2.01312 1.79622 1.87971 -0.41294 -0.27862 0.50395  101 LYS F O   
4455 C CB  . LYS D 101 ? 1.81904 1.54234 1.71759 -0.33541 -0.43956 0.56244  101 LYS F CB  
4456 N N   . CYS D 102 ? 1.87452 1.84627 1.83911 -0.48760 -0.35737 0.52253  102 CYS F N   
4457 C CA  . CYS D 102 ? 1.90991 1.89112 1.85195 -0.51966 -0.32224 0.47821  102 CYS F CA  
4458 C C   . CYS D 102 ? 1.89911 1.83625 1.81387 -0.51026 -0.36360 0.46588  102 CYS F C   
4459 O O   . CYS D 102 ? 1.82868 1.73238 1.75333 -0.48234 -0.41788 0.49179  102 CYS F O   
4460 C CB  . CYS D 102 ? 1.79187 1.94572 1.80751 -0.58674 -0.30693 0.46975  102 CYS F CB  
4461 S SG  . CYS D 102 ? 1.77538 2.00812 1.85527 -0.60094 -0.27380 0.48254  102 CYS F SG  
4462 N N   . GLU D 103 ? 1.99551 1.93509 1.88908 -0.53401 -0.33938 0.42275  103 GLU F N   
4463 C CA  . GLU D 103 ? 1.99200 1.88757 1.86290 -0.52408 -0.37262 0.40149  103 GLU F CA  
4464 C C   . GLU D 103 ? 1.93738 1.88635 1.80902 -0.56555 -0.34060 0.35307  103 GLU F C   
4465 O O   . GLU D 103 ? 1.93175 1.92252 1.81507 -0.59361 -0.29311 0.33222  103 GLU F O   
4466 C CB  . GLU D 103 ? 2.07909 1.78618 1.86472 -0.45081 -0.38570 0.38763  103 GLU F CB  
4467 C CG  . GLU D 103 ? 2.02986 1.69682 1.82696 -0.42539 -0.45157 0.38616  103 GLU F CG  
4468 C CD  . GLU D 103 ? 2.05378 1.53481 1.76230 -0.34213 -0.47377 0.36604  103 GLU F CD  
4469 O OE1 . GLU D 103 ? 2.07802 1.47642 1.72604 -0.29796 -0.44922 0.37599  103 GLU F OE1 
4470 O OE2 . GLU D 103 ? 2.04430 1.46489 1.74350 -0.31681 -0.51632 0.33812  103 GLU F OE2 
4471 N N   . CYS D 104 ? 1.91631 1.86659 1.78784 -0.56857 -0.36932 0.33163  104 CYS F N   
4472 C CA  . CYS D 104 ? 1.85702 1.85743 1.73161 -0.60225 -0.34820 0.28017  104 CYS F CA  
4473 C C   . CYS D 104 ? 1.97136 1.80531 1.77054 -0.55663 -0.34473 0.23941  104 CYS F C   
4474 O O   . CYS D 104 ? 1.97436 1.74342 1.75982 -0.52353 -0.38865 0.23765  104 CYS F O   
4475 C CB  . CYS D 104 ? 1.69959 1.84221 1.63475 -0.63871 -0.38023 0.28674  104 CYS F CB  
4476 S SG  . CYS D 104 ? 1.54649 1.91330 1.55135 -0.69808 -0.37189 0.31326  104 CYS F SG  
4477 N N   . ARG D 105 ? 2.09622 1.85919 1.85316 -0.55270 -0.29430 0.20722  105 ARG F N   
4478 C CA  . ARG D 105 ? 2.20333 1.79731 1.87626 -0.50222 -0.28863 0.17531  105 ARG F CA  
4479 C C   . ARG D 105 ? 2.18887 1.79194 1.86686 -0.53153 -0.25266 0.12145  105 ARG F C   
4480 O O   . ARG D 105 ? 2.13669 1.84513 1.87332 -0.58216 -0.21843 0.10906  105 ARG F O   
4481 C CB  . ARG D 105 ? 2.33338 1.77414 1.92462 -0.44384 -0.25904 0.20025  105 ARG F CB  
4482 C CG  . ARG D 105 ? 2.33876 1.73803 1.91192 -0.39741 -0.30547 0.23985  105 ARG F CG  
4483 C CD  . ARG D 105 ? 2.40333 1.64299 1.87659 -0.32622 -0.27778 0.25619  105 ARG F CD  
4484 N NE  . ARG D 105 ? 2.36020 1.56473 1.82239 -0.27792 -0.32978 0.28483  105 ARG F NE  
4485 C CZ  . ARG D 105 ? 2.37539 1.45691 1.75239 -0.20652 -0.31938 0.30098  105 ARG F CZ  
4486 N NH1 . ARG D 105 ? 2.44826 1.42325 1.73524 -0.17233 -0.25294 0.29951  105 ARG F NH1 
4487 N NH2 . ARG D 105 ? 2.30983 1.37394 1.69415 -0.16551 -0.37573 0.31962  105 ARG F NH2 
4488 N N   . PRO D 106 ? 2.20344 1.69276 1.82492 -0.49662 -0.26340 0.08465  106 PRO F N   
4489 C CA  . PRO D 106 ? 2.17279 1.68147 1.81307 -0.52585 -0.24031 0.02825  106 PRO F CA  
4490 C C   . PRO D 106 ? 2.23339 1.71573 1.88271 -0.54601 -0.17278 0.02041  106 PRO F C   
4491 O O   . PRO D 106 ? 2.32600 1.72038 1.93670 -0.51988 -0.13462 0.05765  106 PRO F O   
4492 C CB  . PRO D 106 ? 2.22216 1.57758 1.78482 -0.46749 -0.26724 -0.00055 106 PRO F CB  
4493 C CG  . PRO D 106 ? 2.21397 1.53961 1.75714 -0.42633 -0.32417 0.02954  106 PRO F CG  
4494 C CD  . PRO D 106 ? 2.25770 1.60381 1.80397 -0.42648 -0.30715 0.08609  106 PRO F CD  
4495 N N   . LYS D 107 ? 2.18763 1.75275 1.89907 -0.59271 -0.15767 -0.03139 107 LYS F N   
4496 C CA  . LYS D 107 ? 2.21728 1.77773 1.97383 -0.62211 -0.09843 -0.05053 107 LYS F CA  
4497 C C   . LYS D 107 ? 2.33307 1.69908 2.01785 -0.57839 -0.06431 -0.06143 107 LYS F C   
4498 O O   . LYS D 107 ? 2.31598 1.65319 2.00257 -0.57975 -0.07302 -0.11264 107 LYS F O   
4499 C CB  . LYS D 107 ? 2.08291 1.81297 1.94013 -0.68384 -0.10582 -0.10969 107 LYS F CB  
4500 N N   . LYS D 108 ? 2.44427 1.67474 2.06129 -0.53479 -0.02366 -0.01059 108 LYS F N   
4501 C CA  . LYS D 108 ? 2.54105 1.57617 2.07324 -0.48396 0.01790  -0.00488 108 LYS F CA  
4502 C C   . LYS D 108 ? 2.53568 1.57254 2.14951 -0.52716 0.06914  -0.04243 108 LYS F C   
4503 O O   . LYS D 108 ? 2.52704 1.61770 2.22814 -0.56766 0.12076  -0.03158 108 LYS F O   
4504 C CB  . LYS D 108 ? 2.62410 1.53865 2.07394 -0.43074 0.06249  0.06196  108 LYS F CB  
4505 N N   . ASP D 109 ? 2.55561 1.53237 2.15234 -0.51730 0.05235  -0.08983 109 ASP F N   
4506 C CA  . ASP D 109 ? 2.54598 1.51164 2.22599 -0.55394 0.09251  -0.13286 109 ASP F CA  
4507 C C   . ASP D 109 ? 2.57554 1.40568 2.18881 -0.51290 0.07557  -0.16695 109 ASP F C   
4508 O O   . ASP D 109 ? 2.54258 1.37946 2.10220 -0.48634 0.01147  -0.19302 109 ASP F O   
4509 C CB  . ASP D 109 ? 2.41925 1.59770 2.24288 -0.63072 0.06778  -0.19361 109 ASP F CB  
4510 N N   . GLU E 1   ? 2.21068 1.41105 1.65697 -0.09865 0.53519  -0.06844 1   GLU A N   
4511 C CA  . GLU E 1   ? 2.36004 1.45514 1.75383 -0.09193 0.46248  -0.07721 1   GLU A CA  
4512 C C   . GLU E 1   ? 2.31770 1.39577 1.77427 -0.15397 0.45601  -0.09342 1   GLU A C   
4513 O O   . GLU E 1   ? 2.39371 1.39819 1.82219 -0.15232 0.39221  -0.09586 1   GLU A O   
4514 C CB  . GLU E 1   ? 2.44120 1.48109 1.85706 -0.08888 0.44372  -0.04884 1   GLU A CB  
4515 N N   . VAL E 2   ? 2.33332 1.47580 1.87418 -0.20454 0.51868  -0.10016 2   VAL A N   
4516 C CA  . VAL E 2   ? 2.24084 1.36931 1.83653 -0.25575 0.52543  -0.11210 2   VAL A CA  
4517 C C   . VAL E 2   ? 2.31967 1.44420 1.84996 -0.24267 0.48893  -0.13996 2   VAL A C   
4518 O O   . VAL E 2   ? 2.28456 1.45863 1.76911 -0.22451 0.50171  -0.15774 2   VAL A O   
4519 C CB  . VAL E 2   ? 2.04290 1.22459 1.71999 -0.30315 0.59684  -0.11680 2   VAL A CB  
4520 C CG1 . VAL E 2   ? 1.96508 1.13588 1.66052 -0.33864 0.60671  -0.13739 2   VAL A CG1 
4521 C CG2 . VAL E 2   ? 1.94108 1.11337 1.69827 -0.32543 0.62929  -0.08785 2   VAL A CG2 
4522 N N   . GLN E 3   ? 2.29242 1.36217 1.82762 -0.25152 0.44170  -0.13637 3   GLN A N   
4523 C CA  . GLN E 3   ? 2.31253 1.38301 1.80466 -0.24633 0.40797  -0.16037 3   GLN A CA  
4524 C C   . GLN E 3   ? 2.21073 1.26478 1.77506 -0.28448 0.40732  -0.14868 3   GLN A C   
4525 O O   . GLN E 3   ? 2.18303 1.19544 1.80993 -0.29739 0.39488  -0.11130 3   GLN A O   
4526 C CB  . GLN E 3   ? 2.45094 1.46618 1.84658 -0.19381 0.32453  -0.16427 3   GLN A CB  
4527 C CG  . GLN E 3   ? 2.54839 1.55021 1.85754 -0.13689 0.31310  -0.16210 3   GLN A CG  
4528 C CD  . GLN E 3   ? 2.64302 1.57335 1.83349 -0.07809 0.22677  -0.17306 3   GLN A CD  
4529 O OE1 . GLN E 3   ? 2.61675 1.53149 1.79393 -0.08387 0.18400  -0.18810 3   GLN A OE1 
4530 N NE2 . GLN E 3   ? 2.74360 1.62553 1.84166 -0.01704 0.19864  -0.16547 3   GLN A NE2 
4531 N N   . LEU E 4   ? 2.29458 1.38322 1.85136 -0.29852 0.42063  -0.17413 4   LEU A N   
4532 C CA  . LEU E 4   ? 2.23439 1.31350 1.84357 -0.31970 0.41392  -0.16101 4   LEU A CA  
4533 C C   . LEU E 4   ? 2.30567 1.37902 1.86726 -0.29882 0.34675  -0.17417 4   LEU A C   
4534 O O   . LEU E 4   ? 2.30496 1.40948 1.79669 -0.28439 0.34377  -0.21004 4   LEU A O   
4535 C CB  . LEU E 4   ? 2.09886 1.21625 1.73535 -0.35120 0.48633  -0.17966 4   LEU A CB  
4536 C CG  . LEU E 4   ? 1.98308 1.09023 1.67802 -0.37288 0.54837  -0.16066 4   LEU A CG  
4537 C CD1 . LEU E 4   ? 1.92069 1.04142 1.61862 -0.39513 0.60671  -0.18312 4   LEU A CD1 
4538 C CD2 . LEU E 4   ? 1.94932 1.01439 1.71601 -0.37222 0.53296  -0.10491 4   LEU A CD2 
4539 N N   . VAL E 5   ? 2.13766 1.17326 1.74613 -0.29749 0.29150  -0.13851 5   VAL A N   
4540 C CA  . VAL E 5   ? 2.19248 1.21329 1.76927 -0.27806 0.21337  -0.14369 5   VAL A CA  
4541 C C   . VAL E 5   ? 2.13254 1.17712 1.79599 -0.29922 0.21631  -0.11480 5   VAL A C   
4542 O O   . VAL E 5   ? 2.07722 1.10656 1.83335 -0.31231 0.22635  -0.06061 5   VAL A O   
4543 C CB  . VAL E 5   ? 2.30409 1.24241 1.85150 -0.24733 0.11681  -0.11949 5   VAL A CB  
4544 C CG1 . VAL E 5   ? 2.37817 1.29629 1.81996 -0.21228 0.11885  -0.14909 5   VAL A CG1 
4545 C CG2 . VAL E 5   ? 2.27536 1.17083 1.92287 -0.26529 0.10310  -0.05646 5   VAL A CG2 
4546 N N   . GLU E 6   ? 2.25245 1.33878 1.88995 -0.29935 0.21129  -0.14433 6   GLU A N   
4547 C CA  . GLU E 6   ? 2.21135 1.33167 1.92566 -0.31314 0.22115  -0.11738 6   GLU A CA  
4548 C C   . GLU E 6   ? 2.25758 1.37040 1.98714 -0.29890 0.12831  -0.10180 6   GLU A C   
4549 O O   . GLU E 6   ? 2.29936 1.39069 1.94827 -0.27866 0.06923  -0.13570 6   GLU A O   
4550 C CB  . GLU E 6   ? 2.14429 1.32374 1.83087 -0.32932 0.29486  -0.15948 6   GLU A CB  
4551 C CG  . GLU E 6   ? 2.07998 1.26983 1.70649 -0.34101 0.36068  -0.20304 6   GLU A CG  
4552 C CD  . GLU E 6   ? 1.99424 1.22938 1.58692 -0.35726 0.40463  -0.24368 6   GLU A CD  
4553 O OE1 . GLU E 6   ? 1.97278 1.21401 1.59874 -0.36662 0.45081  -0.23262 6   GLU A OE1 
4554 O OE2 . GLU E 6   ? 1.94638 1.20689 1.47587 -0.35674 0.39157  -0.28245 6   GLU A OE2 
4555 N N   . SER E 7   ? 2.04244 1.17505 1.87759 -0.30548 0.11874  -0.04585 7   SER A N   
4556 C CA  . SER E 7   ? 2.06465 1.20803 1.94001 -0.29694 0.03629  -0.02418 7   SER A CA  
4557 C C   . SER E 7   ? 2.00288 1.20382 1.99587 -0.30389 0.07318  0.03424  7   SER A C   
4558 O O   . SER E 7   ? 1.93830 1.15810 1.96382 -0.30937 0.16120  0.05454  7   SER A O   
4559 C CB  . SER E 7   ? 2.07530 1.13824 1.96695 -0.28150 -0.08261 0.01324  7   SER A CB  
4560 O OG  . SER E 7   ? 1.99842 1.03425 2.00835 -0.28929 -0.09522 0.09757  7   SER A OG  
4561 N N   . GLY E 8   ? 1.89735 1.12314 1.95362 -0.29779 0.00279  0.06618  8   GLY A N   
4562 C CA  . GLY E 8   ? 1.83018 1.12363 1.99999 -0.29541 0.03148  0.12713  8   GLY A CA  
4563 C C   . GLY E 8   ? 1.87511 1.24159 2.00906 -0.29662 0.06371  0.08042  8   GLY A C   
4564 O O   . GLY E 8   ? 1.83082 1.25802 2.05721 -0.28796 0.08243  0.13351  8   GLY A O   
4565 N N   . GLY E 9   ? 1.97880 1.34471 1.98846 -0.30451 0.06962  -0.00881 9   GLY A N   
4566 C CA  . GLY E 9   ? 1.98489 1.41846 1.96210 -0.31047 0.10124  -0.05137 9   GLY A CA  
4567 C C   . GLY E 9   ? 1.98763 1.46336 2.04242 -0.30425 0.02117  -0.01862 9   GLY A C   
4568 O O   . GLY E 9   ? 1.93892 1.37645 2.03605 -0.29657 -0.08064 0.01329  9   GLY A O   
4569 N N   . GLY E 10  ? 1.97435 1.52537 2.04452 -0.30711 0.06377  -0.02758 11  GLY A N   
4570 C CA  . GLY E 10  ? 1.95510 1.56372 2.10957 -0.30261 -0.00195 0.00464  11  GLY A CA  
4571 C C   . GLY E 10  ? 1.98641 1.68003 2.16420 -0.30070 0.07147  0.00694  11  GLY A C   
4572 O O   . GLY E 10  ? 2.01213 1.70700 2.09951 -0.30748 0.15931  -0.04431 11  GLY A O   
4573 N N   . LEU E 11  ? 1.89897 1.65905 2.19806 -0.28991 0.02713  0.06865  12  LEU A N   
4574 C CA  . LEU E 11  ? 1.92297 1.77167 2.25797 -0.28004 0.08562  0.08298  12  LEU A CA  
4575 C C   . LEU E 11  ? 1.79946 1.68891 2.27970 -0.24621 0.11168  0.19856  12  LEU A C   
4576 O O   . LEU E 11  ? 1.65835 1.53529 2.26121 -0.23851 0.04140  0.28163  12  LEU A O   
4577 C CB  . LEU E 11  ? 1.90473 1.81673 2.26930 -0.29150 0.01806  0.06436  12  LEU A CB  
4578 C CG  . LEU E 11  ? 1.88856 1.90774 2.34174 -0.27683 0.04633  0.10736  12  LEU A CG  
4579 C CD1 . LEU E 11  ? 1.99410 2.03240 2.32792 -0.28124 0.14865  0.03922  12  LEU A CD1 
4580 C CD2 . LEU E 11  ? 1.79905 1.87256 2.32772 -0.28800 -0.05336 0.11475  12  LEU A CD2 
4581 N N   . VAL E 12  ? 1.87091 1.80273 2.33341 -0.22209 0.21115  0.20871  13  VAL A N   
4582 C CA  . VAL E 12  ? 1.72477 1.70649 2.31453 -0.17602 0.25560  0.32466  13  VAL A CA  
4583 C C   . VAL E 12  ? 1.73205 1.79089 2.30274 -0.14866 0.32477  0.32156  13  VAL A C   
4584 O O   . VAL E 12  ? 1.82692 1.85795 2.24497 -0.15688 0.38709  0.23000  13  VAL A O   
4585 C CB  . VAL E 12  ? 1.69655 1.61053 2.25453 -0.15457 0.33151  0.35273  13  VAL A CB  
4586 C CG1 . VAL E 12  ? 1.57368 1.54318 2.22578 -0.09454 0.40688  0.46283  13  VAL A CG1 
4587 C CG2 . VAL E 12  ? 1.63500 1.48689 2.25324 -0.17395 0.25918  0.38808  13  VAL A CG2 
4588 N N   . GLN E 13  ? 1.71645 1.87071 2.44518 -0.11508 0.30945  0.42636  14  GLN A N   
4589 C CA  . GLN E 13  ? 1.69680 1.92727 2.41120 -0.07808 0.38076  0.43567  14  GLN A CA  
4590 C C   . GLN E 13  ? 1.67819 1.86694 2.30639 -0.02386 0.50443  0.45363  14  GLN A C   
4591 O O   . GLN E 13  ? 1.62922 1.77396 2.29729 -0.00152 0.52983  0.51674  14  GLN A O   
4592 C CB  . GLN E 13  ? 1.52962 1.88261 2.45065 -0.04872 0.33613  0.55772  14  GLN A CB  
4593 C CG  . GLN E 13  ? 1.47138 1.85197 2.51414 -0.09261 0.19696  0.57263  14  GLN A CG  
4594 C CD  . GLN E 13  ? 1.32557 1.83971 2.53182 -0.07303 0.15938  0.65314  14  GLN A CD  
4595 O OE1 . GLN E 13  ? 1.37246 1.92606 2.56389 -0.10586 0.10537  0.59169  14  GLN A OE1 
4596 N NE2 . GLN E 13  ? 1.14207 1.73218 2.51203 -0.01631 0.19130  0.79847  14  GLN A NE2 
4597 N N   . PRO E 14  ? 1.83084 2.02223 2.33093 -0.00107 0.57919  0.39667  15  PRO A N   
4598 C CA  . PRO E 14  ? 1.79837 1.93664 2.19676 0.06232  0.69343  0.41226  15  PRO A CA  
4599 C C   . PRO E 14  ? 1.69027 1.87834 2.24124 0.13455  0.73417  0.56832  15  PRO A C   
4600 O O   . PRO E 14  ? 1.59042 1.89264 2.30422 0.16703  0.71505  0.67262  15  PRO A O   
4601 C CB  . PRO E 14  ? 1.77568 1.93967 2.06286 0.08349  0.73878  0.35661  15  PRO A CB  
4602 C CG  . PRO E 14  ? 1.84183 2.01050 2.08569 0.00192  0.66027  0.25054  15  PRO A CG  
4603 C CD  . PRO E 14  ? 1.87924 2.09797 2.29294 -0.03740 0.55817  0.29998  15  PRO A CD  
4604 N N   . GLY E 15  ? 1.77126 1.87621 2.27576 0.16067  0.79196  0.59042  16  GLY A N   
4605 C CA  . GLY E 15  ? 1.70679 1.84415 2.35161 0.22595  0.83536  0.74215  16  GLY A CA  
4606 C C   . GLY E 15  ? 1.65330 1.77261 2.43676 0.18555  0.76530  0.80284  16  GLY A C   
4607 O O   . GLY E 15  ? 1.61187 1.73327 2.49146 0.23329  0.80924  0.92157  16  GLY A O   
4608 N N   . GLY E 16  ? 1.62993 1.72601 2.42004 0.10390  0.65920  0.72854  17  GLY A N   
4609 C CA  . GLY E 16  ? 1.56243 1.63089 2.47238 0.06569  0.57747  0.78042  17  GLY A CA  
4610 C C   . GLY E 16  ? 1.64084 1.59115 2.43017 0.04048  0.60667  0.71350  17  GLY A C   
4611 O O   . GLY E 16  ? 1.74369 1.63036 2.36458 0.05587  0.69418  0.63590  17  GLY A O   
4612 N N   . SER E 17  ? 1.70212 1.61771 2.57803 -0.00076 0.52208  0.74194  18  SER A N   
4613 C CA  . SER E 17  ? 1.74247 1.55885 2.54830 -0.02287 0.54049  0.70741  18  SER A CA  
4614 C C   . SER E 17  ? 1.76121 1.52505 2.53745 -0.09003 0.43017  0.62987  18  SER A C   
4615 O O   . SER E 17  ? 1.74143 1.54018 2.57081 -0.11489 0.33227  0.62174  18  SER A O   
4616 C CB  . SER E 17  ? 1.64089 1.46252 2.59261 0.01238  0.55925  0.84794  18  SER A CB  
4617 O OG  . SER E 17  ? 1.65158 1.55133 2.64459 0.09280  0.63237  0.91778  18  SER A OG  
4618 N N   . LEU E 18  ? 1.86190 1.28463 1.91344 0.02608  0.88256  0.09364  19  LEU A N   
4619 C CA  . LEU E 18  ? 1.86570 1.32358 1.91557 -0.04413 0.80157  0.05881  19  LEU A CA  
4620 C C   . LEU E 18  ? 1.87395 1.36688 1.94360 -0.06782 0.74656  0.05279  19  LEU A C   
4621 O O   . LEU E 18  ? 1.89527 1.36975 1.90594 -0.02904 0.75539  0.05066  19  LEU A O   
4622 C CB  . LEU E 18  ? 1.88349 1.31420 1.78174 -0.03871 0.78400  0.01076  19  LEU A CB  
4623 C CG  . LEU E 18  ? 1.89863 1.35794 1.76950 -0.09469 0.71353  -0.02070 19  LEU A CG  
4624 C CD1 . LEU E 18  ? 1.91303 1.34073 1.63396 -0.07381 0.71872  -0.05941 19  LEU A CD1 
4625 C CD2 . LEU E 18  ? 1.90090 1.40043 1.77268 -0.12567 0.64924  -0.03297 19  LEU A CD2 
4626 N N   . ARG E 19  ? 1.73252 1.26918 1.87747 -0.12561 0.68622  0.04771  20  ARG A N   
4627 C CA  . ARG E 19  ? 1.74003 1.30790 1.89733 -0.14863 0.63303  0.04017  20  ARG A CA  
4628 C C   . ARG E 19  ? 1.75299 1.33501 1.82754 -0.18018 0.57053  0.00304  20  ARG A C   
4629 O O   . ARG E 19  ? 1.74979 1.34192 1.83047 -0.20540 0.54214  -0.00889 20  ARG A O   
4630 C CB  . ARG E 19  ? 1.70360 1.31016 2.01156 -0.17741 0.61417  0.06476  20  ARG A CB  
4631 C CG  . ARG E 19  ? 1.68285 1.32075 2.03340 -0.22582 0.54091  0.04351  20  ARG A CG  
4632 C CD  . ARG E 19  ? 1.64796 1.32013 2.13796 -0.24589 0.51455  0.05891  20  ARG A CD  
4633 N NE  . ARG E 19  ? 1.66333 1.34593 2.14744 -0.23249 0.51807  0.06816  20  ARG A NE  
4634 C CZ  . ARG E 19  ? 1.64350 1.35320 2.23856 -0.23803 0.51150  0.08559  20  ARG A CZ  
4635 N NH1 . ARG E 19  ? 1.59900 1.33067 2.33404 -0.25841 0.49884  0.09532  20  ARG A NH1 
4636 N NH2 . ARG E 19  ? 1.67272 1.38569 2.23967 -0.22155 0.51373  0.09207  20  ARG A NH2 
4637 N N   . LEU E 20  ? 1.71496 1.29412 1.70848 -0.17267 0.55041  -0.01262 21  LEU A N   
4638 C CA  . LEU E 20  ? 1.71851 1.32147 1.65114 -0.20058 0.49438  -0.03597 21  LEU A CA  
4639 C C   . LEU E 20  ? 1.70379 1.34271 1.70429 -0.22905 0.44808  -0.02712 21  LEU A C   
4640 O O   . LEU E 20  ? 1.69683 1.33619 1.75743 -0.22297 0.45742  -0.01007 21  LEU A O   
4641 C CB  . LEU E 20  ? 1.72748 1.30936 1.55682 -0.17917 0.49590  -0.05389 21  LEU A CB  
4642 C CG  . LEU E 20  ? 1.72242 1.26144 1.47595 -0.13973 0.54261  -0.06870 21  LEU A CG  
4643 C CD1 . LEU E 20  ? 1.70988 1.21997 1.37134 -0.10951 0.53969  -0.09169 21  LEU A CD1 
4644 C CD2 . LEU E 20  ? 1.72145 1.27136 1.43715 -0.15719 0.53375  -0.08380 21  LEU A CD2 
4645 N N   . SER E 21  ? 1.72402 1.39092 1.70189 -0.25214 0.39856  -0.03873 22  SER A N   
4646 C CA  . SER E 21  ? 1.71999 1.41623 1.75062 -0.26979 0.35391  -0.03332 22  SER A CA  
4647 C C   . SER E 21  ? 1.74528 1.46137 1.70091 -0.27624 0.31966  -0.03845 22  SER A C   
4648 O O   . SER E 21  ? 1.77237 1.49653 1.65520 -0.27480 0.30934  -0.04796 22  SER A O   
4649 C CB  . SER E 21  ? 1.72324 1.43281 1.82431 -0.27999 0.32205  -0.03667 22  SER A CB  
4650 O OG  . SER E 21  ? 1.69808 1.38898 1.86251 -0.27672 0.35783  -0.02938 22  SER A OG  
4651 N N   . CYS E 22  ? 1.63131 1.35644 1.60788 -0.28158 0.30381  -0.02865 23  CYS A N   
4652 C CA  . CYS E 22  ? 1.65579 1.40097 1.58489 -0.28818 0.27602  -0.02292 23  CYS A CA  
4653 C C   . CYS E 22  ? 1.68831 1.45161 1.66468 -0.29064 0.24306  -0.01542 23  CYS A C   
4654 O O   . CYS E 22  ? 1.67147 1.42517 1.68578 -0.29256 0.24577  -0.00899 23  CYS A O   
4655 C CB  . CYS E 22  ? 1.63230 1.35675 1.53373 -0.28723 0.29132  -0.01870 23  CYS A CB  
4656 S SG  . CYS E 22  ? 1.64318 1.39009 1.51324 -0.30086 0.26160  -0.00274 23  CYS A SG  
4657 N N   . ALA E 23  ? 1.54132 1.32613 1.50616 -0.28282 0.20968  -0.01817 24  ALA A N   
4658 C CA  . ALA E 23  ? 1.60233 1.39886 1.59826 -0.27183 0.17452  -0.01599 24  ALA A CA  
4659 C C   . ALA E 23  ? 1.67161 1.48801 1.61217 -0.26464 0.16212  0.00377  24  ALA A C   
4660 O O   . ALA E 23  ? 1.67213 1.50408 1.55352 -0.26588 0.16919  0.01490  24  ALA A O   
4661 C CB  . ALA E 23  ? 1.64628 1.44578 1.66154 -0.25349 0.13751  -0.03181 24  ALA A CB  
4662 N N   . ALA E 24  ? 1.60728 1.42407 1.57053 -0.25550 0.14638  0.01045  25  ALA A N   
4663 C CA  . ALA E 24  ? 1.67456 1.50669 1.59825 -0.24902 0.14344  0.03726  25  ALA A CA  
4664 C C   . ALA E 24  ? 1.78944 1.63101 1.70052 -0.20894 0.11128  0.04041  25  ALA A C   
4665 O O   . ALA E 24  ? 1.85114 1.67793 1.80237 -0.19253 0.08885  0.01744  25  ALA A O   
4666 C CB  . ALA E 24  ? 1.59666 1.41029 1.54305 -0.26999 0.15944  0.04771  25  ALA A CB  
4667 N N   . SER E 25  ? 1.88183 1.74810 1.73855 -0.18758 0.10942  0.07037  26  SER A N   
4668 C CA  . SER E 25  ? 1.94982 1.82362 1.77355 -0.13297 0.08300  0.08065  26  SER A CA  
4669 C C   . SER E 25  ? 1.92313 1.80936 1.73119 -0.12793 0.10326  0.12333  26  SER A C   
4670 O O   . SER E 25  ? 1.82559 1.73093 1.63151 -0.15912 0.12951  0.15307  26  SER A O   
4671 C CB  . SER E 25  ? 1.91473 1.80887 1.67559 -0.09280 0.06126  0.08505  26  SER A CB  
4672 O OG  . SER E 25  ? 1.90762 1.78728 1.68417 -0.10419 0.04420  0.04931  26  SER A OG  
4673 N N   . GLY E 26  ? 1.98301 1.85638 1.78290 -0.08471 0.08898  0.12592  27  GLY A N   
4674 C CA  . GLY E 26  ? 1.97211 1.85204 1.75538 -0.06791 0.10876  0.16961  27  GLY A CA  
4675 C C   . GLY E 26  ? 1.94277 1.80329 1.76945 -0.11792 0.13121  0.17894  27  GLY A C   
4676 O O   . GLY E 26  ? 1.90711 1.77525 1.72975 -0.11641 0.15142  0.22345  27  GLY A O   
4677 N N   . PHE E 27  ? 2.00723 1.84124 1.87537 -0.15762 0.12747  0.14203  28  PHE A N   
4678 C CA  . PHE E 27  ? 1.95419 1.76126 1.85148 -0.19675 0.14019  0.14651  28  PHE A CA  
4679 C C   . PHE E 27  ? 1.95414 1.73550 1.88617 -0.21708 0.13259  0.10286  28  PHE A C   
4680 O O   . PHE E 27  ? 1.91876 1.70774 1.86616 -0.23032 0.13336  0.08332  28  PHE A O   
4681 C CB  . PHE E 27  ? 1.82897 1.64586 1.73813 -0.23872 0.15847  0.17939  28  PHE A CB  
4682 C CG  . PHE E 27  ? 1.74661 1.56214 1.66989 -0.27130 0.16144  0.15657  28  PHE A CG  
4683 C CD1 . PHE E 27  ? 1.73912 1.58275 1.64292 -0.26288 0.16208  0.14835  28  PHE A CD1 
4684 C CD2 . PHE E 27  ? 1.68025 1.46023 1.62642 -0.30172 0.16235  0.14178  28  PHE A CD2 
4685 C CE1 . PHE E 27  ? 1.66773 1.50459 1.57711 -0.28712 0.16924  0.12636  28  PHE A CE1 
4686 C CE2 . PHE E 27  ? 1.61039 1.38283 1.56069 -0.31861 0.16835  0.12081  28  PHE A CE2 
4687 C CZ  . PHE E 27  ? 1.60338 1.40426 1.53657 -0.31263 0.17452  0.11290  28  PHE A CZ  
4688 N N   . ASP E 28  ? 1.85874 1.61071 1.80200 -0.21556 0.12782  0.08999  29  ASP A N   
4689 C CA  . ASP E 28  ? 1.83191 1.56726 1.81209 -0.22684 0.12382  0.05544  29  ASP A CA  
4690 C C   . ASP E 28  ? 1.68056 1.40208 1.67108 -0.26392 0.14030  0.06068  29  ASP A C   
4691 O O   . ASP E 28  ? 1.62910 1.33519 1.60249 -0.28204 0.14454  0.08341  29  ASP A O   
4692 C CB  . ASP E 28  ? 1.90013 1.61016 1.88063 -0.20944 0.11341  0.04047  29  ASP A CB  
4693 C CG  . ASP E 28  ? 1.85888 1.56145 1.88602 -0.21477 0.11082  0.00959  29  ASP A CG  
4694 O OD1 . ASP E 28  ? 1.76997 1.48493 1.83300 -0.23070 0.12052  0.00322  29  ASP A OD1 
4695 O OD2 . ASP E 28  ? 1.90967 1.59525 1.93799 -0.20002 0.10182  -0.00586 29  ASP A OD2 
4696 N N   . LEU E 29  ? 1.81573 1.53966 1.83717 -0.27011 0.14779  0.04029  30  LEU A N   
4697 C CA  . LEU E 29  ? 1.70759 1.41114 1.72996 -0.28872 0.16453  0.04210  30  LEU A CA  
4698 C C   . LEU E 29  ? 1.69882 1.36810 1.71952 -0.28562 0.16224  0.04002  30  LEU A C   
4699 O O   . LEU E 29  ? 1.66051 1.29962 1.65959 -0.29223 0.16453  0.04765  30  LEU A O   
4700 C CB  . LEU E 29  ? 1.65702 1.37101 1.70989 -0.28799 0.18086  0.02685  30  LEU A CB  
4701 C CG  . LEU E 29  ? 1.65972 1.39899 1.69766 -0.29127 0.18264  0.02761  30  LEU A CG  
4702 C CD1 . LEU E 29  ? 1.59445 1.33001 1.65131 -0.29322 0.20554  0.01635  30  LEU A CD1 
4703 C CD2 . LEU E 29  ? 1.64532 1.38517 1.63917 -0.30384 0.18268  0.04841  30  LEU A CD2 
4704 N N   . TRP E 30  ? 1.66657 1.33693 1.70555 -0.26989 0.15315  0.02699  35  TRP A N   
4705 C CA  . TRP E 30  ? 1.66621 1.30857 1.70047 -0.26107 0.15215  0.02281  35  TRP A CA  
4706 C C   . TRP E 30  ? 1.66570 1.26755 1.64733 -0.26887 0.14074  0.03964  35  TRP A C   
4707 O O   . TRP E 30  ? 1.64274 1.21288 1.60576 -0.26454 0.14177  0.04271  35  TRP A O   
4708 C CB  . TRP E 30  ? 1.74587 1.39776 1.80041 -0.24193 0.13879  0.00441  35  TRP A CB  
4709 C CG  . TRP E 30  ? 1.76014 1.38720 1.79970 -0.22914 0.13585  0.00012  35  TRP A CG  
4710 C CD1 . TRP E 30  ? 1.82353 1.42313 1.81406 -0.21990 0.11915  -0.00101 35  TRP A CD1 
4711 C CD2 . TRP E 30  ? 1.72521 1.35135 1.79083 -0.21843 0.15176  0.00020  35  TRP A CD2 
4712 N NE1 . TRP E 30  ? 1.82875 1.40997 1.80659 -0.20493 0.11867  -0.00567 35  TRP A NE1 
4713 C CE2 . TRP E 30  ? 1.77520 1.37487 1.79999 -0.20138 0.13980  -0.00242 35  TRP A CE2 
4714 C CE3 . TRP E 30  ? 1.67105 1.31565 1.78783 -0.21655 0.17813  0.00589  35  TRP A CE3 
4715 C CZ2 . TRP E 30  ? 1.78129 1.37670 1.81204 -0.17935 0.15183  0.00219  35  TRP A CZ2 
4716 C CZ3 . TRP E 30  ? 1.68116 1.32162 1.81166 -0.19400 0.19543  0.01425  35  TRP A CZ3 
4717 C CH2 . TRP E 30  ? 1.73957 1.35774 1.82601 -0.17409 0.18148  0.01314  35  TRP A CH2 
4718 N N   . TYR E 31  ? 1.69286 1.29219 1.65178 -0.27601 0.12843  0.05346  36  TYR A N   
4719 C CA  . TYR E 31  ? 1.69226 1.25096 1.61713 -0.28804 0.11316  0.07307  36  TYR A CA  
4720 C C   . TYR E 31  ? 1.63915 1.19628 1.57022 -0.31040 0.11248  0.09061  36  TYR A C   
4721 O O   . TYR E 31  ? 1.64692 1.19446 1.57649 -0.32668 0.10155  0.11545  36  TYR A O   
4722 C CB  . TYR E 31  ? 1.76147 1.31721 1.66794 -0.28335 0.10580  0.08673  36  TYR A CB  
4723 C CG  . TYR E 31  ? 1.84552 1.40942 1.74496 -0.25424 0.10497  0.06422  36  TYR A CG  
4724 C CD1 . TYR E 31  ? 1.86668 1.40522 1.74886 -0.23983 0.09633  0.04391  36  TYR A CD1 
4725 C CD2 . TYR E 31  ? 1.92454 1.51940 1.83010 -0.23373 0.10904  0.06218  36  TYR A CD2 
4726 C CE1 . TYR E 31  ? 1.95424 1.50110 1.83441 -0.21160 0.09218  0.01905  36  TYR A CE1 
4727 C CE2 . TYR E 31  ? 2.03224 1.62811 1.93176 -0.19960 0.10072  0.03496  36  TYR A CE2 
4728 C CZ  . TYR E 31  ? 2.04197 1.61544 1.93353 -0.19159 0.09252  0.01187  36  TYR A CZ  
4729 O OH  . TYR E 31  ? 2.15780 1.73364 2.04820 -0.15609 0.08122  -0.01964 36  TYR A OH  
4730 N N   . TYR E 32  ? 1.68043 1.24552 1.62228 -0.31005 0.12431  0.07961  37  TYR A N   
4731 C CA  . TYR E 32  ? 1.64484 1.21286 1.59131 -0.32723 0.12295  0.09003  37  TYR A CA  
4732 C C   . TYR E 32  ? 1.62739 1.17395 1.56402 -0.31213 0.13111  0.07111  37  TYR A C   
4733 O O   . TYR E 32  ? 1.65026 1.17130 1.57423 -0.28772 0.13481  0.05943  37  TYR A O   
4734 C CB  . TYR E 32  ? 1.63225 1.25561 1.59473 -0.33668 0.13775  0.10134  37  TYR A CB  
4735 C CG  . TYR E 32  ? 1.66659 1.30551 1.63364 -0.34522 0.13183  0.13300  37  TYR A CG  
4736 C CD1 . TYR E 32  ? 1.65118 1.28265 1.63425 -0.36735 0.12114  0.16140  37  TYR A CD1 
4737 C CD2 . TYR E 32  ? 1.72930 1.38869 1.68951 -0.32566 0.13698  0.13605  37  TYR A CD2 
4738 C CE1 . TYR E 32  ? 1.67960 1.32859 1.67633 -0.37207 0.12388  0.20008  37  TYR A CE1 
4739 C CE2 . TYR E 32  ? 1.77344 1.44426 1.73085 -0.32148 0.13868  0.16972  37  TYR A CE2 
4740 C CZ  . TYR E 32  ? 1.73907 1.40702 1.71695 -0.34588 0.13619  0.20575  37  TYR A CZ  
4741 O OH  . TYR E 32  ? 1.77164 1.45395 1.75589 -0.33907 0.14555  0.24882  37  TYR A OH  
4742 N N   . SER E 33  ? 1.63428 1.19064 1.57256 -0.32042 0.13589  0.07008  38  SER A N   
4743 C CA  . SER E 33  ? 1.64755 1.17509 1.56573 -0.29814 0.14375  0.05158  38  SER A CA  
4744 C C   . SER E 33  ? 1.61160 1.17847 1.53346 -0.30341 0.16910  0.04407  38  SER A C   
4745 O O   . SER E 33  ? 1.58742 1.18833 1.51850 -0.32657 0.16446  0.05566  38  SER A O   
4746 C CB  . SER E 33  ? 1.69188 1.16623 1.59366 -0.29439 0.10836  0.05024  38  SER A CB  
4747 O OG  . SER E 33  ? 1.73451 1.16344 1.62209 -0.28459 0.08004  0.05536  38  SER A OG  
4748 N N   . ILE E 34  ? 1.57558 1.07154 1.52719 -0.23972 0.22498  -0.11003 39  ILE A N   
4749 C CA  . ILE E 34  ? 1.60842 1.08422 1.49780 -0.22690 0.24267  -0.11897 39  ILE A CA  
4750 C C   . ILE E 34  ? 1.62759 1.15635 1.55916 -0.20105 0.24138  -0.14364 39  ILE A C   
4751 O O   . ILE E 34  ? 1.64494 1.20955 1.59971 -0.19577 0.22515  -0.14943 39  ILE A O   
4752 C CB  . ILE E 34  ? 1.63235 1.05671 1.43589 -0.24366 0.23426  -0.10363 39  ILE A CB  
4753 C CG1 . ILE E 34  ? 1.64581 1.01276 1.38204 -0.26712 0.23714  -0.08609 39  ILE A CG1 
4754 C CG2 . ILE E 34  ? 1.66803 1.07777 1.43400 -0.22599 0.24743  -0.11428 39  ILE A CG2 
4755 C CD1 . ILE E 34  ? 1.66447 1.02850 1.39818 -0.25483 0.26890  -0.08830 39  ILE A CD1 
4756 N N   . HIS E 35  ? 1.55100 1.09168 1.49297 -0.18360 0.25933  -0.15444 40  HIS A N   
4757 C CA  . HIS E 35  ? 1.58561 1.18067 1.55981 -0.16108 0.25620  -0.17381 40  HIS A CA  
4758 C C   . HIS E 35  ? 1.62670 1.20662 1.55486 -0.15019 0.27348  -0.16324 40  HIS A C   
4759 O O   . HIS E 35  ? 1.62547 1.15126 1.50978 -0.15288 0.29452  -0.15121 40  HIS A O   
4760 C CB  . HIS E 35  ? 1.57232 1.20355 1.62032 -0.15216 0.25399  -0.19084 40  HIS A CB  
4761 C CG  . HIS E 35  ? 1.52938 1.16585 1.63778 -0.16267 0.23484  -0.20092 40  HIS A CG  
4762 N ND1 . HIS E 35  ? 1.53411 1.21157 1.69711 -0.15189 0.21078  -0.23499 40  HIS A ND1 
4763 C CD2 . HIS E 35  ? 1.48918 1.09398 1.61191 -0.18198 0.23514  -0.18039 40  HIS A CD2 
4764 C CE1 . HIS E 35  ? 1.49387 1.15768 1.71269 -0.16315 0.19728  -0.23666 40  HIS A CE1 
4765 N NE2 . HIS E 35  ? 1.46536 1.09009 1.66500 -0.18302 0.21125  -0.19869 40  HIS A NE2 
4766 N N   . TRP E 36  ? 1.63269 1.26377 1.57308 -0.13504 0.26543  -0.16750 41  TRP A N   
4767 C CA  . TRP E 36  ? 1.67717 1.30990 1.60014 -0.12171 0.27866  -0.15310 41  TRP A CA  
4768 C C   . TRP E 36  ? 1.71487 1.41887 1.69052 -0.10256 0.27740  -0.16282 41  TRP A C   
4769 O O   . TRP E 36  ? 1.72488 1.49336 1.72754 -0.09608 0.25677  -0.18114 41  TRP A O   
4770 C CB  . TRP E 36  ? 1.70995 1.35021 1.60646 -0.12387 0.26660  -0.13325 41  TRP A CB  
4771 C CG  . TRP E 36  ? 1.67585 1.24635 1.52393 -0.14715 0.25895  -0.11928 41  TRP A CG  
4772 C CD1 . TRP E 36  ? 1.64991 1.21849 1.49644 -0.16442 0.24160  -0.11763 41  TRP A CD1 
4773 C CD2 . TRP E 36  ? 1.67390 1.16274 1.46922 -0.15692 0.26449  -0.10556 41  TRP A CD2 
4774 N NE1 . TRP E 36  ? 1.62966 1.12636 1.42512 -0.18853 0.23206  -0.09919 41  TRP A NE1 
4775 C CE2 . TRP E 36  ? 1.64841 1.09019 1.40645 -0.18452 0.24432  -0.09638 41  TRP A CE2 
4776 C CE3 . TRP E 36  ? 1.70084 1.14864 1.47957 -0.14388 0.28311  -0.10138 41  TRP A CE3 
4777 C CZ2 . TRP E 36  ? 1.65655 1.00812 1.35225 -0.20253 0.23671  -0.08858 41  TRP A CZ2 
4778 C CZ3 . TRP E 36  ? 1.70966 1.06263 1.42862 -0.15679 0.28042  -0.09762 41  TRP A CZ3 
4779 C CH2 . TRP E 36  ? 1.69142 0.99510 1.36473 -0.18743 0.25472  -0.09392 41  TRP A CH2 
4780 N N   . VAL E 37  ? 1.57358 1.26584 1.56105 -0.09226 0.29924  -0.15039 42  VAL A N   
4781 C CA  . VAL E 37  ? 1.60752 1.36431 1.64911 -0.07680 0.29816  -0.14762 42  VAL A CA  
4782 C C   . VAL E 37  ? 1.63527 1.38848 1.66942 -0.06227 0.31653  -0.11757 42  VAL A C   
4783 O O   . VAL E 37  ? 1.63754 1.32194 1.64554 -0.05793 0.34488  -0.10484 42  VAL A O   
4784 C CB  . VAL E 37  ? 1.59806 1.35290 1.68925 -0.07721 0.30845  -0.14871 42  VAL A CB  
4785 C CG1 . VAL E 37  ? 1.63178 1.45915 1.78712 -0.06607 0.29839  -0.14144 42  VAL A CG1 
4786 C CG2 . VAL E 37  ? 1.54737 1.29763 1.66003 -0.09333 0.28843  -0.17273 42  VAL A CG2 
4787 N N   . ARG E 38  ? 1.65163 1.47889 1.70808 -0.05298 0.30059  -0.10620 43  ARG A N   
4788 C CA  . ARG E 38  ? 1.65850 1.49546 1.72708 -0.03934 0.31331  -0.06960 43  ARG A CA  
4789 C C   . ARG E 38  ? 1.65477 1.54892 1.78731 -0.02588 0.31851  -0.05355 43  ARG A C   
4790 O O   . ARG E 38  ? 1.66052 1.61951 1.82576 -0.02931 0.29547  -0.07025 43  ARG A O   
4791 C CB  . ARG E 38  ? 1.66132 1.55610 1.72070 -0.03882 0.29220  -0.05110 43  ARG A CB  
4792 C CG  . ARG E 38  ? 1.66477 1.67593 1.76048 -0.02884 0.27149  -0.04476 43  ARG A CG  
4793 C CD  . ARG E 38  ? 1.66661 1.74612 1.76562 -0.02183 0.26146  -0.00375 43  ARG A CD  
4794 N NE  . ARG E 38  ? 1.66082 1.75504 1.72189 -0.02741 0.24922  -0.00814 43  ARG A NE  
4795 C CZ  . ARG E 38  ? 1.65825 1.85312 1.71834 -0.01841 0.23480  0.01489  43  ARG A CZ  
4796 N NH1 . ARG E 38  ? 1.65591 1.94946 1.74165 -0.00592 0.22554  0.03710  43  ARG A NH1 
4797 N NH2 . ARG E 38  ? 1.64771 1.85302 1.68179 -0.02133 0.22976  0.02034  43  ARG A NH2 
4798 N N   . GLN E 39  ? 1.66990 1.53288 1.82368 -0.01063 0.34785  -0.02220 44  GLN A N   
4799 C CA  . GLN E 39  ? 1.66084 1.57776 1.88703 0.00442  0.35751  0.00726  44  GLN A CA  
4800 C C   . GLN E 39  ? 1.66611 1.61621 1.91985 0.01754  0.35887  0.05110  44  GLN A C   
4801 O O   . GLN E 39  ? 1.68140 1.55806 1.92269 0.02873  0.38478  0.06699  44  GLN A O   
4802 C CB  . GLN E 39  ? 1.65227 1.50574 1.89294 0.01741  0.39973  0.01223  44  GLN A CB  
4803 C CG  . GLN E 39  ? 1.63019 1.54542 1.95937 0.03003  0.40957  0.04381  44  GLN A CG  
4804 C CD  . GLN E 39  ? 1.61641 1.47691 1.95533 0.04498  0.45580  0.04992  44  GLN A CD  
4805 O OE1 . GLN E 39  ? 1.63863 1.40840 1.91195 0.05464  0.48873  0.03557  44  GLN A OE1 
4806 N NE2 . GLN E 39  ? 1.58576 1.50485 2.00537 0.04654  0.45662  0.07307  44  GLN A NE2 
4807 N N   . ALA E 40  ? 1.51584 1.57488 1.80571 0.01572  0.32819  0.07022  45  ALA A N   
4808 C CA  . ALA E 40  ? 1.51324 1.62194 1.84348 0.02705  0.32704  0.12384  45  ALA A CA  
4809 C C   . ALA E 40  ? 1.49944 1.59975 1.90484 0.04721  0.35765  0.16401  45  ALA A C   
4810 O O   . ALA E 40  ? 1.48491 1.58604 1.92183 0.05036  0.36933  0.15608  45  ALA A O   
4811 C CB  . ALA E 40  ? 1.51749 1.75830 1.85886 0.02063  0.28589  0.13607  45  ALA A CB  
4812 N N   . PRO E 41  ? 1.48536 1.57847 1.93111 0.06248  0.37199  0.21268  46  PRO A N   
4813 C CA  . PRO E 41  ? 1.47467 1.55503 2.00000 0.08795  0.40711  0.25307  46  PRO A CA  
4814 C C   . PRO E 41  ? 1.43429 1.62075 2.03155 0.08693  0.39309  0.27773  46  PRO A C   
4815 O O   . PRO E 41  ? 1.42186 1.72207 2.05381 0.07711  0.35576  0.30972  46  PRO A O   
4816 C CB  . PRO E 41  ? 1.47973 1.56927 2.05177 0.09892  0.40700  0.30821  46  PRO A CB  
4817 C CG  . PRO E 41  ? 1.48248 1.61411 2.00510 0.07673  0.36803  0.30492  46  PRO A CG  
4818 C CD  . PRO E 41  ? 1.49544 1.58670 1.92600 0.05842  0.35831  0.23690  46  PRO A CD  
4819 N N   . GLY E 42  ? 1.45074 1.60536 2.07233 0.09641  0.42117  0.26754  47  GLY A N   
4820 C CA  . GLY E 42  ? 1.41278 1.66293 2.11542 0.09199  0.40439  0.29624  47  GLY A CA  
4821 C C   . GLY E 42  ? 1.43355 1.75465 2.10920 0.05991  0.34772  0.26013  47  GLY A C   
4822 O O   . GLY E 42  ? 1.42277 1.83451 2.16575 0.04974  0.31719  0.28499  47  GLY A O   
4823 N N   . LYS E 43  ? 1.36247 1.64437 1.94548 0.04402  0.33011  0.20230  48  LYS A N   
4824 C CA  . LYS E 43  ? 1.40029 1.73856 1.95280 0.01895  0.27807  0.15876  48  LYS A CA  
4825 C C   . LYS E 43  ? 1.40956 1.67613 1.93498 0.00847  0.28470  0.10858  48  LYS A C   
4826 O O   . LYS E 43  ? 1.38271 1.56580 1.90351 0.02014  0.32992  0.11038  48  LYS A O   
4827 C CB  . LYS E 43  ? 1.43538 1.80565 1.91508 0.01283  0.25156  0.13914  48  LYS A CB  
4828 C CG  . LYS E 43  ? 1.42486 1.89494 1.93922 0.01911  0.23516  0.19592  48  LYS A CG  
4829 C CD  . LYS E 43  ? 1.43508 2.01457 2.00673 0.00890  0.19427  0.21469  48  LYS A CD  
4830 C CE  . LYS E 43  ? 1.51337 2.14073 2.02581 -0.00942 0.14282  0.15203  48  LYS A CE  
4831 N NZ  . LYS E 43  ? 1.53712 2.18008 1.96213 -0.00491 0.13746  0.12841  48  LYS A NZ  
4832 N N   . GLY E 44  ? 1.56278 1.86373 2.06945 -0.01240 0.23834  0.06337  49  GLY A N   
4833 C CA  . GLY E 44  ? 1.57044 1.81506 2.06947 -0.02540 0.23589  0.02139  49  GLY A CA  
4834 C C   . GLY E 44  ? 1.56802 1.73203 1.98065 -0.02611 0.25290  -0.01825 49  GLY A C   
4835 O O   . GLY E 44  ? 1.55920 1.70492 1.91752 -0.01754 0.26661  -0.01349 49  GLY A O   
4836 N N   . LEU E 45  ? 1.61467 1.73309 2.02485 -0.03895 0.24845  -0.05154 50  LEU A N   
4837 C CA  . LEU E 45  ? 1.60566 1.65391 1.94212 -0.04289 0.25987  -0.08447 50  LEU A CA  
4838 C C   . LEU E 45  ? 1.64911 1.73259 1.94197 -0.04974 0.22025  -0.12833 50  LEU A C   
4839 O O   . LEU E 45  ? 1.70410 1.85243 2.02049 -0.05467 0.17945  -0.15030 50  LEU A O   
4840 C CB  . LEU E 45  ? 1.58814 1.57917 1.94287 -0.05319 0.27250  -0.09454 50  LEU A CB  
4841 C CG  . LEU E 45  ? 1.54357 1.47905 1.89870 -0.03962 0.32716  -0.05820 50  LEU A CG  
4842 C CD1 . LEU E 45  ? 1.53041 1.40632 1.86663 -0.05033 0.34106  -0.07033 50  LEU A CD1 
4843 C CD2 . LEU E 45  ? 1.53433 1.43022 1.82626 -0.02295 0.35682  -0.04591 50  LEU A CD2 
4844 N N   . GLU E 46  ? 1.62710 1.66652 1.85422 -0.04886 0.23251  -0.14133 51  GLU A N   
4845 C CA  . GLU E 46  ? 1.64306 1.71587 1.82588 -0.04843 0.20664  -0.17564 51  GLU A CA  
4846 C C   . GLU E 46  ? 1.60229 1.60138 1.74507 -0.05616 0.22008  -0.19125 51  GLU A C   
4847 O O   . GLU E 46  ? 1.57464 1.52486 1.68216 -0.05631 0.24516  -0.16535 51  GLU A O   
4848 C CB  . GLU E 46  ? 1.64412 1.77870 1.79865 -0.03554 0.20635  -0.14795 51  GLU A CB  
4849 C CG  . GLU E 46  ? 1.63310 1.79609 1.73445 -0.03001 0.19564  -0.16778 51  GLU A CG  
4850 C CD  . GLU E 46  ? 1.63825 1.89129 1.72450 -0.01637 0.19052  -0.13314 51  GLU A CD  
4851 O OE1 . GLU E 46  ? 1.62301 1.86483 1.72064 -0.01484 0.20959  -0.08118 51  GLU A OE1 
4852 O OE2 . GLU E 46  ? 1.65530 1.99128 1.71833 -0.00562 0.16747  -0.15718 51  GLU A OE2 
4853 N N   . TRP E 47  ? 1.69946 1.68801 1.85239 -0.06377 0.19988  -0.23229 52  TRP A N   
4854 C CA  . TRP E 47  ? 1.64454 1.57674 1.76691 -0.07153 0.20793  -0.24238 52  TRP A CA  
4855 C C   . TRP E 47  ? 1.64155 1.60689 1.71475 -0.06124 0.20646  -0.23947 52  TRP A C   
4856 O O   . TRP E 47  ? 1.65768 1.69277 1.72494 -0.04701 0.18716  -0.26348 52  TRP A O   
4857 C CB  . TRP E 47  ? 1.60904 1.52683 1.77061 -0.07973 0.18535  -0.28261 52  TRP A CB  
4858 C CG  . TRP E 47  ? 1.55620 1.43896 1.69298 -0.08372 0.18762  -0.29292 52  TRP A CG  
4859 C CD1 . TRP E 47  ? 1.51059 1.32821 1.63683 -0.09967 0.20463  -0.27030 52  TRP A CD1 
4860 C CD2 . TRP E 47  ? 1.55614 1.47371 1.67733 -0.06990 0.17281  -0.32475 52  TRP A CD2 
4861 N NE1 . TRP E 47  ? 1.49275 1.30338 1.60663 -0.10026 0.19791  -0.28088 52  TRP A NE1 
4862 C CE2 . TRP E 47  ? 1.52129 1.39256 1.63506 -0.07953 0.18170  -0.31398 52  TRP A CE2 
4863 C CE3 . TRP E 47  ? 1.58798 1.57608 1.69722 -0.04796 0.15431  -0.36027 52  TRP A CE3 
4864 C CZ2 . TRP E 47  ? 1.52715 1.42101 1.63453 -0.06607 0.17581  -0.33326 52  TRP A CZ2 
4865 C CZ3 . TRP E 47  ? 1.57951 1.58889 1.67071 -0.03094 0.15184  -0.38541 52  TRP A CZ3 
4866 C CH2 . TRP E 47  ? 1.55374 1.51646 1.65031 -0.03912 0.16404  -0.36986 52  TRP A CH2 
4867 N N   . VAL E 48  ? 1.58645 1.50535 1.62411 -0.06792 0.22560  -0.20806 53  VAL A N   
4868 C CA  . VAL E 48  ? 1.59309 1.54537 1.59812 -0.06141 0.22386  -0.19022 53  VAL A CA  
4869 C C   . VAL E 48  ? 1.57881 1.52086 1.57808 -0.06452 0.21595  -0.21119 53  VAL A C   
4870 O O   . VAL E 48  ? 1.58002 1.58797 1.57588 -0.04700 0.20678  -0.22729 53  VAL A O   
4871 C CB  . VAL E 48  ? 1.60643 1.51055 1.58668 -0.07028 0.23961  -0.14395 53  VAL A CB  
4872 C CG1 . VAL E 48  ? 1.61053 1.55998 1.57528 -0.06628 0.23289  -0.11441 53  VAL A CG1 
4873 C CG2 . VAL E 48  ? 1.61251 1.52336 1.61053 -0.06240 0.25114  -0.12261 53  VAL A CG2 
4874 N N   . ALA E 49  ? 1.60816 1.47311 1.60651 -0.08421 0.22111  -0.20876 54  ALA A N   
4875 C CA  . ALA E 49  ? 1.60177 1.45950 1.60381 -0.08828 0.21374  -0.21646 54  ALA A CA  
4876 C C   . ALA E 49  ? 1.55447 1.33682 1.56870 -0.11116 0.21514  -0.21697 54  ALA A C   
4877 O O   . ALA E 49  ? 1.52361 1.26171 1.53419 -0.12183 0.22543  -0.20981 54  ALA A O   
4878 C CB  . ALA E 49  ? 1.65152 1.52232 1.62612 -0.09090 0.21540  -0.17622 54  ALA A CB  
4879 N N   . TYR E 50  ? 1.64929 1.42435 1.68099 -0.11649 0.20700  -0.21978 55  TYR A N   
4880 C CA  . TYR E 50  ? 1.59359 1.30651 1.63733 -0.14098 0.20605  -0.20808 55  TYR A CA  
4881 C C   . TYR E 50  ? 1.60639 1.31256 1.65056 -0.15206 0.19821  -0.18384 55  TYR A C   
4882 O O   . TYR E 50  ? 1.67235 1.42919 1.72751 -0.13456 0.19512  -0.18480 55  TYR A O   
4883 C CB  . TYR E 50  ? 1.53707 1.24773 1.64511 -0.13925 0.19801  -0.23860 55  TYR A CB  
4884 C CG  . TYR E 50  ? 1.54882 1.29474 1.71152 -0.12077 0.18219  -0.27619 55  TYR A CG  
4885 C CD1 . TYR E 50  ? 1.56911 1.31154 1.75353 -0.12205 0.17821  -0.26614 55  TYR A CD1 
4886 C CD2 . TYR E 50  ? 1.54405 1.32235 1.74053 -0.10184 0.16933  -0.32312 55  TYR A CD2 
4887 C CE1 . TYR E 50  ? 1.58576 1.35427 1.82261 -0.09869 0.16825  -0.30504 55  TYR A CE1 
4888 C CE2 . TYR E 50  ? 1.55218 1.35129 1.79122 -0.08156 0.15378  -0.36815 55  TYR A CE2 
4889 C CZ  . TYR E 50  ? 1.57095 1.36326 1.83047 -0.07728 0.15630  -0.36064 55  TYR A CZ  
4890 O OH  . TYR E 50  ? 1.58412 1.39239 1.88808 -0.05044 0.14498  -0.41021 55  TYR A OH  
4891 N N   . ILE E 51  ? 1.64709 1.29679 1.68060 -0.18045 0.19569  -0.15795 56  ILE A N   
4892 C CA  . ILE E 51  ? 1.63884 1.27944 1.68565 -0.19765 0.18327  -0.12825 56  ILE A CA  
4893 C C   . ILE E 51  ? 1.57459 1.17991 1.65552 -0.21778 0.17847  -0.12039 56  ILE A C   
4894 O O   . ILE E 51  ? 1.53436 1.10333 1.58956 -0.23035 0.18676  -0.11710 56  ILE A O   
4895 C CB  . ILE E 51  ? 1.63349 1.24343 1.61725 -0.22087 0.17599  -0.08705 56  ILE A CB  
4896 C CG1 . ILE E 51  ? 1.61803 1.22366 1.62310 -0.24357 0.15735  -0.04816 56  ILE A CG1 
4897 C CG2 . ILE E 51  ? 1.59561 1.13793 1.51196 -0.23958 0.18269  -0.08367 56  ILE A CG2 
4898 C CD1 . ILE E 51  ? 1.62503 1.22473 1.59444 -0.26196 0.14108  -0.00576 56  ILE A CD1 
4899 N N   . TYR E 52  ? 1.64419 1.26649 1.78965 -0.21801 0.16745  -0.11250 57  TYR A N   
4900 C CA  . TYR E 52  ? 1.59148 1.19153 1.79137 -0.23692 0.15947  -0.09558 57  TYR A CA  
4901 C C   . TYR E 52  ? 1.58863 1.18352 1.79320 -0.26088 0.14476  -0.04600 57  TYR A C   
4902 O O   . TYR E 52  ? 1.61523 1.23909 1.89451 -0.24942 0.13832  -0.04067 57  TYR A O   
4903 C CB  . TYR E 52  ? 1.59886 1.22278 1.89705 -0.21286 0.15549  -0.13371 57  TYR A CB  
4904 C CG  . TYR E 52  ? 1.57197 1.19423 1.88364 -0.20220 0.15977  -0.17056 57  TYR A CG  
4905 C CD1 . TYR E 52  ? 1.59447 1.22880 1.84439 -0.18879 0.17102  -0.19229 57  TYR A CD1 
4906 C CD2 . TYR E 52  ? 1.52694 1.14049 1.92698 -0.20612 0.14923  -0.17802 57  TYR A CD2 
4907 C CE1 . TYR E 52  ? 1.57272 1.21228 1.84354 -0.18070 0.17234  -0.21841 57  TYR A CE1 
4908 C CE2 . TYR E 52  ? 1.50466 1.12138 1.92872 -0.19963 0.14810  -0.20436 57  TYR A CE2 
4909 C CZ  . TYR E 52  ? 1.52911 1.16038 1.88661 -0.18693 0.15990  -0.22430 57  TYR A CZ  
4910 O OH  . TYR E 52  ? 1.51590 1.15651 1.90567 -0.18226 0.15638  -0.24303 57  TYR A OH  
4911 N N   . PRO E 53  ? 1.66573 1.22245 1.79262 -0.29407 0.13750  -0.00900 58  PRO A N   
4912 C CA  . PRO E 53  ? 1.66568 1.22038 1.78616 -0.32106 0.11567  0.04133  58  PRO A CA  
4913 C C   . PRO E 53  ? 1.65542 1.23383 1.87331 -0.32785 0.10343  0.07252  58  PRO A C   
4914 O O   . PRO E 53  ? 1.68369 1.29937 1.95669 -0.31666 0.09797  0.08989  58  PRO A O   
4915 C CB  . PRO E 53  ? 1.64600 1.14306 1.66564 -0.35773 0.10645  0.06371  58  PRO A CB  
4916 C CG  . PRO E 53  ? 1.65911 1.13361 1.61746 -0.33911 0.12923  0.02239  58  PRO A CG  
4917 C CD  . PRO E 53  ? 1.65534 1.16892 1.69080 -0.30433 0.14838  -0.01630 58  PRO A CD  
4918 N N   . SER E 54  ? 1.57973 1.14306 1.82919 -0.34329 0.10130  0.08506  59  SER A N   
4919 C CA  . SER E 54  ? 1.56230 1.14600 1.91403 -0.35369 0.08692  0.12501  59  SER A CA  
4920 C C   . SER E 54  ? 1.58068 1.19551 2.04881 -0.31329 0.09615  0.08934  59  SER A C   
4921 O O   . SER E 54  ? 1.56553 1.19400 2.13710 -0.31547 0.08641  0.11810  59  SER A O   
4922 C CB  . SER E 54  ? 1.52679 1.09351 1.88470 -0.38280 0.08116  0.15801  59  SER A CB  
4923 O OG  . SER E 54  ? 1.51317 1.07333 1.88434 -0.36471 0.09978  0.11919  59  SER A OG  
4924 N N   . TYR E 55  ? 1.47850 1.10395 1.93195 -0.27625 0.11279  0.02763  62  TYR A N   
4925 C CA  . TYR E 55  ? 1.53139 1.18002 2.07528 -0.23430 0.11963  -0.02132 62  TYR A CA  
4926 C C   . TYR E 55  ? 1.63282 1.32390 2.16442 -0.19915 0.13154  -0.04058 62  TYR A C   
4927 O O   . TYR E 55  ? 1.71276 1.42790 2.32067 -0.16208 0.13803  -0.07060 62  TYR A O   
4928 C CB  . TYR E 55  ? 1.51858 1.15398 2.05862 -0.21783 0.12546  -0.08092 62  TYR A CB  
4929 C CG  . TYR E 55  ? 1.43606 1.04415 2.02573 -0.24216 0.11641  -0.06364 62  TYR A CG  
4930 C CD1 . TYR E 55  ? 1.38509 0.97619 1.92776 -0.28140 0.11449  -0.00594 62  TYR A CD1 
4931 C CD2 . TYR E 55  ? 1.42046 1.02247 2.10050 -0.22575 0.10838  -0.10418 62  TYR A CD2 
4932 C CE1 . TYR E 55  ? 1.33370 0.91473 1.92195 -0.30071 0.11083  0.01914  62  TYR A CE1 
4933 C CE2 . TYR E 55  ? 1.35076 0.93721 2.08950 -0.24937 0.09936  -0.07648 62  TYR A CE2 
4934 C CZ  . TYR E 55  ? 1.31293 0.89500 2.00642 -0.28516 0.10379  -0.01132 62  TYR A CZ  
4935 O OH  . TYR E 55  ? 1.26459 0.84549 2.01841 -0.30549 0.09910  0.02475  62  TYR A OH  
4936 N N   . GLY E 56  ? 1.47652 1.17817 1.91822 -0.20845 0.13480  -0.02143 63  GLY A N   
4937 C CA  . GLY E 56  ? 1.56519 1.31971 1.99331 -0.17556 0.14805  -0.02961 63  GLY A CA  
4938 C C   . GLY E 56  ? 1.64480 1.42423 2.04933 -0.13384 0.16419  -0.10017 63  GLY A C   
4939 O O   . GLY E 56  ? 1.74713 1.57789 2.17882 -0.09051 0.17856  -0.12664 63  GLY A O   
4940 N N   . TYR E 57  ? 1.59995 1.34917 1.95352 -0.14424 0.16269  -0.12936 64  TYR A N   
4941 C CA  . TYR E 57  ? 1.64095 1.41387 1.97334 -0.11141 0.17108  -0.19224 64  TYR A CA  
4942 C C   . TYR E 57  ? 1.64685 1.43191 1.89130 -0.11758 0.17760  -0.18054 64  TYR A C   
4943 O O   . TYR E 57  ? 1.57455 1.31463 1.77500 -0.14964 0.17385  -0.15607 64  TYR A O   
4944 C CB  . TYR E 57  ? 1.56087 1.29530 1.93172 -0.11703 0.16097  -0.23123 64  TYR A CB  
4945 C CG  . TYR E 57  ? 1.54035 1.25749 2.01463 -0.11012 0.15013  -0.24623 64  TYR A CG  
4946 C CD1 . TYR E 57  ? 1.61513 1.35794 2.14098 -0.08424 0.15544  -0.24604 64  TYR A CD1 
4947 C CD2 . TYR E 57  ? 1.44756 1.12542 1.97892 -0.12743 0.13536  -0.25627 64  TYR A CD2 
4948 C CE1 . TYR E 57  ? 1.59829 1.31923 2.22949 -0.07518 0.14565  -0.26029 64  TYR A CE1 
4949 C CE2 . TYR E 57  ? 1.42939 1.08801 2.06988 -0.12247 0.12161  -0.26621 64  TYR A CE2 
4950 C CZ  . TYR E 57  ? 1.50411 1.17997 2.19425 -0.09587 0.12644  -0.27092 64  TYR A CZ  
4951 O OH  . TYR E 57  ? 1.48702 1.13778 2.29699 -0.08829 0.11288  -0.28092 64  TYR A OH  
4952 N N   . THR E 58  ? 1.55889 1.40675 1.77925 -0.08443 0.18867  -0.19642 65  THR A N   
4953 C CA  . THR E 58  ? 1.57437 1.44456 1.72738 -0.08522 0.19406  -0.18419 65  THR A CA  
4954 C C   . THR E 58  ? 1.54295 1.47781 1.68569 -0.04332 0.20174  -0.23606 65  THR A C   
4955 O O   . THR E 58  ? 1.55561 1.56180 1.69662 -0.01082 0.21313  -0.23517 65  THR A O   
4956 C CB  . THR E 58  ? 1.58908 1.48320 1.72160 -0.09665 0.19486  -0.12066 65  THR A CB  
4957 O OG1 . THR E 58  ? 1.61230 1.56218 1.79181 -0.07194 0.20239  -0.10694 65  THR A OG1 
4958 C CG2 . THR E 58  ? 1.49685 1.31646 1.61038 -0.14512 0.17935  -0.07539 65  THR A CG2 
4959 N N   . TYR E 59  ? 1.62800 1.54430 1.76310 -0.04384 0.19498  -0.27731 66  TYR A N   
4960 C CA  . TYR E 59  ? 1.60383 1.57920 1.71886 -0.01156 0.19434  -0.32475 66  TYR A CA  
4961 C C   . TYR E 59  ? 1.59669 1.58111 1.66729 -0.02354 0.19566  -0.30344 66  TYR A C   
4962 O O   . TYR E 59  ? 1.58256 1.50694 1.65083 -0.05300 0.19451  -0.28226 66  TYR A O   
4963 C CB  . TYR E 59  ? 1.56183 1.51448 1.71917 -0.00159 0.17716  -0.39206 66  TYR A CB  
4964 C CG  . TYR E 59  ? 1.56073 1.57407 1.68936 0.03015  0.16880  -0.44700 66  TYR A CG  
4965 C CD1 . TYR E 59  ? 1.58819 1.68391 1.67558 0.06816  0.18248  -0.45513 66  TYR A CD1 
4966 C CD2 . TYR E 59  ? 1.53807 1.53362 1.68111 0.02175  0.14572  -0.48611 66  TYR A CD2 
4967 C CE1 . TYR E 59  ? 1.59353 1.75146 1.64160 0.09748  0.17304  -0.50596 66  TYR A CE1 
4968 C CE2 . TYR E 59  ? 1.55802 1.61081 1.66942 0.04690  0.13084  -0.53627 66  TYR A CE2 
4969 C CZ  . TYR E 59  ? 1.58560 1.71887 1.64305 0.08494  0.14439  -0.54862 66  TYR A CZ  
4970 O OH  . TYR E 59  ? 1.61022 1.80718 1.62327 0.11044  0.12820  -0.59896 66  TYR A OH  
4971 N N   . TYR E 60  ? 1.57860 1.64278 1.61550 0.00228  0.20037  -0.30602 67  TYR A N   
4972 C CA  . TYR E 60  ? 1.57981 1.66689 1.58522 -0.00458 0.20225  -0.27719 67  TYR A CA  
4973 C C   . TYR E 60  ? 1.56964 1.71097 1.56493 0.01561  0.19043  -0.32255 67  TYR A C   
4974 O O   . TYR E 60  ? 1.56776 1.74449 1.56340 0.04126  0.18128  -0.37750 67  TYR A O   
4975 C CB  . TYR E 60  ? 1.59879 1.74476 1.58137 0.00242  0.21417  -0.21862 67  TYR A CB  
4976 C CG  . TYR E 60  ? 1.62579 1.72354 1.61933 -0.02178 0.21739  -0.16753 67  TYR A CG  
4977 C CD1 . TYR E 60  ? 1.64188 1.73556 1.66196 -0.01687 0.21935  -0.17059 67  TYR A CD1 
4978 C CD2 . TYR E 60  ? 1.63694 1.69139 1.61736 -0.04974 0.21525  -0.11624 67  TYR A CD2 
4979 C CE1 . TYR E 60  ? 1.66760 1.72243 1.70079 -0.04349 0.21594  -0.11800 67  TYR A CE1 
4980 C CE2 . TYR E 60  ? 1.65049 1.65722 1.63595 -0.07609 0.20936  -0.07266 67  TYR A CE2 
4981 C CZ  . TYR E 60  ? 1.66229 1.67296 1.67403 -0.07510 0.20809  -0.07048 67  TYR A CZ  
4982 O OH  . TYR E 60  ? 1.64839 1.61586 1.66808 -0.10595 0.19609  -0.02103 67  TYR A OH  
4983 N N   . ALA E 61  ? 1.56124 1.70689 1.54808 0.00420  0.18876  -0.29957 68  ALA A N   
4984 C CA  . ALA E 61  ? 1.57414 1.78141 1.55266 0.01833  0.17333  -0.32806 68  ALA A CA  
4985 C C   . ALA E 61  ? 1.58150 1.90087 1.51880 0.04935  0.17678  -0.32026 68  ALA A C   
4986 O O   . ALA E 61  ? 1.57025 1.92269 1.49456 0.05704  0.19454  -0.27530 68  ALA A O   
4987 C CB  . ALA E 61  ? 1.58632 1.77370 1.57863 -0.00062 0.17438  -0.29319 68  ALA A CB  
4988 N N   . ASP E 62  ? 1.63355 2.01734 1.55161 0.06616  0.15710  -0.36073 69  ASP A N   
4989 C CA  . ASP E 62  ? 1.63521 2.13828 1.50300 0.09990  0.15987  -0.35971 69  ASP A CA  
4990 C C   . ASP E 62  ? 1.62079 2.19093 1.48308 0.09644  0.17249  -0.27679 69  ASP A C   
4991 O O   . ASP E 62  ? 1.59346 2.25251 1.43012 0.11933  0.18803  -0.24053 69  ASP A O   
4992 C CB  . ASP E 62  ? 1.67806 2.22749 1.51799 0.11512  0.12840  -0.42926 69  ASP A CB  
4993 C CG  . ASP E 62  ? 1.68104 2.21008 1.50567 0.13986  0.11980  -0.51362 69  ASP A CG  
4994 O OD1 . ASP E 62  ? 1.65006 2.15431 1.48368 0.15203  0.14469  -0.50826 69  ASP A OD1 
4995 O OD2 . ASP E 62  ? 1.72076 2.25685 1.52911 0.14692  0.08577  -0.58424 69  ASP A OD2 
4996 N N   . SER E 63  ? 1.62549 2.15960 1.51934 0.07060  0.16703  -0.24190 70  SER A N   
4997 C CA  . SER E 63  ? 1.60640 2.19665 1.50937 0.06762  0.17649  -0.16223 70  SER A CA  
4998 C C   . SER E 63  ? 1.56830 2.12981 1.48497 0.06017  0.19807  -0.10259 70  SER A C   
4999 O O   . SER E 63  ? 1.53489 2.17422 1.45554 0.06796  0.20502  -0.03766 70  SER A O   
5000 C CB  . SER E 63  ? 1.63357 2.17827 1.57722 0.04527  0.17003  -0.14008 70  SER A CB  
5001 O OG  . SER E 63  ? 1.62595 2.05583 1.59818 0.02296  0.18665  -0.11833 70  SER A OG  
5002 N N   . VAL E 64  ? 1.62352 2.07717 1.55266 0.04244  0.20465  -0.11855 71  VAL A N   
5003 C CA  . VAL E 64  ? 1.61529 2.02155 1.55963 0.02617  0.21601  -0.06412 71  VAL A CA  
5004 C C   . VAL E 64  ? 1.60189 2.03521 1.53805 0.03922  0.22353  -0.06578 71  VAL A C   
5005 O O   . VAL E 64  ? 1.60339 2.00013 1.55723 0.02234  0.22711  -0.01833 71  VAL A O   
5006 C CB  . VAL E 64  ? 1.64643 1.91593 1.60510 -0.00493 0.21703  -0.07163 71  VAL A CB  
5007 C CG1 . VAL E 64  ? 1.65738 1.90477 1.63227 -0.01221 0.21721  -0.05886 71  VAL A CG1 
5008 C CG2 . VAL E 64  ? 1.65043 1.86366 1.60611 -0.00779 0.21330  -0.13664 71  VAL A CG2 
5009 N N   . LYS E 65  ? 1.65096 2.14378 1.56384 0.06917  0.22451  -0.11939 72  LYS A N   
5010 C CA  . LYS E 65  ? 1.64377 2.15666 1.55724 0.08717  0.23675  -0.12547 72  LYS A CA  
5011 C C   . LYS E 65  ? 1.60640 2.20709 1.53074 0.09705  0.25041  -0.04319 72  LYS A C   
5012 O O   . LYS E 65  ? 1.57330 2.27981 1.48464 0.11506  0.25393  -0.00755 72  LYS A O   
5013 C CB  . LYS E 65  ? 1.64650 2.21307 1.52873 0.12595  0.23690  -0.20335 72  LYS A CB  
5014 N N   . GLY E 66  ? 1.69988 2.26219 1.65517 0.08283  0.25525  -0.00540 74  GLY A N   
5015 C CA  . GLY E 66  ? 1.65532 2.29341 1.63968 0.08468  0.26295  0.08521  74  GLY A CA  
5016 C C   . GLY E 66  ? 1.64486 2.24045 1.65875 0.04642  0.24679  0.15647  74  GLY A C   
5017 O O   . GLY E 66  ? 1.63051 2.19992 1.68320 0.02231  0.23861  0.21896  74  GLY A O   
5018 N N   . ARG E 67  ? 1.58522 2.17174 1.58718 0.04030  0.23937  0.14950  75  ARG A N   
5019 C CA  . ARG E 67  ? 1.58157 2.11442 1.61621 0.00795  0.22499  0.20973  75  ARG A CA  
5020 C C   . ARG E 67  ? 1.63297 2.00734 1.66802 -0.03140 0.21182  0.19088  75  ARG A C   
5021 O O   . ARG E 67  ? 1.62276 1.94278 1.68613 -0.06040 0.19636  0.24513  75  ARG A O   
5022 C CB  . ARG E 67  ? 1.57801 2.14152 1.60753 0.01523  0.22344  0.20660  75  ARG A CB  
5023 C CG  . ARG E 67  ? 1.53026 2.25777 1.54590 0.05320  0.23284  0.22219  75  ARG A CG  
5024 C CD  . ARG E 67  ? 1.52166 2.29076 1.54700 0.05458  0.22595  0.24243  75  ARG A CD  
5025 N NE  . ARG E 67  ? 1.57407 2.25040 1.58318 0.04352  0.21985  0.17601  75  ARG A NE  
5026 C CZ  . ARG E 67  ? 1.60315 2.17057 1.64098 0.01810  0.21565  0.18544  75  ARG A CZ  
5027 N NH1 . ARG E 67  ? 1.59365 2.11434 1.67377 -0.00149 0.21188  0.24929  75  ARG A NH1 
5028 N NH2 . ARG E 67  ? 1.64516 2.14864 1.67176 0.01368  0.21476  0.12969  75  ARG A NH2 
5029 N N   . PHE E 68  ? 1.39716 1.73721 2.23661 0.13856  0.52528  0.10821  76  PHE A N   
5030 C CA  . PHE E 68  ? 1.49773 1.71965 2.29053 0.09135  0.48989  0.07197  76  PHE A CA  
5031 C C   . PHE E 68  ? 1.47311 1.77602 2.29045 0.09541  0.43435  0.04420  76  PHE A C   
5032 O O   . PHE E 68  ? 1.35504 1.78103 2.20826 0.15056  0.42214  0.04489  76  PHE A O   
5033 C CB  . PHE E 68  ? 1.46734 1.54648 2.17309 0.12085  0.49016  0.04857  76  PHE A CB  
5034 C CG  . PHE E 68  ? 1.49089 1.47015 2.16701 0.10861  0.54530  0.07820  76  PHE A CG  
5035 C CD1 . PHE E 68  ? 1.52951 1.56373 2.26039 0.08719  0.59320  0.12325  76  PHE A CD1 
5036 C CD2 . PHE E 68  ? 1.43433 1.26764 2.03339 0.11885  0.55043  0.06668  76  PHE A CD2 
5037 C CE1 . PHE E 68  ? 1.53889 1.48505 2.24945 0.07604  0.64600  0.15422  76  PHE A CE1 
5038 C CE2 . PHE E 68  ? 1.40968 1.15195 1.98390 0.10856  0.60381  0.09873  76  PHE A CE2 
5039 C CZ  . PHE E 68  ? 1.45913 1.25727 2.08972 0.08622  0.65215  0.14154  76  PHE A CZ  
5040 N N   . THR E 69  ? 1.31353 1.54603 2.10949 0.03738  0.40164  0.02003  77  THR A N   
5041 C CA  . THR E 69  ? 1.29593 1.59761 2.11369 0.03486  0.34789  -0.00421 77  THR A CA  
5042 C C   . THR E 69  ? 1.40136 1.57881 2.15338 0.00172  0.31450  -0.04188 77  THR A C   
5043 O O   . THR E 69  ? 1.53157 1.60982 2.25284 -0.06350 0.32182  -0.04475 77  THR A O   
5044 C CB  . THR E 69  ? 1.31029 1.73072 2.21017 -0.01630 0.33839  0.02315  77  THR A CB  
5045 O OG1 . THR E 69  ? 1.18920 1.75456 2.15351 0.03358  0.36139  0.05734  77  THR A OG1 
5046 C CG2 . THR E 69  ? 1.31670 1.78081 2.23029 -0.03830 0.28207  -0.00051 77  THR A CG2 
5047 N N   . ILE E 70  ? 1.37023 1.55625 2.10335 0.04778  0.27747  -0.06987 78  ILE A N   
5048 C CA  . ILE E 70  ? 1.45153 1.54511 2.13027 0.02588  0.24177  -0.10191 78  ILE A CA  
5049 C C   . ILE E 70  ? 1.48730 1.67451 2.21266 -0.01363 0.19586  -0.11051 78  ILE A C   
5050 O O   . ILE E 70  ? 1.38213 1.71078 2.18103 0.00150  0.18642  -0.09449 78  ILE A O   
5051 C CB  . ILE E 70  ? 1.28068 1.32960 1.92071 0.09953  0.22709  -0.11979 78  ILE A CB  
5052 C CG1 . ILE E 70  ? 1.33791 1.24758 1.90161 0.08008  0.21324  -0.14004 78  ILE A CG1 
5053 C CG2 . ILE E 70  ? 1.13624 1.30838 1.83127 0.14621  0.18587  -0.13099 78  ILE A CG2 
5054 C CD1 . ILE E 70  ? 1.13076 0.99421 1.66441 0.14980  0.19790  -0.14803 78  ILE A CD1 
5055 N N   . SER E 71  ? 1.28776 1.39844 1.96874 -0.06401 0.16821  -0.13332 79  SER A N   
5056 C CA  . SER E 71  ? 1.29770 1.49035 2.01753 -0.11192 0.12303  -0.13949 79  SER A CA  
5057 C C   . SER E 71  ? 1.38599 1.47876 2.03423 -0.13672 0.09167  -0.17226 79  SER A C   
5058 O O   . SER E 71  ? 1.43755 1.39381 2.00769 -0.12496 0.11050  -0.18587 79  SER A O   
5059 C CB  . SER E 71  ? 1.33203 1.56627 2.09642 -0.18821 0.13065  -0.11609 79  SER A CB  
5060 O OG  . SER E 71  ? 1.42243 1.52091 2.13206 -0.23260 0.16189  -0.11875 79  SER A OG  
5061 N N   . ALA E 72  ? 1.32158 1.48663 1.99672 -0.17273 0.04527  -0.18078 80  ALA A N   
5062 C CA  . ALA E 72  ? 1.39577 1.48372 2.00456 -0.19558 0.01273  -0.21060 80  ALA A CA  
5063 C C   . ALA E 72  ? 1.40606 1.57076 2.04608 -0.26864 -0.03110 -0.21315 80  ALA A C   
5064 O O   . ALA E 72  ? 1.31212 1.62332 2.04012 -0.27073 -0.04895 -0.19048 80  ALA A O   
5065 C CB  . ALA E 72  ? 1.34022 1.44349 1.94585 -0.11987 -0.00708 -0.21951 80  ALA A CB  
5066 N N   . ASP E 73  ? 1.45398 1.51815 2.01935 -0.32804 -0.04760 -0.23928 81  ASP A N   
5067 C CA  . ASP E 73  ? 1.47666 1.59714 2.05449 -0.40122 -0.09603 -0.24704 81  ASP A CA  
5068 C C   . ASP E 73  ? 1.50240 1.58492 2.01701 -0.38500 -0.12872 -0.27571 81  ASP A C   
5069 O O   . ASP E 73  ? 1.56631 1.50436 1.98162 -0.37822 -0.11487 -0.30176 81  ASP A O   
5070 C CB  . ASP E 73  ? 1.55507 1.59661 2.10208 -0.49125 -0.09274 -0.25419 81  ASP A CB  
5071 C CG  . ASP E 73  ? 1.59709 1.65754 2.12579 -0.57032 -0.14813 -0.27279 81  ASP A CG  
5072 O OD1 . ASP E 73  ? 1.54129 1.74627 2.13840 -0.57426 -0.18635 -0.25595 81  ASP A OD1 
5073 O OD2 . ASP E 73  ? 1.72007 1.65315 2.16847 -0.63019 -0.15332 -0.30285 81  ASP A OD2 
5074 N N   . THR E 74  ? 1.50948 1.72877 2.08801 -0.36979 -0.16777 -0.26515 82  THR A N   
5075 C CA  . THR E 74  ? 1.51141 1.72904 2.05443 -0.34237 -0.19935 -0.28209 82  THR A CA  
5076 C C   . THR E 74  ? 1.61202 1.74183 2.06070 -0.41029 -0.22549 -0.31453 82  THR A C   
5077 O O   . THR E 74  ? 1.64941 1.69436 2.01790 -0.38269 -0.22900 -0.33597 82  THR A O   
5078 C CB  . THR E 74  ? 1.38310 1.78051 2.03003 -0.32301 -0.23561 -0.25849 82  THR A CB  
5079 O OG1 . THR E 74  ? 1.39012 1.86074 2.05553 -0.40570 -0.27622 -0.25644 82  THR A OG1 
5080 C CG2 . THR E 74  ? 1.25470 1.75402 2.00032 -0.27938 -0.21225 -0.22703 82  THR A CG2 
5081 N N   . SER E 75  ? 1.53242 1.68573 1.99082 -0.49804 -0.24661 -0.31667 83  SER A N   
5082 C CA  . SER E 75  ? 1.64305 1.72403 2.01354 -0.56830 -0.28036 -0.35134 83  SER A CA  
5083 C C   . SER E 75  ? 1.74633 1.62589 1.98997 -0.56585 -0.24739 -0.38705 83  SER A C   
5084 O O   . SER E 75  ? 1.81811 1.61827 1.96460 -0.56835 -0.26374 -0.41915 83  SER A O   
5085 C CB  . SER E 75  ? 1.71113 1.85143 2.12598 -0.66511 -0.31000 -0.34239 83  SER A CB  
5086 O OG  . SER E 75  ? 1.81699 1.82384 2.18172 -0.71270 -0.28416 -0.35791 83  SER A OG  
5087 N N   . LYS E 76  ? 1.85655 1.65507 2.09960 -0.55728 -0.19850 -0.37906 84  LYS A N   
5088 C CA  . LYS E 76  ? 1.90323 1.51135 2.03412 -0.55167 -0.16026 -0.40638 84  LYS A CA  
5089 C C   . LYS E 76  ? 1.86147 1.41875 1.96186 -0.45479 -0.12529 -0.39777 84  LYS A C   
5090 O O   . LYS E 76  ? 1.86401 1.26743 1.87642 -0.43665 -0.08651 -0.41104 84  LYS A O   
5091 C CB  . LYS E 76  ? 1.92130 1.46477 2.07072 -0.59281 -0.12269 -0.39698 84  LYS A CB  
5092 N N   . ASN E 77  ? 1.92278 1.60544 2.09778 -0.39291 -0.13922 -0.37313 85  ASN A N   
5093 C CA  . ASN E 77  ? 1.86475 1.51322 2.02546 -0.30107 -0.11577 -0.36017 85  ASN A CA  
5094 C C   . ASN E 77  ? 1.81750 1.36289 1.95969 -0.27328 -0.05663 -0.34751 85  ASN A C   
5095 O O   . ASN E 77  ? 1.75108 1.17695 1.82089 -0.22885 -0.02657 -0.34793 85  ASN A O   
5096 C CB  . ASN E 77  ? 1.85655 1.42267 1.91851 -0.28153 -0.13025 -0.38139 85  ASN A CB  
5097 C CG  . ASN E 77  ? 1.78023 1.40083 1.87607 -0.19340 -0.13904 -0.35806 85  ASN A CG  
5098 O OD1 . ASN E 77  ? 1.76621 1.53423 1.95845 -0.17319 -0.17060 -0.34059 85  ASN A OD1 
5099 N ND2 . ASN E 77  ? 1.70570 1.20722 1.72466 -0.14138 -0.11274 -0.35497 85  ASN A ND2 
5100 N N   . THR E 78  ? 1.77280 1.36904 1.98295 -0.30005 -0.03842 -0.33107 86  THR A N   
5101 C CA  . THR E 78  ? 1.73945 1.23259 1.92610 -0.29263 0.01836  -0.32013 86  THR A CA  
5102 C C   . THR E 78  ? 1.71219 1.31331 1.99982 -0.26381 0.03864  -0.28660 86  THR A C   
5103 O O   . THR E 78  ? 1.74323 1.47197 2.11225 -0.29504 0.01652  -0.27533 86  THR A O   
5104 C CB  . THR E 78  ? 1.80060 1.19145 1.93489 -0.37627 0.02915  -0.34060 86  THR A CB  
5105 O OG1 . THR E 78  ? 1.83996 1.13320 1.87150 -0.39989 0.00681  -0.37741 86  THR A OG1 
5106 C CG2 . THR E 78  ? 1.76545 1.04180 1.87533 -0.36747 0.09208  -0.32623 86  THR A CG2 
5107 N N   . ALA E 79  ? 1.66749 1.21879 1.94741 -0.20340 0.08098  -0.26828 87  ALA A N   
5108 C CA  . ALA E 79  ? 1.64198 1.27602 1.99960 -0.17172 0.10758  -0.23865 87  ALA A CA  
5109 C C   . ALA E 79  ? 1.64644 1.20329 1.99116 -0.20799 0.15777  -0.22537 87  ALA A C   
5110 O O   . ALA E 79  ? 1.63241 1.04502 1.89829 -0.23326 0.18199  -0.23705 87  ALA A O   
5111 C CB  . ALA E 79  ? 1.51698 1.15472 1.87961 -0.08133 0.11779  -0.22524 87  ALA A CB  
5112 N N   . TYR E 80  ? 1.55475 1.21233 1.98082 -0.20778 0.17509  -0.19813 88  TYR A N   
5113 C CA  . TYR E 80  ? 1.55274 1.16394 1.98889 -0.23829 0.22363  -0.17629 88  TYR A CA  
5114 C C   . TYR E 80  ? 1.50454 1.19251 1.99677 -0.17845 0.25884  -0.14233 88  TYR A C   
5115 O O   . TYR E 80  ? 1.48971 1.31480 2.04708 -0.14144 0.23955  -0.13281 88  TYR A O   
5116 C CB  . TYR E 80  ? 1.61023 1.27169 2.09688 -0.32177 0.20837  -0.17124 88  TYR A CB  
5117 C CG  . TYR E 80  ? 1.66854 1.29322 2.11309 -0.38283 0.15972  -0.20614 88  TYR A CG  
5118 C CD1 . TYR E 80  ? 1.69902 1.16568 2.05837 -0.43181 0.16787  -0.23281 88  TYR A CD1 
5119 C CD2 . TYR E 80  ? 1.68241 1.43097 2.17145 -0.39188 0.10664  -0.21175 88  TYR A CD2 
5120 C CE1 . TYR E 80  ? 1.75894 1.18998 2.07076 -0.48722 0.12171  -0.26839 88  TYR A CE1 
5121 C CE2 . TYR E 80  ? 1.73209 1.45337 2.18121 -0.44989 0.06076  -0.24193 88  TYR A CE2 
5122 C CZ  . TYR E 80  ? 1.77494 1.33669 2.13197 -0.49765 0.06697  -0.27227 88  TYR A CZ  
5123 O OH  . TYR E 80  ? 1.82437 1.35689 2.13232 -0.55503 0.01908  -0.30641 88  TYR A OH  
5124 N N   . LEU E 81  ? 1.71520 1.31475 2.18042 -0.16886 0.31157  -0.12367 89  LEU A N   
5125 C CA  . LEU E 81  ? 1.67686 1.34246 2.18899 -0.11856 0.35017  -0.08899 89  LEU A CA  
5126 C C   . LEU E 81  ? 1.69037 1.36915 2.25082 -0.16939 0.38915  -0.05780 89  LEU A C   
5127 O O   . LEU E 81  ? 1.66399 1.22409 2.18699 -0.19432 0.42948  -0.04874 89  LEU A O   
5128 C CB  . LEU E 81  ? 1.54444 1.11229 1.99562 -0.05897 0.37964  -0.08317 89  LEU A CB  
5129 C CG  . LEU E 81  ? 1.46362 1.09791 1.95448 -0.00482 0.41661  -0.04912 89  LEU A CG  
5130 C CD1 . LEU E 81  ? 1.47241 1.28223 2.04369 0.02259  0.39348  -0.04412 89  LEU A CD1 
5131 C CD2 . LEU E 81  ? 1.24792 0.80978 1.68528 0.06099  0.42566  -0.04595 89  LEU A CD2 
5132 N N   . GLN E 82  ? 1.58779 1.41296 2.23654 -0.18434 0.37716  -0.03753 90  GLN A N   
5133 C CA  . GLN E 82  ? 1.56937 1.43800 2.28649 -0.22886 0.40938  0.00161  90  GLN A CA  
5134 C C   . GLN E 82  ? 1.49911 1.43401 2.25098 -0.16659 0.45740  0.04006  90  GLN A C   
5135 O O   . GLN E 82  ? 1.43821 1.51078 2.23770 -0.11510 0.44894  0.05225  90  GLN A O   
5136 C CB  . GLN E 82  ? 1.57033 1.57310 2.36855 -0.27131 0.37061  0.01230  90  GLN A CB  
5137 C CG  . GLN E 82  ? 1.53432 1.61697 2.42669 -0.31583 0.39409  0.06218  90  GLN A CG  
5138 C CD  . GLN E 82  ? 1.55894 1.50881 2.43517 -0.37577 0.42785  0.07075  90  GLN A CD  
5139 O OE1 . GLN E 82  ? 1.51471 1.44564 2.40588 -0.35466 0.48207  0.10280  90  GLN A OE1 
5140 N NE2 . GLN E 82  ? 1.62021 1.47671 2.46535 -0.45084 0.39553  0.04160  90  GLN A NE2 
5141 N N   . MET E 83  ? 1.73266 1.56937 2.45832 -0.16984 0.50878  0.05944  91  MET A N   
5142 C CA  . MET E 83  ? 1.66334 1.55701 2.42208 -0.12113 0.55931  0.10158  91  MET A CA  
5143 C C   . MET E 83  ? 1.62694 1.59640 2.47809 -0.16672 0.58984  0.14989  91  MET A C   
5144 O O   . MET E 83  ? 1.65034 1.53252 2.50673 -0.23640 0.59963  0.15394  91  MET A O   
5145 C CB  . MET E 83  ? 1.63475 1.38043 2.31745 -0.10069 0.59851  0.10247  91  MET A CB  
5146 C CG  . MET E 83  ? 1.64024 1.28257 2.23199 -0.07619 0.56378  0.05738  91  MET A CG  
5147 S SD  . MET E 83  ? 1.53603 0.97272 2.03092 -0.07543 0.60397  0.05861  91  MET A SD  
5148 C CE  . MET E 83  ? 1.57586 0.92472 2.08788 -0.16498 0.63936  0.07170  91  MET A CE  
5149 N N   . ASN E 84  ? 1.87709 1.51031 2.01464 -0.20872 0.05782  -0.20100 92  ASN A N   
5150 C CA  . ASN E 84  ? 1.93645 1.59480 2.11644 -0.22214 0.05034  -0.16788 92  ASN A CA  
5151 C C   . ASN E 84  ? 2.00601 1.72064 2.21005 -0.19966 0.08160  -0.15276 92  ASN A C   
5152 O O   . ASN E 84  ? 2.05042 1.75841 2.27400 -0.21309 0.07864  -0.12383 92  ASN A O   
5153 C CB  . ASN E 84  ? 1.93670 1.65002 2.18462 -0.23086 0.03121  -0.14700 92  ASN A CB  
5154 C CG  . ASN E 84  ? 1.88677 1.55220 2.11642 -0.25390 -0.00259 -0.15451 92  ASN A CG  
5155 O OD1 . ASN E 84  ? 1.89690 1.51531 2.11905 -0.28829 -0.03803 -0.13771 92  ASN A OD1 
5156 N ND2 . ASN E 84  ? 1.83882 1.51279 2.05929 -0.23654 0.00565  -0.17894 92  ASN A ND2 
5157 N N   . SER E 85  ? 1.82095 1.59009 2.02517 -0.16773 0.10860  -0.16875 93  SER A N   
5158 C CA  . SER E 85  ? 1.90870 1.73271 2.12749 -0.14434 0.13670  -0.15229 93  SER A CA  
5159 C C   . SER E 85  ? 1.89760 1.71229 2.07137 -0.12683 0.15534  -0.17319 93  SER A C   
5160 O O   . SER E 85  ? 1.89114 1.76271 2.06776 -0.10378 0.16739  -0.18780 93  SER A O   
5161 C CB  . SER E 85  ? 1.96685 1.88227 2.23375 -0.11903 0.14966  -0.14212 93  SER A CB  
5162 O OG  . SER E 85  ? 1.90501 1.83644 2.16617 -0.10747 0.14615  -0.17259 93  SER A OG  
5163 N N   . LEU E 86  ? 1.97899 1.71792 2.10921 -0.13794 0.15694  -0.17128 94  LEU A N   
5164 C CA  . LEU E 86  ? 1.97033 1.69214 2.06202 -0.12220 0.17567  -0.18203 94  LEU A CA  
5165 C C   . LEU E 86  ? 2.03684 1.82465 2.14319 -0.09662 0.20289  -0.16379 94  LEU A C   
5166 O O   . LEU E 86  ? 2.09396 1.88019 2.20833 -0.09447 0.21604  -0.13599 94  LEU A O   
5167 C CB  . LEU E 86  ? 1.95520 1.56956 1.98877 -0.13424 0.17651  -0.17903 94  LEU A CB  
5168 C CG  . LEU E 86  ? 1.87963 1.43207 1.88312 -0.15128 0.15247  -0.20091 94  LEU A CG  
5169 C CD1 . LEU E 86  ? 1.88450 1.32087 1.82316 -0.16938 0.14245  -0.19670 94  LEU A CD1 
5170 C CD2 . LEU E 86  ? 1.84300 1.40592 1.83555 -0.13459 0.16401  -0.21754 94  LEU A CD2 
5171 N N   . ARG E 87  ? 1.95122 1.79767 2.06305 -0.07880 0.20882  -0.17729 95  ARG A N   
5172 C CA  . ARG E 87  ? 1.94304 1.85330 2.06185 -0.05459 0.23071  -0.15881 95  ARG A CA  
5173 C C   . ARG E 87  ? 1.94428 1.82799 2.03939 -0.04684 0.24653  -0.15058 95  ARG A C   
5174 O O   . ARG E 87  ? 1.94926 1.77303 2.02268 -0.05681 0.24110  -0.16323 95  ARG A O   
5175 C CB  . ARG E 87  ? 1.90259 1.89986 2.03968 -0.04020 0.22223  -0.17594 95  ARG A CB  
5176 C CG  . ARG E 87  ? 1.88759 1.96225 2.03389 -0.01403 0.24053  -0.15134 95  ARG A CG  
5177 C CD  . ARG E 87  ? 1.89078 1.96254 2.05596 -0.01014 0.25743  -0.11708 95  ARG A CD  
5178 N NE  . ARG E 87  ? 1.92405 1.95546 2.10630 -0.03072 0.24247  -0.12183 95  ARG A NE  
5179 C CZ  . ARG E 87  ? 1.91546 1.98780 2.11974 -0.02386 0.23589  -0.12710 95  ARG A CZ  
5180 N NH1 . ARG E 87  ? 1.88121 2.02609 2.08083 0.00513  0.24412  -0.13257 95  ARG A NH1 
5181 N NH2 . ARG E 87  ? 1.95156 1.99001 2.17940 -0.04443 0.22112  -0.12429 95  ARG A NH2 
5182 N N   . ALA E 88  ? 1.91215 1.84562 2.01406 -0.02510 0.26934  -0.12325 96  ALA A N   
5183 C CA  . ALA E 88  ? 1.91144 1.82475 1.99832 -0.01169 0.29302  -0.10087 96  ALA A CA  
5184 C C   . ALA E 88  ? 1.91427 1.83015 2.00493 -0.01716 0.28016  -0.11823 96  ALA A C   
5185 O O   . ALA E 88  ? 1.93386 1.78240 2.00056 -0.01572 0.29377  -0.11067 96  ALA A O   
5186 C CB  . ALA E 88  ? 1.86538 1.85951 1.97202 0.01416  0.31508  -0.06643 96  ALA A CB  
5187 N N   . GLU E 89  ? 1.91384 1.90254 2.03182 -0.02207 0.25495  -0.14014 97  GLU A N   
5188 C CA  . GLU E 89  ? 1.92485 1.92523 2.05945 -0.03088 0.23908  -0.15371 97  GLU A CA  
5189 C C   . GLU E 89  ? 1.92481 1.83966 2.04214 -0.04568 0.23397  -0.17177 97  GLU A C   
5190 O O   . GLU E 89  ? 1.93393 1.83813 2.06265 -0.04688 0.23565  -0.16634 97  GLU A O   
5191 C CB  . GLU E 89  ? 1.92403 1.99560 2.07876 -0.03882 0.20654  -0.18381 97  GLU A CB  
5192 C CG  . GLU E 89  ? 1.91499 2.06609 2.07006 -0.02219 0.20702  -0.17355 97  GLU A CG  
5193 C CD  . GLU E 89  ? 1.89255 2.03211 2.03237 -0.01365 0.21816  -0.17338 97  GLU A CD  
5194 O OE1 . GLU E 89  ? 1.89069 1.96568 2.02365 -0.02616 0.21693  -0.18617 97  GLU A OE1 
5195 O OE2 . GLU E 89  ? 1.86845 2.06723 2.00745 0.00574  0.22791  -0.15525 97  GLU A OE2 
5196 N N   . ASP E 90  ? 1.98164 1.83985 2.07561 -0.05652 0.22723  -0.18810 98  ASP A N   
5197 C CA  . ASP E 90  ? 1.94260 1.72144 2.01427 -0.07008 0.21900  -0.20374 98  ASP A CA  
5198 C C   . ASP E 90  ? 1.96084 1.66348 1.99232 -0.05892 0.24532  -0.18051 98  ASP A C   
5199 O O   . ASP E 90  ? 1.91801 1.55967 1.92652 -0.06425 0.24156  -0.18968 98  ASP A O   
5200 C CB  . ASP E 90  ? 1.91031 1.65227 1.96910 -0.08532 0.20302  -0.21777 98  ASP A CB  
5201 C CG  . ASP E 90  ? 1.88374 1.68972 1.97748 -0.09011 0.18286  -0.23894 98  ASP A CG  
5202 O OD1 . ASP E 90  ? 1.88514 1.75339 2.00045 -0.08310 0.17825  -0.24960 98  ASP A OD1 
5203 O OD2 . ASP E 90  ? 1.86449 1.65535 1.96203 -0.10042 0.17095  -0.24337 98  ASP A OD2 
5204 N N   . THR E 91  ? 1.91790 1.61767 1.93476 -0.03960 0.27507  -0.14890 99  THR A N   
5205 C CA  . THR E 91  ? 1.93599 1.55666 1.90543 -0.02032 0.30855  -0.12349 99  THR A CA  
5206 C C   . THR E 91  ? 1.92181 1.54810 1.90774 -0.01292 0.31421  -0.11699 99  THR A C   
5207 O O   . THR E 91  ? 1.93435 1.64929 1.98093 -0.01164 0.30900  -0.10717 99  THR A O   
5208 C CB  . THR E 91  ? 1.97569 1.61692 1.94425 0.00525  0.34453  -0.08440 99  THR A CB  
5209 O OG1 . THR E 91  ? 2.00736 1.55096 1.91467 0.02892  0.38310  -0.06004 99  THR A OG1 
5210 C CG2 . THR E 91  ? 1.94110 1.70231 1.97617 0.01656  0.34735  -0.06223 99  THR A CG2 
5211 N N   . ALA E 92  ? 1.94073 1.47221 1.87315 -0.00998 0.32125  -0.12186 100 ALA A N   
5212 C CA  . ALA E 92  ? 1.93150 1.46137 1.88018 -0.00161 0.32873  -0.11258 100 ALA A CA  
5213 C C   . ALA E 92  ? 1.91612 1.32286 1.77909 0.00828  0.34151  -0.11607 100 ALA A C   
5214 O O   . ALA E 92  ? 1.90691 1.23478 1.70365 -0.00159 0.33088  -0.13477 100 ALA A O   
5215 C CB  . ALA E 92  ? 1.89403 1.49213 1.90789 -0.02785 0.29020  -0.14110 100 ALA A CB  
5216 N N   . VAL E 93  ? 1.92359 1.31459 1.78804 0.02769  0.36289  -0.09516 101 VAL A N   
5217 C CA  . VAL E 93  ? 1.91438 1.19914 1.70011 0.03759  0.36957  -0.10166 101 VAL A CA  
5218 C C   . VAL E 93  ? 1.86001 1.17190 1.68568 0.01042  0.33096  -0.13094 101 VAL A C   
5219 O O   . VAL E 93  ? 1.84729 1.24560 1.76152 0.00091  0.32077  -0.12792 101 VAL A O   
5220 C CB  . VAL E 93  ? 1.95966 1.20694 1.71920 0.08238  0.42283  -0.05530 101 VAL A CB  
5221 C CG1 . VAL E 93  ? 1.95926 1.31636 1.83191 0.08480  0.42843  -0.02545 101 VAL A CG1 
5222 C CG2 . VAL E 93  ? 1.97173 1.10164 1.63275 0.09746  0.43074  -0.06312 101 VAL A CG2 
5223 N N   . TYR E 94  ? 1.94661 1.18353 1.70814 -0.00360 0.30725  -0.15818 102 TYR A N   
5224 C CA  . TYR E 94  ? 1.88834 1.15022 1.68648 -0.02885 0.27064  -0.18441 102 TYR A CA  
5225 C C   . TYR E 94  ? 1.90941 1.09858 1.65368 -0.01128 0.28195  -0.17576 102 TYR A C   
5226 O O   . TYR E 94  ? 1.95667 1.04176 1.59484 0.00405  0.29252  -0.17322 102 TYR A O   
5227 C CB  . TYR E 94  ? 1.84733 1.10056 1.63116 -0.06003 0.23084  -0.21484 102 TYR A CB  
5228 C CG  . TYR E 94  ? 1.82811 1.17116 1.68055 -0.07508 0.21929  -0.22246 102 TYR A CG  
5229 C CD1 . TYR E 94  ? 1.87799 1.23197 1.72320 -0.06311 0.24127  -0.20561 102 TYR A CD1 
5230 C CD2 . TYR E 94  ? 1.77099 1.18426 1.68943 -0.09631 0.19031  -0.24399 102 TYR A CD2 
5231 C CE1 . TYR E 94  ? 1.88110 1.31846 1.78271 -0.07249 0.23243  -0.20940 102 TYR A CE1 
5232 C CE2 . TYR E 94  ? 1.77073 1.26055 1.73821 -0.10367 0.18306  -0.25016 102 TYR A CE2 
5233 C CZ  . TYR E 94  ? 1.83054 1.33447 1.78916 -0.09200 0.20308  -0.23248 102 TYR A CZ  
5234 O OH  . TYR E 94  ? 1.84628 1.42712 1.84742 -0.09523 0.19751  -0.23539 102 TYR A OH  
5235 N N   . TYR E 95  ? 1.83685 1.07599 1.64979 -0.01128 0.28166  -0.16939 103 TYR A N   
5236 C CA  . TYR E 95  ? 1.86272 1.05032 1.64279 0.00676  0.29360  -0.15668 103 TYR A CA  
5237 C C   . TYR E 95  ? 1.80941 1.01414 1.61978 -0.02022 0.25454  -0.18382 103 TYR A C   
5238 O O   . TYR E 95  ? 1.74542 1.02462 1.63627 -0.04635 0.22957  -0.20378 103 TYR A O   
5239 C CB  . TYR E 95  ? 1.89077 1.12308 1.73817 0.03087  0.32952  -0.11693 103 TYR A CB  
5240 C CG  . TYR E 95  ? 1.94054 1.17881 1.78358 0.06078  0.37252  -0.07839 103 TYR A CG  
5241 C CD1 . TYR E 95  ? 1.93320 1.25630 1.84931 0.04725  0.36767  -0.07459 103 TYR A CD1 
5242 C CD2 . TYR E 95  ? 2.00189 1.16127 1.76494 0.10675  0.42056  -0.04206 103 TYR A CD2 
5243 C CE1 . TYR E 95  ? 1.98021 1.31707 1.89981 0.07660  0.40834  -0.03219 103 TYR A CE1 
5244 C CE2 . TYR E 95  ? 2.03849 1.20443 1.80104 0.13968  0.46618  0.00003  103 TYR A CE2 
5245 C CZ  . TYR E 95  ? 2.02386 1.28270 1.87014 0.12338  0.45932  0.00657  103 TYR A CZ  
5246 O OH  . TYR E 95  ? 2.05763 1.32991 1.90939 0.15817  0.50606  0.05514  103 TYR A OH  
5247 N N   . CYS E 96  ? 1.91931 1.05272 1.66028 -0.01005 0.25159  -0.18220 104 CYS A N   
5248 C CA  . CYS E 96  ? 1.88754 1.03625 1.65777 -0.02850 0.22106  -0.19750 104 CYS A CA  
5249 C C   . CYS E 96  ? 1.93014 1.06782 1.71370 -0.00326 0.24593  -0.17100 104 CYS A C   
5250 O O   . CYS E 96  ? 2.00158 1.08823 1.72920 0.03199  0.28312  -0.14186 104 CYS A O   
5251 C CB  . CYS E 96  ? 1.91102 0.99571 1.59527 -0.04412 0.18579  -0.21589 104 CYS A CB  
5252 S SG  . CYS E 96  ? 2.03990 0.99275 1.56939 -0.01319 0.19887  -0.20167 104 CYS A SG  
5253 N N   . ALA E 97  ? 1.76772 0.95279 1.62812 -0.01782 0.22991  -0.17740 105 ALA A N   
5254 C CA  . ALA E 97  ? 1.79991 0.98699 1.69702 0.00353  0.25469  -0.14873 105 ALA A CA  
5255 C C   . ALA E 97  ? 1.78280 0.97951 1.70835 -0.00960 0.23007  -0.15941 105 ALA A C   
5256 O O   . ALA E 97  ? 1.72879 0.95113 1.67397 -0.03691 0.19612  -0.18753 105 ALA A O   
5257 C CB  . ALA E 97  ? 1.76379 1.02072 1.77232 0.00222  0.27505  -0.13148 105 ALA A CB  
5258 N N   . ARG E 98  ? 1.68531 0.86437 1.61748 0.01417  0.25203  -0.13041 106 ARG A N   
5259 C CA  . ARG E 98  ? 1.68179 0.87106 1.64890 0.00943  0.23822  -0.12978 106 ARG A CA  
5260 C C   . ARG E 98  ? 1.61661 0.86343 1.71190 0.00259  0.25227  -0.12080 106 ARG A C   
5261 O O   . ARG E 98  ? 1.61991 0.88106 1.75874 0.01520  0.28158  -0.09474 106 ARG A O   
5262 C CB  . ARG E 98  ? 1.79022 0.91582 1.67101 0.04293  0.25303  -0.10066 106 ARG A CB  
5263 C CG  . ARG E 98  ? 1.79528 0.94080 1.73553 0.04936  0.25619  -0.08251 106 ARG A CG  
5264 C CD  . ARG E 98  ? 1.92688 1.00998 1.76765 0.08480  0.26776  -0.05327 106 ARG A CD  
5265 N NE  . ARG E 98  ? 1.96186 1.02584 1.80290 0.12678  0.31941  -0.00859 106 ARG A NE  
5266 C CZ  . ARG E 98  ? 2.03361 1.07465 1.85267 0.16059  0.34142  0.02810  106 ARG A CZ  
5267 N NH1 . ARG E 98  ? 2.09507 1.12794 1.88389 0.15720  0.31412  0.02491  106 ARG A NH1 
5268 N NH2 . ARG E 98  ? 2.04530 1.07582 1.87566 0.20117  0.39355  0.07485  106 ARG A NH2 
5269 N N   . HIS E 99  ? 1.74868 1.02594 1.90607 -0.01742 0.23148  -0.13955 107 HIS A N   
5270 C CA  . HIS E 99  ? 1.68953 1.00325 1.96002 -0.02577 0.24145  -0.13477 107 HIS A CA  
5271 C C   . HIS E 99  ? 1.72320 1.01993 2.00754 -0.01020 0.24966  -0.11300 107 HIS A C   
5272 O O   . HIS E 99  ? 1.71190 1.01305 1.99614 -0.01895 0.22922  -0.12902 107 HIS A O   
5273 C CB  . HIS E 99  ? 1.59579 0.95012 1.92399 -0.05777 0.21616  -0.17637 107 HIS A CB  
5274 C CG  . HIS E 99  ? 1.54546 0.91620 1.97050 -0.06874 0.21883  -0.18076 107 HIS A CG  
5275 N ND1 . HIS E 99  ? 1.48565 0.86931 1.94167 -0.08611 0.20013  -0.21571 107 HIS A ND1 
5276 C CD2 . HIS E 99  ? 1.55041 0.92031 2.04702 -0.06386 0.23956  -0.15305 107 HIS A CD2 
5277 C CE1 . HIS E 99  ? 1.46021 0.84084 1.99412 -0.09222 0.20809  -0.21434 107 HIS A CE1 
5278 N NE2 . HIS E 99  ? 1.49425 0.86909 2.05989 -0.08184 0.22986  -0.17593 107 HIS A NE2 
5279 N N   . ALA E 100 ? 1.69614 0.97846 1.99843 0.01572  0.28262  -0.07048 108 ALA A N   
5280 C CA  . ALA E 100 ? 1.73119 0.99960 2.05086 0.03578  0.29675  -0.04145 108 ALA A CA  
5281 C C   . ALA E 100 ? 1.65719 0.95255 2.10644 0.02466  0.31057  -0.03154 108 ALA A C   
5282 O O   . ALA E 100 ? 1.61526 0.93249 2.13235 0.01180  0.31905  -0.02699 108 ALA A O   
5283 C CB  . ALA E 100 ? 1.83261 1.06004 2.07607 0.07827  0.32763  0.00431  108 ALA A CB  
5284 N N   . TRP E 101 ? 1.72083 1.01356 2.20638 0.02767  0.31043  -0.02698 109 TRP A N   
5285 C CA  . TRP E 101 ? 1.65288 0.95713 2.25764 0.01501  0.32200  -0.02159 109 TRP A CA  
5286 C C   . TRP E 101 ? 1.66709 0.96844 2.32915 0.03684  0.35996  0.03489  109 TRP A C   
5287 O O   . TRP E 101 ? 1.61086 0.92459 2.38016 0.01750  0.36622  0.04128  109 TRP A O   
5288 C CB  . TRP E 101 ? 1.64083 0.93921 2.26825 0.01567  0.31596  -0.03079 109 TRP A CB  
5289 C CG  . TRP E 101 ? 1.60648 0.91575 2.20949 -0.00702 0.28403  -0.08157 109 TRP A CG  
5290 C CD1 . TRP E 101 ? 1.64672 0.96064 2.18938 -0.00089 0.26611  -0.08879 109 TRP A CD1 
5291 C CD2 . TRP E 101 ? 1.53341 0.85311 2.17258 -0.03791 0.26646  -0.12729 109 TRP A CD2 
5292 N NE1 . TRP E 101 ? 1.59370 0.92303 2.13944 -0.02282 0.24401  -0.13198 109 TRP A NE1 
5293 C CE2 . TRP E 101 ? 1.52513 0.85474 2.12195 -0.04365 0.24474  -0.15856 109 TRP A CE2 
5294 C CE3 . TRP E 101 ? 1.48510 0.80839 2.18781 -0.06153 0.26469  -0.14197 109 TRP A CE3 
5295 C CZ2 . TRP E 101 ? 1.46732 0.80605 2.07486 -0.06593 0.22734  -0.20450 109 TRP A CZ2 
5296 C CZ3 . TRP E 101 ? 1.43637 0.76627 2.14370 -0.08785 0.24070  -0.19186 109 TRP A CZ3 
5297 C CH2 . TRP E 101 ? 1.42646 0.76189 2.08227 -0.08686 0.22517  -0.22303 109 TRP A CH2 
5298 N N   . TYR E 102 ? 1.64867 0.93134 2.24124 0.07698  0.38503  0.07820  110 TYR A N   
5299 C CA  . TYR E 102 ? 1.65242 0.93669 2.30201 0.10399  0.42787  0.13999  110 TYR A CA  
5300 C C   . TYR E 102 ? 1.61942 0.93058 2.32917 0.08788  0.43443  0.14925  110 TYR A C   
5301 O O   . TYR E 102 ? 1.58879 0.91850 2.40198 0.09113  0.46085  0.19561  110 TYR A O   
5302 C CB  . TYR E 102 ? 1.74631 0.99873 2.28721 0.15672  0.45609  0.18358  110 TYR A CB  
5303 C CG  . TYR E 102 ? 1.74304 0.99896 2.33487 0.19368  0.50835  0.25528  110 TYR A CG  
5304 C CD1 . TYR E 102 ? 1.70557 0.97009 2.39155 0.20767  0.53578  0.30021  110 TYR A CD1 
5305 C CD2 . TYR E 102 ? 1.77299 1.02422 2.32255 0.21816  0.53471  0.28392  110 TYR A CD2 
5306 C CE1 . TYR E 102 ? 1.69136 0.96476 2.43436 0.24311  0.58647  0.37346  110 TYR A CE1 
5307 C CE2 . TYR E 102 ? 1.76166 1.02186 2.36456 0.25693  0.58786  0.35834  110 TYR A CE2 
5308 C CZ  . TYR E 102 ? 1.71790 0.99154 2.42009 0.26851  0.61285  0.40386  110 TYR A CZ  
5309 O OH  . TYR E 102 ? 1.69704 0.98482 2.46171 0.30878  0.66852  0.48530  110 TYR A OH  
5310 N N   . TYR E 103 ? 1.58724 0.90532 2.24028 0.07039  0.41058  0.11134  111 TYR A N   
5311 C CA  . TYR E 103 ? 1.56145 0.91455 2.27408 0.05044  0.40956  0.11635  111 TYR A CA  
5312 C C   . TYR E 103 ? 1.49731 0.87612 2.27406 -0.00289 0.36659  0.06038  111 TYR A C   
5313 O O   . TYR E 103 ? 1.48947 0.89955 2.28992 -0.02425 0.35290  0.05071  111 TYR A O   
5314 C CB  . TYR E 103 ? 1.62078 0.96224 2.22603 0.07414  0.41985  0.12142  111 TYR A CB  
5315 C CG  . TYR E 103 ? 1.69178 0.99485 2.21897 0.13167  0.46538  0.17616  111 TYR A CG  
5316 C CD1 . TYR E 103 ? 1.68489 1.00469 2.28519 0.16071  0.51150  0.24673  111 TYR A CD1 
5317 C CD2 . TYR E 103 ? 1.76829 1.01636 2.14730 0.15739  0.46127  0.15975  111 TYR A CD2 
5318 C CE1 . TYR E 103 ? 1.74542 1.02563 2.26417 0.22097  0.55874  0.29939  111 TYR A CE1 
5319 C CE2 . TYR E 103 ? 1.84690 1.04849 2.13584 0.21265  0.50131  0.20621  111 TYR A CE2 
5320 C CZ  . TYR E 103 ? 1.83143 1.04796 2.18631 0.24776  0.55306  0.27576  111 TYR A CZ  
5321 O OH  . TYR E 103 ? 1.90675 1.07286 2.16221 0.31023  0.59842  0.32453  111 TYR A OH  
5322 N N   . GLY E 104 ? 1.55074 0.91464 2.34694 -0.02080 0.34663  0.02459  112 GLY A N   
5323 C CA  . GLY E 104 ? 1.49646 0.87105 2.34648 -0.06535 0.31094  -0.02753 112 GLY A CA  
5324 C C   . GLY E 104 ? 1.48425 0.87067 2.26021 -0.08138 0.28033  -0.07915 112 GLY A C   
5325 O O   . GLY E 104 ? 1.50959 0.88703 2.18800 -0.06203 0.28078  -0.08532 112 GLY A O   
5326 N N   . TRP E 105 ? 1.64892 1.05270 2.47203 -0.11865 0.25129  -0.11628 113 TRP A N   
5327 C CA  . TRP E 105 ? 1.63615 1.05898 2.40062 -0.13333 0.22446  -0.15964 113 TRP A CA  
5328 C C   . TRP E 105 ? 1.68265 1.13640 2.42763 -0.12373 0.23497  -0.12842 113 TRP A C   
5329 O O   . TRP E 105 ? 1.68642 1.17498 2.49674 -0.14416 0.22630  -0.11608 113 TRP A O   
5330 C CB  . TRP E 105 ? 1.59056 1.02019 2.40179 -0.17226 0.19077  -0.20556 113 TRP A CB  
5331 C CG  . TRP E 105 ? 1.55577 0.94661 2.36744 -0.17843 0.18181  -0.24512 113 TRP A CG  
5332 C CD1 . TRP E 105 ? 1.54592 0.90263 2.42812 -0.18982 0.18461  -0.24493 113 TRP A CD1 
5333 C CD2 . TRP E 105 ? 1.53764 0.91759 2.27877 -0.17021 0.17304  -0.28542 113 TRP A CD2 
5334 N NE1 . TRP E 105 ? 1.53071 0.85544 2.37880 -0.18503 0.17974  -0.28352 113 TRP A NE1 
5335 C CE2 . TRP E 105 ? 1.52536 0.86405 2.29433 -0.17300 0.17433  -0.30760 113 TRP A CE2 
5336 C CE3 . TRP E 105 ? 1.53443 0.93512 2.19662 -0.15997 0.16615  -0.30060 113 TRP A CE3 
5337 C CZ2 . TRP E 105 ? 1.51677 0.84401 2.23319 -0.16045 0.17153  -0.33858 113 TRP A CZ2 
5338 C CZ3 . TRP E 105 ? 1.51697 0.90670 2.13884 -0.15296 0.16044  -0.33207 113 TRP A CZ3 
5339 C CH2 . TRP E 105 ? 1.51186 0.86554 2.16297 -0.15164 0.16528  -0.34997 113 TRP A CH2 
5340 N N   . GLY E 106 ? 1.43722 0.87619 2.09140 -0.09351 0.25190  -0.11487 114 GLY A N   
5341 C CA  . GLY E 106 ? 1.49513 0.94749 2.12200 -0.07379 0.27348  -0.07757 114 GLY A CA  
5342 C C   . GLY E 106 ? 1.54204 0.95618 2.04631 -0.04328 0.28601  -0.07609 114 GLY A C   
5343 O O   . GLY E 106 ? 1.54944 0.92730 2.00060 -0.03114 0.28456  -0.08424 114 GLY A O   
5344 N N   . LEU E 107 ? 0.99150 1.30050 1.59672 0.12626  -0.21822 -0.12609 115 LEU A N   
5345 C CA  . LEU E 107 ? 1.14857 1.41961 1.69862 0.11818  -0.16802 -0.15325 115 LEU A CA  
5346 C C   . LEU E 107 ? 1.24536 1.51591 1.81792 0.12711  -0.11934 -0.14511 115 LEU A C   
5347 O O   . LEU E 107 ? 1.25656 1.51796 1.87841 0.14803  -0.09964 -0.12169 115 LEU A O   
5348 C CB  . LEU E 107 ? 1.17356 1.40613 1.71782 0.12679  -0.16398 -0.15246 115 LEU A CB  
5349 C CG  . LEU E 107 ? 1.08037 1.31885 1.59578 0.11943  -0.20968 -0.16110 115 LEU A CG  
5350 C CD1 . LEU E 107 ? 1.07706 1.28668 1.60547 0.13291  -0.21452 -0.14871 115 LEU A CD1 
5351 C CD2 . LEU E 107 ? 1.11420 1.34834 1.55049 0.09375  -0.20276 -0.19828 115 LEU A CD2 
5352 N N   . ASP E 108 ? 1.20438 1.48583 1.73907 0.11306  -0.09961 -0.16500 116 ASP A N   
5353 C CA  . ASP E 108 ? 1.30033 1.57875 1.84085 0.12314  -0.04858 -0.16334 116 ASP A CA  
5354 C C   . ASP E 108 ? 1.39394 1.61760 1.88265 0.12459  -0.00873 -0.19041 116 ASP A C   
5355 O O   . ASP E 108 ? 1.38792 1.57999 1.86163 0.12250  -0.02018 -0.19662 116 ASP A O   
5356 C CB  . ASP E 108 ? 1.31272 1.62216 1.83247 0.11040  -0.04105 -0.17291 116 ASP A CB  
5357 C CG  . ASP E 108 ? 1.29436 1.59150 1.73589 0.08423  -0.05135 -0.21297 116 ASP A CG  
5358 O OD1 . ASP E 108 ? 1.30420 1.56537 1.69984 0.07557  -0.05239 -0.23656 116 ASP A OD1 
5359 O OD2 . ASP E 108 ? 1.26438 1.58905 1.69058 0.07193  -0.05678 -0.22003 116 ASP A OD2 
5360 N N   . TYR E 109 ? 1.34889 1.56067 1.80807 0.12819  0.03521  -0.20654 117 TYR A N   
5361 C CA  . TYR E 109 ? 1.41609 1.57712 1.84653 0.14075  0.07709  -0.22283 117 TYR A CA  
5362 C C   . TYR E 109 ? 1.41881 1.53274 1.82218 0.13298  0.06476  -0.23525 117 TYR A C   
5363 O O   . TYR E 109 ? 1.41211 1.51515 1.76541 0.10849  0.04525  -0.25807 117 TYR A O   
5364 C CB  . TYR E 109 ? 1.45984 1.60257 1.82342 0.13222  0.10868  -0.25747 117 TYR A CB  
5365 C CG  . TYR E 109 ? 1.46424 1.65059 1.83349 0.13420  0.12232  -0.25328 117 TYR A CG  
5366 C CD1 . TYR E 109 ? 1.42613 1.65376 1.79510 0.11342  0.09006  -0.25147 117 TYR A CD1 
5367 C CD2 . TYR E 109 ? 1.50230 1.68728 1.87199 0.15771  0.16722  -0.25280 117 TYR A CD2 
5368 C CE1 . TYR E 109 ? 1.43206 1.69807 1.80467 0.11358  0.10202  -0.24655 117 TYR A CE1 
5369 C CE2 . TYR E 109 ? 1.50785 1.73494 1.88035 0.15999  0.18160  -0.24742 117 TYR A CE2 
5370 C CZ  . TYR E 109 ? 1.47684 1.74378 1.85161 0.13638  0.14888  -0.24345 117 TYR A CZ  
5371 O OH  . TYR E 109 ? 1.48351 1.79221 1.86140 0.13708  0.16188  -0.23612 117 TYR A OH  
5372 N N   . TRP E 110 ? 1.53178 1.61945 1.96836 0.15395  0.07660  -0.21933 118 TRP A N   
5373 C CA  . TRP E 110 ? 1.52949 1.57599 1.95399 0.14974  0.06292  -0.22210 118 TRP A CA  
5374 C C   . TRP E 110 ? 1.58783 1.57274 1.95928 0.14960  0.09517  -0.24917 118 TRP A C   
5375 O O   . TRP E 110 ? 1.62178 1.59445 1.97128 0.15922  0.12893  -0.26436 118 TRP A O   
5376 C CB  . TRP E 110 ? 1.48294 1.53484 1.97822 0.17315  0.05204  -0.18715 118 TRP A CB  
5377 C CG  . TRP E 110 ? 1.39212 1.48600 1.93107 0.16975  0.00495  -0.16271 118 TRP A CG  
5378 C CD1 . TRP E 110 ? 1.33341 1.48102 1.90618 0.16812  -0.01651 -0.14714 118 TRP A CD1 
5379 C CD2 . TRP E 110 ? 1.33523 1.41859 1.88887 0.17014  -0.02855 -0.15039 118 TRP A CD2 
5380 N NE1 . TRP E 110 ? 1.23212 1.40004 1.83804 0.16830  -0.06346 -0.12798 118 TRP A NE1 
5381 C CE2 . TRP E 110 ? 1.23199 1.36251 1.82584 0.17075  -0.07057 -0.12998 118 TRP A CE2 
5382 C CE3 . TRP E 110 ? 1.35527 1.39346 1.89079 0.17038  -0.02882 -0.15406 118 TRP A CE3 
5383 C CZ2 . TRP E 110 ? 1.14227 1.27573 1.75590 0.17463  -0.11200 -0.11532 118 TRP A CZ2 
5384 C CZ3 . TRP E 110 ? 1.27958 1.32411 1.83601 0.17262  -0.06756 -0.13740 118 TRP A CZ3 
5385 C CH2 . TRP E 110 ? 1.17123 1.26292 1.76501 0.17618  -0.10832 -0.11929 118 TRP A CH2 
5386 N N   . GLY E 111 ? 1.62389 1.56923 1.97497 0.13981  0.08248  -0.25397 119 GLY A N   
5387 C CA  . GLY E 111 ? 1.67040 1.55163 1.97573 0.13814  0.10516  -0.27601 119 GLY A CA  
5388 C C   . GLY E 111 ? 1.69292 1.54351 2.03243 0.17028  0.12935  -0.26353 119 GLY A C   
5389 O O   . GLY E 111 ? 1.67334 1.55666 2.06794 0.19514  0.13833  -0.24118 119 GLY A O   
5390 N N   . GLN E 112 ? 1.66581 1.45280 1.97258 0.16966  0.13862  -0.27767 120 GLN A N   
5391 C CA  . GLN E 112 ? 1.68768 1.43708 2.02062 0.20034  0.15787  -0.26908 120 GLN A CA  
5392 C C   . GLN E 112 ? 1.67240 1.39937 2.03210 0.19953  0.13519  -0.24902 120 GLN A C   
5393 O O   . GLN E 112 ? 1.65386 1.37810 2.06342 0.22648  0.13989  -0.22826 120 GLN A O   
5394 C CB  . GLN E 112 ? 1.74558 1.43001 2.02350 0.20599  0.18275  -0.29961 120 GLN A CB  
5395 C CG  . GLN E 112 ? 1.76056 1.44887 1.98919 0.20073  0.20219  -0.32840 120 GLN A CG  
5396 C CD  . GLN E 112 ? 1.74010 1.44100 1.92592 0.16072  0.18131  -0.34358 120 GLN A CD  
5397 O OE1 . GLN E 112 ? 1.75034 1.41544 1.90547 0.13598  0.16329  -0.35119 120 GLN A OE1 
5398 N NE2 . GLN E 112 ? 1.70897 1.46354 1.89444 0.15386  0.18231  -0.34615 120 GLN A NE2 
5399 N N   . GLY E 113 ? 1.67841 1.39173 2.00539 0.16935  0.11081  -0.25424 121 GLY A N   
5400 C CA  . GLY E 113 ? 1.67050 1.36050 2.01379 0.16612  0.08925  -0.23635 121 GLY A CA  
5401 C C   . GLY E 113 ? 1.73036 1.35592 2.01958 0.14674  0.09018  -0.25461 121 GLY A C   
5402 O O   . GLY E 113 ? 1.77464 1.34822 2.04389 0.15927  0.11175  -0.27043 121 GLY A O   
5403 N N   . THR E 114 ? 1.71161 1.34080 1.97638 0.11699  0.06544  -0.25209 122 THR A N   
5404 C CA  . THR E 114 ? 1.77025 1.34219 1.98915 0.09437  0.06169  -0.26322 122 THR A CA  
5405 C C   . THR E 114 ? 1.77143 1.33464 2.01166 0.09027  0.03829  -0.23689 122 THR A C   
5406 O O   . THR E 114 ? 1.73338 1.34599 1.98882 0.08236  0.01563  -0.22040 122 THR A O   
5407 C CB  . THR E 114 ? 1.77861 1.36552 1.94453 0.05988  0.05557  -0.28389 122 THR A CB  
5408 O OG1 . THR E 114 ? 1.78411 1.35744 1.92212 0.06524  0.07983  -0.31159 122 THR A OG1 
5409 C CG2 . THR E 114 ? 1.83052 1.37594 1.96014 0.03090  0.04200  -0.28463 122 THR A CG2 
5410 N N   . LEU E 115 ? 1.75682 1.25643 1.99629 0.09733  0.04212  -0.23345 123 LEU A N   
5411 C CA  . LEU E 115 ? 1.74786 1.23509 2.01547 0.10125  0.02325  -0.20632 123 LEU A CA  
5412 C C   . LEU E 115 ? 1.79742 1.27122 2.02852 0.06549  0.00278  -0.20054 123 LEU A C   
5413 O O   . LEU E 115 ? 1.85905 1.29164 2.04621 0.04333  0.00707  -0.21736 123 LEU A O   
5414 C CB  . LEU E 115 ? 1.76397 1.18994 2.05230 0.12872  0.03587  -0.20389 123 LEU A CB  
5415 C CG  . LEU E 115 ? 1.77512 1.16622 2.07558 0.12522  0.01619  -0.18100 123 LEU A CG  
5416 C CD1 . LEU E 115 ? 1.69519 1.13579 2.04596 0.14043  -0.00015 -0.15332 123 LEU A CD1 
5417 C CD2 . LEU E 115 ? 1.80869 1.12767 2.11453 0.14719  0.02767  -0.18616 123 LEU A CD2 
5418 N N   . VAL E 116 ? 1.80035 1.31201 2.04963 0.06045  -0.02061 -0.17594 124 VAL A N   
5419 C CA  . VAL E 116 ? 1.84984 1.35928 2.07073 0.02965  -0.04049 -0.16352 124 VAL A CA  
5420 C C   . VAL E 116 ? 1.83516 1.32870 2.08774 0.04287  -0.05592 -0.13404 124 VAL A C   
5421 O O   . VAL E 116 ? 1.76066 1.29142 2.05312 0.06648  -0.06571 -0.11839 124 VAL A O   
5422 C CB  . VAL E 116 ? 1.83335 1.41526 2.03537 0.00986  -0.05561 -0.16394 124 VAL A CB  
5423 C CG1 . VAL E 116 ? 1.86837 1.46740 2.05813 -0.01016 -0.07918 -0.14026 124 VAL A CG1 
5424 C CG2 . VAL E 116 ? 1.86111 1.44347 2.01950 -0.01314 -0.04287 -0.19306 124 VAL A CG2 
5425 N N   . THR E 117 ? 1.93198 1.36832 2.16737 0.02772  -0.06033 -0.12599 125 THR A N   
5426 C CA  . THR E 117 ? 1.92415 1.33471 2.18530 0.03871  -0.07430 -0.09881 125 THR A CA  
5427 C C   . THR E 117 ? 1.97862 1.40280 2.21476 0.00758  -0.09522 -0.07750 125 THR A C   
5428 O O   . THR E 117 ? 2.05637 1.45140 2.25560 -0.02407 -0.09550 -0.08228 125 THR A O   
5429 C CB  . THR E 117 ? 1.95596 1.28196 2.22148 0.05081  -0.06324 -0.10507 125 THR A CB  
5430 O OG1 . THR E 117 ? 1.91240 1.23336 2.20154 0.08280  -0.04185 -0.12339 125 THR A OG1 
5431 C CG2 . THR E 117 ? 1.94537 1.24125 2.23685 0.06175  -0.07879 -0.07738 125 THR A CG2 
5432 N N   . VAL E 118 ? 1.94741 1.41447 2.20431 0.01756  -0.11379 -0.05252 126 VAL A N   
5433 C CA  . VAL E 118 ? 2.00199 1.48889 2.23606 -0.00846 -0.13281 -0.02869 126 VAL A CA  
5434 C C   . VAL E 118 ? 2.01190 1.45023 2.26281 -0.00191 -0.14341 -0.00236 126 VAL A C   
5435 O O   . VAL E 118 ? 1.94444 1.40271 2.22486 0.02294  -0.15613 0.01663  126 VAL A O   
5436 C CB  . VAL E 118 ? 1.95821 1.53269 2.19209 -0.00406 -0.14968 -0.01875 126 VAL A CB  
5437 C CG1 . VAL E 118 ? 2.03508 1.63752 2.23526 -0.03580 -0.16369 0.00098  126 VAL A CG1 
5438 C CG2 . VAL E 118 ? 1.92661 1.54588 2.15243 -0.00278 -0.14098 -0.04584 126 VAL A CG2 
5439 N N   . SER E 119 ? 2.05874 1.43088 2.29019 -0.02420 -0.14093 -0.00112 127 SER A N   
5440 C CA  . SER E 119 ? 2.07916 1.39827 2.32174 -0.02301 -0.15278 0.02370  127 SER A CA  
5441 C C   . SER E 119 ? 2.18325 1.46168 2.39056 -0.06484 -0.15943 0.03211  127 SER A C   
5442 O O   . SER E 119 ? 2.22977 1.49414 2.40955 -0.08710 -0.15082 0.01110  127 SER A O   
5443 C CB  . SER E 119 ? 2.03610 1.28861 2.30957 0.00948  -0.14327 0.01332  127 SER A CB  
5444 O OG  . SER E 119 ? 2.09476 1.27117 2.36052 -0.00266 -0.15177 0.02510  127 SER A OG  
5445 N N   . SER E 120 ? 2.10075 1.36282 2.30930 -0.07635 -0.17679 0.06487  128 SER A N   
5446 C CA  . SER E 120 ? 2.19141 1.41247 2.37262 -0.11744 -0.18765 0.08032  128 SER A CA  
5447 C C   . SER E 120 ? 2.21799 1.33431 2.40148 -0.11502 -0.18850 0.07060  128 SER A C   
5448 O O   . SER E 120 ? 2.28715 1.35654 2.44938 -0.14892 -0.20098 0.08170  128 SER A O   
5449 C CB  . SER E 120 ? 2.21303 1.46920 2.39320 -0.13286 -0.20696 0.12366  128 SER A CB  
5450 O OG  . SER E 120 ? 2.14454 1.40895 2.35531 -0.09708 -0.21280 0.13842  128 SER A OG  
5451 N N   . ALA E 121 ? 2.25240 1.33219 2.46150 -0.07538 -0.17736 0.05071  129 ALA A N   
5452 C CA  . ALA E 121 ? 2.27613 1.25820 2.48553 -0.06680 -0.17827 0.03727  129 ALA A CA  
5453 C C   . ALA E 121 ? 2.32982 1.27482 2.50665 -0.08488 -0.17059 0.00674  129 ALA A C   
5454 O O   . ALA E 121 ? 2.33209 1.32814 2.49179 -0.09715 -0.15959 -0.00865 129 ALA A O   
5455 C CB  . ALA E 121 ? 2.19717 1.16083 2.44346 -0.01703 -0.16622 0.02337  129 ALA A CB  
5456 N N   . SER E 122 ? 2.18777 1.03979 2.35465 -0.08474 -0.17875 -0.00310 130 SER A N   
5457 C CA  . SER E 122 ? 2.24385 1.04493 2.37586 -0.10348 -0.17933 -0.02909 130 SER A CA  
5458 C C   . SER E 122 ? 2.22555 0.98585 2.35867 -0.06319 -0.16008 -0.06959 130 SER A C   
5459 O O   . SER E 122 ? 2.18992 0.92409 2.34966 -0.02456 -0.15427 -0.07373 130 SER A O   
5460 C CB  . SER E 122 ? 2.31143 1.03170 2.42569 -0.13459 -0.20834 -0.01148 130 SER A CB  
5461 O OG  . SER E 122 ? 2.36102 1.02378 2.44165 -0.15009 -0.21334 -0.03794 130 SER A OG  
5462 N N   . THR E 123 ? 2.19781 0.95412 2.30107 -0.07183 -0.15038 -0.09893 131 THR A N   
5463 C CA  . THR E 123 ? 2.19872 0.91721 2.29592 -0.03432 -0.13184 -0.13810 131 THR A CA  
5464 C C   . THR E 123 ? 2.25296 0.86581 2.34196 -0.01838 -0.14749 -0.14761 131 THR A C   
5465 O O   . THR E 123 ? 2.31612 0.86681 2.38088 -0.04952 -0.17444 -0.13945 131 THR A O   
5466 C CB  . THR E 123 ? 2.22119 0.95142 2.28213 -0.05025 -0.12209 -0.16634 131 THR A CB  
5467 O OG1 . THR E 123 ? 2.17405 1.00070 2.24021 -0.06761 -0.11161 -0.15690 131 THR A OG1 
5468 C CG2 . THR E 123 ? 2.21736 0.92269 2.27240 -0.00711 -0.09931 -0.20540 131 THR A CG2 
5469 N N   . LYS E 124 ? 2.37228 0.96548 2.48203 0.03072  -0.13214 -0.16470 132 LYS A N   
5470 C CA  . LYS E 124 ? 2.41504 0.91023 2.51496 0.05533  -0.14468 -0.18084 132 LYS A CA  
5471 C C   . LYS E 124 ? 2.41875 0.90071 2.50470 0.09642  -0.12076 -0.22277 132 LYS A C   
5472 O O   . LYS E 124 ? 2.35813 0.90360 2.47005 0.12758  -0.09126 -0.23016 132 LYS A O   
5473 C CB  . LYS E 124 ? 2.37878 0.85697 2.51745 0.08089  -0.15093 -0.16051 132 LYS A CB  
5474 N N   . GLY E 125 ? 2.68350 1.08359 2.72863 0.09739  -0.13505 -0.24896 133 GLY A N   
5475 C CA  . GLY E 125 ? 2.69694 1.07625 2.72432 0.14172  -0.11471 -0.28929 133 GLY A CA  
5476 C C   . GLY E 125 ? 2.67283 1.03416 2.73145 0.19462  -0.10476 -0.29320 133 GLY A C   
5477 O O   . GLY E 125 ? 2.66979 0.99656 2.74944 0.19375  -0.12442 -0.27153 133 GLY A O   
5478 N N   . PRO E 126 ? 2.66654 1.05251 2.72947 0.24184  -0.07428 -0.31959 134 PRO A N   
5479 C CA  . PRO E 126 ? 2.63375 1.01898 2.73336 0.29363  -0.06083 -0.32048 134 PRO A CA  
5480 C C   . PRO E 126 ? 2.70557 0.98668 2.77711 0.32490  -0.08060 -0.34510 134 PRO A C   
5481 O O   . PRO E 126 ? 2.77929 0.98947 2.80094 0.31245  -0.10232 -0.36632 134 PRO A O   
5482 C CB  . PRO E 126 ? 2.58779 1.05039 2.70159 0.32772  -0.01962 -0.33658 134 PRO A CB  
5483 C CG  . PRO E 126 ? 2.63794 1.08761 2.69832 0.31149  -0.01754 -0.36410 134 PRO A CG  
5484 C CD  . PRO E 126 ? 2.67473 1.09061 2.70871 0.25126  -0.05068 -0.34938 134 PRO A CD  
5485 N N   . SER E 127 ? 2.73441 1.00670 2.83937 0.36785  -0.07464 -0.34267 135 SER A N   
5486 C CA  . SER E 127 ? 2.79559 0.98168 2.87740 0.41186  -0.08715 -0.37093 135 SER A CA  
5487 C C   . SER E 127 ? 2.75760 0.99535 2.86929 0.47350  -0.04934 -0.38470 135 SER A C   
5488 O O   . SER E 127 ? 2.67517 0.99171 2.84113 0.48043  -0.02685 -0.36076 135 SER A O   
5489 C CB  . SER E 127 ? 2.81611 0.94546 2.90416 0.39910  -0.11746 -0.34862 135 SER A CB  
5490 O OG  . SER E 127 ? 2.74388 0.91930 2.88462 0.38431  -0.11683 -0.31231 135 SER A OG  
5491 N N   . VAL E 128 ? 2.75936 0.97245 2.83423 0.51295  -0.03726 -0.41654 136 VAL A N   
5492 C CA  . VAL E 128 ? 2.73977 1.01176 2.83739 0.57089  0.00280  -0.42893 136 VAL A CA  
5493 C C   . VAL E 128 ? 2.82126 1.05598 2.91211 0.61120  0.00211  -0.43784 136 VAL A C   
5494 O O   . VAL E 128 ? 2.91286 1.08377 2.95537 0.61677  -0.01521 -0.46246 136 VAL A O   
5495 C CB  . VAL E 128 ? 2.73744 1.03603 2.80177 0.58770  0.02611  -0.45975 136 VAL A CB  
5496 C CG1 . VAL E 128 ? 2.69442 1.07487 2.79550 0.64133  0.07023  -0.46266 136 VAL A CG1 
5497 C CG2 . VAL E 128 ? 2.66669 1.00420 2.72629 0.53315  0.02487  -0.44783 136 VAL A CG2 
5498 N N   . PHE E 129 ? 2.78828 1.06497 2.92915 0.63898  0.01909  -0.41787 137 PHE A N   
5499 C CA  . PHE E 129 ? 2.85696 1.11329 2.99863 0.68353  0.02458  -0.42761 137 PHE A CA  
5500 C C   . PHE E 129 ? 2.82590 1.16115 2.99964 0.73917  0.06957  -0.43450 137 PHE A C   
5501 O O   . PHE E 129 ? 2.73609 1.14763 2.95192 0.74191  0.09379  -0.41516 137 PHE A O   
5502 C CB  . PHE E 129 ? 2.86173 1.09539 3.03158 0.67301  0.00572  -0.39883 137 PHE A CB  
5503 C CG  . PHE E 129 ? 2.86621 1.04629 3.02109 0.61356  -0.03415 -0.38052 137 PHE A CG  
5504 C CD1 . PHE E 129 ? 2.95849 1.05285 3.06725 0.59377  -0.06970 -0.39390 137 PHE A CD1 
5505 C CD2 . PHE E 129 ? 2.77959 0.99927 2.96920 0.57771  -0.03770 -0.34816 137 PHE A CD2 
5506 C CE1 . PHE E 129 ? 2.96404 1.01466 3.06243 0.53840  -0.10572 -0.37311 137 PHE A CE1 
5507 C CE2 . PHE E 129 ? 2.78485 0.96191 2.96338 0.52395  -0.07282 -0.32895 137 PHE A CE2 
5508 C CZ  . PHE E 129 ? 2.87735 0.97034 3.01038 0.50380  -0.10591 -0.34029 137 PHE A CZ  
5509 N N   . PRO E 130 ? 2.89902 1.22210 3.05611 0.78362  0.07931  -0.46050 138 PRO A N   
5510 C CA  . PRO E 130 ? 2.87281 1.27824 3.06570 0.83629  0.12211  -0.46611 138 PRO A CA  
5511 C C   . PRO E 130 ? 2.82583 1.28184 3.08429 0.85646  0.13934  -0.43411 138 PRO A C   
5512 O O   . PRO E 130 ? 2.84369 1.25778 3.10834 0.84258  0.11722  -0.41567 138 PRO A O   
5513 C CB  . PRO E 130 ? 2.97769 1.34476 3.12887 0.87416  0.11778  -0.50247 138 PRO A CB  
5514 C CG  . PRO E 130 ? 3.05487 1.32394 3.17339 0.85123  0.07394  -0.50401 138 PRO A CG  
5515 C CD  . PRO E 130 ? 3.01037 1.24736 3.12223 0.78862  0.04818  -0.48230 138 PRO A CD  
5516 N N   . LEU E 131 ? 2.76472 1.31551 3.07344 0.88834  0.17841  -0.42619 139 LEU A N   
5517 C CA  . LEU E 131 ? 2.72849 1.33843 3.09965 0.91709  0.19993  -0.39748 139 LEU A CA  
5518 C C   . LEU E 131 ? 2.76095 1.42438 3.16679 0.96892  0.22106  -0.42585 139 LEU A C   
5519 O O   . LEU E 131 ? 2.70835 1.46587 3.15223 0.98854  0.24023  -0.43384 139 LEU A O   
5520 C CB  . LEU E 131 ? 2.63953 1.32146 3.00238 0.91313  0.19826  -0.36267 139 LEU A CB  
5521 C CG  . LEU E 131 ? 2.59158 1.23816 2.95241 0.85548  0.16603  -0.35108 139 LEU A CG  
5522 C CD1 . LEU E 131 ? 2.46952 1.21874 2.90100 0.83335  0.16843  -0.32323 139 LEU A CD1 
5523 C CD2 . LEU E 131 ? 2.63088 1.20536 2.98746 0.83166  0.13859  -0.33717 139 LEU A CD2 
5524 N N   . ALA E 132 ? 2.39157 1.39186 2.98428 0.18305  0.32641  -0.20546 140 ALA A N   
5525 C CA  . ALA E 132 ? 2.42648 1.38986 2.97276 0.24710  0.32716  -0.22100 140 ALA A CA  
5526 C C   . ALA E 132 ? 2.43482 1.50297 3.01547 0.27176  0.37301  -0.22659 140 ALA A C   
5527 O O   . ALA E 132 ? 2.45394 1.60917 3.08813 0.25927  0.38246  -0.21983 140 ALA A O   
5528 C CB  . ALA E 132 ? 2.49897 1.38582 3.00015 0.29003  0.28127  -0.21851 140 ALA A CB  
5529 N N   . PRO E 133 ? 2.43616 1.49855 2.98806 0.30878  0.40143  -0.23826 141 PRO A N   
5530 C CA  . PRO E 133 ? 2.44820 1.61317 3.03963 0.33458  0.44967  -0.23918 141 PRO A CA  
5531 C C   . PRO E 133 ? 2.51370 1.69730 3.09540 0.39778  0.43662  -0.24405 141 PRO A C   
5532 O O   . PRO E 133 ? 2.54639 1.68955 3.06981 0.46286  0.43948  -0.25474 141 PRO A O   
5533 C CB  . PRO E 133 ? 2.43058 1.56268 2.97514 0.35815  0.48386  -0.24526 141 PRO A CB  
5534 C CG  . PRO E 133 ? 2.44497 1.44164 2.90286 0.38247  0.43662  -0.25698 141 PRO A CG  
5535 C CD  . PRO E 133 ? 2.42523 1.38798 2.90735 0.32915  0.39143  -0.25030 141 PRO A CD  
5536 N N   . SER E 134 ? 2.35993 1.60024 2.99084 0.38517  0.41889  -0.23831 142 SER A N   
5537 C CA  . SER E 134 ? 2.42225 1.68413 3.04717 0.44744  0.40202  -0.24476 142 SER A CA  
5538 C C   . SER E 134 ? 2.41299 1.78534 3.08537 0.48562  0.45406  -0.25174 142 SER A C   
5539 O O   . SER E 134 ? 2.36352 1.82334 3.10404 0.44658  0.50061  -0.24617 142 SER A O   
5540 C CB  . SER E 134 ? 2.45765 1.75628 3.12150 0.42601  0.37037  -0.23672 142 SER A CB  
5541 O OG  . SER E 134 ? 2.50992 1.85832 3.18619 0.48644  0.36022  -0.24570 142 SER A OG  
5542 N N   . SER E 135 ? 2.26473 1.63288 2.90344 0.56340  0.44585  -0.26324 143 SER A N   
5543 C CA  . SER E 135 ? 2.26304 1.74810 2.95333 0.60657  0.49829  -0.26829 143 SER A CA  
5544 C C   . SER E 135 ? 2.22679 1.85915 3.04335 0.56705  0.51835  -0.26412 143 SER A C   
5545 O O   . SER E 135 ? 2.19282 1.94005 3.08613 0.56808  0.57398  -0.26143 143 SER A O   
5546 C CB  . SER E 135 ? 2.35605 1.81531 2.99004 0.70241  0.47699  -0.28471 143 SER A CB  
5547 O OG  . SER E 135 ? 2.35497 1.89597 3.05083 0.72136  0.45568  -0.29048 143 SER A OG  
5548 N N   . LYS E 136 ? 2.19461 1.82465 3.03443 0.53342  0.47293  -0.26302 144 LYS A N   
5549 C CA  . LYS E 136 ? 2.16479 1.92130 3.11813 0.49126  0.48151  -0.26332 144 LYS A CA  
5550 C C   . LYS E 136 ? 2.09970 1.88466 3.10244 0.41346  0.51585  -0.25340 144 LYS A C   
5551 O O   . LYS E 136 ? 2.05683 1.95935 3.16417 0.38625  0.54896  -0.25443 144 LYS A O   
5552 C CB  . LYS E 136 ? 2.21401 1.94521 3.15614 0.48492  0.42103  -0.26462 144 LYS A CB  
5553 N N   . SER E 137 ? 2.20298 1.88100 3.13672 0.37701  0.50522  -0.24494 145 SER A N   
5554 C CA  . SER E 137 ? 2.14798 1.83772 3.11417 0.31052  0.53475  -0.23765 145 SER A CA  
5555 C C   . SER E 137 ? 2.10619 1.82528 3.08572 0.31850  0.59579  -0.23185 145 SER A C   
5556 O O   . SER E 137 ? 2.06311 1.80102 3.07861 0.26592  0.62484  -0.22459 145 SER A O   
5557 C CB  . SER E 137 ? 2.14818 1.71853 3.03723 0.27764  0.50580  -0.23214 145 SER A CB  
5558 O OG  . SER E 137 ? 2.18778 1.73644 3.06754 0.26343  0.45819  -0.23027 145 SER A OG  
5559 N N   . THR E 138 ? 2.15896 1.87434 3.10112 0.38567  0.61583  -0.23371 146 THR A N   
5560 C CA  . THR E 138 ? 2.14457 1.89526 3.09395 0.40129  0.68150  -0.22346 146 THR A CA  
5561 C C   . THR E 138 ? 2.10494 2.01086 3.19144 0.37778  0.72584  -0.21693 146 THR A C   
5562 O O   . THR E 138 ? 2.11179 2.10882 3.26029 0.41379  0.72194  -0.22571 146 THR A O   
5563 C CB  . THR E 138 ? 2.19631 1.90019 3.05857 0.48951  0.68802  -0.22955 146 THR A CB  
5564 O OG1 . THR E 138 ? 2.22829 1.78556 2.97655 0.50749  0.63354  -0.23932 146 THR A OG1 
5565 C CG2 . THR E 138 ? 2.19568 1.91522 3.03778 0.50943  0.75838  -0.21499 146 THR A CG2 
5566 N N   . SER E 139 ? 1.94000 1.87638 3.07996 0.31730  0.76461  -0.20260 147 SER A N   
5567 C CA  . SER E 139 ? 1.90570 1.98492 3.18480 0.28979  0.81035  -0.19338 147 SER A CA  
5568 C C   . SER E 139 ? 1.96588 2.07506 3.23769 0.32206  0.88807  -0.17070 147 SER A C   
5569 O O   . SER E 139 ? 1.96628 2.07850 3.26039 0.27941  0.93648  -0.14848 147 SER A O   
5570 C CB  . SER E 139 ? 1.84022 1.93726 3.19231 0.20323  0.80303  -0.19095 147 SER A CB  
5571 O OG  . SER E 139 ? 1.82456 2.03447 3.30130 0.17008  0.85648  -0.17586 147 SER A OG  
5572 N N   . GLY E 140 ? 2.02712 2.15678 3.26246 0.40257  0.90021  -0.17556 148 GLY A N   
5573 C CA  . GLY E 140 ? 2.09768 2.26429 3.31810 0.44608  0.97838  -0.15339 148 GLY A CA  
5574 C C   . GLY E 140 ? 2.15722 2.18507 3.23581 0.45555  0.99627  -0.14060 148 GLY A C   
5575 O O   . GLY E 140 ? 2.19004 2.08940 3.14364 0.48835  0.94564  -0.15834 148 GLY A O   
5576 N N   . GLY E 141 ? 2.17932 2.22928 3.27796 0.42677  1.06655  -0.10912 149 GLY A N   
5577 C CA  . GLY E 141 ? 2.24082 2.15755 3.20465 0.43356  1.08237  -0.09653 149 GLY A CA  
5578 C C   . GLY E 141 ? 2.18761 1.99581 3.11135 0.37356  1.02254  -0.10963 149 GLY A C   
5579 O O   . GLY E 141 ? 2.23857 1.92127 3.03895 0.38814  1.01479  -0.10953 149 GLY A O   
5580 N N   . THR E 142 ? 2.09953 1.95490 3.12171 0.31235  0.97845  -0.12301 150 THR A N   
5581 C CA  . THR E 142 ? 2.08000 1.85496 3.08161 0.25294  0.92659  -0.13478 150 THR A CA  
5582 C C   . THR E 142 ? 2.08394 1.81021 3.04530 0.27220  0.85056  -0.16338 150 THR A C   
5583 O O   . THR E 142 ? 2.06841 1.87323 3.10375 0.27486  0.82566  -0.17477 150 THR A O   
5584 C CB  . THR E 142 ? 2.02012 1.88106 3.15695 0.17162  0.93279  -0.12850 150 THR A CB  
5585 O OG1 . THR E 142 ? 2.00511 1.95331 3.22056 0.16005  1.00730  -0.09906 150 THR A OG1 
5586 C CG2 . THR E 142 ? 2.01332 1.78369 3.11152 0.11567  0.90605  -0.13183 150 THR A CG2 
5587 N N   . ALA E 143 ? 2.11743 1.71429 2.96587 0.28422  0.81215  -0.17401 151 ALA A N   
5588 C CA  . ALA E 143 ? 2.12389 1.66067 2.92917 0.29967  0.74342  -0.19496 151 ALA A CA  
5589 C C   . ALA E 143 ? 2.09352 1.57707 2.89811 0.23629  0.70377  -0.20094 151 ALA A C   
5590 O O   . ALA E 143 ? 2.07475 1.51834 2.85962 0.20390  0.72075  -0.19492 151 ALA A O   
5591 C CB  . ALA E 143 ? 2.16548 1.59549 2.84580 0.37219  0.72572  -0.20472 151 ALA A CB  
5592 N N   . ALA E 144 ? 2.07279 1.55657 2.89609 0.22183  0.65235  -0.21167 152 ALA A N   
5593 C CA  . ALA E 144 ? 2.04214 1.49178 2.87100 0.16565  0.61747  -0.21624 152 ALA A CA  
5594 C C   . ALA E 144 ? 2.04333 1.39162 2.79585 0.18341  0.56610  -0.22370 152 ALA A C   
5595 O O   . ALA E 144 ? 2.08169 1.42066 2.81793 0.21993  0.53887  -0.22639 152 ALA A O   
5596 C CB  . ALA E 144 ? 2.04376 1.58778 2.96619 0.12653  0.60424  -0.21861 152 ALA A CB  
5597 N N   . LEU E 145 ? 2.24696 1.51952 2.95822 0.15680  0.55090  -0.22701 153 LEU A N   
5598 C CA  . LEU E 145 ? 2.23384 1.41619 2.89313 0.15998  0.50136  -0.23249 153 LEU A CA  
5599 C C   . LEU E 145 ? 2.16682 1.33073 2.83953 0.10429  0.48866  -0.23436 153 LEU A C   
5600 O O   . LEU E 145 ? 2.13264 1.31375 2.81942 0.07936  0.51539  -0.23603 153 LEU A O   
5601 C CB  . LEU E 145 ? 2.25514 1.33757 2.82644 0.21395  0.48935  -0.24151 153 LEU A CB  
5602 C CG  . LEU E 145 ? 2.22795 1.25044 2.74808 0.21680  0.50449  -0.24832 153 LEU A CG  
5603 C CD1 . LEU E 145 ? 2.18162 1.12501 2.67890 0.19037  0.46028  -0.25856 153 LEU A CD1 
5604 C CD2 . LEU E 145 ? 2.28464 1.25181 2.72430 0.28924  0.51400  -0.25514 153 LEU A CD2 
5605 N N   . GLY E 146 ? 2.20937 1.33442 2.87570 0.08691  0.44862  -0.23292 154 GLY A N   
5606 C CA  . GLY E 146 ? 2.14652 1.26552 2.83044 0.03828  0.43956  -0.23504 154 GLY A CA  
5607 C C   . GLY E 146 ? 2.13188 1.18955 2.80095 0.02544  0.39855  -0.23149 154 GLY A C   
5608 O O   . GLY E 146 ? 2.17326 1.17208 2.81052 0.05379  0.37086  -0.22824 154 GLY A O   
5609 N N   . CYS E 147 ? 2.16011 1.23459 2.85734 -0.01849 0.39512  -0.23164 155 CYS A N   
5610 C CA  . CYS E 147 ? 2.14084 1.17854 2.84480 -0.04259 0.36477  -0.22409 155 CYS A CA  
5611 C C   . CYS E 147 ? 2.12337 1.23451 2.86994 -0.08102 0.37356  -0.21068 155 CYS A C   
5612 O O   . CYS E 147 ? 2.10000 1.27694 2.87000 -0.09526 0.39687  -0.21801 155 CYS A O   
5613 C CB  . CYS E 147 ? 2.09701 1.08158 2.79117 -0.05181 0.35126  -0.24098 155 CYS A CB  
5614 S SG  . CYS E 147 ? 2.16021 1.02779 2.79573 -0.00651 0.31545  -0.25584 155 CYS A SG  
5615 N N   . LEU E 148 ? 2.03089 1.12545 2.78422 -0.09647 0.35385  -0.19031 156 LEU A N   
5616 C CA  . LEU E 148 ? 2.03039 1.18628 2.81002 -0.12655 0.36249  -0.17279 156 LEU A CA  
5617 C C   . LEU E 148 ? 1.99261 1.12893 2.79411 -0.15928 0.35275  -0.16330 156 LEU A C   
5618 O O   . LEU E 148 ? 2.01601 1.09019 2.81535 -0.16234 0.32917  -0.14753 156 LEU A O   
5619 C CB  . LEU E 148 ? 2.11274 1.27304 2.87719 -0.11168 0.35407  -0.14879 156 LEU A CB  
5620 C CG  . LEU E 148 ? 2.14048 1.35185 2.91366 -0.13408 0.36129  -0.12554 156 LEU A CG  
5621 C CD1 . LEU E 148 ? 2.11046 1.40608 2.90357 -0.14377 0.38276  -0.14419 156 LEU A CD1 
5622 C CD2 . LEU E 148 ? 2.24276 1.44168 2.98749 -0.11130 0.34794  -0.10180 156 LEU A CD2 
5623 N N   . VAL E 149 ? 1.98787 1.17805 2.81545 -0.18332 0.36917  -0.17347 157 VAL A N   
5624 C CA  . VAL E 149 ? 1.95589 1.15008 2.81693 -0.21391 0.36565  -0.16638 157 VAL A CA  
5625 C C   . VAL E 149 ? 1.97906 1.24092 2.85159 -0.23289 0.38484  -0.14072 157 VAL A C   
5626 O O   . VAL E 149 ? 1.97023 1.29717 2.84042 -0.23184 0.40313  -0.15259 157 VAL A O   
5627 C CB  . VAL E 149 ? 1.90475 1.10844 2.78126 -0.21906 0.36842  -0.19875 157 VAL A CB  
5628 C CG1 . VAL E 149 ? 1.89380 1.12702 2.81657 -0.24909 0.36867  -0.19273 157 VAL A CG1 
5629 C CG2 . VAL E 149 ? 1.92173 1.04649 2.77444 -0.19566 0.34725  -0.22000 157 VAL A CG2 
5630 N N   . LYS E 150 ? 1.90465 1.14567 2.78516 -0.24832 0.37949  -0.10479 158 LYS A N   
5631 C CA  . LYS E 150 ? 1.95790 1.24784 2.83000 -0.25806 0.39885  -0.07113 158 LYS A CA  
5632 C C   . LYS E 150 ? 1.94295 1.25872 2.85855 -0.29316 0.41278  -0.04643 158 LYS A C   
5633 O O   . LYS E 150 ? 1.91634 1.18687 2.87254 -0.31366 0.39650  -0.04098 158 LYS A O   
5634 C CB  . LYS E 150 ? 2.04327 1.28289 2.87800 -0.24231 0.38492  -0.04077 158 LYS A CB  
5635 C CG  . LYS E 150 ? 2.12625 1.39721 2.93691 -0.24731 0.40184  0.00054  158 LYS A CG  
5636 C CD  . LYS E 150 ? 2.19249 1.50698 2.95986 -0.21443 0.40492  -0.01134 158 LYS A CD  
5637 C CE  . LYS E 150 ? 2.31453 1.62698 3.03612 -0.20592 0.40948  0.03213  158 LYS A CE  
5638 N NZ  . LYS E 150 ? 2.32593 1.68397 3.05301 -0.23091 0.44013  0.06185  158 LYS A NZ  
5639 N N   . ASP E 151 ? 1.91300 1.30463 2.82161 -0.29747 0.44208  -0.03258 159 ASP A N   
5640 C CA  . ASP E 151 ? 1.91579 1.35074 2.85877 -0.32624 0.46750  0.00166  159 ASP A CA  
5641 C C   . ASP E 151 ? 1.83458 1.28367 2.84927 -0.35043 0.46470  -0.01830 159 ASP A C   
5642 O O   . ASP E 151 ? 1.83581 1.25610 2.90427 -0.38001 0.45704  0.00460  159 ASP A O   
5643 C CB  . ASP E 151 ? 1.97643 1.36232 2.91206 -0.34233 0.46759  0.05868  159 ASP A CB  
5644 C CG  . ASP E 151 ? 2.08214 1.46387 2.94203 -0.31417 0.47202  0.08065  159 ASP A CG  
5645 O OD1 . ASP E 151 ? 2.11777 1.56283 2.94174 -0.29042 0.48631  0.06196  159 ASP A OD1 
5646 O OD2 . ASP E 151 ? 2.14371 1.45548 2.97920 -0.31373 0.45699  0.11495  159 ASP A OD2 
5647 N N   . TYR E 152 ? 1.82486 1.31829 2.84205 -0.33680 0.46782  -0.06270 160 TYR A N   
5648 C CA  . TYR E 152 ? 1.76830 1.28724 2.84678 -0.35132 0.46500  -0.08743 160 TYR A CA  
5649 C C   . TYR E 152 ? 1.77325 1.38682 2.85128 -0.34234 0.49391  -0.10269 160 TYR A C   
5650 O O   . TYR E 152 ? 1.81006 1.45188 2.83294 -0.31870 0.50419  -0.11250 160 TYR A O   
5651 C CB  . TYR E 152 ? 1.73183 1.18938 2.80753 -0.33682 0.43114  -0.13309 160 TYR A CB  
5652 C CG  . TYR E 152 ? 1.72239 1.19339 2.75205 -0.30882 0.43274  -0.17226 160 TYR A CG  
5653 C CD1 . TYR E 152 ? 1.70445 1.22409 2.74766 -0.30318 0.43919  -0.20514 160 TYR A CD1 
5654 C CD2 . TYR E 152 ? 1.73989 1.17517 2.71770 -0.28836 0.42673  -0.17593 160 TYR A CD2 
5655 C CE1 . TYR E 152 ? 1.70011 1.22122 2.70385 -0.28163 0.43765  -0.23844 160 TYR A CE1 
5656 C CE2 . TYR E 152 ? 1.72961 1.17774 2.67849 -0.26942 0.42870  -0.20810 160 TYR A CE2 
5657 C CZ  . TYR E 152 ? 1.70734 1.19300 2.66802 -0.26801 0.43325  -0.23824 160 TYR A CZ  
5658 O OH  . TYR E 152 ? 1.69903 1.18798 2.63341 -0.25298 0.43249  -0.26832 160 TYR A OH  
5659 N N   . PHE E 153 ? 2.22211 1.05004 2.25661 -0.24476 0.52285  0.07775  161 PHE A N   
5660 C CA  . PHE E 153 ? 2.14127 1.10124 2.30847 -0.22778 0.48935  0.09755  161 PHE A CA  
5661 C C   . PHE E 153 ? 2.14503 1.17840 2.36959 -0.31959 0.45246  0.09879  161 PHE A C   
5662 O O   . PHE E 153 ? 2.21150 1.16861 2.37129 -0.38899 0.47181  0.08517  161 PHE A O   
5663 C CB  . PHE E 153 ? 2.13605 1.05851 2.30069 -0.17962 0.53095  0.10658  161 PHE A CB  
5664 C CG  . PHE E 153 ? 2.06177 1.11251 2.35162 -0.13678 0.49879  0.12599  161 PHE A CG  
5665 C CD1 . PHE E 153 ? 1.98369 1.08297 2.32117 -0.04651 0.47805  0.12992  161 PHE A CD1 
5666 C CD2 . PHE E 153 ? 2.06063 1.18198 2.42180 -0.18447 0.48898  0.13872  161 PHE A CD2 
5667 C CE1 . PHE E 153 ? 1.91495 1.12496 2.36140 -0.00302 0.44445  0.14495  161 PHE A CE1 
5668 C CE2 . PHE E 153 ? 2.00470 1.24129 2.47350 -0.13959 0.45965  0.15594  161 PHE A CE2 
5669 C CZ  . PHE E 153 ? 1.94079 1.21789 2.44786 -0.04752 0.43609  0.15846  161 PHE A CZ  
5670 N N   . PRO E 154 ? 1.99343 1.16932 2.33589 -0.32296 0.39648  0.11204  162 PRO A N   
5671 C CA  . PRO E 154 ? 1.91457 1.18500 2.34120 -0.25200 0.36187  0.12605  162 PRO A CA  
5672 C C   . PRO E 154 ? 1.91168 1.20869 2.33399 -0.25972 0.32831  0.12401  162 PRO A C   
5673 O O   . PRO E 154 ? 1.98434 1.22187 2.32722 -0.31181 0.33355  0.11088  162 PRO A O   
5674 C CB  . PRO E 154 ? 1.84936 1.24840 2.39714 -0.26655 0.32239  0.14121  162 PRO A CB  
5675 C CG  . PRO E 154 ? 1.87709 1.28601 2.41725 -0.36636 0.30699  0.13209  162 PRO A CG  
5676 C CD  . PRO E 154 ? 1.97562 1.23347 2.38639 -0.40173 0.36098  0.11338  162 PRO A CD  
5677 N N   . GLU E 155 ? 1.84504 1.22778 2.35102 -0.20530 0.29425  0.13754  163 GLU A N   
5678 C CA  . GLU E 155 ? 1.83707 1.25985 2.35641 -0.21376 0.26195  0.14276  163 GLU A CA  
5679 C C   . GLU E 155 ? 1.84037 1.33696 2.39539 -0.28817 0.21456  0.14595  163 GLU A C   
5680 O O   . GLU E 155 ? 1.80525 1.35773 2.41549 -0.31859 0.19599  0.14760  163 GLU A O   
5681 C CB  . GLU E 155 ? 1.73624 1.23543 2.35255 -0.13988 0.23573  0.15779  163 GLU A CB  
5682 C CG  . GLU E 155 ? 1.72685 1.15108 2.29686 -0.07182 0.27607  0.15041  163 GLU A CG  
5683 C CD  . GLU E 155 ? 1.76991 1.16214 2.28924 -0.07984 0.28585  0.15082  163 GLU A CD  
5684 O OE1 . GLU E 155 ? 1.87718 1.17581 2.27932 -0.11768 0.31963  0.13745  163 GLU A OE1 
5685 O OE2 . GLU E 155 ? 1.69808 1.15531 2.29334 -0.04707 0.26144  0.16494  163 GLU A OE2 
5686 N N   . PRO E 156 ? 1.80267 1.30007 2.32344 -0.31621 0.19538  0.14657  164 PRO A N   
5687 C CA  . PRO E 156 ? 1.85003 1.29436 2.31065 -0.28502 0.21672  0.14847  164 PRO A CA  
5688 C C   . PRO E 156 ? 1.98715 1.31034 2.30354 -0.32098 0.25349  0.12815  164 PRO A C   
5689 O O   . PRO E 156 ? 2.05237 1.33333 2.31473 -0.38159 0.25362  0.11083  164 PRO A O   
5690 C CB  . PRO E 156 ? 1.81482 1.35639 2.34386 -0.29354 0.16518  0.16836  164 PRO A CB  
5691 C CG  . PRO E 156 ? 1.83501 1.42105 2.37464 -0.36392 0.12561  0.16159  164 PRO A CG  
5692 C CD  . PRO E 156 ? 1.79617 1.37508 2.35849 -0.37371 0.14116  0.15045  164 PRO A CD  
5693 N N   . VAL E 157 ? 1.99404 1.26168 2.25016 -0.28244 0.28353  0.12934  165 VAL A N   
5694 C CA  . VAL E 157 ? 2.12769 1.28281 2.24142 -0.30552 0.31559  0.11166  165 VAL A CA  
5695 C C   . VAL E 157 ? 2.16834 1.34817 2.26924 -0.28989 0.30791  0.12771  165 VAL A C   
5696 O O   . VAL E 157 ? 2.09032 1.32368 2.26492 -0.23560 0.31083  0.14805  165 VAL A O   
5697 C CB  . VAL E 157 ? 2.15464 1.19310 2.18208 -0.26512 0.37544  0.09527  165 VAL A CB  
5698 C CG1 . VAL E 157 ? 2.28802 1.21868 2.17319 -0.27002 0.40756  0.08065  165 VAL A CG1 
5699 C CG2 . VAL E 157 ? 2.15748 1.14524 2.16483 -0.29520 0.38976  0.07957  165 VAL A CG2 
5700 N N   . THR E 158 ? 2.20867 1.34942 2.21840 -0.33619 0.29766  0.11881  166 THR A N   
5701 C CA  . THR E 158 ? 2.28631 1.43856 2.26274 -0.32261 0.29597  0.13580  166 THR A CA  
5702 C C   . THR E 158 ? 2.41610 1.44401 2.24488 -0.30510 0.34758  0.11948  166 THR A C   
5703 O O   . THR E 158 ? 2.51336 1.44363 2.23477 -0.33931 0.35917  0.08974  166 THR A O   
5704 C CB  . THR E 158 ? 2.36854 1.56655 2.33790 -0.37710 0.24374  0.13822  166 THR A CB  
5705 O OG1 . THR E 158 ? 2.53385 1.63007 2.36077 -0.41836 0.24986  0.10870  166 THR A OG1 
5706 C CG2 . THR E 158 ? 2.26434 1.55361 2.34572 -0.41153 0.19454  0.13819  166 THR A CG2 
5707 N N   . VAL E 159 ? 2.40095 1.43201 2.22742 -0.25152 0.37870  0.13855  167 VAL A N   
5708 C CA  . VAL E 159 ? 2.52063 1.44249 2.21280 -0.22279 0.43151  0.12585  167 VAL A CA  
5709 C C   . VAL E 159 ? 2.61414 1.55797 2.27432 -0.20771 0.43757  0.15070  167 VAL A C   
5710 O O   . VAL E 159 ? 2.52935 1.53898 2.27483 -0.16259 0.45288  0.18027  167 VAL A O   
5711 C CB  . VAL E 159 ? 2.42893 1.32180 2.14287 -0.15938 0.47780  0.12222  167 VAL A CB  
5712 C CG1 . VAL E 159 ? 2.56384 1.33736 2.12762 -0.13125 0.53086  0.10503  167 VAL A CG1 
5713 C CG2 . VAL E 159 ? 2.33315 1.20986 2.08354 -0.16739 0.47279  0.10373  167 VAL A CG2 
5714 N N   . SER E 160 ? 2.60728 1.49721 2.14827 -0.24471 0.42443  0.13934  168 SER A N   
5715 C CA  . SER E 160 ? 2.73685 1.61748 2.20553 -0.22427 0.44117  0.15982  168 SER A CA  
5716 C C   . SER E 160 ? 2.86807 1.63046 2.19149 -0.18751 0.49956  0.14210  168 SER A C   
5717 O O   . SER E 160 ? 2.87663 1.55494 2.14283 -0.18573 0.52029  0.11066  168 SER A O   
5718 C CB  . SER E 160 ? 2.88254 1.76583 2.29003 -0.27445 0.39207  0.15556  168 SER A CB  
5719 O OG  . SER E 160 ? 3.06184 1.89251 2.34316 -0.25310 0.41531  0.16454  168 SER A OG  
5720 N N   . TRP E 161 ? 2.93507 1.68721 2.19199 -0.15604 0.52774  0.16363  169 TRP A N   
5721 C CA  . TRP E 161 ? 3.07688 1.72200 2.18898 -0.11518 0.58363  0.14944  169 TRP A CA  
5722 C C   . TRP E 161 ? 3.29891 1.88312 2.25668 -0.12419 0.57912  0.14707  169 TRP A C   
5723 O O   . TRP E 161 ? 3.29856 1.94780 2.28234 -0.12047 0.56897  0.18200  169 TRP A O   
5724 C CB  . TRP E 161 ? 2.97296 1.66363 2.15528 -0.04768 0.63894  0.17960  169 TRP A CB  
5725 C CG  . TRP E 161 ? 2.83957 1.52932 2.09649 -0.01801 0.65995  0.16472  169 TRP A CG  
5726 C CD1 . TRP E 161 ? 2.63638 1.41798 2.06066 -0.01642 0.63737  0.17503  169 TRP A CD1 
5727 C CD2 . TRP E 161 ? 2.90370 1.49000 2.06103 0.02038  0.70597  0.13530  169 TRP A CD2 
5728 N NE1 . TRP E 161 ? 2.56618 1.30867 2.00046 0.02271  0.66642  0.15388  169 TRP A NE1 
5729 C CE2 . TRP E 161 ? 2.72004 1.34258 1.99219 0.04513  0.70932  0.12978  169 TRP A CE2 
5730 C CE3 . TRP E 161 ? 3.09472 1.55730 2.07114 0.04028  0.74286  0.11202  169 TRP A CE3 
5731 C CZ2 . TRP E 161 ? 2.70270 1.24197 1.91373 0.08911  0.74903  0.10280  169 TRP A CZ2 
5732 C CZ3 . TRP E 161 ? 3.07318 1.45331 1.99152 0.08177  0.78230  0.08535  169 TRP A CZ3 
5733 C CH2 . TRP E 161 ? 2.86865 1.28742 1.90367 0.10569  0.78549  0.08138  169 TRP A CH2 
5734 N N   . ASN E 162 ? 3.27512 1.72897 2.06821 -0.13300 0.58599  0.10564  170 ASN A N   
5735 C CA  . ASN E 162 ? 3.50627 1.87988 2.12690 -0.13248 0.58206  0.09470  170 ASN A CA  
5736 C C   . ASN E 162 ? 3.56379 1.99356 2.20273 -0.17886 0.51860  0.10280  170 ASN A C   
5737 O O   . ASN E 162 ? 3.63973 2.07777 2.21346 -0.15936 0.51965  0.12579  170 ASN A O   
5738 C CB  . ASN E 162 ? 3.50656 1.87146 2.06466 -0.06277 0.64495  0.12553  170 ASN A CB  
5739 C CG  . ASN E 162 ? 3.43969 1.76489 1.99539 -0.01083 0.70647  0.11886  170 ASN A CG  
5740 O OD1 . ASN E 162 ? 3.27377 1.66598 1.97402 -0.00167 0.71600  0.12868  170 ASN A OD1 
5741 N ND2 . ASN E 162 ? 3.55771 1.76988 1.94268 0.02765  0.74587  0.09933  170 ASN A ND2 
5742 N N   . SER E 163 ? 3.37042 1.83737 2.09503 -0.23791 0.46398  0.08360  171 SER A N   
5743 C CA  . SER E 163 ? 3.41484 1.94385 2.17408 -0.28495 0.39660  0.08602  171 SER A CA  
5744 C C   . SER E 163 ? 3.30445 1.94685 2.15652 -0.25810 0.39809  0.14161  171 SER A C   
5745 O O   . SER E 163 ? 3.42243 2.07426 2.21429 -0.25971 0.37190  0.15423  171 SER A O   
5746 C CB  . SER E 163 ? 3.70310 2.13159 2.28659 -0.30719 0.36307  0.04844  171 SER A CB  
5747 O OG  . SER E 163 ? 3.82737 2.18401 2.26315 -0.25183 0.40664  0.05840  171 SER A OG  
5748 N N   . GLY E 164 ? 3.26273 1.98735 2.26182 -0.23111 0.42836  0.17454  172 GLY A N   
5749 C CA  . GLY E 164 ? 3.12509 1.96320 2.24536 -0.21164 0.42744  0.22739  172 GLY A CA  
5750 C C   . GLY E 164 ? 3.13308 1.96714 2.21008 -0.15363 0.48769  0.26813  172 GLY A C   
5751 O O   . GLY E 164 ? 2.97476 1.90106 2.18247 -0.13052 0.50443  0.31365  172 GLY A O   
5752 N N   . ALA E 165 ? 3.18510 1.91448 2.08477 -0.12864 0.52135  0.25333  173 ALA A N   
5753 C CA  . ALA E 165 ? 3.20481 1.93241 2.05119 -0.07328 0.57938  0.29574  173 ALA A CA  
5754 C C   . ALA E 165 ? 3.04466 1.81785 2.00209 -0.02706 0.64330  0.32218  173 ALA A C   
5755 O O   . ALA E 165 ? 2.93968 1.79511 1.99806 -0.00116 0.67092  0.37388  173 ALA A O   
5756 C CB  . ALA E 165 ? 3.41869 2.01735 2.04002 -0.05163 0.59990  0.26900  173 ALA A CB  
5757 N N   . LEU E 166 ? 3.19653 1.91668 2.14060 -0.01580 0.66617  0.28689  174 LEU A N   
5758 C CA  . LEU E 166 ? 3.05713 1.81499 2.09947 0.03276  0.72300  0.30379  174 LEU A CA  
5759 C C   . LEU E 166 ? 2.84745 1.72222 2.10629 0.01691  0.69343  0.32076  174 LEU A C   
5760 O O   . LEU E 166 ? 2.79327 1.66595 2.10096 -0.01170 0.65718  0.28880  174 LEU A O   
5761 C CB  . LEU E 166 ? 3.12775 1.78226 2.07238 0.05393  0.75275  0.25781  174 LEU A CB  
5762 C CG  . LEU E 166 ? 3.00399 1.69400 2.04700 0.10810  0.80629  0.26717  174 LEU A CG  
5763 C CD1 . LEU E 166 ? 2.95734 1.71047 2.04375 0.15568  0.86058  0.31859  174 LEU A CD1 
5764 C CD2 . LEU E 166 ? 3.09843 1.67181 2.01604 0.13612  0.83856  0.22238  174 LEU A CD2 
5765 N N   . THR E 167 ? 2.82957 1.80352 2.21779 0.03661  0.70912  0.37159  175 THR A N   
5766 C CA  . THR E 167 ? 2.63072 1.71482 2.22532 0.02562  0.67684  0.38827  175 THR A CA  
5767 C C   . THR E 167 ? 2.50217 1.65301 2.23103 0.07623  0.72688  0.41840  175 THR A C   
5768 O O   . THR E 167 ? 2.35552 1.56582 2.23312 0.08463  0.71106  0.41166  175 THR A O   
5769 C CB  . THR E 167 ? 2.60012 1.75351 2.25432 -0.01153 0.62617  0.42004  175 THR A CB  
5770 O OG1 . THR E 167 ? 2.70377 1.84069 2.26738 0.00376  0.65752  0.45692  175 THR A OG1 
5771 C CG2 . THR E 167 ? 2.67866 1.80008 2.27050 -0.06642 0.55960  0.38292  175 THR A CG2 
5772 N N   . SER E 168 ? 2.48155 1.62395 2.16009 0.11207  0.78664  0.45086  176 SER A N   
5773 C CA  . SER E 168 ? 2.38190 1.59580 2.19714 0.15801  0.83759  0.48323  176 SER A CA  
5774 C C   . SER E 168 ? 2.35336 1.54773 2.20108 0.19432  0.85874  0.44463  176 SER A C   
5775 O O   . SER E 168 ? 2.47154 1.56812 2.16839 0.21218  0.88446  0.40880  176 SER A O   
5776 C CB  . SER E 168 ? 2.48472 1.67882 2.21122 0.19175  0.90636  0.52216  176 SER A CB  
5777 O OG  . SER E 168 ? 2.64809 1.72408 2.15473 0.20340  0.92933  0.49138  176 SER A OG  
5778 N N   . GLY E 169 ? 2.28783 1.57090 2.32919 0.20787  0.84447  0.45024  177 GLY A N   
5779 C CA  . GLY E 169 ? 2.26698 1.54092 2.35316 0.25116  0.86316  0.41611  177 GLY A CA  
5780 C C   . GLY E 169 ? 2.28291 1.48654 2.29953 0.23657  0.82543  0.36243  177 GLY A C   
5781 O O   . GLY E 169 ? 2.30951 1.46464 2.29069 0.27629  0.85081  0.32910  177 GLY A O   
5782 N N   . VAL E 170 ? 2.28036 1.47735 2.27764 0.18205  0.76721  0.35421  178 VAL A N   
5783 C CA  . VAL E 170 ? 2.26274 1.40539 2.21809 0.16307  0.73110  0.30900  178 VAL A CA  
5784 C C   . VAL E 170 ? 2.05916 1.29236 2.19965 0.16584  0.68585  0.30955  178 VAL A C   
5785 O O   . VAL E 170 ? 1.96134 1.28708 2.22956 0.14766  0.65287  0.34171  178 VAL A O   
5786 C CB  . VAL E 170 ? 2.36466 1.44624 2.19005 0.10235  0.69499  0.29546  178 VAL A CB  
5787 C CG1 . VAL E 170 ? 2.36417 1.37535 2.13357 0.08595  0.67361  0.24901  178 VAL A CG1 
5788 C CG2 . VAL E 170 ? 2.55510 1.55750 2.20551 0.10216  0.73166  0.29988  178 VAL A CG2 
5789 N N   . HIS E 171 ? 2.27923 1.48009 2.42820 0.19382  0.68476  0.27364  179 HIS A N   
5790 C CA  . HIS E 171 ? 2.06678 1.33738 2.37168 0.21077  0.64473  0.26613  179 HIS A CA  
5791 C C   . HIS E 171 ? 2.05620 1.25828 2.28598 0.19167  0.62032  0.22861  179 HIS A C   
5792 O O   . HIS E 171 ? 2.03507 1.16331 2.19732 0.22688  0.64637  0.19689  179 HIS A O   
5793 C CB  . HIS E 171 ? 1.92152 1.22874 2.32724 0.28001  0.67386  0.26254  179 HIS A CB  
5794 C CG  . HIS E 171 ? 1.97188 1.32548 2.42082 0.29867  0.71596  0.29762  179 HIS A CG  
5795 N ND1 . HIS E 171 ? 1.86355 1.32800 2.48519 0.29728  0.69864  0.33519  179 HIS A ND1 
5796 C CD2 . HIS E 171 ? 2.12040 1.42286 2.46143 0.31993  0.77729  0.30270  179 HIS A CD2 
5797 C CE1 . HIS E 171 ? 1.94607 1.42799 2.56948 0.31475  0.75116  0.36435  179 HIS A CE1 
5798 N NE2 . HIS E 171 ? 2.10429 1.49141 2.55712 0.33096  0.79994  0.34530  179 HIS A NE2 
5799 N N   . THR E 172 ? 2.02392 1.23790 2.24188 0.13253  0.57642  0.23304  180 THR A N   
5800 C CA  . THR E 172 ? 1.98811 1.16663 2.17963 0.10942  0.54722  0.20545  180 THR A CA  
5801 C C   . THR E 172 ? 1.78130 1.03296 2.12566 0.14813  0.51759  0.20288  180 THR A C   
5802 O O   . THR E 172 ? 1.68183 1.03221 2.15842 0.13807  0.47388  0.22509  180 THR A O   
5803 C CB  . THR E 172 ? 2.05551 1.24778 2.21821 0.03786  0.50488  0.21278  180 THR A CB  
5804 O OG1 . THR E 172 ? 2.22986 1.36181 2.25797 0.00936  0.52684  0.21636  180 THR A OG1 
5805 C CG2 . THR E 172 ? 2.04464 1.19138 2.16742 0.00958  0.48500  0.18416  180 THR A CG2 
5806 N N   . PHE E 173 ? 2.04003 1.27928 1.79128 0.06165  0.45828  0.00595  181 PHE A N   
5807 C CA  . PHE E 173 ? 2.11338 1.43765 1.85081 0.05224  0.47471  -0.00097 181 PHE A CA  
5808 C C   . PHE E 173 ? 2.11021 1.41752 1.87418 0.04387  0.48678  0.00186  181 PHE A C   
5809 O O   . PHE E 173 ? 2.06491 1.30865 1.86307 0.05223  0.48381  0.02187  181 PHE A O   
5810 C CB  . PHE E 173 ? 2.21308 1.61233 1.93448 0.07799  0.48082  0.02965  181 PHE A CB  
5811 C CG  . PHE E 173 ? 2.22325 1.66756 1.91513 0.08184  0.47343  0.02102  181 PHE A CG  
5812 C CD1 . PHE E 173 ? 2.21021 1.61414 1.90076 0.10045  0.46126  0.03546  181 PHE A CD1 
5813 C CD2 . PHE E 173 ? 2.20444 1.72964 1.87166 0.06632  0.47805  -0.00359 181 PHE A CD2 
5814 C CE1 . PHE E 173 ? 2.20574 1.65278 1.87133 0.10528  0.45643  0.02922  181 PHE A CE1 
5815 C CE2 . PHE E 173 ? 2.20570 1.77540 1.85219 0.06906  0.47144  -0.01033 181 PHE A CE2 
5816 C CZ  . PHE E 173 ? 2.20845 1.73985 1.85447 0.08894  0.46182  0.00731  181 PHE A CZ  
5817 N N   . PRO E 174 ? 2.10327 1.46521 1.85392 0.02731  0.50006  -0.01922 182 PRO A N   
5818 C CA  . PRO E 174 ? 2.10704 1.46089 1.88041 0.02344  0.51494  -0.01346 182 PRO A CA  
5819 C C   . PRO E 174 ? 2.18027 1.55544 1.96969 0.05191  0.52595  0.03383  182 PRO A C   
5820 O O   . PRO E 174 ? 2.23570 1.64669 2.01248 0.07428  0.52403  0.05994  182 PRO A O   
5821 C CB  . PRO E 174 ? 2.09071 1.51330 1.83525 0.00500  0.52623  -0.04623 182 PRO A CB  
5822 C CG  . PRO E 174 ? 2.04538 1.47407 1.76748 -0.01307 0.51336  -0.08002 182 PRO A CG  
5823 C CD  . PRO E 174 ? 2.08144 1.50256 1.79969 0.00759  0.50058  -0.05533 182 PRO A CD  
5824 N N   . ALA E 175 ? 2.17447 1.52799 1.99430 0.05165  0.53927  0.04647  183 ALA A N   
5825 C CA  . ALA E 175 ? 2.23001 1.60011 2.07205 0.07745  0.55343  0.09388  183 ALA A CA  
5826 C C   . ALA E 175 ? 2.23859 1.70477 2.04772 0.08711  0.57387  0.10007  183 ALA A C   
5827 O O   . ALA E 175 ? 2.19673 1.70601 1.97463 0.07018  0.57818  0.06418  183 ALA A O   
5828 C CB  . ALA E 175 ? 2.16802 1.47327 2.06362 0.07420  0.55983  0.10857  183 ALA A CB  
5829 N N   . VAL E 176 ? 2.26734 1.76665 2.08300 0.11576  0.58603  0.14603  184 VAL A N   
5830 C CA  . VAL E 176 ? 2.25605 1.84313 2.04283 0.13084  0.60750  0.15970  184 VAL A CA  
5831 C C   . VAL E 176 ? 2.25562 1.82767 2.08233 0.14858  0.62966  0.20421  184 VAL A C   
5832 O O   . VAL E 176 ? 2.27357 1.79687 2.14237 0.16266  0.62743  0.24169  184 VAL A O   
5833 C CB  . VAL E 176 ? 2.28121 1.94266 2.02948 0.15291  0.60401  0.17598  184 VAL A CB  
5834 C CG1 . VAL E 176 ? 2.26362 1.95693 1.97262 0.13336  0.58618  0.12953  184 VAL A CG1 
5835 C CG2 . VAL E 176 ? 2.32413 1.94727 2.09961 0.17580  0.59665  0.21836  184 VAL A CG2 
5836 N N   . LEU E 177 ? 2.25304 1.86631 2.06802 0.14822  0.65148  0.19983  185 LEU A N   
5837 C CA  . LEU E 177 ? 2.24379 1.85980 2.09179 0.16886  0.67783  0.24626  185 LEU A CA  
5838 C C   . LEU E 177 ? 2.26550 1.95723 2.08462 0.20227  0.68988  0.28610  185 LEU A C   
5839 O O   . LEU E 177 ? 2.25571 2.02896 2.02523 0.21211  0.70216  0.27854  185 LEU A O   
5840 C CB  . LEU E 177 ? 2.19818 1.83039 2.04133 0.15900  0.69852  0.22724  185 LEU A CB  
5841 C CG  . LEU E 177 ? 2.17459 1.77235 2.07534 0.16932  0.72227  0.26769  185 LEU A CG  
5842 C CD1 . LEU E 177 ? 2.18491 1.69373 2.15327 0.16486  0.70719  0.29034  185 LEU A CD1 
5843 C CD2 . LEU E 177 ? 2.12632 1.71767 2.02866 0.15245  0.73666  0.23763  185 LEU A CD2 
5844 N N   . GLN E 178 ? 2.25054 1.91454 2.09952 0.22081  0.68488  0.32763  186 GLN A N   
5845 C CA  . GLN E 178 ? 2.26676 1.99706 2.09310 0.25512  0.69686  0.37079  186 GLN A CA  
5846 C C   . GLN E 178 ? 2.23818 2.01800 2.06275 0.27545  0.73098  0.40352  186 GLN A C   
5847 O O   . GLN E 178 ? 2.20827 1.94639 2.07754 0.26979  0.74689  0.41589  186 GLN A O   
5848 C CB  . GLN E 178 ? 2.28386 1.96188 2.15407 0.27194  0.68929  0.41366  186 GLN A CB  
5849 C CG  . GLN E 178 ? 2.29294 1.88447 2.18981 0.24940  0.65959  0.38571  186 GLN A CG  
5850 C CD  . GLN E 178 ? 2.27045 1.79387 2.22340 0.26439  0.65431  0.42759  186 GLN A CD  
5851 O OE1 . GLN E 178 ? 2.28420 1.81620 2.22664 0.28418  0.64601  0.44789  186 GLN A OE1 
5852 N NE2 . GLN E 178 ? 2.21648 1.67197 2.23177 0.25534  0.65883  0.44040  186 GLN A NE2 
5853 N N   . SER E 179 ? 2.25411 2.12598 2.02551 0.30011  0.74219  0.41688  187 SER A N   
5854 C CA  . SER E 179 ? 2.22695 2.15630 1.98387 0.32369  0.77550  0.44676  187 SER A CA  
5855 C C   . SER E 179 ? 2.20070 2.08263 2.02531 0.33956  0.80013  0.50564  187 SER A C   
5856 O O   . SER E 179 ? 2.17350 2.07718 2.00388 0.35047  0.82977  0.52530  187 SER A O   
5857 C CB  . SER E 179 ? 2.23980 2.26921 1.93580 0.35520  0.78114  0.46484  187 SER A CB  
5858 O OG  . SER E 179 ? 2.24356 2.27144 1.96472 0.38610  0.78965  0.52607  187 SER A OG  
5859 N N   . SER E 180 ? 2.28076 2.09795 2.15849 0.34155  0.78871  0.53416  188 SER A N   
5860 C CA  . SER E 180 ? 2.24197 2.00267 2.19630 0.35026  0.80784  0.58493  188 SER A CA  
5861 C C   . SER E 180 ? 2.20848 1.91818 2.20425 0.32425  0.81420  0.56316  188 SER A C   
5862 O O   . SER E 180 ? 2.16259 1.86054 2.20722 0.33467  0.84192  0.60350  188 SER A O   
5863 C CB  . SER E 180 ? 2.24805 1.93725 2.25159 0.35050  0.78661  0.60497  188 SER A CB  
5864 O OG  . SER E 180 ? 2.26739 1.89209 2.27850 0.31789  0.75321  0.55334  188 SER A OG  
5865 N N   . GLY E 181 ? 2.21262 1.89285 2.19213 0.29147  0.79038  0.50205  189 GLY A N   
5866 C CA  . GLY E 181 ? 2.17830 1.80403 2.19865 0.26597  0.79264  0.47880  189 GLY A CA  
5867 C C   . GLY E 181 ? 2.17732 1.70580 2.25173 0.24083  0.76311  0.46076  189 GLY A C   
5868 O O   . GLY E 181 ? 2.14464 1.62168 2.26206 0.22071  0.76323  0.44573  189 GLY A O   
5869 N N   . LEU E 182 ? 2.20687 1.70925 2.27959 0.24335  0.73794  0.46224  190 LEU A N   
5870 C CA  . LEU E 182 ? 2.19318 1.60550 2.30597 0.22254  0.70669  0.44143  190 LEU A CA  
5871 C C   . LEU E 182 ? 2.23610 1.65264 2.29136 0.20362  0.67930  0.38480  190 LEU A C   
5872 O O   . LEU E 182 ? 2.27853 1.76564 2.27133 0.21200  0.68056  0.37320  190 LEU A O   
5873 C CB  . LEU E 182 ? 2.16256 1.53481 2.31907 0.24142  0.69886  0.48588  190 LEU A CB  
5874 C CG  . LEU E 182 ? 2.09346 1.42930 2.33226 0.25063  0.71863  0.53674  190 LEU A CG  
5875 C CD1 . LEU E 182 ? 2.07215 1.39491 2.34241 0.27676  0.72022  0.58871  190 LEU A CD1 
5876 C CD2 . LEU E 182 ? 2.03761 1.28694 2.33918 0.22392  0.70103  0.51552  190 LEU A CD2 
5877 N N   . TYR E 183 ? 2.20588 1.54857 2.28388 0.17853  0.65478  0.35035  191 TYR A N   
5878 C CA  . TYR E 183 ? 2.23248 1.57174 2.26246 0.16003  0.63008  0.29911  191 TYR A CA  
5879 C C   . TYR E 183 ? 2.22552 1.54425 2.24718 0.17242  0.60804  0.30853  191 TYR A C   
5880 O O   . TYR E 183 ? 2.17325 1.45100 2.23833 0.18825  0.60492  0.34579  191 TYR A O   
5881 C CB  . TYR E 183 ? 2.16747 1.43625 2.22184 0.13043  0.61429  0.25958  191 TYR A CB  
5882 C CG  . TYR E 183 ? 2.18545 1.47521 2.23419 0.11415  0.63217  0.23545  191 TYR A CG  
5883 C CD1 . TYR E 183 ? 2.23027 1.57295 2.21933 0.10173  0.63456  0.19431  191 TYR A CD1 
5884 C CD2 . TYR E 183 ? 2.13162 1.38594 2.23808 0.11089  0.64600  0.25271  191 TYR A CD2 
5885 C CE1 . TYR E 183 ? 2.19757 1.55497 2.18076 0.08785  0.65067  0.17014  191 TYR A CE1 
5886 C CE2 . TYR E 183 ? 2.14310 1.41466 2.24432 0.09805  0.66347  0.23076  191 TYR A CE2 
5887 C CZ  . TYR E 183 ? 2.16691 1.48836 2.20456 0.08707  0.66577  0.18881  191 TYR A CZ  
5888 O OH  . TYR E 183 ? 2.12452 1.45963 2.15596 0.07545  0.68313  0.16524  191 TYR A OH  
5889 N N   . SER E 184 ? 2.20269 1.55081 2.16970 0.16566  0.59336  0.27463  192 SER A N   
5890 C CA  . SER E 184 ? 2.19517 1.52661 2.14951 0.17805  0.57326  0.28024  192 SER A CA  
5891 C C   . SER E 184 ? 2.20808 1.53947 2.11949 0.15837  0.55326  0.23046  192 SER A C   
5892 O O   . SER E 184 ? 2.26604 1.65357 2.13891 0.14439  0.55959  0.20035  192 SER A O   
5893 C CB  . SER E 184 ? 2.25958 1.66387 2.18907 0.20864  0.58652  0.31812  192 SER A CB  
5894 O OG  . SER E 184 ? 2.23724 1.61128 2.16970 0.22527  0.56982  0.33380  192 SER A OG  
5895 N N   . LEU E 185 ? 2.30407 1.57327 2.22228 0.15853  0.52968  0.22249  193 LEU A N   
5896 C CA  . LEU E 185 ? 2.29895 1.56434 2.17946 0.14221  0.51229  0.17984  193 LEU A CA  
5897 C C   . LEU E 185 ? 2.27772 1.51709 2.14853 0.16063  0.49448  0.19009  193 LEU A C   
5898 O O   . LEU E 185 ? 2.25563 1.46603 2.15308 0.18350  0.49271  0.22623  193 LEU A O   
5899 C CB  . LEU E 185 ? 2.21058 1.40740 2.10866 0.11453  0.50107  0.14390  193 LEU A CB  
5900 C CG  . LEU E 185 ? 2.11849 1.21656 2.06432 0.11703  0.48408  0.15380  193 LEU A CG  
5901 C CD1 . LEU E 185 ? 2.08161 1.12886 2.00841 0.11812  0.45863  0.13378  193 LEU A CD1 
5902 C CD2 . LEU E 185 ? 2.06466 1.11913 2.04597 0.09554  0.48644  0.13819  193 LEU A CD2 
5903 N N   . SER E 186 ? 2.20641 1.45160 2.04126 0.15008  0.48165  0.15708  194 SER A N   
5904 C CA  . SER E 186 ? 2.19893 1.42960 2.01529 0.16771  0.46667  0.16196  194 SER A CA  
5905 C C   . SER E 186 ? 2.14994 1.34729 1.94445 0.14811  0.45126  0.12026  194 SER A C   
5906 O O   . SER E 186 ? 2.17775 1.42401 1.94625 0.12804  0.45651  0.09136  194 SER A O   
5907 C CB  . SER E 186 ? 2.30480 1.62807 2.08851 0.18696  0.47673  0.18024  194 SER A CB  
5908 O OG  . SER E 186 ? 2.37921 1.78289 2.13706 0.17032  0.48902  0.15993  194 SER A OG  
5909 N N   . SER E 187 ? 2.37881 1.49295 2.18398 0.15444  0.43241  0.11697  195 SER A N   
5910 C CA  . SER E 187 ? 2.33419 1.41105 2.11699 0.14070  0.41836  0.08182  195 SER A CA  
5911 C C   . SER E 187 ? 2.35350 1.42776 2.10901 0.16391  0.40819  0.08859  195 SER A C   
5912 O O   . SER E 187 ? 2.35834 1.39322 2.12643 0.18945  0.39985  0.11366  195 SER A O   
5913 C CB  . SER E 187 ? 2.27410 1.25475 2.08512 0.12978  0.40342  0.06757  195 SER A CB  
5914 O OG  . SER E 187 ? 2.24605 1.18355 2.03233 0.12552  0.38847  0.04085  195 SER A OG  
5915 N N   . VAL E 188 ? 2.35355 1.46591 2.07429 0.15540  0.40894  0.06603  196 VAL A N   
5916 C CA  . VAL E 188 ? 2.37489 1.49183 2.06879 0.17841  0.40208  0.07290  196 VAL A CA  
5917 C C   . VAL E 188 ? 2.32766 1.39897 2.00141 0.16728  0.39180  0.04207  196 VAL A C   
5918 O O   . VAL E 188 ? 2.28146 1.33293 1.95951 0.14014  0.39204  0.01530  196 VAL A O   
5919 C CB  . VAL E 188 ? 2.44899 1.67113 2.12028 0.18596  0.41507  0.08347  196 VAL A CB  
5920 C CG1 . VAL E 188 ? 2.51003 1.77109 2.19575 0.20768  0.42412  0.12146  196 VAL A CG1 
5921 C CG2 . VAL E 188 ? 2.46183 1.74846 2.12268 0.15421  0.42502  0.05469  196 VAL A CG2 
5922 N N   . VAL E 189 ? 2.50275 1.55333 2.15426 0.19111  0.38346  0.04779  197 VAL A N   
5923 C CA  . VAL E 189 ? 2.46978 1.48221 2.09713 0.18608  0.37619  0.02293  197 VAL A CA  
5924 C C   . VAL E 189 ? 2.50466 1.55058 2.10166 0.21023  0.37821  0.03225  197 VAL A C   
5925 O O   . VAL E 189 ? 2.53434 1.56098 2.12686 0.24247  0.37218  0.05518  197 VAL A O   
5926 C CB  . VAL E 189 ? 2.43952 1.34184 2.07495 0.19162  0.35694  0.01419  197 VAL A CB  
5927 C CG1 . VAL E 189 ? 2.47310 1.32806 2.12014 0.22365  0.34450  0.03989  197 VAL A CG1 
5928 C CG2 . VAL E 189 ? 2.42067 1.28501 2.02403 0.19379  0.35037  -0.00706 197 VAL A CG2 
5929 N N   . THR E 190 ? 2.53113 1.62800 2.10999 0.19479  0.38753  0.01494  198 THR A N   
5930 C CA  . THR E 190 ? 2.55997 1.68776 2.11257 0.21661  0.39072  0.02275  198 THR A CA  
5931 C C   . THR E 190 ? 2.53399 1.57002 2.06617 0.23528  0.37804  0.01583  198 THR A C   
5932 O O   . THR E 190 ? 2.49052 1.48373 2.01652 0.21772  0.37540  -0.00761 198 THR A O   
5933 C CB  . THR E 190 ? 2.55609 1.76559 2.10241 0.19254  0.40443  0.00645  198 THR A CB  
5934 O OG1 . THR E 190 ? 2.49394 1.66132 2.03845 0.16663  0.40412  -0.02212 198 THR A OG1 
5935 C CG2 . THR E 190 ? 2.58383 1.87927 2.14789 0.17270  0.41382  0.00771  198 THR A CG2 
5936 N N   . VAL E 191 ? 2.70443 1.70945 2.22492 0.27242  0.37013  0.03625  199 VAL A N   
5937 C CA  . VAL E 191 ? 2.69765 1.61101 2.19574 0.29759  0.35505  0.03159  199 VAL A CA  
5938 C C   . VAL E 191 ? 2.71815 1.66237 2.18456 0.32708  0.36226  0.04260  199 VAL A C   
5939 O O   . VAL E 191 ? 2.74162 1.76627 2.21131 0.33537  0.37425  0.06149  199 VAL A O   
5940 C CB  . VAL E 191 ? 2.71187 1.55204 2.22687 0.31739  0.33735  0.04438  199 VAL A CB  
5941 C CG1 . VAL E 191 ? 2.69116 1.50189 2.24171 0.28813  0.33150  0.03456  199 VAL A CG1 
5942 C CG2 . VAL E 191 ? 2.73970 1.62584 2.26342 0.34188  0.34322  0.07598  199 VAL A CG2 
5943 N N   . PRO E 192 ? 2.89376 1.78235 2.32852 0.34383  0.35675  0.03173  200 PRO A N   
5944 C CA  . PRO E 192 ? 2.91058 1.82916 2.31535 0.37479  0.36580  0.04410  200 PRO A CA  
5945 C C   . PRO E 192 ? 2.93618 1.85038 2.34055 0.41178  0.36033  0.07008  200 PRO A C   
5946 O O   . PRO E 192 ? 2.94552 1.78731 2.35792 0.42529  0.34303  0.07317  200 PRO A O   
5947 C CB  . PRO E 192 ? 2.91232 1.75113 2.28165 0.38917  0.35791  0.02725  200 PRO A CB  
5948 C CG  . PRO E 192 ? 2.88931 1.68478 2.27349 0.35441  0.35035  0.00346  200 PRO A CG  
5949 C CD  . PRO E 192 ? 2.88315 1.68014 2.30629 0.33845  0.34235  0.00911  200 PRO A CD  
5950 N N   . SER E 193 ? 3.50142 2.05554 1.87697 0.53376  0.76715  -0.19866 201 SER A N   
5951 C CA  . SER E 193 ? 3.51105 1.93213 1.78527 0.54044  0.69181  -0.35138 201 SER A CA  
5952 C C   . SER E 193 ? 3.68909 2.19196 1.76914 0.57828  0.66123  -0.41667 201 SER A C   
5953 O O   . SER E 193 ? 3.77813 2.18685 1.73155 0.56499  0.56194  -0.51896 201 SER A O   
5954 C CB  . SER E 193 ? 3.44421 1.78210 1.81433 0.57626  0.73358  -0.41766 201 SER A CB  
5955 O OG  . SER E 193 ? 3.27738 1.57019 1.83518 0.55384  0.78101  -0.33525 201 SER A OG  
5956 N N   . SER E 194 ? 3.72401 2.40057 1.77679 0.62620  0.74230  -0.35923 202 SER A N   
5957 C CA  . SER E 194 ? 3.89780 2.67028 1.76335 0.66463  0.71937  -0.40758 202 SER A CA  
5958 C C   . SER E 194 ? 3.95861 2.71027 1.70831 0.61905  0.62672  -0.39551 202 SER A C   
5959 O O   . SER E 194 ? 4.10342 2.83342 1.68743 0.63691  0.55212  -0.48734 202 SER A O   
5960 C CB  . SER E 194 ? 3.92625 2.90154 1.79544 0.70831  0.82640  -0.31608 202 SER A CB  
5961 O OG  . SER E 194 ? 3.85724 2.91613 1.78168 0.66870  0.85278  -0.17082 202 SER A OG  
5962 N N   . SER E 195 ? 3.85221 2.61275 1.68823 0.56249  0.62694  -0.28341 203 SER A N   
5963 C CA  . SER E 195 ? 3.90113 2.64501 1.64088 0.51540  0.53983  -0.26701 203 SER A CA  
5964 C C   . SER E 195 ? 3.94167 2.51214 1.61369 0.48222  0.42260  -0.38448 203 SER A C   
5965 O O   . SER E 195 ? 4.05830 2.61054 1.58311 0.47052  0.33540  -0.42699 203 SER A O   
5966 C CB  . SER E 195 ? 3.76679 2.54976 1.63188 0.46199  0.56176  -0.13230 203 SER A CB  
5967 O OG  . SER E 195 ? 3.64667 2.30116 1.64398 0.41577  0.53821  -0.13822 203 SER A OG  
5968 N N   . LEU E 196 ? 3.97313 2.41039 1.75003 0.46497  0.41458  -0.43557 204 LEU A N   
5969 C CA  . LEU E 196 ? 3.91409 2.17459 1.63272 0.43364  0.30371  -0.55493 204 LEU A CA  
5970 C C   . LEU E 196 ? 3.98960 2.21057 1.61555 0.37195  0.19715  -0.54754 204 LEU A C   
5971 O O   . LEU E 196 ? 3.96093 2.17489 1.67533 0.31066  0.19069  -0.46581 204 LEU A O   
5972 C CB  . LEU E 196 ? 4.03432 2.26511 1.62994 0.49756  0.27561  -0.69020 204 LEU A CB  
5973 N N   . GLY E 197 ? 4.10170 2.29855 1.55090 0.38953  0.10992  -0.63429 205 GLY A N   
5974 C CA  . GLY E 197 ? 4.16837 2.34648 1.51404 0.33942  0.00963  -0.62238 205 GLY A CA  
5975 C C   . GLY E 197 ? 4.28530 2.60435 1.50496 0.37948  0.02179  -0.58256 205 GLY A C   
5976 O O   . GLY E 197 ? 4.36845 2.67312 1.47825 0.34914  -0.06808 -0.58331 205 GLY A O   
5977 N N   . THR E 198 ? 4.30059 2.75400 1.52879 0.44566  0.12734  -0.54798 206 THR A N   
5978 C CA  . THR E 198 ? 4.41042 3.00536 1.52184 0.48287  0.14836  -0.50101 206 THR A CA  
5979 C C   . THR E 198 ? 4.33205 3.00642 1.50430 0.43239  0.16996  -0.36442 206 THR A C   
5980 O O   . THR E 198 ? 4.42481 3.14176 1.48303 0.42427  0.11969  -0.33924 206 THR A O   
5981 C CB  . THR E 198 ? 4.44313 3.16487 1.55643 0.56093  0.25918  -0.49763 206 THR A CB  
5982 O OG1 . THR E 198 ? 4.30423 3.12497 1.57426 0.54872  0.37000  -0.36996 206 THR A OG1 
5983 C CG2 . THR E 198 ? 4.45925 3.09716 1.58480 0.60270  0.25914  -0.62052 206 THR A CG2 
5984 N N   . GLN E 199 ? 4.16443 2.85723 1.51629 0.40103  0.24020  -0.27755 207 GLN A N   
5985 C CA  . GLN E 199 ? 4.07395 2.82698 1.50406 0.34942  0.24997  -0.15678 207 GLN A CA  
5986 C C   . GLN E 199 ? 4.01059 2.64118 1.47967 0.27373  0.15851  -0.17558 207 GLN A C   
5987 O O   . GLN E 199 ? 3.92939 2.44957 1.48455 0.25141  0.14769  -0.22300 207 GLN A O   
5988 C CB  . GLN E 199 ? 3.92831 2.76477 1.53380 0.35670  0.36330  -0.05356 207 GLN A CB  
5989 N N   . THR E 200 ? 4.05028 2.70181 1.45605 0.23266  0.09255  -0.13743 208 THR A N   
5990 C CA  . THR E 200 ? 3.99294 2.54871 1.43596 0.15535  0.00688  -0.14577 208 THR A CA  
5991 C C   . THR E 200 ? 3.81103 2.38625 1.45219 0.11611  0.06465  -0.06130 208 THR A C   
5992 O O   . THR E 200 ? 3.75807 2.44408 1.49029 0.13836  0.15133  0.03132  208 THR A O   
5993 C CB  . THR E 200 ? 4.08411 2.67080 1.41455 0.12382  -0.07454 -0.12039 208 THR A CB  
5994 O OG1 . THR E 200 ? 4.07095 2.80117 1.42242 0.14254  -0.00992 -0.01539 208 THR A OG1 
5995 C CG2 . THR E 200 ? 4.27253 2.80981 1.40485 0.15950  -0.15315 -0.21767 208 THR A CG2 
5996 N N   . TYR E 201 ? 3.84796 2.31297 1.55242 0.05645  0.00984  -0.09413 209 TYR A N   
5997 C CA  . TYR E 201 ? 3.78168 2.24497 1.67262 0.02132  0.05631  -0.03186 209 TYR A CA  
5998 C C   . TYR E 201 ? 3.77558 2.17986 1.68671 -0.06289 -0.03057 -0.03332 209 TYR A C   
5999 O O   . TYR E 201 ? 3.67510 1.94980 1.54607 -0.09916 -0.10262 -0.11624 209 TYR A O   
6000 C CB  . TYR E 201 ? 3.66005 2.03810 1.63846 0.04815  0.10759  -0.08055 209 TYR A CB  
6001 C CG  . TYR E 201 ? 3.64422 2.10682 1.65486 0.12423  0.21271  -0.05052 209 TYR A CG  
6002 C CD1 . TYR E 201 ? 3.61220 2.21525 1.69582 0.14355  0.28601  0.06321  209 TYR A CD1 
6003 C CD2 . TYR E 201 ? 3.60481 2.00929 1.57465 0.17465  0.23473  -0.13581 209 TYR A CD2 
6004 C CE1 . TYR E 201 ? 3.53906 2.22410 1.65139 0.20641  0.37872  0.09727  209 TYR A CE1 
6005 C CE2 . TYR E 201 ? 3.59641 2.08963 1.59887 0.24085  0.33254  -0.10572 209 TYR A CE2 
6006 C CZ  . TYR E 201 ? 3.57181 2.20608 1.64460 0.25410  0.40458  0.01415  209 TYR A CZ  
6007 O OH  . TYR E 201 ? 3.51745 2.24480 1.62230 0.31362  0.49894  0.05094  209 TYR A OH  
6008 N N   . ILE E 202 ? 3.62144 2.12198 1.59486 -0.09577 -0.02724 0.05676  210 ILE A N   
6009 C CA  . ILE E 202 ? 3.59283 2.06649 1.59474 -0.17669 -0.10266 0.06589  210 ILE A CA  
6010 C C   . ILE E 202 ? 3.46294 2.01979 1.64474 -0.19444 -0.04447 0.15962  210 ILE A C   
6011 O O   . ILE E 202 ? 3.39113 2.06924 1.61631 -0.16224 0.01000  0.24054  210 ILE A O   
6012 C CB  . ILE E 202 ? 3.64990 2.16354 1.51536 -0.20237 -0.18521 0.07008  210 ILE A CB  
6013 C CG1 . ILE E 202 ? 3.69995 2.12708 1.38262 -0.17782 -0.25159 -0.02664 210 ILE A CG1 
6014 C CG2 . ILE E 202 ? 3.60106 2.10222 1.50613 -0.28968 -0.26007 0.08581  210 ILE A CG2 
6015 C CD1 . ILE E 202 ? 3.80985 2.31710 1.38728 -0.10340 -0.21291 -0.01569 210 ILE A CD1 
6016 N N   . CYS E 203 ? 3.55619 2.04769 1.83917 -0.24571 -0.06149 0.14784  211 CYS A N   
6017 C CA  . CYS E 203 ? 3.31323 1.88071 1.76593 -0.26352 -0.01827 0.22838  211 CYS A CA  
6018 C C   . CYS E 203 ? 3.36950 1.99478 1.81943 -0.33284 -0.08792 0.25755  211 CYS A C   
6019 O O   . CYS E 203 ? 3.46052 2.01220 1.83356 -0.39339 -0.17233 0.20264  211 CYS A O   
6020 C CB  . CYS E 203 ? 2.97938 1.45287 1.55577 -0.27277 0.01269  0.20453  211 CYS A CB  
6021 S SG  . CYS E 203 ? 2.85380 1.20501 1.42004 -0.36768 -0.07951 0.13799  211 CYS A SG  
6022 N N   . ASN E 204 ? 3.21917 1.97889 1.75314 -0.32225 -0.05455 0.34491  212 ASN A N   
6023 C CA  . ASN E 204 ? 3.25984 2.10052 1.80183 -0.38083 -0.11411 0.38039  212 ASN A CA  
6024 C C   . ASN E 204 ? 2.98308 1.86249 1.69679 -0.41436 -0.09649 0.41741  212 ASN A C   
6025 O O   . ASN E 204 ? 2.74954 1.71398 1.58665 -0.37382 -0.03380 0.48381  212 ASN A O   
6026 C CB  . ASN E 204 ? 3.29278 2.25720 1.79957 -0.34816 -0.10276 0.44528  212 ASN A CB  
6027 C CG  . ASN E 204 ? 3.36696 2.32334 1.77997 -0.27741 -0.05777 0.43888  212 ASN A CG  
6028 O OD1 . ASN E 204 ? 3.21129 2.22901 1.69904 -0.22471 0.01728  0.49387  212 ASN A OD1 
6029 N ND2 . ASN E 204 ? 3.56632 2.45059 1.81513 -0.27560 -0.10633 0.37221  212 ASN A ND2 
6030 N N   . VAL E 205 ? 3.27341 2.09280 1.99233 -0.48498 -0.15297 0.37601  213 VAL A N   
6031 C CA  . VAL E 205 ? 2.95045 1.80903 1.81862 -0.52370 -0.14467 0.40303  213 VAL A CA  
6032 C C   . VAL E 205 ? 3.05769 2.03201 1.93249 -0.58000 -0.20104 0.43772  213 VAL A C   
6033 O O   . VAL E 205 ? 3.32125 2.27932 2.07276 -0.62736 -0.27657 0.40947  213 VAL A O   
6034 C CB  . VAL E 205 ? 2.71127 1.43121 1.58364 -0.57058 -0.16924 0.33617  213 VAL A CB  
6035 C CG1 . VAL E 205 ? 2.40644 1.15418 1.45039 -0.58198 -0.13042 0.36584  213 VAL A CG1 
6036 C CG2 . VAL E 205 ? 2.72528 1.30990 1.52902 -0.52360 -0.14327 0.27797  213 VAL A CG2 
6037 N N   . ASN E 206 ? 2.94915 2.03744 1.97291 -0.57566 -0.16938 0.49585  214 ASN A N   
6038 C CA  . ASN E 206 ? 2.99327 2.20724 2.05602 -0.62607 -0.21498 0.52936  214 ASN A CA  
6039 C C   . ASN E 206 ? 2.62802 1.88747 1.84765 -0.65341 -0.19803 0.54260  214 ASN A C   
6040 O O   . ASN E 206 ? 2.36837 1.62732 1.70640 -0.60196 -0.13379 0.56515  214 ASN A O   
6041 C CB  . ASN E 206 ? 3.06668 2.41177 2.14962 -0.58068 -0.19897 0.59428  214 ASN A CB  
6042 C CG  . ASN E 206 ? 3.03554 2.52233 2.19994 -0.62348 -0.23550 0.63056  214 ASN A CG  
6043 O OD1 . ASN E 206 ? 3.24209 2.76147 2.32583 -0.67597 -0.30212 0.62196  214 ASN A OD1 
6044 N ND2 . ASN E 206 ? 2.76139 2.33521 2.08977 -0.59873 -0.19494 0.67032  214 ASN A ND2 
6045 N N   . HIS E 207 ? 3.04018 2.34018 2.25803 -0.73505 -0.25863 0.52901  215 HIS A N   
6046 C CA  . HIS E 207 ? 2.73951 2.10438 2.09575 -0.77095 -0.25140 0.53942  215 HIS A CA  
6047 C C   . HIS E 207 ? 2.84775 2.37743 2.23196 -0.81007 -0.29526 0.57472  215 HIS A C   
6048 O O   . HIS E 207 ? 2.87880 2.42173 2.20041 -0.89149 -0.36232 0.55400  215 HIS A O   
6049 C CB  . HIS E 207 ? 2.56331 1.80896 1.88641 -0.84168 -0.28330 0.48210  215 HIS A CB  
6050 C CG  . HIS E 207 ? 2.27888 1.58937 1.75981 -0.83300 -0.25204 0.47311  215 HIS A CG  
6051 N ND1 . HIS E 207 ? 2.16783 1.44840 1.66094 -0.83424 -0.26598 0.39908  215 HIS A ND1 
6052 C CD2 . HIS E 207 ? 2.15562 1.58462 1.79422 -0.78226 -0.20250 0.51185  215 HIS A CD2 
6053 C CE1 . HIS E 207 ? 2.01711 1.38752 1.65838 -0.79015 -0.22277 0.39508  215 HIS A CE1 
6054 N NE2 . HIS E 207 ? 1.96756 1.42270 1.69881 -0.76125 -0.18694 0.45871  215 HIS A NE2 
6055 N N   . LYS E 208 ? 1.86078 2.51127 2.49457 -0.31859 0.17352  -0.01709 216 LYS A N   
6056 C CA  . LYS E 208 ? 1.73191 2.57294 2.34249 -0.31432 0.20581  -0.02730 216 LYS A CA  
6057 C C   . LYS E 208 ? 1.70503 2.41442 2.29223 -0.39375 0.22667  0.04315  216 LYS A C   
6058 O O   . LYS E 208 ? 1.67166 2.50608 2.30893 -0.43120 0.23835  -0.00883 216 LYS A O   
6059 C CB  . LYS E 208 ? 1.55421 2.53915 2.03652 -0.21358 0.24708  0.03327  216 LYS A CB  
6060 N N   . PRO E 209 ? 1.86448 2.33283 2.37767 -0.41947 0.23286  0.15786  217 PRO A N   
6061 C CA  . PRO E 209 ? 1.79902 2.11650 2.30249 -0.49622 0.24963  0.21757  217 PRO A CA  
6062 C C   . PRO E 209 ? 1.88841 2.14447 2.52940 -0.57683 0.23439  0.12236  217 PRO A C   
6063 O O   . PRO E 209 ? 1.83893 2.08865 2.50081 -0.63347 0.25799  0.12521  217 PRO A O   
6064 C CB  . PRO E 209 ? 1.72359 1.79003 2.13658 -0.49841 0.24804  0.33764  217 PRO A CB  
6065 C CG  . PRO E 209 ? 1.67475 1.82742 2.00008 -0.41857 0.25812  0.37311  217 PRO A CG  
6066 C CD  . PRO E 209 ? 1.80060 2.16274 2.20787 -0.36929 0.23900  0.25201  217 PRO A CD  
6067 N N   . SER E 210 ? 1.76195 1.96289 2.49360 -0.58514 0.20380  0.03926  218 SER A N   
6068 C CA  . SER E 210 ? 1.79739 1.93556 2.65487 -0.66192 0.20499  -0.06087 218 SER A CA  
6069 C C   . SER E 210 ? 1.83812 2.21296 2.80736 -0.66146 0.19308  -0.21578 218 SER A C   
6070 O O   . SER E 210 ? 1.84530 2.17887 2.92449 -0.72897 0.20063  -0.31644 218 SER A O   
6071 C CB  . SER E 210 ? 1.83199 1.70381 2.70581 -0.67900 0.19229  -0.04279 218 SER A CB  
6072 O OG  . SER E 210 ? 1.90890 1.82112 2.79117 -0.62052 0.15866  -0.07605 218 SER A OG  
6073 N N   . ASN E 211 ? 1.66854 2.28297 2.60771 -0.58420 0.18071  -0.23924 219 ASN A N   
6074 C CA  . ASN E 211 ? 1.63511 2.49680 2.67092 -0.56860 0.16535  -0.38642 219 ASN A CA  
6075 C C   . ASN E 211 ? 1.70012 2.45648 2.82588 -0.58907 0.14068  -0.47303 219 ASN A C   
6076 O O   . ASN E 211 ? 1.67482 2.53798 2.91258 -0.63032 0.13836  -0.60944 219 ASN A O   
6077 C CB  . ASN E 211 ? 1.56348 2.59785 2.67860 -0.63159 0.18664  -0.47478 219 ASN A CB  
6078 C CG  . ASN E 211 ? 1.44323 2.83192 2.56449 -0.56352 0.18124  -0.55174 219 ASN A CG  
6079 O OD1 . ASN E 211 ? 1.41505 2.93092 2.56179 -0.50219 0.15561  -0.62393 219 ASN A OD1 
6080 N ND2 . ASN E 211 ? 1.36622 2.91879 2.46081 -0.56779 0.20729  -0.53600 219 ASN A ND2 
6081 N N   . THR E 212 ? 1.86341 2.41675 2.93707 -0.55885 0.12490  -0.39600 220 THR A N   
6082 C CA  . THR E 212 ? 1.91287 2.34997 3.05252 -0.56723 0.10544  -0.45973 220 THR A CA  
6083 C C   . THR E 212 ? 1.93019 2.48814 3.05017 -0.47324 0.07306  -0.47729 220 THR A C   
6084 O O   . THR E 212 ? 1.94230 2.53710 2.96772 -0.40165 0.06939  -0.38957 220 THR A O   
6085 C CB  . THR E 212 ? 1.95671 2.08246 3.05982 -0.59482 0.11160  -0.37108 220 THR A CB  
6086 O OG1 . THR E 212 ? 1.91165 1.92064 3.00120 -0.66169 0.14601  -0.32206 220 THR A OG1 
6087 C CG2 . THR E 212 ? 1.98626 1.98626 3.16797 -0.62277 0.11092  -0.45348 220 THR A CG2 
6088 N N   . LYS E 213 ? 1.81957 2.42728 3.02701 -0.47523 0.05660  -0.59206 221 LYS A N   
6089 C CA  . LYS E 213 ? 1.80604 2.53559 3.01059 -0.38686 0.02695  -0.62721 221 LYS A CA  
6090 C C   . LYS E 213 ? 1.86572 2.42503 3.11809 -0.39893 0.01122  -0.66314 221 LYS A C   
6091 O O   . LYS E 213 ? 1.85466 2.39016 3.19461 -0.46332 0.02222  -0.76537 221 LYS A O   
6092 C CB  . LYS E 213 ? 1.68323 2.70899 2.94729 -0.36456 0.02302  -0.75048 221 LYS A CB  
6093 C CG  . LYS E 213 ? 1.60871 2.82762 2.81863 -0.24478 0.00927  -0.74467 221 LYS A CG  
6094 C CD  . LYS E 213 ? 1.59516 2.82920 2.68374 -0.19595 0.03428  -0.61788 221 LYS A CD  
6095 C CE  . LYS E 213 ? 1.46777 2.91273 2.49399 -0.07261 0.04169  -0.61937 221 LYS A CE  
6096 N NZ  . LYS E 213 ? 1.32087 3.05480 2.37835 -0.05085 0.05096  -0.71295 221 LYS A NZ  
6097 N N   . VAL E 214 ? 1.82358 2.26621 3.01692 -0.33877 -0.00828 -0.58213 222 VAL A N   
6098 C CA  . VAL E 214 ? 1.87405 2.14613 3.09570 -0.33870 -0.02143 -0.59710 222 VAL A CA  
6099 C C   . VAL E 214 ? 1.88202 2.22010 3.07738 -0.24076 -0.05293 -0.58376 222 VAL A C   
6100 O O   . VAL E 214 ? 1.90113 2.22863 3.02035 -0.18697 -0.05891 -0.48920 222 VAL A O   
6101 C CB  . VAL E 214 ? 1.92761 1.93346 3.10407 -0.37462 -0.00825 -0.49973 222 VAL A CB  
6102 C CG1 . VAL E 214 ? 1.94188 1.83829 3.16724 -0.47082 0.03148  -0.54341 222 VAL A CG1 
6103 C CG2 . VAL E 214 ? 1.92798 1.92203 3.01094 -0.35088 -0.00804 -0.37776 222 VAL A CG2 
6104 N N   . ASP E 215 ? 1.87545 2.27563 3.13312 -0.21975 -0.06801 -0.68015 223 ASP A N   
6105 C CA  . ASP E 215 ? 1.87390 2.32920 3.11548 -0.12479 -0.09565 -0.67629 223 ASP A CA  
6106 C C   . ASP E 215 ? 1.93632 2.21099 3.20313 -0.12846 -0.10715 -0.68529 223 ASP A C   
6107 O O   . ASP E 215 ? 1.93191 2.22179 3.26272 -0.14747 -0.10691 -0.78391 223 ASP A O   
6108 C CB  . ASP E 215 ? 1.78485 2.49058 3.06281 -0.07415 -0.10348 -0.77431 223 ASP A CB  
6109 C CG  . ASP E 215 ? 1.71140 2.59334 2.92791 -0.02292 -0.08894 -0.73374 223 ASP A CG  
6110 O OD1 . ASP E 215 ? 1.72204 2.57475 2.90134 -0.07127 -0.06697 -0.67526 223 ASP A OD1 
6111 O OD2 . ASP E 215 ? 1.63331 2.67483 2.83094 0.07134  -0.09329 -0.75684 223 ASP A OD2 
6112 N N   . LYS E 216 ? 1.99466 2.10542 3.20636 -0.10730 -0.11441 -0.58329 224 LYS A N   
6113 C CA  . LYS E 216 ? 2.03595 1.95924 3.25445 -0.10793 -0.11850 -0.57300 224 LYS A CA  
6114 C C   . LYS E 216 ? 2.03918 1.99326 3.25311 -0.01952 -0.14905 -0.56800 224 LYS A C   
6115 O O   . LYS E 216 ? 2.01854 2.05837 3.19514 0.04407  -0.16423 -0.51791 224 LYS A O   
6116 C CB  . LYS E 216 ? 2.05250 1.78196 3.21317 -0.13176 -0.10825 -0.46772 224 LYS A CB  
6117 N N   . LYS E 217 ? 2.09474 1.96597 3.34312 -0.01709 -0.15003 -0.61919 225 LYS A N   
6118 C CA  . LYS E 217 ? 2.09136 1.97213 3.34023 0.06411  -0.17699 -0.61853 225 LYS A CA  
6119 C C   . LYS E 217 ? 2.10033 1.81034 3.30089 0.09254  -0.18515 -0.52285 225 LYS A C   
6120 O O   . LYS E 217 ? 2.13130 1.67074 3.31452 0.04983  -0.16267 -0.49783 225 LYS A O   
6121 C CB  . LYS E 217 ? 2.10026 1.98617 3.40524 0.05508  -0.17158 -0.72467 225 LYS A CB  
6122 N N   . VAL E 218 ? 2.18022 1.94134 3.35787 0.16929  -0.21207 -0.47308 226 VAL A N   
6123 C CA  . VAL E 218 ? 2.14602 1.78930 3.28415 0.20739  -0.22616 -0.38943 226 VAL A CA  
6124 C C   . VAL E 218 ? 2.11508 1.73701 3.27484 0.26850  -0.24198 -0.41782 226 VAL A C   
6125 O O   . VAL E 218 ? 2.04644 1.79144 3.23265 0.32158  -0.25641 -0.45819 226 VAL A O   
6126 C CB  . VAL E 218 ? 2.06213 1.77756 3.16189 0.24152  -0.23858 -0.31592 226 VAL A CB  
6127 C CG1 . VAL E 218 ? 1.99326 1.60183 3.05709 0.27040  -0.25412 -0.23652 226 VAL A CG1 
6128 C CG2 . VAL E 218 ? 2.10160 1.85501 3.17554 0.18484  -0.21897 -0.29345 226 VAL A CG2 
6129 N N   . GLU E 219 ? 2.32252 1.78341 3.46341 0.26841  -0.23409 -0.39352 227 GLU A N   
6130 C CA  . GLU E 219 ? 2.30415 1.72213 3.45675 0.32229  -0.24231 -0.41647 227 GLU A CA  
6131 C C   . GLU E 219 ? 2.29073 1.58221 3.39489 0.36611  -0.24848 -0.33223 227 GLU A C   
6132 O O   . GLU E 219 ? 2.32481 1.52420 3.38620 0.34087  -0.23545 -0.27341 227 GLU A O   
6133 C CB  . GLU E 219 ? 2.40783 1.75833 3.58739 0.27333  -0.20923 -0.50329 227 GLU A CB  
6134 C CG  . GLU E 219 ? 2.38136 1.88795 3.61795 0.28040  -0.22012 -0.60153 227 GLU A CG  
6135 C CD  . GLU E 219 ? 2.46259 1.93311 3.73413 0.20683  -0.18306 -0.70172 227 GLU A CD  
6136 O OE1 . GLU E 219 ? 2.54200 1.85136 3.79142 0.14749  -0.14020 -0.69264 227 GLU A OE1 
6137 O OE2 . GLU E 219 ? 2.43299 2.03943 3.75303 0.20961  -0.19175 -0.79364 227 GLU A OE2 
6138 N N   . PRO E 220 ? 2.43032 1.72115 3.53764 0.43825  -0.26796 -0.32403 228 PRO A N   
6139 C CA  . PRO E 220 ? 2.39941 1.60566 3.46173 0.49223  -0.27858 -0.24235 228 PRO A CA  
6140 C C   . PRO E 220 ? 2.53447 1.55691 3.54148 0.46977  -0.23974 -0.21128 228 PRO A C   
6141 O O   . PRO E 220 ? 2.65361 1.57783 3.66021 0.42720  -0.19767 -0.26355 228 PRO A O   
6142 C CB  . PRO E 220 ? 2.33198 1.55915 3.41411 0.56569  -0.29668 -0.25923 228 PRO A CB  
6143 C CG  . PRO E 220 ? 2.26211 1.63211 3.39947 0.56614  -0.30829 -0.33081 228 PRO A CG  
6144 C CD  . PRO E 220 ? 2.37035 1.75172 3.52165 0.48149  -0.28274 -0.38756 228 PRO A CD  
6145 N N   . LYS E 221 ? 2.50396 1.48286 3.46097 0.50172  -0.24818 -0.12828 229 LYS A N   
6146 C CA  . LYS E 221 ? 2.62545 1.42927 3.51289 0.50501  -0.20672 -0.08414 229 LYS A CA  
6147 C C   . LYS E 221 ? 2.65136 1.37732 3.49744 0.58703  -0.20150 -0.04886 229 LYS A C   
6148 O O   . LYS E 221 ? 2.79045 1.35063 3.58236 0.59390  -0.14660 -0.04479 229 LYS A O   
6149 C CB  . LYS E 221 ? 2.58717 1.39236 3.43360 0.50096  -0.21669 -0.01313 229 LYS A CB  
6150 N N   . THR F 5   ? 1.88282 2.07984 2.21669 0.06699  -0.10965 0.23795  5   THR B N   
6151 C CA  . THR F 5   ? 1.91077 2.06443 2.34736 0.05455  -0.13319 0.21667  5   THR B CA  
6152 C C   . THR F 5   ? 1.90915 2.14102 2.43289 0.02703  -0.14135 0.15045  5   THR B C   
6153 O O   . THR F 5   ? 1.87072 2.17399 2.34788 0.02145  -0.14814 0.12960  5   THR B O   
6154 C CB  . THR F 5   ? 1.90002 1.93124 2.26012 0.08559  -0.18540 0.27051  5   THR B CB  
6155 O OG1 . THR F 5   ? 1.87915 1.91647 2.18708 0.09166  -0.22886 0.25963  5   THR B OG1 
6156 C CG2 . THR F 5   ? 1.89745 1.84378 2.10610 0.11348  -0.17930 0.33422  5   THR B CG2 
6157 N N   . GLN F 6   ? 1.66915 1.88478 2.32270 0.01120  -0.13630 0.12074  6   GLN B N   
6158 C CA  . GLN F 6   ? 1.64270 1.91300 2.38192 -0.00911 -0.13856 0.06208  6   GLN B CA  
6159 C C   . GLN F 6   ? 1.62857 1.82623 2.41554 0.01887  -0.18104 0.09620  6   GLN B C   
6160 O O   . GLN F 6   ? 1.63813 1.74834 2.43576 0.03970  -0.19748 0.15348  6   GLN B O   
6161 C CB  . GLN F 6   ? 1.64326 1.96103 2.50646 -0.05708 -0.08012 -0.00922 6   GLN B CB  
6162 C CG  . GLN F 6   ? 1.58275 2.01593 2.44104 -0.10290 -0.06176 -0.07626 6   GLN B CG  
6163 C CD  . GLN F 6   ? 1.58482 2.05286 2.52589 -0.16624 -0.00089 -0.14710 6   GLN B CD  
6164 O OE1 . GLN F 6   ? 1.59762 2.10531 2.51001 -0.20274 0.02180  -0.14680 6   GLN B OE1 
6165 N NE2 . GLN F 6   ? 1.57624 2.02643 2.61786 -0.18299 0.02903  -0.20590 6   GLN B NE2 
6166 N N   . SER F 7   ? 1.69593 1.93841 2.51575 0.01544  -0.20133 0.06888  7   SER B N   
6167 C CA  . SER F 7   ? 1.67286 1.86808 2.55454 0.03768  -0.24495 0.11009  7   SER B CA  
6168 C C   . SER F 7   ? 1.61945 1.89250 2.59840 0.02273  -0.23251 0.05400  7   SER B C   
6169 O O   . SER F 7   ? 1.57788 1.92729 2.49116 0.00541  -0.23719 0.01531  7   SER B O   
6170 C CB  . SER F 7   ? 1.67135 1.80689 2.40163 0.06044  -0.31839 0.18347  7   SER B CB  
6171 O OG  . SER F 7   ? 1.65779 1.83753 2.25392 0.05609  -0.32631 0.16240  7   SER B OG  
6172 N N   . PRO F 8   ? 1.51097 1.76888 2.65244 0.02975  -0.21177 0.05179  8   PRO B N   
6173 C CA  . PRO F 8   ? 1.52084 1.69524 2.76646 0.05268  -0.21171 0.11069  8   PRO B CA  
6174 C C   . PRO F 8   ? 1.55899 1.70145 2.86450 0.03765  -0.14191 0.07310  8   PRO B C   
6175 O O   . PRO F 8   ? 1.57995 1.76953 2.87820 0.00272  -0.08551 -0.00805 8   PRO B O   
6176 C CB  . PRO F 8   ? 1.46585 1.66247 2.87974 0.06604  -0.20486 0.11532  8   PRO B CB  
6177 C CG  . PRO F 8   ? 1.45015 1.73183 2.88533 0.03677  -0.14691 0.01156  8   PRO B CG  
6178 C CD  . PRO F 8   ? 1.46004 1.79056 2.70813 0.01378  -0.17514 -0.01318 8   PRO B CD  
6179 N N   . SER F 9   ? 1.52746 1.58914 2.88971 0.05703  -0.14960 0.13765  9   SER B N   
6180 C CA  . SER F 9   ? 1.56286 1.58423 2.99464 0.04228  -0.08599 0.10950  9   SER B CA  
6181 C C   . SER F 9   ? 1.56754 1.59623 3.16441 0.02726  -0.00509 0.03229  9   SER B C   
6182 O O   . SER F 9   ? 1.62369 1.65075 3.22838 -0.01030 0.06016  -0.03999 9   SER B O   
6183 C CB  . SER F 9   ? 1.54147 1.47590 3.00946 0.06665  -0.11661 0.20464  9   SER B CB  
6184 O OG  . SER F 9   ? 1.54554 1.45726 2.84175 0.07541  -0.18369 0.27194  9   SER B OG  
6185 N N   . SER F 10  ? 1.39988 1.43337 3.12596 0.05254  -0.00482 0.04810  10  SER B N   
6186 C CA  . SER F 10  ? 1.40652 1.43253 3.29542 0.04606  0.08442  -0.02228 10  SER B CA  
6187 C C   . SER F 10  ? 1.33875 1.41222 3.32087 0.07357  0.07010  -0.00301 10  SER B C   
6188 O O   . SER F 10  ? 1.28504 1.36847 3.26379 0.10386  -0.01147 0.09336  10  SER B O   
6189 C CB  . SER F 10  ? 1.41447 1.34399 3.45543 0.06273  0.13272  0.00667  10  SER B CB  
6190 O OG  . SER F 10  ? 1.40660 1.29891 3.45683 0.09722  0.05677  0.12897  10  SER B OG  
6191 N N   . LEU F 11  ? 1.37179 1.47249 3.43218 0.05714  0.15093  -0.09303 11  LEU B N   
6192 C CA  . LEU F 11  ? 1.30619 1.46995 3.44546 0.07834  0.14481  -0.08411 11  LEU B CA  
6193 C C   . LEU F 11  ? 1.32594 1.47552 3.61171 0.07233  0.26533  -0.17164 11  LEU B C   
6194 O O   . LEU F 11  ? 1.40891 1.52390 3.65927 0.02714  0.34679  -0.27389 11  LEU B O   
6195 C CB  . LEU F 11  ? 1.29224 1.55154 3.25838 0.05250  0.08157  -0.10593 11  LEU B CB  
6196 C CG  . LEU F 11  ? 1.32736 1.64353 3.20114 -0.00569 0.13902  -0.22875 11  LEU B CG  
6197 C CD1 . LEU F 11  ? 1.28542 1.66426 3.23908 -0.01032 0.18467  -0.27994 11  LEU B CD1 
6198 C CD2 . LEU F 11  ? 1.32254 1.69736 2.99320 -0.03429 0.06947  -0.22813 11  LEU B CD2 
6199 N N   . SER F 12  ? 1.35314 1.52648 3.80144 0.11521  0.27745  -0.12594 12  SER B N   
6200 C CA  . SER F 12  ? 1.36867 1.53245 3.96629 0.12051  0.39731  -0.19862 12  SER B CA  
6201 C C   . SER F 12  ? 1.30554 1.57528 3.93481 0.13470  0.37169  -0.18108 12  SER B C   
6202 O O   . SER F 12  ? 1.26839 1.57526 3.99108 0.17986  0.29963  -0.06299 12  SER B O   
6203 C CB  . SER F 12  ? 1.46058 1.53107 4.29156 0.17247  0.46688  -0.14609 12  SER B CB  
6204 O OG  . SER F 12  ? 1.53035 1.49804 4.33534 0.15299  0.50293  -0.17507 12  SER B OG  
6205 N N   . ALA F 13  ? 1.29706 1.62040 3.84130 0.08877  0.42315  -0.29171 13  ALA B N   
6206 C CA  . ALA F 13  ? 1.25593 1.67545 3.84968 0.09779  0.42705  -0.29331 13  ALA B CA  
6207 C C   . ALA F 13  ? 1.35615 1.74076 4.08217 0.09614  0.58158  -0.38659 13  ALA B C   
6208 O O   . ALA F 13  ? 1.46498 1.73802 4.26147 0.09559  0.68215  -0.43711 13  ALA B O   
6209 C CB  . ALA F 13  ? 1.16687 1.68579 3.54831 0.04426  0.35521  -0.33596 13  ALA B CB  
6210 N N   . SER F 14  ? 1.33150 1.80444 4.08898 0.09460  0.60544  -0.40930 14  SER B N   
6211 C CA  . SER F 14  ? 1.43726 1.88031 4.29635 0.08840  0.75984  -0.50578 14  SER B CA  
6212 C C   . SER F 14  ? 1.42770 1.93969 4.09991 0.00567  0.78197  -0.62788 14  SER B C   
6213 O O   . SER F 14  ? 1.33322 1.91974 3.82035 -0.03978 0.67779  -0.62872 14  SER B O   
6214 C CB  . SER F 14  ? 1.46159 1.92918 4.51349 0.15567  0.77908  -0.41224 14  SER B CB  
6215 O OG  . SER F 14  ? 1.33247 1.91906 4.37466 0.17796  0.63998  -0.29802 14  SER B OG  
6216 N N   . VAL F 15  ? 1.53705 2.02171 4.26083 -0.01487 0.92341  -0.72819 15  VAL B N   
6217 C CA  . VAL F 15  ? 1.55953 2.09648 4.10227 -0.10757 0.95967  -0.85301 15  VAL B CA  
6218 C C   . VAL F 15  ? 1.42311 2.12397 3.90762 -0.11260 0.85750  -0.80582 15  VAL B C   
6219 O O   . VAL F 15  ? 1.38826 2.14106 4.00500 -0.05018 0.83688  -0.72015 15  VAL B O   
6220 C CB  . VAL F 15  ? 1.75549 2.18779 4.32194 -0.13543 1.12573  -0.95956 15  VAL B CB  
6221 C CG1 . VAL F 15  ? 1.81931 2.22431 4.56333 -0.05358 1.16336  -0.87280 15  VAL B CG1 
6222 C CG2 . VAL F 15  ? 1.78514 2.28265 4.15899 -0.23953 1.15518  -1.07976 15  VAL B CG2 
6223 N N   . GLY F 16  ? 1.39103 2.16533 3.66228 -0.19061 0.78517  -0.85085 16  GLY B N   
6224 C CA  . GLY F 16  ? 1.27286 2.19558 3.46271 -0.20726 0.68610  -0.81492 16  GLY B CA  
6225 C C   . GLY F 16  ? 1.16349 2.13703 3.29898 -0.17309 0.52379  -0.69731 16  GLY B C   
6226 O O   . GLY F 16  ? 1.07286 2.14801 3.07470 -0.21032 0.43638  -0.68869 16  GLY B O   
6227 N N   . ASP F 17  ? 1.15283 2.05217 3.38312 -0.10665 0.48458  -0.60631 17  ASP B N   
6228 C CA  . ASP F 17  ? 1.07473 2.00152 3.24445 -0.07606 0.33763  -0.49349 17  ASP B CA  
6229 C C   . ASP F 17  ? 1.04742 1.98812 3.00333 -0.13122 0.27109  -0.52360 17  ASP B C   
6230 O O   . ASP F 17  ? 1.12340 1.99402 3.02416 -0.16123 0.31317  -0.57673 17  ASP B O   
6231 C CB  . ASP F 17  ? 1.10711 1.93910 3.41047 -0.00813 0.32285  -0.39990 17  ASP B CB  
6232 C CG  . ASP F 17  ? 1.11250 1.94912 3.65003 0.05388  0.37222  -0.33808 17  ASP B CG  
6233 O OD1 . ASP F 17  ? 1.13845 2.00406 3.75207 0.04447  0.47620  -0.40761 17  ASP B OD1 
6234 O OD2 . ASP F 17  ? 1.09373 1.90699 3.74022 0.10893  0.31004  -0.21638 17  ASP B OD2 
6235 N N   . ARG F 18  ? 1.10900 2.14050 2.95196 -0.14410 0.16882  -0.48358 18  ARG B N   
6236 C CA  . ARG F 18  ? 1.06768 2.11458 2.72786 -0.18033 0.09807  -0.48494 18  ARG B CA  
6237 C C   . ARG F 18  ? 1.12938 2.07970 2.77526 -0.13698 0.04679  -0.41094 18  ARG B C   
6238 O O   . ARG F 18  ? 1.14800 2.05574 2.88280 -0.07971 0.00532  -0.32212 18  ARG B O   
6239 C CB  . ARG F 18  ? 0.93259 2.08320 2.49374 -0.19235 0.00302  -0.44618 18  ARG B CB  
6240 N N   . VAL F 19  ? 1.25315 1.37552 3.86604 0.06226  0.34931  -0.58998 19  VAL B N   
6241 C CA  . VAL F 19  ? 1.27162 1.34212 3.78651 0.10858  0.27031  -0.57218 19  VAL B CA  
6242 C C   . VAL F 19  ? 1.23995 1.27447 3.64855 0.09789  0.27967  -0.53004 19  VAL B C   
6243 O O   . VAL F 19  ? 1.20810 1.23283 3.56606 0.06387  0.35031  -0.50343 19  VAL B O   
6244 C CB  . VAL F 19  ? 1.31350 1.33678 3.74754 0.13980  0.25758  -0.56749 19  VAL B CB  
6245 C CG1 . VAL F 19  ? 1.29656 1.29265 3.64563 0.11087  0.33855  -0.53984 19  VAL B CG1 
6246 C CG2 . VAL F 19  ? 1.35326 1.30983 3.68194 0.18644  0.17360  -0.54793 19  VAL B CG2 
6247 N N   . THR F 20  ? 1.36691 1.37788 3.73682 0.12897  0.20683  -0.52588 20  THR B N   
6248 C CA  . THR F 20  ? 1.34904 1.32865 3.62396 0.12441  0.21012  -0.49273 20  THR B CA  
6249 C C   . THR F 20  ? 1.40637 1.32291 3.55920 0.17328  0.14263  -0.47810 20  THR B C   
6250 O O   . THR F 20  ? 1.45374 1.36348 3.62637 0.20981  0.06626  -0.50168 20  THR B O   
6251 C CB  . THR F 20  ? 1.32574 1.34325 3.68788 0.10553  0.19900  -0.50689 20  THR B CB  
6252 O OG1 . THR F 20  ? 1.28139 1.33834 3.72628 0.05273  0.27788  -0.50587 20  THR B OG1 
6253 C CG2 . THR F 20  ? 1.33184 1.31087 3.59020 0.11884  0.17548  -0.48260 20  THR B CG2 
6254 N N   . ILE F 21  ? 1.27996 1.14635 3.30932 0.17211  0.17241  -0.43914 21  ILE B N   
6255 C CA  . ILE F 21  ? 1.34157 1.14464 3.24517 0.21059  0.12442  -0.41750 21  ILE B CA  
6256 C C   . ILE F 21  ? 1.34719 1.16036 3.19322 0.20280  0.12290  -0.40205 21  ILE B C   
6257 O O   . ILE F 21  ? 1.28773 1.13389 3.16425 0.16352  0.17393  -0.39314 21  ILE B O   
6258 C CB  . ILE F 21  ? 1.40055 1.15782 3.17194 0.19676  0.15339  -0.37087 21  ILE B CB  
6259 C CG1 . ILE F 21  ? 1.38223 1.13006 3.22089 0.20006  0.16477  -0.39105 21  ILE B CG1 
6260 C CG2 . ILE F 21  ? 1.54527 1.24688 3.17344 0.22796  0.09794  -0.34189 21  ILE B CG2 
6261 C CD1 . ILE F 21  ? 1.44342 1.14058 3.16205 0.18171  0.19207  -0.34746 21  ILE B CD1 
6262 N N   . THR F 22  ? 1.34754 1.12895 3.10739 0.24150  0.06227  -0.40061 22  THR B N   
6263 C CA  . THR F 22  ? 1.38001 1.16828 3.07495 0.24328  0.05751  -0.39150 22  THR B CA  
6264 C C   . THR F 22  ? 1.53194 1.28306 3.04906 0.25813  0.05095  -0.35007 22  THR B C   
6265 O O   . THR F 22  ? 1.64404 1.35242 3.09253 0.28495  0.01136  -0.34209 22  THR B O   
6266 C CB  . THR F 22  ? 1.36885 1.16337 3.14115 0.27768  -0.01019 -0.44023 22  THR B CB  
6267 O OG1 . THR F 22  ? 1.26666 1.10739 3.20579 0.25199  0.00200  -0.47059 22  THR B OG1 
6268 C CG2 . THR F 22  ? 1.40333 1.20161 3.10934 0.28289  -0.01535 -0.43680 22  THR B CG2 
6269 N N   . CYS F 23  ? 1.49862 1.26765 2.94686 0.23872  0.08981  -0.32291 23  CYS B N   
6270 C CA  . CYS F 23  ? 1.65687 1.41178 2.95084 0.24205  0.10331  -0.27960 23  CYS B CA  
6271 C C   . CYS F 23  ? 1.71184 1.48322 2.96308 0.26799  0.08376  -0.29594 23  CYS B C   
6272 O O   . CYS F 23  ? 1.58984 1.38896 2.92186 0.25874  0.09130  -0.31947 23  CYS B O   
6273 C CB  . CYS F 23  ? 1.61854 1.38791 2.88394 0.19209  0.17484  -0.23276 23  CYS B CB  
6274 S SG  . CYS F 23  ? 1.82332 1.58169 2.92091 0.18468  0.19864  -0.17097 23  CYS B SG  
6275 N N   . ARG F 24  ? 1.79755 1.54854 2.91891 0.30046  0.05762  -0.28428 24  ARG B N   
6276 C CA  . ARG F 24  ? 1.88330 1.64779 2.94514 0.33322  0.03899  -0.30455 24  ARG B CA  
6277 C C   . ARG F 24  ? 1.94823 1.74810 2.92591 0.31405  0.09849  -0.26396 24  ARG B C   
6278 O O   . ARG F 24  ? 2.04747 1.84559 2.95203 0.28974  0.13449  -0.21368 24  ARG B O   
6279 C CB  . ARG F 24  ? 2.09723 1.81990 3.05755 0.38332  -0.02474 -0.32078 24  ARG B CB  
6280 C CG  . ARG F 24  ? 2.17644 1.90512 3.08696 0.42679  -0.05715 -0.35969 24  ARG B CG  
6281 C CD  . ARG F 24  ? 1.96115 1.71286 3.00948 0.42493  -0.06838 -0.40484 24  ARG B CD  
6282 N NE  . ARG F 24  ? 1.85789 1.58488 3.02579 0.43494  -0.12801 -0.44583 24  ARG B NE  
6283 C CZ  . ARG F 24  ? 1.91495 1.61126 3.08457 0.48030  -0.20464 -0.49504 24  ARG B CZ  
6284 N NH1 . ARG F 24  ? 2.07530 1.75743 3.12393 0.52236  -0.23004 -0.51316 24  ARG B NH1 
6285 N NH2 . ARG F 24  ? 1.81333 1.49502 3.11224 0.48427  -0.25725 -0.52962 24  ARG B NH2 
6286 N N   . ALA F 25  ? 1.91322 1.74461 2.90972 0.32550  0.10448  -0.28731 25  ALA B N   
6287 C CA  . ALA F 25  ? 1.94639 1.82038 2.88475 0.31463  0.15517  -0.25914 25  ALA B CA  
6288 C C   . ALA F 25  ? 2.03659 1.92502 2.91930 0.36616  0.12900  -0.29843 25  ALA B C   
6289 O O   . ALA F 25  ? 1.94099 1.85607 2.87273 0.37094  0.13605  -0.32047 25  ALA B O   
6290 C CB  . ALA F 25  ? 1.75921 1.65805 2.79584 0.26935  0.19625  -0.24632 25  ALA B CB  
6291 N N   . SER F 26  ? 2.07868 1.94179 2.85521 0.40685  0.09316  -0.31008 26  SER B N   
6292 C CA  . SER F 26  ? 2.19231 2.06174 2.89711 0.46174  0.06506  -0.35347 26  SER B CA  
6293 C C   . SER F 26  ? 2.18527 2.11700 2.86056 0.46319  0.11930  -0.34434 26  SER B C   
6294 O O   . SER F 26  ? 2.14081 2.08600 2.82845 0.50075  0.10038  -0.39257 26  SER B O   
6295 C CB  . SER F 26  ? 2.47243 2.30600 3.03092 0.49579  0.03375  -0.35008 26  SER B CB  
6296 O OG  . SER F 26  ? 2.63253 2.47138 3.10986 0.46266  0.07771  -0.28445 26  SER B OG  
6297 N N   . GLN F 27  ? 2.29187 2.26156 2.93544 0.42426  0.18268  -0.28549 27  GLN B N   
6298 C CA  . GLN F 27  ? 2.20261 2.23679 2.86633 0.41588  0.23325  -0.27556 27  GLN B CA  
6299 C C   . GLN F 27  ? 1.94140 1.97123 2.74934 0.38426  0.23111  -0.28416 27  GLN B C   
6300 O O   . GLN F 27  ? 1.84417 1.85912 2.70668 0.33381  0.24970  -0.24718 27  GLN B O   
6301 C CB  . GLN F 27  ? 2.28837 2.36474 2.88761 0.37922  0.29668  -0.20821 27  GLN B CB  
6302 C CG  . GLN F 27  ? 2.56227 2.65289 3.01080 0.40417  0.30971  -0.19204 27  GLN B CG  
6303 C CD  . GLN F 27  ? 2.75997 2.78221 3.13720 0.39846  0.27479  -0.17108 27  GLN B CD  
6304 O OE1 . GLN F 27  ? 2.74762 2.71062 3.15994 0.41742  0.21518  -0.20785 27  GLN B OE1 
6305 N NE2 . GLN F 27  ? 2.92847 2.95763 3.21047 0.37122  0.30823  -0.11063 27  GLN B NE2 
6306 N N   . ALA F 28  ? 1.90433 1.94231 2.76794 0.41332  0.20722  -0.33284 28  ALA B N   
6307 C CA  . ALA F 28  ? 1.69566 1.72247 2.68764 0.38051  0.20150  -0.33763 28  ALA B CA  
6308 C C   . ALA F 28  ? 1.62028 1.68728 2.63244 0.33594  0.25864  -0.28704 28  ALA B C   
6309 O O   . ALA F 28  ? 1.58487 1.69034 2.61084 0.35011  0.27152  -0.29611 28  ALA B O   
6310 C CB  . ALA F 28  ? 1.63648 1.65427 2.67907 0.42189  0.15557  -0.39917 28  ALA B CB  
6311 N N   . ALA F 29  ? 1.56901 1.62495 2.58463 0.28433  0.28874  -0.23622 29  ALA B N   
6312 C CA  . ALA F 29  ? 1.49469 1.57767 2.52976 0.23726  0.33562  -0.18677 29  ALA B CA  
6313 C C   . ALA F 29  ? 1.34663 1.39452 2.48183 0.19349  0.32930  -0.18326 29  ALA B C   
6314 O O   . ALA F 29  ? 1.30940 1.33204 2.45956 0.14756  0.34801  -0.15074 29  ALA B O   
6315 C CB  . ALA F 29  ? 1.58185 1.66915 2.54651 0.20695  0.37104  -0.13192 29  ALA B CB  
6316 N N   . TYR F 30  ? 1.37967 1.42073 2.57921 0.21063  0.29897  -0.22109 36  TYR B N   
6317 C CA  . TYR F 30  ? 1.27260 1.28837 2.55726 0.16943  0.29557  -0.21291 36  TYR B CA  
6318 C C   . TYR F 30  ? 1.22238 1.20101 2.54226 0.11263  0.31241  -0.18489 36  TYR B C   
6319 O O   . TYR F 30  ? 1.17954 1.14461 2.52871 0.06540  0.33208  -0.15428 36  TYR B O   
6320 C CB  . TYR F 30  ? 1.25429 1.30226 2.53771 0.15452  0.32095  -0.18352 36  TYR B CB  
6321 C CG  . TYR F 30  ? 1.30371 1.40490 2.55355 0.21059  0.31780  -0.20914 36  TYR B CG  
6322 C CD1 . TYR F 30  ? 1.38091 1.53507 2.55198 0.22604  0.35377  -0.18847 36  TYR B CD1 
6323 C CD2 . TYR F 30  ? 1.28294 1.38124 2.57972 0.24854  0.27907  -0.25562 36  TYR B CD2 
6324 C CE1 . TYR F 30  ? 1.43447 1.64729 2.57464 0.27756  0.35956  -0.21428 36  TYR B CE1 
6325 C CE2 . TYR F 30  ? 1.32967 1.48081 2.59708 0.30526  0.27926  -0.28645 36  TYR B CE2 
6326 C CZ  . TYR F 30  ? 1.40553 1.61853 2.59427 0.31959  0.32362  -0.26622 36  TYR B CZ  
6327 O OH  . TYR F 30  ? 1.45958 1.73493 2.61758 0.37564  0.33288  -0.29826 36  TYR B OH  
6328 N N   . GLY F 31  ? 1.35194 1.31248 2.66987 0.11785  0.30320  -0.19740 37  GLY B N   
6329 C CA  . GLY F 31  ? 1.30049 1.23278 2.66151 0.06867  0.32236  -0.17887 37  GLY B CA  
6330 C C   . GLY F 31  ? 1.30994 1.24254 2.62749 0.02404  0.36948  -0.12605 37  GLY B C   
6331 O O   . GLY F 31  ? 1.26392 1.17332 2.61635 -0.02446 0.39048  -0.10715 37  GLY B O   
6332 N N   . ARG F 32  ? 1.31675 1.27289 2.55496 0.03723  0.38595  -0.10090 38  ARG B N   
6333 C CA  . ARG F 32  ? 1.30994 1.26184 2.50645 -0.00495 0.42367  -0.05044 38  ARG B CA  
6334 C C   . ARG F 32  ? 1.34190 1.26420 2.51813 -0.01766 0.43180  -0.04181 38  ARG B C   
6335 O O   . ARG F 32  ? 1.31471 1.22521 2.44819 -0.04875 0.45711  -0.00245 38  ARG B O   
6336 C CB  . ARG F 32  ? 1.35673 1.35085 2.48661 0.00810  0.43890  -0.02197 38  ARG B CB  
6337 C CG  . ARG F 32  ? 1.37166 1.41036 2.50863 0.04775  0.42586  -0.04526 38  ARG B CG  
6338 C CD  . ARG F 32  ? 1.28429 1.32545 2.47582 0.02502  0.42633  -0.03849 38  ARG B CD  
6339 N NE  . ARG F 32  ? 1.29837 1.39548 2.48516 0.05738  0.42679  -0.04478 38  ARG B NE  
6340 C CZ  . ARG F 32  ? 1.24683 1.35467 2.47905 0.04666  0.42229  -0.03865 38  ARG B CZ  
6341 N NH1 . ARG F 32  ? 1.19420 1.25300 2.46857 0.00222  0.41430  -0.02356 38  ARG B NH1 
6342 N NH2 . ARG F 32  ? 1.26030 1.42926 2.49460 0.08189  0.42543  -0.04850 38  ARG B NH2 
6343 N N   . VAL F 33  ? 1.39623 1.30412 2.60807 0.00712  0.40577  -0.07986 39  VAL B N   
6344 C CA  . VAL F 33  ? 1.44339 1.32516 2.63969 0.00708  0.40431  -0.07817 39  VAL B CA  
6345 C C   . VAL F 33  ? 1.36526 1.22086 2.58648 -0.04269 0.43777  -0.05903 39  VAL B C   
6346 O O   . VAL F 33  ? 1.23388 1.08672 2.50693 -0.07367 0.45428  -0.06214 39  VAL B O   
6347 C CB  . VAL F 33  ? 1.41977 1.29456 2.67000 0.04449  0.36342  -0.12794 39  VAL B CB  
6348 C CG1 . VAL F 33  ? 1.42270 1.26921 2.68945 0.04207  0.35930  -0.13372 39  VAL B CG1 
6349 C CG2 . VAL F 33  ? 1.51939 1.40785 2.71350 0.09666  0.32775  -0.14503 39  VAL B CG2 
6350 N N   . ALA F 34  ? 1.34975 1.18015 2.52762 -0.04992 0.44537  -0.03998 40  ALA B N   
6351 C CA  . ALA F 34  ? 1.23801 1.03745 2.42795 -0.08887 0.47414  -0.02910 40  ALA B CA  
6352 C C   . ALA F 34  ? 1.31223 1.08532 2.50638 -0.06773 0.45683  -0.04674 40  ALA B C   
6353 O O   . ALA F 34  ? 1.43590 1.20641 2.59654 -0.03097 0.42295  -0.05062 40  ALA B O   
6354 C CB  . ALA F 34  ? 1.15829 0.94369 2.27846 -0.12640 0.49983  0.02144  40  ALA B CB  
6355 N N   . TRP F 35  ? 1.38151 1.13213 2.61240 -0.09045 0.47934  -0.05790 41  TRP B N   
6356 C CA  . TRP F 35  ? 1.43179 1.15447 2.67696 -0.07032 0.46330  -0.07797 41  TRP B CA  
6357 C C   . TRP F 35  ? 1.40064 1.08042 2.59761 -0.10079 0.48846  -0.05423 41  TRP B C   
6358 O O   . TRP F 35  ? 1.28423 0.95971 2.48388 -0.13986 0.52800  -0.04705 41  TRP B O   
6359 C CB  . TRP F 35  ? 1.37070 1.11267 2.73194 -0.05670 0.46194  -0.13181 41  TRP B CB  
6360 C CG  . TRP F 35  ? 1.35176 1.13030 2.77582 -0.03213 0.43465  -0.16005 41  TRP B CG  
6361 C CD1 . TRP F 35  ? 1.29768 1.10448 2.76107 -0.05109 0.44872  -0.16338 41  TRP B CD1 
6362 C CD2 . TRP F 35  ? 1.38030 1.16217 2.83163 0.01691  0.38035  -0.18975 41  TRP B CD2 
6363 N NE1 . TRP F 35  ? 1.28727 1.11570 2.80555 -0.01657 0.40695  -0.19569 41  TRP B NE1 
6364 C CE2 . TRP F 35  ? 1.33310 1.14737 2.84260 0.02597  0.36447  -0.21304 41  TRP B CE2 
6365 C CE3 . TRP F 35  ? 1.44846 1.20121 2.87704 0.05381  0.33760  -0.19844 41  TRP B CE3 
6366 C CZ2 . TRP F 35  ? 1.34745 1.16726 2.89154 0.07149  0.30769  -0.24734 41  TRP B CZ2 
6367 C CZ3 . TRP F 35  ? 1.47101 1.22855 2.93004 0.09830  0.28114  -0.22981 41  TRP B CZ3 
6368 C CH2 . TRP F 35  ? 1.41889 1.21055 2.93438 0.10722  0.26693  -0.25521 41  TRP B CH2 
6369 N N   . TYR F 36  ? 1.46410 1.10488 2.61588 -0.08158 0.46006  -0.04483 42  TYR B N   
6370 C CA  . TYR F 36  ? 1.46261 1.04954 2.56247 -0.10290 0.46889  -0.02396 42  TYR B CA  
6371 C C   . TYR F 36  ? 1.50997 1.06509 2.65466 -0.07148 0.44433  -0.06298 42  TYR B C   
6372 O O   . TYR F 36  ? 1.55911 1.12212 2.74036 -0.03051 0.40394  -0.08722 42  TYR B O   
6373 C CB  . TYR F 36  ? 1.53553 1.09504 2.53115 -0.11366 0.45014  0.03382  42  TYR B CB  
6374 C CG  . TYR F 36  ? 1.47170 1.06698 2.42656 -0.14100 0.47069  0.07431  42  TYR B CG  
6375 C CD1 . TYR F 36  ? 1.32497 0.91011 2.25858 -0.18564 0.50216  0.09874  42  TYR B CD1 
6376 C CD2 . TYR F 36  ? 1.56195 1.19916 2.49737 -0.11961 0.45549  0.08617  42  TYR B CD2 
6377 C CE1 . TYR F 36  ? 1.24323 0.86261 2.15150 -0.20764 0.51473  0.13397  42  TYR B CE1 
6378 C CE2 . TYR F 36  ? 1.49739 1.17388 2.40702 -0.13938 0.47431  0.11790  42  TYR B CE2 
6379 C CZ  . TYR F 36  ? 1.32399 0.99280 2.22671 -0.18307 0.50214  0.14194  42  TYR B CZ  
6380 O OH  . TYR F 36  ? 1.24707 0.95687 2.13667 -0.19947 0.51499  0.17097  42  TYR B OH  
6381 N N   . GLN F 37  ? 1.59705 1.11079 2.73337 -0.08872 0.46375  -0.06935 43  GLN B N   
6382 C CA  . GLN F 37  ? 1.62692 1.10914 2.81356 -0.05971 0.44676  -0.11246 43  GLN B CA  
6383 C C   . GLN F 37  ? 1.70445 1.10678 2.80553 -0.06438 0.41883  -0.08214 43  GLN B C   
6384 O O   . GLN F 37  ? 1.68542 1.05577 2.72475 -0.10218 0.44413  -0.05519 43  GLN B O   
6385 C CB  . GLN F 37  ? 1.55872 1.06450 2.81897 -0.07380 0.50043  -0.15770 43  GLN B CB  
6386 C CG  . GLN F 37  ? 1.57476 1.06535 2.91073 -0.03818 0.48973  -0.21376 43  GLN B CG  
6387 C CD  . GLN F 37  ? 1.53082 1.06169 2.94586 -0.05221 0.55321  -0.26150 43  GLN B CD  
6388 O OE1 . GLN F 37  ? 1.50026 1.06736 3.02951 -0.02112 0.55534  -0.31749 43  GLN B OE1 
6389 N NE2 . GLN F 37  ? 1.52631 1.05215 2.88095 -0.10031 0.60520  -0.23894 43  GLN B NE2 
6390 N N   . GLN F 38  ? 1.58167 0.94456 2.67585 -0.02779 0.36069  -0.08442 44  GLN B N   
6391 C CA  . GLN F 38  ? 1.67212 0.94901 2.68735 -0.03127 0.32256  -0.05310 44  GLN B CA  
6392 C C   . GLN F 38  ? 1.68108 0.91660 2.76246 0.00563  0.29862  -0.10938 44  GLN B C   
6393 O O   . GLN F 38  ? 1.70123 0.93732 2.84044 0.05055  0.25374  -0.14021 44  GLN B O   
6394 C CB  . GLN F 38  ? 1.78947 1.04266 2.72789 -0.02327 0.27102  -0.00239 44  GLN B CB  
6395 C CG  . GLN F 38  ? 1.89767 1.05421 2.75786 -0.02764 0.22138  0.03409  44  GLN B CG  
6396 C CD  . GLN F 38  ? 1.88956 1.01640 2.66285 -0.08185 0.24196  0.09359  44  GLN B CD  
6397 O OE1 . GLN F 38  ? 1.96027 1.07506 2.65309 -0.10360 0.22400  0.15602  44  GLN B OE1 
6398 N NE2 . GLN F 38  ? 1.80335 0.91887 2.59199 -0.10485 0.27917  0.07454  44  GLN B NE2 
6399 N N   . LYS F 39  ? 1.70766 0.90930 2.78373 -0.01131 0.32827  -0.12709 45  LYS B N   
6400 C CA  . LYS F 39  ? 1.73561 0.88974 2.86296 0.02323  0.30799  -0.18095 45  LYS B CA  
6401 C C   . LYS F 39  ? 1.84468 0.89702 2.90086 0.03631  0.23251  -0.14864 45  LYS B C   
6402 O O   . LYS F 39  ? 1.90094 0.92103 2.85865 0.00724  0.20895  -0.07933 45  LYS B O   
6403 C CB  . LYS F 39  ? 1.71634 0.86347 2.84147 -0.00073 0.36724  -0.20967 45  LYS B CB  
6404 N N   . PRO F 40  ? 1.93533 0.93597 3.04468 0.08016  0.19174  -0.19799 46  PRO B N   
6405 C CA  . PRO F 40  ? 2.04676 0.93787 3.09047 0.09353  0.11004  -0.16718 46  PRO B CA  
6406 C C   . PRO F 40  ? 2.11916 0.93704 3.03485 0.04187  0.10310  -0.09752 46  PRO B C   
6407 O O   . PRO F 40  ? 2.11645 0.89993 3.00988 0.02181  0.13054  -0.11070 46  PRO B O   
6408 C CB  . PRO F 40  ? 2.04654 0.89783 3.17514 0.14179  0.08949  -0.24395 46  PRO B CB  
6409 C CG  . PRO F 40  ? 1.96790 0.92667 3.23238 0.17017  0.13815  -0.31281 46  PRO B CG  
6410 C CD  . PRO F 40  ? 1.86166 0.91236 3.11017 0.12589  0.20839  -0.28336 46  PRO B CD  
6411 N N   . GLY F 41  ? 2.24097 1.03495 3.07222 0.01998  0.06524  -0.02391 47  GLY B N   
6412 C CA  . GLY F 41  ? 2.30233 1.03138 3.02087 -0.03151 0.05021  0.05111  47  GLY B CA  
6413 C C   . GLY F 41  ? 2.23129 0.98022 2.92137 -0.07966 0.11151  0.06234  47  GLY B C   
6414 O O   . GLY F 41  ? 2.26757 0.93496 2.90335 -0.10531 0.09333  0.08100  47  GLY B O   
6415 N N   . LYS F 42  ? 2.10217 0.95233 2.82455 -0.09335 0.17742  0.05356  48  LYS B N   
6416 C CA  . LYS F 42  ? 2.02075 0.89307 2.72048 -0.13648 0.23482  0.05954  48  LYS B CA  
6417 C C   . LYS F 42  ? 1.94166 0.89760 2.62105 -0.16960 0.27045  0.10850  48  LYS B C   
6418 O O   . LYS F 42  ? 1.97925 0.96340 2.64173 -0.16457 0.24900  0.14573  48  LYS B O   
6419 C CB  . LYS F 42  ? 1.97032 0.87391 2.74410 -0.11476 0.28417  -0.01978 48  LYS B CB  
6420 N N   . ALA F 43  ? 1.91730 0.91066 2.59341 -0.20325 0.32459  0.10743  49  ALA B N   
6421 C CA  . ALA F 43  ? 1.81602 0.88139 2.47594 -0.23647 0.35681  0.15104  49  ALA B CA  
6422 C C   . ALA F 43  ? 1.75948 0.91667 2.49389 -0.21127 0.39198  0.11319  49  ALA B C   
6423 O O   . ALA F 43  ? 1.73217 0.90694 2.52454 -0.19652 0.42313  0.05650  49  ALA B O   
6424 C CB  . ALA F 43  ? 1.78496 0.84808 2.39524 -0.28022 0.38048  0.16630  49  ALA B CB  
6425 N N   . PRO F 44  ? 1.69789 0.91374 2.43307 -0.20579 0.38762  0.14140  50  PRO B N   
6426 C CA  . PRO F 44  ? 1.64738 0.94568 2.45161 -0.18489 0.41585  0.10722  50  PRO B CA  
6427 C C   . PRO F 44  ? 1.51001 0.84434 2.33329 -0.21630 0.46777  0.09812  50  PRO B C   
6428 O O   . PRO F 44  ? 1.47511 0.81759 2.24920 -0.25304 0.47852  0.14069  50  PRO B O   
6429 C CB  . PRO F 44  ? 1.69422 1.03457 2.46698 -0.17971 0.39866  0.14886  50  PRO B CB  
6430 C CG  . PRO F 44  ? 1.81524 1.09054 2.52009 -0.18072 0.35258  0.18916  50  PRO B CG  
6431 C CD  . PRO F 44  ? 1.77677 0.98012 2.45030 -0.21222 0.35113  0.20041  50  PRO B CD  
6432 N N   . LYS F 45  ? 1.64147 0.99868 2.53462 -0.20208 0.49610  0.04256  51  LYS B N   
6433 C CA  . LYS F 45  ? 1.56831 0.95902 2.48065 -0.23145 0.54473  0.03237  51  LYS B CA  
6434 C C   . LYS F 45  ? 1.50527 0.97157 2.48117 -0.21754 0.55405  0.02023  51  LYS B C   
6435 O O   . LYS F 45  ? 1.54567 1.03869 2.57535 -0.17803 0.53120  -0.00589 51  LYS B O   
6436 C CB  . LYS F 45  ? 1.59366 0.96379 2.53808 -0.23180 0.57788  -0.01883 51  LYS B CB  
6437 N N   . LEU F 46  ? 1.54785 1.06247 2.48997 -0.23583 0.56569  0.03492  52  LEU B N   
6438 C CA  . LEU F 46  ? 1.49425 1.06824 2.49394 -0.22545 0.57090  0.02459  52  LEU B CA  
6439 C C   . LEU F 46  ? 1.47616 1.07682 2.54309 -0.22372 0.59960  -0.02141 52  LEU B C   
6440 O O   . LEU F 46  ? 1.49946 1.08819 2.52771 -0.24007 0.62057  -0.03165 52  LEU B O   
6441 C CB  . LEU F 46  ? 1.46326 1.07096 2.39203 -0.23837 0.55620  0.06037  52  LEU B CB  
6442 N N   . LEU F 47  ? 1.32834 0.96428 2.49625 -0.20651 0.60024  -0.04807 53  LEU B N   
6443 C CA  . LEU F 47  ? 1.31216 0.98322 2.55636 -0.20672 0.62541  -0.08937 53  LEU B CA  
6444 C C   . LEU F 47  ? 1.27194 0.98712 2.53119 -0.20729 0.61646  -0.08693 53  LEU B C   
6445 O O   . LEU F 47  ? 1.27869 1.00725 2.52246 -0.22183 0.63269  -0.09489 53  LEU B O   
6446 C CB  . LEU F 47  ? 1.32523 1.00520 2.68416 -0.17586 0.61886  -0.13708 53  LEU B CB  
6447 N N   . ILE F 48  ? 1.24700 0.97612 2.53284 -0.19401 0.59054  -0.07556 54  ILE B N   
6448 C CA  . ILE F 48  ? 1.21692 0.98011 2.53533 -0.19251 0.57893  -0.08056 54  ILE B CA  
6449 C C   . ILE F 48  ? 1.20608 0.97028 2.46940 -0.19195 0.55911  -0.04508 54  ILE B C   
6450 O O   . ILE F 48  ? 1.21910 0.97929 2.47712 -0.17530 0.54597  -0.03351 54  ILE B O   
6451 C CB  . ILE F 48  ? 1.20463 0.99460 2.66432 -0.17345 0.56779  -0.12320 54  ILE B CB  
6452 C CG1 . ILE F 48  ? 1.21236 1.01716 2.74468 -0.17552 0.59142  -0.16113 54  ILE B CG1 
6453 C CG2 . ILE F 48  ? 1.18183 0.99740 2.67704 -0.17208 0.54827  -0.12727 54  ILE B CG2 
6454 C CD1 . ILE F 48  ? 1.21765 1.03118 2.70407 -0.19758 0.61463  -0.15776 54  ILE B CD1 
6455 N N   . TYR F 49  ? 1.65799 0.95472 2.32864 -0.22674 0.34254  -0.14235 55  TYR B N   
6456 C CA  . TYR F 49  ? 1.67624 0.98236 2.28796 -0.22084 0.29261  -0.16782 55  TYR B CA  
6457 C C   . TYR F 49  ? 1.68246 0.97341 2.32024 -0.22781 0.27440  -0.18028 55  TYR B C   
6458 O O   . TYR F 49  ? 1.68000 0.93301 2.36654 -0.23842 0.30970  -0.16526 55  TYR B O   
6459 C CB  . TYR F 49  ? 1.72033 0.96512 2.21199 -0.20495 0.29680  -0.17551 55  TYR B CB  
6460 C CG  . TYR F 49  ? 1.77343 0.91866 2.19757 -0.19433 0.33846  -0.16552 55  TYR B CG  
6461 C CD1 . TYR F 49  ? 1.79276 0.89666 2.22205 -0.18954 0.39567  -0.13856 55  TYR B CD1 
6462 C CD2 . TYR F 49  ? 1.81911 0.91090 2.16682 -0.18402 0.31986  -0.18327 55  TYR B CD2 
6463 C CE1 . TYR F 49  ? 1.86703 0.87875 2.22294 -0.17263 0.43746  -0.12583 55  TYR B CE1 
6464 C CE2 . TYR F 49  ? 1.88826 0.88202 2.16094 -0.16772 0.35891  -0.17135 55  TYR B CE2 
6465 C CZ  . TYR F 49  ? 1.91687 0.87094 2.19209 -0.16107 0.41979  -0.14071 55  TYR B CZ  
6466 O OH  . TYR F 49  ? 2.00677 0.86287 2.19870 -0.13835 0.46353  -0.12454 55  TYR B OH  
6467 N N   . LYS F 50  ? 1.76197 1.08569 2.37343 -0.22160 0.21853  -0.20824 56  LYS B N   
6468 C CA  . LYS F 50  ? 1.76489 1.08784 2.40914 -0.22499 0.18460  -0.22762 56  LYS B CA  
6469 C C   . LYS F 50  ? 1.72082 1.09254 2.50178 -0.23725 0.18219  -0.22608 56  LYS B C   
6470 O O   . LYS F 50  ? 1.71442 1.06592 2.54963 -0.24554 0.17164  -0.23526 56  LYS B O   
6471 C CB  . LYS F 50  ? 1.80880 1.02637 2.38691 -0.22474 0.20989  -0.22196 56  LYS B CB  
6472 C CG  . LYS F 50  ? 1.86179 1.01366 2.30366 -0.20626 0.22293  -0.22387 56  LYS B CG  
6473 C CD  . LYS F 50  ? 1.92188 0.98720 2.28513 -0.19591 0.21526  -0.23446 56  LYS B CD  
6474 C CE  . LYS F 50  ? 1.98348 0.97050 2.21058 -0.16997 0.23455  -0.23741 56  LYS B CE  
6475 N NZ  . LYS F 50  ? 2.04124 0.93172 2.23276 -0.16279 0.30305  -0.20190 56  LYS B NZ  
6476 N N   . ALA F 51  ? 1.59444 1.02622 2.43512 -0.23708 0.19142  -0.21641 57  ALA B N   
6477 C CA  . ALA F 51  ? 1.55772 1.04889 2.53075 -0.24161 0.18325  -0.22225 57  ALA B CA  
6478 C C   . ALA F 51  ? 1.53220 0.97220 2.58113 -0.26236 0.23739  -0.20410 57  ALA B C   
6479 O O   . ALA F 51  ? 1.49773 0.98299 2.66807 -0.26826 0.24084  -0.20917 57  ALA B O   
6480 C CB  . ALA F 51  ? 1.55891 1.11197 2.58280 -0.22957 0.11336  -0.25915 57  ALA B CB  
6481 N N   . SER F 52  ? 1.59168 0.93890 2.57160 -0.27050 0.28092  -0.18374 65  SER B N   
6482 C CA  . SER F 52  ? 1.60707 0.90101 2.64317 -0.28801 0.34813  -0.15588 65  SER B CA  
6483 C C   . SER F 52  ? 1.67189 0.87988 2.59695 -0.28152 0.41037  -0.12318 65  SER B C   
6484 O O   . SER F 52  ? 1.70559 0.89050 2.67248 -0.28929 0.47249  -0.09609 65  SER B O   
6485 C CB  . SER F 52  ? 1.64598 0.90639 2.75245 -0.30432 0.34283  -0.16261 65  SER B CB  
6486 O OG  . SER F 52  ? 1.68831 0.88490 2.68625 -0.29596 0.32073  -0.16867 65  SER B OG  
6487 N N   . GLU F 53  ? 1.70667 0.86944 2.49489 -0.26354 0.39567  -0.12779 66  GLU B N   
6488 C CA  . GLU F 53  ? 1.77395 0.85436 2.45232 -0.24760 0.44823  -0.10364 66  GLU B CA  
6489 C C   . GLU F 53  ? 1.75953 0.87202 2.44149 -0.23967 0.47374  -0.09195 66  GLU B C   
6490 O O   . GLU F 53  ? 1.70659 0.89672 2.43704 -0.24250 0.44003  -0.10531 66  GLU B O   
6491 C CB  . GLU F 53  ? 1.82936 0.86254 2.36787 -0.22525 0.41562  -0.12257 66  GLU B CB  
6492 C CG  . GLU F 53  ? 1.87168 0.84869 2.36693 -0.22383 0.39127  -0.13488 66  GLU B CG  
6493 C CD  . GLU F 53  ? 1.92178 0.82349 2.44824 -0.23475 0.44526  -0.10383 66  GLU B CD  
6494 O OE1 . GLU F 53  ? 1.99707 0.82766 2.46293 -0.22099 0.50943  -0.07223 66  GLU B OE1 
6495 O OE2 . GLU F 53  ? 1.91903 0.82954 2.52722 -0.25414 0.42237  -0.11167 66  GLU B OE2 
6496 N N   . LEU F 54  ? 1.88818 0.93705 2.51316 -0.22532 0.53328  -0.06631 67  LEU B N   
6497 C CA  . LEU F 54  ? 1.89031 0.95965 2.52351 -0.21510 0.56363  -0.05379 67  LEU B CA  
6498 C C   . LEU F 54  ? 1.96432 0.97582 2.46201 -0.18153 0.57005  -0.05630 67  LEU B C   
6499 O O   . LEU F 54  ? 2.04687 0.97745 2.44891 -0.16140 0.59143  -0.05040 67  LEU B O   
6500 C CB  . LEU F 54  ? 1.90775 0.96673 2.61879 -0.22435 0.63159  -0.02373 67  LEU B CB  
6501 C CG  . LEU F 54  ? 1.94578 1.00913 2.66576 -0.21009 0.68210  -0.00450 67  LEU B CG  
6502 C CD1 . LEU F 54  ? 1.89411 1.01638 2.76610 -0.23508 0.70918  0.00399  67  LEU B CD1 
6503 C CD2 . LEU F 54  ? 2.06942 1.04220 2.68346 -0.18112 0.74192  0.02115  67  LEU B CD2 
6504 N N   . TYR F 55  ? 1.94501 0.99494 2.43517 -0.17258 0.54846  -0.06734 68  TYR B N   
6505 C CA  . TYR F 55  ? 2.00641 1.00734 2.38636 -0.13934 0.54826  -0.07698 68  TYR B CA  
6506 C C   . TYR F 55  ? 2.10321 1.04356 2.43964 -0.11173 0.61129  -0.05373 68  TYR B C   
6507 O O   . TYR F 55  ? 2.10877 1.06723 2.51897 -0.12199 0.65537  -0.02913 68  TYR B O   
6508 C CB  . TYR F 55  ? 1.95395 1.00949 2.35663 -0.13962 0.51438  -0.09079 68  TYR B CB  
6509 C CG  . TYR F 55  ? 1.98050 1.00341 2.29042 -0.11411 0.48682  -0.11605 68  TYR B CG  
6510 C CD1 . TYR F 55  ? 1.95276 0.99048 2.23242 -0.12013 0.43819  -0.14237 68  TYR B CD1 
6511 C CD2 . TYR F 55  ? 2.03253 1.01533 2.29344 -0.08182 0.50652  -0.11808 68  TYR B CD2 
6512 C CE1 . TYR F 55  ? 1.96753 0.98134 2.17827 -0.09832 0.41222  -0.17078 68  TYR B CE1 
6513 C CE2 . TYR F 55  ? 2.04306 0.99852 2.23409 -0.05696 0.47618  -0.14855 68  TYR B CE2 
6514 C CZ  . TYR F 55  ? 2.00670 0.97826 2.17717 -0.06721 0.43025  -0.17513 68  TYR B CZ  
6515 O OH  . TYR F 55  ? 2.00991 0.95887 2.12514 -0.04354 0.40018  -0.21024 68  TYR B OH  
6516 N N   . ALA F 56  ? 2.08298 0.95411 2.29855 -0.07195 0.61462  -0.06457 69  ALA B N   
6517 C CA  . ALA F 56  ? 2.19655 1.00957 2.35258 -0.03353 0.67170  -0.04488 69  ALA B CA  
6518 C C   . ALA F 56  ? 2.18587 1.04439 2.39845 -0.02848 0.68362  -0.04033 69  ALA B C   
6519 O O   . ALA F 56  ? 2.11820 1.01737 2.35268 -0.03240 0.63959  -0.06246 69  ALA B O   
6520 C CB  . ALA F 56  ? 2.27583 1.00955 2.28642 0.01806  0.66098  -0.06700 69  ALA B CB  
6521 N N   . GLY F 57  ? 2.14652 0.99690 2.38395 -0.01894 0.74519  -0.01052 70  GLY B N   
6522 C CA  . GLY F 57  ? 2.15103 1.04579 2.44708 -0.01291 0.75996  -0.00573 70  GLY B CA  
6523 C C   . GLY F 57  ? 2.05567 1.03322 2.49566 -0.05885 0.75717  0.00275  70  GLY B C   
6524 O O   . GLY F 57  ? 2.08813 1.09681 2.58709 -0.05504 0.79033  0.01517  70  GLY B O   
6525 N N   . VAL F 58  ? 1.98512 1.00142 2.48123 -0.09669 0.71557  -0.00759 71  VAL B N   
6526 C CA  . VAL F 58  ? 1.89184 0.98850 2.52175 -0.13183 0.70489  -0.00633 71  VAL B CA  
6527 C C   . VAL F 58  ? 1.92218 1.02467 2.62905 -0.14351 0.76667  0.01801  71  VAL B C   
6528 O O   . VAL F 58  ? 1.97064 1.02170 2.64797 -0.14473 0.80304  0.03523  71  VAL B O   
6529 C CB  . VAL F 58  ? 1.79323 0.92729 2.45930 -0.16137 0.64940  -0.02330 71  VAL B CB  
6530 C CG1 . VAL F 58  ? 1.71090 0.92780 2.50623 -0.18626 0.63194  -0.02761 71  VAL B CG1 
6531 C CG2 . VAL F 58  ? 1.77267 0.90203 2.36513 -0.15065 0.59689  -0.04462 71  VAL B CG2 
6532 N N   . PRO F 59  ? 1.90745 1.06836 2.71439 -0.15125 0.78284  0.02058  72  PRO B N   
6533 C CA  . PRO F 59  ? 1.94357 1.11420 2.83286 -0.16140 0.84836  0.04234  72  PRO B CA  
6534 C C   . PRO F 59  ? 1.86638 1.04763 2.84120 -0.19860 0.85006  0.04490  72  PRO B C   
6535 O O   . PRO F 59  ? 1.80312 1.01958 2.81798 -0.21903 0.79153  0.02262  72  PRO B O   
6536 C CB  . PRO F 59  ? 1.92515 1.16994 2.91228 -0.16276 0.84394  0.03150  72  PRO B CB  
6537 C CG  . PRO F 59  ? 1.94269 1.18099 2.84910 -0.13648 0.80043  0.01684  72  PRO B CG  
6538 C CD  . PRO F 59  ? 1.88434 1.09292 2.71621 -0.14225 0.74982  0.00549  72  PRO B CD  
6539 N N   . SER F 60  ? 1.96223 1.11201 2.96690 -0.20492 0.91923  0.07310  74  SER B N   
6540 C CA  . SER F 60  ? 1.93705 1.09068 3.03958 -0.24161 0.92738  0.07732  74  SER B CA  
6541 C C   . SER F 60  ? 1.85231 1.10020 3.12125 -0.27127 0.89081  0.04881  74  SER B C   
6542 O O   . SER F 60  ? 1.82890 1.09118 3.17560 -0.29808 0.86268  0.03550  74  SER B O   
6543 C CB  . SER F 60  ? 2.03387 1.14065 3.15467 -0.24353 1.01934  0.11828  74  SER B CB  
6544 O OG  . SER F 60  ? 2.12257 1.14498 3.07936 -0.20290 1.05596  0.14372  74  SER B OG  
6545 N N   . ARG F 61  ? 1.81108 1.12177 3.13479 -0.26229 0.88667  0.03566  75  ARG B N   
6546 C CA  . ARG F 61  ? 1.73829 1.13774 3.21367 -0.28143 0.84894  0.00389  75  ARG B CA  
6547 C C   . ARG F 61  ? 1.67040 1.09697 3.13350 -0.28458 0.76243  -0.02650 75  ARG B C   
6548 O O   . ARG F 61  ? 1.61998 1.11170 3.20418 -0.29761 0.72425  -0.05554 75  ARG B O   
6549 C CB  . ARG F 61  ? 1.71652 1.16945 3.23059 -0.26355 0.85799  -0.00520 75  ARG B CB  
6550 C CG  . ARG F 61  ? 1.66067 1.13821 3.11202 -0.24228 0.79109  -0.02616 75  ARG B CG  
6551 C CD  . ARG F 61  ? 1.73078 1.22402 3.16541 -0.21593 0.81172  -0.02401 75  ARG B CD  
6552 N NE  . ARG F 61  ? 1.81448 1.23887 3.10312 -0.18938 0.83289  -0.00225 75  ARG B NE  
6553 C CZ  . ARG F 61  ? 1.91024 1.32990 3.16141 -0.16044 0.85787  0.00324  75  ARG B CZ  
6554 N NH1 . ARG F 61  ? 1.93453 1.41341 3.27846 -0.15556 0.86830  -0.00910 75  ARG B NH1 
6555 N NH2 . ARG F 61  ? 1.99110 1.34614 3.10962 -0.13167 0.86892  0.01683  75  ARG B NH2 
6556 N N   . PHE F 62  ? 1.67194 1.05330 2.99457 -0.26947 0.73072  -0.02291 76  PHE B N   
6557 C CA  . PHE F 62  ? 1.61623 1.02223 2.91633 -0.27066 0.65515  -0.04756 76  PHE B CA  
6558 C C   . PHE F 62  ? 1.63456 1.00738 2.93298 -0.28776 0.64275  -0.04975 76  PHE B C   
6559 O O   . PHE F 62  ? 1.70051 0.99845 2.92861 -0.28846 0.68355  -0.02624 76  PHE B O   
6560 C CB  . PHE F 62  ? 1.60965 0.98829 2.77202 -0.24806 0.62798  -0.04512 76  PHE B CB  
6561 C CG  . PHE F 62  ? 1.60353 1.01328 2.76782 -0.23058 0.62640  -0.04616 76  PHE B CG  
6562 C CD1 . PHE F 62  ? 1.56432 1.03823 2.77468 -0.22674 0.57513  -0.06537 76  PHE B CD1 
6563 C CD2 . PHE F 62  ? 1.67210 1.04570 2.79122 -0.21351 0.67565  -0.02810 76  PHE B CD2 
6564 C CE1 . PHE F 62  ? 1.58681 1.08117 2.79556 -0.20942 0.57218  -0.06484 76  PHE B CE1 
6565 C CE2 . PHE F 62  ? 1.69236 1.09208 2.81589 -0.19587 0.66963  -0.03164 76  PHE B CE2 
6566 C CZ  . PHE F 62  ? 1.64587 1.10328 2.81528 -0.19563 0.61781  -0.04930 76  PHE B CZ  
6567 N N   . SER F 63  ? 1.61594 1.04256 2.98619 -0.29621 0.58328  -0.07943 77  SER B N   
6568 C CA  . SER F 63  ? 1.59725 0.99895 2.97818 -0.31055 0.56100  -0.08797 77  SER B CA  
6569 C C   . SER F 63  ? 1.55850 1.03024 2.98259 -0.30456 0.47944  -0.12614 77  SER B C   
6570 O O   . SER F 63  ? 1.54729 1.08798 3.02049 -0.29196 0.45018  -0.14376 77  SER B O   
6571 C CB  . SER F 63  ? 1.64062 1.02495 3.14029 -0.33588 0.61065  -0.07766 77  SER B CB  
6572 O OG  . SER F 63  ? 1.61245 1.06504 3.25456 -0.34224 0.62460  -0.09032 77  SER B OG  
6573 N N   . GLY F 64  ? 1.55150 1.00289 2.94340 -0.30764 0.44105  -0.13882 78  GLY B N   
6574 C CA  . GLY F 64  ? 1.52924 1.04804 2.95900 -0.29641 0.36324  -0.17634 78  GLY B CA  
6575 C C   . GLY F 64  ? 1.51023 1.02413 3.02255 -0.30973 0.33643  -0.19807 78  GLY B C   
6576 O O   . GLY F 64  ? 1.55131 0.99241 3.05525 -0.32867 0.37463  -0.17914 78  GLY B O   
6577 N N   . SER F 65  ? 1.49344 1.08414 3.08410 -0.29529 0.26786  -0.23879 79  SER B N   
6578 C CA  . SER F 65  ? 1.47212 1.06829 3.14189 -0.30049 0.22295  -0.26972 79  SER B CA  
6579 C C   . SER F 65  ? 1.48845 1.16433 3.14940 -0.26616 0.13528  -0.31096 79  SER B C   
6580 O O   . SER F 65  ? 1.51918 1.24734 3.13548 -0.24170 0.11796  -0.31215 79  SER B O   
6581 C CB  . SER F 65  ? 1.46599 1.07624 3.32113 -0.32240 0.24539  -0.28241 79  SER B CB  
6582 O OG  . SER F 65  ? 1.42798 1.11095 3.37418 -0.31110 0.24618  -0.29759 79  SER B OG  
6583 N N   . ARG F 66  ? 1.44033 1.12264 3.13935 -0.26148 0.08033  -0.34331 80  ARG B N   
6584 C CA  . ARG F 66  ? 1.46787 1.22132 3.13836 -0.22311 -0.00414 -0.38208 80  ARG B CA  
6585 C C   . ARG F 66  ? 1.42856 1.22431 3.24506 -0.21315 -0.06517 -0.43334 80  ARG B C   
6586 O O   . ARG F 66  ? 1.39685 1.13785 3.25772 -0.23604 -0.06449 -0.43814 80  ARG B O   
6587 C CB  . ARG F 66  ? 1.50675 1.22234 3.02124 -0.21698 -0.02203 -0.37299 80  ARG B CB  
6588 C CG  . ARG F 66  ? 1.53171 1.31690 3.02372 -0.17829 -0.10983 -0.41569 80  ARG B CG  
6589 C CD  . ARG F 66  ? 1.53771 1.26918 2.94600 -0.18268 -0.13377 -0.42288 80  ARG B CD  
6590 N NE  . ARG F 66  ? 1.56641 1.36891 2.92053 -0.14225 -0.20965 -0.45755 80  ARG B NE  
6591 C CZ  . ARG F 66  ? 1.59549 1.37946 2.82260 -0.13470 -0.22642 -0.45742 80  ARG B CZ  
6592 N NH1 . ARG F 66  ? 1.60831 1.30165 2.74327 -0.16130 -0.17770 -0.42772 80  ARG B NH1 
6593 N NH2 . ARG F 66  ? 1.61374 1.47512 2.80355 -0.09495 -0.29406 -0.49010 80  ARG B NH2 
6594 N N   . SER F 67  ? 1.34712 1.23589 3.24150 -0.17658 -0.11748 -0.47220 83  SER B N   
6595 C CA  . SER F 67  ? 1.31198 1.25469 3.34619 -0.15425 -0.19080 -0.53246 83  SER B CA  
6596 C C   . SER F 67  ? 1.34798 1.34733 3.30440 -0.10455 -0.27643 -0.56708 83  SER B C   
6597 O O   . SER F 67  ? 1.36649 1.45374 3.37106 -0.05428 -0.34045 -0.61056 83  SER B O   
6598 C CB  . SER F 67  ? 1.29280 1.30376 3.47449 -0.13741 -0.19911 -0.56282 83  SER B CB  
6599 O OG  . SER F 67  ? 1.28313 1.35560 3.59848 -0.10513 -0.28089 -0.62996 83  SER B OG  
6600 N N   . GLY F 68  ? 1.40473 1.35490 3.23519 -0.11387 -0.27780 -0.54923 84  GLY B N   
6601 C CA  . GLY F 68  ? 1.43792 1.44170 3.18435 -0.06845 -0.35259 -0.57902 84  GLY B CA  
6602 C C   . GLY F 68  ? 1.52251 1.57225 3.12904 -0.03930 -0.34811 -0.55528 84  GLY B C   
6603 O O   . GLY F 68  ? 1.55288 1.56438 3.02578 -0.05214 -0.32437 -0.52559 84  GLY B O   
6604 N N   . THR F 69  ? 1.40790 1.53922 3.04523 0.00289  -0.37276 -0.56993 85  THR B N   
6605 C CA  . THR F 69  ? 1.50514 1.67600 3.02189 0.02913  -0.35972 -0.54008 85  THR B CA  
6606 C C   . THR F 69  ? 1.54188 1.70304 3.07953 0.01559  -0.30079 -0.50640 85  THR B C   
6607 O O   . THR F 69  ? 1.62998 1.82388 3.08875 0.03972  -0.29025 -0.48180 85  THR B O   
6608 C CB  . THR F 69  ? 1.53062 1.80343 3.03139 0.10097  -0.43741 -0.57837 85  THR B CB  
6609 O OG1 . THR F 69  ? 1.52014 1.84862 3.11505 0.13780  -0.45748 -0.60194 85  THR B OG1 
6610 C CG2 . THR F 69  ? 1.44589 1.73893 2.98145 0.12195  -0.51150 -0.63085 85  THR B CG2 
6611 N N   . ASP F 70  ? 1.43403 1.55044 3.07824 -0.02192 -0.26115 -0.50405 86  ASP B N   
6612 C CA  . ASP F 70  ? 1.44669 1.55919 3.13406 -0.03235 -0.21099 -0.48198 86  ASP B CA  
6613 C C   . ASP F 70  ? 1.38882 1.40858 3.05381 -0.09186 -0.12828 -0.43634 86  ASP B C   
6614 O O   . ASP F 70  ? 1.31250 1.29059 3.07277 -0.12526 -0.10468 -0.44239 86  ASP B O   
6615 C CB  . ASP F 70  ? 1.41016 1.57168 3.26634 -0.01310 -0.24353 -0.53056 86  ASP B CB  
6616 C CG  . ASP F 70  ? 1.48990 1.73654 3.34688 0.05145  -0.29148 -0.55555 86  ASP B CG  
6617 O OD1 . ASP F 70  ? 1.57786 1.83525 3.30648 0.07207  -0.28046 -0.52143 86  ASP B OD1 
6618 O OD2 . ASP F 70  ? 1.44470 1.74534 3.43249 0.08362  -0.34042 -0.61009 86  ASP B OD2 
6619 N N   . PHE F 71  ? 1.49103 1.47799 3.03319 -0.10248 -0.08388 -0.39094 87  PHE B N   
6620 C CA  . PHE F 71  ? 1.44149 1.34272 2.94707 -0.14797 -0.00885 -0.34977 87  PHE B CA  
6621 C C   . PHE F 71  ? 1.43642 1.34007 2.99465 -0.15402 0.03716  -0.33250 87  PHE B C   
6622 O O   . PHE F 71  ? 1.50019 1.44765 3.03252 -0.12629 0.02580  -0.32824 87  PHE B O   
6623 C CB  . PHE F 71  ? 1.47380 1.33564 2.82411 -0.15385 0.00945  -0.31751 87  PHE B CB  
6624 C CG  . PHE F 71  ? 1.48705 1.34904 2.77591 -0.14584 -0.03537 -0.33623 87  PHE B CG  
6625 C CD1 . PHE F 71  ? 1.54234 1.48267 2.82421 -0.10585 -0.10218 -0.36592 87  PHE B CD1 
6626 C CD2 . PHE F 71  ? 1.45474 1.23841 2.68727 -0.17295 -0.01168 -0.32553 87  PHE B CD2 
6627 C CE1 . PHE F 71  ? 1.54915 1.49450 2.77427 -0.09593 -0.14504 -0.38609 87  PHE B CE1 
6628 C CE2 . PHE F 71  ? 1.46967 1.25241 2.64336 -0.16331 -0.05601 -0.34654 87  PHE B CE2 
6629 C CZ  . PHE F 71  ? 1.50890 1.37506 2.68185 -0.12616 -0.12335 -0.37786 87  PHE B CZ  
6630 N N   . THR F 72  ? 1.44184 1.29511 3.06412 -0.18861 0.09254  -0.31902 88  THR B N   
6631 C CA  . THR F 72  ? 1.43659 1.29673 3.11601 -0.19318 0.13599  -0.30682 88  THR B CA  
6632 C C   . THR F 72  ? 1.41266 1.19354 3.02045 -0.22338 0.21146  -0.26125 88  THR B C   
6633 O O   . THR F 72  ? 1.38459 1.10058 2.96227 -0.24829 0.24100  -0.24586 88  THR B O   
6634 C CB  . THR F 72  ? 1.39383 1.28699 3.25078 -0.19994 0.13442  -0.34020 88  THR B CB  
6635 O OG1 . THR F 72  ? 1.33374 1.16175 3.23459 -0.24181 0.18860  -0.32245 88  THR B OG1 
6636 C CG2 . THR F 72  ? 1.40215 1.36136 3.33847 -0.17024 0.05427  -0.39334 88  THR B CG2 
6637 N N   . LEU F 73  ? 1.45741 1.24333 3.03870 -0.21559 0.23943  -0.24215 89  LEU B N   
6638 C CA  . LEU F 73  ? 1.44478 1.16824 2.97299 -0.23410 0.30784  -0.20498 89  LEU B CA  
6639 C C   . LEU F 73  ? 1.43180 1.17508 3.08172 -0.24162 0.34587  -0.20997 89  LEU B C   
6640 O O   . LEU F 73  ? 1.45750 1.26303 3.17737 -0.22093 0.31988  -0.23264 89  LEU B O   
6641 C CB  . LEU F 73  ? 1.48243 1.19675 2.89417 -0.21796 0.30777  -0.18252 89  LEU B CB  
6642 C CG  . LEU F 73  ? 1.48062 1.13726 2.83617 -0.22692 0.36834  -0.15053 89  LEU B CG  
6643 C CD1 . LEU F 73  ? 1.46420 1.04515 2.76048 -0.24608 0.40728  -0.13296 89  LEU B CD1 
6644 C CD2 . LEU F 73  ? 1.51201 1.16496 2.77123 -0.21010 0.35609  -0.13484 89  LEU B CD2 
6645 N N   . THR F 74  ? 1.48766 1.17824 3.15900 -0.26775 0.40851  -0.18889 90  THR B N   
6646 C CA  . THR F 74  ? 1.47531 1.18407 3.27634 -0.28084 0.45376  -0.19269 90  THR B CA  
6647 C C   . THR F 74  ? 1.50619 1.16506 3.24029 -0.28475 0.52425  -0.15456 90  THR B C   
6648 O O   . THR F 74  ? 1.52025 1.10651 3.14723 -0.29163 0.55853  -0.12365 90  THR B O   
6649 C CB  . THR F 74  ? 1.44246 1.13863 3.35447 -0.30850 0.46883  -0.20195 90  THR B CB  
6650 O OG1 . THR F 74  ? 1.40754 1.15957 3.39671 -0.29798 0.39471  -0.24636 90  THR B OG1 
6651 C CG2 . THR F 74  ? 1.46445 1.17843 3.51716 -0.32645 0.52756  -0.20131 90  THR B CG2 
6652 N N   . ILE F 75  ? 1.44832 1.14764 3.24290 -0.27446 0.54117  -0.16104 91  ILE B N   
6653 C CA  . ILE F 75  ? 1.48538 1.15312 3.24322 -0.27280 0.60601  -0.13250 91  ILE B CA  
6654 C C   . ILE F 75  ? 1.50411 1.20286 3.41607 -0.29035 0.65521  -0.14012 91  ILE B C   
6655 O O   . ILE F 75  ? 1.47025 1.24134 3.51265 -0.28614 0.62718  -0.17732 91  ILE B O   
6656 C CB  . ILE F 75  ? 1.49841 1.18920 3.20199 -0.24433 0.58403  -0.13541 91  ILE B CB  
6657 C CG1 . ILE F 75  ? 1.51024 1.15491 3.05625 -0.23158 0.55817  -0.11689 91  ILE B CG1 
6658 C CG2 . ILE F 75  ? 1.54697 1.23315 3.26977 -0.23903 0.64381  -0.12153 91  ILE B CG2 
6659 C CD1 . ILE F 75  ? 1.55004 1.20462 3.04639 -0.20655 0.54411  -0.11398 91  ILE B CD1 
6660 N N   . SER F 76  ? 1.56349 1.20827 3.46216 -0.30726 0.72921  -0.10596 92  SER B N   
6661 C CA  . SER F 76  ? 1.59049 1.26114 3.64332 -0.32966 0.78616  -0.10703 92  SER B CA  
6662 C C   . SER F 76  ? 1.58641 1.30817 3.69660 -0.31460 0.81504  -0.11542 92  SER B C   
6663 O O   . SER F 76  ? 1.55317 1.35072 3.81326 -0.31642 0.79613  -0.15425 92  SER B O   
6664 C CB  . SER F 76  ? 1.67117 1.26503 3.66754 -0.34361 0.85716  -0.06146 92  SER B CB  
6665 O OG  . SER F 76  ? 1.71935 1.27565 3.63818 -0.33081 0.92617  -0.02593 92  SER B OG  
6666 N N   . SER F 77  ? 1.62228 1.30544 3.61680 -0.29531 0.85643  -0.08461 93  SER B N   
6667 C CA  . SER F 77  ? 1.62325 1.35067 3.65431 -0.27562 0.88097  -0.09263 93  SER B CA  
6668 C C   . SER F 77  ? 1.59161 1.31744 3.50723 -0.24221 0.82487  -0.10166 93  SER B C   
6669 O O   . SER F 77  ? 1.64271 1.30862 3.41373 -0.22512 0.83676  -0.07419 93  SER B O   
6670 C CB  . SER F 77  ? 1.69811 1.38775 3.69716 -0.27354 0.97429  -0.05218 93  SER B CB  
6671 O OG  . SER F 77  ? 1.74224 1.34568 3.56417 -0.25838 0.98807  -0.01586 93  SER B OG  
6672 N N   . LEU F 78  ? 1.53763 1.32538 3.51621 -0.23030 0.76204  -0.14074 94  LEU B N   
6673 C CA  . LEU F 78  ? 1.51784 1.30068 3.39513 -0.19914 0.71444  -0.14458 94  LEU B CA  
6674 C C   . LEU F 78  ? 1.58494 1.35698 3.42047 -0.17728 0.75578  -0.13136 94  LEU B C   
6675 O O   . LEU F 78  ? 1.60049 1.42666 3.53576 -0.16933 0.77410  -0.15211 94  LEU B O   
6676 C CB  . LEU F 78  ? 1.49195 1.34218 3.44503 -0.18296 0.64623  -0.18703 94  LEU B CB  
6677 C CG  . LEU F 78  ? 1.53631 1.37491 3.38337 -0.15201 0.59376  -0.18589 94  LEU B CG  
6678 C CD1 . LEU F 78  ? 1.52948 1.29546 3.22365 -0.15532 0.58956  -0.15043 94  LEU B CD1 
6679 C CD2 . LEU F 78  ? 1.53146 1.42456 3.43093 -0.13399 0.52364  -0.22147 94  LEU B CD2 
6680 N N   . GLN F 79  ? 1.65526 1.36125 3.34817 -0.16399 0.76653  -0.10214 95  GLN B N   
6681 C CA  . GLN F 79  ? 1.74165 1.43639 3.38672 -0.13571 0.79483  -0.09422 95  GLN B CA  
6682 C C   . GLN F 79  ? 1.76357 1.44489 3.32684 -0.11017 0.73406  -0.10184 95  GLN B C   
6683 O O   . GLN F 79  ? 1.71229 1.37173 3.21869 -0.11604 0.68650  -0.09920 95  GLN B O   
6684 C CB  . GLN F 79  ? 1.80359 1.43230 3.35194 -0.12954 0.85554  -0.05900 95  GLN B CB  
6685 C CG  . GLN F 79  ? 1.78677 1.40958 3.39590 -0.15662 0.91946  -0.04038 95  GLN B CG  
6686 C CD  . GLN F 79  ? 1.75917 1.45291 3.52738 -0.16828 0.96251  -0.05432 95  GLN B CD  
6687 O OE1 . GLN F 79  ? 1.68276 1.43142 3.57856 -0.19106 0.93590  -0.08190 95  GLN B OE1 
6688 N NE2 . GLN F 79  ? 1.80786 1.50385 3.57330 -0.14995 1.02917  -0.03805 95  GLN B NE2 
6689 N N   . PRO F 80  ? 1.78329 1.47714 3.34177 -0.08133 0.73473  -0.11064 96  PRO B N   
6690 C CA  . PRO F 80  ? 1.79438 1.47656 3.29527 -0.05904 0.67415  -0.11845 96  PRO B CA  
6691 C C   . PRO F 80  ? 1.77633 1.38793 3.14897 -0.05746 0.65284  -0.09597 96  PRO B C   
6692 O O   . PRO F 80  ? 1.73751 1.33925 3.07408 -0.05242 0.60027  -0.09714 96  PRO B O   
6693 C CB  . PRO F 80  ? 1.84510 1.54470 3.36124 -0.02719 0.68876  -0.13060 96  PRO B CB  
6694 C CG  . PRO F 80  ? 1.84027 1.58664 3.45538 -0.03585 0.75136  -0.13701 96  PRO B CG  
6695 C CD  . PRO F 80  ? 1.83750 1.55288 3.43616 -0.06531 0.79146  -0.11177 96  PRO B CD  
6696 N N   . GLU F 81  ? 1.87314 1.43477 3.17630 -0.05904 0.69282  -0.07607 97  GLU B N   
6697 C CA  . GLU F 81  ? 1.84021 1.33811 3.02996 -0.05579 0.66870  -0.06262 97  GLU B CA  
6698 C C   . GLU F 81  ? 1.74010 1.24272 2.92692 -0.08141 0.62629  -0.06187 97  GLU B C   
6699 O O   . GLU F 81  ? 1.70136 1.17188 2.82000 -0.07892 0.58933  -0.05686 97  GLU B O   
6700 C CB  . GLU F 81  ? 1.89245 1.33747 3.00881 -0.04878 0.71697  -0.04618 97  GLU B CB  
6701 C CG  . GLU F 81  ? 2.01100 1.46009 3.13579 -0.02242 0.77286  -0.04300 97  GLU B CG  
6702 C CD  . GLU F 81  ? 2.01668 1.50413 3.23147 -0.04336 0.82948  -0.03570 97  GLU B CD  
6703 O OE1 . GLU F 81  ? 2.03283 1.48321 3.21071 -0.05200 0.87054  -0.01540 97  GLU B OE1 
6704 O OE2 . GLU F 81  ? 2.00095 1.55333 3.32584 -0.04978 0.83310  -0.05131 97  GLU B OE2 
6705 N N   . ASP F 82  ? 1.76546 1.31020 3.03061 -0.10457 0.63032  -0.06850 98  ASP B N   
6706 C CA  . ASP F 82  ? 1.68302 1.23619 2.94343 -0.12408 0.59075  -0.07021 98  ASP B CA  
6707 C C   . ASP F 82  ? 1.67248 1.27016 2.96950 -0.11533 0.53759  -0.08363 98  ASP B C   
6708 O O   . ASP F 82  ? 1.64035 1.28072 2.99258 -0.12423 0.51137  -0.09682 98  ASP B O   
6709 C CB  . ASP F 82  ? 1.64647 1.22104 2.97605 -0.14861 0.61388  -0.07447 98  ASP B CB  
6710 C CG  . ASP F 82  ? 1.68408 1.21465 2.98638 -0.15328 0.67685  -0.05662 98  ASP B CG  
6711 O OD1 . ASP F 82  ? 1.72456 1.19684 2.92135 -0.13821 0.68981  -0.04189 98  ASP B OD1 
6712 O OD2 . ASP F 82  ? 1.68060 1.23349 3.06877 -0.16970 0.71383  -0.05766 98  ASP B OD2 
6713 N N   . PHE F 83  ? 1.63825 1.22473 2.90399 -0.09349 0.51895  -0.08131 99  PHE B N   
6714 C CA  . PHE F 83  ? 1.64836 1.26364 2.92846 -0.07952 0.47023  -0.08735 99  PHE B CA  
6715 C C   . PHE F 83  ? 1.61293 1.19268 2.80773 -0.08380 0.43986  -0.06740 99  PHE B C   
6716 O O   . PHE F 83  ? 1.60959 1.13786 2.73883 -0.08011 0.44431  -0.05363 99  PHE B O   
6717 C CB  . PHE F 83  ? 1.71073 1.33035 3.00975 -0.05254 0.46736  -0.09515 99  PHE B CB  
6718 C CG  . PHE F 83  ? 1.72932 1.34776 3.00392 -0.03308 0.42022  -0.09026 99  PHE B CG  
6719 C CD1 . PHE F 83  ? 1.75585 1.42514 3.08116 -0.01962 0.38735  -0.10595 99  PHE B CD1 
6720 C CD2 . PHE F 83  ? 1.72970 1.29364 2.93253 -0.02457 0.40854  -0.07061 99  PHE B CD2 
6721 C CE1 . PHE F 83  ? 1.79293 1.45496 3.08440 0.00400  0.34785  -0.09636 99  PHE B CE1 
6722 C CE2 . PHE F 83  ? 1.75610 1.31193 2.93735 -0.00779 0.37075  -0.05973 99  PHE B CE2 
6723 C CZ  . PHE F 83  ? 1.79437 1.39737 3.01349 0.00775  0.34246  -0.06976 99  PHE B CZ  
6724 N N   . ALA F 84  ? 1.53990 1.50013 2.60417 -0.12848 0.48115  -0.10623 100 ALA B N   
6725 C CA  . ALA F 84  ? 1.50985 1.42581 2.57031 -0.12499 0.51055  -0.10193 100 ALA B CA  
6726 C C   . ALA F 84  ? 1.59420 1.51124 2.59725 -0.06727 0.48626  -0.06783 100 ALA B C   
6727 O O   . ALA F 84  ? 1.66014 1.61529 2.63080 -0.02726 0.45164  -0.04996 100 ALA B O   
6728 C CB  . ALA F 84  ? 1.41056 1.33614 2.48164 -0.18851 0.48423  -0.14288 100 ALA B CB  
6729 N N   . THR F 85  ? 1.51667 1.39720 2.50992 -0.06227 0.50583  -0.06246 101 THR B N   
6730 C CA  . THR F 85  ? 1.58313 1.46944 2.51980 -0.01811 0.47553  -0.03944 101 THR B CA  
6731 C C   . THR F 85  ? 1.55761 1.45329 2.48253 -0.06426 0.42783  -0.07005 101 THR B C   
6732 O O   . THR F 85  ? 1.46910 1.34146 2.42742 -0.10944 0.44999  -0.09424 101 THR B O   
6733 C CB  . THR F 85  ? 1.59549 1.42990 2.52515 0.03777  0.54250  0.00117  101 THR B CB  
6734 O OG1 . THR F 85  ? 1.60493 1.43021 2.54760 0.08466  0.59126  0.03462  101 THR B OG1 
6735 C CG2 . THR F 85  ? 1.66018 1.51018 2.52530 0.08857  0.50881  0.02468  101 THR B CG2 
6736 N N   . TYR F 86  ? 1.53971 1.47450 2.42209 -0.05256 0.36338  -0.07211 102 TYR B N   
6737 C CA  . TYR F 86  ? 1.51369 1.46096 2.38632 -0.09408 0.31443  -0.09882 102 TYR B CA  
6738 C C   . TYR F 86  ? 1.56516 1.49893 2.39679 -0.06020 0.30412  -0.08486 102 TYR B C   
6739 O O   . TYR F 86  ? 1.63653 1.58333 2.43116 -0.00172 0.29962  -0.06064 102 TYR B O   
6740 C CB  . TYR F 86  ? 1.53034 1.52980 2.39902 -0.11687 0.25117  -0.11890 102 TYR B CB  
6741 C CG  . TYR F 86  ? 1.46184 1.47764 2.36974 -0.15721 0.25665  -0.13561 102 TYR B CG  
6742 C CD1 . TYR F 86  ? 1.49970 1.52181 2.42351 -0.13429 0.28469  -0.12303 102 TYR B CD1 
6743 C CD2 . TYR F 86  ? 1.33296 1.36000 2.26081 -0.21492 0.23660  -0.16205 102 TYR B CD2 
6744 C CE1 . TYR F 86  ? 1.44112 1.47888 2.40124 -0.17148 0.29088  -0.13994 102 TYR B CE1 
6745 C CE2 . TYR F 86  ? 1.25280 1.29921 2.21283 -0.24939 0.24292  -0.17713 102 TYR B CE2 
6746 C CZ  . TYR F 86  ? 1.31751 1.36807 2.29455 -0.22941 0.26975  -0.16776 102 TYR B CZ  
6747 O OH  . TYR F 86  ? 1.24419 1.31489 2.25368 -0.26383 0.27698  -0.18429 102 TYR B OH  
6748 N N   . TYR F 87  ? 1.55114 1.46474 2.38905 -0.09474 0.30079  -0.10125 103 TYR B N   
6749 C CA  . TYR F 87  ? 1.59675 1.49407 2.40068 -0.06948 0.29355  -0.09148 103 TYR B CA  
6750 C C   . TYR F 87  ? 1.56961 1.48845 2.36541 -0.10660 0.23587  -0.11717 103 TYR B C   
6751 O O   . TYR F 87  ? 1.45953 1.39086 2.28312 -0.15817 0.22003  -0.14035 103 TYR B O   
6752 C CB  . TYR F 87  ? 1.55005 1.39509 2.37447 -0.06963 0.35547  -0.08371 103 TYR B CB  
6753 C CG  . TYR F 87  ? 1.56935 1.37845 2.40530 -0.02629 0.42622  -0.05173 103 TYR B CG  
6754 C CD1 . TYR F 87  ? 1.63905 1.43255 2.43408 0.04134  0.44852  -0.01256 103 TYR B CD1 
6755 C CD2 . TYR F 87  ? 1.50058 1.29138 2.39069 -0.05124 0.47550  -0.06022 103 TYR B CD2 
6756 C CE1 . TYR F 87  ? 1.64091 1.39735 2.44781 0.08617  0.52105  0.02406  103 TYR B CE1 
6757 C CE2 . TYR F 87  ? 1.51183 1.26285 2.42066 -0.01128 0.54817  -0.02907 103 TYR B CE2 
6758 C CZ  . TYR F 87  ? 1.58161 1.31316 2.44838 0.05885  0.57241  0.01637  103 TYR B CZ  
6759 O OH  . TYR F 87  ? 1.58275 1.27145 2.46814 0.10477  0.65135  0.05504  103 TYR B OH  
6760 N N   . CYS F 88  ? 1.59163 1.51551 2.34947 -0.07726 0.20816  -0.11173 104 CYS B N   
6761 C CA  . CYS F 88  ? 1.57008 1.50641 2.32177 -0.10551 0.16049  -0.13250 104 CYS B CA  
6762 C C   . CYS F 88  ? 1.57694 1.48048 2.31397 -0.09598 0.17689  -0.12687 104 CYS B C   
6763 O O   . CYS F 88  ? 1.64968 1.53549 2.35953 -0.04806 0.20324  -0.10495 104 CYS B O   
6764 C CB  . CYS F 88  ? 1.65411 1.63206 2.38319 -0.08487 0.10816  -0.14152 104 CYS B CB  
6765 S SG  . CYS F 88  ? 1.76084 1.75449 2.43961 -0.00539 0.11263  -0.12094 104 CYS B SG  
6766 N N   . GLN F 89  ? 1.62575 1.52457 2.38056 -0.13894 0.16283  -0.14486 105 GLN B N   
6767 C CA  . GLN F 89  ? 1.61216 1.48348 2.36364 -0.13977 0.17845  -0.14492 105 GLN B CA  
6768 C C   . GLN F 89  ? 1.62074 1.50516 2.35531 -0.14743 0.12896  -0.15620 105 GLN B C   
6769 O O   . GLN F 89  ? 1.51222 1.41640 2.26447 -0.18482 0.09804  -0.17120 105 GLN B O   
6770 C CB  . GLN F 89  ? 1.46342 1.32571 2.25783 -0.18221 0.20953  -0.16011 105 GLN B CB  
6771 C CG  . GLN F 89  ? 1.44352 1.28044 2.24662 -0.18418 0.23586  -0.16396 105 GLN B CG  
6772 C CD  . GLN F 89  ? 1.27922 1.13311 2.12673 -0.23286 0.24564  -0.19176 105 GLN B CD  
6773 O OE1 . GLN F 89  ? 1.18437 1.07417 2.03928 -0.26403 0.21104  -0.20558 105 GLN B OE1 
6774 N NE2 . GLN F 89  ? 1.24226 1.07554 2.12277 -0.23834 0.29551  -0.20178 105 GLN B NE2 
6775 N N   . GLN F 90  ? 1.74759 1.62117 2.44920 -0.11003 0.12478  -0.14773 106 GLN B N   
6776 C CA  . GLN F 90  ? 1.75997 1.64421 2.45007 -0.11575 0.08078  -0.16129 106 GLN B CA  
6777 C C   . GLN F 90  ? 1.65914 1.52750 2.36771 -0.14812 0.08263  -0.16917 106 GLN B C   
6778 O O   . GLN F 90  ? 1.60287 1.48194 2.31677 -0.16713 0.04697  -0.18054 106 GLN B O   
6779 C CB  . GLN F 90  ? 1.88965 1.77561 2.53799 -0.06371 0.07466  -0.15440 106 GLN B CB  
6780 N N   . ARG F 91  ? 1.70444 1.55000 2.42782 -0.15351 0.12572  -0.16474 107 ARG B N   
6781 C CA  . ARG F 91  ? 1.60549 1.44672 2.35121 -0.18218 0.13030  -0.17640 107 ARG B CA  
6782 C C   . ARG F 91  ? 1.66452 1.49727 2.39019 -0.16940 0.10682  -0.17717 107 ARG B C   
6783 O O   . ARG F 91  ? 1.78755 1.61577 2.48083 -0.13603 0.09129  -0.17083 107 ARG B O   
6784 C CB  . ARG F 91  ? 1.43953 1.31237 2.21406 -0.22698 0.10866  -0.19121 107 ARG B CB  
6785 C CG  . ARG F 91  ? 1.34113 1.22656 2.14832 -0.25100 0.14012  -0.20070 107 ARG B CG  
6786 C CD  . ARG F 91  ? 1.33131 1.19632 2.16447 -0.25010 0.19419  -0.20835 107 ARG B CD  
6787 N NE  . ARG F 91  ? 1.34953 1.20189 2.18511 -0.24577 0.20205  -0.21318 107 ARG B NE  
6788 C CZ  . ARG F 91  ? 1.24291 1.12030 2.11097 -0.27416 0.20615  -0.23655 107 ARG B CZ  
6789 N NH1 . ARG F 91  ? 1.11876 1.04045 2.01573 -0.30794 0.20048  -0.25792 107 ARG B NH1 
6790 N NH2 . ARG F 91  ? 1.27634 1.14033 2.14848 -0.26636 0.21708  -0.24042 107 ARG B NH2 
6791 N N   . GLY F 92  ? 1.50744 1.34517 2.25370 -0.19491 0.10278  -0.18769 108 GLY B N   
6792 C CA  . GLY F 92  ? 1.56135 1.38787 2.29348 -0.18288 0.08660  -0.18820 108 GLY B CA  
6793 C C   . GLY F 92  ? 1.56247 1.37329 2.31092 -0.18318 0.12409  -0.19188 108 GLY B C   
6794 O O   . GLY F 92  ? 1.59451 1.38665 2.35150 -0.17259 0.16939  -0.18769 108 GLY B O   
6795 N N   . TRP F 93  ? 1.56232 1.38201 2.32227 -0.19642 0.10902  -0.20052 109 TRP B N   
6796 C CA  . TRP F 93  ? 1.57863 1.38580 2.35653 -0.19416 0.14303  -0.20742 109 TRP B CA  
6797 C C   . TRP F 93  ? 1.73463 1.50124 2.48549 -0.15428 0.17493  -0.19164 109 TRP B C   
6798 O O   . TRP F 93  ? 1.84028 1.59609 2.55177 -0.12528 0.15260  -0.18078 109 TRP B O   
6799 C CB  . TRP F 93  ? 1.55686 1.37507 2.33905 -0.19993 0.11785  -0.21365 109 TRP B CB  
6800 C CG  . TRP F 93  ? 1.40719 1.27012 2.22482 -0.23195 0.10744  -0.22981 109 TRP B CG  
6801 C CD1 . TRP F 93  ? 1.34812 1.23570 2.16549 -0.23970 0.07038  -0.22707 109 TRP B CD1 
6802 C CD2 . TRP F 93  ? 1.30066 1.19606 2.16047 -0.25679 0.13558  -0.25238 109 TRP B CD2 
6803 N NE1 . TRP F 93  ? 1.23026 1.16894 2.07960 -0.26295 0.07124  -0.24267 109 TRP B NE1 
6804 C CE2 . TRP F 93  ? 1.19499 1.14360 2.07225 -0.27577 0.10886  -0.26309 109 TRP B CE2 
6805 C CE3 . TRP F 93  ? 1.28444 1.17167 2.17293 -0.26355 0.18332  -0.26624 109 TRP B CE3 
6806 C CZ2 . TRP F 93  ? 1.09698 1.10142 2.01590 -0.30060 0.12301  -0.29219 109 TRP B CZ2 
6807 C CZ3 . TRP F 93  ? 1.15653 1.09173 2.09471 -0.29341 0.20062  -0.29865 109 TRP B CZ3 
6808 C CH2 . TRP F 93  ? 1.07993 1.07853 2.03141 -0.31147 0.16792  -0.31396 109 TRP B CH2 
6809 N N   . TYR F 94  ? 1.58410 1.33135 2.35853 -0.15102 0.23008  -0.19131 114 TYR B N   
6810 C CA  . TYR F 94  ? 1.70775 1.41442 2.45883 -0.10849 0.27273  -0.16927 114 TYR B CA  
6811 C C   . TYR F 94  ? 1.77649 1.47766 2.48862 -0.07585 0.27066  -0.14656 114 TYR B C   
6812 O O   . TYR F 94  ? 1.85270 1.53159 2.52765 -0.02883 0.29233  -0.12294 114 TYR B O   
6813 C CB  . TYR F 94  ? 1.79332 1.48565 2.51409 -0.08217 0.26106  -0.16302 114 TYR B CB  
6814 C CG  . TYR F 94  ? 1.74463 1.44412 2.50111 -0.10746 0.26258  -0.18329 114 TYR B CG  
6815 C CD1 . TYR F 94  ? 1.62987 1.34536 2.44531 -0.14365 0.28967  -0.20631 114 TYR B CD1 
6816 C CD2 . TYR F 94  ? 1.79275 1.49084 2.52708 -0.09508 0.23442  -0.18375 114 TYR B CD2 
6817 C CE1 . TYR F 94  ? 1.57578 1.31019 2.42536 -0.16383 0.28798  -0.22826 114 TYR B CE1 
6818 C CE2 . TYR F 94  ? 1.75032 1.45937 2.51732 -0.11505 0.23426  -0.20103 114 TYR B CE2 
6819 C CZ  . TYR F 94  ? 1.64093 1.37080 2.46456 -0.14822 0.25997  -0.22286 114 TYR B CZ  
6820 O OH  . TYR F 94  ? 1.59038 1.34198 2.44754 -0.16463 0.25751  -0.24292 114 TYR B OH  
6821 N N   . LEU F 95  ? 1.70113 1.42799 2.41881 -0.09611 0.24404  -0.15264 115 LEU B N   
6822 C CA  . LEU F 95  ? 1.76738 1.49992 2.44954 -0.06523 0.23336  -0.13531 115 LEU B CA  
6823 C C   . LEU F 95  ? 1.68182 1.42776 2.39303 -0.09065 0.24218  -0.13999 115 LEU B C   
6824 O O   . LEU F 95  ? 1.56545 1.33628 2.30576 -0.13421 0.21809  -0.16071 115 LEU B O   
6825 C CB  . LEU F 95  ? 1.80351 1.56276 2.45313 -0.05856 0.17078  -0.14281 115 LEU B CB  
6826 C CG  . LEU F 95  ? 1.83998 1.62308 2.46013 -0.03232 0.14679  -0.13692 115 LEU B CG  
6827 C CD1 . LEU F 95  ? 1.89529 1.66641 2.47568 0.02704  0.18076  -0.11127 115 LEU B CD1 
6828 C CD2 . LEU F 95  ? 1.85359 1.66490 2.46187 -0.03729 0.08806  -0.15635 115 LEU B CD2 
6829 N N   . PHE F 96  ? 1.84927 1.58061 2.55272 -0.06104 0.27941  -0.11916 116 PHE B N   
6830 C CA  . PHE F 96  ? 1.78160 1.52753 2.50838 -0.08051 0.28403  -0.12285 116 PHE B CA  
6831 C C   . PHE F 96  ? 1.85786 1.62199 2.54654 -0.04416 0.26313  -0.10542 116 PHE B C   
6832 O O   . PHE F 96  ? 1.82964 1.62654 2.52119 -0.06607 0.22040  -0.11902 116 PHE B O   
6833 C CB  . PHE F 96  ? 1.71511 1.43140 2.48845 -0.08902 0.35434  -0.12131 116 PHE B CB  
6834 C CG  . PHE F 96  ? 1.56252 1.29389 2.39186 -0.14545 0.35863  -0.15709 116 PHE B CG  
6835 C CD1 . PHE F 96  ? 1.53204 1.26580 2.37452 -0.16247 0.35222  -0.17438 116 PHE B CD1 
6836 C CD2 . PHE F 96  ? 1.44462 1.19698 2.31235 -0.17960 0.36584  -0.17589 116 PHE B CD2 
6837 C CE1 . PHE F 96  ? 1.38216 1.14535 2.27504 -0.21003 0.35256  -0.21039 116 PHE B CE1 
6838 C CE2 . PHE F 96  ? 1.29605 1.07719 2.21263 -0.22777 0.36699  -0.21312 116 PHE B CE2 
6839 C CZ  . PHE F 96  ? 1.26319 1.05355 2.19205 -0.24200 0.35927  -0.23089 116 PHE B CZ  
6840 N N   . THR F 97  ? 1.77004 1.51898 2.42407 0.01332  0.29307  -0.07558 117 THR B N   
6841 C CA  . THR F 97  ? 1.81288 1.59307 2.42720 0.05638  0.27056  -0.06109 117 THR B CA  
6842 C C   . THR F 97  ? 1.77633 1.57252 2.41792 0.03624  0.27182  -0.06442 117 THR B C   
6843 O O   . THR F 97  ? 1.76763 1.60082 2.41404 0.01108  0.22218  -0.08506 117 THR B O   
6844 C CB  . THR F 97  ? 1.84856 1.66937 2.43130 0.06080  0.20267  -0.08110 117 THR B CB  
6845 O OG1 . THR F 97  ? 1.87729 1.68293 2.43508 0.08110  0.20434  -0.07863 117 THR B OG1 
6846 C CG2 . THR F 97  ? 1.88619 1.75212 2.43229 0.10850  0.17958  -0.07405 117 THR B CG2 
6847 N N   . PHE F 98  ? 1.79418 1.55852 2.46084 0.04469  0.33445  -0.04514 118 PHE B N   
6848 C CA  . PHE F 98  ? 1.75698 1.53520 2.44998 0.02906  0.34009  -0.04759 118 PHE B CA  
6849 C C   . PHE F 98  ? 1.81166 1.62407 2.46273 0.08412  0.32277  -0.02602 118 PHE B C   
6850 O O   . PHE F 98  ? 1.85725 1.67101 2.46370 0.14579  0.33576  0.00181  118 PHE B O   
6851 C CB  . PHE F 98  ? 1.69835 1.43281 2.44036 0.01934  0.41579  -0.03849 118 PHE B CB  
6852 C CG  . PHE F 98  ? 1.58197 1.31567 2.38184 -0.05035 0.41802  -0.07691 118 PHE B CG  
6853 C CD1 . PHE F 98  ? 1.51760 1.29069 2.33168 -0.09275 0.37320  -0.10274 118 PHE B CD1 
6854 C CD2 . PHE F 98  ? 1.51532 1.21543 2.35741 -0.07135 0.46672  -0.08890 118 PHE B CD2 
6855 C CE1 . PHE F 98  ? 1.37617 1.16045 2.23745 -0.15058 0.37418  -0.13746 118 PHE B CE1 
6856 C CE2 . PHE F 98  ? 1.37507 1.09085 2.27050 -0.13216 0.46563  -0.13025 118 PHE B CE2 
6857 C CZ  . PHE F 98  ? 1.30228 1.06269 2.20340 -0.16953 0.41834  -0.15322 118 PHE B CZ  
6858 N N   . GLY F 99  ? 1.74350 1.58981 2.40972 0.06365  0.29421  -0.03984 119 GLY B N   
6859 C CA  . GLY F 99  ? 1.78596 1.67869 2.41975 0.11039  0.26951  -0.02859 119 GLY B CA  
6860 C C   . GLY F 99  ? 1.78749 1.66551 2.41290 0.16662  0.32806  0.01277  119 GLY B C   
6861 O O   . GLY F 99  ? 1.75286 1.57918 2.41142 0.15941  0.39261  0.02958  119 GLY B O   
6862 N N   . GLN F 100 ? 1.85144 1.78098 2.43563 0.22514  0.30567  0.02701  120 GLN B N   
6863 C CA  . GLN F 100 ? 1.85300 1.77884 2.42008 0.29274  0.35854  0.07337  120 GLN B CA  
6864 C C   . GLN F 100 ? 1.81328 1.71246 2.43375 0.26314  0.39809  0.07746  120 GLN B C   
6865 O O   . GLN F 100 ? 1.79802 1.65442 2.43119 0.29641  0.47034  0.11610  120 GLN B O   
6866 C CB  . GLN F 100 ? 1.88272 1.89059 2.39999 0.35630  0.31480  0.07778  120 GLN B CB  
6867 C CG  . GLN F 100 ? 1.88396 1.89996 2.37011 0.44298  0.36697  0.13306  120 GLN B CG  
6868 C CD  . GLN F 100 ? 1.90107 2.01668 2.33536 0.50986  0.31737  0.13100  120 GLN B CD  
6869 O OE1 . GLN F 100 ? 1.91243 2.08818 2.33751 0.48996  0.24599  0.08384  120 GLN B OE1 
6870 N NE2 . GLN F 100 ? 1.89764 2.03500 2.30202 0.59132  0.35748  0.18046  120 GLN B NE2 
6871 N N   . GLY F 101 ? 1.74049 1.66440 2.39472 0.20262  0.35494  0.03851  121 GLY B N   
6872 C CA  . GLY F 101 ? 1.70002 1.60905 2.40414 0.17083  0.38422  0.03513  121 GLY B CA  
6873 C C   . GLY F 101 ? 1.72082 1.69071 2.41478 0.19948  0.35379  0.03705  121 GLY B C   
6874 O O   . GLY F 101 ? 1.75367 1.76394 2.40261 0.26937  0.34507  0.06095  121 GLY B O   
6875 N N   . THR F 102 ? 1.96430 1.23816 2.75077 0.25751  0.76483  0.16234  122 THR B N   
6876 C CA  . THR F 102 ? 2.00451 1.26404 2.74758 0.29007  0.70863  0.14575  122 THR B CA  
6877 C C   . THR F 102 ? 1.94934 1.23638 2.74495 0.28084  0.73394  0.14896  122 THR B C   
6878 O O   . THR F 102 ? 1.84993 1.20652 2.74195 0.22616  0.73766  0.13698  122 THR B O   
6879 C CB  . THR F 102 ? 1.99157 1.28948 2.74962 0.26597  0.63083  0.11152  122 THR B CB  
6880 O OG1 . THR F 102 ? 2.04176 1.30988 2.75113 0.27294  0.60860  0.10941  122 THR B OG1 
6881 C CG2 . THR F 102 ? 2.03553 1.31922 2.74707 0.30420  0.57436  0.09248  122 THR B CG2 
6882 N N   . LYS F 103 ? 2.05300 1.28911 2.78789 0.33622  0.75314  0.16542  123 LYS B N   
6883 C CA  . LYS F 103 ? 2.01379 1.26729 2.78631 0.33672  0.77136  0.16726  123 LYS B CA  
6884 C C   . LYS F 103 ? 2.00596 1.29683 2.79064 0.33686  0.69965  0.13205  123 LYS B C   
6885 O O   . LYS F 103 ? 2.07336 1.34342 2.79058 0.38173  0.64444  0.11542  123 LYS B O   
6886 C CB  . LYS F 103 ? 2.07779 1.26783 2.77761 0.40346  0.81255  0.19571  123 LYS B CB  
6887 N N   . VAL F 104 ? 1.98902 1.34000 2.86371 0.28574  0.70047  0.11890  124 VAL B N   
6888 C CA  . VAL F 104 ? 1.97177 1.36341 2.86591 0.28021  0.63867  0.08554  124 VAL B CA  
6889 C C   . VAL F 104 ? 1.96101 1.35446 2.86663 0.30283  0.65340  0.08542  124 VAL B C   
6890 O O   . VAL F 104 ? 1.87132 1.30554 2.86165 0.25326  0.68223  0.08612  124 VAL B O   
6891 C CB  . VAL F 104 ? 1.86592 1.33733 2.85854 0.20222  0.61788  0.06502  124 VAL B CB  
6892 C CG1 . VAL F 104 ? 1.84719 1.35995 2.85701 0.19423  0.55452  0.03094  124 VAL B CG1 
6893 C CG2 . VAL F 104 ? 1.87871 1.34880 2.85711 0.18797  0.60561  0.06577  124 VAL B CG2 
6894 N N   . GLU F 105 ? 2.10794 1.46439 2.93312 0.38054  0.63406  0.08296  125 GLU B N   
6895 C CA  . GLU F 105 ? 2.10518 1.47338 2.93540 0.41426  0.63562  0.07525  125 GLU B CA  
6896 C C   . GLU F 105 ? 2.08872 1.51250 2.93771 0.41115  0.56706  0.03236  125 GLU B C   
6897 O O   . GLU F 105 ? 2.09770 1.53787 2.93473 0.39898  0.51642  0.01138  125 GLU B O   
6898 C CB  . GLU F 105 ? 2.18825 1.50991 2.93343 0.50525  0.65038  0.09117  125 GLU B CB  
6899 N N   . ILE F 106 ? 2.07859 1.53282 2.95778 0.42147  0.56790  0.01915  126 ILE B N   
6900 C CA  . ILE F 106 ? 2.05445 1.56931 2.95476 0.41994  0.51066  -0.02223 126 ILE B CA  
6901 C C   . ILE F 106 ? 2.09576 1.63351 2.95981 0.50353  0.49940  -0.03927 126 ILE B C   
6902 O O   . ILE F 106 ? 2.09688 1.61504 2.96581 0.52543  0.54558  -0.01945 126 ILE B O   
6903 C CB  . ILE F 106 ? 1.94082 1.50373 2.94881 0.32347  0.51682  -0.03204 126 ILE B CB  
6904 C CG1 . ILE F 106 ? 1.89356 1.46515 2.95159 0.31287  0.55793  -0.02581 126 ILE B CG1 
6905 C CG2 . ILE F 106 ? 1.88179 1.44552 2.94537 0.24655  0.54212  -0.01282 126 ILE B CG2 
6906 C CD1 . ILE F 106 ? 1.78060 1.41260 2.94418 0.22575  0.54851  -0.04673 126 ILE B CD1 
6907 N N   . LYS F 107 ? 2.03372 1.62304 2.86389 0.55322  0.43923  -0.07724 127 LYS B N   
6908 C CA  . LYS F 107 ? 2.06284 1.71012 2.87055 0.63815  0.42069  -0.10409 127 LYS B CA  
6909 C C   . LYS F 107 ? 1.99457 1.69635 2.86386 0.60891  0.42893  -0.12042 127 LYS B C   
6910 O O   . LYS F 107 ? 1.92661 1.65574 2.84862 0.53685  0.41406  -0.13354 127 LYS B O   
6911 C CB  . LYS F 107 ? 2.09897 1.81031 2.86432 0.69684  0.35423  -0.14503 127 LYS B CB  
6912 C CG  . LYS F 107 ? 2.16478 1.83264 2.87654 0.73788  0.33908  -0.13774 127 LYS B CG  
6913 C CD  . LYS F 107 ? 2.17746 1.92378 2.87020 0.78894  0.26961  -0.18680 127 LYS B CD  
6914 N N   . ARG F 108 ? 2.06387 1.78294 2.93404 0.66103  0.45376  -0.12015 128 ARG B N   
6915 C CA  . ARG F 108 ? 2.00084 1.75950 2.92937 0.63296  0.47115  -0.13054 128 ARG B CA  
6916 C C   . ARG F 108 ? 2.02084 1.87117 2.93605 0.72193  0.45262  -0.16455 128 ARG B C   
6917 O O   . ARG F 108 ? 2.00823 1.85812 2.94627 0.73658  0.48796  -0.15715 128 ARG B O   
6918 C CB  . ARG F 108 ? 1.97124 1.65267 2.93725 0.58283  0.53853  -0.08840 128 ARG B CB  
6919 N N   . THR F 109 ? 1.99483 1.93661 2.88059 0.78159  0.39792  -0.20487 129 THR B N   
6920 C CA  . THR F 109 ? 1.98722 2.05974 2.88617 0.85241  0.37395  -0.25035 129 THR B CA  
6921 C C   . THR F 109 ? 2.01427 2.07308 2.93340 0.90224  0.40964  -0.24425 129 THR B C   
6922 O O   . THR F 109 ? 1.98273 2.05007 2.92937 0.89277  0.44065  -0.23886 129 THR B O   
6923 C CB  . THR F 109 ? 1.91468 2.06044 2.84499 0.81100  0.37524  -0.25972 129 THR B CB  
6924 O OG1 . THR F 109 ? 1.88362 1.98232 2.86014 0.77520  0.42150  -0.24227 129 THR B OG1 
6925 C CG2 . THR F 109 ? 1.86708 1.98125 2.81494 0.72005  0.36448  -0.24694 129 THR B CG2 
6926 N N   . VAL F 110 ? 2.00921 2.03956 2.91621 0.95004  0.41373  -0.23577 130 VAL B N   
6927 C CA  . VAL F 110 ? 2.05179 2.01460 2.94208 0.98894  0.47048  -0.19249 130 VAL B CA  
6928 C C   . VAL F 110 ? 2.03173 2.03536 2.95805 1.00663  0.49908  -0.19958 130 VAL B C   
6929 O O   . VAL F 110 ? 2.00154 2.13040 2.98306 1.03061  0.46854  -0.25304 130 VAL B O   
6930 C CB  . VAL F 110 ? 2.09513 2.08396 2.97685 1.05275  0.46247  -0.19284 130 VAL B CB  
6931 C CG1 . VAL F 110 ? 2.15948 2.07085 2.98676 1.10282  0.52521  -0.13464 130 VAL B CG1 
6932 C CG2 . VAL F 110 ? 2.10866 2.06350 2.96000 1.03458  0.43107  -0.19007 130 VAL B CG2 
6933 N N   . ALA F 111 ? 2.10583 2.00883 3.01161 0.98990  0.56109  -0.14764 131 ALA B N   
6934 C CA  . ALA F 111 ? 2.08632 2.00833 3.02517 0.99698  0.59423  -0.14812 131 ALA B CA  
6935 C C   . ALA F 111 ? 2.21678 2.06249 3.11987 1.04394  0.65645  -0.09733 131 ALA B C   
6936 O O   . ALA F 111 ? 2.27971 2.02835 3.12914 1.04428  0.68912  -0.04862 131 ALA B O   
6937 C CB  . ALA F 111 ? 2.01975 1.89506 2.98815 0.91179  0.61632  -0.13422 131 ALA B CB  
6938 N N   . ALA F 112 ? 2.18811 2.08251 3.11778 1.08514  0.67485  -0.10848 132 ALA B N   
6939 C CA  . ALA F 112 ? 2.32405 2.14952 3.21605 1.13317  0.73731  -0.05875 132 ALA B CA  
6940 C C   . ALA F 112 ? 2.34131 2.05904 3.23477 1.07786  0.79888  -0.01363 132 ALA B C   
6941 O O   . ALA F 112 ? 2.25793 1.98806 3.20354 1.01720  0.79555  -0.03152 132 ALA B O   
6942 C CB  . ALA F 112 ? 2.37110 2.28912 3.29510 1.19552  0.73677  -0.08608 132 ALA B CB  
6943 N N   . PRO F 113 ? 2.44711 2.06130 3.28729 1.09366  0.85864  0.04602  133 PRO B N   
6944 C CA  . PRO F 113 ? 2.46558 1.98417 3.31930 1.03831  0.92458  0.08883  133 PRO B CA  
6945 C C   . PRO F 113 ? 2.50002 2.03588 3.39491 1.05046  0.95580  0.08378  133 PRO B C   
6946 O O   . PRO F 113 ? 2.55228 2.15408 3.44600 1.11898  0.94384  0.06293  133 PRO B O   
6947 C CB  . PRO F 113 ? 2.58252 2.00487 3.36183 1.06847  0.97867  0.14905  133 PRO B CB  
6948 C CG  . PRO F 113 ? 2.66308 2.13182 3.38991 1.16069  0.95475  0.14260  133 PRO B CG  
6949 C CD  . PRO F 113 ? 2.56043 2.14597 3.32625 1.16489  0.87310  0.07784  133 PRO B CD  
6950 N N   . SER F 114 ? 2.71194 1.57006 2.22983 0.15921  0.59121  0.36620  134 SER B N   
6951 C CA  . SER F 114 ? 2.87160 1.61418 2.27850 0.11234  0.67552  0.33403  134 SER B CA  
6952 C C   . SER F 114 ? 2.80617 1.59697 2.25757 0.14954  0.63572  0.34139  134 SER B C   
6953 O O   . SER F 114 ? 2.86938 1.60169 2.18580 0.11723  0.57467  0.35730  134 SER B O   
6954 C CB  . SER F 114 ? 3.07066 1.64025 2.22184 0.01798  0.68021  0.33485  134 SER B CB  
6955 O OG  . SER F 114 ? 3.04335 1.60996 2.10549 0.00960  0.55780  0.37844  134 SER B OG  
6956 N N   . VAL F 115 ? 2.70290 1.60234 2.34769 0.21867  0.67173  0.32843  135 VAL B N   
6957 C CA  . VAL F 115 ? 2.58826 1.55571 2.30652 0.26702  0.62649  0.34018  135 VAL B CA  
6958 C C   . VAL F 115 ? 2.74463 1.59499 2.33703 0.22279  0.68388  0.31609  135 VAL B C   
6959 O O   . VAL F 115 ? 2.88751 1.63893 2.41522 0.18023  0.78943  0.28023  135 VAL B O   
6960 C CB  . VAL F 115 ? 2.37328 1.48517 2.33100 0.35461  0.64994  0.33520  135 VAL B CB  
6961 C CG1 . VAL F 115 ? 2.20953 1.39729 2.24446 0.40726  0.59184  0.35336  135 VAL B CG1 
6962 C CG2 . VAL F 115 ? 2.22952 1.45102 2.30783 0.38996  0.60921  0.35144  135 VAL B CG2 
6963 N N   . PHE F 116 ? 2.57905 1.44180 2.13765 0.23053  0.61533  0.33317  136 PHE B N   
6964 C CA  . PHE F 116 ? 2.70653 1.47501 2.16000 0.19508  0.65800  0.31226  136 PHE B CA  
6965 C C   . PHE F 116 ? 2.55374 1.41232 2.11426 0.25432  0.60933  0.32572  136 PHE B C   
6966 O O   . PHE F 116 ? 2.36526 1.34432 2.03563 0.30662  0.52118  0.35544  136 PHE B O   
6967 C CB  . PHE F 116 ? 2.89717 1.54236 2.11775 0.10989  0.61994  0.31573  136 PHE B CB  
6968 C CG  . PHE F 116 ? 3.05787 1.58728 2.14219 0.04109  0.67867  0.29983  136 PHE B CG  
6969 C CD1 . PHE F 116 ? 3.14852 1.60408 2.22706 0.01676  0.80771  0.25906  136 PHE B CD1 
6970 C CD2 . PHE F 116 ? 3.10596 1.59876 2.07039 0.00139  0.60638  0.32486  136 PHE B CD2 
6971 C CE1 . PHE F 116 ? 3.28649 1.63274 2.23682 -0.05101 0.86657  0.24148  136 PHE B CE1 
6972 C CE2 . PHE F 116 ? 3.24758 1.62518 2.07682 -0.06445 0.66196  0.31152  136 PHE B CE2 
6973 C CZ  . PHE F 116 ? 3.33894 1.64279 2.15905 -0.09311 0.79420  0.26863  136 PHE B CZ  
6974 N N   . ILE F 117 ? 2.79808 1.58922 2.31283 0.23978  0.66690  0.30277  137 ILE B N   
6975 C CA  . ILE F 117 ? 2.67970 1.53001 2.26946 0.28567  0.63337  0.31145  137 ILE B CA  
6976 C C   . ILE F 117 ? 2.86484 1.60258 2.28364 0.22216  0.64292  0.29475  137 ILE B C   
6977 O O   . ILE F 117 ? 3.04560 1.65975 2.34459 0.16375  0.72823  0.26401  137 ILE B O   
6978 C CB  . ILE F 117 ? 2.53214 1.43403 2.29383 0.35538  0.70954  0.29849  137 ILE B CB  
6979 C CG1 . ILE F 117 ? 2.35464 1.36587 2.28433 0.41337  0.71124  0.30808  137 ILE B CG1 
6980 C CG2 . ILE F 117 ? 2.38699 1.35013 2.22104 0.40391  0.66515  0.31327  137 ILE B CG2 
6981 C CD1 . ILE F 117 ? 2.10689 1.26437 2.16712 0.47639  0.60784  0.34456  137 ILE B CD1 
6982 N N   . PHE F 118 ? 2.63906 1.42202 2.04914 0.23150  0.55781  0.31175  138 PHE B N   
6983 C CA  . PHE F 118 ? 2.80310 1.49670 2.06385 0.17452  0.55752  0.29473  138 PHE B CA  
6984 C C   . PHE F 118 ? 2.68391 1.43627 2.04064 0.22390  0.54491  0.29733  138 PHE B C   
6985 O O   . PHE F 118 ? 2.51644 1.38193 1.96770 0.26925  0.45476  0.32376  138 PHE B O   
6986 C CB  . PHE F 118 ? 2.89571 1.57449 2.01713 0.12097  0.45548  0.30921  138 PHE B CB  
6987 C CG  . PHE F 118 ? 3.05653 1.63547 2.02792 0.05380  0.47622  0.30288  138 PHE B CG  
6988 C CD1 . PHE F 118 ? 2.99429 1.60107 2.01888 0.07074  0.47935  0.31699  138 PHE B CD1 
6989 C CD2 . PHE F 118 ? 3.26725 1.72046 2.03886 -0.02944 0.49561  0.28134  138 PHE B CD2 
6990 C CE1 . PHE F 118 ? 3.14384 1.64801 2.01957 0.00525  0.50218  0.31113  138 PHE B CE1 
6991 C CE2 . PHE F 118 ? 3.40525 1.75836 2.02643 -0.09461 0.51507  0.27657  138 PHE B CE2 
6992 C CZ  . PHE F 118 ? 3.34583 1.72098 2.01683 -0.07741 0.51923  0.29212  138 PHE B CZ  
6993 N N   . PRO F 119 ? 2.83475 1.51042 2.16576 0.21432  0.63159  0.27025  139 PRO B N   
6994 C CA  . PRO F 119 ? 2.72496 1.44418 2.13667 0.25925  0.62284  0.27362  139 PRO B CA  
6995 C C   . PRO F 119 ? 2.81949 1.53036 2.12239 0.21500  0.54619  0.27268  139 PRO B C   
6996 O O   . PRO F 119 ? 2.97831 1.63894 2.13581 0.14786  0.50784  0.26667  139 PRO B O   
6997 C CB  . PRO F 119 ? 2.79373 1.41166 2.19346 0.25444  0.75026  0.24157  139 PRO B CB  
6998 C CG  . PRO F 119 ? 2.85147 1.42237 2.24292 0.23790  0.82270  0.22706  139 PRO B CG  
6999 C CD  . PRO F 119 ? 2.96829 1.52694 2.23741 0.17871  0.75474  0.23625  139 PRO B CD  
7000 N N   . PRO F 120 ? 2.71962 1.48408 2.09097 0.25141  0.51647  0.27889  140 PRO B N   
7001 C CA  . PRO F 120 ? 2.82028 1.56928 2.08675 0.20387  0.45814  0.26845  140 PRO B CA  
7002 C C   . PRO F 120 ? 3.05959 1.66528 2.15618 0.12613  0.53270  0.23035  140 PRO B C   
7003 O O   . PRO F 120 ? 3.10481 1.62841 2.19881 0.12671  0.64103  0.21021  140 PRO B O   
7004 C CB  . PRO F 120 ? 2.65602 1.47564 2.04100 0.26232  0.44185  0.27821  140 PRO B CB  
7005 C CG  . PRO F 120 ? 2.50792 1.34182 2.02943 0.33185  0.51652  0.28784  140 PRO B CG  
7006 C CD  . PRO F 120 ? 2.48571 1.33893 2.03604 0.33811  0.52208  0.29783  140 PRO B CD  
7007 N N   . SER F 121 ? 2.98659 1.56414 1.94235 0.05855  0.47325  0.21914  141 SER B N   
7008 C CA  . SER F 121 ? 3.19983 1.64773 1.98359 -0.02246 0.53365  0.18119  141 SER B CA  
7009 C C   . SER F 121 ? 3.21260 1.63148 2.00110 -0.02135 0.57720  0.15869  141 SER B C   
7010 O O   . SER F 121 ? 3.09716 1.60181 1.98250 0.02349  0.52542  0.17208  141 SER B O   
7011 C CB  . SER F 121 ? 3.33408 1.76948 1.96861 -0.09262 0.44757  0.17639  141 SER B CB  
7012 O OG  . SER F 121 ? 3.48654 1.84094 1.98810 -0.15894 0.47551  0.13957  141 SER B OG  
7013 N N   . ASP F 122 ? 3.28870 1.58029 1.96967 -0.07303 0.67837  0.12286  142 ASP B N   
7014 C CA  . ASP F 122 ? 3.31532 1.56041 1.97813 -0.08269 0.72692  0.09740  142 ASP B CA  
7015 C C   . ASP F 122 ? 3.36575 1.65943 1.97567 -0.11500 0.63538  0.08968  142 ASP B C   
7016 O O   . ASP F 122 ? 3.31259 1.62752 1.97423 -0.09180 0.63856  0.08432  142 ASP B O   
7017 C CB  . ASP F 122 ? 3.47185 1.56672 2.00226 -0.14883 0.84356  0.05552  142 ASP B CB  
7018 C CG  . ASP F 122 ? 3.64769 1.68172 1.98894 -0.24531 0.81533  0.03274  142 ASP B CG  
7019 O OD1 . ASP F 122 ? 3.65470 1.74029 1.97658 -0.25178 0.73366  0.05526  142 ASP B OD1 
7020 O OD2 . ASP F 122 ? 3.77339 1.70708 1.98370 -0.31447 0.87334  -0.00705 142 ASP B OD2 
7021 N N   . GLU F 123 ? 3.38650 1.69813 1.89488 -0.16782 0.55255  0.08840  143 GLU B N   
7022 C CA  . GLU F 123 ? 3.40065 1.77878 1.87782 -0.19271 0.45255  0.08103  143 GLU B CA  
7023 C C   . GLU F 123 ? 3.22422 1.74667 1.86476 -0.11765 0.36234  0.11554  143 GLU B C   
7024 O O   . GLU F 123 ? 3.19371 1.77105 1.86855 -0.11234 0.31985  0.10637  143 GLU B O   
7025 C CB  . GLU F 123 ? 3.46578 1.82954 1.79937 -0.26179 0.38061  0.07393  143 GLU B CB  
7026 C CG  . GLU F 123 ? 3.44973 1.88288 1.74729 -0.29197 0.27551  0.06028  143 GLU B CG  
7027 C CD  . GLU F 123 ? 3.51393 1.92698 1.66466 -0.35809 0.20304  0.05412  143 GLU B CD  
7028 O OE1 . GLU F 123 ? 3.58963 1.93071 1.66116 -0.38146 0.23462  0.06322  143 GLU B OE1 
7029 O OE2 . GLU F 123 ? 3.47649 1.94486 1.59006 -0.38718 0.11417  0.03917  143 GLU B OE2 
7030 N N   . GLN F 124 ? 3.35176 1.93697 2.09291 -0.06266 0.33436  0.15268  144 GLN B N   
7031 C CA  . GLN F 124 ? 3.15348 1.87587 2.05410 0.00865  0.25460  0.18476  144 GLN B CA  
7032 C C   . GLN F 124 ? 3.03751 1.77150 2.05046 0.06445  0.31300  0.18719  144 GLN B C   
7033 O O   . GLN F 124 ? 2.94807 1.76067 2.03214 0.08954  0.25972  0.19108  144 GLN B O   
7034 C CB  . GLN F 124 ? 3.02173 1.80527 2.00510 0.05332  0.21932  0.22155  144 GLN B CB  
7035 C CG  . GLN F 124 ? 2.82845 1.75629 1.93193 0.10082  0.10588  0.24933  144 GLN B CG  
7036 C CD  . GLN F 124 ? 2.60891 1.61109 1.86324 0.17511  0.10602  0.28511  144 GLN B CD  
7037 O OE1 . GLN F 124 ? 2.62509 1.57513 1.87819 0.18285  0.17320  0.29066  144 GLN B OE1 
7038 N NE2 . GLN F 124 ? 2.38621 1.51317 1.77338 0.22792  0.03288  0.30636  144 GLN B NE2 
7039 N N   . LEU F 125 ? 3.13612 1.78762 2.16186 0.08246  0.42366  0.18323  145 LEU B N   
7040 C CA  . LEU F 125 ? 3.02713 1.66874 2.14131 0.13263  0.48513  0.18466  145 LEU B CA  
7041 C C   . LEU F 125 ? 3.13225 1.73437 2.16872 0.08867  0.48923  0.15379  145 LEU B C   
7042 O O   . LEU F 125 ? 3.02717 1.67064 2.14195 0.12742  0.47962  0.16087  145 LEU B O   
7043 C CB  . LEU F 125 ? 3.02846 1.57070 2.14736 0.14794  0.60782  0.17760  145 LEU B CB  
7044 C CG  . LEU F 125 ? 2.91153 1.49088 2.12488 0.19678  0.62187  0.20303  145 LEU B CG  
7045 C CD1 . LEU F 125 ? 2.95425 1.42325 2.15155 0.19601  0.74895  0.18412  145 LEU B CD1 
7046 C CD2 . LEU F 125 ? 2.65614 1.35913 2.04887 0.28664  0.57385  0.24062  145 LEU B CD2 
7047 N N   . LYS F 126 ? 3.07058 1.59117 1.94832 0.00457  0.50424  0.11792  146 LYS B N   
7048 C CA  . LYS F 126 ? 3.17471 1.65970 1.96811 -0.04751 0.50648  0.08222  146 LYS B CA  
7049 C C   . LYS F 126 ? 3.13089 1.73746 1.97087 -0.04270 0.38982  0.08710  146 LYS B C   
7050 O O   . LYS F 126 ? 3.14343 1.75188 1.97747 -0.05613 0.39042  0.06595  146 LYS B O   
7051 C CB  . LYS F 126 ? 3.37777 1.76071 1.99099 -0.14090 0.53881  0.04305  146 LYS B CB  
7052 C CG  . LYS F 126 ? 3.48324 1.80784 1.99443 -0.20380 0.56517  -0.00181 146 LYS B CG  
7053 C CD  . LYS F 126 ? 3.64846 1.91662 1.98833 -0.29700 0.55130  -0.03561 146 LYS B CD  
7054 N N   . SER F 127 ? 3.14435 1.85143 2.03357 -0.02403 0.29210  0.11288  147 SER B N   
7055 C CA  . SER F 127 ? 3.06933 1.89911 2.01905 -0.01461 0.18090  0.11681  147 SER B CA  
7056 C C   . SER F 127 ? 2.87400 1.78331 1.97899 0.06000  0.17196  0.14168  147 SER B C   
7057 O O   . SER F 127 ? 2.80146 1.80534 1.95882 0.06501  0.09357  0.13863  147 SER B O   
7058 C CB  . SER F 127 ? 3.01376 1.92254 1.97293 -0.01396 0.08036  0.13803  147 SER B CB  
7059 O OG  . SER F 127 ? 3.16909 1.99725 1.97884 -0.08001 0.08856  0.12069  147 SER B OG  
7060 N N   . GLY F 128 ? 3.04596 1.92107 2.22551 0.11689  0.24832  0.16461  148 GLY B N   
7061 C CA  . GLY F 128 ? 2.82899 1.77887 2.15357 0.19108  0.23705  0.19287  148 GLY B CA  
7062 C C   . GLY F 128 ? 2.60725 1.66185 2.06198 0.25603  0.18384  0.23499  148 GLY B C   
7063 O O   . GLY F 128 ? 2.38735 1.52173 1.96630 0.31628  0.15904  0.25945  148 GLY B O   
7064 N N   . THR F 129 ? 3.07339 1.36014 2.41004 -0.10737 0.36015  0.57552  149 THR B N   
7065 C CA  . THR F 129 ? 2.96319 1.34290 2.35821 -0.05528 0.31230  0.59736  149 THR B CA  
7066 C C   . THR F 129 ? 2.92236 1.29874 2.40550 -0.01175 0.33750  0.57161  149 THR B C   
7067 O O   . THR F 129 ? 2.94852 1.31208 2.41913 -0.03494 0.38520  0.52107  149 THR B O   
7068 C CB  . THR F 129 ? 2.89558 1.40431 2.23463 -0.08011 0.28587  0.57996  149 THR B CB  
7069 O OG1 . THR F 129 ? 2.94749 1.45924 2.20036 -0.13382 0.27853  0.58736  149 THR B OG1 
7070 C CG2 . THR F 129 ? 2.79938 1.38645 2.18389 -0.03567 0.23606  0.60971  149 THR B CG2 
7071 N N   . ALA F 130 ? 2.90737 1.30236 2.47678 0.04621  0.30577  0.60441  150 ALA B N   
7072 C CA  . ALA F 130 ? 2.86807 1.26507 2.53410 0.09033  0.32718  0.58354  150 ALA B CA  
7073 C C   . ALA F 130 ? 2.76849 1.28108 2.45646 0.11154  0.29341  0.58017  150 ALA B C   
7074 O O   . ALA F 130 ? 2.72933 1.29978 2.40984 0.12050  0.24183  0.61659  150 ALA B O   
7075 C CB  . ALA F 130 ? 2.89298 1.21747 2.65837 0.14296  0.32232  0.62318  150 ALA B CB  
7076 N N   . SER F 131 ? 2.70061 1.24172 2.40708 0.11418  0.32625  0.53500  151 SER B N   
7077 C CA  . SER F 131 ? 2.61762 1.25024 2.34480 0.13367  0.30583  0.52791  151 SER B CA  
7078 C C   . SER F 131 ? 2.61205 1.23242 2.43338 0.16695  0.33771  0.50286  151 SER B C   
7079 O O   . SER F 131 ? 2.64513 1.22584 2.46074 0.15200  0.38994  0.46084  151 SER B O   
7080 C CB  . SER F 131 ? 2.59240 1.28323 2.22998 0.09948  0.31332  0.49939  151 SER B CB  
7081 O OG  . SER F 131 ? 2.59011 1.31535 2.15589 0.07305  0.28036  0.52113  151 SER B OG  
7082 N N   . VAL F 132 ? 2.49601 1.15786 2.40068 0.20617  0.30813  0.52470  152 VAL B N   
7083 C CA  . VAL F 132 ? 2.49027 1.16142 2.49217 0.23626  0.33557  0.49872  152 VAL B CA  
7084 C C   . VAL F 132 ? 2.44174 1.19070 2.41648 0.22942  0.32944  0.47982  152 VAL B C   
7085 O O   . VAL F 132 ? 2.41117 1.21694 2.34435 0.22333  0.28732  0.50307  152 VAL B O   
7086 C CB  . VAL F 132 ? 2.50457 1.18245 2.62642 0.28384  0.30723  0.53373  152 VAL B CB  
7087 C CG1 . VAL F 132 ? 2.50792 1.19413 2.74101 0.31198  0.34622  0.49813  152 VAL B CG1 
7088 C CG2 . VAL F 132 ? 2.55266 1.14850 2.68270 0.29390  0.29992  0.57170  152 VAL B CG2 
7089 N N   . VAL F 133 ? 2.48848 1.23250 2.48031 0.22730  0.37620  0.43660  153 VAL B N   
7090 C CA  . VAL F 133 ? 2.45474 1.24889 2.40585 0.21759  0.38324  0.41644  153 VAL B CA  
7091 C C   . VAL F 133 ? 2.46482 1.28197 2.51436 0.24007  0.40359  0.39447  153 VAL B C   
7092 O O   . VAL F 133 ? 2.49747 1.28222 2.63269 0.25598  0.43345  0.37732  153 VAL B O   
7093 C CB  . VAL F 133 ? 2.46413 1.22948 2.31886 0.18462  0.42333  0.38566  153 VAL B CB  
7094 C CG1 . VAL F 133 ? 2.44424 1.23743 2.26905 0.18089  0.44578  0.36273  153 VAL B CG1 
7095 C CG2 . VAL F 133 ? 2.45480 1.22882 2.21295 0.15977  0.39673  0.40578  153 VAL B CG2 
7096 N N   . CYS F 134 ? 2.37114 1.24377 2.41069 0.23941  0.39225  0.39152  154 CYS B N   
7097 C CA  . CYS F 134 ? 2.39548 1.29772 2.51971 0.25141  0.41481  0.36526  154 CYS B CA  
7098 C C   . CYS F 134 ? 2.38098 1.28817 2.42985 0.23104  0.44278  0.34181  154 CYS B C   
7099 O O   . CYS F 134 ? 2.35133 1.28464 2.33121 0.22332  0.41700  0.35987  154 CYS B O   
7100 C CB  . CYS F 134 ? 2.41786 1.39037 2.62782 0.27219  0.36630  0.39076  154 CYS B CB  
7101 S SG  . CYS F 134 ? 2.47579 1.50058 2.82383 0.28785  0.39151  0.35637  154 CYS B SG  
7102 N N   . LEU F 135 ? 2.40519 1.28100 2.46498 0.22229  0.49895  0.30229  155 LEU B N   
7103 C CA  . LEU F 135 ? 2.40200 1.26182 2.38047 0.20258  0.53446  0.28204  155 LEU B CA  
7104 C C   . LEU F 135 ? 2.43607 1.32500 2.48161 0.20274  0.55734  0.25636  155 LEU B C   
7105 O O   . LEU F 135 ? 2.47360 1.37793 2.62852 0.21146  0.57474  0.23355  155 LEU B O   
7106 C CB  . LEU F 135 ? 2.42512 1.22448 2.34585 0.18203  0.58497  0.25538  155 LEU B CB  
7107 C CG  . LEU F 135 ? 2.43679 1.20996 2.26868 0.16166  0.62588  0.23786  155 LEU B CG  
7108 C CD1 . LEU F 135 ? 2.39125 1.18031 2.12473 0.16452  0.59454  0.27151  155 LEU B CD1 
7109 C CD2 . LEU F 135 ? 2.48168 1.20212 2.25741 0.13536  0.67307  0.21109  155 LEU B CD2 
7110 N N   . LEU F 136 ? 2.40996 1.30709 2.39431 0.19279  0.56031  0.25839  156 LEU B N   
7111 C CA  . LEU F 136 ? 2.45554 1.37297 2.48466 0.18283  0.58941  0.22976  156 LEU B CA  
7112 C C   . LEU F 136 ? 2.45252 1.31066 2.37491 0.16382  0.63753  0.21715  156 LEU B C   
7113 O O   . LEU F 136 ? 2.42087 1.26874 2.25937 0.16461  0.62493  0.23984  156 LEU B O   
7114 C CB  . LEU F 136 ? 2.47025 1.45201 2.52880 0.18565  0.54646  0.24617  156 LEU B CB  
7115 C CG  . LEU F 136 ? 2.51056 1.57060 2.68061 0.19988  0.49654  0.25926  156 LEU B CG  
7116 C CD1 . LEU F 136 ? 2.46818 1.52462 2.63509 0.21991  0.44961  0.29841  156 LEU B CD1 
7117 C CD2 . LEU F 136 ? 2.55009 1.66348 2.70864 0.18567  0.47115  0.26478  156 LEU B CD2 
7118 N N   . ASN F 137 ? 2.58052 1.39741 2.50380 0.14738  0.69437  0.18268  157 ASN B N   
7119 C CA  . ASN F 137 ? 2.58701 1.33858 2.39389 0.12925  0.73817  0.17878  157 ASN B CA  
7120 C C   . ASN F 137 ? 2.63946 1.37778 2.46708 0.10776  0.78879  0.14433  157 ASN B C   
7121 O O   . ASN F 137 ? 2.67984 1.45795 2.62056 0.10050  0.80513  0.10919  157 ASN B O   
7122 C CB  . ASN F 137 ? 2.60294 1.30688 2.36037 0.11588  0.76879  0.16715  157 ASN B CB  
7123 C CG  . ASN F 137 ? 2.61283 1.25704 2.22905 0.10124  0.79684  0.17968  157 ASN B CG  
7124 O OD1 . ASN F 137 ? 2.58706 1.22277 2.13634 0.11230  0.78246  0.20908  157 ASN B OD1 
7125 N ND2 . ASN F 137 ? 2.65854 1.26050 2.22645 0.07672  0.83743  0.15910  157 ASN B ND2 
7126 N N   . ASN F 138 ? 2.62790 1.31067 2.34796 0.09808  0.81515  0.15505  158 ASN B N   
7127 C CA  . ASN F 138 ? 2.68407 1.32968 2.39570 0.07008  0.87534  0.12225  158 ASN B CA  
7128 C C   . ASN F 138 ? 2.71570 1.43064 2.54528 0.06117  0.87016  0.09320  158 ASN B C   
7129 O O   . ASN F 138 ? 2.75480 1.49808 2.67505 0.04109  0.90395  0.04849  158 ASN B O   
7130 C CB  . ASN F 138 ? 2.73212 1.33125 2.43173 0.04246  0.93644  0.08643  158 ASN B CB  
7131 C CG  . ASN F 138 ? 2.71953 1.27051 2.31342 0.04476  0.93549  0.11067  158 ASN B CG  
7132 O OD1 . ASN F 138 ? 2.73691 1.29129 2.36092 0.03504  0.94816  0.08911  158 ASN B OD1 
7133 N ND2 . ASN F 138 ? 2.70005 1.20908 2.17116 0.05678  0.92222  0.15437  158 ASN B ND2 
7134 N N   . PHE F 139 ? 2.62257 1.37335 2.45188 0.07396  0.82708  0.11728  159 PHE B N   
7135 C CA  . PHE F 139 ? 2.65714 1.48443 2.58359 0.06066  0.81402  0.09382  159 PHE B CA  
7136 C C   . PHE F 139 ? 2.65382 1.45390 2.51058 0.04878  0.82266  0.10131  159 PHE B C   
7137 O O   . PHE F 139 ? 2.61146 1.35537 2.36595 0.06686  0.81490  0.13760  159 PHE B O   
7138 C CB  . PHE F 139 ? 2.64814 1.57010 2.67179 0.08490  0.74292  0.11249  159 PHE B CB  
7139 C CG  . PHE F 139 ? 2.60094 1.53029 2.56544 0.10552  0.68761  0.15852  159 PHE B CG  
7140 C CD1 . PHE F 139 ? 2.53602 1.42374 2.42720 0.12837  0.66852  0.19343  159 PHE B CD1 
7141 C CD2 . PHE F 139 ? 2.62107 1.60710 2.60565 0.09695  0.65587  0.16286  159 PHE B CD2 
7142 C CE1 . PHE F 139 ? 2.48356 1.38546 2.32649 0.14465  0.62104  0.23143  159 PHE B CE1 
7143 C CE2 . PHE F 139 ? 2.58112 1.57485 2.51190 0.11206  0.60998  0.20086  159 PHE B CE2 
7144 C CZ  . PHE F 139 ? 2.50910 1.46131 2.37218 0.13729  0.59314  0.23503  159 PHE B CZ  
7145 N N   . TYR F 140 ? 1.89836 1.18435 3.34110 -0.17687 0.83552  -0.15166 160 TYR B N   
7146 C CA  . TYR F 140 ? 1.92445 1.25301 3.45533 -0.21950 0.75901  -0.24264 160 TYR B CA  
7147 C C   . TYR F 140 ? 2.06707 1.60827 3.79759 -0.24201 0.69927  -0.28324 160 TYR B C   
7148 O O   . TYR F 140 ? 2.11510 1.73132 3.95834 -0.23920 0.74221  -0.23411 160 TYR B O   
7149 C CB  . TYR F 140 ? 1.87740 1.10718 3.43802 -0.24297 0.79064  -0.23714 160 TYR B CB  
7150 N N   . PRO F 141 ? 1.82322 1.47210 3.59264 -0.25631 0.59651  -0.37563 161 PRO B N   
7151 C CA  . PRO F 141 ? 1.76348 1.35143 3.40305 -0.25417 0.53608  -0.44305 161 PRO B CA  
7152 C C   . PRO F 141 ? 1.79270 1.39524 3.22094 -0.20577 0.51429  -0.42946 161 PRO B C   
7153 O O   . PRO F 141 ? 1.84749 1.47437 3.22504 -0.17563 0.55438  -0.35999 161 PRO B O   
7154 C CB  . PRO F 141 ? 1.80788 1.54767 3.61092 -0.28381 0.43612  -0.54392 161 PRO B CB  
7155 C CG  . PRO F 141 ? 1.92786 1.85579 3.83987 -0.27007 0.41580  -0.52899 161 PRO B CG  
7156 C CD  . PRO F 141 ? 1.92386 1.78561 3.86398 -0.26534 0.52499  -0.42454 161 PRO B CD  
7157 N N   . ARG F 142 ? 1.88844 1.48244 3.19724 -0.19720 0.45091  -0.49490 162 ARG B N   
7158 C CA  . ARG F 142 ? 1.90450 1.50791 3.02087 -0.15658 0.43954  -0.47775 162 ARG B CA  
7159 C C   . ARG F 142 ? 2.07521 1.87917 3.20796 -0.13966 0.37592  -0.49379 162 ARG B C   
7160 O O   . ARG F 142 ? 2.11072 1.93064 3.10756 -0.10769 0.38328  -0.45354 162 ARG B O   
7161 C CB  . ARG F 142 ? 1.78271 1.29985 2.76162 -0.15182 0.40310  -0.54083 162 ARG B CB  
7162 N N   . GLU F 143 ? 1.77360 1.72603 3.07003 -0.15805 0.31443  -0.54972 163 GLU B N   
7163 C CA  . GLU F 143 ? 1.87074 2.01903 3.17932 -0.13556 0.24328  -0.57580 163 GLU B CA  
7164 C C   . GLU F 143 ? 1.86076 2.06655 3.21746 -0.11589 0.28481  -0.49401 163 GLU B C   
7165 O O   . GLU F 143 ? 1.81843 2.08560 3.35539 -0.13141 0.29094  -0.49236 163 GLU B O   
7166 C CB  . GLU F 143 ? 1.82082 2.10180 3.28505 -0.15514 0.15398  -0.67790 163 GLU B CB  
7167 C CG  . GLU F 143 ? 1.76036 2.24169 3.20590 -0.12236 0.06894  -0.71960 163 GLU B CG  
7168 C CD  . GLU F 143 ? 1.71100 2.31539 3.27185 -0.10644 0.06868  -0.68032 163 GLU B CD  
7169 O OE1 . GLU F 143 ? 1.69439 2.28394 3.43221 -0.13334 0.09984  -0.66993 163 GLU B OE1 
7170 O OE2 . GLU F 143 ? 1.68456 2.39845 3.15929 -0.06631 0.03941  -0.65841 163 GLU B OE2 
7171 N N   . ALA F 144 ? 1.95751 2.13814 3.15836 -0.08172 0.31476  -0.42668 164 ALA B N   
7172 C CA  . ALA F 144 ? 1.92274 2.12887 3.14055 -0.05619 0.35868  -0.34227 164 ALA B CA  
7173 C C   . ALA F 144 ? 1.92821 2.23252 3.02314 -0.01767 0.31907  -0.31980 164 ALA B C   
7174 O O   . ALA F 144 ? 1.94666 2.16839 2.87437 -0.00123 0.34544  -0.27943 164 ALA B O   
7175 C CB  . ALA F 144 ? 1.90949 1.93567 3.06113 -0.05140 0.45711  -0.26281 164 ALA B CB  
7176 N N   . LYS F 145 ? 1.82545 2.30469 2.99990 -0.00248 0.25266  -0.34975 165 LYS B N   
7177 C CA  . LYS F 145 ? 1.85436 2.42599 2.90403 0.03648  0.21493  -0.32435 165 LYS B CA  
7178 C C   . LYS F 145 ? 1.88912 2.38576 2.86313 0.06407  0.27840  -0.21881 165 LYS B C   
7179 O O   . LYS F 145 ? 1.87309 2.40846 2.94722 0.08005  0.29419  -0.18082 165 LYS B O   
7180 C CB  . LYS F 145 ? 1.80155 2.57029 2.95257 0.05643  0.13167  -0.37530 165 LYS B CB  
7181 N N   . VAL F 146 ? 2.10287 2.48848 2.90783 0.07037  0.31454  -0.17565 166 VAL B N   
7182 C CA  . VAL F 146 ? 2.10992 2.41429 2.83109 0.09867  0.36822  -0.08042 166 VAL B CA  
7183 C C   . VAL F 146 ? 2.17713 2.58662 2.81323 0.13240  0.32536  -0.04773 166 VAL B C   
7184 O O   . VAL F 146 ? 2.22066 2.69457 2.76782 0.13098  0.28162  -0.08064 166 VAL B O   
7185 C CB  . VAL F 146 ? 2.07735 2.20523 2.66971 0.09079  0.42595  -0.05350 166 VAL B CB  
7186 C CG1 . VAL F 146 ? 2.05423 2.09579 2.57098 0.12318  0.47624  0.03942  166 VAL B CG1 
7187 C CG2 . VAL F 146 ? 2.01931 2.03919 2.68364 0.06346  0.46690  -0.08348 166 VAL B CG2 
7188 N N   . SER F 147 ? 2.14393 2.56889 2.80364 0.16534  0.33966  0.01858  167 SER B N   
7189 C CA  . SER F 147 ? 2.20210 2.71571 2.79062 0.20422  0.30218  0.06200  167 SER B CA  
7190 C C   . SER F 147 ? 2.20711 2.59984 2.70054 0.22900  0.35522  0.15785  167 SER B C   
7191 O O   . SER F 147 ? 2.15515 2.44561 2.69656 0.23114  0.41078  0.18934  167 SER B O   
7192 C CB  . SER F 147 ? 2.19965 2.86293 2.92651 0.22951  0.25274  0.04082  167 SER B CB  
7193 O OG  . SER F 147 ? 2.19409 2.99531 2.97135 0.22042  0.18199  -0.04580 167 SER B OG  
7194 N N   . TRP F 148 ? 2.44777 2.85088 2.80758 0.24926  0.33891  0.20470  168 TRP B N   
7195 C CA  . TRP F 148 ? 2.45200 2.74292 2.72136 0.27402  0.37926  0.29479  168 TRP B CA  
7196 C C   . TRP F 148 ? 2.53506 2.91303 2.78938 0.32065  0.34078  0.34664  168 TRP B C   
7197 O O   . TRP F 148 ? 2.58777 3.09935 2.82512 0.33172  0.28345  0.32225  168 TRP B O   
7198 C CB  . TRP F 148 ? 2.42337 2.62401 2.54326 0.25447  0.40073  0.31498  168 TRP B CB  
7199 C CG  . TRP F 148 ? 2.31846 2.37407 2.42526 0.22821  0.45347  0.29717  168 TRP B CG  
7200 C CD1 . TRP F 148 ? 2.29388 2.33489 2.40132 0.19224  0.45426  0.22560  168 TRP B CD1 
7201 C CD2 . TRP F 148 ? 2.20941 2.11054 2.29417 0.24338  0.50928  0.34880  168 TRP B CD2 
7202 N NE1 . TRP F 148 ? 2.18511 2.06904 2.26686 0.18529  0.50766  0.23168  168 TRP B NE1 
7203 C CE2 . TRP F 148 ? 2.12103 1.91918 2.18832 0.21724  0.54238  0.30575  168 TRP B CE2 
7204 C CE3 . TRP F 148 ? 2.16424 2.00327 2.23927 0.28194  0.53063  0.42385  168 TRP B CE3 
7205 C CZ2 . TRP F 148 ? 1.98556 1.62476 2.02187 0.23120  0.59605  0.33508  168 TRP B CZ2 
7206 C CZ3 . TRP F 148 ? 2.00102 1.68500 2.05135 0.29387  0.58339  0.45072  168 TRP B CZ3 
7207 C CH2 . TRP F 148 ? 1.90807 1.49545 1.93794 0.26980  0.61582  0.40619  168 TRP B CH2 
7208 N N   . TYR F 149 ? 2.29187 2.59257 2.54675 0.35386  0.36958  0.41623  169 TYR B N   
7209 C CA  . TYR F 149 ? 2.38106 2.74846 2.62611 0.40545  0.33298  0.46793  169 TYR B CA  
7210 C C   . TYR F 149 ? 2.33924 2.56908 2.48523 0.43087  0.36740  0.55891  169 TYR B C   
7211 O O   . TYR F 149 ? 2.26472 2.40235 2.45864 0.44606  0.40791  0.58358  169 TYR B O   
7212 C CB  . TYR F 149 ? 2.37113 2.82878 2.78111 0.43051  0.31546  0.43926  169 TYR B CB  
7213 C CG  . TYR F 149 ? 2.31816 2.90738 2.84486 0.40323  0.27799  0.34487  169 TYR B CG  
7214 C CD1 . TYR F 149 ? 2.34932 3.09221 2.87270 0.42213  0.20442  0.30851  169 TYR B CD1 
7215 C CD2 . TYR F 149 ? 2.23091 2.78653 2.86877 0.36186  0.31422  0.29188  169 TYR B CD2 
7216 C CE1 . TYR F 149 ? 2.28576 3.14867 2.92187 0.40024  0.16286  0.21491  169 TYR B CE1 
7217 C CE2 . TYR F 149 ? 2.18578 2.85347 2.93879 0.33500  0.27648  0.20449  169 TYR B CE2 
7218 C CZ  . TYR F 149 ? 2.21097 3.03401 2.96707 0.35427  0.19814  0.16279  169 TYR B CZ  
7219 O OH  . TYR F 149 ? 2.15713 3.09332 3.03334 0.33128  0.15264  0.06869  169 TYR B OH  
7220 N N   . VAL F 150 ? 2.59606 2.81260 2.60725 0.43718  0.35176  0.60896  170 VAL B N   
7221 C CA  . VAL F 150 ? 2.44692 2.53483 2.36724 0.46131  0.37581  0.69738  170 VAL B CA  
7222 C C   . VAL F 150 ? 2.51663 2.66079 2.44402 0.52235  0.33481  0.74752  170 VAL B C   
7223 O O   . VAL F 150 ? 2.62187 2.86287 2.49050 0.54117  0.28791  0.76165  170 VAL B O   
7224 C CB  . VAL F 150 ? 2.36916 2.40335 2.14875 0.43142  0.38651  0.73037  170 VAL B CB  
7225 C CG1 . VAL F 150 ? 2.23038 2.12050 1.93334 0.45183  0.41103  0.81839  170 VAL B CG1 
7226 C CG2 . VAL F 150 ? 2.30800 2.29870 2.08884 0.37692  0.41988  0.66928  170 VAL B CG2 
7227 N N   . ASP F 151 ? 3.48820 1.47741 2.28451 0.56551  0.06661  0.31414  171 ASP B N   
7228 C CA  . ASP F 151 ? 3.45843 1.53258 2.41119 0.59467  0.14355  0.37816  171 ASP B CA  
7229 C C   . ASP F 151 ? 3.31875 1.73229 2.65681 0.52096  0.21437  0.41022  171 ASP B C   
7230 O O   . ASP F 151 ? 3.24221 1.88139 2.81213 0.43454  0.17542  0.43056  171 ASP B O   
7231 C CB  . ASP F 151 ? 3.46970 1.54455 2.39462 0.53864  0.01106  0.37393  171 ASP B CB  
7232 C CG  . ASP F 151 ? 3.71256 1.41355 2.25758 0.63494  -0.04664 0.35812  171 ASP B CG  
7233 O OD1 . ASP F 151 ? 3.95846 1.39624 2.24291 0.74471  0.01597  0.34562  171 ASP B OD1 
7234 O OD2 . ASP F 151 ? 3.74614 1.41292 2.25405 0.60341  -0.15663 0.36090  171 ASP B OD2 
7235 N N   . ASN F 152 ? 3.30441 1.74795 2.70940 0.55427  0.31155  0.41671  172 ASN B N   
7236 C CA  . ASN F 152 ? 3.20427 1.93773 2.96120 0.49095  0.37122  0.44572  172 ASN B CA  
7237 C C   . ASN F 152 ? 3.17516 2.18475 3.12883 0.32746  0.23396  0.38455  172 ASN B C   
7238 O O   . ASN F 152 ? 3.10272 2.35504 3.32802 0.25191  0.22989  0.41087  172 ASN B O   
7239 C CB  . ASN F 152 ? 3.13781 1.93714 3.07507 0.54218  0.48839  0.54715  172 ASN B CB  
7240 C CG  . ASN F 152 ? 3.18678 1.70742 2.90661 0.71830  0.62625  0.61442  172 ASN B CG  
7241 O OD1 . ASN F 152 ? 3.32013 1.56669 2.70575 0.79404  0.59699  0.57771  172 ASN B OD1 
7242 N ND2 . ASN F 152 ? 3.11137 1.69644 3.01677 0.78808  0.77441  0.71947  172 ASN B ND2 
7243 N N   . ALA F 153 ? 3.02660 1.99568 2.83559 0.27568  0.11988  0.30823  173 ALA B N   
7244 C CA  . ALA F 153 ? 3.01279 2.23616 2.98264 0.13589  -0.00381 0.25161  173 ALA B CA  
7245 C C   . ALA F 153 ? 3.01312 2.25257 2.96363 0.11043  -0.02248 0.19280  173 ALA B C   
7246 O O   . ALA F 153 ? 3.02724 2.06698 2.73498 0.14200  -0.06412 0.16449  173 ALA B O   
7247 C CB  . ALA F 153 ? 3.01417 2.21759 2.86195 0.08026  -0.15059 0.23136  173 ALA B CB  
7248 N N   . LEU F 154 ? 2.86957 2.34381 3.07741 0.04875  -0.00173 0.17501  174 LEU B N   
7249 C CA  . LEU F 154 ? 2.83723 2.35215 3.06566 0.02057  -0.01634 0.11836  174 LEU B CA  
7250 C C   . LEU F 154 ? 2.79868 2.30729 2.88441 -0.04335 -0.15207 0.06144  174 LEU B C   
7251 O O   . LEU F 154 ? 2.71319 2.34722 2.83145 -0.11394 -0.25232 0.05370  174 LEU B O   
7252 C CB  . LEU F 154 ? 2.71709 2.50011 3.25399 -0.04779 -0.00101 0.10151  174 LEU B CB  
7253 N N   . GLN F 155 ? 3.04358 2.41392 2.98298 -0.01929 -0.15627 0.03255  175 GLN B N   
7254 C CA  . GLN F 155 ? 2.96839 2.28677 2.74826 -0.06650 -0.27938 -0.00030 175 GLN B CA  
7255 C C   . GLN F 155 ? 2.78066 2.27837 2.69781 -0.13549 -0.31025 -0.05442 175 GLN B C   
7256 O O   . GLN F 155 ? 2.80399 2.29001 2.78623 -0.10747 -0.23122 -0.06964 175 GLN B O   
7257 C CB  . GLN F 155 ? 3.05401 2.04357 2.52933 0.01397  -0.27281 0.01546  175 GLN B CB  
7258 C CG  . GLN F 155 ? 3.15201 1.92495 2.44783 0.09746  -0.24568 0.06185  175 GLN B CG  
7259 C CD  . GLN F 155 ? 3.13199 1.96611 2.42324 0.04356  -0.35958 0.07435  175 GLN B CD  
7260 O OE1 . GLN F 155 ? 3.09201 1.87009 2.25528 -0.00184 -0.49162 0.06656  175 GLN B OE1 
7261 N NE2 . GLN F 155 ? 3.14348 2.09903 2.58978 0.04610  -0.31246 0.10442  175 GLN B NE2 
7262 N N   . SER F 156 ? 2.93854 2.60484 2.90413 -0.22046 -0.42400 -0.07797 176 SER B N   
7263 C CA  . SER F 156 ? 2.58876 2.42519 2.66544 -0.28083 -0.46046 -0.12849 176 SER B CA  
7264 C C   . SER F 156 ? 2.40514 2.17241 2.32001 -0.31282 -0.57121 -0.12257 176 SER B C   
7265 O O   . SER F 156 ? 2.44144 2.08628 2.19860 -0.30971 -0.64728 -0.08119 176 SER B O   
7266 C CB  . SER F 156 ? 2.16467 2.30997 2.47717 -0.35136 -0.48997 -0.15651 176 SER B CB  
7267 O OG  . SER F 156 ? 1.88271 2.18711 2.24270 -0.41029 -0.56244 -0.19671 176 SER B OG  
7268 N N   . GLY F 157 ? 2.36355 2.21232 2.33071 -0.34492 -0.58514 -0.15852 177 GLY B N   
7269 C CA  . GLY F 157 ? 2.25968 2.08358 2.11865 -0.38346 -0.68824 -0.14258 177 GLY B CA  
7270 C C   . GLY F 157 ? 2.47530 1.99909 2.07004 -0.34914 -0.73664 -0.09258 177 GLY B C   
7271 O O   . GLY F 157 ? 2.38938 1.88924 1.89998 -0.38189 -0.83274 -0.05706 177 GLY B O   
7272 N N   . ASN F 158 ? 2.44930 1.74365 1.91451 -0.27373 -0.66172 -0.08108 178 ASN B N   
7273 C CA  . ASN F 158 ? 2.67774 1.65208 1.86102 -0.22835 -0.70187 -0.04331 178 ASN B CA  
7274 C C   . ASN F 158 ? 2.95852 1.72917 2.03723 -0.15611 -0.59559 -0.05304 178 ASN B C   
7275 O O   . ASN F 158 ? 3.13946 1.62070 1.96154 -0.10434 -0.61447 -0.02616 178 ASN B O   
7276 C CB  . ASN F 158 ? 2.84675 1.68615 1.90474 -0.18828 -0.72794 -0.00997 178 ASN B CB  
7277 C CG  . ASN F 158 ? 3.01700 1.94678 2.21582 -0.14445 -0.60832 -0.02023 178 ASN B CG  
7278 O OD1 . ASN F 158 ? 3.07532 2.07872 2.40648 -0.11979 -0.49413 -0.04448 178 ASN B OD1 
7279 N ND2 . ASN F 158 ? 3.06950 1.99380 2.25246 -0.13629 -0.63886 0.00701  178 ASN B ND2 
7280 N N   . SER F 159 ? 2.76508 1.67251 2.03027 -0.14957 -0.49164 -0.08755 179 SER B N   
7281 C CA  . SER F 159 ? 2.91877 1.66372 2.12025 -0.07720 -0.38271 -0.08592 179 SER B CA  
7282 C C   . SER F 159 ? 2.82694 1.61004 2.07639 -0.11878 -0.39533 -0.10676 179 SER B C   
7283 O O   . SER F 159 ? 2.65602 1.67955 2.13383 -0.17321 -0.39099 -0.14464 179 SER B O   
7284 C CB  . SER F 159 ? 2.94413 1.80369 2.34076 -0.03127 -0.25267 -0.09193 179 SER B CB  
7285 O OG  . SER F 159 ? 2.80559 1.96141 2.46934 -0.09993 -0.26762 -0.12675 179 SER B OG  
7286 N N   . GLN F 160 ? 3.01505 1.55438 2.04493 -0.09123 -0.41212 -0.08207 180 GLN B N   
7287 C CA  . GLN F 160 ? 2.96600 1.51336 2.03371 -0.12372 -0.41141 -0.09143 180 GLN B CA  
7288 C C   . GLN F 160 ? 3.06011 1.46393 2.08316 -0.04386 -0.29079 -0.08203 180 GLN B C   
7289 O O   . GLN F 160 ? 3.19515 1.34621 1.97969 0.03163  -0.26659 -0.04953 180 GLN B O   
7290 C CB  . GLN F 160 ? 2.97191 1.37382 1.84650 -0.17135 -0.54028 -0.05736 180 GLN B CB  
7291 N N   . GLU F 161 ? 2.84476 1.41374 2.10097 -0.05429 -0.21511 -0.10835 181 GLU B N   
7292 C CA  . GLU F 161 ? 2.87420 1.36182 2.15144 0.01816  -0.09660 -0.09032 181 GLU B CA  
7293 C C   . GLU F 161 ? 2.85883 1.28814 2.11494 -0.01065 -0.10802 -0.08687 181 GLU B C   
7294 O O   . GLU F 161 ? 2.77717 1.33532 2.14017 -0.09255 -0.17509 -0.11287 181 GLU B O   
7295 C CB  . GLU F 161 ? 2.77965 1.49384 2.36300 0.02935  -0.00663 -0.10995 181 GLU B CB  
7296 C CG  . GLU F 161 ? 2.83538 1.51365 2.41166 0.10975  0.07348  -0.07482 181 GLU B CG  
7297 C CD  . GLU F 161 ? 2.74601 1.67708 2.63312 0.08891  0.11318  -0.09263 181 GLU B CD  
7298 O OE1 . GLU F 161 ? 2.73795 1.80790 2.69509 0.03179  0.04742  -0.12337 181 GLU B OE1 
7299 O OE2 . GLU F 161 ? 2.65716 1.64545 2.71965 0.13026  0.20544  -0.06856 181 GLU B OE2 
7300 N N   . SER F 162 ? 2.97104 1.20948 2.09046 0.06111  -0.03762 -0.04902 182 SER B N   
7301 C CA  . SER F 162 ? 2.96307 1.14620 2.07648 0.03823  -0.03511 -0.03726 182 SER B CA  
7302 C C   . SER F 162 ? 2.97401 1.09710 2.11721 0.12792  0.09468  -0.00174 182 SER B C   
7303 O O   . SER F 162 ? 3.07740 1.04580 2.05289 0.22412  0.15667  0.03408  182 SER B O   
7304 C CB  . SER F 162 ? 3.09584 1.03595 1.90393 0.01331  -0.13922 -0.00888 182 SER B CB  
7305 O OG  . SER F 162 ? 3.08838 0.99127 1.91044 -0.02224 -0.14360 0.00768  182 SER B OG  
7306 N N   . VAL F 163 ? 2.73974 0.99044 2.10268 0.10081  0.13628  -0.00621 183 VAL B N   
7307 C CA  . VAL F 163 ? 2.70711 0.96347 2.17707 0.17773  0.25827  0.03571  183 VAL B CA  
7308 C C   . VAL F 163 ? 2.72434 0.90195 2.16192 0.15973  0.26185  0.06073  183 VAL B C   
7309 O O   . VAL F 163 ? 2.64946 0.90341 2.17565 0.06720  0.19133  0.03092  183 VAL B O   
7310 C CB  . VAL F 163 ? 2.51638 1.04559 2.36451 0.16637  0.31259  0.01451  183 VAL B CB  
7311 C CG1 . VAL F 163 ? 2.49066 1.02302 2.44881 0.25982  0.43747  0.08100  183 VAL B CG1 
7312 C CG2 . VAL F 163 ? 2.50043 1.13354 2.40207 0.15555  0.28575  -0.01702 183 VAL B CG2 
7313 N N   . THR F 164 ? 2.84588 0.88114 2.16672 0.25144  0.34929  0.12156  184 THR B N   
7314 C CA  . THR F 164 ? 2.88789 0.85724 2.19213 0.24092  0.36455  0.15550  184 THR B CA  
7315 C C   . THR F 164 ? 2.64774 0.86996 2.34950 0.21279  0.42020  0.15348  184 THR B C   
7316 O O   . THR F 164 ? 2.46051 0.89232 2.43004 0.19363  0.43068  0.11905  184 THR B O   
7317 C CB  . THR F 164 ? 3.13976 0.91739 2.19557 0.35205  0.43668  0.22104  184 THR B CB  
7318 O OG1 . THR F 164 ? 3.09573 0.98373 2.34693 0.44375  0.56722  0.26854  184 THR B OG1 
7319 C CG2 . THR F 164 ? 3.35306 0.96596 2.07252 0.39289  0.38643  0.21105  184 THR B CG2 
7320 N N   . GLU F 165 ? 2.73081 0.92796 2.47370 0.21086  0.45136  0.19348  185 GLU B N   
7321 C CA  . GLU F 165 ? 2.53169 0.94149 2.64143 0.19470  0.50505  0.20551  185 GLU B CA  
7322 C C   . GLU F 165 ? 2.58268 0.97171 2.72361 0.31244  0.62829  0.29292  185 GLU B C   
7323 O O   . GLU F 165 ? 2.79725 0.98458 2.63495 0.39893  0.66843  0.34183  185 GLU B O   
7324 C CB  . GLU F 165 ? 2.47512 0.89311 2.64390 0.10809  0.45591  0.20078  185 GLU B CB  
7325 N N   . GLN F 166 ? 2.38830 0.99499 2.89928 0.31955  0.68288  0.31518  186 GLN B N   
7326 C CA  . GLN F 166 ? 2.43733 1.07241 3.02905 0.43039  0.79819  0.41493  186 GLN B CA  
7327 C C   . GLN F 166 ? 2.63523 1.12011 2.96326 0.47400  0.82576  0.47048  186 GLN B C   
7328 O O   . GLN F 166 ? 2.59310 1.07860 2.95683 0.40977  0.78985  0.46674  186 GLN B O   
7329 C CB  . GLN F 166 ? 2.20389 1.10334 3.24624 0.40475  0.82202  0.43724  186 GLN B CB  
7330 C CG  . GLN F 166 ? 2.01806 1.08488 3.33475 0.35699  0.78093  0.37679  186 GLN B CG  
7331 C CD  . GLN F 166 ? 1.88067 1.17131 3.55472 0.38365  0.82665  0.43921  186 GLN B CD  
7332 O OE1 . GLN F 166 ? 1.69759 1.16235 3.68757 0.31539  0.77441  0.39291  186 GLN B OE1 
7333 N NE2 . GLN F 166 ? 2.00029 1.28990 3.60887 0.47607  0.91554  0.54524  186 GLN B NE2 
7334 N N   . ASP F 167 ? 2.85778 1.21785 2.91615 0.58075  0.88542  0.51798  187 ASP B N   
7335 C CA  . ASP F 167 ? 3.07163 1.28676 2.86325 0.63227  0.91345  0.56488  187 ASP B CA  
7336 C C   . ASP F 167 ? 2.96679 1.34877 3.03073 0.64511  0.98050  0.63886  187 ASP B C   
7337 O O   . ASP F 167 ? 2.80597 1.40342 3.20301 0.66620  1.03823  0.68317  187 ASP B O   
7338 C CB  . ASP F 167 ? 3.32929 1.41028 2.81524 0.75516  0.97916  0.59909  187 ASP B CB  
7339 C CG  . ASP F 167 ? 3.54771 1.52076 2.81218 0.82970  1.03566  0.65665  187 ASP B CG  
7340 O OD1 . ASP F 167 ? 3.68081 1.48048 2.68885 0.78769  0.96167  0.62232  187 ASP B OD1 
7341 O OD2 . ASP F 167 ? 3.58162 1.65755 2.94376 0.92538  1.15069  0.74004  187 ASP B OD2 
7342 N N   . SER F 168 ? 3.05538 1.34643 2.98558 0.62308  0.96106  0.65453  188 SER B N   
7343 C CA  . SER F 168 ? 2.94567 1.39872 3.14048 0.62196  1.01290  0.72323  188 SER B CA  
7344 C C   . SER F 168 ? 3.00575 1.56808 3.28551 0.74621  1.14013  0.82329  188 SER B C   
7345 O O   . SER F 168 ? 2.83408 1.62158 3.46924 0.74142  1.18539  0.88543  188 SER B O   
7346 C CB  . SER F 168 ? 3.06998 1.38289 3.05219 0.58396  0.96944  0.72719  188 SER B CB  
7347 O OG  . SER F 168 ? 3.37997 1.45402 2.92165 0.66135  0.97767  0.73076  188 SER B OG  
7348 N N   . LYS F 169 ? 3.24602 1.66673 3.21631 0.85313  1.19557  0.84230  189 LYS B N   
7349 C CA  . LYS F 169 ? 3.33571 1.85405 3.35026 0.97502  1.32481  0.94687  189 LYS B CA  
7350 C C   . LYS F 169 ? 3.20827 1.90399 3.46799 0.99667  1.36730  0.97678  189 LYS B C   
7351 O O   . LYS F 169 ? 3.04073 1.97476 3.65913 0.98954  1.41219  1.05236  189 LYS B O   
7352 C CB  . LYS F 169 ? 3.68672 1.96487 3.23396 1.08752  1.37384  0.95585  189 LYS B CB  
7353 N N   . ASP F 170 ? 3.28696 1.87153 3.36188 1.01174  1.34312  0.92170  190 ASP B N   
7354 C CA  . ASP F 170 ? 3.19025 1.92714 3.46852 1.03072  1.38064  0.95506  190 ASP B CA  
7355 C C   . ASP F 170 ? 2.89527 1.80081 3.53589 0.91502  1.29677  0.90240  190 ASP B C   
7356 O O   . ASP F 170 ? 2.77040 1.85461 3.67762 0.90838  1.31846  0.94641  190 ASP B O   
7357 C CB  . ASP F 170 ? 3.39604 1.95542 3.34047 1.09625  1.39286  0.92235  190 ASP B CB  
7358 C CG  . ASP F 170 ? 3.43912 1.79617 3.13651 1.03016  1.27678  0.80176  190 ASP B CG  
7359 O OD1 . ASP F 170 ? 3.22680 1.65625 3.12435 0.92669  1.18965  0.73663  190 ASP B OD1 
7360 O OD2 . ASP F 170 ? 3.69727 1.82294 2.99520 1.08028  1.26970  0.77354  190 ASP B OD2 
7361 N N   . SER F 171 ? 2.79766 1.64345 3.44171 0.82068  1.19866  0.81054  191 SER B N   
7362 C CA  . SER F 171 ? 2.53763 1.52755 3.49751 0.71272  1.11671  0.74351  191 SER B CA  
7363 C C   . SER F 171 ? 2.50940 1.50380 3.46610 0.71130  1.09340  0.70091  191 SER B C   
7364 O O   . SER F 171 ? 2.30741 1.47034 3.57093 0.64909  1.05257  0.67413  191 SER B O   
7365 C CB  . SER F 171 ? 2.33399 1.58201 3.72108 0.67501  1.13278  0.80370  191 SER B CB  
7366 O OG  . SER F 171 ? 2.35985 1.61266 3.75658 0.67955  1.15997  0.85121  191 SER B OG  
7367 N N   . THR F 172 ? 2.72029 1.52795 3.32673 0.77747  1.11367  0.69271  192 THR B N   
7368 C CA  . THR F 172 ? 2.71999 1.49211 3.26195 0.77364  1.08340  0.64462  192 THR B CA  
7369 C C   . THR F 172 ? 2.79935 1.36325 3.05408 0.72319  0.99226  0.54552  192 THR B C   
7370 O O   . THR F 172 ? 2.91030 1.32741 2.95041 0.70785  0.96153  0.52823  192 THR B O   
7371 C CB  . THR F 172 ? 2.90204 1.63314 3.27852 0.88215  1.17307  0.71749  192 THR B CB  
7372 O OG1 . THR F 172 ? 3.17317 1.67702 3.14247 0.95195  1.19823  0.71917  192 THR B OG1 
7373 C CG2 . THR F 172 ? 2.84187 1.77577 3.49050 0.92270  1.26232  0.83386  192 THR B CG2 
7374 N N   . TYR F 173 ? 2.63052 1.54357 2.04778 0.07574  0.60772  0.09021  193 TYR B N   
7375 C CA  . TYR F 173 ? 2.59218 1.58694 1.93873 0.10610  0.52958  0.07708  193 TYR B CA  
7376 C C   . TYR F 173 ? 2.51993 1.57964 1.92716 0.10779  0.54253  0.08094  193 TYR B C   
7377 O O   . TYR F 173 ? 2.50598 1.54659 1.99600 0.09351  0.61128  0.09135  193 TYR B O   
7378 C CB  . TYR F 173 ? 2.60353 1.69712 2.02602 0.08697  0.43527  0.06141  193 TYR B CB  
7379 C CG  . TYR F 173 ? 2.69164 1.73151 2.09640 0.07895  0.41960  0.05011  193 TYR B CG  
7380 C CD1 . TYR F 173 ? 2.72015 1.73653 2.26740 0.03563  0.45608  0.04986  193 TYR B CD1 
7381 C CD2 . TYR F 173 ? 2.73750 1.75948 1.99529 0.11392  0.36408  0.03225  193 TYR B CD2 
7382 C CE1 . TYR F 173 ? 2.80207 1.76478 2.34360 0.02531  0.44203  0.03441  193 TYR B CE1 
7383 C CE2 . TYR F 173 ? 2.83007 1.79989 2.07639 0.10921  0.34494  0.01777  193 TYR B CE2 
7384 C CZ  . TYR F 173 ? 2.86523 1.80022 2.25408 0.06358  0.38514  0.01988  193 TYR B CZ  
7385 O OH  . TYR F 173 ? 2.93908 1.81559 2.32492 0.05620  0.36761  0.00080  193 TYR B OH  
7386 N N   . SER F 174 ? 2.48428 1.62219 1.85258 0.12422  0.47680  0.06952  194 SER B N   
7387 C CA  . SER F 174 ? 2.43316 1.63592 1.86460 0.12297  0.47306  0.07053  194 SER B CA  
7388 C C   . SER F 174 ? 2.40646 1.71090 1.85689 0.11478  0.38359  0.06522  194 SER B C   
7389 O O   . SER F 174 ? 2.40043 1.71835 1.73479 0.13271  0.33716  0.04918  194 SER B O   
7390 C CB  . SER F 174 ? 2.42266 1.57790 1.72563 0.16399  0.51741  0.05858  194 SER B CB  
7391 O OG  . SER F 174 ? 2.45954 1.52997 1.75389 0.17154  0.60644  0.06869  194 SER B OG  
7392 N N   . LEU F 175 ? 2.31539 1.69031 1.90792 0.09031  0.36104  0.07857  195 LEU B N   
7393 C CA  . LEU F 175 ? 2.30630 1.77440 1.93153 0.07842  0.28267  0.08428  195 LEU B CA  
7394 C C   . LEU F 175 ? 2.28028 1.77474 1.93212 0.07885  0.28354  0.09140  195 LEU B C   
7395 O O   . LEU F 175 ? 2.27418 1.73376 1.98039 0.08257  0.33634  0.09307  195 LEU B O   
7396 C CB  . LEU F 175 ? 2.33026 1.85607 2.10232 0.05339  0.24596  0.09661  195 LEU B CB  
7397 C CG  . LEU F 175 ? 2.34669 1.96981 2.13807 0.04596  0.16043  0.10509  195 LEU B CG  
7398 C CD1 . LEU F 175 ? 2.40558 2.06772 2.25936 0.03640  0.12200  0.09507  195 LEU B CD1 
7399 C CD2 . LEU F 175 ? 2.33133 2.00084 2.22554 0.03854  0.14320  0.13060  195 LEU B CD2 
7400 N N   . SER F 176 ? 2.28669 1.84299 1.90310 0.07344  0.22652  0.09400  196 SER B N   
7401 C CA  . SER F 176 ? 2.27960 1.85251 1.91691 0.06860  0.22629  0.10043  196 SER B CA  
7402 C C   . SER F 176 ? 2.28321 1.93215 1.95261 0.04806  0.15873  0.12501  196 SER B C   
7403 O O   . SER F 176 ? 2.27648 1.97152 1.85762 0.04562  0.11734  0.11501  196 SER B O   
7404 C CB  . SER F 176 ? 2.27659 1.82690 1.78521 0.08806  0.24905  0.06596  196 SER B CB  
7405 O OG  . SER F 176 ? 2.25141 1.84985 1.65363 0.08919  0.20223  0.04787  196 SER B OG  
7406 N N   . SER F 177 ? 2.22587 1.88921 2.01724 0.03752  0.14729  0.15643  197 SER B N   
7407 C CA  . SER F 177 ? 2.24029 1.96508 2.05589 0.02328  0.08766  0.18876  197 SER B CA  
7408 C C   . SER F 177 ? 2.24509 1.94873 2.07270 0.01356  0.09763  0.20556  197 SER B C   
7409 O O   . SER F 177 ? 2.24062 1.89276 2.13559 0.02077  0.13758  0.20378  197 SER B O   
7410 C CB  . SER F 177 ? 2.26312 2.02284 2.20099 0.02599  0.05530  0.21352  197 SER B CB  
7411 O OG  . SER F 177 ? 2.28166 2.10212 2.21720 0.01987  -0.00519 0.24709  197 SER B OG  
7412 N N   . THR F 178 ? 2.21946 1.96325 1.98541 -0.00449 0.06317  0.21988  198 THR B N   
7413 C CA  . THR F 178 ? 2.24543 1.96249 2.01525 -0.02167 0.07584  0.23370  198 THR B CA  
7414 C C   . THR F 178 ? 2.26267 2.00582 2.06957 -0.03474 0.03025  0.29132  198 THR B C   
7415 O O   . THR F 178 ? 2.24581 2.05618 1.99872 -0.04339 -0.01321 0.30643  198 THR B O   
7416 C CB  . THR F 178 ? 2.26313 1.99662 1.92232 -0.03655 0.08950  0.19416  198 THR B CB  
7417 O OG1 . THR F 178 ? 2.24204 1.95969 1.84164 -0.01260 0.12024  0.14236  198 THR B OG1 
7418 C CG2 . THR F 178 ? 2.31265 2.00100 2.00016 -0.05442 0.11942  0.19313  198 THR B CG2 
7419 N N   . LEU F 179 ? 2.21934 1.90852 2.11704 -0.02949 0.03916  0.32238  199 LEU B N   
7420 C CA  . LEU F 179 ? 2.24407 1.92486 2.16986 -0.03642 0.00605  0.38262  199 LEU B CA  
7421 C C   . LEU F 179 ? 2.28285 1.92492 2.15960 -0.07067 0.03014  0.38729  199 LEU B C   
7422 O O   . LEU F 179 ? 2.30965 1.88327 2.22998 -0.07209 0.06927  0.36956  199 LEU B O   
7423 C CB  . LEU F 179 ? 2.25429 1.88544 2.30271 -0.00718 0.00528  0.40544  199 LEU B CB  
7424 C CG  . LEU F 179 ? 2.29822 1.88540 2.37455 -0.00503 -0.02059 0.46836  199 LEU B CG  
7425 C CD1 . LEU F 179 ? 2.31001 1.95803 2.32325 -0.00886 -0.07423 0.51660  199 LEU B CD1 
7426 C CD2 . LEU F 179 ? 2.31736 1.85936 2.51778 0.03416  -0.02577 0.48022  199 LEU B CD2 
7427 N N   . THR F 180 ? 2.31545 2.00501 2.10878 -0.09981 0.00885  0.40683  200 THR B N   
7428 C CA  . THR F 180 ? 2.36116 2.02564 2.11020 -0.14188 0.03667  0.40333  200 THR B CA  
7429 C C   . THR F 180 ? 2.38686 2.02431 2.13286 -0.16184 0.01606  0.48041  200 THR B C   
7430 O O   . THR F 180 ? 2.35874 2.04739 2.07654 -0.15115 -0.02832 0.52570  200 THR B O   
7431 C CB  . THR F 180 ? 2.34178 2.08700 1.98936 -0.16508 0.04099  0.35075  200 THR B CB  
7432 O OG1 . THR F 180 ? 2.33790 2.08472 1.97856 -0.13994 0.06488  0.28299  200 THR B OG1 
7433 C CG2 . THR F 180 ? 2.39953 2.13415 2.01366 -0.21460 0.07077  0.34020  200 THR B CG2 
7434 N N   . LEU F 181 ? 2.43549 1.98630 2.21145 -0.18689 0.04884  0.49502  201 LEU B N   
7435 C CA  . LEU F 181 ? 2.48356 1.97432 2.25522 -0.20616 0.03992  0.57407  201 LEU B CA  
7436 C C   . LEU F 181 ? 2.55718 1.97128 2.34062 -0.25415 0.09106  0.55750  201 LEU B C   
7437 O O   . LEU F 181 ? 2.56626 1.99579 2.35698 -0.26818 0.12581  0.48039  201 LEU B O   
7438 C CB  . LEU F 181 ? 2.49038 1.92281 2.33643 -0.15401 0.00695  0.62899  201 LEU B CB  
7439 C CG  . LEU F 181 ? 2.48555 1.85680 2.44108 -0.11592 0.02341  0.59317  201 LEU B CG  
7440 C CD1 . LEU F 181 ? 2.55011 1.79450 2.56420 -0.12256 0.04970  0.61411  201 LEU B CD1 
7441 C CD2 . LEU F 181 ? 2.45309 1.85812 2.46729 -0.05859 -0.02040 0.60838  201 LEU B CD2 
7442 N N   . SER F 182 ? 2.56207 1.89786 2.33873 -0.28068 0.09580  0.62803  202 SER B N   
7443 C CA  . SER F 182 ? 2.64224 1.89125 2.44485 -0.33072 0.14625  0.61409  202 SER B CA  
7444 C C   . SER F 182 ? 2.67562 1.80669 2.58576 -0.29720 0.15819  0.60754  202 SER B C   
7445 O O   . SER F 182 ? 2.64449 1.74740 2.60266 -0.23924 0.12504  0.63828  202 SER B O   
7446 C CB  . SER F 182 ? 2.70669 1.90866 2.45135 -0.38074 0.15525  0.69441  202 SER B CB  
7447 O OG  . SER F 182 ? 2.75946 1.83553 2.53711 -0.35100 0.13850  0.77958  202 SER B OG  
7448 N N   . LYS F 183 ? 2.60518 1.67525 2.55977 -0.33311 0.20503  0.55922  203 LYS B N   
7449 C CA  . LYS F 183 ? 2.62690 1.59117 2.68701 -0.30145 0.21770  0.54109  203 LYS B CA  
7450 C C   . LYS F 183 ? 2.66529 1.50622 2.75820 -0.27420 0.19227  0.63493  203 LYS B C   
7451 O O   . LYS F 183 ? 2.65404 1.43255 2.83341 -0.22229 0.18131  0.62809  203 LYS B O   
7452 C CB  . LYS F 183 ? 2.69115 1.61238 2.79166 -0.35023 0.27039  0.47287  203 LYS B CB  
7453 N N   . ALA F 184 ? 2.73691 1.54818 2.75652 -0.30103 0.18006  0.72203  204 ALA B N   
7454 C CA  . ALA F 184 ? 2.80938 1.49874 2.83988 -0.26571 0.15148  0.81742  204 ALA B CA  
7455 C C   . ALA F 184 ? 2.75018 1.48361 2.80992 -0.18196 0.09395  0.83441  204 ALA B C   
7456 O O   . ALA F 184 ? 2.79675 1.44921 2.93791 -0.12818 0.07628  0.84228  204 ALA B O   
7457 C CB  . ALA F 184 ? 2.93440 1.59719 2.85823 -0.30925 0.15269  0.90943  204 ALA B CB  
7458 N N   . ASP F 185 ? 2.85247 1.72110 2.85530 -0.16979 0.06417  0.83064  205 ASP B N   
7459 C CA  . ASP F 185 ? 2.80293 1.72934 2.84066 -0.09701 0.01096  0.83770  205 ASP B CA  
7460 C C   . ASP F 185 ? 2.73822 1.68695 2.88263 -0.06175 0.02109  0.75594  205 ASP B C   
7461 O O   . ASP F 185 ? 2.71299 1.69157 2.91586 -0.00170 -0.01603 0.75569  205 ASP B O   
7462 C CB  . ASP F 185 ? 2.74829 1.81600 2.70366 -0.10000 -0.01922 0.84263  205 ASP B CB  
7463 C CG  . ASP F 185 ? 2.79466 1.86616 2.63451 -0.15060 -0.01306 0.90386  205 ASP B CG  
7464 O OD1 . ASP F 185 ? 2.85878 1.88526 2.65263 -0.12674 -0.04476 0.99107  205 ASP B OD1 
7465 O OD2 . ASP F 185 ? 2.77458 1.89677 2.56738 -0.21214 0.02475  0.86278  205 ASP B OD2 
7466 N N   . TYR F 186 ? 2.67986 1.62277 2.85074 -0.09624 0.07131  0.68341  206 TYR B N   
7467 C CA  . TYR F 186 ? 2.63024 1.57789 2.89897 -0.06005 0.08712  0.61251  206 TYR B CA  
7468 C C   . TYR F 186 ? 2.67890 1.50002 3.04092 -0.03170 0.09112  0.62266  206 TYR B C   
7469 O O   . TYR F 186 ? 2.64714 1.46975 3.09775 0.02353  0.07652  0.60054  206 TYR B O   
7470 C CB  . TYR F 186 ? 2.60005 1.60021 2.85289 -0.09474 0.13524  0.52586  206 TYR B CB  
7471 C CG  . TYR F 186 ? 2.54320 1.56055 2.87948 -0.05379 0.15408  0.45682  206 TYR B CG  
7472 C CD1 . TYR F 186 ? 2.47515 1.56513 2.83639 -0.01280 0.13408  0.44715  206 TYR B CD1 
7473 C CD2 . TYR F 186 ? 2.56100 1.52318 2.95557 -0.05678 0.19420  0.39954  206 TYR B CD2 
7474 C CE1 . TYR F 186 ? 2.42474 1.53004 2.85989 0.02021  0.15936  0.38761  206 TYR B CE1 
7475 C CE2 . TYR F 186 ? 2.50653 1.48975 2.97092 -0.01725 0.21479  0.33785  206 TYR B CE2 
7476 C CZ  . TYR F 186 ? 2.43781 1.49112 2.91933 0.01948  0.20009  0.33505  206 TYR B CZ  
7477 O OH  . TYR F 186 ? 2.38777 1.46205 2.93604 0.05416  0.22881  0.27632  206 TYR B OH  
7478 N N   . GLU F 187 ? 2.72765 1.43836 3.07700 -0.06901 0.11193  0.65207  207 GLU B N   
7479 C CA  . GLU F 187 ? 2.77986 1.35917 3.21774 -0.03550 0.10897  0.66474  207 GLU B CA  
7480 C C   . GLU F 187 ? 2.83883 1.35120 3.27314 0.01689  0.05457  0.75490  207 GLU B C   
7481 O O   . GLU F 187 ? 2.90541 1.31231 3.41553 0.06011  0.04190  0.76447  207 GLU B O   
7482 C CB  . GLU F 187 ? 2.85503 1.32463 3.29839 -0.09216 0.15376  0.65462  207 GLU B CB  
7483 C CG  . GLU F 187 ? 2.82693 1.37236 3.25452 -0.14761 0.20350  0.56746  207 GLU B CG  
7484 C CD  . GLU F 187 ? 2.73697 1.37604 3.22001 -0.10880 0.21365  0.47631  207 GLU B CD  
7485 O OE1 . GLU F 187 ? 2.71474 1.31397 3.29216 -0.05599 0.20625  0.45421  207 GLU B OE1 
7486 O OE2 . GLU F 187 ? 2.69608 1.44626 3.12490 -0.12952 0.23074  0.42613  207 GLU B OE2 
7487 N N   . LYS F 188 ? 3.00084 1.47678 3.01340 -0.21422 0.13236  0.74830  208 LYS B N   
7488 C CA  . LYS F 188 ? 2.99475 1.47425 3.01414 -0.17357 0.13014  0.82456  208 LYS B CA  
7489 C C   . LYS F 188 ? 2.93384 1.50507 2.97710 -0.09058 0.13726  0.81055  208 LYS B C   
7490 O O   . LYS F 188 ? 2.94066 1.52333 2.99246 -0.04336 0.13260  0.86256  208 LYS B O   
7491 C CB  . LYS F 188 ? 2.95000 1.53388 2.97077 -0.23073 0.12602  0.89136  208 LYS B CB  
7492 N N   . HIS F 189 ? 2.86869 1.50513 2.92281 -0.07060 0.14960  0.74187  209 HIS B N   
7493 C CA  . HIS F 189 ? 2.81346 1.55063 2.90091 -0.00504 0.16261  0.72479  209 HIS B CA  
7494 C C   . HIS F 189 ? 2.83797 1.51737 2.91849 0.03731  0.18128  0.65631  209 HIS B C   
7495 O O   . HIS F 189 ? 2.86743 1.48077 2.91608 0.01028  0.18278  0.61221  209 HIS B O   
7496 C CB  . HIS F 189 ? 2.71248 1.63267 2.82640 -0.03055 0.16483  0.71902  209 HIS B CB  
7497 C CG  . HIS F 189 ? 2.67716 1.68383 2.79892 -0.06447 0.14784  0.78234  209 HIS B CG  
7498 N ND1 . HIS F 189 ? 2.60700 1.73169 2.73053 -0.12285 0.14042  0.77997  209 HIS B ND1 
7499 C CD2 . HIS F 189 ? 2.70361 1.70186 2.82678 -0.04274 0.13681  0.84979  209 HIS B CD2 
7500 C CE1 . HIS F 189 ? 2.58564 1.77631 2.71317 -0.13895 0.12781  0.84332  209 HIS B CE1 
7501 N NE2 . HIS F 189 ? 2.64635 1.75926 2.77019 -0.09017 0.12596  0.88939  209 HIS B NE2 
7502 N N   . LYS F 190 ? 2.75781 1.47599 2.86963 0.10529  0.19680  0.64390  210 LYS B N   
7503 C CA  . LYS F 190 ? 2.78283 1.45355 2.88815 0.15145  0.22018  0.58454  210 LYS B CA  
7504 C C   . LYS F 190 ? 2.71641 1.51242 2.84776 0.16346  0.25008  0.54736  210 LYS B C   
7505 O O   . LYS F 190 ? 2.71069 1.49016 2.80971 0.15414  0.26701  0.50222  210 LYS B O   
7506 C CB  . LYS F 190 ? 2.84543 1.44266 2.96547 0.22357  0.21922  0.59128  210 LYS B CB  
7507 N N   . VAL F 191 ? 2.65027 1.56913 2.83873 0.18551  0.25746  0.56342  211 VAL B N   
7508 C CA  . VAL F 191 ? 2.59326 1.61798 2.81666 0.19660  0.29033  0.52685  211 VAL B CA  
7509 C C   . VAL F 191 ? 2.52843 1.63731 2.74436 0.13967  0.28456  0.52515  211 VAL B C   
7510 O O   . VAL F 191 ? 2.49148 1.67733 2.72719 0.10997  0.25926  0.55928  211 VAL B O   
7511 C CB  . VAL F 191 ? 2.58016 1.71020 2.88137 0.24260  0.30045  0.53228  211 VAL B CB  
7512 C CG1 . VAL F 191 ? 2.54386 1.77693 2.88941 0.24258  0.33867  0.49340  211 VAL B CG1 
7513 C CG2 . VAL F 191 ? 2.64188 1.69513 2.94912 0.30667  0.30415  0.52633  211 VAL B CG2 
7514 N N   . TYR F 192 ? 2.57426 1.67161 2.75732 0.13001  0.30749  0.48483  212 TYR B N   
7515 C CA  . TYR F 192 ? 2.51911 1.69466 2.69245 0.08812  0.30385  0.47371  212 TYR B CA  
7516 C C   . TYR F 192 ? 2.50539 1.73454 2.70573 0.11139  0.34516  0.44352  212 TYR B C   
7517 O O   . TYR F 192 ? 2.52949 1.69018 2.68552 0.13176  0.37562  0.41420  212 TYR B O   
7518 C CB  . TYR F 192 ? 2.53104 1.63290 2.62744 0.05493  0.28944  0.45332  212 TYR B CB  
7519 C CG  . TYR F 192 ? 2.54252 1.61756 2.62391 0.01132  0.25099  0.48199  212 TYR B CG  
7520 C CD1 . TYR F 192 ? 2.60119 1.57329 2.67663 0.02112  0.24027  0.50425  212 TYR B CD1 
7521 C CD2 . TYR F 192 ? 2.49955 1.65316 2.57487 -0.04046 0.22688  0.48710  212 TYR B CD2 
7522 C CE1 . TYR F 192 ? 2.62183 1.55961 2.68498 -0.02526 0.21118  0.53563  212 TYR B CE1 
7523 C CE2 . TYR F 192 ? 2.51415 1.65088 2.57957 -0.08725 0.19829  0.51533  212 TYR B CE2 
7524 C CZ  . TYR F 192 ? 2.57771 1.60158 2.63719 -0.08231 0.19285  0.54235  212 TYR B CZ  
7525 O OH  . TYR F 192 ? 2.60278 1.59828 2.65346 -0.13471 0.17031  0.57563  212 TYR B OH  
7526 N N   . ALA F 193 ? 2.47197 1.82304 2.74648 0.10942  0.34748  0.45067  213 ALA B N   
7527 C CA  . ALA F 193 ? 2.46867 1.88192 2.79052 0.12283  0.38762  0.42460  213 ALA B CA  
7528 C C   . ALA F 193 ? 2.42618 1.90455 2.74291 0.08717  0.37942  0.41316  213 ALA B C   
7529 O O   . ALA F 193 ? 2.38963 1.92628 2.70634 0.05660  0.33854  0.42739  213 ALA B O   
7530 C CB  . ALA F 193 ? 2.47922 1.99188 2.90390 0.14895  0.39471  0.42867  213 ALA B CB  
7531 N N   . CYS F 194 ? 2.42197 1.88979 2.73286 0.09316  0.42000  0.38795  214 CYS B N   
7532 C CA  . CYS F 194 ? 2.39095 1.90952 2.69887 0.06807  0.41581  0.37355  214 CYS B CA  
7533 C C   . CYS F 194 ? 2.41606 1.97642 2.79609 0.07859  0.46472  0.35624  214 CYS B C   
7534 O O   . CYS F 194 ? 2.44154 1.92888 2.79245 0.09732  0.51572  0.34733  214 CYS B O   
7535 C CB  . CYS F 194 ? 2.38013 1.80817 2.57539 0.06249  0.41350  0.36088  214 CYS B CB  
7536 S SG  . CYS F 194 ? 2.35887 1.80993 2.53227 0.05189  0.42405  0.33893  214 CYS B SG  
7537 N N   . GLU F 195 ? 2.35445 2.03686 2.83239 0.06643  0.45077  0.34996  215 GLU B N   
7538 C CA  . GLU F 195 ? 2.36060 2.09946 2.92949 0.06752  0.49316  0.32686  215 GLU B CA  
7539 C C   . GLU F 195 ? 2.35470 2.10739 2.91309 0.04328  0.48927  0.31048  215 GLU B C   
7540 O O   . GLU F 195 ? 2.32951 2.11016 2.85033 0.02747  0.43997  0.31237  215 GLU B O   
7541 C CB  . GLU F 195 ? 2.30726 2.18163 3.00113 0.07535  0.47640  0.31965  215 GLU B CB  
7542 C CG  . GLU F 195 ? 2.21801 2.16891 3.03001 0.07364  0.51931  0.28564  215 GLU B CG  
7543 C CD  . GLU F 195 ? 2.09422 2.20742 3.02712 0.07821  0.48434  0.26747  215 GLU B CD  
7544 O OE1 . GLU F 195 ? 2.09819 2.25365 3.02168 0.09545  0.43867  0.28964  215 GLU B OE1 
7545 O OE2 . GLU F 195 ? 1.98562 2.18347 3.02294 0.06621  0.50305  0.23039  215 GLU B OE2 
7546 N N   . VAL F 196 ? 2.33740 2.06484 2.92544 0.04082  0.54338  0.29426  216 VAL B N   
7547 C CA  . VAL F 196 ? 2.30170 2.03278 2.89138 0.02176  0.54447  0.27743  216 VAL B CA  
7548 C C   . VAL F 196 ? 2.21762 2.02894 2.94731 0.00981  0.58050  0.25096  216 VAL B C   
7549 O O   . VAL F 196 ? 2.21463 1.98271 2.97223 0.01261  0.64665  0.24907  216 VAL B O   
7550 C CB  . VAL F 196 ? 2.34323 1.93136 2.80859 0.02989  0.58026  0.28706  216 VAL B CB  
7551 C CG1 . VAL F 196 ? 2.31890 1.90289 2.78137 0.01577  0.57514  0.27113  216 VAL B CG1 
7552 C CG2 . VAL F 196 ? 2.35036 1.86747 2.68727 0.04453  0.54576  0.30278  216 VAL B CG2 
7553 N N   . THR F 197 ? 2.19895 2.13680 3.02177 -0.00346 0.53762  0.22660  217 THR B N   
7554 C CA  . THR F 197 ? 2.08973 2.11476 3.05444 -0.01888 0.56181  0.18864  217 THR B CA  
7555 C C   . THR F 197 ? 2.12052 2.07083 3.05510 -0.03767 0.58081  0.17760  217 THR B C   
7556 O O   . THR F 197 ? 2.12320 2.09656 3.02756 -0.04180 0.52910  0.16761  217 THR B O   
7557 C CB  . THR F 197 ? 1.96461 2.16319 3.03748 -0.01687 0.50301  0.16263  217 THR B CB  
7558 O OG1 . THR F 197 ? 1.98433 2.20843 2.98862 -0.01868 0.43711  0.17142  217 THR B OG1 
7559 C CG2 . THR F 197 ? 1.93375 2.19495 3.04327 0.00840  0.49587  0.17446  217 THR B CG2 
7560 N N   . GLN F 198 ? 2.14935 2.00198 3.07998 -0.04600 0.65628  0.18265  218 GLN B N   
7561 C CA  . GLN F 198 ? 2.19893 1.95302 3.09585 -0.06134 0.68936  0.18041  218 GLN B CA  
7562 C C   . GLN F 198 ? 2.13359 1.92847 3.18131 -0.09055 0.74850  0.14970  218 GLN B C   
7563 O O   . GLN F 198 ? 2.15457 1.88909 3.20948 -0.09721 0.82511  0.16353  218 GLN B O   
7564 C CB  . GLN F 198 ? 2.30588 1.89046 3.04372 -0.04404 0.73553  0.22260  218 GLN B CB  
7565 C CG  . GLN F 198 ? 2.37041 1.83243 3.04333 -0.05006 0.76825  0.23054  218 GLN B CG  
7566 C CD  . GLN F 198 ? 2.44008 1.74423 2.96785 -0.02839 0.83029  0.27311  218 GLN B CD  
7567 O OE1 . GLN F 198 ? 2.44356 1.72968 2.99113 -0.02957 0.89490  0.28705  218 GLN B OE1 
7568 N NE2 . GLN F 198 ? 2.48634 1.68367 2.86683 -0.00386 0.81045  0.29022  218 GLN B NE2 
7569 N N   . GLY F 199 ? 2.62525 2.15508 2.53488 0.23947  0.74782  -0.12855 219 GLY B N   
7570 C CA  . GLY F 199 ? 2.60703 2.10966 2.62329 0.19487  0.79667  -0.18415 219 GLY B CA  
7571 C C   . GLY F 199 ? 2.54320 2.11602 2.72729 0.15692  0.78679  -0.19124 219 GLY B C   
7572 O O   . GLY F 199 ? 2.51809 2.23215 2.77627 0.14413  0.70515  -0.18049 219 GLY B O   
7573 N N   . THR F 200 ? 2.54421 2.01736 2.78628 0.14250  0.87406  -0.20724 220 THR B N   
7574 C CA  . THR F 200 ? 2.48481 2.01326 2.88602 0.11190  0.88103  -0.21797 220 THR B CA  
7575 C C   . THR F 200 ? 2.46456 1.96621 2.84401 0.15026  0.88160  -0.16460 220 THR B C   
7576 O O   . THR F 200 ? 2.42363 1.90818 2.89803 0.14013  0.92770  -0.17075 220 THR B O   
7577 C CB  . THR F 200 ? 2.47194 1.91847 2.95942 0.07108  0.97990  -0.26649 220 THR B CB  
7578 O OG1 . THR F 200 ? 2.51031 1.77875 2.88515 0.10426  1.07867  -0.23888 220 THR B OG1 
7579 C CG2 . THR F 200 ? 2.49968 1.97423 3.02258 0.02918  0.97312  -0.32986 220 THR B CG2 
7580 N N   . THR F 201 ? 2.51237 2.01427 2.77431 0.19361  0.83221  -0.11705 221 THR B N   
7581 C CA  . THR F 201 ? 2.49678 1.96632 2.73152 0.23199  0.82893  -0.07374 221 THR B CA  
7582 C C   . THR F 201 ? 2.53093 2.09426 2.73233 0.24618  0.72774  -0.03488 221 THR B C   
7583 O O   . THR F 201 ? 2.57128 2.13061 2.65425 0.26692  0.70192  -0.01726 221 THR B O   
7584 C CB  . THR F 201 ? 2.49768 1.81220 2.59198 0.28038  0.91005  -0.05733 221 THR B CB  
7585 O OG1 . THR F 201 ? 2.47522 1.70153 2.62241 0.26957  1.00959  -0.07811 221 THR B OG1 
7586 C CG2 . THR F 201 ? 2.48931 1.78523 2.51555 0.32982  0.88324  -0.01646 221 THR B CG2 
7587 N N   . SER F 202 ? 2.35524 2.00836 2.66524 0.23355  0.67049  -0.02197 222 SER B N   
7588 C CA  . SER F 202 ? 2.40035 2.13733 2.69333 0.24068  0.57771  0.02067  222 SER B CA  
7589 C C   . SER F 202 ? 2.40086 2.08269 2.67053 0.27481  0.57032  0.05613  222 SER B C   
7590 O O   . SER F 202 ? 2.40377 2.13225 2.75888 0.27287  0.52483  0.07385  222 SER B O   
7591 C CB  . SER F 202 ? 2.38902 2.26406 2.80648 0.20904  0.51035  0.01498  222 SER B CB  
7592 O OG  . SER F 202 ? 2.39095 2.34670 2.78089 0.18981  0.47515  0.00158  222 SER B OG  
7593 N N   . VAL F 203 ? 2.49478 2.07551 2.64387 0.31149  0.61326  0.06348  225 VAL B N   
7594 C CA  . VAL F 203 ? 2.47557 1.99910 2.60426 0.34785  0.61204  0.08392  225 VAL B CA  
7595 C C   . VAL F 203 ? 2.52092 2.10898 2.64569 0.34393  0.52205  0.12271  225 VAL B C   
7596 O O   . VAL F 203 ? 2.57329 2.23473 2.66780 0.32328  0.47380  0.13948  225 VAL B O   
7597 C CB  . VAL F 203 ? 2.44463 1.85196 2.44062 0.39612  0.67958  0.07758  225 VAL B CB  
7598 C CG1 . VAL F 203 ? 2.40106 1.72642 2.41459 0.40299  0.77747  0.04992  225 VAL B CG1 
7599 C CG2 . VAL F 203 ? 2.47781 1.89028 2.35161 0.40371  0.67014  0.08133  225 VAL B CG2 
7600 N N   . THR F 204 ? 2.37045 1.93262 2.53227 0.36230  0.49986  0.13724  226 THR B N   
7601 C CA  . THR F 204 ? 2.39613 2.00142 2.55965 0.35440  0.42006  0.17569  226 THR B CA  
7602 C C   . THR F 204 ? 2.34238 1.87129 2.49188 0.39017  0.41911  0.17645  226 THR B C   
7603 O O   . THR F 204 ? 2.30399 1.77945 2.49827 0.41509  0.45738  0.15531  226 THR B O   
7604 C CB  . THR F 204 ? 2.43741 2.13360 2.71455 0.32181  0.35720  0.20019  226 THR B CB  
7605 O OG1 . THR F 204 ? 2.47531 2.24745 2.77875 0.29418  0.36215  0.18542  226 THR B OG1 
7606 C CG2 . THR F 204 ? 2.46415 2.20290 2.72621 0.30671  0.28127  0.24977  226 THR B CG2 
7607 N N   . LYS F 205 ? 2.39258 1.92426 2.48576 0.39185  0.37422  0.19728  227 LYS B N   
7608 C CA  . LYS F 205 ? 2.35366 1.82207 2.44438 0.42108  0.35914  0.19286  227 LYS B CA  
7609 C C   . LYS F 205 ? 2.37755 1.88859 2.49563 0.38900  0.27949  0.23206  227 LYS B C   
7610 O O   . LYS F 205 ? 2.41108 1.99158 2.49496 0.35761  0.25095  0.25750  227 LYS B O   
7611 C CB  . LYS F 205 ? 2.32324 1.72601 2.29608 0.46895  0.40628  0.16134  227 LYS B CB  
7612 C CG  . LYS F 205 ? 2.29717 1.63445 2.26768 0.50843  0.39660  0.14217  227 LYS B CG  
7613 C CD  . LYS F 205 ? 2.28631 1.58144 2.12844 0.55947  0.43146  0.11166  227 LYS B CD  
7614 C CE  . LYS F 205 ? 2.27486 1.50965 2.11153 0.60651  0.42353  0.08158  227 LYS B CE  
7615 N NZ  . LYS F 205 ? 2.24331 1.41891 2.11652 0.64349  0.47923  0.06324  227 LYS B NZ  
7616 N N   . SER F 206 ? 2.26692 1.73409 2.44641 0.39729  0.24634  0.23734  228 SER B N   
7617 C CA  . SER F 206 ? 2.29332 1.78647 2.51664 0.36129  0.17449  0.28123  228 SER B CA  
7618 C C   . SER F 206 ? 2.28422 1.69675 2.52134 0.38294  0.15219  0.26449  228 SER B C   
7619 O O   . SER F 206 ? 2.25820 1.60499 2.46888 0.43103  0.18969  0.21773  228 SER B O   
7620 C CB  . SER F 206 ? 2.31393 1.85221 2.63500 0.33712  0.14048  0.32019  228 SER B CB  
7621 O OG  . SER F 206 ? 2.33287 1.87295 2.69467 0.30883  0.07651  0.36912  228 SER B OG  
7622 N N   . PHE F 207 ? 2.26650 1.68352 2.54426 0.34738  0.09172  0.30287  229 PHE B N   
7623 C CA  . PHE F 207 ? 2.27879 1.61332 2.58905 0.36072  0.06176  0.28634  229 PHE B CA  
7624 C C   . PHE F 207 ? 2.30836 1.63807 2.69963 0.31823  0.00002  0.34610  229 PHE B C   
7625 O O   . PHE F 207 ? 2.32011 1.72192 2.72423 0.27831  -0.02000 0.40233  229 PHE B O   
7626 C CB  . PHE F 207 ? 2.30855 1.63232 2.54628 0.36638  0.06135  0.24919  229 PHE B CB  
7627 C CG  . PHE F 207 ? 2.35887 1.74877 2.58622 0.30759  0.02231  0.28761  229 PHE B CG  
7628 C CD1 . PHE F 207 ? 2.40383 1.76473 2.69683 0.26647  -0.03141 0.31639  229 PHE B CD1 
7629 C CD2 . PHE F 207 ? 2.36533 1.84402 2.51794 0.29418  0.04225  0.29369  229 PHE B CD2 
7630 C CE1 . PHE F 207 ? 2.44909 1.87660 2.73869 0.20802  -0.06018 0.35442  229 PHE B CE1 
7631 C CE2 . PHE F 207 ? 2.41099 1.96366 2.55616 0.24214  0.00966  0.32740  229 PHE B CE2 
7632 C CZ  . PHE F 207 ? 2.45039 1.98152 2.66665 0.19643  -0.03954 0.35953  229 PHE B CZ  
7633 N N   . ASN F 208 ? 2.38634 1.62660 2.82682 0.33058  -0.02956 0.33380  230 ASN B N   
7634 C CA  . ASN F 208 ? 2.42123 1.62651 2.93526 0.29546  -0.08572 0.39027  230 ASN B CA  
7635 C C   . ASN F 208 ? 2.47505 1.64371 2.98167 0.26181  -0.11504 0.38105  230 ASN B C   
7636 O O   . ASN F 208 ? 2.49169 1.60253 2.98177 0.29335  -0.10855 0.31507  230 ASN B O   
7637 C CB  . ASN F 208 ? 2.41761 1.53934 3.00542 0.33745  -0.09937 0.38235  230 ASN B CB  
7638 C CG  . ASN F 208 ? 2.38023 1.55021 2.98808 0.37085  -0.06868 0.37994  230 ASN B CG  
7639 O OD1 . ASN F 208 ? 2.37291 1.63612 2.96684 0.34814  -0.05835 0.41167  230 ASN B OD1 
7640 N ND2 . ASN F 208 ? 2.36603 1.47867 3.01255 0.42561  -0.05456 0.33766  230 ASN B ND2 
7641 N N   . ARG F 209 ? 2.32731 1.54301 2.84308 0.19828  -0.14384 0.44315  231 ARG B N   
7642 C CA  . ARG F 209 ? 2.39581 1.59480 2.91517 0.15412  -0.16900 0.43306  231 ARG B CA  
7643 C C   . ARG F 209 ? 2.46863 1.53640 3.04318 0.17805  -0.19345 0.38761  231 ARG B C   
7644 O O   . ARG F 209 ? 2.50348 1.55001 3.07160 0.16879  -0.20387 0.33399  231 ARG B O   
7645 C CB  . ARG F 209 ? 2.43297 1.67966 2.98120 0.08044  -0.19770 0.52120  231 ARG B CB  
7646 C CG  . ARG F 209 ? 2.51193 1.65027 3.14444 0.04606  -0.24050 0.56227  231 ARG B CG  
7647 C CD  . ARG F 209 ? 2.56317 1.72881 3.21311 -0.03090 -0.25850 0.58675  231 ARG B CD  
7648 N NE  . ARG F 209 ? 2.66211 1.74841 3.38496 -0.07882 -0.29095 0.66706  231 ARG B NE  
7649 C CZ  . ARG F 209 ? 2.77004 1.75523 3.55796 -0.11841 -0.31738 0.65631  231 ARG B CZ  
7650 N NH1 . ARG F 209 ? 2.77788 1.73654 3.56981 -0.10937 -0.32025 0.55955  231 ARG B NH1 
7651 N NH2 . ARG F 209 ? 2.87918 1.78894 3.72655 -0.16536 -0.34048 0.74148  231 ARG B NH2 
7652 N N   . GLY F 210 ? 2.60380 1.59388 3.23105 0.21252  -0.20389 0.40241  232 GLY B N   
7653 C CA  . GLY F 210 ? 2.64301 1.50283 3.32293 0.24409  -0.22876 0.35650  232 GLY B CA  
7654 C C   . GLY F 210 ? 2.62214 1.46946 3.25391 0.30950  -0.19793 0.25806  232 GLY B C   
7655 O O   . GLY F 210 ? 2.67773 1.47080 3.31491 0.31311  -0.21689 0.19864  232 GLY B O   
7656 N N   . GLU F 211 ? 2.68322 1.58172 3.26944 0.35895  -0.15052 0.24069  233 GLU B N   
7657 C CA  . GLU F 211 ? 2.66102 1.54690 3.19068 0.42868  -0.11056 0.15557  233 GLU B CA  
7658 C C   . GLU F 211 ? 2.73184 1.61972 3.21778 0.41951  -0.12299 0.10038  233 GLU B C   
7659 O O   . GLU F 211 ? 2.76238 1.58754 3.24336 0.46975  -0.12752 0.02798  233 GLU B O   
7660 C CB  . GLU F 211 ? 2.57781 1.54646 3.04244 0.45362  -0.04928 0.15687  233 GLU B CB  
7661 N N   . CYS F 212 ? 2.66132 1.62900 3.11769 0.36153  -0.12935 0.12950  234 CYS B N   
7662 C CA  . CYS F 212 ? 2.74135 1.73222 3.16608 0.34755  -0.14615 0.07524  234 CYS B CA  
7663 C C   . CYS F 212 ? 2.81645 1.70194 3.30789 0.35515  -0.19051 0.02369  234 CYS B C   
7664 O O   . CYS F 212 ? 2.84201 1.71987 3.29164 0.40366  -0.18789 -0.06222 234 CYS B O   
7665 C CB  . CYS F 212 ? 2.78590 1.86015 3.22006 0.26377  -0.16628 0.13059  234 CYS B CB  
7666 S SG  . CYS F 212 ? 2.72417 1.91066 3.10343 0.24633  -0.12739 0.20467  234 CYS B SG  
# 
