data_9EJH
# 
_entry.id   9EJH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EJH         pdb_00009ejh 10.2210/pdb9ejh/pdb 
WWPDB D_1000290630 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-26 ? 
2 'Structure model' 1 1 2025-04-02 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_citation.title' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EJH 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-27 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9EJG 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jamie.rossjohn@monash.edu 
_pdbx_contact_author.name_first         Jamie 
_pdbx_contact_author.name_last          Rossjohn 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2020-7522 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lim, J.J.'    1 ? 
'Loh, T.J.'    2 ? 
'Reid, H.H.'   3 ? 
'Rossjohn, J.' 4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_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                     'WITHHELD AT REQUEST OF AUTHORS' 
_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 'Lim, J.J.'    1 ? 
primary 'Loh, T.J.'    2 ? 
primary 'Rossjohn, J.' 3 ? 
# 
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 'HLA class II histocompatibility antigen, DQ alpha 1 chain' 20667.074 1   ? ? ?                      ? 
2 polymer     man 'MHC class II HLA-DQ-beta-1'                                22640.520 1   ? ? ?                      ? 
3 polymer     man 'HLA class II histocompatibility antigen gamma chain'       1313.628  1   ? ? 'UNP residues 110-122' ? 
4 polymer     man 'G9 T cell receptor alpha chain'                            22841.359 1   ? ? ?                      ? 
5 polymer     man 'G9 T cell receptor beta chain'                             27296.340 1   ? ? ?                      ? 
6 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose                    221.208   2   ? ? ?                      ? 
7 non-polymer syn 'ACETATE ION'                                               59.044    4   ? ? ?                      ? 
8 non-polymer syn GLYCEROL                                                    92.094    1   ? ? ?                      ? 
9 water       nat water                                                       18.015    297 ? ? ?                      ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'DC-1 alpha chain,DC-alpha,HLA-DCA,MHC class II DQA1'                                 
3 'HLA-DR antigens-associated invariant chain,Ia antigen-associated invariant chain,Ii' 
# 
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 
;EDIVADHVASYGVNLYQSYGPSGQYTHEFDGDEQFYVDLGRKETVWSLPVLRQFRFDPQFALTNIAVLKHNLNSLIKRSN
STAATNEVPEVTVFSKSPVTLGQPNILICLVDNIFPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKISYLTLLPSAE
ESYDCKVEHWGLDKPLLKHWEPE
;
;EDIVADHVASYGVNLYQSYGPSGQYTHEFDGDEQFYVDLGRKETVWSLPVLRQFRFDPQFALTNIAVLKHNLNSLIKRSN
STAATNEVPEVTVFSKSPVTLGQPNILICLVDNIFPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKISYLTLLPSAE
ESYDCKVEHWGLDKPLLKHWEPE
;
A ? 
2 'polypeptide(L)' no no 
;RDSPEDFVYQFKGMCYFTNGTERVRLVSRSIYNREEIVRFDSDVGEFRAVTLLGLPAAEYWNSQKDILERKRAAVDRVCR
HNYQLELRTTLQRRVEPTVTISPSRTEALNHHNLLVCSVTDFYPAQIKVRWFRNDQEETAGVVSTPLIRNGDWTFQILVM
LEMTPQRGDVYTCHVEHPSLQSPITVEWRAQSTG
;
;RDSPEDFVYQFKGMCYFTNGTERVRLVSRSIYNREEIVRFDSDVGEFRAVTLLGLPAAEYWNSQKDILERKRAAVDRVCR
HNYQLELRTTLQRRVEPTVTISPSRTEALNHHNLLVCSVTDFYPAQIKVRWFRNDQEETAGVVSTPLIRNGDWTFQILVM
LEMTPQRGDVYTCHVEHPSLQSPITVEWRAQSTG
;
B ? 
3 'polypeptide(L)' no no ATPLLMQALPMGA ATPLLMQALPMGA C ? 
4 'polypeptide(L)' no no 
;MQRKEVEQDPGPFNVPEGATVAFNCTYSNSASQSFFWYRQDCRKEPKLLMSVYSSGNEDGRFTAQLNRASQYISLLIRDS
KLSDSATYLCVVMGFQKLVFGTGTRLLVSPNIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVL
DMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESS
;
;MQRKEVEQDPGPFNVPEGATVAFNCTYSNSASQSFFWYRQDCRKEPKLLMSVYSSGNEDGRFTAQLNRASQYISLLIRDS
KLSDSATYLCVVMGFQKLVFGTGTRLLVSPNIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVL
DMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESS
;
D ? 
5 'polypeptide(L)' no no 
;MGVTQTPRYLIKTRGQQVTLSCSPISGHRSVSWYQQTPGQGLQFLFEYFSETQRNKGNFPGRFSGRQFSNSRSEMNVSTL
ELGDSALYLCASSLRAESGELFFGEGSRLTVLEDLNKVFPPEVAVFEPSEAEISHTQKATLVCLATGFFPDHVELSWWVN
GKEVHSGVCTDPQPLKEQPALNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGR
AD
;
;MGVTQTPRYLIKTRGQQVTLSCSPISGHRSVSWYQQTPGQGLQFLFEYFSETQRNKGNFPGRFSGRQFSNSRSEMNVSTL
ELGDSALYLCASSLRAESGELFFGEGSRLTVLEDLNKVFPPEVAVFEPSEAEISHTQKATLVCLATGFFPDHVELSWWVN
GKEVHSGVCTDPQPLKEQPALNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGR
AD
;
E ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
6 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
7 'ACETATE ION'                            ACT 
8 GLYCEROL                                 GOL 
9 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   ASP n 
1 3   ILE n 
1 4   VAL n 
1 5   ALA n 
1 6   ASP n 
1 7   HIS n 
1 8   VAL n 
1 9   ALA n 
1 10  SER n 
1 11  TYR n 
1 12  GLY n 
1 13  VAL n 
1 14  ASN n 
1 15  LEU n 
1 16  TYR n 
1 17  GLN n 
1 18  SER n 
1 19  TYR n 
1 20  GLY n 
1 21  PRO n 
1 22  SER n 
1 23  GLY n 
1 24  GLN n 
1 25  TYR n 
1 26  THR n 
1 27  HIS n 
1 28  GLU n 
1 29  PHE n 
1 30  ASP n 
1 31  GLY n 
1 32  ASP n 
1 33  GLU n 
1 34  GLN n 
1 35  PHE n 
1 36  TYR n 
1 37  VAL n 
1 38  ASP n 
1 39  LEU n 
1 40  GLY n 
1 41  ARG n 
1 42  LYS n 
1 43  GLU n 
1 44  THR n 
1 45  VAL n 
1 46  TRP n 
1 47  SER n 
1 48  LEU n 
1 49  PRO n 
1 50  VAL n 
1 51  LEU n 
1 52  ARG n 
1 53  GLN n 
1 54  PHE n 
1 55  ARG n 
1 56  PHE n 
1 57  ASP n 
1 58  PRO n 
1 59  GLN n 
1 60  PHE n 
1 61  ALA n 
1 62  LEU n 
1 63  THR n 
1 64  ASN n 
1 65  ILE n 
1 66  ALA n 
1 67  VAL n 
1 68  LEU n 
1 69  LYS n 
1 70  HIS n 
1 71  ASN n 
1 72  LEU n 
1 73  ASN n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  LYS n 
1 78  ARG n 
1 79  SER n 
1 80  ASN n 
1 81  SER n 
1 82  THR n 
1 83  ALA n 
1 84  ALA n 
1 85  THR n 
1 86  ASN n 
1 87  GLU n 
1 88  VAL n 
1 89  PRO n 
1 90  GLU n 
1 91  VAL n 
1 92  THR n 
1 93  VAL n 
1 94  PHE n 
1 95  SER n 
1 96  LYS n 
1 97  SER n 
1 98  PRO n 
1 99  VAL n 
1 100 THR n 
1 101 LEU n 
1 102 GLY n 
1 103 GLN n 
1 104 PRO n 
1 105 ASN n 
1 106 ILE n 
1 107 LEU n 
1 108 ILE n 
1 109 CYS n 
1 110 LEU n 
1 111 VAL n 
1 112 ASP n 
1 113 ASN n 
1 114 ILE n 
1 115 PHE n 
1 116 PRO n 
1 117 PRO n 
1 118 VAL n 
1 119 VAL n 
1 120 ASN n 
1 121 ILE n 
1 122 THR n 
1 123 TRP n 
1 124 LEU n 
1 125 SER n 
1 126 ASN n 
1 127 GLY n 
1 128 HIS n 
1 129 SER n 
1 130 VAL n 
1 131 THR n 
1 132 GLU n 
1 133 GLY n 
1 134 VAL n 
1 135 SER n 
1 136 GLU n 
1 137 THR n 
1 138 SER n 
1 139 PHE n 
1 140 LEU n 
1 141 SER n 
1 142 LYS n 
1 143 SER n 
1 144 ASP n 
1 145 HIS n 
1 146 SER n 
1 147 PHE n 
1 148 PHE n 
1 149 LYS n 
1 150 ILE n 
1 151 SER n 
1 152 TYR n 
1 153 LEU n 
1 154 THR n 
1 155 LEU n 
1 156 LEU n 
1 157 PRO n 
1 158 SER n 
1 159 ALA n 
1 160 GLU n 
1 161 GLU n 
1 162 SER n 
1 163 TYR n 
1 164 ASP n 
1 165 CYS n 
1 166 LYS n 
1 167 VAL n 
1 168 GLU n 
1 169 HIS n 
1 170 TRP n 
1 171 GLY n 
1 172 LEU n 
1 173 ASP n 
1 174 LYS n 
1 175 PRO n 
1 176 LEU n 
1 177 LEU n 
1 178 LYS n 
1 179 HIS n 
1 180 TRP n 
1 181 GLU n 
1 182 PRO n 
1 183 GLU n 
2 1   ARG n 
2 2   ASP n 
2 3   SER n 
2 4   PRO n 
2 5   GLU n 
2 6   ASP n 
2 7   PHE n 
2 8   VAL n 
2 9   TYR n 
2 10  GLN n 
2 11  PHE n 
2 12  LYS n 
2 13  GLY n 
2 14  MET n 
2 15  CYS n 
2 16  TYR n 
2 17  PHE n 
2 18  THR n 
2 19  ASN n 
2 20  GLY n 
2 21  THR n 
2 22  GLU n 
2 23  ARG n 
2 24  VAL n 
2 25  ARG n 
2 26  LEU n 
2 27  VAL n 
2 28  SER n 
2 29  ARG n 
2 30  SER n 
2 31  ILE n 
2 32  TYR n 
2 33  ASN n 
2 34  ARG n 
2 35  GLU n 
2 36  GLU n 
2 37  ILE n 
2 38  VAL n 
2 39  ARG n 
2 40  PHE n 
2 41  ASP n 
2 42  SER n 
2 43  ASP n 
2 44  VAL n 
2 45  GLY n 
2 46  GLU n 
2 47  PHE n 
2 48  ARG n 
2 49  ALA n 
2 50  VAL n 
2 51  THR n 
2 52  LEU n 
2 53  LEU n 
2 54  GLY n 
2 55  LEU n 
2 56  PRO n 
2 57  ALA n 
2 58  ALA n 
2 59  GLU n 
2 60  TYR n 
2 61  TRP n 
2 62  ASN n 
2 63  SER n 
2 64  GLN n 
2 65  LYS n 
2 66  ASP n 
2 67  ILE n 
2 68  LEU n 
2 69  GLU n 
2 70  ARG n 
2 71  LYS n 
2 72  ARG n 
2 73  ALA n 
2 74  ALA n 
2 75  VAL n 
2 76  ASP n 
2 77  ARG n 
2 78  VAL n 
2 79  CYS n 
2 80  ARG n 
2 81  HIS n 
2 82  ASN n 
2 83  TYR n 
2 84  GLN n 
2 85  LEU n 
2 86  GLU n 
2 87  LEU n 
2 88  ARG n 
2 89  THR n 
2 90  THR n 
2 91  LEU n 
2 92  GLN n 
2 93  ARG n 
2 94  ARG n 
2 95  VAL n 
2 96  GLU n 
2 97  PRO n 
2 98  THR n 
2 99  VAL n 
2 100 THR n 
2 101 ILE n 
2 102 SER n 
2 103 PRO n 
2 104 SER n 
2 105 ARG n 
2 106 THR n 
2 107 GLU n 
2 108 ALA n 
2 109 LEU n 
2 110 ASN n 
2 111 HIS n 
2 112 HIS n 
2 113 ASN n 
2 114 LEU n 
2 115 LEU n 
2 116 VAL n 
2 117 CYS n 
2 118 SER n 
2 119 VAL n 
2 120 THR n 
2 121 ASP n 
2 122 PHE n 
2 123 TYR n 
2 124 PRO n 
2 125 ALA n 
2 126 GLN n 
2 127 ILE n 
2 128 LYS n 
2 129 VAL n 
2 130 ARG n 
2 131 TRP n 
2 132 PHE n 
2 133 ARG n 
2 134 ASN n 
2 135 ASP n 
2 136 GLN n 
2 137 GLU n 
2 138 GLU n 
2 139 THR n 
2 140 ALA n 
2 141 GLY n 
2 142 VAL n 
2 143 VAL n 
2 144 SER n 
2 145 THR n 
2 146 PRO n 
2 147 LEU n 
2 148 ILE n 
2 149 ARG n 
2 150 ASN n 
2 151 GLY n 
2 152 ASP n 
2 153 TRP n 
2 154 THR n 
2 155 PHE n 
2 156 GLN n 
2 157 ILE n 
2 158 LEU n 
2 159 VAL n 
2 160 MET n 
2 161 LEU n 
2 162 GLU n 
2 163 MET n 
2 164 THR n 
2 165 PRO n 
2 166 GLN n 
2 167 ARG n 
2 168 GLY n 
2 169 ASP n 
2 170 VAL n 
2 171 TYR n 
2 172 THR n 
2 173 CYS n 
2 174 HIS n 
2 175 VAL n 
2 176 GLU n 
2 177 HIS n 
2 178 PRO n 
2 179 SER n 
2 180 LEU n 
2 181 GLN n 
2 182 SER n 
2 183 PRO n 
2 184 ILE n 
2 185 THR n 
2 186 VAL n 
2 187 GLU n 
2 188 TRP n 
2 189 ARG n 
2 190 ALA n 
2 191 GLN n 
2 192 SER n 
2 193 THR n 
2 194 GLY n 
3 1   ALA n 
3 2   THR n 
3 3   PRO n 
3 4   LEU n 
3 5   LEU n 
3 6   MET n 
3 7   GLN n 
3 8   ALA n 
3 9   LEU n 
3 10  PRO n 
3 11  MET n 
3 12  GLY n 
3 13  ALA n 
4 1   MET n 
4 2   GLN n 
4 3   ARG n 
4 4   LYS n 
4 5   GLU n 
4 6   VAL n 
4 7   GLU n 
4 8   GLN n 
4 9   ASP n 
4 10  PRO n 
4 11  GLY n 
4 12  PRO n 
4 13  PHE n 
4 14  ASN n 
4 15  VAL n 
4 16  PRO n 
4 17  GLU n 
4 18  GLY n 
4 19  ALA n 
4 20  THR n 
4 21  VAL n 
4 22  ALA n 
4 23  PHE n 
4 24  ASN n 
4 25  CYS n 
4 26  THR n 
4 27  TYR n 
4 28  SER n 
4 29  ASN n 
4 30  SER n 
4 31  ALA n 
4 32  SER n 
4 33  GLN n 
4 34  SER n 
4 35  PHE n 
4 36  PHE n 
4 37  TRP n 
4 38  TYR n 
4 39  ARG n 
4 40  GLN n 
4 41  ASP n 
4 42  CYS n 
4 43  ARG n 
4 44  LYS n 
4 45  GLU n 
4 46  PRO n 
4 47  LYS n 
4 48  LEU n 
4 49  LEU n 
4 50  MET n 
4 51  SER n 
4 52  VAL n 
4 53  TYR n 
4 54  SER n 
4 55  SER n 
4 56  GLY n 
4 57  ASN n 
4 58  GLU n 
4 59  ASP n 
4 60  GLY n 
4 61  ARG n 
4 62  PHE n 
4 63  THR n 
4 64  ALA n 
4 65  GLN n 
4 66  LEU n 
4 67  ASN n 
4 68  ARG n 
4 69  ALA n 
4 70  SER n 
4 71  GLN n 
4 72  TYR n 
4 73  ILE n 
4 74  SER n 
4 75  LEU n 
4 76  LEU n 
4 77  ILE n 
4 78  ARG n 
4 79  ASP n 
4 80  SER n 
4 81  LYS n 
4 82  LEU n 
4 83  SER n 
4 84  ASP n 
4 85  SER n 
4 86  ALA n 
4 87  THR n 
4 88  TYR n 
4 89  LEU n 
4 90  CYS n 
4 91  VAL n 
4 92  VAL n 
4 93  MET n 
4 94  GLY n 
4 95  PHE n 
4 96  GLN n 
4 97  LYS n 
4 98  LEU n 
4 99  VAL n 
4 100 PHE n 
4 101 GLY n 
4 102 THR n 
4 103 GLY n 
4 104 THR n 
4 105 ARG n 
4 106 LEU n 
4 107 LEU n 
4 108 VAL n 
4 109 SER n 
4 110 PRO n 
4 111 ASN n 
4 112 ILE n 
4 113 GLN n 
4 114 ASN n 
4 115 PRO n 
4 116 ASP n 
4 117 PRO n 
4 118 ALA n 
4 119 VAL n 
4 120 TYR n 
4 121 GLN n 
4 122 LEU n 
4 123 ARG n 
4 124 ASP n 
4 125 SER n 
4 126 LYS n 
4 127 SER n 
4 128 SER n 
4 129 ASP n 
4 130 LYS n 
4 131 SER n 
4 132 VAL n 
4 133 CYS n 
4 134 LEU n 
4 135 PHE n 
4 136 THR n 
4 137 ASP n 
4 138 PHE n 
4 139 ASP n 
4 140 SER n 
4 141 GLN n 
4 142 THR n 
4 143 ASN n 
4 144 VAL n 
4 145 SER n 
4 146 GLN n 
4 147 SER n 
4 148 LYS n 
4 149 ASP n 
4 150 SER n 
4 151 ASP n 
4 152 VAL n 
4 153 TYR n 
4 154 ILE n 
4 155 THR n 
4 156 ASP n 
4 157 LYS n 
4 158 CYS n 
4 159 VAL n 
4 160 LEU n 
4 161 ASP n 
4 162 MET n 
4 163 ARG n 
4 164 SER n 
4 165 MET n 
4 166 ASP n 
4 167 PHE n 
4 168 LYS n 
4 169 SER n 
4 170 ASN n 
4 171 SER n 
4 172 ALA n 
4 173 VAL n 
4 174 ALA n 
4 175 TRP n 
4 176 SER n 
4 177 ASN n 
4 178 LYS n 
4 179 SER n 
4 180 ASP n 
4 181 PHE n 
4 182 ALA n 
4 183 CYS n 
4 184 ALA n 
4 185 ASN n 
4 186 ALA n 
4 187 PHE n 
4 188 ASN n 
4 189 ASN n 
4 190 SER n 
4 191 ILE n 
4 192 ILE n 
4 193 PRO n 
4 194 GLU n 
4 195 ASP n 
4 196 THR n 
4 197 PHE n 
4 198 PHE n 
4 199 PRO n 
4 200 SER n 
4 201 PRO n 
4 202 GLU n 
4 203 SER n 
4 204 SER n 
5 1   MET n 
5 2   GLY n 
5 3   VAL n 
5 4   THR n 
5 5   GLN n 
5 6   THR n 
5 7   PRO n 
5 8   ARG n 
5 9   TYR n 
5 10  LEU n 
5 11  ILE n 
5 12  LYS n 
5 13  THR n 
5 14  ARG n 
5 15  GLY n 
5 16  GLN n 
5 17  GLN n 
5 18  VAL n 
5 19  THR n 
5 20  LEU n 
5 21  SER n 
5 22  CYS n 
5 23  SER n 
5 24  PRO n 
5 25  ILE n 
5 26  SER n 
5 27  GLY n 
5 28  HIS n 
5 29  ARG n 
5 30  SER n 
5 31  VAL n 
5 32  SER n 
5 33  TRP n 
5 34  TYR n 
5 35  GLN n 
5 36  GLN n 
5 37  THR n 
5 38  PRO n 
5 39  GLY n 
5 40  GLN n 
5 41  GLY n 
5 42  LEU n 
5 43  GLN n 
5 44  PHE n 
5 45  LEU n 
5 46  PHE n 
5 47  GLU n 
5 48  TYR n 
5 49  PHE n 
5 50  SER n 
5 51  GLU n 
5 52  THR n 
5 53  GLN n 
5 54  ARG n 
5 55  ASN n 
5 56  LYS n 
5 57  GLY n 
5 58  ASN n 
5 59  PHE n 
5 60  PRO n 
5 61  GLY n 
5 62  ARG n 
5 63  PHE n 
5 64  SER n 
5 65  GLY n 
5 66  ARG n 
5 67  GLN n 
5 68  PHE n 
5 69  SER n 
5 70  ASN n 
5 71  SER n 
5 72  ARG n 
5 73  SER n 
5 74  GLU n 
5 75  MET n 
5 76  ASN n 
5 77  VAL n 
5 78  SER n 
5 79  THR n 
5 80  LEU n 
5 81  GLU n 
5 82  LEU n 
5 83  GLY n 
5 84  ASP n 
5 85  SER n 
5 86  ALA n 
5 87  LEU n 
5 88  TYR n 
5 89  LEU n 
5 90  CYS n 
5 91  ALA n 
5 92  SER n 
5 93  SER n 
5 94  LEU n 
5 95  ARG n 
5 96  ALA n 
5 97  GLU n 
5 98  SER n 
5 99  GLY n 
5 100 GLU n 
5 101 LEU n 
5 102 PHE n 
5 103 PHE n 
5 104 GLY n 
5 105 GLU n 
5 106 GLY n 
5 107 SER n 
5 108 ARG n 
5 109 LEU n 
5 110 THR n 
5 111 VAL n 
5 112 LEU n 
5 113 GLU n 
5 114 ASP n 
5 115 LEU n 
5 116 ASN n 
5 117 LYS n 
5 118 VAL n 
5 119 PHE n 
5 120 PRO n 
5 121 PRO n 
5 122 GLU n 
5 123 VAL n 
5 124 ALA n 
5 125 VAL n 
5 126 PHE n 
5 127 GLU n 
5 128 PRO n 
5 129 SER n 
5 130 GLU n 
5 131 ALA n 
5 132 GLU n 
5 133 ILE n 
5 134 SER n 
5 135 HIS n 
5 136 THR n 
5 137 GLN n 
5 138 LYS n 
5 139 ALA n 
5 140 THR n 
5 141 LEU n 
5 142 VAL n 
5 143 CYS n 
5 144 LEU n 
5 145 ALA n 
5 146 THR n 
5 147 GLY n 
5 148 PHE n 
5 149 PHE n 
5 150 PRO n 
5 151 ASP n 
5 152 HIS n 
5 153 VAL n 
5 154 GLU n 
5 155 LEU n 
5 156 SER n 
5 157 TRP n 
5 158 TRP n 
5 159 VAL n 
5 160 ASN n 
5 161 GLY n 
5 162 LYS n 
5 163 GLU n 
5 164 VAL n 
5 165 HIS n 
5 166 SER n 
5 167 GLY n 
5 168 VAL n 
5 169 CYS n 
5 170 THR n 
5 171 ASP n 
5 172 PRO n 
5 173 GLN n 
5 174 PRO n 
5 175 LEU n 
5 176 LYS n 
5 177 GLU n 
5 178 GLN n 
5 179 PRO n 
5 180 ALA n 
5 181 LEU n 
5 182 ASN n 
5 183 ASP n 
5 184 SER n 
5 185 ARG n 
5 186 TYR n 
5 187 ALA n 
5 188 LEU n 
5 189 SER n 
5 190 SER n 
5 191 ARG n 
5 192 LEU n 
5 193 ARG n 
5 194 VAL n 
5 195 SER n 
5 196 ALA n 
5 197 THR n 
5 198 PHE n 
5 199 TRP n 
5 200 GLN n 
5 201 ASN n 
5 202 PRO n 
5 203 ARG n 
5 204 ASN n 
5 205 HIS n 
5 206 PHE n 
5 207 ARG n 
5 208 CYS n 
5 209 GLN n 
5 210 VAL n 
5 211 GLN n 
5 212 PHE n 
5 213 TYR n 
5 214 GLY n 
5 215 LEU n 
5 216 SER n 
5 217 GLU n 
5 218 ASN n 
5 219 ASP n 
5 220 GLU n 
5 221 TRP n 
5 222 THR n 
5 223 GLN n 
5 224 ASP n 
5 225 ARG n 
5 226 ALA n 
5 227 LYS n 
5 228 PRO n 
5 229 VAL n 
5 230 THR n 
5 231 GLN n 
5 232 ILE n 
5 233 VAL n 
5 234 SER n 
5 235 ALA n 
5 236 GLU n 
5 237 ALA n 
5 238 TRP n 
5 239 GLY n 
5 240 ARG n 
5 241 ALA n 
5 242 ASP 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' 1 183 human ? HLA-DQA1      ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Baculovirus expression vector pFastBac1-HM' 274590 ? ? ? ? ? ? ? ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 194 human ? HLA-DQB1      ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Baculovirus expression vector pFastBac1-HM' 274590 ? ? ? ? ? ? ? ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 13  human ? 'CD74, DHLAG' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Baculovirus expression vector pFastBac1-HM' 274590 ? ? ? ? ? ? ? ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 204 human ? ?             ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)'                 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ?           ? ? ? ? ? ? 
5 1 sample 'Biological sequence' 1 242 human ? ?             ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)'                 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ?           ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ACT non-polymer                  . 'ACETATE ION'                            ? 'C2 H3 O2 -1'    59.044  
ALA 'L-peptide linking'          y ALANINE                                  ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE                               ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking'          y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
GOL non-polymer                  . GLYCEROL                                 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       
92.094  
HIS 'L-peptide linking'          y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                  . WATER                                    ? 'H2 O'           18.015  
ILE 'L-peptide linking'          y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE                               ? 'C5 H11 N O2 S'  149.211 
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 
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 A . n 
A 1 2   ASP 2   2   2   ASP ASP A . n 
A 1 3   ILE 3   3   3   ILE ILE A . n 
A 1 4   VAL 4   4   4   VAL VAL A . n 
A 1 5   ALA 5   5   5   ALA ALA A . n 
A 1 6   ASP 6   6   6   ASP ASP A . n 
A 1 7   HIS 7   7   7   HIS HIS A . n 
A 1 8   VAL 8   8   8   VAL VAL A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  TYR 11  11  11  TYR TYR A . n 
A 1 12  GLY 12  11  11  GLY GLY A A n 
A 1 13  VAL 13  12  12  VAL VAL A . n 
A 1 14  ASN 14  13  13  ASN ASN A . n 
A 1 15  LEU 15  14  14  LEU LEU A . n 
A 1 16  TYR 16  15  15  TYR TYR A . n 
A 1 17  GLN 17  16  16  GLN GLN A . n 
A 1 18  SER 18  17  17  SER SER A . n 
A 1 19  TYR 19  18  18  TYR TYR A . n 
A 1 20  GLY 20  19  19  GLY GLY A . n 
A 1 21  PRO 21  20  20  PRO PRO A . n 
A 1 22  SER 22  21  21  SER SER A . n 
A 1 23  GLY 23  22  22  GLY GLY A . n 
A 1 24  GLN 24  23  23  GLN GLN A . n 
A 1 25  TYR 25  24  24  TYR TYR A . n 
A 1 26  THR 26  25  25  THR THR A . n 
A 1 27  HIS 27  26  26  HIS HIS A . n 
A 1 28  GLU 28  27  27  GLU GLU A . n 
A 1 29  PHE 29  28  28  PHE PHE A . n 
A 1 30  ASP 30  29  29  ASP ASP A . n 
A 1 31  GLY 31  30  30  GLY GLY A . n 
A 1 32  ASP 32  31  31  ASP ASP A . n 
A 1 33  GLU 33  32  32  GLU GLU A . n 
A 1 34  GLN 34  33  33  GLN GLN A . n 
A 1 35  PHE 35  34  34  PHE PHE A . n 
A 1 36  TYR 36  35  35  TYR TYR A . n 
A 1 37  VAL 37  36  36  VAL VAL A . n 
A 1 38  ASP 38  37  37  ASP ASP A . n 
A 1 39  LEU 39  38  38  LEU LEU A . n 
A 1 40  GLY 40  39  39  GLY GLY A . n 
A 1 41  ARG 41  40  40  ARG ARG A . n 
A 1 42  LYS 42  41  41  LYS LYS A . n 
A 1 43  GLU 43  42  42  GLU GLU A . n 
A 1 44  THR 44  43  43  THR THR A . n 
A 1 45  VAL 45  44  44  VAL VAL A . n 
A 1 46  TRP 46  45  45  TRP TRP A . n 
A 1 47  SER 47  46  46  SER SER A . n 
A 1 48  LEU 48  47  47  LEU LEU A . n 
A 1 49  PRO 49  48  48  PRO PRO A . n 
A 1 50  VAL 50  49  49  VAL VAL A . n 
A 1 51  LEU 51  50  50  LEU LEU A . n 
A 1 52  ARG 52  51  51  ARG ARG A . n 
A 1 53  GLN 53  52  52  GLN GLN A . n 
A 1 54  PHE 54  53  53  PHE PHE A . n 
A 1 55  ARG 55  54  54  ARG ARG A . n 
A 1 56  PHE 56  56  56  PHE PHE A . n 
A 1 57  ASP 57  57  57  ASP ASP A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  GLN 59  59  59  GLN GLN A . n 
A 1 60  PHE 60  60  60  PHE PHE A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  VAL 67  67  67  VAL VAL A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  HIS 70  70  70  HIS HIS A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  ASN 73  73  73  ASN ASN A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ILE 76  76  76  ILE ILE A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  ARG 78  78  78  ARG ARG A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  ASN 80  80  80  ASN ASN A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  THR 82  82  82  THR THR A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 THR 100 100 100 THR THR A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 CYS 109 109 109 CYS CYS A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 ASN 113 113 113 ASN ASN A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 PHE 115 115 115 PHE PHE A . n 
A 1 116 PRO 116 116 116 PRO PRO A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 ASN 120 120 120 ASN ASN A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 THR 122 122 122 THR THR A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 SER 125 125 125 SER SER A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 HIS 128 128 128 HIS HIS A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 SER 135 135 135 SER SER A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 SER 138 138 138 SER SER A . n 
A 1 139 PHE 139 139 139 PHE PHE A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 LYS 142 142 142 LYS LYS A . n 
A 1 143 SER 143 143 143 SER SER A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 HIS 145 145 145 HIS HIS A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 PHE 148 148 148 PHE PHE A . n 
A 1 149 LYS 149 149 149 LYS LYS A . n 
A 1 150 ILE 150 150 150 ILE ILE A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 THR 154 154 154 THR THR A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 TYR 163 163 163 TYR TYR A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 CYS 165 165 165 CYS CYS A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 HIS 169 169 169 HIS HIS A . n 
A 1 170 TRP 170 170 170 TRP TRP A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 LYS 178 178 178 LYS LYS A . n 
A 1 179 HIS 179 179 179 HIS HIS A . n 
A 1 180 TRP 180 180 180 TRP TRP A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 PRO 182 182 182 PRO PRO A . n 
A 1 183 GLU 183 183 ?   ?   ?   A . n 
B 2 1   ARG 1   1   ?   ?   ?   B . n 
B 2 2   ASP 2   2   ?   ?   ?   B . n 
B 2 3   SER 3   3   3   SER SER B . n 
B 2 4   PRO 4   4   4   PRO PRO B . n 
B 2 5   GLU 5   5   5   GLU GLU B . n 
B 2 6   ASP 6   6   6   ASP ASP B . n 
B 2 7   PHE 7   7   7   PHE PHE B . n 
B 2 8   VAL 8   8   8   VAL VAL B . n 
B 2 9   TYR 9   9   9   TYR TYR B . n 
B 2 10  GLN 10  10  10  GLN GLN B . n 
B 2 11  PHE 11  11  11  PHE PHE B . n 
B 2 12  LYS 12  12  12  LYS LYS B . n 
B 2 13  GLY 13  13  13  GLY GLY B . n 
B 2 14  MET 14  14  14  MET MET B . n 
B 2 15  CYS 15  15  15  CYS CYS B . n 
B 2 16  TYR 16  16  16  TYR TYR B . n 
B 2 17  PHE 17  17  17  PHE PHE B . n 
B 2 18  THR 18  18  18  THR THR B . n 
B 2 19  ASN 19  19  19  ASN ASN B . n 
B 2 20  GLY 20  20  20  GLY GLY B . n 
B 2 21  THR 21  21  21  THR THR B . n 
B 2 22  GLU 22  22  22  GLU GLU B . n 
B 2 23  ARG 23  23  23  ARG ARG B . n 
B 2 24  VAL 24  24  24  VAL VAL B . n 
B 2 25  ARG 25  25  25  ARG ARG B . n 
B 2 26  LEU 26  26  26  LEU LEU B . n 
B 2 27  VAL 27  27  27  VAL VAL B . n 
B 2 28  SER 28  28  28  SER SER B . n 
B 2 29  ARG 29  29  29  ARG ARG B . n 
B 2 30  SER 30  30  30  SER SER B . n 
B 2 31  ILE 31  31  31  ILE ILE B . n 
B 2 32  TYR 32  32  32  TYR TYR B . n 
B 2 33  ASN 33  33  33  ASN ASN B . n 
B 2 34  ARG 34  34  34  ARG ARG B . n 
B 2 35  GLU 35  35  35  GLU GLU B . n 
B 2 36  GLU 36  36  36  GLU GLU B . n 
B 2 37  ILE 37  37  37  ILE ILE B . n 
B 2 38  VAL 38  38  38  VAL VAL B . n 
B 2 39  ARG 39  39  39  ARG ARG B . n 
B 2 40  PHE 40  40  40  PHE PHE B . n 
B 2 41  ASP 41  41  41  ASP ASP B . n 
B 2 42  SER 42  42  42  SER SER B . n 
B 2 43  ASP 43  43  43  ASP ASP B . n 
B 2 44  VAL 44  44  44  VAL VAL B . n 
B 2 45  GLY 45  45  45  GLY GLY B . n 
B 2 46  GLU 46  46  46  GLU GLU B . n 
B 2 47  PHE 47  47  47  PHE PHE B . n 
B 2 48  ARG 48  48  48  ARG ARG B . n 
B 2 49  ALA 49  49  49  ALA ALA B . n 
B 2 50  VAL 50  50  50  VAL VAL B . n 
B 2 51  THR 51  51  51  THR THR B . n 
B 2 52  LEU 52  52  52  LEU LEU B . n 
B 2 53  LEU 53  53  53  LEU LEU B . n 
B 2 54  GLY 54  54  54  GLY GLY B . n 
B 2 55  LEU 55  55  55  LEU LEU B . n 
B 2 56  PRO 56  56  56  PRO PRO B . n 
B 2 57  ALA 57  57  57  ALA ALA B . n 
B 2 58  ALA 58  58  58  ALA ALA B . n 
B 2 59  GLU 59  59  59  GLU GLU B . n 
B 2 60  TYR 60  60  60  TYR TYR B . n 
B 2 61  TRP 61  61  61  TRP TRP B . n 
B 2 62  ASN 62  62  62  ASN ASN B . n 
B 2 63  SER 63  63  63  SER SER B . n 
B 2 64  GLN 64  64  64  GLN GLN B . n 
B 2 65  LYS 65  65  65  LYS LYS B . n 
B 2 66  ASP 66  66  66  ASP ASP B . n 
B 2 67  ILE 67  67  67  ILE ILE B . n 
B 2 68  LEU 68  68  68  LEU LEU B . n 
B 2 69  GLU 69  69  69  GLU GLU B . n 
B 2 70  ARG 70  70  70  ARG ARG B . n 
B 2 71  LYS 71  71  71  LYS LYS B . n 
B 2 72  ARG 72  72  72  ARG ARG B . n 
B 2 73  ALA 73  73  73  ALA ALA B . n 
B 2 74  ALA 74  74  74  ALA ALA B . n 
B 2 75  VAL 75  75  75  VAL VAL B . n 
B 2 76  ASP 76  76  76  ASP ASP B . n 
B 2 77  ARG 77  77  77  ARG ARG B . n 
B 2 78  VAL 78  78  78  VAL VAL B . n 
B 2 79  CYS 79  79  79  CYS CYS B . n 
B 2 80  ARG 80  80  80  ARG ARG B . n 
B 2 81  HIS 81  81  81  HIS HIS B . n 
B 2 82  ASN 82  82  82  ASN ASN B . n 
B 2 83  TYR 83  83  83  TYR TYR B . n 
B 2 84  GLN 84  84  84  GLN GLN B . n 
B 2 85  LEU 85  85  85  LEU LEU B . n 
B 2 86  GLU 86  86  86  GLU GLU B . n 
B 2 87  LEU 87  87  87  LEU LEU B . n 
B 2 88  ARG 88  88  88  ARG ARG B . n 
B 2 89  THR 89  89  89  THR THR B . n 
B 2 90  THR 90  90  90  THR THR B . n 
B 2 91  LEU 91  91  91  LEU LEU B . n 
B 2 92  GLN 92  92  92  GLN GLN B . n 
B 2 93  ARG 93  93  93  ARG ARG B . n 
B 2 94  ARG 94  94  94  ARG ARG B . n 
B 2 95  VAL 95  95  95  VAL VAL B . n 
B 2 96  GLU 96  96  96  GLU GLU B . n 
B 2 97  PRO 97  97  97  PRO PRO B . n 
B 2 98  THR 98  98  98  THR THR B . n 
B 2 99  VAL 99  99  99  VAL VAL B . n 
B 2 100 THR 100 100 100 THR THR B . n 
B 2 101 ILE 101 101 101 ILE ILE B . n 
B 2 102 SER 102 102 102 SER SER B . n 
B 2 103 PRO 103 103 103 PRO PRO B . n 
B 2 104 SER 104 104 104 SER SER B . n 
B 2 105 ARG 105 105 105 ARG ARG B . n 
B 2 106 THR 106 106 106 THR THR B . n 
B 2 107 GLU 107 107 ?   ?   ?   B . n 
B 2 108 ALA 108 108 ?   ?   ?   B . n 
B 2 109 LEU 109 109 ?   ?   ?   B . n 
B 2 110 ASN 110 110 ?   ?   ?   B . n 
B 2 111 HIS 111 111 ?   ?   ?   B . n 
B 2 112 HIS 112 112 112 HIS HIS B . n 
B 2 113 ASN 113 113 113 ASN ASN B . n 
B 2 114 LEU 114 114 114 LEU LEU B . n 
B 2 115 LEU 115 115 115 LEU LEU B . n 
B 2 116 VAL 116 116 116 VAL VAL B . n 
B 2 117 CYS 117 117 117 CYS CYS B . n 
B 2 118 SER 118 118 118 SER SER B . n 
B 2 119 VAL 119 119 119 VAL VAL B . n 
B 2 120 THR 120 120 120 THR THR B . n 
B 2 121 ASP 121 121 121 ASP ASP B . n 
B 2 122 PHE 122 122 122 PHE PHE B . n 
B 2 123 TYR 123 123 123 TYR TYR B . n 
B 2 124 PRO 124 124 124 PRO PRO B . n 
B 2 125 ALA 125 125 125 ALA ALA B . n 
B 2 126 GLN 126 126 126 GLN GLN B . n 
B 2 127 ILE 127 127 127 ILE ILE B . n 
B 2 128 LYS 128 128 128 LYS LYS B . n 
B 2 129 VAL 129 129 129 VAL VAL B . n 
B 2 130 ARG 130 130 130 ARG ARG B . n 
B 2 131 TRP 131 131 131 TRP TRP B . n 
B 2 132 PHE 132 132 132 PHE PHE B . n 
B 2 133 ARG 133 133 133 ARG ARG B . n 
B 2 134 ASN 134 134 134 ASN ASN B . n 
B 2 135 ASP 135 135 135 ASP ASP B . n 
B 2 136 GLN 136 136 136 GLN GLN B . n 
B 2 137 GLU 137 137 137 GLU GLU B . n 
B 2 138 GLU 138 138 138 GLU GLU B . n 
B 2 139 THR 139 139 139 THR THR B . n 
B 2 140 ALA 140 140 140 ALA ALA B . n 
B 2 141 GLY 141 141 141 GLY GLY B . n 
B 2 142 VAL 142 142 142 VAL VAL B . n 
B 2 143 VAL 143 143 143 VAL VAL B . n 
B 2 144 SER 144 144 144 SER SER B . n 
B 2 145 THR 145 145 145 THR THR B . n 
B 2 146 PRO 146 146 146 PRO PRO B . n 
B 2 147 LEU 147 147 147 LEU LEU B . n 
B 2 148 ILE 148 148 148 ILE ILE B . n 
B 2 149 ARG 149 149 149 ARG ARG B . n 
B 2 150 ASN 150 150 150 ASN ASN B . n 
B 2 151 GLY 151 151 151 GLY GLY B . n 
B 2 152 ASP 152 152 152 ASP ASP B . n 
B 2 153 TRP 153 153 153 TRP TRP B . n 
B 2 154 THR 154 154 154 THR THR B . n 
B 2 155 PHE 155 155 155 PHE PHE B . n 
B 2 156 GLN 156 156 156 GLN GLN B . n 
B 2 157 ILE 157 157 157 ILE ILE B . n 
B 2 158 LEU 158 158 158 LEU LEU B . n 
B 2 159 VAL 159 159 159 VAL VAL B . n 
B 2 160 MET 160 160 160 MET MET B . n 
B 2 161 LEU 161 161 161 LEU LEU B . n 
B 2 162 GLU 162 162 162 GLU GLU B . n 
B 2 163 MET 163 163 163 MET MET B . n 
B 2 164 THR 164 164 164 THR THR B . n 
B 2 165 PRO 165 165 165 PRO PRO B . n 
B 2 166 GLN 166 166 166 GLN GLN B . n 
B 2 167 ARG 167 167 167 ARG ARG B . n 
B 2 168 GLY 168 168 168 GLY GLY B . n 
B 2 169 ASP 169 169 169 ASP ASP B . n 
B 2 170 VAL 170 170 170 VAL VAL B . n 
B 2 171 TYR 171 171 171 TYR TYR B . n 
B 2 172 THR 172 172 172 THR THR B . n 
B 2 173 CYS 173 173 173 CYS CYS B . n 
B 2 174 HIS 174 174 174 HIS HIS B . n 
B 2 175 VAL 175 175 175 VAL VAL B . n 
B 2 176 GLU 176 176 176 GLU GLU B . n 
B 2 177 HIS 177 177 177 HIS HIS B . n 
B 2 178 PRO 178 178 178 PRO PRO B . n 
B 2 179 SER 179 179 179 SER SER B . n 
B 2 180 LEU 180 180 180 LEU LEU B . n 
B 2 181 GLN 181 181 181 GLN GLN B . n 
B 2 182 SER 182 182 182 SER SER B . n 
B 2 183 PRO 183 183 183 PRO PRO B . n 
B 2 184 ILE 184 184 184 ILE ILE B . n 
B 2 185 THR 185 185 185 THR THR B . n 
B 2 186 VAL 186 186 186 VAL VAL B . n 
B 2 187 GLU 187 187 187 GLU GLU B . n 
B 2 188 TRP 188 188 188 TRP TRP B . n 
B 2 189 ARG 189 189 189 ARG ARG B . n 
B 2 190 ALA 190 190 190 ALA ALA B . n 
B 2 191 GLN 191 191 191 GLN GLN B . n 
B 2 192 SER 192 192 192 SER SER B . n 
B 2 193 THR 193 193 193 THR THR B . n 
B 2 194 GLY 194 194 194 GLY GLY B . n 
C 3 1   ALA 1   -1  -1  ALA ALA C . n 
C 3 2   THR 2   0   0   THR THR C . n 
C 3 3   PRO 3   1   1   PRO PRO C . n 
C 3 4   LEU 4   2   2   LEU LEU C . n 
C 3 5   LEU 5   3   3   LEU LEU C . n 
C 3 6   MET 6   4   4   MET MET C . n 
C 3 7   GLN 7   5   5   GLN GLN C . n 
C 3 8   ALA 8   6   6   ALA ALA C . n 
C 3 9   LEU 9   7   7   LEU LEU C . n 
C 3 10  PRO 10  8   8   PRO PRO C . n 
C 3 11  MET 11  9   9   MET MET C . n 
C 3 12  GLY 12  10  10  GLY GLY C . n 
C 3 13  ALA 13  11  ?   ?   ?   C . n 
D 4 1   MET 1   -1  ?   ?   ?   D . n 
D 4 2   GLN 2   0   ?   ?   ?   D . n 
D 4 3   ARG 3   1   ?   ?   ?   D . n 
D 4 4   LYS 4   2   2   LYS LYS D . n 
D 4 5   GLU 5   3   3   GLU GLU D . n 
D 4 6   VAL 6   4   4   VAL VAL D . n 
D 4 7   GLU 7   5   5   GLU GLU D . n 
D 4 8   GLN 8   6   6   GLN GLN D . n 
D 4 9   ASP 9   7   7   ASP ASP D . n 
D 4 10  PRO 10  8   8   PRO PRO D . n 
D 4 11  GLY 11  9   9   GLY GLY D . n 
D 4 12  PRO 12  10  10  PRO PRO D . n 
D 4 13  PHE 13  11  11  PHE PHE D . n 
D 4 14  ASN 14  12  12  ASN ASN D . n 
D 4 15  VAL 15  13  13  VAL VAL D . n 
D 4 16  PRO 16  14  14  PRO PRO D . n 
D 4 17  GLU 17  15  15  GLU GLU D . n 
D 4 18  GLY 18  16  16  GLY GLY D . n 
D 4 19  ALA 19  17  17  ALA ALA D . n 
D 4 20  THR 20  18  18  THR THR D . n 
D 4 21  VAL 21  19  19  VAL VAL D . n 
D 4 22  ALA 22  20  20  ALA ALA D . n 
D 4 23  PHE 23  21  21  PHE PHE D . n 
D 4 24  ASN 24  22  22  ASN ASN D . n 
D 4 25  CYS 25  23  23  CYS CYS D . n 
D 4 26  THR 26  24  24  THR THR D . n 
D 4 27  TYR 27  25  25  TYR TYR D . n 
D 4 28  SER 28  26  26  SER SER D . n 
D 4 29  ASN 29  27  27  ASN ASN D . n 
D 4 30  SER 30  28  28  SER SER D . n 
D 4 31  ALA 31  29  29  ALA ALA D . n 
D 4 32  SER 32  36  36  SER SER D . n 
D 4 33  GLN 33  37  37  GLN GLN D . n 
D 4 34  SER 34  38  38  SER SER D . n 
D 4 35  PHE 35  39  39  PHE PHE D . n 
D 4 36  PHE 36  40  40  PHE PHE D . n 
D 4 37  TRP 37  41  41  TRP TRP D . n 
D 4 38  TYR 38  42  42  TYR TYR D . n 
D 4 39  ARG 39  43  43  ARG ARG D . n 
D 4 40  GLN 40  44  44  GLN GLN D . n 
D 4 41  ASP 41  45  45  ASP ASP D . n 
D 4 42  CYS 42  46  46  CYS CYS D . n 
D 4 43  ARG 43  47  47  ARG ARG D . n 
D 4 44  LYS 44  48  48  LYS LYS D . n 
D 4 45  GLU 45  49  49  GLU GLU D . n 
D 4 46  PRO 46  50  50  PRO PRO D . n 
D 4 47  LYS 47  51  51  LYS LYS D . n 
D 4 48  LEU 48  52  52  LEU LEU D . n 
D 4 49  LEU 49  53  53  LEU LEU D . n 
D 4 50  MET 50  54  54  MET MET D . n 
D 4 51  SER 51  55  55  SER SER D . n 
D 4 52  VAL 52  56  56  VAL VAL D . n 
D 4 53  TYR 53  57  57  TYR TYR D . n 
D 4 54  SER 54  58  58  SER SER D . n 
D 4 55  SER 55  63  63  SER SER D . n 
D 4 56  GLY 56  64  64  GLY GLY D . n 
D 4 57  ASN 57  65  65  ASN ASN D . n 
D 4 58  GLU 58  67  67  GLU GLU D . n 
D 4 59  ASP 59  68  68  ASP ASP D . n 
D 4 60  GLY 60  74  74  GLY GLY D . n 
D 4 61  ARG 61  75  75  ARG ARG D . n 
D 4 62  PHE 62  76  76  PHE PHE D . n 
D 4 63  THR 63  77  77  THR THR D . n 
D 4 64  ALA 64  78  78  ALA ALA D . n 
D 4 65  GLN 65  79  79  GLN GLN D . n 
D 4 66  LEU 66  80  80  LEU LEU D . n 
D 4 67  ASN 67  81  81  ASN ASN D . n 
D 4 68  ARG 68  82  82  ARG ARG D . n 
D 4 69  ALA 69  83  83  ALA ALA D . n 
D 4 70  SER 70  84  84  SER SER D . n 
D 4 71  GLN 71  85  85  GLN GLN D . n 
D 4 72  TYR 72  86  86  TYR TYR D . n 
D 4 73  ILE 73  87  87  ILE ILE D . n 
D 4 74  SER 74  88  88  SER SER D . n 
D 4 75  LEU 75  89  89  LEU LEU D . n 
D 4 76  LEU 76  90  90  LEU LEU D . n 
D 4 77  ILE 77  91  91  ILE ILE D . n 
D 4 78  ARG 78  92  92  ARG ARG D . n 
D 4 79  ASP 79  93  93  ASP ASP D . n 
D 4 80  SER 80  94  94  SER SER D . n 
D 4 81  LYS 81  95  95  LYS LYS D . n 
D 4 82  LEU 82  96  96  LEU LEU D . n 
D 4 83  SER 83  97  97  SER SER D . n 
D 4 84  ASP 84  98  98  ASP ASP D . n 
D 4 85  SER 85  99  99  SER SER D . n 
D 4 86  ALA 86  100 100 ALA ALA D . n 
D 4 87  THR 87  101 101 THR THR D . n 
D 4 88  TYR 88  102 102 TYR TYR D . n 
D 4 89  LEU 89  103 103 LEU LEU D . n 
D 4 90  CYS 90  104 104 CYS CYS D . n 
D 4 91  VAL 91  105 105 VAL VAL D . n 
D 4 92  VAL 92  106 106 VAL VAL D . n 
D 4 93  MET 93  107 107 MET MET D . n 
D 4 94  GLY 94  108 108 GLY GLY D . n 
D 4 95  PHE 95  109 109 PHE PHE D . n 
D 4 96  GLN 96  110 110 GLN GLN D . n 
D 4 97  LYS 97  111 111 LYS LYS D . n 
D 4 98  LEU 98  112 112 LEU LEU D . n 
D 4 99  VAL 99  113 113 VAL VAL D . n 
D 4 100 PHE 100 114 114 PHE PHE D . n 
D 4 101 GLY 101 115 115 GLY GLY D . n 
D 4 102 THR 102 116 116 THR THR D . n 
D 4 103 GLY 103 117 117 GLY GLY D . n 
D 4 104 THR 104 118 118 THR THR D . n 
D 4 105 ARG 105 119 119 ARG ARG D . n 
D 4 106 LEU 106 120 120 LEU LEU D . n 
D 4 107 LEU 107 121 121 LEU LEU D . n 
D 4 108 VAL 108 122 122 VAL VAL D . n 
D 4 109 SER 109 123 123 SER SER D . n 
D 4 110 PRO 110 124 124 PRO PRO D . n 
D 4 111 ASN 111 125 125 ASN ASN D . n 
D 4 112 ILE 112 126 126 ILE ILE D . n 
D 4 113 GLN 113 127 127 GLN GLN D . n 
D 4 114 ASN 114 128 128 ASN ASN D . n 
D 4 115 PRO 115 129 129 PRO PRO D . n 
D 4 116 ASP 116 130 130 ASP ASP D . n 
D 4 117 PRO 117 131 131 PRO PRO D . n 
D 4 118 ALA 118 132 132 ALA ALA D . n 
D 4 119 VAL 119 133 133 VAL VAL D . n 
D 4 120 TYR 120 134 134 TYR TYR D . n 
D 4 121 GLN 121 135 135 GLN GLN D . n 
D 4 122 LEU 122 136 136 LEU LEU D . n 
D 4 123 ARG 123 137 137 ARG ARG D . n 
D 4 124 ASP 124 138 138 ASP ASP D . n 
D 4 125 SER 125 139 139 SER SER D . n 
D 4 126 LYS 126 140 140 LYS LYS D . n 
D 4 127 SER 127 141 141 SER SER D . n 
D 4 128 SER 128 142 ?   ?   ?   D . n 
D 4 129 ASP 129 143 143 ASP ASP D . n 
D 4 130 LYS 130 144 144 LYS LYS D . n 
D 4 131 SER 131 145 145 SER SER D . n 
D 4 132 VAL 132 146 146 VAL VAL D . n 
D 4 133 CYS 133 147 147 CYS CYS D . n 
D 4 134 LEU 134 148 148 LEU LEU D . n 
D 4 135 PHE 135 149 149 PHE PHE D . n 
D 4 136 THR 136 150 150 THR THR D . n 
D 4 137 ASP 137 151 151 ASP ASP D . n 
D 4 138 PHE 138 152 152 PHE PHE D . n 
D 4 139 ASP 139 153 153 ASP ASP D . n 
D 4 140 SER 140 154 154 SER SER D . n 
D 4 141 GLN 141 155 155 GLN GLN D . n 
D 4 142 THR 142 156 156 THR THR D . n 
D 4 143 ASN 143 157 157 ASN ASN D . n 
D 4 144 VAL 144 158 158 VAL VAL D . n 
D 4 145 SER 145 159 159 SER SER D . n 
D 4 146 GLN 146 160 160 GLN GLN D . n 
D 4 147 SER 147 161 161 SER SER D . n 
D 4 148 LYS 148 162 162 LYS LYS D . n 
D 4 149 ASP 149 163 163 ASP ASP D . n 
D 4 150 SER 150 164 164 SER SER D . n 
D 4 151 ASP 151 165 165 ASP ASP D . n 
D 4 152 VAL 152 166 166 VAL VAL D . n 
D 4 153 TYR 153 167 167 TYR TYR D . n 
D 4 154 ILE 154 168 168 ILE ILE D . n 
D 4 155 THR 155 169 169 THR THR D . n 
D 4 156 ASP 156 170 170 ASP ASP D . n 
D 4 157 LYS 157 171 171 LYS LYS D . n 
D 4 158 CYS 158 172 172 CYS CYS D . n 
D 4 159 VAL 159 173 173 VAL VAL D . n 
D 4 160 LEU 160 174 174 LEU LEU D . n 
D 4 161 ASP 161 175 175 ASP ASP D . n 
D 4 162 MET 162 176 176 MET MET D . n 
D 4 163 ARG 163 177 177 ARG ARG D . n 
D 4 164 SER 164 178 178 SER SER D . n 
D 4 165 MET 165 179 179 MET MET D . n 
D 4 166 ASP 166 180 180 ASP ASP D . n 
D 4 167 PHE 167 181 181 PHE PHE D . n 
D 4 168 LYS 168 182 182 LYS LYS D . n 
D 4 169 SER 169 183 183 SER SER D . n 
D 4 170 ASN 170 184 184 ASN ASN D . n 
D 4 171 SER 171 185 185 SER SER D . n 
D 4 172 ALA 172 186 186 ALA ALA D . n 
D 4 173 VAL 173 187 187 VAL VAL D . n 
D 4 174 ALA 174 188 188 ALA ALA D . n 
D 4 175 TRP 175 189 189 TRP TRP D . n 
D 4 176 SER 176 190 190 SER SER D . n 
D 4 177 ASN 177 191 191 ASN ASN D . n 
D 4 178 LYS 178 192 192 LYS LYS D . n 
D 4 179 SER 179 193 193 SER SER D . n 
D 4 180 ASP 180 194 194 ASP ASP D . n 
D 4 181 PHE 181 195 195 PHE PHE D . n 
D 4 182 ALA 182 196 196 ALA ALA D . n 
D 4 183 CYS 183 197 197 CYS CYS D . n 
D 4 184 ALA 184 198 198 ALA ALA D . n 
D 4 185 ASN 185 199 199 ASN ASN D . n 
D 4 186 ALA 186 200 200 ALA ALA D . n 
D 4 187 PHE 187 201 201 PHE PHE D . n 
D 4 188 ASN 188 202 202 ASN ASN D . n 
D 4 189 ASN 189 203 203 ASN ASN D . n 
D 4 190 SER 190 204 204 SER SER D . n 
D 4 191 ILE 191 205 ?   ?   ?   D . n 
D 4 192 ILE 192 206 206 ILE ILE D . n 
D 4 193 PRO 193 207 207 PRO PRO D . n 
D 4 194 GLU 194 208 208 GLU GLU D . n 
D 4 195 ASP 195 209 209 ASP ASP D . n 
D 4 196 THR 196 210 210 THR THR D . n 
D 4 197 PHE 197 211 211 PHE PHE D . n 
D 4 198 PHE 198 212 212 PHE PHE D . n 
D 4 199 PRO 199 213 213 PRO PRO D . n 
D 4 200 SER 200 214 ?   ?   ?   D . n 
D 4 201 PRO 201 215 ?   ?   ?   D . n 
D 4 202 GLU 202 216 ?   ?   ?   D . n 
D 4 203 SER 203 217 ?   ?   ?   D . n 
D 4 204 SER 204 218 ?   ?   ?   D . n 
E 5 1   MET 1   2   ?   ?   ?   E . n 
E 5 2   GLY 2   3   3   GLY GLY E . n 
E 5 3   VAL 3   4   4   VAL VAL E . n 
E 5 4   THR 4   5   5   THR THR E . n 
E 5 5   GLN 5   6   6   GLN GLN E . n 
E 5 6   THR 6   7   7   THR THR E . n 
E 5 7   PRO 7   8   8   PRO PRO E . n 
E 5 8   ARG 8   9   9   ARG ARG E . n 
E 5 9   TYR 9   10  10  TYR TYR E . n 
E 5 10  LEU 10  11  11  LEU LEU E . n 
E 5 11  ILE 11  12  12  ILE ILE E . n 
E 5 12  LYS 12  13  13  LYS LYS E . n 
E 5 13  THR 13  14  14  THR THR E . n 
E 5 14  ARG 14  15  15  ARG ARG E . n 
E 5 15  GLY 15  16  16  GLY GLY E . n 
E 5 16  GLN 16  17  17  GLN GLN E . n 
E 5 17  GLN 17  18  18  GLN GLN E . n 
E 5 18  VAL 18  19  19  VAL VAL E . n 
E 5 19  THR 19  20  20  THR THR E . n 
E 5 20  LEU 20  21  21  LEU LEU E . n 
E 5 21  SER 21  22  22  SER SER E . n 
E 5 22  CYS 22  23  23  CYS CYS E . n 
E 5 23  SER 23  24  24  SER SER E . n 
E 5 24  PRO 24  25  25  PRO PRO E . n 
E 5 25  ILE 25  26  26  ILE ILE E . n 
E 5 26  SER 26  27  27  SER SER E . n 
E 5 27  GLY 27  28  28  GLY GLY E . n 
E 5 28  HIS 28  29  29  HIS HIS E . n 
E 5 29  ARG 29  37  37  ARG ARG E . n 
E 5 30  SER 30  38  38  SER SER E . n 
E 5 31  VAL 31  39  39  VAL VAL E . n 
E 5 32  SER 32  40  40  SER SER E . n 
E 5 33  TRP 33  41  41  TRP TRP E . n 
E 5 34  TYR 34  42  42  TYR TYR E . n 
E 5 35  GLN 35  43  43  GLN GLN E . n 
E 5 36  GLN 36  44  44  GLN GLN E . n 
E 5 37  THR 37  45  45  THR THR E . n 
E 5 38  PRO 38  46  46  PRO PRO E . n 
E 5 39  GLY 39  47  47  GLY GLY E . n 
E 5 40  GLN 40  48  48  GLN GLN E . n 
E 5 41  GLY 41  49  49  GLY GLY E . n 
E 5 42  LEU 42  50  50  LEU LEU E . n 
E 5 43  GLN 43  51  51  GLN GLN E . n 
E 5 44  PHE 44  52  52  PHE PHE E . n 
E 5 45  LEU 45  53  53  LEU LEU E . n 
E 5 46  PHE 46  54  54  PHE PHE E . n 
E 5 47  GLU 47  55  55  GLU GLU E . n 
E 5 48  TYR 48  56  56  TYR TYR E . n 
E 5 49  PHE 49  57  57  PHE PHE E . n 
E 5 50  SER 50  58  58  SER SER E . n 
E 5 51  GLU 51  63  63  GLU GLU E . n 
E 5 52  THR 52  64  64  THR THR E . n 
E 5 53  GLN 53  65  65  GLN GLN E . n 
E 5 54  ARG 54  66  66  ARG ARG E . n 
E 5 55  ASN 55  67  67  ASN ASN E . n 
E 5 56  LYS 56  68  68  LYS LYS E . n 
E 5 57  GLY 57  69  69  GLY GLY E . n 
E 5 58  ASN 58  70  70  ASN ASN E . n 
E 5 59  PHE 59  71  71  PHE PHE E . n 
E 5 60  PRO 60  72  72  PRO PRO E . n 
E 5 61  GLY 61  74  74  GLY GLY E . n 
E 5 62  ARG 62  75  75  ARG ARG E . n 
E 5 63  PHE 63  76  76  PHE PHE E . n 
E 5 64  SER 64  77  77  SER SER E . n 
E 5 65  GLY 65  78  78  GLY GLY E . n 
E 5 66  ARG 66  79  79  ARG ARG E . n 
E 5 67  GLN 67  80  80  GLN GLN E . n 
E 5 68  PHE 68  81  81  PHE PHE E . n 
E 5 69  SER 69  83  83  SER SER E . n 
E 5 70  ASN 70  84  84  ASN ASN E . n 
E 5 71  SER 71  85  85  SER SER E . n 
E 5 72  ARG 72  86  86  ARG ARG E . n 
E 5 73  SER 73  87  87  SER SER E . n 
E 5 74  GLU 74  88  88  GLU GLU E . n 
E 5 75  MET 75  89  89  MET MET E . n 
E 5 76  ASN 76  90  90  ASN ASN E . n 
E 5 77  VAL 77  91  91  VAL VAL E . n 
E 5 78  SER 78  92  92  SER SER E . n 
E 5 79  THR 79  93  93  THR THR E . n 
E 5 80  LEU 80  94  94  LEU LEU E . n 
E 5 81  GLU 81  95  95  GLU GLU E . n 
E 5 82  LEU 82  96  96  LEU LEU E . n 
E 5 83  GLY 83  97  97  GLY GLY E . n 
E 5 84  ASP 84  98  98  ASP ASP E . n 
E 5 85  SER 85  99  99  SER SER E . n 
E 5 86  ALA 86  100 100 ALA ALA E . n 
E 5 87  LEU 87  101 101 LEU LEU E . n 
E 5 88  TYR 88  102 102 TYR TYR E . n 
E 5 89  LEU 89  103 103 LEU LEU E . n 
E 5 90  CYS 90  104 104 CYS CYS E . n 
E 5 91  ALA 91  105 105 ALA ALA E . n 
E 5 92  SER 92  106 106 SER SER E . n 
E 5 93  SER 93  107 107 SER SER E . n 
E 5 94  LEU 94  108 108 LEU LEU E . n 
E 5 95  ARG 95  109 109 ARG ARG E . n 
E 5 96  ALA 96  110 110 ALA ALA E . n 
E 5 97  GLU 97  111 111 GLU GLU E . n 
E 5 98  SER 98  112 112 SER SER E . n 
E 5 99  GLY 99  113 113 GLY GLY E . n 
E 5 100 GLU 100 114 114 GLU GLU E . n 
E 5 101 LEU 101 115 115 LEU LEU E . n 
E 5 102 PHE 102 116 116 PHE PHE E . n 
E 5 103 PHE 103 117 117 PHE PHE E . n 
E 5 104 GLY 104 118 118 GLY GLY E . n 
E 5 105 GLU 105 119 119 GLU GLU E . n 
E 5 106 GLY 106 120 120 GLY GLY E . n 
E 5 107 SER 107 121 121 SER SER E . n 
E 5 108 ARG 108 122 122 ARG ARG E . n 
E 5 109 LEU 109 123 123 LEU LEU E . n 
E 5 110 THR 110 124 124 THR THR E . n 
E 5 111 VAL 111 125 125 VAL VAL E . n 
E 5 112 LEU 112 126 126 LEU LEU E . n 
E 5 113 GLU 113 127 127 GLU GLU E . n 
E 5 114 ASP 114 128 128 ASP ASP E . n 
E 5 115 LEU 115 129 129 LEU LEU E . n 
E 5 116 ASN 116 130 130 ASN ASN E . n 
E 5 117 LYS 117 131 131 LYS LYS E . n 
E 5 118 VAL 118 132 132 VAL VAL E . n 
E 5 119 PHE 119 133 133 PHE PHE E . n 
E 5 120 PRO 120 134 134 PRO PRO E . n 
E 5 121 PRO 121 135 135 PRO PRO E . n 
E 5 122 GLU 122 136 136 GLU GLU E . n 
E 5 123 VAL 123 137 137 VAL VAL E . n 
E 5 124 ALA 124 138 138 ALA ALA E . n 
E 5 125 VAL 125 139 139 VAL VAL E . n 
E 5 126 PHE 126 140 140 PHE PHE E . n 
E 5 127 GLU 127 141 141 GLU GLU E . n 
E 5 128 PRO 128 142 142 PRO PRO E . n 
E 5 129 SER 129 143 143 SER SER E . n 
E 5 130 GLU 130 144 144 GLU GLU E . n 
E 5 131 ALA 131 145 145 ALA ALA E . n 
E 5 132 GLU 132 146 146 GLU GLU E . n 
E 5 133 ILE 133 147 147 ILE ILE E . n 
E 5 134 SER 134 148 148 SER SER E . n 
E 5 135 HIS 135 149 149 HIS HIS E . n 
E 5 136 THR 136 150 150 THR THR E . n 
E 5 137 GLN 137 151 151 GLN GLN E . n 
E 5 138 LYS 138 152 152 LYS LYS E . n 
E 5 139 ALA 139 153 153 ALA ALA E . n 
E 5 140 THR 140 154 154 THR THR E . n 
E 5 141 LEU 141 155 155 LEU LEU E . n 
E 5 142 VAL 142 156 156 VAL VAL E . n 
E 5 143 CYS 143 157 157 CYS CYS E . n 
E 5 144 LEU 144 158 158 LEU LEU E . n 
E 5 145 ALA 145 159 159 ALA ALA E . n 
E 5 146 THR 146 160 160 THR THR E . n 
E 5 147 GLY 147 161 161 GLY GLY E . n 
E 5 148 PHE 148 162 162 PHE PHE E . n 
E 5 149 PHE 149 163 163 PHE PHE E . n 
E 5 150 PRO 150 164 164 PRO PRO E . n 
E 5 151 ASP 151 165 165 ASP ASP E . n 
E 5 152 HIS 152 166 166 HIS HIS E . n 
E 5 153 VAL 153 167 167 VAL VAL E . n 
E 5 154 GLU 154 168 168 GLU GLU E . n 
E 5 155 LEU 155 169 169 LEU LEU E . n 
E 5 156 SER 156 170 170 SER SER E . n 
E 5 157 TRP 157 171 171 TRP TRP E . n 
E 5 158 TRP 158 172 172 TRP TRP E . n 
E 5 159 VAL 159 173 173 VAL VAL E . n 
E 5 160 ASN 160 174 174 ASN ASN E . n 
E 5 161 GLY 161 175 175 GLY GLY E . n 
E 5 162 LYS 162 176 176 LYS LYS E . n 
E 5 163 GLU 163 177 177 GLU GLU E . n 
E 5 164 VAL 164 178 178 VAL VAL E . n 
E 5 165 HIS 165 179 179 HIS HIS E . n 
E 5 166 SER 166 180 180 SER SER E . n 
E 5 167 GLY 167 181 181 GLY GLY E . n 
E 5 168 VAL 168 182 182 VAL VAL E . n 
E 5 169 CYS 169 183 183 CYS CYS E . n 
E 5 170 THR 170 184 184 THR THR E . n 
E 5 171 ASP 171 185 185 ASP ASP E . n 
E 5 172 PRO 172 186 186 PRO PRO E . n 
E 5 173 GLN 173 187 187 GLN GLN E . n 
E 5 174 PRO 174 188 188 PRO PRO E . n 
E 5 175 LEU 175 189 189 LEU LEU E . n 
E 5 176 LYS 176 190 190 LYS LYS E . n 
E 5 177 GLU 177 191 191 GLU GLU E . n 
E 5 178 GLN 178 192 192 GLN GLN E . n 
E 5 179 PRO 179 193 193 PRO PRO E . n 
E 5 180 ALA 180 194 194 ALA ALA E . n 
E 5 181 LEU 181 195 195 LEU LEU E . n 
E 5 182 ASN 182 196 196 ASN ASN E . n 
E 5 183 ASP 183 197 197 ASP ASP E . n 
E 5 184 SER 184 198 198 SER SER E . n 
E 5 185 ARG 185 199 199 ARG ARG E . n 
E 5 186 TYR 186 200 200 TYR TYR E . n 
E 5 187 ALA 187 201 201 ALA ALA E . n 
E 5 188 LEU 188 202 202 LEU LEU E . n 
E 5 189 SER 189 203 203 SER SER E . n 
E 5 190 SER 190 204 204 SER SER E . n 
E 5 191 ARG 191 205 205 ARG ARG E . n 
E 5 192 LEU 192 206 206 LEU LEU E . n 
E 5 193 ARG 193 207 207 ARG ARG E . n 
E 5 194 VAL 194 208 208 VAL VAL E . n 
E 5 195 SER 195 209 209 SER SER E . n 
E 5 196 ALA 196 210 210 ALA ALA E . n 
E 5 197 THR 197 211 211 THR THR E . n 
E 5 198 PHE 198 212 212 PHE PHE E . n 
E 5 199 TRP 199 213 213 TRP TRP E . n 
E 5 200 GLN 200 214 214 GLN GLN E . n 
E 5 201 ASN 201 215 215 ASN ASN E . n 
E 5 202 PRO 202 216 216 PRO PRO E . n 
E 5 203 ARG 203 217 217 ARG ARG E . n 
E 5 204 ASN 204 218 218 ASN ASN E . n 
E 5 205 HIS 205 219 219 HIS HIS E . n 
E 5 206 PHE 206 220 220 PHE PHE E . n 
E 5 207 ARG 207 221 221 ARG ARG E . n 
E 5 208 CYS 208 222 222 CYS CYS E . n 
E 5 209 GLN 209 223 223 GLN GLN E . n 
E 5 210 VAL 210 224 224 VAL VAL E . n 
E 5 211 GLN 211 225 225 GLN GLN E . n 
E 5 212 PHE 212 226 226 PHE PHE E . n 
E 5 213 TYR 213 227 227 TYR TYR E . n 
E 5 214 GLY 214 228 228 GLY GLY E . n 
E 5 215 LEU 215 229 229 LEU LEU E . n 
E 5 216 SER 216 230 230 SER SER E . n 
E 5 217 GLU 217 231 231 GLU GLU E . n 
E 5 218 ASN 218 232 232 ASN ASN E . n 
E 5 219 ASP 219 233 233 ASP ASP E . n 
E 5 220 GLU 220 234 234 GLU GLU E . n 
E 5 221 TRP 221 235 235 TRP TRP E . n 
E 5 222 THR 222 236 236 THR THR E . n 
E 5 223 GLN 223 237 237 GLN GLN E . n 
E 5 224 ASP 224 238 238 ASP ASP E . n 
E 5 225 ARG 225 239 239 ARG ARG E . n 
E 5 226 ALA 226 240 240 ALA ALA E . n 
E 5 227 LYS 227 241 241 LYS LYS E . n 
E 5 228 PRO 228 242 242 PRO PRO E . n 
E 5 229 VAL 229 243 243 VAL VAL E . n 
E 5 230 THR 230 244 244 THR THR E . n 
E 5 231 GLN 231 245 245 GLN GLN E . n 
E 5 232 ILE 232 246 246 ILE ILE E . n 
E 5 233 VAL 233 247 247 VAL VAL E . n 
E 5 234 SER 234 248 248 SER SER E . n 
E 5 235 ALA 235 249 249 ALA ALA E . n 
E 5 236 GLU 236 250 250 GLU GLU E . n 
E 5 237 ALA 237 251 251 ALA ALA E . n 
E 5 238 TRP 238 252 252 TRP TRP E . n 
E 5 239 GLY 239 253 253 GLY GLY E . n 
E 5 240 ARG 240 254 254 ARG ARG E . n 
E 5 241 ALA 241 255 255 ALA ALA E . n 
E 5 242 ASP 242 256 ?   ?   ?   E . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
F 6 NAG 1  201 183 NAG NAG A . 
G 7 ACT 1  201 201 ACT ACT B . 
H 6 NAG 1  202 202 NAG NAG B . 
I 7 ACT 1  203 204 ACT ACT B . 
J 8 GOL 1  204 205 GOL GOL B . 
K 7 ACT 1  301 301 ACT ACT E . 
L 7 ACT 1  302 302 ACT ACT E . 
M 9 HOH 1  301 201 HOH HOH A . 
M 9 HOH 2  302 2   HOH HOH A . 
M 9 HOH 3  303 86  HOH HOH A . 
M 9 HOH 4  304 112 HOH HOH A . 
M 9 HOH 5  305 79  HOH HOH A . 
M 9 HOH 6  306 53  HOH HOH A . 
M 9 HOH 7  307 114 HOH HOH A . 
M 9 HOH 8  308 3   HOH HOH A . 
M 9 HOH 9  309 51  HOH HOH A . 
M 9 HOH 10 310 4   HOH HOH A . 
M 9 HOH 11 311 49  HOH HOH A . 
M 9 HOH 12 312 45  HOH HOH A . 
M 9 HOH 13 313 75  HOH HOH A . 
M 9 HOH 14 314 74  HOH HOH A . 
M 9 HOH 15 315 12  HOH HOH A . 
M 9 HOH 16 316 69  HOH HOH A . 
M 9 HOH 17 317 78  HOH HOH A . 
M 9 HOH 18 318 36  HOH HOH A . 
M 9 HOH 19 319 156 HOH HOH A . 
M 9 HOH 20 320 101 HOH HOH A . 
M 9 HOH 21 321 5   HOH HOH A . 
M 9 HOH 22 322 197 HOH HOH A . 
M 9 HOH 23 323 147 HOH HOH A . 
M 9 HOH 24 324 28  HOH HOH A . 
M 9 HOH 25 325 98  HOH HOH A . 
M 9 HOH 26 326 90  HOH HOH A . 
M 9 HOH 27 327 253 HOH HOH A . 
M 9 HOH 28 328 31  HOH HOH A . 
M 9 HOH 29 329 27  HOH HOH A . 
M 9 HOH 30 330 165 HOH HOH A . 
M 9 HOH 31 331 70  HOH HOH A . 
M 9 HOH 32 332 247 HOH HOH A . 
M 9 HOH 33 333 11  HOH HOH A . 
M 9 HOH 34 334 185 HOH HOH A . 
M 9 HOH 35 335 93  HOH HOH A . 
M 9 HOH 36 336 210 HOH HOH A . 
M 9 HOH 37 337 265 HOH HOH A . 
M 9 HOH 38 338 221 HOH HOH A . 
M 9 HOH 39 339 95  HOH HOH A . 
M 9 HOH 40 340 223 HOH HOH A . 
M 9 HOH 41 341 243 HOH HOH A . 
M 9 HOH 42 342 246 HOH HOH A . 
M 9 HOH 43 343 254 HOH HOH A . 
M 9 HOH 44 344 262 HOH HOH A . 
M 9 HOH 45 345 286 HOH HOH A . 
M 9 HOH 46 346 257 HOH HOH A . 
M 9 HOH 47 347 264 HOH HOH A . 
M 9 HOH 48 348 255 HOH HOH A . 
M 9 HOH 49 349 258 HOH HOH A . 
M 9 HOH 50 350 256 HOH HOH A . 
M 9 HOH 51 351 289 HOH HOH A . 
M 9 HOH 52 352 244 HOH HOH A . 
M 9 HOH 53 353 288 HOH HOH A . 
M 9 HOH 54 354 263 HOH HOH A . 
M 9 HOH 55 355 172 HOH HOH A . 
M 9 HOH 56 356 214 HOH HOH A . 
M 9 HOH 57 357 225 HOH HOH A . 
M 9 HOH 58 358 206 HOH HOH A . 
M 9 HOH 59 359 245 HOH HOH A . 
M 9 HOH 60 360 174 HOH HOH A . 
M 9 HOH 61 361 167 HOH HOH A . 
M 9 HOH 62 362 152 HOH HOH A . 
M 9 HOH 63 363 62  HOH HOH A . 
N 9 HOH 1  301 123 HOH HOH B . 
N 9 HOH 2  302 47  HOH HOH B . 
N 9 HOH 3  303 128 HOH HOH B . 
N 9 HOH 4  304 76  HOH HOH B . 
N 9 HOH 5  305 104 HOH HOH B . 
N 9 HOH 6  306 301 HOH HOH B . 
N 9 HOH 7  307 1   HOH HOH B . 
N 9 HOH 8  308 182 HOH HOH B . 
N 9 HOH 9  309 63  HOH HOH B . 
N 9 HOH 10 310 179 HOH HOH B . 
N 9 HOH 11 311 6   HOH HOH B . 
N 9 HOH 12 312 84  HOH HOH B . 
N 9 HOH 13 313 38  HOH HOH B . 
N 9 HOH 14 314 56  HOH HOH B . 
N 9 HOH 15 315 135 HOH HOH B . 
N 9 HOH 16 316 8   HOH HOH B . 
N 9 HOH 17 317 10  HOH HOH B . 
N 9 HOH 18 318 163 HOH HOH B . 
N 9 HOH 19 319 102 HOH HOH B . 
N 9 HOH 20 320 290 HOH HOH B . 
N 9 HOH 21 321 88  HOH HOH B . 
N 9 HOH 22 322 124 HOH HOH B . 
N 9 HOH 23 323 30  HOH HOH B . 
N 9 HOH 24 324 105 HOH HOH B . 
N 9 HOH 25 325 77  HOH HOH B . 
N 9 HOH 26 326 37  HOH HOH B . 
N 9 HOH 27 327 115 HOH HOH B . 
N 9 HOH 28 328 21  HOH HOH B . 
N 9 HOH 29 329 113 HOH HOH B . 
N 9 HOH 30 330 67  HOH HOH B . 
N 9 HOH 31 331 218 HOH HOH B . 
N 9 HOH 32 332 52  HOH HOH B . 
N 9 HOH 33 333 125 HOH HOH B . 
N 9 HOH 34 334 54  HOH HOH B . 
N 9 HOH 35 335 195 HOH HOH B . 
N 9 HOH 36 336 230 HOH HOH B . 
N 9 HOH 37 337 44  HOH HOH B . 
N 9 HOH 38 338 120 HOH HOH B . 
N 9 HOH 39 339 127 HOH HOH B . 
N 9 HOH 40 340 92  HOH HOH B . 
N 9 HOH 41 341 162 HOH HOH B . 
N 9 HOH 42 342 29  HOH HOH B . 
N 9 HOH 43 343 25  HOH HOH B . 
N 9 HOH 44 344 138 HOH HOH B . 
N 9 HOH 45 345 215 HOH HOH B . 
N 9 HOH 46 346 292 HOH HOH B . 
N 9 HOH 47 347 97  HOH HOH B . 
N 9 HOH 48 348 202 HOH HOH B . 
N 9 HOH 49 349 251 HOH HOH B . 
N 9 HOH 50 350 213 HOH HOH B . 
N 9 HOH 51 351 296 HOH HOH B . 
N 9 HOH 52 352 23  HOH HOH B . 
N 9 HOH 53 353 119 HOH HOH B . 
N 9 HOH 54 354 284 HOH HOH B . 
N 9 HOH 55 355 304 HOH HOH B . 
N 9 HOH 56 356 260 HOH HOH B . 
N 9 HOH 57 357 303 HOH HOH B . 
N 9 HOH 58 358 170 HOH HOH B . 
N 9 HOH 59 359 96  HOH HOH B . 
N 9 HOH 60 360 183 HOH HOH B . 
N 9 HOH 61 361 249 HOH HOH B . 
N 9 HOH 62 362 259 HOH HOH B . 
N 9 HOH 63 363 161 HOH HOH B . 
N 9 HOH 64 364 241 HOH HOH B . 
N 9 HOH 65 365 308 HOH HOH B . 
N 9 HOH 66 366 193 HOH HOH B . 
N 9 HOH 67 367 307 HOH HOH B . 
N 9 HOH 68 368 252 HOH HOH B . 
N 9 HOH 69 369 261 HOH HOH B . 
N 9 HOH 70 370 242 HOH HOH B . 
N 9 HOH 71 371 46  HOH HOH B . 
N 9 HOH 72 372 176 HOH HOH B . 
N 9 HOH 73 373 306 HOH HOH B . 
N 9 HOH 74 374 299 HOH HOH B . 
N 9 HOH 75 375 150 HOH HOH B . 
N 9 HOH 76 376 199 HOH HOH B . 
N 9 HOH 77 377 291 HOH HOH B . 
N 9 HOH 78 378 89  HOH HOH B . 
N 9 HOH 79 379 287 HOH HOH B . 
N 9 HOH 80 380 248 HOH HOH B . 
N 9 HOH 81 381 224 HOH HOH B . 
N 9 HOH 82 382 181 HOH HOH B . 
N 9 HOH 83 383 305 HOH HOH B . 
O 9 HOH 1  101 298 HOH HOH C . 
O 9 HOH 2  102 153 HOH HOH C . 
O 9 HOH 3  103 175 HOH HOH C . 
P 9 HOH 1  301 82  HOH HOH D . 
P 9 HOH 2  302 142 HOH HOH D . 
P 9 HOH 3  303 13  HOH HOH D . 
P 9 HOH 4  304 59  HOH HOH D . 
P 9 HOH 5  305 18  HOH HOH D . 
P 9 HOH 6  306 72  HOH HOH D . 
P 9 HOH 7  307 41  HOH HOH D . 
P 9 HOH 8  308 192 HOH HOH D . 
P 9 HOH 9  309 141 HOH HOH D . 
P 9 HOH 10 310 187 HOH HOH D . 
P 9 HOH 11 311 61  HOH HOH D . 
P 9 HOH 12 312 194 HOH HOH D . 
P 9 HOH 13 313 143 HOH HOH D . 
P 9 HOH 14 314 229 HOH HOH D . 
P 9 HOH 15 315 160 HOH HOH D . 
P 9 HOH 16 316 64  HOH HOH D . 
P 9 HOH 17 317 60  HOH HOH D . 
P 9 HOH 18 318 42  HOH HOH D . 
P 9 HOH 19 319 94  HOH HOH D . 
P 9 HOH 20 320 83  HOH HOH D . 
P 9 HOH 21 321 122 HOH HOH D . 
P 9 HOH 22 322 212 HOH HOH D . 
P 9 HOH 23 323 133 HOH HOH D . 
P 9 HOH 24 324 279 HOH HOH D . 
P 9 HOH 25 325 58  HOH HOH D . 
P 9 HOH 26 326 154 HOH HOH D . 
P 9 HOH 27 327 275 HOH HOH D . 
P 9 HOH 28 328 166 HOH HOH D . 
P 9 HOH 29 329 285 HOH HOH D . 
P 9 HOH 30 330 107 HOH HOH D . 
P 9 HOH 31 331 277 HOH HOH D . 
P 9 HOH 32 332 171 HOH HOH D . 
P 9 HOH 33 333 200 HOH HOH D . 
P 9 HOH 34 334 134 HOH HOH D . 
P 9 HOH 35 335 139 HOH HOH D . 
P 9 HOH 36 336 108 HOH HOH D . 
P 9 HOH 37 337 184 HOH HOH D . 
P 9 HOH 38 338 168 HOH HOH D . 
P 9 HOH 39 339 294 HOH HOH D . 
P 9 HOH 40 340 272 HOH HOH D . 
P 9 HOH 41 341 164 HOH HOH D . 
P 9 HOH 42 342 228 HOH HOH D . 
P 9 HOH 43 343 91  HOH HOH D . 
P 9 HOH 44 344 276 HOH HOH D . 
P 9 HOH 45 345 278 HOH HOH D . 
P 9 HOH 46 346 236 HOH HOH D . 
P 9 HOH 47 347 231 HOH HOH D . 
P 9 HOH 48 348 208 HOH HOH D . 
P 9 HOH 49 349 273 HOH HOH D . 
P 9 HOH 50 350 234 HOH HOH D . 
P 9 HOH 51 351 109 HOH HOH D . 
P 9 HOH 52 352 140 HOH HOH D . 
P 9 HOH 53 353 159 HOH HOH D . 
P 9 HOH 54 354 198 HOH HOH D . 
P 9 HOH 55 355 205 HOH HOH D . 
P 9 HOH 56 356 209 HOH HOH D . 
P 9 HOH 57 357 266 HOH HOH D . 
P 9 HOH 58 358 280 HOH HOH D . 
P 9 HOH 59 359 274 HOH HOH D . 
Q 9 HOH 1  401 57  HOH HOH E . 
Q 9 HOH 2  402 203 HOH HOH E . 
Q 9 HOH 3  403 110 HOH HOH E . 
Q 9 HOH 4  404 43  HOH HOH E . 
Q 9 HOH 5  405 189 HOH HOH E . 
Q 9 HOH 6  406 50  HOH HOH E . 
Q 9 HOH 7  407 155 HOH HOH E . 
Q 9 HOH 8  408 55  HOH HOH E . 
Q 9 HOH 9  409 39  HOH HOH E . 
Q 9 HOH 10 410 146 HOH HOH E . 
Q 9 HOH 11 411 136 HOH HOH E . 
Q 9 HOH 12 412 17  HOH HOH E . 
Q 9 HOH 13 413 191 HOH HOH E . 
Q 9 HOH 14 414 148 HOH HOH E . 
Q 9 HOH 15 415 132 HOH HOH E . 
Q 9 HOH 16 416 190 HOH HOH E . 
Q 9 HOH 17 417 65  HOH HOH E . 
Q 9 HOH 18 418 9   HOH HOH E . 
Q 9 HOH 19 419 85  HOH HOH E . 
Q 9 HOH 20 420 19  HOH HOH E . 
Q 9 HOH 21 421 137 HOH HOH E . 
Q 9 HOH 22 422 7   HOH HOH E . 
Q 9 HOH 23 423 16  HOH HOH E . 
Q 9 HOH 24 424 68  HOH HOH E . 
Q 9 HOH 25 425 196 HOH HOH E . 
Q 9 HOH 26 426 14  HOH HOH E . 
Q 9 HOH 27 427 22  HOH HOH E . 
Q 9 HOH 28 428 66  HOH HOH E . 
Q 9 HOH 29 429 99  HOH HOH E . 
Q 9 HOH 30 430 226 HOH HOH E . 
Q 9 HOH 31 431 35  HOH HOH E . 
Q 9 HOH 32 432 207 HOH HOH E . 
Q 9 HOH 33 433 87  HOH HOH E . 
Q 9 HOH 34 434 15  HOH HOH E . 
Q 9 HOH 35 435 116 HOH HOH E . 
Q 9 HOH 36 436 20  HOH HOH E . 
Q 9 HOH 37 437 34  HOH HOH E . 
Q 9 HOH 38 438 26  HOH HOH E . 
Q 9 HOH 39 439 297 HOH HOH E . 
Q 9 HOH 40 440 204 HOH HOH E . 
Q 9 HOH 41 441 131 HOH HOH E . 
Q 9 HOH 42 442 177 HOH HOH E . 
Q 9 HOH 43 443 71  HOH HOH E . 
Q 9 HOH 44 444 145 HOH HOH E . 
Q 9 HOH 45 445 186 HOH HOH E . 
Q 9 HOH 46 446 130 HOH HOH E . 
Q 9 HOH 47 447 169 HOH HOH E . 
Q 9 HOH 48 448 80  HOH HOH E . 
Q 9 HOH 49 449 33  HOH HOH E . 
Q 9 HOH 50 450 188 HOH HOH E . 
Q 9 HOH 51 451 106 HOH HOH E . 
Q 9 HOH 52 452 129 HOH HOH E . 
Q 9 HOH 53 453 237 HOH HOH E . 
Q 9 HOH 54 454 235 HOH HOH E . 
Q 9 HOH 55 455 103 HOH HOH E . 
Q 9 HOH 56 456 118 HOH HOH E . 
Q 9 HOH 57 457 111 HOH HOH E . 
Q 9 HOH 58 458 268 HOH HOH E . 
Q 9 HOH 59 459 73  HOH HOH E . 
Q 9 HOH 60 460 48  HOH HOH E . 
Q 9 HOH 61 461 217 HOH HOH E . 
Q 9 HOH 62 462 126 HOH HOH E . 
Q 9 HOH 63 463 227 HOH HOH E . 
Q 9 HOH 64 464 180 HOH HOH E . 
Q 9 HOH 65 465 270 HOH HOH E . 
Q 9 HOH 66 466 173 HOH HOH E . 
Q 9 HOH 67 467 233 HOH HOH E . 
Q 9 HOH 68 468 158 HOH HOH E . 
Q 9 HOH 69 469 281 HOH HOH E . 
Q 9 HOH 70 470 32  HOH HOH E . 
Q 9 HOH 71 471 293 HOH HOH E . 
Q 9 HOH 72 472 149 HOH HOH E . 
Q 9 HOH 73 473 222 HOH HOH E . 
Q 9 HOH 74 474 219 HOH HOH E . 
Q 9 HOH 75 475 267 HOH HOH E . 
Q 9 HOH 76 476 282 HOH HOH E . 
Q 9 HOH 77 477 300 HOH HOH E . 
Q 9 HOH 78 478 295 HOH HOH E . 
Q 9 HOH 79 479 81  HOH HOH E . 
Q 9 HOH 80 480 238 HOH HOH E . 
Q 9 HOH 81 481 283 HOH HOH E . 
Q 9 HOH 82 482 211 HOH HOH E . 
Q 9 HOH 83 483 144 HOH HOH E . 
Q 9 HOH 84 484 220 HOH HOH E . 
Q 9 HOH 85 485 269 HOH HOH E . 
Q 9 HOH 86 486 216 HOH HOH E . 
Q 9 HOH 87 487 302 HOH HOH E . 
Q 9 HOH 88 488 271 HOH HOH E . 
Q 9 HOH 89 489 178 HOH HOH E . 
# 
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 A GLU 1   ? CG  ? A GLU 1   CG  
2   1 Y 1 A GLU 1   ? CD  ? A GLU 1   CD  
3   1 Y 1 A GLU 1   ? OE1 ? A GLU 1   OE1 
4   1 Y 1 A GLU 1   ? OE2 ? A GLU 1   OE2 
5   1 Y 1 A LYS 41  ? CG  ? A LYS 42  CG  
6   1 Y 1 A LYS 41  ? CD  ? A LYS 42  CD  
7   1 Y 1 A LYS 41  ? CE  ? A LYS 42  CE  
8   1 Y 1 A LYS 41  ? NZ  ? A LYS 42  NZ  
9   1 Y 1 A GLU 42  ? CG  ? A GLU 43  CG  
10  1 Y 1 A GLU 42  ? CD  ? A GLU 43  CD  
11  1 Y 1 A GLU 42  ? OE1 ? A GLU 43  OE1 
12  1 Y 1 A GLU 42  ? OE2 ? A GLU 43  OE2 
13  1 Y 1 A ARG 54  ? CG  ? A ARG 55  CG  
14  1 Y 1 A ARG 54  ? CD  ? A ARG 55  CD  
15  1 Y 1 A ARG 54  ? NE  ? A ARG 55  NE  
16  1 Y 1 A ARG 54  ? CZ  ? A ARG 55  CZ  
17  1 Y 1 A ARG 54  ? NH1 ? A ARG 55  NH1 
18  1 Y 1 A ARG 54  ? NH2 ? A ARG 55  NH2 
19  1 Y 1 A LYS 69  ? CG  ? A LYS 69  CG  
20  1 Y 1 A LYS 69  ? CD  ? A LYS 69  CD  
21  1 Y 1 A LYS 69  ? CE  ? A LYS 69  CE  
22  1 Y 1 A LYS 69  ? NZ  ? A LYS 69  NZ  
23  1 Y 1 A ARG 78  ? CG  ? A ARG 78  CG  
24  1 Y 1 A ARG 78  ? CD  ? A ARG 78  CD  
25  1 Y 1 A ARG 78  ? NE  ? A ARG 78  NE  
26  1 Y 1 A ARG 78  ? CZ  ? A ARG 78  CZ  
27  1 Y 1 A ARG 78  ? NH1 ? A ARG 78  NH1 
28  1 Y 1 A ARG 78  ? NH2 ? A ARG 78  NH2 
29  1 Y 1 A ASN 80  ? CG  ? A ASN 80  CG  
30  1 Y 1 A ASN 80  ? OD1 ? A ASN 80  OD1 
31  1 Y 1 A ASN 80  ? ND2 ? A ASN 80  ND2 
32  1 Y 1 A GLN 103 ? CG  ? A GLN 103 CG  
33  1 Y 1 A GLN 103 ? CD  ? A GLN 103 CD  
34  1 Y 1 A GLN 103 ? OE1 ? A GLN 103 OE1 
35  1 Y 1 A GLN 103 ? NE2 ? A GLN 103 NE2 
36  1 Y 1 A ASN 126 ? CG  ? A ASN 126 CG  
37  1 Y 1 A ASN 126 ? OD1 ? A ASN 126 OD1 
38  1 Y 1 A ASN 126 ? ND2 ? A ASN 126 ND2 
39  1 Y 1 A GLU 132 ? CG  ? A GLU 132 CG  
40  1 Y 1 A GLU 132 ? CD  ? A GLU 132 CD  
41  1 Y 1 A GLU 132 ? OE1 ? A GLU 132 OE1 
42  1 Y 1 A GLU 132 ? OE2 ? A GLU 132 OE2 
43  1 Y 1 A GLU 160 ? CG  ? A GLU 160 CG  
44  1 Y 1 A GLU 160 ? CD  ? A GLU 160 CD  
45  1 Y 1 A GLU 160 ? OE1 ? A GLU 160 OE1 
46  1 Y 1 A GLU 160 ? OE2 ? A GLU 160 OE2 
47  1 Y 1 A LYS 174 ? CG  ? A LYS 174 CG  
48  1 Y 1 A LYS 174 ? CD  ? A LYS 174 CD  
49  1 Y 1 A LYS 174 ? CE  ? A LYS 174 CE  
50  1 Y 1 A LYS 174 ? NZ  ? A LYS 174 NZ  
51  1 Y 1 A GLU 181 ? CG  ? A GLU 181 CG  
52  1 Y 1 A GLU 181 ? CD  ? A GLU 181 CD  
53  1 Y 1 A GLU 181 ? OE1 ? A GLU 181 OE1 
54  1 Y 1 A GLU 181 ? OE2 ? A GLU 181 OE2 
55  1 Y 1 B LYS 65  ? CG  ? B LYS 65  CG  
56  1 Y 1 B LYS 65  ? CD  ? B LYS 65  CD  
57  1 Y 1 B LYS 65  ? CE  ? B LYS 65  CE  
58  1 Y 1 B LYS 65  ? NZ  ? B LYS 65  NZ  
59  1 Y 1 B ARG 105 ? CG  ? B ARG 105 CG  
60  1 Y 1 B ARG 105 ? CD  ? B ARG 105 CD  
61  1 Y 1 B ARG 105 ? NE  ? B ARG 105 NE  
62  1 Y 1 B ARG 105 ? CZ  ? B ARG 105 CZ  
63  1 Y 1 B ARG 105 ? NH1 ? B ARG 105 NH1 
64  1 Y 1 B ARG 105 ? NH2 ? B ARG 105 NH2 
65  1 Y 1 B GLU 162 ? CG  ? B GLU 162 CG  
66  1 Y 1 B GLU 162 ? CD  ? B GLU 162 CD  
67  1 Y 1 B GLU 162 ? OE1 ? B GLU 162 OE1 
68  1 Y 1 B GLU 162 ? OE2 ? B GLU 162 OE2 
69  1 Y 1 B GLN 181 ? CG  ? B GLN 181 CG  
70  1 Y 1 B GLN 181 ? CD  ? B GLN 181 CD  
71  1 Y 1 B GLN 181 ? OE1 ? B GLN 181 OE1 
72  1 Y 1 B GLN 181 ? NE2 ? B GLN 181 NE2 
73  1 Y 1 D ASN 125 ? CG  ? D ASN 111 CG  
74  1 Y 1 D ASN 125 ? OD1 ? D ASN 111 OD1 
75  1 Y 1 D ASN 125 ? ND2 ? D ASN 111 ND2 
76  1 Y 1 D GLN 127 ? CG  ? D GLN 113 CG  
77  1 Y 1 D GLN 127 ? CD  ? D GLN 113 CD  
78  1 Y 1 D GLN 127 ? OE1 ? D GLN 113 OE1 
79  1 Y 1 D GLN 127 ? NE2 ? D GLN 113 NE2 
80  1 Y 1 D ARG 137 ? CG  ? D ARG 123 CG  
81  1 Y 1 D ARG 137 ? CD  ? D ARG 123 CD  
82  1 Y 1 D ARG 137 ? NE  ? D ARG 123 NE  
83  1 Y 1 D ARG 137 ? CZ  ? D ARG 123 CZ  
84  1 Y 1 D ARG 137 ? NH1 ? D ARG 123 NH1 
85  1 Y 1 D ARG 137 ? NH2 ? D ARG 123 NH2 
86  1 Y 1 D LYS 140 ? CG  ? D LYS 126 CG  
87  1 Y 1 D LYS 140 ? CD  ? D LYS 126 CD  
88  1 Y 1 D LYS 140 ? CE  ? D LYS 126 CE  
89  1 Y 1 D LYS 140 ? NZ  ? D LYS 126 NZ  
90  1 Y 1 D SER 141 ? OG  ? D SER 127 OG  
91  1 Y 1 D ASP 143 ? CG  ? D ASP 129 CG  
92  1 Y 1 D ASP 143 ? OD1 ? D ASP 129 OD1 
93  1 Y 1 D ASP 143 ? OD2 ? D ASP 129 OD2 
94  1 Y 1 D LYS 144 ? CG  ? D LYS 130 CG  
95  1 Y 1 D LYS 144 ? CD  ? D LYS 130 CD  
96  1 Y 1 D LYS 144 ? CE  ? D LYS 130 CE  
97  1 Y 1 D LYS 144 ? NZ  ? D LYS 130 NZ  
98  1 Y 1 D GLN 155 ? CG  ? D GLN 141 CG  
99  1 Y 1 D GLN 155 ? CD  ? D GLN 141 CD  
100 1 Y 1 D GLN 155 ? OE1 ? D GLN 141 OE1 
101 1 Y 1 D GLN 155 ? NE2 ? D GLN 141 NE2 
102 1 Y 1 D ASN 157 ? CG  ? D ASN 143 CG  
103 1 Y 1 D ASN 157 ? OD1 ? D ASN 143 OD1 
104 1 Y 1 D ASN 157 ? ND2 ? D ASN 143 ND2 
105 1 Y 1 D GLN 160 ? CG  ? D GLN 146 CG  
106 1 Y 1 D GLN 160 ? CD  ? D GLN 146 CD  
107 1 Y 1 D GLN 160 ? OE1 ? D GLN 146 OE1 
108 1 Y 1 D GLN 160 ? NE2 ? D GLN 146 NE2 
109 1 Y 1 D LYS 162 ? CG  ? D LYS 148 CG  
110 1 Y 1 D LYS 162 ? CD  ? D LYS 148 CD  
111 1 Y 1 D LYS 162 ? CE  ? D LYS 148 CE  
112 1 Y 1 D LYS 162 ? NZ  ? D LYS 148 NZ  
113 1 Y 1 D ASP 163 ? CG  ? D ASP 149 CG  
114 1 Y 1 D ASP 163 ? OD1 ? D ASP 149 OD1 
115 1 Y 1 D ASP 163 ? OD2 ? D ASP 149 OD2 
116 1 Y 1 D SER 164 ? OG  ? D SER 150 OG  
117 1 Y 1 D ASP 165 ? CG  ? D ASP 151 CG  
118 1 Y 1 D ASP 165 ? OD1 ? D ASP 151 OD1 
119 1 Y 1 D ASP 165 ? OD2 ? D ASP 151 OD2 
120 1 Y 1 D ASP 170 ? CG  ? D ASP 156 CG  
121 1 Y 1 D ASP 170 ? OD1 ? D ASP 156 OD1 
122 1 Y 1 D ASP 170 ? OD2 ? D ASP 156 OD2 
123 1 Y 1 D ARG 177 ? CG  ? D ARG 163 CG  
124 1 Y 1 D ARG 177 ? CD  ? D ARG 163 CD  
125 1 Y 1 D ARG 177 ? NE  ? D ARG 163 NE  
126 1 Y 1 D ARG 177 ? CZ  ? D ARG 163 CZ  
127 1 Y 1 D ARG 177 ? NH1 ? D ARG 163 NH1 
128 1 Y 1 D ARG 177 ? NH2 ? D ARG 163 NH2 
129 1 Y 1 D SER 178 ? OG  ? D SER 164 OG  
130 1 Y 1 D ASP 180 ? CG  ? D ASP 166 CG  
131 1 Y 1 D ASP 180 ? OD1 ? D ASP 166 OD1 
132 1 Y 1 D ASP 180 ? OD2 ? D ASP 166 OD2 
133 1 Y 1 D ASN 191 ? CG  ? D ASN 177 CG  
134 1 Y 1 D ASN 191 ? OD1 ? D ASN 177 OD1 
135 1 Y 1 D ASN 191 ? ND2 ? D ASN 177 ND2 
136 1 Y 1 D LYS 192 ? CG  ? D LYS 178 CG  
137 1 Y 1 D LYS 192 ? CD  ? D LYS 178 CD  
138 1 Y 1 D LYS 192 ? CE  ? D LYS 178 CE  
139 1 Y 1 D LYS 192 ? NZ  ? D LYS 178 NZ  
140 1 Y 1 D SER 193 ? OG  ? D SER 179 OG  
141 1 Y 1 D ASP 194 ? CG  ? D ASP 180 CG  
142 1 Y 1 D ASP 194 ? OD1 ? D ASP 180 OD1 
143 1 Y 1 D ASP 194 ? OD2 ? D ASP 180 OD2 
144 1 Y 1 D ASN 199 ? CG  ? D ASN 185 CG  
145 1 Y 1 D ASN 199 ? OD1 ? D ASN 185 OD1 
146 1 Y 1 D ASN 199 ? ND2 ? D ASN 185 ND2 
147 1 Y 1 D ASN 203 ? CG  ? D ASN 189 CG  
148 1 Y 1 D ASN 203 ? OD1 ? D ASN 189 OD1 
149 1 Y 1 D ASN 203 ? ND2 ? D ASN 189 ND2 
150 1 Y 1 D SER 204 ? OG  ? D SER 190 OG  
151 1 Y 1 D ILE 206 ? CG1 ? D ILE 192 CG1 
152 1 Y 1 D ILE 206 ? CG2 ? D ILE 192 CG2 
153 1 Y 1 D ILE 206 ? CD1 ? D ILE 192 CD1 
154 1 Y 1 D PRO 207 ? CG  ? D PRO 193 CG  
155 1 Y 1 D PRO 207 ? CD  ? D PRO 193 CD  
156 1 Y 1 D GLU 208 ? CG  ? D GLU 194 CG  
157 1 Y 1 D GLU 208 ? CD  ? D GLU 194 CD  
158 1 Y 1 D GLU 208 ? OE1 ? D GLU 194 OE1 
159 1 Y 1 D GLU 208 ? OE2 ? D GLU 194 OE2 
160 1 Y 1 D ASP 209 ? CG  ? D ASP 195 CG  
161 1 Y 1 D ASP 209 ? OD1 ? D ASP 195 OD1 
162 1 Y 1 D ASP 209 ? OD2 ? D ASP 195 OD2 
163 1 Y 1 E GLU 144 ? CG  ? E GLU 130 CG  
164 1 Y 1 E GLU 144 ? CD  ? E GLU 130 CD  
165 1 Y 1 E GLU 144 ? OE1 ? E GLU 130 OE1 
166 1 Y 1 E GLU 144 ? OE2 ? E GLU 130 OE2 
167 1 Y 1 E ILE 147 ? CG1 ? E ILE 133 CG1 
168 1 Y 1 E ILE 147 ? CG2 ? E ILE 133 CG2 
169 1 Y 1 E ILE 147 ? CD1 ? E ILE 133 CD1 
170 1 Y 1 E GLN 151 ? CG  ? E GLN 137 CG  
171 1 Y 1 E GLN 151 ? CD  ? E GLN 137 CD  
172 1 Y 1 E GLN 151 ? OE1 ? E GLN 137 OE1 
173 1 Y 1 E GLN 151 ? NE2 ? E GLN 137 NE2 
174 1 Y 1 E LYS 176 ? CG  ? E LYS 162 CG  
175 1 Y 1 E LYS 176 ? CD  ? E LYS 162 CD  
176 1 Y 1 E LYS 176 ? CE  ? E LYS 162 CE  
177 1 Y 1 E LYS 176 ? NZ  ? E LYS 162 NZ  
178 1 Y 1 E GLN 187 ? CG  ? E GLN 173 CG  
179 1 Y 1 E GLN 187 ? CD  ? E GLN 173 CD  
180 1 Y 1 E GLN 187 ? OE1 ? E GLN 173 OE1 
181 1 Y 1 E GLN 187 ? NE2 ? E GLN 173 NE2 
182 1 Y 1 E GLN 192 ? CG  ? E GLN 178 CG  
183 1 Y 1 E GLN 192 ? CD  ? E GLN 178 CD  
184 1 Y 1 E GLN 192 ? OE1 ? E GLN 178 OE1 
185 1 Y 1 E GLN 192 ? NE2 ? E GLN 178 NE2 
186 1 Y 1 E ASP 197 ? CG  ? E ASP 183 CG  
187 1 Y 1 E ASP 197 ? OD1 ? E ASP 183 OD1 
188 1 Y 1 E ASP 197 ? OD2 ? E ASP 183 OD2 
189 1 Y 1 E ARG 217 ? CG  ? E ARG 203 CG  
190 1 Y 1 E ARG 217 ? CD  ? E ARG 203 CD  
191 1 Y 1 E ARG 217 ? NE  ? E ARG 203 NE  
192 1 Y 1 E ARG 217 ? CZ  ? E ARG 203 CZ  
193 1 Y 1 E ARG 217 ? NH1 ? E ARG 203 NH1 
194 1 Y 1 E ARG 217 ? NH2 ? E ARG 203 NH2 
195 1 Y 1 E GLU 231 ? CG  ? E GLU 217 CG  
196 1 Y 1 E GLU 231 ? CD  ? E GLU 217 CD  
197 1 Y 1 E GLU 231 ? OE1 ? E GLU 217 OE1 
198 1 Y 1 E GLU 231 ? OE2 ? E GLU 217 OE2 
199 1 Y 1 E ASN 232 ? CG  ? E ASN 218 CG  
200 1 Y 1 E ASN 232 ? OD1 ? E ASN 218 OD1 
201 1 Y 1 E ASN 232 ? ND2 ? E ASN 218 ND2 
202 1 Y 1 E GLU 234 ? CG  ? E GLU 220 CG  
203 1 Y 1 E GLU 234 ? CD  ? E GLU 220 CD  
204 1 Y 1 E GLU 234 ? OE1 ? E GLU 220 OE1 
205 1 Y 1 E GLU 234 ? OE2 ? E GLU 220 OE2 
206 1 Y 1 E ARG 254 ? CG  ? E ARG 240 CG  
207 1 Y 1 E ARG 254 ? CD  ? E ARG 240 CD  
208 1 Y 1 E ARG 254 ? NE  ? E ARG 240 NE  
209 1 Y 1 E ARG 254 ? CZ  ? E ARG 240 CZ  
210 1 Y 1 E ARG 254 ? NH1 ? E ARG 240 NH1 
211 1 Y 1 E ARG 254 ? NH2 ? E ARG 240 NH2 
# 
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  ? ? ? 1.19.2_4158 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.19.2_4158 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.312 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EJH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     92.974 
_cell.length_a_esd                 ? 
_cell.length_b                     43.272 
_cell.length_b_esd                 ? 
_cell.length_c                     257.958 
_cell.length_c_esd                 ? 
_cell.volume                       1037793.710 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9EJH 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y (x,y,-x+z)' 
_symmetry.space_group_name_H-M             'I 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EJH 
_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             2.74 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.08 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '8% Tacsimate, pH 8.0, 20-24% w/v PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-08-15 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.95373 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95373 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          37.35 
_reflns.entry_id                                       9EJH 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.45 
_reflns.d_resolution_low                               45.22 
_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                                     38503 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.988 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.45 
_reflns_shell.d_res_low                                     2.55 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4311 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.735 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               41.82 
_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                                 9EJH 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.45 
_refine.ls_d_res_low                             45.22 
_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                     38486 
_refine.ls_number_reflns_R_free                  1954 
_refine.ls_number_reflns_R_work                  36532 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_percent_reflns_R_free                 5.08 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1783 
_refine.ls_R_factor_R_free                       0.2316 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1756 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       '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             1.1100 
_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                 22.3322 
_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                            0.2559 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.45 
_refine_hist.d_res_low                        45.22 
_refine_hist.number_atoms_solvent             297 
_refine_hist.number_atoms_total               6638 
_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        6291 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         50 
_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' ? 0.0034  ? 6493 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5793  ? 8844 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0435  ? 996  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0044  ? 1145 ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.7294 ? 2270 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.45 2.51  . . 143 2564 99.89  . . . . 0.2496 . . . . . . . . . . . 0.3356 
'X-RAY DIFFRACTION' 2.51 2.58  . . 127 2610 99.89  . . . . 0.2282 . . . . . . . . . . . 0.2701 
'X-RAY DIFFRACTION' 2.58 2.66  . . 144 2558 100.00 . . . . 0.2044 . . . . . . . . . . . 0.2704 
'X-RAY DIFFRACTION' 2.66 2.74  . . 121 2579 99.93  . . . . 0.1993 . . . . . . . . . . . 0.2612 
'X-RAY DIFFRACTION' 2.74 2.84  . . 166 2564 99.96  . . . . 0.2010 . . . . . . . . . . . 0.2680 
'X-RAY DIFFRACTION' 2.84 2.95  . . 142 2590 99.93  . . . . 0.1885 . . . . . . . . . . . 0.3077 
'X-RAY DIFFRACTION' 2.95 3.09  . . 153 2601 100.00 . . . . 0.1833 . . . . . . . . . . . 0.2707 
'X-RAY DIFFRACTION' 3.09 3.25  . . 152 2540 99.93  . . . . 0.1728 . . . . . . . . . . . 0.2374 
'X-RAY DIFFRACTION' 3.25 3.45  . . 163 2597 99.96  . . . . 0.1660 . . . . . . . . . . . 0.2339 
'X-RAY DIFFRACTION' 3.45 3.72  . . 139 2607 99.96  . . . . 0.1578 . . . . . . . . . . . 0.1969 
'X-RAY DIFFRACTION' 3.72 4.09  . . 96  2669 100.00 . . . . 0.1562 . . . . . . . . . . . 0.2197 
'X-RAY DIFFRACTION' 4.09 4.69  . . 143 2616 99.96  . . . . 0.1407 . . . . . . . . . . . 0.1809 
'X-RAY DIFFRACTION' 4.69 5.90  . . 133 2658 99.96  . . . . 0.1634 . . . . . . . . . . . 0.1951 
'X-RAY DIFFRACTION' 5.90 45.22 . . 132 2779 99.79  . . . . 0.2028 . . . . . . . . . . . 0.2336 
# 
_struct.entry_id                     9EJH 
_struct.title                        'Peptide-independent T cell receptor recognition of HLA-DQ2' 
_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        9EJH 
_struct_keywords.text            'T cell receptor, immune receptor, human leukocyte antigen, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
H N N 6 ? 
I N N 7 ? 
J N N 8 ? 
K N N 7 ? 
L N N 7 ? 
M N N 9 ? 
N N N 9 ? 
O N N 9 ? 
P N N 9 ? 
Q N N 9 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP DQA1_HUMAN   P01909 ? 1 
;EDIVADHVASYGVNLYQSYGPSGQYTHEFDGDEQFYVDLGRKETVWCLPVLRQFRFDPQFALTNIAVLKHNLNSLIKRSN
STAATNEVPEVTVFSKSPVTLGQPNILICLVDNIFPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKISYLTLLPSAE
ESYDCKVEHWGLDKPLLKHWEPE
;
24  
2 UNP O19712_HUMAN O19712 ? 2 
;RDSPEDFVYQFKGMCYFTNGTERVRLVSRSIYNREEIVRFDSDVGEFRAVTLLGLPAAEYWNSQKDILERKRAAVDRVCR
HNYQLELRTTLQRRVEPTVTISPSRTEALNHHNLLVCSVTDFYPAQIKVRWFRNDQEETAGVVSTPLIRNGDWTFQILVM
LEMTPQRGDVYTCHVEHPSLQSPITVEWRAQS
;
1   
3 UNP HG2A_HUMAN   P04233 ? 3 ATPLLMQALPMGA 110 
4 PDB 9EJH         9EJH   ? 4 ? 1   
5 PDB 9EJH         9EJH   ? 5 ? 1   
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9EJH A 1 ? 183 ? P01909 24  ? 206 ? 1  183 
2 2 9EJH B 1 ? 192 ? O19712 1   ? 192 ? 1  192 
3 3 9EJH C 1 ? 13  ? P04233 110 ? 122 ? -1 11  
4 4 9EJH D 1 ? 204 ? 9EJH   -1  ? 218 ? -1 218 
5 5 9EJH E 1 ? 242 ? 9EJH   2   ? 256 ? 2  256 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9EJH SER A 47  ? UNP P01909 CYS 70 conflict         46  1 
2 9EJH THR B 193 ? UNP O19712 ?   ?  'expression tag' 193 2 
2 9EJH GLY B 194 ? UNP O19712 ?   ?  'expression tag' 194 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   pentameric 
_pdbx_struct_assembly.oligomeric_count     5 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'surface plasmon resonance' 
_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 LEU A 48  ? PHE A 54  ? LEU A 47  PHE A 53  5 ? 7  
HELX_P HELX_P2  AA2 ASP A 57  ? SER A 79  ? ASP A 57  SER A 79  1 ? 23 
HELX_P HELX_P3  AA3 THR B 51  ? LEU B 53  ? THR B 51  LEU B 53  5 ? 3  
HELX_P HELX_P4  AA4 GLY B 54  ? SER B 63  ? GLY B 54  SER B 63  1 ? 10 
HELX_P HELX_P5  AA5 GLN B 64  ? VAL B 78  ? GLN B 64  VAL B 78  1 ? 15 
HELX_P HELX_P6  AA6 VAL B 78  ? THR B 89  ? VAL B 78  THR B 89  1 ? 12 
HELX_P HELX_P7  AA7 THR B 90  ? ARG B 93  ? THR B 90  ARG B 93  5 ? 4  
HELX_P HELX_P8  AA8 LYS D 81  ? SER D 85  ? LYS D 95  SER D 99  5 ? 5  
HELX_P HELX_P9  AA9 ARG D 163 ? ASP D 166 ? ARG D 177 ASP D 180 5 ? 4  
HELX_P HELX_P10 AB1 ALA D 182 ? PHE D 187 ? ALA D 196 PHE D 201 1 ? 6  
HELX_P HELX_P11 AB2 GLU E 81  ? SER E 85  ? GLU E 95  SER E 99  5 ? 5  
HELX_P HELX_P12 AB3 ASP E 114 ? VAL E 118 ? ASP E 128 VAL E 132 5 ? 5  
HELX_P HELX_P13 AB4 SER E 129 ? GLN E 137 ? SER E 143 GLN E 151 1 ? 9  
HELX_P HELX_P14 AB5 ALA E 196 ? GLN E 200 ? ALA E 210 GLN E 214 1 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?   ? A CYS 109 SG  ? ? ? 1_555 A CYS 165 SG ? ? A CYS 109 A CYS 165 1_555 ? ? ? ? ? ? ? 2.035 ? ?               
disulf2 disulf ?   ? B CYS 15  SG  ? ? ? 1_555 B CYS 79  SG ? ? B CYS 15  B CYS 79  1_555 ? ? ? ? ? ? ? 2.043 ? ?               
disulf3 disulf ?   ? B CYS 117 SG  ? ? ? 1_555 B CYS 173 SG ? ? B CYS 117 B CYS 173 1_555 ? ? ? ? ? ? ? 2.023 ? ?               
disulf4 disulf ?   ? D CYS 25  SG  ? ? ? 1_555 D CYS 90  SG ? ? D CYS 23  D CYS 104 1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf5 disulf ?   ? D CYS 133 SG  ? ? ? 1_555 D CYS 183 SG ? ? D CYS 147 D CYS 197 1_555 ? ? ? ? ? ? ? 2.036 ? ?               
disulf6 disulf ?   ? D CYS 158 SG  ? ? ? 1_555 E CYS 169 SG ? ? D CYS 172 E CYS 183 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf7 disulf ?   ? E CYS 22  SG  ? ? ? 1_555 E CYS 90  SG ? ? E CYS 23  E CYS 104 1_555 ? ? ? ? ? ? ? 2.028 ? ?               
disulf8 disulf ?   ? E CYS 143 SG  ? ? ? 1_555 E CYS 208 SG ? ? E CYS 157 E CYS 222 1_555 ? ? ? ? ? ? ? 2.022 ? ?               
covale1 covale one ? A ASN 120 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 120 A NAG 201 1_555 ? ? ? ? ? ? ? 1.437 ? N-Glycosylation 
covale2 covale one ? B ASN 19  ND2 ? ? ? 1_555 H NAG .   C1 ? ? B ASN 19  B NAG 202 1_555 ? ? ? ? ? ? ? 1.443 ? N-Glycosylation 
# 
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 F .   ? ASN A 120 ? NAG A 201 ? 1_555 ASN A 120 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG H .   ? ASN B 19  ? NAG B 202 ? 1_555 ASN B 19  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  CYS A 109 ? CYS A 165 ? CYS A 109 ? 1_555 CYS A 165 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
4  CYS B 15  ? CYS B 79  ? CYS B 15  ? 1_555 CYS B 79  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
5  CYS B 117 ? CYS B 173 ? CYS B 117 ? 1_555 CYS B 173 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
6  CYS D 25  ? CYS D 90  ? CYS D 23  ? 1_555 CYS D 104 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7  CYS D 133 ? CYS D 183 ? CYS D 147 ? 1_555 CYS D 197 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8  CYS D 158 ? CYS E 169 ? CYS D 172 ? 1_555 CYS E 183 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9  CYS E 22  ? CYS E 90  ? CYS E 23  ? 1_555 CYS E 104 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
10 CYS E 143 ? CYS E 208 ? CYS E 157 ? 1_555 CYS E 222 ? 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 TYR 11  A . ? TYR 11  A GLY 12  A A GLY 11  A 1 -1.66  
2 GLY 20  A . ? GLY 19  A PRO 21  A ? PRO 20  A 1 -6.32  
3 PHE 115 A . ? PHE 115 A PRO 116 A ? PRO 116 A 1 -2.67  
4 TYR 123 B . ? TYR 123 B PRO 124 B ? PRO 124 B 1 3.13   
5 THR 6   E . ? THR 7   E PRO 7   E ? PRO 8   E 1 -10.53 
6 PHE 149 E . ? PHE 163 E PRO 150 E ? PRO 164 E 1 0.27   
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 5 ? 
AA9 ? 5 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 4 ? 
AB5 ? 6 ? 
AB6 ? 4 ? 
AB7 ? 4 ? 
AB8 ? 4 ? 
AB9 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? 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 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
AB5 5 6 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 43  ? TRP A 46  ? GLU A 42  TRP A 45  
AA1 2 ASP A 32  ? ASP A 38  ? ASP A 31  ASP A 37  
AA1 3 SER A 22  ? PHE A 29  ? SER A 21  PHE A 28  
AA1 4 HIS A 7   ? GLN A 17  ? HIS A 7   GLN A 16  
AA1 5 VAL B 8   ? THR B 18  ? VAL B 8   THR B 18  
AA1 6 ARG B 23  ? TYR B 32  ? ARG B 23  TYR B 32  
AA1 7 GLU B 35  ? ASP B 41  ? GLU B 35  ASP B 41  
AA1 8 PHE B 47  ? ALA B 49  ? PHE B 47  ALA B 49  
AA2 1 GLU A 90  ? SER A 95  ? GLU A 90  SER A 95  
AA2 2 ASN A 105 ? ILE A 114 ? ASN A 105 ILE A 114 
AA2 3 PHE A 147 ? LEU A 155 ? PHE A 147 LEU A 155 
AA2 4 VAL A 134 ? GLU A 136 ? VAL A 134 GLU A 136 
AA3 1 GLU A 90  ? SER A 95  ? GLU A 90  SER A 95  
AA3 2 ASN A 105 ? ILE A 114 ? ASN A 105 ILE A 114 
AA3 3 PHE A 147 ? LEU A 155 ? PHE A 147 LEU A 155 
AA3 4 LEU A 140 ? SER A 141 ? LEU A 140 SER A 141 
AA4 1 HIS A 128 ? VAL A 130 ? HIS A 128 VAL A 130 
AA4 2 ASN A 120 ? SER A 125 ? ASN A 120 SER A 125 
AA4 3 TYR A 163 ? GLU A 168 ? TYR A 163 GLU A 168 
AA4 4 LEU A 176 ? TRP A 180 ? LEU A 176 TRP A 180 
AA5 1 THR B 98  ? SER B 104 ? THR B 98  SER B 104 
AA5 2 LEU B 114 ? PHE B 122 ? LEU B 114 PHE B 122 
AA5 3 PHE B 155 ? GLU B 162 ? PHE B 155 GLU B 162 
AA5 4 VAL B 142 ? SER B 144 ? VAL B 142 SER B 144 
AA6 1 THR B 98  ? SER B 104 ? THR B 98  SER B 104 
AA6 2 LEU B 114 ? PHE B 122 ? LEU B 114 PHE B 122 
AA6 3 PHE B 155 ? GLU B 162 ? PHE B 155 GLU B 162 
AA6 4 ILE B 148 ? ARG B 149 ? ILE B 148 ARG B 149 
AA7 1 GLN B 136 ? GLU B 138 ? GLN B 136 GLU B 138 
AA7 2 LYS B 128 ? ARG B 133 ? LYS B 128 ARG B 133 
AA7 3 VAL B 170 ? GLU B 176 ? VAL B 170 GLU B 176 
AA7 4 ILE B 184 ? ARG B 189 ? ILE B 184 ARG B 189 
AA8 1 VAL D 6   ? GLN D 8   ? VAL D 4   GLN D 6   
AA8 2 VAL D 21  ? TYR D 27  ? VAL D 19  TYR D 25  
AA8 3 TYR D 72  ? ILE D 77  ? TYR D 86  ILE D 91  
AA8 4 PHE D 62  ? ASN D 67  ? PHE D 76  ASN D 81  
AA8 5 ASN D 57  ? ASP D 59  ? ASN D 65  ASP D 68  
AA9 1 PHE D 13  ? PRO D 16  ? PHE D 11  PRO D 14  
AA9 2 THR D 104 ? SER D 109 ? THR D 118 SER D 123 
AA9 3 ALA D 86  ? GLY D 94  ? ALA D 100 GLY D 108 
AA9 4 SER D 34  ? GLN D 40  ? SER D 38  GLN D 44  
AA9 5 PRO D 46  ? SER D 51  ? PRO D 50  SER D 55  
AB1 1 PHE D 13  ? PRO D 16  ? PHE D 11  PRO D 14  
AB1 2 THR D 104 ? SER D 109 ? THR D 118 SER D 123 
AB1 3 ALA D 86  ? GLY D 94  ? ALA D 100 GLY D 108 
AB1 4 LYS D 97  ? PHE D 100 ? LYS D 111 PHE D 114 
AB2 1 ALA D 118 ? ARG D 123 ? ALA D 132 ARG D 137 
AB2 2 SER D 131 ? THR D 136 ? SER D 145 THR D 150 
AB2 3 PHE D 167 ? SER D 176 ? PHE D 181 SER D 190 
AB2 4 VAL D 152 ? ILE D 154 ? VAL D 166 ILE D 168 
AB3 1 ALA D 118 ? ARG D 123 ? ALA D 132 ARG D 137 
AB3 2 SER D 131 ? THR D 136 ? SER D 145 THR D 150 
AB3 3 PHE D 167 ? SER D 176 ? PHE D 181 SER D 190 
AB3 4 CYS D 158 ? MET D 162 ? CYS D 172 MET D 176 
AB4 1 THR E 4   ? THR E 6   ? THR E 5   THR E 7   
AB4 2 VAL E 18  ? SER E 23  ? VAL E 19  SER E 24  
AB4 3 SER E 73  ? VAL E 77  ? SER E 87  VAL E 91  
AB4 4 PHE E 63  ? GLN E 67  ? PHE E 76  GLN E 80  
AB5 1 TYR E 9   ? THR E 13  ? TYR E 10  THR E 14  
AB5 2 SER E 107 ? LEU E 112 ? SER E 121 LEU E 126 
AB5 3 ALA E 86  ? SER E 93  ? ALA E 100 SER E 107 
AB5 4 SER E 30  ? THR E 37  ? SER E 38  THR E 45  
AB5 5 GLY E 41  ? PHE E 49  ? GLY E 49  PHE E 57  
AB5 6 THR E 52  ? LYS E 56  ? THR E 64  LYS E 68  
AB6 1 TYR E 9   ? THR E 13  ? TYR E 10  THR E 14  
AB6 2 SER E 107 ? LEU E 112 ? SER E 121 LEU E 126 
AB6 3 ALA E 86  ? SER E 93  ? ALA E 100 SER E 107 
AB6 4 PHE E 102 ? PHE E 103 ? PHE E 116 PHE E 117 
AB7 1 GLU E 122 ? PHE E 126 ? GLU E 136 PHE E 140 
AB7 2 LYS E 138 ? PHE E 148 ? LYS E 152 PHE E 162 
AB7 3 TYR E 186 ? SER E 195 ? TYR E 200 SER E 209 
AB7 4 VAL E 168 ? THR E 170 ? VAL E 182 THR E 184 
AB8 1 GLU E 122 ? PHE E 126 ? GLU E 136 PHE E 140 
AB8 2 LYS E 138 ? PHE E 148 ? LYS E 152 PHE E 162 
AB8 3 TYR E 186 ? SER E 195 ? TYR E 200 SER E 209 
AB8 4 LEU E 175 ? LYS E 176 ? LEU E 189 LYS E 190 
AB9 1 LYS E 162 ? VAL E 164 ? LYS E 176 VAL E 178 
AB9 2 VAL E 153 ? VAL E 159 ? VAL E 167 VAL E 173 
AB9 3 PHE E 206 ? PHE E 212 ? PHE E 220 PHE E 226 
AB9 4 GLN E 231 ? ALA E 237 ? GLN E 245 ALA E 251 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 43  ? O GLU A 42  N ASP A 38  ? N ASP A 37  
AA1 2 3 O GLN A 34  ? O GLN A 33  N HIS A 27  ? N HIS A 26  
AA1 3 4 O GLN A 24  ? O GLN A 23  N LEU A 15  ? N LEU A 14  
AA1 4 5 N TYR A 11  ? N TYR A 11  O GLY B 13  ? O GLY B 13  
AA1 5 6 N TYR B 16  ? N TYR B 16  O ARG B 25  ? O ARG B 25  
AA1 6 7 N TYR B 32  ? N TYR B 32  O GLU B 35  ? O GLU B 35  
AA1 7 8 N ARG B 39  ? N ARG B 39  O ARG B 48  ? O ARG B 48  
AA2 1 2 N GLU A 90  ? N GLU A 90  O ASP A 112 ? O ASP A 112 
AA2 2 3 N ILE A 114 ? N ILE A 114 O PHE A 147 ? O PHE A 147 
AA2 3 4 O TYR A 152 ? O TYR A 152 N SER A 135 ? N SER A 135 
AA3 1 2 N GLU A 90  ? N GLU A 90  O ASP A 112 ? O ASP A 112 
AA3 2 3 N ILE A 114 ? N ILE A 114 O PHE A 147 ? O PHE A 147 
AA3 3 4 O PHE A 148 ? O PHE A 148 N LEU A 140 ? N LEU A 140 
AA4 1 2 O HIS A 128 ? O HIS A 128 N SER A 125 ? N SER A 125 
AA4 2 3 N THR A 122 ? N THR A 122 O LYS A 166 ? O LYS A 166 
AA4 3 4 N CYS A 165 ? N CYS A 165 O LYS A 178 ? O LYS A 178 
AA5 1 2 N THR B 100 ? N THR B 100 O SER B 118 ? O SER B 118 
AA5 2 3 N VAL B 119 ? N VAL B 119 O ILE B 157 ? O ILE B 157 
AA5 3 4 O MET B 160 ? O MET B 160 N VAL B 143 ? N VAL B 143 
AA6 1 2 N THR B 100 ? N THR B 100 O SER B 118 ? O SER B 118 
AA6 2 3 N VAL B 119 ? N VAL B 119 O ILE B 157 ? O ILE B 157 
AA6 3 4 O GLN B 156 ? O GLN B 156 N ILE B 148 ? N ILE B 148 
AA7 1 2 O GLN B 136 ? O GLN B 136 N ARG B 133 ? N ARG B 133 
AA7 2 3 N ARG B 130 ? N ARG B 130 O HIS B 174 ? O HIS B 174 
AA7 3 4 N TYR B 171 ? N TYR B 171 O TRP B 188 ? O TRP B 188 
AA8 1 2 N GLU D 7   ? N GLU D 5   O THR D 26  ? O THR D 24  
AA8 2 3 N CYS D 25  ? N CYS D 23  O ILE D 73  ? O ILE D 87  
AA8 3 4 O LEU D 76  ? O LEU D 90  N THR D 63  ? N THR D 77  
AA8 4 5 O ALA D 64  ? O ALA D 78  N ASN D 57  ? N ASN D 65  
AA9 1 2 N PHE D 13  ? N PHE D 11  O ARG D 105 ? O ARG D 119 
AA9 2 3 O LEU D 106 ? O LEU D 120 N ALA D 86  ? N ALA D 100 
AA9 3 4 O THR D 87  ? O THR D 101 N GLN D 40  ? N GLN D 44  
AA9 4 5 N ARG D 39  ? N ARG D 43  O LYS D 47  ? O LYS D 51  
AB1 1 2 N PHE D 13  ? N PHE D 11  O ARG D 105 ? O ARG D 119 
AB1 2 3 O LEU D 106 ? O LEU D 120 N ALA D 86  ? N ALA D 100 
AB1 3 4 N VAL D 92  ? N VAL D 106 O VAL D 99  ? O VAL D 113 
AB2 1 2 N TYR D 120 ? N TYR D 134 O LEU D 134 ? O LEU D 148 
AB2 2 3 N CYS D 133 ? N CYS D 147 O ALA D 174 ? O ALA D 188 
AB2 3 4 O TRP D 175 ? O TRP D 189 N TYR D 153 ? N TYR D 167 
AB3 1 2 N TYR D 120 ? N TYR D 134 O LEU D 134 ? O LEU D 148 
AB3 2 3 N CYS D 133 ? N CYS D 147 O ALA D 174 ? O ALA D 188 
AB3 3 4 O PHE D 167 ? O PHE D 181 N MET D 162 ? N MET D 176 
AB4 1 2 N THR E 6   ? N THR E 7   O SER E 21  ? O SER E 22  
AB4 2 3 N LEU E 20  ? N LEU E 21  O MET E 75  ? O MET E 89  
AB4 3 4 O ASN E 76  ? O ASN E 90  N SER E 64  ? N SER E 77  
AB5 1 2 N LYS E 12  ? N LYS E 13  O LEU E 112 ? O LEU E 126 
AB5 2 3 O SER E 107 ? O SER E 121 N TYR E 88  ? N TYR E 102 
AB5 3 4 O LEU E 89  ? O LEU E 103 N TYR E 34  ? N TYR E 42  
AB5 4 5 N VAL E 31  ? N VAL E 39  O TYR E 48  ? O TYR E 56  
AB5 5 6 N GLU E 47  ? N GLU E 55  O ARG E 54  ? O ARG E 66  
AB6 1 2 N LYS E 12  ? N LYS E 13  O LEU E 112 ? O LEU E 126 
AB6 2 3 O SER E 107 ? O SER E 121 N TYR E 88  ? N TYR E 102 
AB6 3 4 N SER E 92  ? N SER E 106 O PHE E 102 ? O PHE E 116 
AB7 1 2 N PHE E 126 ? N PHE E 140 O VAL E 142 ? O VAL E 156 
AB7 2 3 N ALA E 145 ? N ALA E 159 O LEU E 188 ? O LEU E 202 
AB7 3 4 O ARG E 191 ? O ARG E 205 N CYS E 169 ? N CYS E 183 
AB8 1 2 N PHE E 126 ? N PHE E 140 O VAL E 142 ? O VAL E 156 
AB8 2 3 N ALA E 145 ? N ALA E 159 O LEU E 188 ? O LEU E 202 
AB8 3 4 O ALA E 187 ? O ALA E 201 N LEU E 175 ? N LEU E 189 
AB9 1 2 O LYS E 162 ? O LYS E 176 N VAL E 159 ? N VAL E 173 
AB9 2 3 N SER E 156 ? N SER E 170 O GLN E 209 ? O GLN E 223 
AB9 3 4 N PHE E 212 ? N PHE E 226 O GLN E 231 ? O GLN E 245 
# 
_pdbx_entry_details.entry_id                   9EJH 
_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     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   D HOH 341 ? ? O   D HOH 343 ? ? 2.16 
2 1 NH1 E ARG 75  ? ? OD2 E ASP 98  ? ? 2.17 
3 1 OD2 A ASP 37  ? ? NH1 A ARG 40  ? ? 2.18 
# 
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 ASP A 57  ? ? -56.37  109.74  
2  1 ASN B 33  ? ? 54.87   -106.68 
3  1 VAL B 78  ? ? -92.84  -62.43  
4  1 THR B 89  ? ? -133.07 -89.82  
5  1 ASN B 113 ? ? -147.73 14.09   
6  1 PRO B 124 ? ? -79.74  -168.67 
7  1 PRO D 8   ? ? -72.21  -74.74  
8  1 ARG D 47  ? ? 55.12   13.87   
9  1 LYS D 48  ? ? -112.10 -165.62 
10 1 ALA D 100 ? ? -172.75 -178.71 
11 1 ASP D 130 ? ? -142.00 59.11   
12 1 LYS D 140 ? ? -114.31 62.58   
13 1 LEU E 53  ? ? -92.05  -66.43  
14 1 SER E 85  ? ? 67.82   -3.22   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -x,y,-z             
3 x+1/2,y+1/2,z+1/2   
4 -x+1/2,y+1/2,-z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_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[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined -1.81793704954 16.8463522276  45.7272373108  0.237048922876 ? 0.00574541221921  ? -0.048819429273 
? 0.271046388108 ? 0.0193495260289    ? 0.252478209314 ? 0.128289948761   ? -0.0179501841622 ? -0.157390588174   ? 0.0415508153298 
? 0.0720708363726 ? 0.213321697986  ? -0.130682868385  ? -0.0797988373228 ? -0.202183511237  ? 0.071161723232   ? 0.173539442499 ? 
0.0640792245214   ? -0.0394173224527 ? -0.284562368524  ? 0.000206374863608  ? 
2  'X-RAY DIFFRACTION' ? refined -0.37523457244 28.222581023   51.9907538602  0.265667319246 ? 0.0800275133565   ? 0.0167381594512 
? 0.259326406876 ? -0.00826599555559  ? 0.236779115504 ? 0.0919878588399  ? 0.0994501858783  ? 0.139022548307    ? 0.0938366173714 
? 0.0572635802528 ? 0.11760768037   ? -0.0626069260453 ? -0.215356363064  ? 0.0777744656388  ? 0.288553484819   ? 0.0512928662433 
? 0.104954862625    ? -0.133652308509  ? -0.187886972412  ? -6.65689628184e-05 ? 
3  'X-RAY DIFFRACTION' ? refined -10.1378952855 24.1171290596  36.0430153553  0.276536350861 ? 0.118208727713    ? 
-0.0526291389293  ? 0.3944185656   ? -0.00609794075713  ? 0.278010706222 ? 0.574787659932   ? 0.317828338679   ? -0.229966312186   
? 0.178912058157  ? -0.14639641708  ? 0.539553998836  ? 0.0497779824129  ? 0.584561712518   ? 0.0432381961703  ? -0.292892493869  
? -0.00954628175823 ? 0.234371418838    ? -0.392096263224  ? -0.483611808364  ? 0.142367344268     ? 
4  'X-RAY DIFFRACTION' ? refined -11.587227127  13.8430489672  63.2171337262  0.218187398482 ? 0.0183545136771   ? 0.0535315319519 
? 0.489772280232 ? 0.00273175522128   ? 0.307810210465 ? 0.458634949903   ? -0.0400072430039 ? -0.0200798046279  ? 0.597716579167  
? -0.144250808089 ? 0.539350618463  ? -0.0657253041175 ? -0.22803178729   ? -0.111046962872  ? 0.0775330735633  ? 0.021520812309 ? 
0.123441275385    ? -0.0353783218347 ? -0.492608428047  ? 0.00026368713324   ? 
5  'X-RAY DIFFRACTION' ? refined 3.51367690879  16.8458691136  36.6184464649  0.173434462042 ? 0.0116468578852   ? 
-0.0121185274156  ? 0.179749638335 ? -0.00959457001671  ? 0.195054874296 ? 0.0766741160814  ? 0.0844321173119  ? -0.168738457791   
? 0.423228296736  ? 0.0665408385444 ? 0.83524948068   ? 0.0238656854719  ? 0.0699010029078  ? 0.0420940972176  ? -0.110564031135  
? -0.0397435279441  ? -0.0157707739123  ? -0.104031241394  ? -0.138570728992  ? -0.000930218136022 ? 
6  'X-RAY DIFFRACTION' ? refined 11.4911838926  6.86936985503  74.0175635343  0.256044843894 ? 0.0130571869671   ? 
-0.0129303256781  ? 0.264917258203 ? 0.00811224176563   ? 0.248451638524 ? 0.0357534724911  ? -0.239486513117  ? 0.410856368324    
? 0.176128463533  ? -0.304114738901 ? 1.20897996572   ? 0.0797117581522  ? 0.106392511494   ? -0.0932421891789 ? 0.0117693712845  
? -0.0345978927626  ? 0.000487098505495 ? 0.11557697862    ? 0.135111730515   ? -1.68294123028e-05 ? 
7  'X-RAY DIFFRACTION' ? refined 1.05963845024  26.2738211307  37.2757357448  0.369651739595 ? 0.0413536512472   ? 
-0.0348735453807  ? 0.393523420141 ? 0.00983655939189   ? 0.376566725348 ? 0.00697794777859 ? 0.0204742018848  ? 0.0293478364823   
? 0.0345347111204 ? 0.071804618764  ? 0.0380289411996 ? 0.206261381492   ? 0.28070102525    ? -0.0544841061042 ? 0.192491870442   
? 0.129460046736    ? -0.0177445821551  ? -0.374975541514  ? -0.0177467820465 ? 6.19221421951e-05  ? 
8  'X-RAY DIFFRACTION' ? refined 6.83987495115  -1.84275496587 8.66100454323  0.215095705876 ? -0.022100919004   ? 
-0.0202683634531  ? 0.19449331017  ? -0.000348304866145 ? 0.188063857251 ? 1.00488115058    ? -0.217283908097  ? 0.495997000372    
? 0.366477741777  ? 0.492994433933  ? 0.941101588492  ? 0.0480768818446  ? 0.0977313818648  ? 0.0508895214443  ? 0.00301880987227 
? -0.038175790393   ? -0.0131862153439  ? 0.132440176708   ? -0.0972029526347 ? 0.0124318207366    ? 
9  'X-RAY DIFFRACTION' ? refined 25.0050349776  -22.7381233098 -9.18168619117 0.610442669323 ? 0.0505010680726   ? 
-0.0841579877087  ? 0.379689935617 ? -0.0536707082994   ? 0.352746432196 ? 0.398629183182   ? 0.0750229582444  ? 0.00938777059969  
? 0.261420369294  ? 0.0590542017929 ? 0.732729890285  ? 0.326472843897   ? 0.292861722978   ? -0.217673101448  ? -0.311093871507  
? -0.191997968704   ? 0.099731598341    ? 0.240690010662   ? 0.0840287484235  ? 1.93402771001e-05  ? 
10 'X-RAY DIFFRACTION' ? refined 30.5123746676  -8.96741284435 22.0820007407  0.302402469156 ? 0.0172229879541   ? 0.0290761030283 
? 0.232467864903 ? 0.000843692776145  ? 0.347482008977 ? 0.0875998503281  ? -0.0757060299996 ? -0.10415971897    ? 0.0460023578858 
? 0.0551164543613 ? 0.0709564428601 ? 0.0927638340118  ? 0.188007813753   ? 0.198449059795   ? -0.500450292593  ? -0.0259598134741 
? -0.203324602028   ? -0.0563708507013 ? 0.233195226232   ? -0.000106398136265 ? 
11 'X-RAY DIFFRACTION' ? refined 26.9706128792  -3.78970357148 28.5995435793  0.274819237341 ? 0.0335434597795   ? 0.0006179717515 
? 0.147412372384 ? -0.00138788750677  ? 0.23670560474  ? 0.18365002707    ? 0.0364265821122  ? 0.0131287384393   ? 0.350811160775  
? 0.172543665461  ? 0.0858108323279 ? -0.0467178472177 ? -0.105249305083  ? 0.086273294412   ? 0.241489907638   ? 0.130139841996 ? 
-0.189296727396   ? -0.0293098616723 ? 0.152510155927   ? 0.00646943264453   ? 
12 'X-RAY DIFFRACTION' ? refined 16.1339395868  -5.12276202094 29.6039691761  0.225541134081 ? -0.0165799148978  ? 
-0.00863557221999 ? 0.155172018576 ? -0.0214993249836   ? 0.242292453555 ? 0.344089442442   ? 0.0825701297681  ? -0.145571884298   
? 0.354974988268  ? -0.286140803027 ? 0.215490660097  ? -0.0229074983213 ? -0.0326246961488 ? -0.133149190462  ? 0.0221310084185  
? 0.0827072546143   ? 0.0130176669355   ? 0.0979457879346  ? -0.0154920564    ? -1.0562421211e-05  ? 
13 'X-RAY DIFFRACTION' ? refined 21.9324616612  -3.39009246166 27.696549814   0.190685354512 ? -0.00829459067679 ? 
-0.00278481747676 ? 0.141552834648 ? 0.0101422713903    ? 0.199068023258 ? 0.347345688296   ? -0.0205433470011 ? -0.12937227076    
? 0.312665855342  ? 0.311526586086  ? 0.447544688929  ? -0.0901968195829 ? -0.0074943994094 ? 0.0577266535566  ? -0.0727893896222 
? 0.107046484287    ? -0.0341694491484  ? 0.00176932851638 ? 0.0144473367087  ? 1.19679784965e-05  ? 
14 'X-RAY DIFFRACTION' ? refined 33.1393352106  -18.6056570127 3.80212268642  0.301652005258 ? 0.082375847084    ? 0.0558071878284 
? 0.233994840117 ? -0.0267584062767   ? 0.250546439497 ? 0.632306696897   ? -0.235553031682  ? -0.0614741297969  ? 0.202047684327  
? -0.158658920109 ? 0.198737560545  ? 0.0539792712745  ? 0.106309140884   ? -0.156144599552  ? -0.101663421538  ? -0.0490265843635 
? -0.0764660158806  ? 0.0926957468593  ? 0.0421573595431  ? -0.00245826730389  ? 
15 'X-RAY DIFFRACTION' ? refined 28.4608102928  -18.0851308571 4.59320969337  0.343360695291 ? -0.0666884814121  ? 
-0.00209052158333 ? 0.365697021971 ? -0.00543146901097  ? 0.36242474034  ? 0.0600317308744  ? -0.0756512507311 ? -0.00896718794658 
? 0.294427082862  ? 0.338481333603  ? 0.45653854974   ? 0.167525989638   ? 0.227027075549   ? 0.025241924109   ? -0.176609848946  
? 0.174863317831    ? -0.011700298255   ? 0.0818606188656  ? -0.331601795231  ? -9.28202099582e-05 ? 
16 'X-RAY DIFFRACTION' ? refined 39.3396878101  -15.9777750013 3.6548286625   0.253262583584 ? 0.0330770830168   ? 0.0769626178525 
? 0.363326935164 ? -0.0179087246879   ? 0.322961642516 ? 0.382635150421   ? -0.0886353830458 ? -0.019759410712   ? 0.720515918808  
? 0.313720010458  ? 0.352180794987  ? 0.0422187980844  ? 0.270365125612   ? -0.077491367916  ? -0.18794692571   ? 0.0548954609617 
? -0.337828968668   ? 0.179823124495   ? 0.28940428758    ? 0.0752413047077    ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  A 1   A 1   ? A 21  A 20  ? ? 
;chain 'A' and (resid 1 through 20 )
;
2  'X-RAY DIFFRACTION' 2  A 22  A 21  ? A 57  A 57  ? ? 
;chain 'A' and (resid 21 through 57 )
;
3  'X-RAY DIFFRACTION' 3  A 58  A 58  ? A 78  A 78  ? ? 
;chain 'A' and (resid 58 through 78 )
;
4  'X-RAY DIFFRACTION' 4  A 79  A 79  ? A 182 A 182 ? ? 
;chain 'A' and (resid 79 through 182 )
;
5  'X-RAY DIFFRACTION' 5  C 1   B 3   ? C 86  B 88  ? ? 
;chain 'B' and (resid 3 through 88 )
;
6  'X-RAY DIFFRACTION' 6  C 87  B 89  ? C 187 B 194 ? ? 
;chain 'B' and (resid 89 through 194 )
;
7  'X-RAY DIFFRACTION' 7  H 1   C -1  ? H 12  C 10  ? ? 
;chain 'C' and (resid -1 through 10 )
;
8  'X-RAY DIFFRACTION' 8  I 1   D 2   ? I 114 D 131 ? ? 
;chain 'D' and (resid 2 through 131 )
;
9  'X-RAY DIFFRACTION' 9  I 115 D 132 ? I 194 D 213 ? ? 
;chain 'D' and (resid 132 through 213 )
;
10 'X-RAY DIFFRACTION' 10 J 1   E 3   ? J 12  E 14  ? ? 
;chain 'E' and (resid 3 through 14 )
;
11 'X-RAY DIFFRACTION' 11 J 13  E 15  ? J 28  E 37  ? ? 
;chain 'E' and (resid 15 through 37 )
;
12 'X-RAY DIFFRACTION' 12 J 29  E 38  ? J 61  E 75  ? ? 
;chain 'E' and (resid 38 through 75 )
;
13 'X-RAY DIFFRACTION' 13 J 62  E 76  ? J 105 E 120 ? ? 
;chain 'E' and (resid 76 through 120 )
;
14 'X-RAY DIFFRACTION' 14 J 106 E 121 ? J 158 E 173 ? ? 
;chain 'E' and (resid 121 through 173 )
;
15 'X-RAY DIFFRACTION' 15 J 159 E 174 ? J 184 E 199 ? ? 
;chain 'E' and (resid 174 through 199 )
;
16 'X-RAY DIFFRACTION' 16 J 185 E 200 ? J 240 E 255 ? ? 
;chain 'E' and (resid 200 through 255 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 183 ? A GLU 183 
2  1 Y 1 B ARG 1   ? B ARG 1   
3  1 Y 1 B ASP 2   ? B ASP 2   
4  1 Y 1 B GLU 107 ? B GLU 107 
5  1 Y 1 B ALA 108 ? B ALA 108 
6  1 Y 1 B LEU 109 ? B LEU 109 
7  1 Y 1 B ASN 110 ? B ASN 110 
8  1 Y 1 B HIS 111 ? B HIS 111 
9  1 Y 1 C ALA 11  ? C ALA 13  
10 1 Y 1 D MET -1  ? D MET 1   
11 1 Y 1 D GLN 0   ? D GLN 2   
12 1 Y 1 D ARG 1   ? D ARG 3   
13 1 Y 1 D SER 142 ? D SER 128 
14 1 Y 1 D ILE 205 ? D ILE 191 
15 1 Y 1 D SER 214 ? D SER 200 
16 1 Y 1 D PRO 215 ? D PRO 201 
17 1 Y 1 D GLU 216 ? D GLU 202 
18 1 Y 1 D SER 217 ? D SER 203 
19 1 Y 1 D SER 218 ? D SER 204 
20 1 Y 1 E MET 2   ? E MET 1   
21 1 Y 1 E ASP 256 ? E ASP 242 
# 
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 
ACT C    C N N 1   
ACT O    O N N 2   
ACT OXT  O N N 3   
ACT CH3  C N N 4   
ACT H1   H N N 5   
ACT H2   H N N 6   
ACT H3   H N N 7   
ALA N    N N N 8   
ALA CA   C N S 9   
ALA C    C N N 10  
ALA O    O N N 11  
ALA CB   C N N 12  
ALA OXT  O N N 13  
ALA H    H N N 14  
ALA H2   H N N 15  
ALA HA   H N N 16  
ALA HB1  H N N 17  
ALA HB2  H N N 18  
ALA HB3  H N N 19  
ALA HXT  H N N 20  
ARG N    N N N 21  
ARG CA   C N S 22  
ARG C    C N N 23  
ARG O    O N N 24  
ARG CB   C N N 25  
ARG CG   C N N 26  
ARG CD   C N N 27  
ARG NE   N N N 28  
ARG CZ   C N N 29  
ARG NH1  N N N 30  
ARG NH2  N N N 31  
ARG OXT  O N N 32  
ARG H    H N N 33  
ARG H2   H N N 34  
ARG HA   H N N 35  
ARG HB2  H N N 36  
ARG HB3  H N N 37  
ARG HG2  H N N 38  
ARG HG3  H N N 39  
ARG HD2  H N N 40  
ARG HD3  H N N 41  
ARG HE   H N N 42  
ARG HH11 H N N 43  
ARG HH12 H N N 44  
ARG HH21 H N N 45  
ARG HH22 H N N 46  
ARG HXT  H N N 47  
ASN N    N N N 48  
ASN CA   C N S 49  
ASN C    C N N 50  
ASN O    O N N 51  
ASN CB   C N N 52  
ASN CG   C N N 53  
ASN OD1  O N N 54  
ASN ND2  N N N 55  
ASN OXT  O N N 56  
ASN H    H N N 57  
ASN H2   H N N 58  
ASN HA   H N N 59  
ASN HB2  H N N 60  
ASN HB3  H N N 61  
ASN HD21 H N N 62  
ASN HD22 H N N 63  
ASN HXT  H N N 64  
ASP N    N N N 65  
ASP CA   C N S 66  
ASP C    C N N 67  
ASP O    O N N 68  
ASP CB   C N N 69  
ASP CG   C N N 70  
ASP OD1  O N N 71  
ASP OD2  O N N 72  
ASP OXT  O N N 73  
ASP H    H N N 74  
ASP H2   H N N 75  
ASP HA   H N N 76  
ASP HB2  H N N 77  
ASP HB3  H N N 78  
ASP HD2  H N N 79  
ASP HXT  H N N 80  
CYS N    N N N 81  
CYS CA   C N R 82  
CYS C    C N N 83  
CYS O    O N N 84  
CYS CB   C N N 85  
CYS SG   S N N 86  
CYS OXT  O N N 87  
CYS H    H N N 88  
CYS H2   H N N 89  
CYS HA   H N N 90  
CYS HB2  H N N 91  
CYS HB3  H N N 92  
CYS HG   H N N 93  
CYS HXT  H N N 94  
GLN N    N N N 95  
GLN CA   C N S 96  
GLN C    C N N 97  
GLN O    O N N 98  
GLN CB   C N N 99  
GLN CG   C N N 100 
GLN CD   C N N 101 
GLN OE1  O N N 102 
GLN NE2  N N N 103 
GLN OXT  O N N 104 
GLN H    H N N 105 
GLN H2   H N N 106 
GLN HA   H N N 107 
GLN HB2  H N N 108 
GLN HB3  H N N 109 
GLN HG2  H N N 110 
GLN HG3  H N N 111 
GLN HE21 H N N 112 
GLN HE22 H N N 113 
GLN HXT  H N N 114 
GLU N    N N N 115 
GLU CA   C N S 116 
GLU C    C N N 117 
GLU O    O N N 118 
GLU CB   C N N 119 
GLU CG   C N N 120 
GLU CD   C N N 121 
GLU OE1  O N N 122 
GLU OE2  O N N 123 
GLU OXT  O N N 124 
GLU H    H N N 125 
GLU H2   H N N 126 
GLU HA   H N N 127 
GLU HB2  H N N 128 
GLU HB3  H N N 129 
GLU HG2  H N N 130 
GLU HG3  H N N 131 
GLU HE2  H N N 132 
GLU HXT  H N N 133 
GLY N    N N N 134 
GLY CA   C N N 135 
GLY C    C N N 136 
GLY O    O N N 137 
GLY OXT  O N N 138 
GLY H    H N N 139 
GLY H2   H N N 140 
GLY HA2  H N N 141 
GLY HA3  H N N 142 
GLY HXT  H N N 143 
GOL C1   C N N 144 
GOL O1   O N N 145 
GOL C2   C N N 146 
GOL O2   O N N 147 
GOL C3   C N N 148 
GOL O3   O N N 149 
GOL H11  H N N 150 
GOL H12  H N N 151 
GOL HO1  H N N 152 
GOL H2   H N N 153 
GOL HO2  H N N 154 
GOL H31  H N N 155 
GOL H32  H N N 156 
GOL HO3  H N N 157 
HIS N    N N N 158 
HIS CA   C N S 159 
HIS C    C N N 160 
HIS O    O N N 161 
HIS CB   C N N 162 
HIS CG   C Y N 163 
HIS ND1  N Y N 164 
HIS CD2  C Y N 165 
HIS CE1  C Y N 166 
HIS NE2  N Y N 167 
HIS OXT  O N N 168 
HIS H    H N N 169 
HIS H2   H N N 170 
HIS HA   H N N 171 
HIS HB2  H N N 172 
HIS HB3  H N N 173 
HIS HD1  H N N 174 
HIS HD2  H N N 175 
HIS HE1  H N N 176 
HIS HE2  H N N 177 
HIS HXT  H N N 178 
HOH O    O N N 179 
HOH H1   H N N 180 
HOH H2   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 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
GLN N   CA   sing N N 89  
GLN N   H    sing N N 90  
GLN N   H2   sing N N 91  
GLN CA  C    sing N N 92  
GLN CA  CB   sing N N 93  
GLN CA  HA   sing N N 94  
GLN C   O    doub N N 95  
GLN C   OXT  sing N N 96  
GLN CB  CG   sing N N 97  
GLN CB  HB2  sing N N 98  
GLN CB  HB3  sing N N 99  
GLN CG  CD   sing N N 100 
GLN CG  HG2  sing N N 101 
GLN CG  HG3  sing N N 102 
GLN CD  OE1  doub N N 103 
GLN CD  NE2  sing N N 104 
GLN NE2 HE21 sing N N 105 
GLN NE2 HE22 sing N N 106 
GLN OXT HXT  sing N N 107 
GLU N   CA   sing N N 108 
GLU N   H    sing N N 109 
GLU N   H2   sing N N 110 
GLU CA  C    sing N N 111 
GLU CA  CB   sing N N 112 
GLU CA  HA   sing N N 113 
GLU C   O    doub N N 114 
GLU C   OXT  sing N N 115 
GLU CB  CG   sing N N 116 
GLU CB  HB2  sing N N 117 
GLU CB  HB3  sing N N 118 
GLU CG  CD   sing N N 119 
GLU CG  HG2  sing N N 120 
GLU CG  HG3  sing N N 121 
GLU CD  OE1  doub N N 122 
GLU CD  OE2  sing N N 123 
GLU OE2 HE2  sing N N 124 
GLU OXT HXT  sing N N 125 
GLY N   CA   sing N N 126 
GLY N   H    sing N N 127 
GLY N   H2   sing N N 128 
GLY CA  C    sing N N 129 
GLY CA  HA2  sing N N 130 
GLY CA  HA3  sing N N 131 
GLY C   O    doub N N 132 
GLY C   OXT  sing N N 133 
GLY OXT HXT  sing N N 134 
GOL C1  O1   sing N N 135 
GOL C1  C2   sing N N 136 
GOL C1  H11  sing N N 137 
GOL C1  H12  sing N N 138 
GOL O1  HO1  sing N N 139 
GOL C2  O2   sing N N 140 
GOL C2  C3   sing N N 141 
GOL C2  H2   sing N N 142 
GOL O2  HO2  sing N N 143 
GOL C3  O3   sing N N 144 
GOL C3  H31  sing N N 145 
GOL C3  H32  sing N N 146 
GOL O3  HO3  sing N N 147 
HIS N   CA   sing N N 148 
HIS N   H    sing N N 149 
HIS N   H2   sing N N 150 
HIS CA  C    sing N N 151 
HIS CA  CB   sing N N 152 
HIS CA  HA   sing N N 153 
HIS C   O    doub N N 154 
HIS C   OXT  sing N N 155 
HIS CB  CG   sing N N 156 
HIS CB  HB2  sing N N 157 
HIS CB  HB3  sing N N 158 
HIS CG  ND1  sing Y N 159 
HIS CG  CD2  doub Y N 160 
HIS ND1 CE1  doub Y N 161 
HIS ND1 HD1  sing N N 162 
HIS CD2 NE2  sing Y N 163 
HIS CD2 HD2  sing N N 164 
HIS CE1 NE2  sing Y N 165 
HIS CE1 HE1  sing N N 166 
HIS NE2 HE2  sing N N 167 
HIS OXT HXT  sing N N 168 
HOH O   H1   sing N N 169 
HOH O   H2   sing N N 170 
ILE N   CA   sing N N 171 
ILE N   H    sing N N 172 
ILE N   H2   sing N N 173 
ILE CA  C    sing N N 174 
ILE CA  CB   sing N N 175 
ILE CA  HA   sing N N 176 
ILE C   O    doub N N 177 
ILE C   OXT  sing N N 178 
ILE CB  CG1  sing N N 179 
ILE CB  CG2  sing N N 180 
ILE CB  HB   sing N N 181 
ILE CG1 CD1  sing N N 182 
ILE CG1 HG12 sing N N 183 
ILE CG1 HG13 sing N N 184 
ILE CG2 HG21 sing N N 185 
ILE CG2 HG22 sing N N 186 
ILE CG2 HG23 sing N N 187 
ILE CD1 HD11 sing N N 188 
ILE CD1 HD12 sing N N 189 
ILE CD1 HD13 sing N N 190 
ILE OXT HXT  sing N N 191 
LEU N   CA   sing N N 192 
LEU N   H    sing N N 193 
LEU N   H2   sing N N 194 
LEU CA  C    sing N N 195 
LEU CA  CB   sing N N 196 
LEU CA  HA   sing N N 197 
LEU C   O    doub N N 198 
LEU C   OXT  sing N N 199 
LEU CB  CG   sing N N 200 
LEU CB  HB2  sing N N 201 
LEU CB  HB3  sing N N 202 
LEU CG  CD1  sing N N 203 
LEU CG  CD2  sing N N 204 
LEU CG  HG   sing N N 205 
LEU CD1 HD11 sing N N 206 
LEU CD1 HD12 sing N N 207 
LEU CD1 HD13 sing N N 208 
LEU CD2 HD21 sing N N 209 
LEU CD2 HD22 sing N N 210 
LEU CD2 HD23 sing N N 211 
LEU OXT HXT  sing N N 212 
LYS N   CA   sing N N 213 
LYS N   H    sing N N 214 
LYS N   H2   sing N N 215 
LYS CA  C    sing N N 216 
LYS CA  CB   sing N N 217 
LYS CA  HA   sing N N 218 
LYS C   O    doub N N 219 
LYS C   OXT  sing N N 220 
LYS CB  CG   sing N N 221 
LYS CB  HB2  sing N N 222 
LYS CB  HB3  sing N N 223 
LYS CG  CD   sing N N 224 
LYS CG  HG2  sing N N 225 
LYS CG  HG3  sing N N 226 
LYS CD  CE   sing N N 227 
LYS CD  HD2  sing N N 228 
LYS CD  HD3  sing N N 229 
LYS CE  NZ   sing N N 230 
LYS CE  HE2  sing N N 231 
LYS CE  HE3  sing N N 232 
LYS NZ  HZ1  sing N N 233 
LYS NZ  HZ2  sing N N 234 
LYS NZ  HZ3  sing N N 235 
LYS OXT HXT  sing N N 236 
MET N   CA   sing N N 237 
MET N   H    sing N N 238 
MET N   H2   sing N N 239 
MET CA  C    sing N N 240 
MET CA  CB   sing N N 241 
MET CA  HA   sing N N 242 
MET C   O    doub N N 243 
MET C   OXT  sing N N 244 
MET CB  CG   sing N N 245 
MET CB  HB2  sing N N 246 
MET CB  HB3  sing N N 247 
MET CG  SD   sing N N 248 
MET CG  HG2  sing N N 249 
MET CG  HG3  sing N N 250 
MET SD  CE   sing N N 251 
MET CE  HE1  sing N N 252 
MET CE  HE2  sing N N 253 
MET CE  HE3  sing N N 254 
MET OXT HXT  sing N N 255 
NAG C1  C2   sing N N 256 
NAG C1  O1   sing N N 257 
NAG C1  O5   sing N N 258 
NAG C1  H1   sing N N 259 
NAG C2  C3   sing N N 260 
NAG C2  N2   sing N N 261 
NAG C2  H2   sing N N 262 
NAG C3  C4   sing N N 263 
NAG C3  O3   sing N N 264 
NAG C3  H3   sing N N 265 
NAG C4  C5   sing N N 266 
NAG C4  O4   sing N N 267 
NAG C4  H4   sing N N 268 
NAG C5  C6   sing N N 269 
NAG C5  O5   sing N N 270 
NAG C5  H5   sing N N 271 
NAG C6  O6   sing N N 272 
NAG C6  H61  sing N N 273 
NAG C6  H62  sing N N 274 
NAG C7  C8   sing N N 275 
NAG C7  N2   sing N N 276 
NAG C7  O7   doub N N 277 
NAG C8  H81  sing N N 278 
NAG C8  H82  sing N N 279 
NAG C8  H83  sing N N 280 
NAG N2  HN2  sing N N 281 
NAG O1  HO1  sing N N 282 
NAG O3  HO3  sing N N 283 
NAG O4  HO4  sing N N 284 
NAG O6  HO6  sing N N 285 
PHE N   CA   sing N N 286 
PHE N   H    sing N N 287 
PHE N   H2   sing N N 288 
PHE CA  C    sing N N 289 
PHE CA  CB   sing N N 290 
PHE CA  HA   sing N N 291 
PHE C   O    doub N N 292 
PHE C   OXT  sing N N 293 
PHE CB  CG   sing N N 294 
PHE CB  HB2  sing N N 295 
PHE CB  HB3  sing N N 296 
PHE CG  CD1  doub Y N 297 
PHE CG  CD2  sing Y N 298 
PHE CD1 CE1  sing Y N 299 
PHE CD1 HD1  sing N N 300 
PHE CD2 CE2  doub Y N 301 
PHE CD2 HD2  sing N N 302 
PHE CE1 CZ   doub Y N 303 
PHE CE1 HE1  sing N N 304 
PHE CE2 CZ   sing Y N 305 
PHE CE2 HE2  sing N N 306 
PHE CZ  HZ   sing N N 307 
PHE OXT HXT  sing N N 308 
PRO N   CA   sing N N 309 
PRO N   CD   sing N N 310 
PRO N   H    sing N N 311 
PRO CA  C    sing N N 312 
PRO CA  CB   sing N N 313 
PRO CA  HA   sing N N 314 
PRO C   O    doub N N 315 
PRO C   OXT  sing N N 316 
PRO CB  CG   sing N N 317 
PRO CB  HB2  sing N N 318 
PRO CB  HB3  sing N N 319 
PRO CG  CD   sing N N 320 
PRO CG  HG2  sing N N 321 
PRO CG  HG3  sing N N 322 
PRO CD  HD2  sing N N 323 
PRO CD  HD3  sing N N 324 
PRO OXT HXT  sing N N 325 
SER N   CA   sing N N 326 
SER N   H    sing N N 327 
SER N   H2   sing N N 328 
SER CA  C    sing N N 329 
SER CA  CB   sing N N 330 
SER CA  HA   sing N N 331 
SER C   O    doub N N 332 
SER C   OXT  sing N N 333 
SER CB  OG   sing N N 334 
SER CB  HB2  sing N N 335 
SER CB  HB3  sing N N 336 
SER OG  HG   sing N N 337 
SER OXT HXT  sing N N 338 
THR N   CA   sing N N 339 
THR N   H    sing N N 340 
THR N   H2   sing N N 341 
THR CA  C    sing N N 342 
THR CA  CB   sing N N 343 
THR CA  HA   sing N N 344 
THR C   O    doub N N 345 
THR C   OXT  sing N N 346 
THR CB  OG1  sing N N 347 
THR CB  CG2  sing N N 348 
THR CB  HB   sing N N 349 
THR OG1 HG1  sing N N 350 
THR CG2 HG21 sing N N 351 
THR CG2 HG22 sing N N 352 
THR CG2 HG23 sing N N 353 
THR OXT HXT  sing N N 354 
TRP N   CA   sing N N 355 
TRP N   H    sing N N 356 
TRP N   H2   sing N N 357 
TRP CA  C    sing N N 358 
TRP CA  CB   sing N N 359 
TRP CA  HA   sing N N 360 
TRP C   O    doub N N 361 
TRP C   OXT  sing N N 362 
TRP CB  CG   sing N N 363 
TRP CB  HB2  sing N N 364 
TRP CB  HB3  sing N N 365 
TRP CG  CD1  doub Y N 366 
TRP CG  CD2  sing Y N 367 
TRP CD1 NE1  sing Y N 368 
TRP CD1 HD1  sing N N 369 
TRP CD2 CE2  doub Y N 370 
TRP CD2 CE3  sing Y N 371 
TRP NE1 CE2  sing Y N 372 
TRP NE1 HE1  sing N N 373 
TRP CE2 CZ2  sing Y N 374 
TRP CE3 CZ3  doub Y N 375 
TRP CE3 HE3  sing N N 376 
TRP CZ2 CH2  doub Y N 377 
TRP CZ2 HZ2  sing N N 378 
TRP CZ3 CH2  sing Y N 379 
TRP CZ3 HZ3  sing N N 380 
TRP CH2 HH2  sing N N 381 
TRP OXT HXT  sing N N 382 
TYR N   CA   sing N N 383 
TYR N   H    sing N N 384 
TYR N   H2   sing N N 385 
TYR CA  C    sing N N 386 
TYR CA  CB   sing N N 387 
TYR CA  HA   sing N N 388 
TYR C   O    doub N N 389 
TYR C   OXT  sing N N 390 
TYR CB  CG   sing N N 391 
TYR CB  HB2  sing N N 392 
TYR CB  HB3  sing N N 393 
TYR CG  CD1  doub Y N 394 
TYR CG  CD2  sing Y N 395 
TYR CD1 CE1  sing Y N 396 
TYR CD1 HD1  sing N N 397 
TYR CD2 CE2  doub Y N 398 
TYR CD2 HD2  sing N N 399 
TYR CE1 CZ   doub Y N 400 
TYR CE1 HE1  sing N N 401 
TYR CE2 CZ   sing Y N 402 
TYR CE2 HE2  sing N N 403 
TYR CZ  OH   sing N N 404 
TYR OH  HH   sing N N 405 
TYR OXT HXT  sing N N 406 
VAL N   CA   sing N N 407 
VAL N   H    sing N N 408 
VAL N   H2   sing N N 409 
VAL CA  C    sing N N 410 
VAL CA  CB   sing N N 411 
VAL CA  HA   sing N N 412 
VAL C   O    doub N N 413 
VAL C   OXT  sing N N 414 
VAL CB  CG1  sing N N 415 
VAL CB  CG2  sing N N 416 
VAL CB  HB   sing N N 417 
VAL CG1 HG11 sing N N 418 
VAL CG1 HG12 sing N N 419 
VAL CG1 HG13 sing N N 420 
VAL CG2 HG21 sing N N 421 
VAL CG2 HG22 sing N N 422 
VAL CG2 HG23 sing N N 423 
VAL OXT HXT  sing N N 424 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6V1A 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'I 1 2 1' 
_space_group.name_Hall        'C 2y (x,y,-x+z)' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9EJH 
_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]   0.010756 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000059 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.023110 
_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]   0.003877 
_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 ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-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   ? 2.95620   5.68133   47.64191  1.000 70.03131  ? 1   GLU A N   1 
ATOM   2    C CA  . GLU A 1 1   ? 4.11556   6.55342   47.48944  1.000 66.47911  ? 1   GLU A CA  1 
ATOM   3    C C   . GLU A 1 1   ? 5.30240   5.76193   46.95308  1.000 78.09399  ? 1   GLU A C   1 
ATOM   4    O O   . GLU A 1 1   ? 6.31252   5.59823   47.63967  1.000 86.64734  ? 1   GLU A O   1 
ATOM   5    C CB  . GLU A 1 1   ? 4.46817   7.21554   48.82491  1.000 53.49031  ? 1   GLU A CB  1 
ATOM   6    N N   . ASP A 1 2   ? 5.17375   5.27993   45.71371  1.000 70.71214  ? 2   ASP A N   1 
ATOM   7    C CA  . ASP A 1 2   ? 6.16738   4.35773   45.17222  1.000 70.43406  ? 2   ASP A CA  1 
ATOM   8    C C   . ASP A 1 2   ? 7.51294   5.04017   44.93933  1.000 64.37825  ? 2   ASP A C   1 
ATOM   9    O O   . ASP A 1 2   ? 8.56359   4.44156   45.19870  1.000 64.76128  ? 2   ASP A O   1 
ATOM   10   C CB  . ASP A 1 2   ? 5.64389   3.72172   43.88435  1.000 74.50758  ? 2   ASP A CB  1 
ATOM   11   C CG  . ASP A 1 2   ? 4.83238   2.46506   44.14718  1.000 79.25245  ? 2   ASP A CG  1 
ATOM   12   O OD1 . ASP A 1 2   ? 5.27352   1.63384   44.96972  1.000 74.34905  ? 2   ASP A OD1 1 
ATOM   13   O OD2 . ASP A 1 2   ? 3.75260   2.30976   43.53919  1.000 87.67514  ? 2   ASP A OD2 1 
ATOM   14   N N   . ILE A 1 3   ? 7.51116   6.28728   44.46259  1.000 51.82787  ? 3   ILE A N   1 
ATOM   15   C CA  . ILE A 1 3   ? 8.77088   6.98568   44.21721  1.000 49.25500  ? 3   ILE A CA  1 
ATOM   16   C C   . ILE A 1 3   ? 9.47283   7.25929   45.54086  1.000 40.11566  ? 3   ILE A C   1 
ATOM   17   O O   . ILE A 1 3   ? 8.88610   7.82626   46.47240  1.000 52.32208  ? 3   ILE A O   1 
ATOM   18   C CB  . ILE A 1 3   ? 8.53737   8.28856   43.43815  1.000 44.55488  ? 3   ILE A CB  1 
ATOM   19   C CG1 . ILE A 1 3   ? 7.92622   7.99557   42.06779  1.000 36.12008  ? 3   ILE A CG1 1 
ATOM   20   C CG2 . ILE A 1 3   ? 9.84874   9.04718   43.28216  1.000 32.47356  ? 3   ILE A CG2 1 
ATOM   21   C CD1 . ILE A 1 3   ? 7.79366   9.21599   41.18486  1.000 27.95802  ? 3   ILE A CD1 1 
ATOM   22   N N   . VAL A 1 4   ? 10.73933  6.86461   45.62704  1.000 39.59820  ? 4   VAL A N   1 
ATOM   23   C CA  . VAL A 1 4   ? 11.53769  7.03025   46.83506  1.000 41.93278  ? 4   VAL A CA  1 
ATOM   24   C C   . VAL A 1 4   ? 12.38657  8.28525   46.69143  1.000 37.85447  ? 4   VAL A C   1 
ATOM   25   O O   . VAL A 1 4   ? 13.06680  8.47427   45.67307  1.000 38.22997  ? 4   VAL A O   1 
ATOM   26   C CB  . VAL A 1 4   ? 12.41479  5.79455   47.09550  1.000 36.13287  ? 4   VAL A CB  1 
ATOM   27   C CG1 . VAL A 1 4   ? 13.14361  5.93321   48.41981  1.000 33.88210  ? 4   VAL A CG1 1 
ATOM   28   C CG2 . VAL A 1 4   ? 11.56378  4.53727   47.08370  1.000 40.95054  ? 4   VAL A CG2 1 
ATOM   29   N N   . ALA A 1 5   ? 12.34549  9.14382   47.70980  1.000 34.98617  ? 5   ALA A N   1 
ATOM   30   C CA  . ALA A 1 5   ? 13.11499  10.37760  47.71633  1.000 30.52893  ? 5   ALA A CA  1 
ATOM   31   C C   . ALA A 1 5   ? 13.34974  10.80995  49.15550  1.000 23.36569  ? 5   ALA A C   1 
ATOM   32   O O   . ALA A 1 5   ? 12.64172  10.39163  50.07467  1.000 26.48910  ? 5   ALA A O   1 
ATOM   33   C CB  . ALA A 1 5   ? 12.40647  11.48968  46.93412  1.000 24.10629  ? 5   ALA A CB  1 
ATOM   34   N N   . ASP A 1 6   ? 14.37091  11.64887  49.34160  1.000 23.80338  ? 6   ASP A N   1 
ATOM   35   C CA  . ASP A 1 6   ? 14.59931  12.25424  50.64827  1.000 20.63824  ? 6   ASP A CA  1 
ATOM   36   C C   . ASP A 1 6   ? 13.46403  13.19774  51.01191  1.000 29.08318  ? 6   ASP A C   1 
ATOM   37   O O   . ASP A 1 6   ? 13.01562  13.23158  52.16330  1.000 28.77388  ? 6   ASP A O   1 
ATOM   38   C CB  . ASP A 1 6   ? 15.92825  13.01402  50.66476  1.000 27.17184  ? 6   ASP A CB  1 
ATOM   39   C CG  . ASP A 1 6   ? 17.12976  12.10690  50.48322  1.000 29.68065  ? 6   ASP A CG  1 
ATOM   40   O OD1 . ASP A 1 6   ? 16.94767  10.87258  50.41782  1.000 25.61045  ? 6   ASP A OD1 1 
ATOM   41   O OD2 . ASP A 1 6   ? 18.26028  12.63432  50.40567  1.000 23.41302  ? 6   ASP A OD2 1 
ATOM   42   N N   . HIS A 1 7   ? 12.99007  13.97389  50.04517  1.000 29.07138  ? 7   HIS A N   1 
ATOM   43   C CA  . HIS A 1 7   ? 11.94775  14.95245  50.29174  1.000 30.44005  ? 7   HIS A CA  1 
ATOM   44   C C   . HIS A 1 7   ? 10.97726  14.95656  49.12140  1.000 30.12157  ? 7   HIS A C   1 
ATOM   45   O O   . HIS A 1 7   ? 11.37780  14.78675  47.96696  1.000 27.42486  ? 7   HIS A O   1 
ATOM   46   C CB  . HIS A 1 7   ? 12.55086  16.34495  50.51631  1.000 21.55150  ? 7   HIS A CB  1 
ATOM   47   C CG  . HIS A 1 7   ? 13.55143  16.38570  51.62919  1.000 31.34182  ? 7   HIS A CG  1 
ATOM   48   N ND1 . HIS A 1 7   ? 13.19374  16.27284  52.95694  1.000 30.71545  ? 7   HIS A ND1 1 
ATOM   49   C CD2 . HIS A 1 7   ? 14.90038  16.50574  51.61214  1.000 24.66630  ? 7   HIS A CD2 1 
ATOM   50   C CE1 . HIS A 1 7   ? 14.27819  16.33614  53.70897  1.000 26.14762  ? 7   HIS A CE1 1 
ATOM   51   N NE2 . HIS A 1 7   ? 15.32654  16.47618  52.91764  1.000 26.10145  ? 7   HIS A NE2 1 
ATOM   52   N N   . VAL A 1 8   ? 9.69708   15.12494  49.43501  1.000 32.28855  ? 8   VAL A N   1 
ATOM   53   C CA  . VAL A 1 8   ? 8.63225   15.18338  48.44375  1.000 23.92883  ? 8   VAL A CA  1 
ATOM   54   C C   . VAL A 1 8   ? 7.82395   16.44100  48.70840  1.000 30.93907  ? 8   VAL A C   1 
ATOM   55   O O   . VAL A 1 8   ? 7.46525   16.72419  49.85761  1.000 28.48205  ? 8   VAL A O   1 
ATOM   56   C CB  . VAL A 1 8   ? 7.72724   13.93830  48.49537  1.000 26.66717  ? 8   VAL A CB  1 
ATOM   57   C CG1 . VAL A 1 8   ? 6.65193   14.02238  47.43137  1.000 19.70118  ? 8   VAL A CG1 1 
ATOM   58   C CG2 . VAL A 1 8   ? 8.55461   12.67879  48.32120  1.000 36.80312  ? 8   VAL A CG2 1 
ATOM   59   N N   . ALA A 1 9   ? 7.54844   17.19755  47.65479  1.000 26.72264  ? 9   ALA A N   1 
ATOM   60   C CA  . ALA A 1 9   ? 6.77299   18.41761  47.77262  1.000 26.08232  ? 9   ALA A CA  1 
ATOM   61   C C   . ALA A 1 9   ? 5.68915   18.44465  46.70414  1.000 25.81307  ? 9   ALA A C   1 
ATOM   62   O O   . ALA A 1 9   ? 5.80926   17.82193  45.64875  1.000 21.69994  ? 9   ALA A O   1 
ATOM   63   C CB  . ALA A 1 9   ? 7.66785   19.65585  47.65398  1.000 17.78437  ? 9   ALA A CB  1 
ATOM   64   N N   . SER A 1 10  ? 4.61352   19.16465  47.00340  1.000 22.37909  ? 10  SER A N   1 
ATOM   65   C CA  . SER A 1 10  ? 3.55998   19.45496  46.04373  1.000 22.53224  ? 10  SER A CA  1 
ATOM   66   C C   . SER A 1 10  ? 3.45279   20.96419  45.90209  1.000 21.46699  ? 10  SER A C   1 
ATOM   67   O O   . SER A 1 10  ? 3.09203   21.65839  46.85889  1.000 23.41939  ? 10  SER A O   1 
ATOM   68   C CB  . SER A 1 10  ? 2.22118   18.86051  46.47822  1.000 24.14842  ? 10  SER A CB  1 
ATOM   69   O OG  . SER A 1 10  ? 2.16725   17.47134  46.21233  1.000 33.88217  ? 10  SER A OG  1 
ATOM   70   N N   . TYR A 1 11  ? 3.75379   21.46508  44.70721  1.000 22.71175  ? 11  TYR A N   1 
ATOM   71   C CA  . TYR A 1 11  ? 3.68867   22.88806  44.39704  1.000 22.18974  ? 11  TYR A CA  1 
ATOM   72   C C   . TYR A 1 11  ? 2.74822   23.08813  43.20146  1.000 24.99583  ? 11  TYR A C   1 
ATOM   73   O O   . TYR A 1 11  ? 3.20645   23.40725  42.10060  1.000 25.41173  ? 11  TYR A O   1 
ATOM   74   C CB  . TYR A 1 11  ? 5.06867   23.44460  44.07276  1.000 26.16163  ? 11  TYR A CB  1 
ATOM   75   C CG  . TYR A 1 11  ? 6.15837   23.22432  45.09690  1.000 24.17931  ? 11  TYR A CG  1 
ATOM   76   C CD1 . TYR A 1 11  ? 5.98313   23.57913  46.43197  1.000 25.53168  ? 11  TYR A CD1 1 
ATOM   77   C CD2 . TYR A 1 11  ? 7.38864   22.69190  44.71301  1.000 21.87004  ? 11  TYR A CD2 1 
ATOM   78   C CE1 . TYR A 1 11  ? 7.00298   23.39486  47.36116  1.000 29.33946  ? 11  TYR A CE1 1 
ATOM   79   C CE2 . TYR A 1 11  ? 8.40755   22.50503  45.62545  1.000 23.04727  ? 11  TYR A CE2 1 
ATOM   80   C CZ  . TYR A 1 11  ? 8.21591   22.86141  46.94433  1.000 31.46878  ? 11  TYR A CZ  1 
ATOM   81   O OH  . TYR A 1 11  ? 9.24041   22.66741  47.84313  1.000 25.12985  ? 11  TYR A OH  1 
ATOM   82   N N   . GLY A 1 12  A 1.44219   22.91187  43.40568  1.000 19.81946  ? 11  GLY A N   1 
ATOM   83   C CA  . GLY A 1 12  A 0.86355   22.51129  44.67287  1.000 22.45599  ? 11  GLY A CA  1 
ATOM   84   C C   . GLY A 1 12  A -0.15155  21.40435  44.48214  1.000 18.88446  ? 11  GLY A C   1 
ATOM   85   O O   . GLY A 1 12  A -0.13109  20.69850  43.47560  1.000 27.52703  ? 11  GLY A O   1 
ATOM   86   N N   . VAL A 1 13  ? -1.03436  21.23966  45.45841  1.000 21.66863  ? 12  VAL A N   1 
ATOM   87   C CA  . VAL A 1 13  ? -2.17234  20.33651  45.34738  1.000 24.08207  ? 12  VAL A CA  1 
ATOM   88   C C   . VAL A 1 13  ? -3.36604  21.16986  44.90193  1.000 29.82513  ? 12  VAL A C   1 
ATOM   89   O O   . VAL A 1 13  ? -3.79259  22.08656  45.61664  1.000 25.54279  ? 12  VAL A O   1 
ATOM   90   C CB  . VAL A 1 13  ? -2.45673  19.61320  46.67521  1.000 25.60810  ? 12  VAL A CB  1 
ATOM   91   C CG1 . VAL A 1 13  ? -3.55784  18.58722  46.48986  1.000 26.23006  ? 12  VAL A CG1 1 
ATOM   92   C CG2 . VAL A 1 13  ? -1.20311  18.94424  47.20100  1.000 23.07643  ? 12  VAL A CG2 1 
ATOM   93   N N   . ASN A 1 14  ? -3.88231  20.87617  43.70967  1.000 28.25455  ? 13  ASN A N   1 
ATOM   94   C CA  . ASN A 1 14  ? -5.02591  21.57582  43.13360  1.000 32.62234  ? 13  ASN A CA  1 
ATOM   95   C C   . ASN A 1 14  ? -6.21724  20.63283  43.14321  1.000 32.67711  ? 13  ASN A C   1 
ATOM   96   O O   . ASN A 1 14  ? -6.15565  19.55070  42.54909  1.000 31.57728  ? 13  ASN A O   1 
ATOM   97   C CB  . ASN A 1 14  ? -4.74351  22.03197  41.70159  1.000 32.57550  ? 13  ASN A CB  1 
ATOM   98   C CG  . ASN A 1 14  ? -3.57699  22.98881  41.60287  1.000 29.16971  ? 13  ASN A CG  1 
ATOM   99   O OD1 . ASN A 1 14  ? -3.74920  24.15160  41.23490  1.000 34.92968  ? 13  ASN A OD1 1 
ATOM   100  N ND2 . ASN A 1 14  ? -2.37798  22.50258  41.91278  1.000 23.41155  ? 13  ASN A ND2 1 
ATOM   101  N N   . LEU A 1 15  ? -7.29802  21.04728  43.79744  1.000 30.62132  ? 14  LEU A N   1 
ATOM   102  C CA  . LEU A 1 15  ? -8.48992  20.22385  43.93620  1.000 27.99849  ? 14  LEU A CA  1 
ATOM   103  C C   . LEU A 1 15  ? -9.71279  21.01476  43.50156  1.000 41.34168  ? 14  LEU A C   1 
ATOM   104  O O   . LEU A 1 15  ? -9.84322  22.19725  43.82873  1.000 40.03748  ? 14  LEU A O   1 
ATOM   105  C CB  . LEU A 1 15  ? -8.66121  19.74656  45.38132  1.000 31.33822  ? 14  LEU A CB  1 
ATOM   106  C CG  . LEU A 1 15  ? -10.00471 19.14548  45.79531  1.000 31.39996  ? 14  LEU A CG  1 
ATOM   107  C CD1 . LEU A 1 15  ? -10.28273 17.86590  45.04236  1.000 33.52435  ? 14  LEU A CD1 1 
ATOM   108  C CD2 . LEU A 1 15  ? -10.01425 18.89077  47.28983  1.000 28.67516  ? 14  LEU A CD2 1 
ATOM   109  N N   . TYR A 1 16  ? -10.59734 20.36093  42.74893  1.000 36.30079  ? 15  TYR A N   1 
ATOM   110  C CA  . TYR A 1 16  ? -11.89014 20.93567  42.40580  1.000 31.02512  ? 15  TYR A CA  1 
ATOM   111  C C   . TYR A 1 16  ? -12.90615 19.81223  42.27811  1.000 31.26484  ? 15  TYR A C   1 
ATOM   112  O O   . TYR A 1 16  ? -12.62772 18.79890  41.62949  1.000 36.50387  ? 15  TYR A O   1 
ATOM   113  C CB  . TYR A 1 16  ? -11.82150 21.74239  41.10659  1.000 29.91383  ? 15  TYR A CB  1 
ATOM   114  C CG  . TYR A 1 16  ? -13.10761 22.48239  40.81731  1.000 39.84091  ? 15  TYR A CG  1 
ATOM   115  C CD1 . TYR A 1 16  ? -13.33622 23.74727  41.34788  1.000 42.38174  ? 15  TYR A CD1 1 
ATOM   116  C CD2 . TYR A 1 16  ? -14.10157 21.91298  40.02629  1.000 46.20598  ? 15  TYR A CD2 1 
ATOM   117  C CE1 . TYR A 1 16  ? -14.51375 24.42808  41.09448  1.000 45.30231  ? 15  TYR A CE1 1 
ATOM   118  C CE2 . TYR A 1 16  ? -15.28630 22.58683  39.76865  1.000 44.46293  ? 15  TYR A CE2 1 
ATOM   119  C CZ  . TYR A 1 16  ? -15.48464 23.84394  40.30528  1.000 44.96296  ? 15  TYR A CZ  1 
ATOM   120  O OH  . TYR A 1 16  ? -16.65506 24.52474  40.05619  1.000 45.14735  ? 15  TYR A OH  1 
ATOM   121  N N   . GLN A 1 17  ? -14.07602 19.99204  42.89437  1.000 35.06922  ? 16  GLN A N   1 
ATOM   122  C CA  . GLN A 1 17  ? -15.13992 18.99595  42.86115  1.000 39.62415  ? 16  GLN A CA  1 
ATOM   123  C C   . GLN A 1 17  ? -16.46585 19.64903  42.48927  1.000 43.00047  ? 16  GLN A C   1 
ATOM   124  O O   . GLN A 1 17  ? -16.67278 20.84643  42.71064  1.000 40.10286  ? 16  GLN A O   1 
ATOM   125  C CB  . GLN A 1 17  ? -15.26724 18.26377  44.21563  1.000 35.04706  ? 16  GLN A CB  1 
ATOM   126  C CG  . GLN A 1 17  ? -15.39283 19.18867  45.42236  1.000 36.99364  ? 16  GLN A CG  1 
ATOM   127  C CD  . GLN A 1 17  ? -15.20647 18.46468  46.74970  1.000 41.52466  ? 16  GLN A CD  1 
ATOM   128  O OE1 . GLN A 1 17  ? -15.51688 17.28195  46.87598  1.000 42.37004  ? 16  GLN A OE1 1 
ATOM   129  N NE2 . GLN A 1 17  ? -14.68848 19.17699  47.74382  1.000 45.80726  ? 16  GLN A NE2 1 
ATOM   130  N N   . SER A 1 18  ? -17.36411 18.84256  41.91369  1.000 38.46105  ? 17  SER A N   1 
ATOM   131  C CA  . SER A 1 18  ? -18.66965 19.35506  41.50250  1.000 35.17307  ? 17  SER A CA  1 
ATOM   132  C C   . SER A 1 18  ? -19.55735 19.66766  42.70455  1.000 39.24383  ? 17  SER A C   1 
ATOM   133  O O   . SER A 1 18  ? -20.27615 20.67319  42.70488  1.000 45.52827  ? 17  SER A O   1 
ATOM   134  C CB  . SER A 1 18  ? -19.36231 18.35428  40.57521  1.000 26.34521  ? 17  SER A CB  1 
ATOM   135  O OG  . SER A 1 18  ? -19.61125 17.12469  41.23515  1.000 40.08589  ? 17  SER A OG  1 
ATOM   136  N N   . TYR A 1 19  ? -19.52902 18.82292  43.73298  1.000 40.85409  ? 18  TYR A N   1 
ATOM   137  C CA  . TYR A 1 19  ? -20.34047 19.06765  44.91882  1.000 44.86463  ? 18  TYR A CA  1 
ATOM   138  C C   . TYR A 1 19  ? -19.85720 20.32998  45.62158  1.000 44.67041  ? 18  TYR A C   1 
ATOM   139  O O   . TYR A 1 19  ? -18.69132 20.42448  46.01907  1.000 48.70858  ? 18  TYR A O   1 
ATOM   140  C CB  . TYR A 1 19  ? -20.28905 17.87290  45.86602  1.000 51.30269  ? 18  TYR A CB  1 
ATOM   141  C CG  . TYR A 1 19  ? -21.28475 17.96757  47.00102  1.000 62.93638  ? 18  TYR A CG  1 
ATOM   142  C CD1 . TYR A 1 19  ? -20.91790 18.49926  48.23288  1.000 56.07754  ? 18  TYR A CD1 1 
ATOM   143  C CD2 . TYR A 1 19  ? -22.59698 17.53360  46.83695  1.000 62.51138  ? 18  TYR A CD2 1 
ATOM   144  C CE1 . TYR A 1 19  ? -21.82920 18.59050  49.27248  1.000 65.55063  ? 18  TYR A CE1 1 
ATOM   145  C CE2 . TYR A 1 19  ? -23.51410 17.61971  47.87038  1.000 61.53919  ? 18  TYR A CE2 1 
ATOM   146  C CZ  . TYR A 1 19  ? -23.12468 18.14898  49.08500  1.000 62.09216  ? 18  TYR A CZ  1 
ATOM   147  O OH  . TYR A 1 19  ? -24.03207 18.23665  50.11416  1.000 77.61633  ? 18  TYR A OH  1 
ATOM   148  N N   . GLY A 1 20  ? -20.75855 21.29259  45.77912  1.000 46.19918  ? 19  GLY A N   1 
ATOM   149  C CA  . GLY A 1 20  ? -20.41717 22.59294  46.29730  1.000 59.01349  ? 19  GLY A CA  1 
ATOM   150  C C   . GLY A 1 20  ? -20.94564 23.68215  45.38694  1.000 59.07440  ? 19  GLY A C   1 
ATOM   151  O O   . GLY A 1 20  ? -21.97552 24.30730  45.66098  1.000 71.17497  ? 19  GLY A O   1 
ATOM   152  N N   . PRO A 1 21  ? -20.23925 23.94011  44.27528  1.000 59.23974  ? 20  PRO A N   1 
ATOM   153  C CA  . PRO A 1 21  ? -18.93735 23.35425  43.93101  1.000 56.44501  ? 20  PRO A CA  1 
ATOM   154  C C   . PRO A 1 21  ? -17.80164 24.01115  44.71768  1.000 54.31396  ? 20  PRO A C   1 
ATOM   155  O O   . PRO A 1 21  ? -17.88985 25.19543  45.04722  1.000 56.42556  ? 20  PRO A O   1 
ATOM   156  C CB  . PRO A 1 21  ? -18.81321 23.63739  42.43233  1.000 35.91202  ? 20  PRO A CB  1 
ATOM   157  C CG  . PRO A 1 21  ? -19.59900 24.88448  42.23475  1.000 50.48220  ? 20  PRO A CG  1 
ATOM   158  C CD  . PRO A 1 21  ? -20.74996 24.81088  43.20414  1.000 49.07382  ? 20  PRO A CD  1 
ATOM   159  N N   . SER A 1 22  ? -16.75324 23.25236  45.02462  1.000 54.63440  ? 21  SER A N   1 
ATOM   160  C CA  . SER A 1 22  ? -15.67810 23.74024  45.87389  1.000 42.82375  ? 21  SER A CA  1 
ATOM   161  C C   . SER A 1 22  ? -14.32223 23.35240  45.30123  1.000 48.34533  ? 21  SER A C   1 
ATOM   162  O O   . SER A 1 22  ? -14.18581 22.36219  44.57634  1.000 37.68636  ? 21  SER A O   1 
ATOM   163  C CB  . SER A 1 22  ? -15.81242 23.20428  47.30629  1.000 40.85830  ? 21  SER A CB  1 
ATOM   164  O OG  . SER A 1 22  ? -16.15848 21.82873  47.31038  1.000 50.64399  ? 21  SER A OG  1 
ATOM   165  N N   . GLY A 1 23  ? -13.31530 24.15939  45.64022  1.000 42.28842  ? 22  GLY A N   1 
ATOM   166  C CA  . GLY A 1 23  ? -11.94968 23.88051  45.26222  1.000 36.06656  ? 22  GLY A CA  1 
ATOM   167  C C   . GLY A 1 23  ? -11.01898 24.07649  46.44248  1.000 40.94862  ? 22  GLY A C   1 
ATOM   168  O O   . GLY A 1 23  ? -11.40287 24.59940  47.49335  1.000 42.46542  ? 22  GLY A O   1 
ATOM   169  N N   . GLN A 1 24  ? -9.77746  23.63902  46.25908  1.000 31.16974  ? 23  GLN A N   1 
ATOM   170  C CA  . GLN A 1 24  ? -8.76259  23.81717  47.28277  1.000 32.66299  ? 23  GLN A CA  1 
ATOM   171  C C   . GLN A 1 24  ? -7.40906  23.94792  46.60457  1.000 31.88563  ? 23  GLN A C   1 
ATOM   172  O O   . GLN A 1 24  ? -7.11680  23.23116  45.64263  1.000 28.73899  ? 23  GLN A O   1 
ATOM   173  C CB  . GLN A 1 24  ? -8.75018  22.65337  48.28250  1.000 26.03645  ? 23  GLN A CB  1 
ATOM   174  C CG  . GLN A 1 24  ? -7.78793  22.86234  49.44809  1.000 27.05200  ? 23  GLN A CG  1 
ATOM   175  C CD  . GLN A 1 24  ? -7.64616  21.63461  50.34077  1.000 33.56898  ? 23  GLN A CD  1 
ATOM   176  O OE1 . GLN A 1 24  ? -8.35577  21.48749  51.33708  1.000 33.14249  ? 23  GLN A OE1 1 
ATOM   177  N NE2 . GLN A 1 24  ? -6.71776  20.75345  49.98898  1.000 24.33203  ? 23  GLN A NE2 1 
ATOM   178  N N   . TYR A 1 25  ? -6.60060  24.88320  47.09631  1.000 32.53615  ? 24  TYR A N   1 
ATOM   179  C CA  . TYR A 1 25  ? -5.22946  25.05693  46.63793  1.000 29.88624  ? 24  TYR A CA  1 
ATOM   180  C C   . TYR A 1 25  ? -4.31669  25.10707  47.85222  1.000 32.90146  ? 24  TYR A C   1 
ATOM   181  O O   . TYR A 1 25  ? -4.49355  25.96204  48.72640  1.000 31.04104  ? 24  TYR A O   1 
ATOM   182  C CB  . TYR A 1 25  ? -5.05213  26.32964  45.80550  1.000 18.24182  ? 24  TYR A CB  1 
ATOM   183  C CG  . TYR A 1 25  ? -3.68480  26.36457  45.17458  1.000 29.31760  ? 24  TYR A CG  1 
ATOM   184  C CD1 . TYR A 1 25  ? -2.58051  26.84779  45.87334  1.000 22.87053  ? 24  TYR A CD1 1 
ATOM   185  C CD2 . TYR A 1 25  ? -3.48409  25.85704  43.89405  1.000 20.95836  ? 24  TYR A CD2 1 
ATOM   186  C CE1 . TYR A 1 25  ? -1.32048  26.84519  45.29902  1.000 26.66739  ? 24  TYR A CE1 1 
ATOM   187  C CE2 . TYR A 1 25  ? -2.23708  25.85383  43.31516  1.000 23.53176  ? 24  TYR A CE2 1 
ATOM   188  C CZ  . TYR A 1 25  ? -1.15662  26.34734  44.01549  1.000 26.77736  ? 24  TYR A CZ  1 
ATOM   189  O OH  . TYR A 1 25  ? 0.08340   26.33204  43.42603  1.000 24.50707  ? 24  TYR A OH  1 
ATOM   190  N N   . THR A 1 26  ? -3.33008  24.21347  47.89069  1.000 30.84302  ? 25  THR A N   1 
ATOM   191  C CA  . THR A 1 26  ? -2.34879  24.17864  48.96335  1.000 26.16342  ? 25  THR A CA  1 
ATOM   192  C C   . THR A 1 26  ? -0.98571  23.83433  48.38850  1.000 25.84189  ? 25  THR A C   1 
ATOM   193  O O   . THR A 1 26  ? -0.86620  23.34795  47.26265  1.000 26.93891  ? 25  THR A O   1 
ATOM   194  C CB  . THR A 1 26  ? -2.69106  23.13822  50.03885  1.000 31.31110  ? 25  THR A CB  1 
ATOM   195  O OG1 . THR A 1 26  ? -2.75498  21.83928  49.43336  1.000 26.39048  ? 25  THR A OG1 1 
ATOM   196  C CG2 . THR A 1 26  ? -4.01268  23.44679  50.71495  1.000 26.14889  ? 25  THR A CG2 1 
ATOM   197  N N   . HIS A 1 27  ? 0.04593   24.09003  49.18249  1.000 26.65411  ? 26  HIS A N   1 
ATOM   198  C CA  . HIS A 1 27  ? 1.35881   23.51190  48.96097  1.000 21.95824  ? 26  HIS A CA  1 
ATOM   199  C C   . HIS A 1 27  ? 1.69255   22.60743  50.13497  1.000 26.48143  ? 26  HIS A C   1 
ATOM   200  O O   . HIS A 1 27  ? 1.29680   22.87109  51.27355  1.000 27.05040  ? 26  HIS A O   1 
ATOM   201  C CB  . HIS A 1 27  ? 2.44010   24.58071  48.79335  1.000 22.20633  ? 26  HIS A CB  1 
ATOM   202  C CG  . HIS A 1 27  ? 2.42733   25.23953  47.45161  1.000 24.83812  ? 26  HIS A CG  1 
ATOM   203  N ND1 . HIS A 1 27  ? 3.51448   25.91934  46.94535  1.000 22.14495  ? 26  HIS A ND1 1 
ATOM   204  C CD2 . HIS A 1 27  ? 1.46078   25.31490  46.50532  1.000 25.70756  ? 26  HIS A CD2 1 
ATOM   205  C CE1 . HIS A 1 27  ? 3.21724   26.38695  45.74509  1.000 26.23590  ? 26  HIS A CE1 1 
ATOM   206  N NE2 . HIS A 1 27  ? 1.97639   26.03647  45.45579  1.000 21.43243  ? 26  HIS A NE2 1 
ATOM   207  N N   . GLU A 1 28  ? 2.40648   21.52800  49.84426  1.000 25.88519  ? 27  GLU A N   1 
ATOM   208  C CA  . GLU A 1 28  ? 2.79905   20.55696  50.85083  1.000 23.33844  ? 27  GLU A CA  1 
ATOM   209  C C   . GLU A 1 28  ? 4.28984   20.29178  50.73063  1.000 23.19149  ? 27  GLU A C   1 
ATOM   210  O O   . GLU A 1 28  ? 4.82829   20.22464  49.62110  1.000 27.15027  ? 27  GLU A O   1 
ATOM   211  C CB  . GLU A 1 28  ? 2.01400   19.24260  50.70424  1.000 26.09799  ? 27  GLU A CB  1 
ATOM   212  C CG  . GLU A 1 28  ? 0.49657   19.38548  50.85937  1.000 25.83742  ? 27  GLU A CG  1 
ATOM   213  C CD  . GLU A 1 28  ? -0.24773  18.06636  50.66565  1.000 28.37809  ? 27  GLU A CD  1 
ATOM   214  O OE1 . GLU A 1 28  ? 0.39784   17.04585  50.35014  1.000 29.19877  ? 27  GLU A OE1 1 
ATOM   215  O OE2 . GLU A 1 28  ? -1.48488  18.05098  50.82971  1.000 36.40407  ? 27  GLU A OE2 1 
ATOM   216  N N   . PHE A 1 29  ? 4.96056   20.16939  51.87389  1.000 27.26704  ? 28  PHE A N   1 
ATOM   217  C CA  . PHE A 1 29  ? 6.35551   19.74984  51.91019  1.000 22.85971  ? 28  PHE A CA  1 
ATOM   218  C C   . PHE A 1 29  ? 6.50034   18.61990  52.91782  1.000 21.11440  ? 28  PHE A C   1 
ATOM   219  O O   . PHE A 1 29  ? 6.18039   18.79232  54.09908  1.000 24.40015  ? 28  PHE A O   1 
ATOM   220  C CB  . PHE A 1 29  ? 7.29462   20.90450  52.25578  1.000 20.69894  ? 28  PHE A CB  1 
ATOM   221  C CG  . PHE A 1 29  ? 8.73732   20.55256  52.08999  1.000 28.11889  ? 28  PHE A CG  1 
ATOM   222  C CD1 . PHE A 1 29  ? 9.33303   20.61252  50.84281  1.000 22.26681  ? 28  PHE A CD1 1 
ATOM   223  C CD2 . PHE A 1 29  ? 9.48905   20.11947  53.16928  1.000 28.45007  ? 28  PHE A CD2 1 
ATOM   224  C CE1 . PHE A 1 29  ? 10.66009  20.26744  50.67626  1.000 31.69004  ? 28  PHE A CE1 1 
ATOM   225  C CE2 . PHE A 1 29  ? 10.81831  19.77038  53.00984  1.000 22.72051  ? 28  PHE A CE2 1 
ATOM   226  C CZ  . PHE A 1 29  ? 11.40274  19.84633  51.76212  1.000 24.62776  ? 28  PHE A CZ  1 
ATOM   227  N N   . ASP A 1 30  ? 6.98141   17.47125  52.44367  1.000 18.12599  ? 29  ASP A N   1 
ATOM   228  C CA  . ASP A 1 30  ? 7.07793   16.25046  53.24553  1.000 23.08726  ? 29  ASP A CA  1 
ATOM   229  C C   . ASP A 1 30  ? 5.77069   15.95516  53.97152  1.000 28.01325  ? 29  ASP A C   1 
ATOM   230  O O   . ASP A 1 30  ? 5.75844   15.60146  55.15162  1.000 27.62919  ? 29  ASP A O   1 
ATOM   231  C CB  . ASP A 1 30  ? 8.24610   16.32204  54.23087  1.000 23.48693  ? 29  ASP A CB  1 
ATOM   232  C CG  . ASP A 1 30  ? 9.58733   16.19827  53.54301  1.000 29.44561  ? 29  ASP A CG  1 
ATOM   233  O OD1 . ASP A 1 30  ? 9.62034   15.69011  52.39712  1.000 35.50797  ? 29  ASP A OD1 1 
ATOM   234  O OD2 . ASP A 1 30  ? 10.60710  16.60608  54.13972  1.000 29.84007  ? 29  ASP A OD2 1 
ATOM   235  N N   . GLY A 1 31  ? 4.65686   16.11614  53.25799  1.000 20.57853  ? 30  GLY A N   1 
ATOM   236  C CA  . GLY A 1 31  ? 3.36224   15.72130  53.76204  1.000 23.52591  ? 30  GLY A CA  1 
ATOM   237  C C   . GLY A 1 31  ? 2.68718   16.70195  54.69558  1.000 29.04536  ? 30  GLY A C   1 
ATOM   238  O O   . GLY A 1 31  ? 1.62024   16.38137  55.23148  1.000 34.93851  ? 30  GLY A O   1 
ATOM   239  N N   . ASP A 1 32  ? 3.26041   17.87800  54.91294  1.000 24.38603  ? 31  ASP A N   1 
ATOM   240  C CA  . ASP A 1 32  ? 2.66213   18.88488  55.77438  1.000 28.49790  ? 31  ASP A CA  1 
ATOM   241  C C   . ASP A 1 32  ? 2.22474   20.07969  54.94332  1.000 24.67198  ? 31  ASP A C   1 
ATOM   242  O O   . ASP A 1 32  ? 2.84429   20.41362  53.93006  1.000 26.67221  ? 31  ASP A O   1 
ATOM   243  C CB  . ASP A 1 32  ? 3.64036   19.34344  56.86078  1.000 31.26932  ? 31  ASP A CB  1 
ATOM   244  C CG  . ASP A 1 32  ? 3.87898   18.28590  57.91521  1.000 29.42390  ? 31  ASP A CG  1 
ATOM   245  O OD1 . ASP A 1 32  ? 2.89034   17.72591  58.43796  1.000 34.18396  ? 31  ASP A OD1 1 
ATOM   246  O OD2 . ASP A 1 32  ? 5.05846   18.00719  58.21365  1.000 33.10104  ? 31  ASP A OD2 1 
ATOM   247  N N   . GLU A 1 33  ? 1.16485   20.73408  55.39604  1.000 24.49906  ? 32  GLU A N   1 
ATOM   248  C CA  . GLU A 1 33  ? 0.58654   21.85523  54.66757  1.000 30.37958  ? 32  GLU A CA  1 
ATOM   249  C C   . GLU A 1 33  ? 1.40777   23.11615  54.91262  1.000 28.44548  ? 32  GLU A C   1 
ATOM   250  O O   . GLU A 1 33  ? 1.50866   23.58715  56.05038  1.000 34.36885  ? 32  GLU A O   1 
ATOM   251  C CB  . GLU A 1 33  ? -0.86316  22.05844  55.09662  1.000 34.24243  ? 32  GLU A CB  1 
ATOM   252  C CG  . GLU A 1 33  ? -1.56125  23.24353  54.46487  1.000 34.32478  ? 32  GLU A CG  1 
ATOM   253  C CD  . GLU A 1 33  ? -3.00681  23.33095  54.90036  1.000 44.69485  ? 32  GLU A CD  1 
ATOM   254  O OE1 . GLU A 1 33  ? -3.43760  22.46038  55.68919  1.000 40.89141  ? 32  GLU A OE1 1 
ATOM   255  O OE2 . GLU A 1 33  ? -3.71210  24.26187  54.45877  1.000 39.67739  ? 32  GLU A OE2 1 
ATOM   256  N N   . GLN A 1 34  ? 2.00028   23.65684  53.84634  1.000 24.29333  ? 33  GLN A N   1 
ATOM   257  C CA  . GLN A 1 34  ? 2.72766   24.91425  53.96155  1.000 23.44946  ? 33  GLN A CA  1 
ATOM   258  C C   . GLN A 1 34  ? 1.77824   26.10377  53.99748  1.000 28.66630  ? 33  GLN A C   1 
ATOM   259  O O   . GLN A 1 34  ? 1.97757   27.03878  54.78237  1.000 31.49088  ? 33  GLN A O   1 
ATOM   260  C CB  . GLN A 1 34  ? 3.71214   25.06025  52.80547  1.000 21.64020  ? 33  GLN A CB  1 
ATOM   261  C CG  . GLN A 1 34  ? 4.89171   24.10479  52.86041  1.000 24.43535  ? 33  GLN A CG  1 
ATOM   262  C CD  . GLN A 1 34  ? 5.78259   24.22834  51.63580  1.000 25.25250  ? 33  GLN A CD  1 
ATOM   263  O OE1 . GLN A 1 34  ? 5.32961   24.04694  50.50601  1.000 27.78096  ? 33  GLN A OE1 1 
ATOM   264  N NE2 . GLN A 1 34  ? 7.05072   24.55159  51.85370  1.000 28.93236  ? 33  GLN A NE2 1 
ATOM   265  N N   . PHE A 1 35  ? 0.75057   26.08810  53.15418  1.000 31.71785  ? 34  PHE A N   1 
ATOM   266  C CA  . PHE A 1 35  ? -0.26114  27.13673  53.13404  1.000 28.22438  ? 34  PHE A CA  1 
ATOM   267  C C   . PHE A 1 35  ? -1.43329  26.65896  52.29620  1.000 31.81872  ? 34  PHE A C   1 
ATOM   268  O O   . PHE A 1 35  ? -1.30900  25.73213  51.49045  1.000 35.99395  ? 34  PHE A O   1 
ATOM   269  C CB  . PHE A 1 35  ? 0.28234   28.46189  52.57228  1.000 31.00060  ? 34  PHE A CB  1 
ATOM   270  C CG  . PHE A 1 35  ? 0.64252   28.41232  51.10728  1.000 22.13059  ? 34  PHE A CG  1 
ATOM   271  C CD1 . PHE A 1 35  ? -0.30006  28.70128  50.13108  1.000 28.48016  ? 34  PHE A CD1 1 
ATOM   272  C CD2 . PHE A 1 35  ? 1.93012   28.09475  50.70961  1.000 24.19195  ? 34  PHE A CD2 1 
ATOM   273  C CE1 . PHE A 1 35  ? 0.03406   28.66258  48.78078  1.000 31.02092  ? 34  PHE A CE1 1 
ATOM   274  C CE2 . PHE A 1 35  ? 2.27611   28.05876  49.36494  1.000 27.29903  ? 34  PHE A CE2 1 
ATOM   275  C CZ  . PHE A 1 35  ? 1.32348   28.34260  48.39766  1.000 26.21244  ? 34  PHE A CZ  1 
ATOM   276  N N   . TYR A 1 36  ? -2.57120  27.31274  52.48987  1.000 30.42341  ? 35  TYR A N   1 
ATOM   277  C CA  . TYR A 1 36  ? -3.68805  27.20629  51.56911  1.000 25.34906  ? 35  TYR A CA  1 
ATOM   278  C C   . TYR A 1 36  ? -4.05529  28.60620  51.11243  1.000 27.24635  ? 35  TYR A C   1 
ATOM   279  O O   . TYR A 1 36  ? -3.78119  29.58997  51.80561  1.000 31.40400  ? 35  TYR A O   1 
ATOM   280  C CB  . TYR A 1 36  ? -4.90656  26.51108  52.20537  1.000 24.42461  ? 35  TYR A CB  1 
ATOM   281  C CG  . TYR A 1 36  ? -5.64497  27.32773  53.24946  1.000 36.93440  ? 35  TYR A CG  1 
ATOM   282  C CD1 . TYR A 1 36  ? -6.67703  28.19265  52.88885  1.000 30.61490  ? 35  TYR A CD1 1 
ATOM   283  C CD2 . TYR A 1 36  ? -5.32741  27.21652  54.59747  1.000 31.88897  ? 35  TYR A CD2 1 
ATOM   284  C CE1 . TYR A 1 36  ? -7.35531  28.93364  53.83913  1.000 37.61437  ? 35  TYR A CE1 1 
ATOM   285  C CE2 . TYR A 1 36  ? -6.00342  27.95121  55.55448  1.000 25.35585  ? 35  TYR A CE2 1 
ATOM   286  C CZ  . TYR A 1 36  ? -7.01306  28.80722  55.17221  1.000 45.41278  ? 35  TYR A CZ  1 
ATOM   287  O OH  . TYR A 1 36  ? -7.67943  29.53737  56.12908  1.000 45.51151  ? 35  TYR A OH  1 
ATOM   288  N N   . VAL A 1 37  ? -4.65853  28.69567  49.93364  1.000 32.33622  ? 36  VAL A N   1 
ATOM   289  C CA  . VAL A 1 37  ? -5.21453  29.94990  49.44588  1.000 36.09562  ? 36  VAL A CA  1 
ATOM   290  C C   . VAL A 1 37  ? -6.71111  29.92877  49.70055  1.000 41.71702  ? 36  VAL A C   1 
ATOM   291  O O   . VAL A 1 37  ? -7.42108  29.02712  49.23619  1.000 34.05303  ? 36  VAL A O   1 
ATOM   292  C CB  . VAL A 1 37  ? -4.91564  30.17675  47.95835  1.000 34.39252  ? 36  VAL A CB  1 
ATOM   293  C CG1 . VAL A 1 37  ? -5.77510  31.31817  47.43267  1.000 36.27716  ? 36  VAL A CG1 1 
ATOM   294  C CG2 . VAL A 1 37  ? -3.44393  30.49229  47.75940  1.000 28.55188  ? 36  VAL A CG2 1 
ATOM   295  N N   . ASP A 1 38  ? -7.18600  30.91290  50.45013  1.000 41.54375  ? 37  ASP A N   1 
ATOM   296  C CA  . ASP A 1 38  ? -8.61666  31.10388  50.62762  1.000 40.67223  ? 37  ASP A CA  1 
ATOM   297  C C   . ASP A 1 38  ? -9.19197  31.59060  49.30680  1.000 37.13627  ? 37  ASP A C   1 
ATOM   298  O O   . ASP A 1 38  ? -9.02605  32.75293  48.93448  1.000 36.79210  ? 37  ASP A O   1 
ATOM   299  C CB  . ASP A 1 38  ? -8.87795  32.09897  51.74530  1.000 42.97162  ? 37  ASP A CB  1 
ATOM   300  C CG  . ASP A 1 38  ? -10.31391 32.10562  52.17246  1.000 47.51806  ? 37  ASP A CG  1 
ATOM   301  O OD1 . ASP A 1 38  ? -11.20270 32.19740  51.29619  1.000 48.12199  ? 37  ASP A OD1 1 
ATOM   302  O OD2 . ASP A 1 38  ? -10.55310 31.99022  53.39125  1.000 55.99694  ? 37  ASP A OD2 1 
ATOM   303  N N   . LEU A 1 39  ? -9.86712  30.69905  48.58365  1.000 36.14232  ? 38  LEU A N   1 
ATOM   304  C CA  . LEU A 1 39  ? -10.33489 31.05847  47.25070  1.000 42.66472  ? 38  LEU A CA  1 
ATOM   305  C C   . LEU A 1 39  ? -11.45808 32.08756  47.31834  1.000 39.24611  ? 38  LEU A C   1 
ATOM   306  O O   . LEU A 1 39  ? -11.52811 32.99153  46.47916  1.000 51.94300  ? 38  LEU A O   1 
ATOM   307  C CB  . LEU A 1 39  ? -10.77007 29.80135  46.50093  1.000 30.52240  ? 38  LEU A CB  1 
ATOM   308  C CG  . LEU A 1 39  ? -9.61968  28.81755  46.27212  1.000 33.64495  ? 38  LEU A CG  1 
ATOM   309  C CD1 . LEU A 1 39  ? -10.13680 27.46620  45.79515  1.000 33.60133  ? 38  LEU A CD1 1 
ATOM   310  C CD2 . LEU A 1 39  ? -8.58658  29.38639  45.29332  1.000 25.09934  ? 38  LEU A CD2 1 
ATOM   311  N N   . GLY A 1 40  ? -12.32904 31.98615  48.32283  1.000 47.10851  ? 39  GLY A N   1 
ATOM   312  C CA  . GLY A 1 40  ? -13.38021 32.97842  48.47334  1.000 44.15614  ? 39  GLY A CA  1 
ATOM   313  C C   . GLY A 1 40  ? -12.84881 34.35124  48.84390  1.000 50.01995  ? 39  GLY A C   1 
ATOM   314  O O   . GLY A 1 40  ? -13.28554 35.36303  48.28956  1.000 49.01699  ? 39  GLY A O   1 
ATOM   315  N N   . ARG A 1 41  ? -11.90217 34.40864  49.78248  1.000 44.09988  ? 40  ARG A N   1 
ATOM   316  C CA  . ARG A 1 41  ? -11.35337 35.67523  50.25278  1.000 45.45162  ? 40  ARG A CA  1 
ATOM   317  C C   . ARG A 1 41  ? -10.12512 36.13188  49.47322  1.000 55.37926  ? 40  ARG A C   1 
ATOM   318  O O   . ARG A 1 41  ? -9.66233  37.25855  49.68725  1.000 52.05700  ? 40  ARG A O   1 
ATOM   319  C CB  . ARG A 1 41  ? -11.00143 35.57144  51.73987  1.000 50.96579  ? 40  ARG A CB  1 
ATOM   320  C CG  . ARG A 1 41  ? -12.18180 35.18316  52.61392  1.000 50.34179  ? 40  ARG A CG  1 
ATOM   321  C CD  . ARG A 1 41  ? -11.76529 34.80036  54.03353  1.000 52.81867  ? 40  ARG A CD  1 
ATOM   322  N NE  . ARG A 1 41  ? -12.89808 34.28081  54.79373  1.000 72.55945  ? 40  ARG A NE  1 
ATOM   323  C CZ  . ARG A 1 41  ? -13.26080 33.00459  54.83537  1.000 73.59499  ? 40  ARG A CZ  1 
ATOM   324  N NH1 . ARG A 1 41  ? -12.57671 32.06888  54.19997  1.000 71.42724  ? 40  ARG A NH1 1 
ATOM   325  N NH2 . ARG A 1 41  ? -14.33941 32.65854  55.53277  1.000 82.95832  ? 40  ARG A NH2 1 
ATOM   326  N N   . LYS A 1 42  ? -9.59027  35.29418  48.58206  1.000 51.77008  ? 41  LYS A N   1 
ATOM   327  C CA  . LYS A 1 42  ? -8.41057  35.63309  47.78484  1.000 32.93446  ? 41  LYS A CA  1 
ATOM   328  C C   . LYS A 1 42  ? -7.23058  36.01488  48.67846  1.000 36.08485  ? 41  LYS A C   1 
ATOM   329  O O   . LYS A 1 42  ? -6.56432  37.03083  48.46782  1.000 44.94973  ? 41  LYS A O   1 
ATOM   330  C CB  . LYS A 1 42  ? -8.72521  36.74703  46.78369  1.000 45.55372  ? 41  LYS A CB  1 
ATOM   331  N N   . GLU A 1 43  ? -6.97147  35.18351  49.68876  1.000 38.41505  ? 42  GLU A N   1 
ATOM   332  C CA  . GLU A 1 43  ? -5.90720  35.43219  50.65225  1.000 39.41375  ? 42  GLU A CA  1 
ATOM   333  C C   . GLU A 1 43  ? -5.06216  34.17826  50.83966  1.000 47.55935  ? 42  GLU A C   1 
ATOM   334  O O   . GLU A 1 43  ? -5.58730  33.06023  50.86557  1.000 31.83727  ? 42  GLU A O   1 
ATOM   335  C CB  . GLU A 1 43  ? -6.47603  35.88362  52.00280  1.000 40.54818  ? 42  GLU A CB  1 
ATOM   336  N N   . THR A 1 44  ? -3.75014  34.37226  50.97012  1.000 40.46901  ? 43  THR A N   1 
ATOM   337  C CA  . THR A 1 44  ? -2.81920  33.28249  51.24078  1.000 35.64969  ? 43  THR A CA  1 
ATOM   338  C C   . THR A 1 44  ? -2.65161  33.12175  52.74887  1.000 38.51663  ? 43  THR A C   1 
ATOM   339  O O   . THR A 1 44  ? -2.25100  34.06850  53.43325  1.000 36.16365  ? 43  THR A O   1 
ATOM   340  C CB  . THR A 1 44  ? -1.46969  33.55501  50.58067  1.000 32.13641  ? 43  THR A CB  1 
ATOM   341  O OG1 . THR A 1 44  ? -1.62782  33.55835  49.15607  1.000 34.35365  ? 43  THR A OG1 1 
ATOM   342  C CG2 . THR A 1 44  ? -0.45943  32.48942  50.97588  1.000 32.08154  ? 43  THR A CG2 1 
ATOM   343  N N   . VAL A 1 45  ? -2.94199  31.92629  53.26272  1.000 37.68127  ? 44  VAL A N   1 
ATOM   344  C CA  . VAL A 1 45  ? -2.92039  31.65133  54.69839  1.000 35.13436  ? 44  VAL A CA  1 
ATOM   345  C C   . VAL A 1 45  ? -1.77475  30.68581  54.97767  1.000 34.70034  ? 44  VAL A C   1 
ATOM   346  O O   . VAL A 1 45  ? -1.89500  29.47591  54.75313  1.000 38.46601  ? 44  VAL A O   1 
ATOM   347  C CB  . VAL A 1 45  ? -4.25254  31.08131  55.19482  1.000 40.98091  ? 44  VAL A CB  1 
ATOM   348  C CG1 . VAL A 1 45  ? -4.17626  30.80178  56.69255  1.000 28.40093  ? 44  VAL A CG1 1 
ATOM   349  C CG2 . VAL A 1 45  ? -5.39248  32.03288  54.87411  1.000 39.31458  ? 44  VAL A CG2 1 
ATOM   350  N N   . TRP A 1 46  ? -0.67132  31.20793  55.50273  1.000 31.09344  ? 45  TRP A N   1 
ATOM   351  C CA  . TRP A 1 46  ? 0.48012   30.37923  55.82830  1.000 35.66896  ? 45  TRP A CA  1 
ATOM   352  C C   . TRP A 1 46  ? 0.22075   29.56282  57.08672  1.000 31.96759  ? 45  TRP A C   1 
ATOM   353  O O   . TRP A 1 46  ? -0.30223  30.07326  58.07831  1.000 37.28792  ? 45  TRP A O   1 
ATOM   354  C CB  . TRP A 1 46  ? 1.72275   31.25056  56.00688  1.000 34.91025  ? 45  TRP A CB  1 
ATOM   355  C CG  . TRP A 1 46  ? 2.04349   32.02735  54.77610  1.000 37.11462  ? 45  TRP A CG  1 
ATOM   356  C CD1 . TRP A 1 46  ? 1.66380   33.30760  54.48984  1.000 34.13678  ? 45  TRP A CD1 1 
ATOM   357  C CD2 . TRP A 1 46  ? 2.78879   31.56630  53.64462  1.000 38.14058  ? 45  TRP A CD2 1 
ATOM   358  N NE1 . TRP A 1 46  ? 2.13673   33.67634  53.25223  1.000 39.11580  ? 45  TRP A NE1 1 
ATOM   359  C CE2 . TRP A 1 46  ? 2.83229   32.62583  52.71322  1.000 38.61746  ? 45  TRP A CE2 1 
ATOM   360  C CE3 . TRP A 1 46  ? 3.42814   30.36339  53.33037  1.000 26.33114  ? 45  TRP A CE3 1 
ATOM   361  C CZ2 . TRP A 1 46  ? 3.49189   32.51904  51.49037  1.000 33.00950  ? 45  TRP A CZ2 1 
ATOM   362  C CZ3 . TRP A 1 46  ? 4.08733   30.25911  52.11951  1.000 27.24980  ? 45  TRP A CZ3 1 
ATOM   363  C CH2 . TRP A 1 46  ? 4.10868   31.33025  51.20914  1.000 32.93497  ? 45  TRP A CH2 1 
ATOM   364  N N   . SER A 1 47  ? 0.59271   28.28249  57.03761  1.000 37.25222  ? 46  SER A N   1 
ATOM   365  C CA  . SER A 1 47  ? 0.34763   27.35385  58.13244  1.000 34.19070  ? 46  SER A CA  1 
ATOM   366  C C   . SER A 1 47  ? 1.54333   27.17802  59.05476  1.000 38.81966  ? 46  SER A C   1 
ATOM   367  O O   . SER A 1 47  ? 1.38381   26.64039  60.15565  1.000 49.62868  ? 46  SER A O   1 
ATOM   368  C CB  . SER A 1 47  ? -0.07031  25.98358  57.58705  1.000 35.93417  ? 46  SER A CB  1 
ATOM   369  O OG  . SER A 1 47  ? -1.35994  26.05301  57.00153  1.000 59.09404  ? 46  SER A OG  1 
ATOM   370  N N   . LEU A 1 48  ? 2.72655   27.60807  58.63872  1.000 41.06411  ? 47  LEU A N   1 
ATOM   371  C CA  . LEU A 1 48  ? 3.91598   27.55257  59.47405  1.000 36.07945  ? 47  LEU A CA  1 
ATOM   372  C C   . LEU A 1 48  ? 4.44120   28.97276  59.62214  1.000 39.96363  ? 47  LEU A C   1 
ATOM   373  O O   . LEU A 1 48  ? 4.69418   29.63922  58.60345  1.000 46.51664  ? 47  LEU A O   1 
ATOM   374  C CB  . LEU A 1 48  ? 4.96911   26.63664  58.84839  1.000 40.72006  ? 47  LEU A CB  1 
ATOM   375  C CG  . LEU A 1 48  ? 6.18808   26.24347  59.67833  1.000 44.76532  ? 47  LEU A CG  1 
ATOM   376  C CD1 . LEU A 1 48  ? 5.77506   25.41780  60.88128  1.000 38.39671  ? 47  LEU A CD1 1 
ATOM   377  C CD2 . LEU A 1 48  ? 7.18246   25.47892  58.81682  1.000 29.83475  ? 47  LEU A CD2 1 
ATOM   378  N N   . PRO A 1 49  ? 4.61676   29.48083  60.84268  1.000 38.46919  ? 48  PRO A N   1 
ATOM   379  C CA  . PRO A 1 49  ? 4.89714   30.91843  61.00597  1.000 39.64517  ? 48  PRO A CA  1 
ATOM   380  C C   . PRO A 1 49  ? 6.13914   31.40326  60.27663  1.000 38.85174  ? 48  PRO A C   1 
ATOM   381  O O   . PRO A 1 49  ? 6.16445   32.55507  59.82590  1.000 41.55126  ? 48  PRO A O   1 
ATOM   382  C CB  . PRO A 1 49  ? 5.05059   31.07213  62.52711  1.000 44.16775  ? 48  PRO A CB  1 
ATOM   383  C CG  . PRO A 1 49  ? 4.33512   29.90165  63.10294  1.000 44.48007  ? 48  PRO A CG  1 
ATOM   384  C CD  . PRO A 1 49  ? 4.54197   28.78262  62.13614  1.000 39.60364  ? 48  PRO A CD  1 
ATOM   385  N N   . VAL A 1 50  ? 7.17176   30.56710  60.14376  1.000 44.08842  ? 49  VAL A N   1 
ATOM   386  C CA  . VAL A 1 50  ? 8.39145   31.00651  59.47739  1.000 38.53770  ? 49  VAL A CA  1 
ATOM   387  C C   . VAL A 1 50  ? 8.15982   31.25774  57.99185  1.000 34.45905  ? 49  VAL A C   1 
ATOM   388  O O   . VAL A 1 50  ? 8.91809   32.00569  57.36446  1.000 47.28690  ? 49  VAL A O   1 
ATOM   389  C CB  . VAL A 1 50  ? 9.51890   29.97991  59.70841  1.000 43.76894  ? 49  VAL A CB  1 
ATOM   390  C CG1 . VAL A 1 50  ? 9.19874   28.65876  59.02101  1.000 38.41058  ? 49  VAL A CG1 1 
ATOM   391  C CG2 . VAL A 1 50  ? 10.85855  30.53136  59.23981  1.000 28.86215  ? 49  VAL A CG2 1 
ATOM   392  N N   . LEU A 1 51  ? 7.11396   30.67280  57.41260  1.000 39.02763  ? 50  LEU A N   1 
ATOM   393  C CA  . LEU A 1 51  ? 6.81949   30.88045  56.00292  1.000 36.79657  ? 50  LEU A CA  1 
ATOM   394  C C   . LEU A 1 51  ? 6.11164   32.20240  55.73123  1.000 39.09889  ? 50  LEU A C   1 
ATOM   395  O O   . LEU A 1 51  ? 5.95974   32.57646  54.56385  1.000 41.73127  ? 50  LEU A O   1 
ATOM   396  C CB  . LEU A 1 51  ? 5.97142   29.72151  55.47051  1.000 37.50508  ? 50  LEU A CB  1 
ATOM   397  C CG  . LEU A 1 51  ? 6.50152   28.30967  55.72793  1.000 42.10893  ? 50  LEU A CG  1 
ATOM   398  C CD1 . LEU A 1 51  ? 5.63758   27.27762  55.01936  1.000 29.40797  ? 50  LEU A CD1 1 
ATOM   399  C CD2 . LEU A 1 51  ? 7.95494   28.18801  55.29738  1.000 34.93560  ? 50  LEU A CD2 1 
ATOM   400  N N   . ARG A 1 52  ? 5.68131   32.92132  56.76837  1.000 35.49023  ? 51  ARG A N   1 
ATOM   401  C CA  . ARG A 1 52  ? 4.96273   34.17011  56.54666  1.000 34.81963  ? 51  ARG A CA  1 
ATOM   402  C C   . ARG A 1 52  ? 5.85287   35.25178  55.95207  1.000 43.16783  ? 51  ARG A C   1 
ATOM   403  O O   . ARG A 1 52  ? 5.33555   36.24430  55.42885  1.000 43.37467  ? 51  ARG A O   1 
ATOM   404  C CB  . ARG A 1 52  ? 4.33291   34.64871  57.85444  1.000 38.35233  ? 51  ARG A CB  1 
ATOM   405  C CG  . ARG A 1 52  ? 3.10075   33.84844  58.23538  1.000 42.58086  ? 51  ARG A CG  1 
ATOM   406  C CD  . ARG A 1 52  ? 2.81505   33.87631  59.72793  1.000 56.45037  ? 51  ARG A CD  1 
ATOM   407  N NE  . ARG A 1 52  ? 1.76886   32.91840  60.06897  1.000 57.51002  ? 51  ARG A NE  1 
ATOM   408  C CZ  . ARG A 1 52  ? 1.39753   32.61399  61.30434  1.000 61.71032  ? 51  ARG A CZ  1 
ATOM   409  N NH1 . ARG A 1 52  ? 1.96676   33.17967  62.35700  1.000 52.76505  ? 51  ARG A NH1 1 
ATOM   410  N NH2 . ARG A 1 52  ? 0.43435   31.71468  61.48793  1.000 67.65345  ? 51  ARG A NH2 1 
ATOM   411  N N   . GLN A 1 53  ? 7.17471   35.07807  56.00274  1.000 41.56845  ? 52  GLN A N   1 
ATOM   412  C CA  . GLN A 1 53  ? 8.06339   36.01417  55.32832  1.000 36.45252  ? 52  GLN A CA  1 
ATOM   413  C C   . GLN A 1 53  ? 7.88720   35.98056  53.81828  1.000 43.43946  ? 52  GLN A C   1 
ATOM   414  O O   . GLN A 1 53  ? 8.28087   36.93255  53.13867  1.000 46.55580  ? 52  GLN A O   1 
ATOM   415  C CB  . GLN A 1 53  ? 9.51617   35.70543  55.67777  1.000 44.86121  ? 52  GLN A CB  1 
ATOM   416  C CG  . GLN A 1 53  ? 9.98509   34.35116  55.17684  1.000 45.46199  ? 52  GLN A CG  1 
ATOM   417  C CD  . GLN A 1 53  ? 11.35087  33.98786  55.70264  1.000 35.85495  ? 52  GLN A CD  1 
ATOM   418  O OE1 . GLN A 1 53  ? 12.32360  34.70922  55.48512  1.000 54.21886  ? 52  GLN A OE1 1 
ATOM   419  N NE2 . GLN A 1 53  ? 11.43132  32.87183  56.41514  1.000 44.77031  ? 52  GLN A NE2 1 
ATOM   420  N N   . PHE A 1 54  ? 7.32016   34.90823  53.27929  1.000 41.08427  ? 53  PHE A N   1 
ATOM   421  C CA  . PHE A 1 54  ? 7.11855   34.78498  51.84631  1.000 39.74772  ? 53  PHE A CA  1 
ATOM   422  C C   . PHE A 1 54  ? 5.81043   35.44348  51.43286  1.000 42.83680  ? 53  PHE A C   1 
ATOM   423  O O   . PHE A 1 54  ? 4.90955   35.66877  52.24433  1.000 39.92862  ? 53  PHE A O   1 
ATOM   424  C CB  . PHE A 1 54  ? 7.11754   33.31638  51.42223  1.000 31.83449  ? 53  PHE A CB  1 
ATOM   425  C CG  . PHE A 1 54  ? 8.39627   32.60357  51.72587  1.000 36.29979  ? 53  PHE A CG  1 
ATOM   426  C CD1 . PHE A 1 54  ? 9.61372   33.22423  51.51312  1.000 30.03125  ? 53  PHE A CD1 1 
ATOM   427  C CD2 . PHE A 1 54  ? 8.38350   31.32172  52.23838  1.000 30.74120  ? 53  PHE A CD2 1 
ATOM   428  C CE1 . PHE A 1 54  ? 10.79588  32.57557  51.79048  1.000 29.91263  ? 53  PHE A CE1 1 
ATOM   429  C CE2 . PHE A 1 54  ? 9.56362   30.66523  52.52253  1.000 30.54650  ? 53  PHE A CE2 1 
ATOM   430  C CZ  . PHE A 1 54  ? 10.77310  31.29405  52.29831  1.000 35.41680  ? 53  PHE A CZ  1 
ATOM   431  N N   . ARG A 1 55  ? 5.72278   35.75575  50.14512  1.000 42.30142  ? 54  ARG A N   1 
ATOM   432  C CA  . ARG A 1 55  ? 4.51672   36.28659  49.53215  1.000 37.63811  ? 54  ARG A CA  1 
ATOM   433  C C   . ARG A 1 55  ? 4.13819   35.37293  48.37675  1.000 38.61517  ? 54  ARG A C   1 
ATOM   434  O O   . ARG A 1 55  ? 4.99091   35.02193  47.55621  1.000 51.81753  ? 54  ARG A O   1 
ATOM   435  C CB  . ARG A 1 55  ? 4.73376   37.72337  49.04646  1.000 34.72365  ? 54  ARG A CB  1 
ATOM   436  N N   . PHE A 1 56  ? 2.87291   34.96808  48.32488  1.000 34.18827  ? 56  PHE A N   1 
ATOM   437  C CA  . PHE A 1 56  ? 2.37300   34.11369  47.25275  1.000 37.98520  ? 56  PHE A CA  1 
ATOM   438  C C   . PHE A 1 56  ? 1.06838   34.70179  46.73072  1.000 37.33394  ? 56  PHE A C   1 
ATOM   439  O O   . PHE A 1 56  ? 0.03749   34.64253  47.40984  1.000 38.43338  ? 56  PHE A O   1 
ATOM   440  C CB  . PHE A 1 56  ? 2.17624   32.67587  47.73429  1.000 34.82322  ? 56  PHE A CB  1 
ATOM   441  C CG  . PHE A 1 56  ? 1.66127   31.75465  46.67407  1.000 28.42717  ? 56  PHE A CG  1 
ATOM   442  C CD1 . PHE A 1 56  ? 2.53504   31.14027  45.79202  1.000 30.53359  ? 56  PHE A CD1 1 
ATOM   443  C CD2 . PHE A 1 56  ? 0.30491   31.51206  46.54917  1.000 23.58133  ? 56  PHE A CD2 1 
ATOM   444  C CE1 . PHE A 1 56  ? 2.06656   30.29497  44.80607  1.000 24.47875  ? 56  PHE A CE1 1 
ATOM   445  C CE2 . PHE A 1 56  ? -0.17348  30.66865  45.56906  1.000 23.57636  ? 56  PHE A CE2 1 
ATOM   446  C CZ  . PHE A 1 56  ? 0.70852   30.05568  44.69342  1.000 29.82026  ? 56  PHE A CZ  1 
ATOM   447  N N   . ASP A 1 57  ? 1.11830   35.26308  45.53083  1.000 42.31616  ? 57  ASP A N   1 
ATOM   448  C CA  . ASP A 1 57  ? -0.02450  35.88593  44.87901  1.000 44.79265  ? 57  ASP A CA  1 
ATOM   449  C C   . ASP A 1 57  ? -1.17493  34.89156  44.76871  1.000 48.41577  ? 57  ASP A C   1 
ATOM   450  O O   . ASP A 1 57  ? -1.09430  33.93846  43.98423  1.000 40.34942  ? 57  ASP A O   1 
ATOM   451  C CB  . ASP A 1 57  ? 0.38903   36.39610  43.49628  1.000 49.71381  ? 57  ASP A CB  1 
ATOM   452  C CG  . ASP A 1 57  ? -0.65576  37.29169  42.85751  1.000 56.02115  ? 57  ASP A CG  1 
ATOM   453  O OD1 . ASP A 1 57  ? -1.79253  37.38164  43.37645  1.000 42.88853  ? 57  ASP A OD1 1 
ATOM   454  O OD2 . ASP A 1 57  ? -0.32441  37.91570  41.82826  1.000 48.03227  ? 57  ASP A OD2 1 
ATOM   455  N N   . PRO A 1 58  ? -2.26336  35.07575  45.52484  1.000 45.25183  ? 58  PRO A N   1 
ATOM   456  C CA  . PRO A 1 58  ? -3.36998  34.10656  45.46188  1.000 38.46493  ? 58  PRO A CA  1 
ATOM   457  C C   . PRO A 1 58  ? -4.07800  34.06571  44.11400  1.000 47.06033  ? 58  PRO A C   1 
ATOM   458  O O   . PRO A 1 58  ? -4.92891  33.18858  43.91434  1.000 43.29464  ? 58  PRO A O   1 
ATOM   459  C CB  . PRO A 1 58  ? -4.31618  34.57293  46.57974  1.000 30.85901  ? 58  PRO A CB  1 
ATOM   460  C CG  . PRO A 1 58  ? -3.98804  35.99520  46.79926  1.000 41.01606  ? 58  PRO A CG  1 
ATOM   461  C CD  . PRO A 1 58  ? -2.52711  36.16027  46.48573  1.000 38.86170  ? 58  PRO A CD  1 
ATOM   462  N N   . GLN A 1 59  ? -3.75125  34.96836  43.18363  1.000 44.92255  ? 59  GLN A N   1 
ATOM   463  C CA  . GLN A 1 59  ? -4.35986  34.90997  41.85850  1.000 48.40775  ? 59  GLN A CA  1 
ATOM   464  C C   . GLN A 1 59  ? -3.87834  33.69827  41.06805  1.000 41.16370  ? 59  GLN A C   1 
ATOM   465  O O   . GLN A 1 59  ? -4.63912  33.13979  40.27041  1.000 37.47528  ? 59  GLN A O   1 
ATOM   466  C CB  . GLN A 1 59  ? -4.06742  36.19585  41.08517  1.000 46.31322  ? 59  GLN A CB  1 
ATOM   467  C CG  . GLN A 1 59  ? -4.87021  36.34440  39.80405  1.000 44.82719  ? 59  GLN A CG  1 
ATOM   468  C CD  . GLN A 1 59  ? -6.35585  36.50818  40.06656  1.000 56.17352  ? 59  GLN A CD  1 
ATOM   469  O OE1 . GLN A 1 59  ? -6.76309  37.26204  40.95255  1.000 62.32464  ? 59  GLN A OE1 1 
ATOM   470  N NE2 . GLN A 1 59  ? -7.17401  35.79285  39.30212  1.000 63.67836  ? 59  GLN A NE2 1 
ATOM   471  N N   . PHE A 1 60  ? -2.62764  33.27655  41.26868  1.000 40.40011  ? 60  PHE A N   1 
ATOM   472  C CA  . PHE A 1 60  ? -2.14698  32.07632  40.58951  1.000 38.02805  ? 60  PHE A CA  1 
ATOM   473  C C   . PHE A 1 60  ? -2.96964  30.85251  40.96868  1.000 32.95203  ? 60  PHE A C   1 
ATOM   474  O O   . PHE A 1 60  ? -3.17183  29.95942  40.13696  1.000 33.47841  ? 60  PHE A O   1 
ATOM   475  C CB  . PHE A 1 60  ? -0.67189  31.83633  40.90920  1.000 41.91513  ? 60  PHE A CB  1 
ATOM   476  C CG  . PHE A 1 60  ? 0.24386   32.89690  40.37719  1.000 62.81065  ? 60  PHE A CG  1 
ATOM   477  C CD1 . PHE A 1 60  ? 0.39696   33.07599  39.01160  1.000 74.95472  ? 60  PHE A CD1 1 
ATOM   478  C CD2 . PHE A 1 60  ? 0.96457   33.70502  41.24087  1.000 67.86034  ? 60  PHE A CD2 1 
ATOM   479  C CE1 . PHE A 1 60  ? 1.24120   34.04864  38.52029  1.000 83.68646  ? 60  PHE A CE1 1 
ATOM   480  C CE2 . PHE A 1 60  ? 1.81179   34.67970  40.75365  1.000 70.30669  ? 60  PHE A CE2 1 
ATOM   481  C CZ  . PHE A 1 60  ? 1.95041   34.85181  39.39416  1.000 86.95711  ? 60  PHE A CZ  1 
ATOM   482  N N   . ALA A 1 61  ? -3.44563  30.79169  42.21578  1.000 28.42893  ? 61  ALA A N   1 
ATOM   483  C CA  . ALA A 1 61  ? -4.28744  29.67637  42.63741  1.000 35.18922  ? 61  ALA A CA  1 
ATOM   484  C C   . ALA A 1 61  ? -5.65856  29.74197  41.97828  1.000 34.64171  ? 61  ALA A C   1 
ATOM   485  O O   . ALA A 1 61  ? -6.17840  28.72270  41.51048  1.000 34.22140  ? 61  ALA A O   1 
ATOM   486  C CB  . ALA A 1 61  ? -4.42724  29.67016  44.16054  1.000 25.68918  ? 61  ALA A CB  1 
ATOM   487  N N   . LEU A 1 62  ? -6.25908  30.93454  41.94161  1.000 39.53732  ? 62  LEU A N   1 
ATOM   488  C CA  . LEU A 1 62  ? -7.56313  31.10343  41.30878  1.000 38.36552  ? 62  LEU A CA  1 
ATOM   489  C C   . LEU A 1 62  ? -7.51058  30.74666  39.83086  1.000 34.42907  ? 62  LEU A C   1 
ATOM   490  O O   . LEU A 1 62  ? -8.43169  30.11172  39.30241  1.000 42.16896  ? 62  LEU A O   1 
ATOM   491  C CB  . LEU A 1 62  ? -8.04223  32.54196  41.48969  1.000 41.65306  ? 62  LEU A CB  1 
ATOM   492  C CG  . LEU A 1 62  ? -8.42801  32.94071  42.90973  1.000 42.31973  ? 62  LEU A CG  1 
ATOM   493  C CD1 . LEU A 1 62  ? -8.37432  34.44723  43.06498  1.000 46.12805  ? 62  LEU A CD1 1 
ATOM   494  C CD2 . LEU A 1 62  ? -9.81844  32.42030  43.21713  1.000 40.97727  ? 62  LEU A CD2 1 
ATOM   495  N N   . THR A 1 63  ? -6.44511  31.16082  39.14422  1.000 32.37619  ? 63  THR A N   1 
ATOM   496  C CA  . THR A 1 63  ? -6.28975  30.81393  37.73787  1.000 30.42049  ? 63  THR A CA  1 
ATOM   497  C C   . THR A 1 63  ? -6.20672  29.30320  37.56259  1.000 33.58001  ? 63  THR A C   1 
ATOM   498  O O   . THR A 1 63  ? -6.86570  28.72913  36.68843  1.000 40.52199  ? 63  THR A O   1 
ATOM   499  C CB  . THR A 1 63  ? -5.04856  31.50240  37.17071  1.000 34.69498  ? 63  THR A CB  1 
ATOM   500  O OG1 . THR A 1 63  ? -5.18943  32.92173  37.30530  1.000 42.02406  ? 63  THR A OG1 1 
ATOM   501  C CG2 . THR A 1 63  ? -4.86313  31.15753  35.70620  1.000 28.88440  ? 63  THR A CG2 1 
ATOM   502  N N   . ASN A 1 64  ? -5.41747  28.64049  38.40838  1.000 31.61388  ? 64  ASN A N   1 
ATOM   503  C CA  . ASN A 1 64  ? -5.28662  27.18980  38.32761  1.000 33.75289  ? 64  ASN A CA  1 
ATOM   504  C C   . ASN A 1 64  ? -6.61908  26.49291  38.57103  1.000 36.61869  ? 64  ASN A C   1 
ATOM   505  O O   . ASN A 1 64  ? -7.00782  25.59662  37.81350  1.000 40.72056  ? 64  ASN A O   1 
ATOM   506  C CB  . ASN A 1 64  ? -4.23847  26.70256  39.32443  1.000 34.87907  ? 64  ASN A CB  1 
ATOM   507  C CG  . ASN A 1 64  ? -2.94926  26.29916  38.65134  1.000 31.08500  ? 64  ASN A CG  1 
ATOM   508  O OD1 . ASN A 1 64  ? -2.66065  26.72266  37.52901  1.000 33.93168  ? 64  ASN A OD1 1 
ATOM   509  N ND2 . ASN A 1 64  ? -2.16692  25.46675  39.32729  1.000 32.84682  ? 64  ASN A ND2 1 
ATOM   510  N N   . ILE A 1 65  ? -7.33519  26.88577  39.62678  1.000 34.97003  ? 65  ILE A N   1 
ATOM   511  C CA  . ILE A 1 65  ? -8.59470  26.21451  39.93700  1.000 36.97964  ? 65  ILE A CA  1 
ATOM   512  C C   . ILE A 1 65  ? -9.59181  26.40233  38.80043  1.000 39.49750  ? 65  ILE A C   1 
ATOM   513  O O   . ILE A 1 65  ? -10.34735 25.48338  38.46027  1.000 37.02383  ? 65  ILE A O   1 
ATOM   514  C CB  . ILE A 1 65  ? -9.15787  26.71101  41.27988  1.000 40.48690  ? 65  ILE A CB  1 
ATOM   515  C CG1 . ILE A 1 65  ? -8.20180  26.35042  42.41779  1.000 44.89414  ? 65  ILE A CG1 1 
ATOM   516  C CG2 . ILE A 1 65  ? -10.52447 26.10255  41.53309  1.000 34.41153  ? 65  ILE A CG2 1 
ATOM   517  C CD1 . ILE A 1 65  ? -7.82548  24.87996  42.45850  1.000 25.46830  ? 65  ILE A CD1 1 
ATOM   518  N N   . ALA A 1 66  ? -9.59065  27.58581  38.17808  1.000 34.71686  ? 66  ALA A N   1 
ATOM   519  C CA  . ALA A 1 66  ? -10.47855 27.83234  37.04595  1.000 35.06897  ? 66  ALA A CA  1 
ATOM   520  C C   . ALA A 1 66  ? -10.18168 26.88052  35.89353  1.000 37.28551  ? 66  ALA A C   1 
ATOM   521  O O   . ALA A 1 66  ? -11.09777 26.45056  35.18553  1.000 38.85866  ? 66  ALA A O   1 
ATOM   522  C CB  . ALA A 1 66  ? -10.35611 29.28651  36.58953  1.000 32.20649  ? 66  ALA A CB  1 
ATOM   523  N N   . VAL A 1 67  ? -8.90597  26.54156  35.68876  1.000 40.27281  ? 67  VAL A N   1 
ATOM   524  C CA  . VAL A 1 67  ? -8.55170  25.53781  34.68880  1.000 31.50028  ? 67  VAL A CA  1 
ATOM   525  C C   . VAL A 1 67  ? -9.09426  24.17309  35.09288  1.000 31.07461  ? 67  VAL A C   1 
ATOM   526  O O   . VAL A 1 67  ? -9.59735  23.41460  34.25451  1.000 42.50800  ? 67  VAL A O   1 
ATOM   527  C CB  . VAL A 1 67  ? -7.02461  25.50762  34.48385  1.000 35.29920  ? 67  VAL A CB  1 
ATOM   528  C CG1 . VAL A 1 67  ? -6.61301  24.31920  33.62405  1.000 28.55384  ? 67  VAL A CG1 1 
ATOM   529  C CG2 . VAL A 1 67  ? -6.55616  26.81194  33.86286  1.000 25.94926  ? 67  VAL A CG2 1 
ATOM   530  N N   . LEU A 1 68  ? -9.00672  23.84019  36.38370  1.000 32.62989  ? 68  LEU A N   1 
ATOM   531  C CA  . LEU A 1 68  ? -9.55159  22.57086  36.85805  1.000 38.62848  ? 68  LEU A CA  1 
ATOM   532  C C   . LEU A 1 68  ? -11.05434 22.48328  36.61669  1.000 43.61739  ? 68  LEU A C   1 
ATOM   533  O O   . LEU A 1 68  ? -11.56514 21.42571  36.23012  1.000 39.45898  ? 68  LEU A O   1 
ATOM   534  C CB  . LEU A 1 68  ? -9.24156  22.37937  38.34195  1.000 30.08012  ? 68  LEU A CB  1 
ATOM   535  C CG  . LEU A 1 68  ? -7.93942  21.64540  38.66880  1.000 30.90230  ? 68  LEU A CG  1 
ATOM   536  C CD1 . LEU A 1 68  ? -6.72018  22.53345  38.48418  1.000 28.55922  ? 68  LEU A CD1 1 
ATOM   537  C CD2 . LEU A 1 68  ? -7.99130  21.08027  40.07234  1.000 23.51469  ? 68  LEU A CD2 1 
ATOM   538  N N   . LYS A 1 69  ? -11.78135 23.58002  36.84542  1.000 35.59373  ? 69  LYS A N   1 
ATOM   539  C CA  . LYS A 1 69  ? -13.21446 23.58000  36.57390  1.000 45.78993  ? 69  LYS A CA  1 
ATOM   540  C C   . LYS A 1 69  ? -13.48509 23.26049  35.10983  1.000 38.29232  ? 69  LYS A C   1 
ATOM   541  O O   . LYS A 1 69  ? -14.34664 22.43411  34.78858  1.000 50.15912  ? 69  LYS A O   1 
ATOM   542  C CB  . LYS A 1 69  ? -13.82650 24.92938  36.95506  1.000 41.51627  ? 69  LYS A CB  1 
ATOM   543  N N   . HIS A 1 70  ? -12.74187 23.89812  34.20652  1.000 33.59022  ? 70  HIS A N   1 
ATOM   544  C CA  . HIS A 1 70  ? -12.90417 23.62651  32.78410  1.000 37.93022  ? 70  HIS A CA  1 
ATOM   545  C C   . HIS A 1 70  ? -12.58274 22.17079  32.46418  1.000 45.23344  ? 70  HIS A C   1 
ATOM   546  O O   . HIS A 1 70  ? -13.36520 21.48113  31.80040  1.000 45.61302  ? 70  HIS A O   1 
ATOM   547  C CB  . HIS A 1 70  ? -12.01608 24.57342  31.97717  1.000 45.37338  ? 70  HIS A CB  1 
ATOM   548  C CG  . HIS A 1 70  ? -11.92084 24.22558  30.52556  1.000 63.14960  ? 70  HIS A CG  1 
ATOM   549  N ND1 . HIS A 1 70  ? -10.91397 23.43441  30.01606  1.000 65.26285  ? 70  HIS A ND1 1 
ATOM   550  C CD2 . HIS A 1 70  ? -12.70318 24.56387  29.47372  1.000 69.81218  ? 70  HIS A CD2 1 
ATOM   551  C CE1 . HIS A 1 70  ? -11.08069 23.29924  28.71257  1.000 56.69963  ? 70  HIS A CE1 1 
ATOM   552  N NE2 . HIS A 1 70  ? -12.15882 23.97512  28.35836  1.000 67.22411  ? 70  HIS A NE2 1 
ATOM   553  N N   . ASN A 1 71  ? -11.43777 21.68043  32.94271  1.000 41.41869  ? 71  ASN A N   1 
ATOM   554  C CA  . ASN A 1 71  ? -11.03820 20.31236  32.62821  1.000 38.24302  ? 71  ASN A CA  1 
ATOM   555  C C   . ASN A 1 71  ? -12.00208 19.29738  33.22837  1.000 34.86106  ? 71  ASN A C   1 
ATOM   556  O O   . ASN A 1 71  ? -12.30172 18.27480  32.60130  1.000 40.66812  ? 71  ASN A O   1 
ATOM   557  C CB  . ASN A 1 71  ? -9.61374  20.05742  33.11709  1.000 34.80216  ? 71  ASN A CB  1 
ATOM   558  C CG  . ASN A 1 71  ? -8.59199  20.87957  32.36776  1.000 43.91895  ? 71  ASN A CG  1 
ATOM   559  O OD1 . ASN A 1 71  ? -8.93537  21.62656  31.45038  1.000 38.25515  ? 71  ASN A OD1 1 
ATOM   560  N ND2 . ASN A 1 71  ? -7.32812  20.75472  32.75710  1.000 39.18174  ? 71  ASN A ND2 1 
ATOM   561  N N   . LEU A 1 72  ? -12.49498 19.55674  34.44175  1.000 42.24401  ? 72  LEU A N   1 
ATOM   562  C CA  . LEU A 1 72  ? -13.41461 18.61548  35.07288  1.000 50.39614  ? 72  LEU A CA  1 
ATOM   563  C C   . LEU A 1 72  ? -14.68623 18.45351  34.25041  1.000 57.69060  ? 72  LEU A C   1 
ATOM   564  O O   . LEU A 1 72  ? -15.20544 17.33889  34.11347  1.000 52.85251  ? 72  LEU A O   1 
ATOM   565  C CB  . LEU A 1 72  ? -13.74887 19.06633  36.49599  1.000 40.15932  ? 72  LEU A CB  1 
ATOM   566  C CG  . LEU A 1 72  ? -14.76099 18.17371  37.22202  1.000 40.44528  ? 72  LEU A CG  1 
ATOM   567  C CD1 . LEU A 1 72  ? -14.21259 16.75874  37.35997  1.000 37.20043  ? 72  LEU A CD1 1 
ATOM   568  C CD2 . LEU A 1 72  ? -15.14033 18.74693  38.58212  1.000 42.93283  ? 72  LEU A CD2 1 
ATOM   569  N N   . ASN A 1 73  ? -15.19697 19.55482  33.68786  1.000 45.98133  ? 73  ASN A N   1 
ATOM   570  C CA  . ASN A 1 73  ? -16.37946 19.47530  32.83462  1.000 48.03913  ? 73  ASN A CA  1 
ATOM   571  C C   . ASN A 1 73  ? -16.12924 18.58554  31.62248  1.000 54.23949  ? 73  ASN A C   1 
ATOM   572  O O   . ASN A 1 73  ? -16.98447 17.77226  31.25138  1.000 51.39248  ? 73  ASN A O   1 
ATOM   573  C CB  . ASN A 1 73  ? -16.80148 20.87598  32.38942  1.000 55.93412  ? 73  ASN A CB  1 
ATOM   574  C CG  . ASN A 1 73  ? -17.45747 21.67198  33.50314  1.000 69.45252  ? 73  ASN A CG  1 
ATOM   575  O OD1 . ASN A 1 73  ? -18.09894 21.10806  34.39370  1.000 71.82967  ? 73  ASN A OD1 1 
ATOM   576  N ND2 . ASN A 1 73  ? -17.30441 22.99263  33.45529  1.000 67.08713  ? 73  ASN A ND2 1 
ATOM   577  N N   . SER A 1 74  ? -14.95792 18.72322  30.99647  1.000 43.91828  ? 74  SER A N   1 
ATOM   578  C CA  . SER A 1 74  ? -14.63022 17.90278  29.83582  1.000 41.03605  ? 74  SER A CA  1 
ATOM   579  C C   . SER A 1 74  ? -14.58725 16.42042  30.19282  1.000 48.71912  ? 74  SER A C   1 
ATOM   580  O O   . SER A 1 74  ? -15.05194 15.57465  29.41982  1.000 51.34828  ? 74  SER A O   1 
ATOM   581  C CB  . SER A 1 74  ? -13.29302 18.35534  29.24731  1.000 39.52557  ? 74  SER A CB  1 
ATOM   582  O OG  . SER A 1 74  ? -12.84037 17.46061  28.24779  1.000 71.63648  ? 74  SER A OG  1 
ATOM   583  N N   . LEU A 1 75  ? -14.04591 16.08701  31.36637  1.000 47.27147  ? 75  LEU A N   1 
ATOM   584  C CA  . LEU A 1 75  ? -13.86019 14.68797  31.73456  1.000 44.04270  ? 75  LEU A CA  1 
ATOM   585  C C   . LEU A 1 75  ? -15.15268 14.02941  32.20077  1.000 46.57155  ? 75  LEU A C   1 
ATOM   586  O O   . LEU A 1 75  ? -15.30237 12.81047  32.05731  1.000 48.66685  ? 75  LEU A O   1 
ATOM   587  C CB  . LEU A 1 75  ? -12.78725 14.56810  32.81960  1.000 44.78311  ? 75  LEU A CB  1 
ATOM   588  C CG  . LEU A 1 75  ? -11.36431 14.94591  32.40326  1.000 38.26624  ? 75  LEU A CG  1 
ATOM   589  C CD1 . LEU A 1 75  ? -10.41912 14.80505  33.57455  1.000 37.44973  ? 75  LEU A CD1 1 
ATOM   590  C CD2 . LEU A 1 75  ? -10.89047 14.09459  31.23277  1.000 36.04768  ? 75  LEU A CD2 1 
ATOM   591  N N   . ILE A 1 76  ? -16.08406 14.79841  32.77080  1.000 45.37636  ? 76  ILE A N   1 
ATOM   592  C CA  . ILE A 1 76  ? -17.38702 14.23530  33.11706  1.000 44.92421  ? 76  ILE A CA  1 
ATOM   593  C C   . ILE A 1 76  ? -18.10366 13.76644  31.85942  1.000 51.58812  ? 76  ILE A C   1 
ATOM   594  O O   . ILE A 1 76  ? -18.75663 12.71519  31.85055  1.000 48.25296  ? 76  ILE A O   1 
ATOM   595  C CB  . ILE A 1 76  ? -18.22844 15.26032  33.89915  1.000 49.85984  ? 76  ILE A CB  1 
ATOM   596  C CG1 . ILE A 1 76  ? -17.57501 15.57827  35.24146  1.000 42.58323  ? 76  ILE A CG1 1 
ATOM   597  C CG2 . ILE A 1 76  ? -19.63993 14.74235  34.11919  1.000 50.47075  ? 76  ILE A CG2 1 
ATOM   598  C CD1 . ILE A 1 76  ? -18.21199 16.74296  35.95325  1.000 46.54930  ? 76  ILE A CD1 1 
ATOM   599  N N   . LYS A 1 77  ? -17.97949 14.53218  30.77315  1.000 49.65354  ? 77  LYS A N   1 
ATOM   600  C CA  . LYS A 1 77  ? -18.54162 14.11185  29.49490  1.000 54.53439  ? 77  LYS A CA  1 
ATOM   601  C C   . LYS A 1 77  ? -17.79381 12.90735  28.93644  1.000 52.81682  ? 77  LYS A C   1 
ATOM   602  O O   . LYS A 1 77  ? -18.40878 11.91110  28.53904  1.000 60.83341  ? 77  LYS A O   1 
ATOM   603  C CB  . LYS A 1 77  ? -18.50531 15.27472  28.50168  1.000 48.76536  ? 77  LYS A CB  1 
ATOM   604  C CG  . LYS A 1 77  ? -19.23316 16.52323  28.97813  1.000 56.71729  ? 77  LYS A CG  1 
ATOM   605  C CD  . LYS A 1 77  ? -19.16378 17.64097  27.94622  1.000 55.63099  ? 77  LYS A CD  1 
ATOM   606  C CE  . LYS A 1 77  ? -19.91555 18.87780  28.41910  1.000 70.21027  ? 77  LYS A CE  1 
ATOM   607  N NZ  . LYS A 1 77  ? -21.36985 18.61838  28.62624  1.000 85.98146  ? 77  LYS A NZ  1 
ATOM   608  N N   . ARG A 1 78  ? -16.46116 12.97780  28.90685  1.000 49.53360  ? 78  ARG A N   1 
ATOM   609  C CA  . ARG A 1 78  ? -15.67395 11.94602  28.24220  1.000 49.27327  ? 78  ARG A CA  1 
ATOM   610  C C   . ARG A 1 78  ? -15.73422 10.60778  28.96630  1.000 48.08632  ? 78  ARG A C   1 
ATOM   611  O O   . ARG A 1 78  ? -15.56074 9.56478   28.32666  1.000 57.46858  ? 78  ARG A O   1 
ATOM   612  C CB  . ARG A 1 78  ? -14.21968 12.40388  28.09923  1.000 39.96331  ? 78  ARG A CB  1 
ATOM   613  N N   . SER A 1 79  ? -15.98090 10.60845  30.27489  1.000 45.43589  ? 79  SER A N   1 
ATOM   614  C CA  . SER A 1 79  ? -16.07102 9.37866   31.04993  1.000 47.63490  ? 79  SER A CA  1 
ATOM   615  C C   . SER A 1 79  ? -17.50087 8.87524   31.18235  1.000 54.65434  ? 79  SER A C   1 
ATOM   616  O O   . SER A 1 79  ? -17.75295 7.97251   31.98698  1.000 57.21190  ? 79  SER A O   1 
ATOM   617  C CB  . SER A 1 79  ? -15.46287 9.57766   32.44169  1.000 45.62663  ? 79  SER A CB  1 
ATOM   618  O OG  . SER A 1 79  ? -16.28604 10.39905  33.25383  1.000 44.89109  ? 79  SER A OG  1 
ATOM   619  N N   . ASN A 1 80  ? -18.43338 9.43104   30.40365  1.000 54.41667  ? 80  ASN A N   1 
ATOM   620  C CA  . ASN A 1 80  ? -19.85998 9.10803   30.50235  1.000 58.76373  ? 80  ASN A CA  1 
ATOM   621  C C   . ASN A 1 80  ? -20.35961 9.25943   31.93787  1.000 53.82251  ? 80  ASN A C   1 
ATOM   622  O O   . ASN A 1 80  ? -21.09360 8.41518   32.45606  1.000 55.19743  ? 80  ASN A O   1 
ATOM   623  C CB  . ASN A 1 80  ? -20.15688 7.70659   29.96088  1.000 45.85415  ? 80  ASN A CB  1 
ATOM   624  N N   . SER A 1 81  ? -19.94007 10.34861  32.58767  1.000 47.51659  ? 81  SER A N   1 
ATOM   625  C CA  . SER A 1 81  ? -20.41398 10.71781  33.92357  1.000 49.98491  ? 81  SER A CA  1 
ATOM   626  C C   . SER A 1 81  ? -20.03950 9.66291   34.96489  1.000 47.87382  ? 81  SER A C   1 
ATOM   627  O O   . SER A 1 81  ? -20.87282 9.20991   35.75249  1.000 59.67441  ? 81  SER A O   1 
ATOM   628  C CB  . SER A 1 81  ? -21.92581 10.97049  33.91850  1.000 50.25464  ? 81  SER A CB  1 
ATOM   629  O OG  . SER A 1 81  ? -22.26404 12.04553  33.05835  1.000 70.80775  ? 81  SER A OG  1 
ATOM   630  N N   . THR A 1 82  ? -18.76940 9.26613   34.96474  1.000 45.48855  ? 82  THR A N   1 
ATOM   631  C CA  . THR A 1 82  ? -18.26427 8.34548   35.97881  1.000 48.54812  ? 82  THR A CA  1 
ATOM   632  C C   . THR A 1 82  ? -18.00282 9.13497   37.25516  1.000 47.31009  ? 82  THR A C   1 
ATOM   633  O O   . THR A 1 82  ? -17.11392 9.99152   37.29146  1.000 43.83128  ? 82  THR A O   1 
ATOM   634  C CB  . THR A 1 82  ? -16.99742 7.64489   35.49944  1.000 51.06303  ? 82  THR A CB  1 
ATOM   635  O OG1 . THR A 1 82  ? -17.30456 6.81988   34.36997  1.000 49.56695  ? 82  THR A OG1 1 
ATOM   636  C CG2 . THR A 1 82  ? -16.41770 6.78052   36.61395  1.000 40.01343  ? 82  THR A CG2 1 
ATOM   637  N N   . ALA A 1 83  ? -18.77606 8.85727   38.29925  1.000 44.60967  ? 83  ALA A N   1 
ATOM   638  C CA  . ALA A 1 83  ? -18.70413 9.63970   39.52255  1.000 43.44327  ? 83  ALA A CA  1 
ATOM   639  C C   . ALA A 1 83  ? -17.72359 9.01928   40.51501  1.000 40.27971  ? 83  ALA A C   1 
ATOM   640  O O   . ALA A 1 83  ? -17.27334 7.88050   40.36582  1.000 39.41107  ? 83  ALA A O   1 
ATOM   641  C CB  . ALA A 1 83  ? -20.09084 9.77812   40.15105  1.000 39.33267  ? 83  ALA A CB  1 
ATOM   642  N N   . ALA A 1 84  ? -17.39163 9.79482   41.54236  1.000 35.43743  ? 84  ALA A N   1 
ATOM   643  C CA  . ALA A 1 84  ? -16.45111 9.33350   42.55109  1.000 38.18224  ? 84  ALA A CA  1 
ATOM   644  C C   . ALA A 1 84  ? -17.05233 8.20146   43.37585  1.000 37.88996  ? 84  ALA A C   1 
ATOM   645  O O   . ALA A 1 84  ? -18.27010 8.09962   43.54496  1.000 40.02596  ? 84  ALA A O   1 
ATOM   646  C CB  . ALA A 1 84  ? -16.04021 10.48500  43.46760  1.000 37.51515  ? 84  ALA A CB  1 
ATOM   647  N N   . THR A 1 85  ? -16.17782 7.34055   43.88547  1.000 45.73327  ? 85  THR A N   1 
ATOM   648  C CA  . THR A 1 85  ? -16.56746 6.23937   44.75455  1.000 41.30455  ? 85  THR A CA  1 
ATOM   649  C C   . THR A 1 85  ? -16.29686 6.62438   46.20198  1.000 45.81960  ? 85  THR A C   1 
ATOM   650  O O   . THR A 1 85  ? -15.19341 7.07196   46.53001  1.000 57.33335  ? 85  THR A O   1 
ATOM   651  C CB  . THR A 1 85  ? -15.80140 4.96652   44.39685  1.000 34.06295  ? 85  THR A CB  1 
ATOM   652  O OG1 . THR A 1 85  ? -16.13439 4.56705   43.06197  1.000 44.02275  ? 85  THR A OG1 1 
ATOM   653  C CG2 . THR A 1 85  ? -16.14628 3.84632   45.36609  1.000 40.29609  ? 85  THR A CG2 1 
ATOM   654  N N   . ASN A 1 86  ? -17.30351 6.46007   47.05934  1.000 48.99027  ? 86  ASN A N   1 
ATOM   655  C CA  . ASN A 1 86  ? -17.15153 6.79578   48.46973  1.000 40.40254  ? 86  ASN A CA  1 
ATOM   656  C C   . ASN A 1 86  ? -16.31684 5.73076   49.17124  1.000 40.68848  ? 86  ASN A C   1 
ATOM   657  O O   . ASN A 1 86  ? -16.69196 4.55448   49.19638  1.000 50.43617  ? 86  ASN A O   1 
ATOM   658  C CB  . ASN A 1 86  ? -18.51701 6.92350   49.13984  1.000 47.74777  ? 86  ASN A CB  1 
ATOM   659  C CG  . ASN A 1 86  ? -19.37055 8.02287   48.53559  1.000 48.58041  ? 86  ASN A CG  1 
ATOM   660  O OD1 . ASN A 1 86  ? -18.85692 9.01787   48.02971  1.000 50.86532  ? 86  ASN A OD1 1 
ATOM   661  N ND2 . ASN A 1 86  ? -20.68699 7.84918   48.59632  1.000 59.18558  ? 86  ASN A ND2 1 
ATOM   662  N N   . GLU A 1 87  ? -15.18539 6.13621   49.73415  1.000 46.31265  ? 87  GLU A N   1 
ATOM   663  C CA  . GLU A 1 87  ? -14.39684 5.24176   50.56479  1.000 46.08342  ? 87  GLU A CA  1 
ATOM   664  C C   . GLU A 1 87  ? -14.85660 5.34932   52.01103  1.000 41.50180  ? 87  GLU A C   1 
ATOM   665  O O   . GLU A 1 87  ? -15.50638 6.31596   52.41374  1.000 42.21989  ? 87  GLU A O   1 
ATOM   666  C CB  . GLU A 1 87  ? -12.90690 5.56871   50.46280  1.000 38.28838  ? 87  GLU A CB  1 
ATOM   667  C CG  . GLU A 1 87  ? -12.40738 5.72400   49.03909  1.000 48.99757  ? 87  GLU A CG  1 
ATOM   668  C CD  . GLU A 1 87  ? -12.41815 4.41879   48.26721  1.000 51.92213  ? 87  GLU A CD  1 
ATOM   669  O OE1 . GLU A 1 87  ? -12.39952 3.34512   48.90699  1.000 62.22993  ? 87  GLU A OE1 1 
ATOM   670  O OE2 . GLU A 1 87  ? -12.44185 4.47050   47.01864  1.000 54.20925  ? 87  GLU A OE2 1 
ATOM   671  N N   . VAL A 1 88  ? -14.51972 4.32849   52.79892  1.000 48.38371  ? 88  VAL A N   1 
ATOM   672  C CA  . VAL A 1 88  ? -14.79819 4.31956   54.22757  1.000 37.76505  ? 88  VAL A CA  1 
ATOM   673  C C   . VAL A 1 88  ? -13.63137 5.00842   54.92974  1.000 40.04353  ? 88  VAL A C   1 
ATOM   674  O O   . VAL A 1 88  ? -12.51304 4.46562   54.92336  1.000 41.99779  ? 88  VAL A O   1 
ATOM   675  C CB  . VAL A 1 88  ? -14.99675 2.89372   54.76140  1.000 51.64353  ? 88  VAL A CB  1 
ATOM   676  C CG1 . VAL A 1 88  ? -15.35581 2.93587   56.23936  1.000 45.79515  ? 88  VAL A CG1 1 
ATOM   677  C CG2 . VAL A 1 88  ? -16.07775 2.17131   53.97031  1.000 43.84993  ? 88  VAL A CG2 1 
ATOM   678  N N   . PRO A 1 89  ? -13.82742 6.18603   55.51586  1.000 34.85544  ? 89  PRO A N   1 
ATOM   679  C CA  . PRO A 1 89  ? -12.73059 6.83382   56.23530  1.000 39.03025  ? 89  PRO A CA  1 
ATOM   680  C C   . PRO A 1 89  ? -12.38145 6.07368   57.50516  1.000 45.10633  ? 89  PRO A C   1 
ATOM   681  O O   . PRO A 1 89  ? -13.18116 5.31055   58.05009  1.000 50.69699  ? 89  PRO A O   1 
ATOM   682  C CB  . PRO A 1 89  ? -13.28325 8.22742   56.55192  1.000 42.68740  ? 89  PRO A CB  1 
ATOM   683  C CG  . PRO A 1 89  ? -14.76069 8.05071   56.56204  1.000 37.28070  ? 89  PRO A CG  1 
ATOM   684  C CD  . PRO A 1 89  ? -15.06014 6.99156   55.53712  1.000 43.40363  ? 89  PRO A CD  1 
ATOM   685  N N   . GLU A 1 90  ? -11.14871 6.28223   57.96247  1.000 49.64094  ? 90  GLU A N   1 
ATOM   686  C CA  . GLU A 1 90  ? -10.66611 5.74389   59.22683  1.000 41.89437  ? 90  GLU A CA  1 
ATOM   687  C C   . GLU A 1 90  ? -10.35900 6.90307   60.16063  1.000 36.54652  ? 90  GLU A C   1 
ATOM   688  O O   . GLU A 1 90  ? -9.66298  7.84794   59.77410  1.000 37.86771  ? 90  GLU A O   1 
ATOM   689  C CB  . GLU A 1 90  ? -9.42189  4.88244   59.02627  1.000 54.02296  ? 90  GLU A CB  1 
ATOM   690  C CG  . GLU A 1 90  ? -9.57672  3.82669   57.95369  1.000 62.85729  ? 90  GLU A CG  1 
ATOM   691  C CD  . GLU A 1 90  ? -8.31192  3.01783   57.75888  1.000 88.57906  ? 90  GLU A CD  1 
ATOM   692  O OE1 . GLU A 1 90  ? -7.47881  2.97958   58.69544  1.000 76.43752  ? 90  GLU A OE1 1 
ATOM   693  O OE2 . GLU A 1 90  ? -8.15094  2.42859   56.66702  1.000 75.38050  ? 90  GLU A OE2 1 
ATOM   694  N N   . VAL A 1 91  ? -10.87721 6.82928   61.38286  1.000 48.78151  ? 91  VAL A N   1 
ATOM   695  C CA  . VAL A 1 91  ? -10.80092 7.92144   62.34463  1.000 45.82095  ? 91  VAL A CA  1 
ATOM   696  C C   . VAL A 1 91  ? -10.04776 7.44245   63.57565  1.000 43.28120  ? 91  VAL A C   1 
ATOM   697  O O   . VAL A 1 91  ? -10.30628 6.34423   64.08117  1.000 39.53716  ? 91  VAL A O   1 
ATOM   698  C CB  . VAL A 1 91  ? -12.20092 8.43280   62.72432  1.000 39.01105  ? 91  VAL A CB  1 
ATOM   699  C CG1 . VAL A 1 91  ? -12.09868 9.57017   63.72886  1.000 35.55498  ? 91  VAL A CG1 1 
ATOM   700  C CG2 . VAL A 1 91  ? -12.93867 8.87469   61.47635  1.000 37.49434  ? 91  VAL A CG2 1 
ATOM   701  N N   . THR A 1 92  ? -9.11786  8.26787   64.05047  1.000 35.73586  ? 92  THR A N   1 
ATOM   702  C CA  . THR A 1 92  ? -8.33882  7.98384   65.24591  1.000 37.23719  ? 92  THR A CA  1 
ATOM   703  C C   . THR A 1 92  ? -8.21996  9.26641   66.05231  1.000 47.79118  ? 92  THR A C   1 
ATOM   704  O O   . THR A 1 92  ? -7.90792  10.32329  65.49253  1.000 39.67400  ? 92  THR A O   1 
ATOM   705  C CB  . THR A 1 92  ? -6.94467  7.45269   64.89495  1.000 35.98413  ? 92  THR A CB  1 
ATOM   706  O OG1 . THR A 1 92  ? -7.04657  6.51939   63.81612  1.000 47.02763  ? 92  THR A OG1 1 
ATOM   707  C CG2 . THR A 1 92  ? -6.32076  6.75527   66.09475  1.000 45.55925  ? 92  THR A CG2 1 
ATOM   708  N N   . VAL A 1 93  ? -8.47491  9.17524   67.35705  1.000 35.56436  ? 93  VAL A N   1 
ATOM   709  C CA  . VAL A 1 93  ? -8.38813  10.31609  68.25974  1.000 39.38642  ? 93  VAL A CA  1 
ATOM   710  C C   . VAL A 1 93  ? -7.27102  10.04761  69.25941  1.000 38.28760  ? 93  VAL A C   1 
ATOM   711  O O   . VAL A 1 93  ? -7.14646  8.93034   69.77563  1.000 39.47858  ? 93  VAL A O   1 
ATOM   712  C CB  . VAL A 1 93  ? -9.72989  10.58743  68.96686  1.000 45.76296  ? 93  VAL A CB  1 
ATOM   713  C CG1 . VAL A 1 93  ? -10.17736 9.37537   69.77012  1.000 64.06618  ? 93  VAL A CG1 1 
ATOM   714  C CG2 . VAL A 1 93  ? -9.63559  11.82409  69.85080  1.000 41.49995  ? 93  VAL A CG2 1 
ATOM   715  N N   . PHE A 1 94  ? -6.44383  11.06230  69.50431  1.000 36.20031  ? 94  PHE A N   1 
ATOM   716  C CA  . PHE A 1 94  ? -5.30773  10.93630  70.40660  1.000 33.66008  ? 94  PHE A CA  1 
ATOM   717  C C   . PHE A 1 94  ? -4.85747  12.33019  70.81583  1.000 33.91744  ? 94  PHE A C   1 
ATOM   718  O O   . PHE A 1 94  ? -5.21330  13.32652  70.18355  1.000 40.48592  ? 94  PHE A O   1 
ATOM   719  C CB  . PHE A 1 94  ? -4.15389  10.15440  69.76249  1.000 26.84891  ? 94  PHE A CB  1 
ATOM   720  C CG  . PHE A 1 94  ? -3.72820  10.68550  68.42184  1.000 29.05856  ? 94  PHE A CG  1 
ATOM   721  C CD1 . PHE A 1 94  ? -4.33413  10.23295  67.26018  1.000 36.25654  ? 94  PHE A CD1 1 
ATOM   722  C CD2 . PHE A 1 94  ? -2.71216  11.62589  68.31969  1.000 26.71165  ? 94  PHE A CD2 1 
ATOM   723  C CE1 . PHE A 1 94  ? -3.94062  10.71453  66.01905  1.000 37.75986  ? 94  PHE A CE1 1 
ATOM   724  C CE2 . PHE A 1 94  ? -2.31464  12.11311  67.08211  1.000 33.56176  ? 94  PHE A CE2 1 
ATOM   725  C CZ  . PHE A 1 94  ? -2.93164  11.65503  65.93061  1.000 33.14482  ? 94  PHE A CZ  1 
ATOM   726  N N   . SER A 1 95  ? -4.06929  12.38882  71.88189  1.000 36.44223  ? 95  SER A N   1 
ATOM   727  C CA  . SER A 1 95  ? -3.62001  13.65704  72.43182  1.000 40.13812  ? 95  SER A CA  1 
ATOM   728  C C   . SER A 1 95  ? -2.24134  14.01093  71.89035  1.000 40.66850  ? 95  SER A C   1 
ATOM   729  O O   . SER A 1 95  ? -1.42608  13.13561  71.59091  1.000 39.66801  ? 95  SER A O   1 
ATOM   730  C CB  . SER A 1 95  ? -3.58897  13.61149  73.96172  1.000 31.45848  ? 95  SER A CB  1 
ATOM   731  O OG  . SER A 1 95  ? -2.71328  12.60226  74.42309  1.000 42.26696  ? 95  SER A OG  1 
ATOM   732  N N   . LYS A 1 96  ? -1.99509  15.31551  71.76010  1.000 39.63509  ? 96  LYS A N   1 
ATOM   733  C CA  . LYS A 1 96  ? -0.70586  15.78253  71.26489  1.000 38.71103  ? 96  LYS A CA  1 
ATOM   734  C C   . LYS A 1 96  ? 0.41415   15.46320  72.24835  1.000 41.52558  ? 96  LYS A C   1 
ATOM   735  O O   . LYS A 1 96  ? 1.54200   15.16815  71.83799  1.000 46.03547  ? 96  LYS A O   1 
ATOM   736  C CB  . LYS A 1 96  ? -0.77531  17.28524  70.98951  1.000 37.06761  ? 96  LYS A CB  1 
ATOM   737  C CG  . LYS A 1 96  ? 0.53408   17.91493  70.52421  1.000 44.59051  ? 96  LYS A CG  1 
ATOM   738  C CD  . LYS A 1 96  ? 0.36481   19.41616  70.29128  1.000 34.17904  ? 96  LYS A CD  1 
ATOM   739  C CE  . LYS A 1 96  ? 1.62624   20.05322  69.72379  1.000 42.51833  ? 96  LYS A CE  1 
ATOM   740  N NZ  . LYS A 1 96  ? 2.12018   19.38785  68.47882  1.000 43.68578  ? 96  LYS A NZ  1 
ATOM   741  N N   . SER A 1 97  ? 0.12146   15.50314  73.53990  1.000 46.55533  ? 97  SER A N   1 
ATOM   742  C CA  . SER A 1 97  ? 1.09927   15.34115  74.60634  1.000 43.95917  ? 97  SER A CA  1 
ATOM   743  C C   . SER A 1 97  ? 0.60624   14.30073  75.59083  1.000 42.09401  ? 97  SER A C   1 
ATOM   744  O O   . SER A 1 97  ? -0.56667  13.90936  75.56498  1.000 44.66344  ? 97  SER A O   1 
ATOM   745  C CB  . SER A 1 97  ? 1.33602   16.68187  75.32409  1.000 33.43331  ? 97  SER A CB  1 
ATOM   746  O OG  . SER A 1 97  ? 1.65830   17.70703  74.39830  1.000 60.25606  ? 97  SER A OG  1 
ATOM   747  N N   . PRO A 1 98  ? 1.48215   13.80160  76.46413  1.000 45.49643  ? 98  PRO A N   1 
ATOM   748  C CA  . PRO A 1 98  ? 1.01230   12.94525  77.55941  1.000 51.02877  ? 98  PRO A CA  1 
ATOM   749  C C   . PRO A 1 98  ? 0.01993   13.68899  78.44329  1.000 47.28213  ? 98  PRO A C   1 
ATOM   750  O O   . PRO A 1 98  ? 0.18307   14.87704  78.73059  1.000 46.42915  ? 98  PRO A O   1 
ATOM   751  C CB  . PRO A 1 98  ? 2.29767   12.59732  78.31753  1.000 44.42540  ? 98  PRO A CB  1 
ATOM   752  C CG  . PRO A 1 98  ? 3.37446   12.72000  77.30104  1.000 45.54927  ? 98  PRO A CG  1 
ATOM   753  C CD  . PRO A 1 98  ? 2.95475   13.84126  76.38909  1.000 40.53050  ? 98  PRO A CD  1 
ATOM   754  N N   . VAL A 1 99  ? -1.01392  12.97299  78.87502  1.000 43.84277  ? 99  VAL A N   1 
ATOM   755  C CA  . VAL A 1 99  ? -2.14151  13.58361  79.57455  1.000 55.70571  ? 99  VAL A CA  1 
ATOM   756  C C   . VAL A 1 99  ? -1.76747  13.84986  81.02631  1.000 50.73655  ? 99  VAL A C   1 
ATOM   757  O O   . VAL A 1 99  ? -1.41086  12.92815  81.76707  1.000 52.45547  ? 99  VAL A O   1 
ATOM   758  C CB  . VAL A 1 99  ? -3.38942  12.69469  79.49337  1.000 48.79319  ? 99  VAL A CB  1 
ATOM   759  C CG1 . VAL A 1 99  ? -4.51684  13.30792  80.30370  1.000 56.98153  ? 99  VAL A CG1 1 
ATOM   760  C CG2 . VAL A 1 99  ? -3.80572  12.49727  78.04485  1.000 51.69820  ? 99  VAL A CG2 1 
ATOM   761  N N   . THR A 1 100 ? -1.86872  15.11050  81.43874  1.000 54.23159  ? 100 THR A N   1 
ATOM   762  C CA  . THR A 1 100 ? -1.74052  15.49900  82.83747  1.000 51.41437  ? 100 THR A CA  1 
ATOM   763  C C   . THR A 1 100 ? -2.95442  16.33627  83.20809  1.000 50.12171  ? 100 THR A C   1 
ATOM   764  O O   . THR A 1 100 ? -3.14336  17.42903  82.66408  1.000 45.73095  ? 100 THR A O   1 
ATOM   765  C CB  . THR A 1 100 ? -0.44635  16.27894  83.08683  1.000 52.47706  ? 100 THR A CB  1 
ATOM   766  O OG1 . THR A 1 100 ? 0.65884   15.36756  83.12793  1.000 55.07710  ? 100 THR A OG1 1 
ATOM   767  C CG2 . THR A 1 100 ? -0.52118  17.03412  84.40703  1.000 58.27937  ? 100 THR A CG2 1 
ATOM   768  N N   . LEU A 1 101 ? -3.77709  15.81984  84.12042  1.000 55.00324  ? 101 LEU A N   1 
ATOM   769  C CA  . LEU A 1 101 ? -4.98246  16.52557  84.54058  1.000 41.08347  ? 101 LEU A CA  1 
ATOM   770  C C   . LEU A 1 101 ? -4.64973  17.94811  84.97062  1.000 43.38660  ? 101 LEU A C   1 
ATOM   771  O O   . LEU A 1 101 ? -3.73477  18.17228  85.76786  1.000 46.43583  ? 101 LEU A O   1 
ATOM   772  C CB  . LEU A 1 101 ? -5.66414  15.77137  85.68526  1.000 44.75328  ? 101 LEU A CB  1 
ATOM   773  C CG  . LEU A 1 101 ? -6.21069  14.37850  85.36488  1.000 53.66191  ? 101 LEU A CG  1 
ATOM   774  C CD1 . LEU A 1 101 ? -6.93091  13.79244  86.56877  1.000 51.45850  ? 101 LEU A CD1 1 
ATOM   775  C CD2 . LEU A 1 101 ? -7.13417  14.42247  84.15808  1.000 54.19212  ? 101 LEU A CD2 1 
ATOM   776  N N   . GLY A 1 102 ? -5.37913  18.91237  84.40980  1.000 41.03867  ? 102 GLY A N   1 
ATOM   777  C CA  . GLY A 1 102 ? -5.16943  20.30973  84.71400  1.000 44.70287  ? 102 GLY A CA  1 
ATOM   778  C C   . GLY A 1 102 ? -4.10060  21.00374  83.89409  1.000 56.35196  ? 102 GLY A C   1 
ATOM   779  O O   . GLY A 1 102 ? -4.00118  22.23586  83.95823  1.000 52.16497  ? 102 GLY A O   1 
ATOM   780  N N   . GLN A 1 103 ? -3.29645  20.26123  83.12888  1.000 57.43507  ? 103 GLN A N   1 
ATOM   781  C CA  . GLN A 1 103 ? -2.27119  20.87126  82.29117  1.000 50.88724  ? 103 GLN A CA  1 
ATOM   782  C C   . GLN A 1 103 ? -2.75390  20.99359  80.84935  1.000 56.23599  ? 103 GLN A C   1 
ATOM   783  O O   . GLN A 1 103 ? -3.37956  20.06404  80.32458  1.000 39.59819  ? 103 GLN A O   1 
ATOM   784  C CB  . GLN A 1 103 ? -0.98388  20.04717  82.32516  1.000 53.35535  ? 103 GLN A CB  1 
ATOM   785  N N   . PRO A 1 104 ? -2.46673  22.12210  80.19621  1.000 42.70788  ? 104 PRO A N   1 
ATOM   786  C CA  . PRO A 1 104 ? -2.95052  22.33088  78.82332  1.000 49.34598  ? 104 PRO A CA  1 
ATOM   787  C C   . PRO A 1 104 ? -2.46999  21.24221  77.87262  1.000 52.32885  ? 104 PRO A C   1 
ATOM   788  O O   . PRO A 1 104 ? -1.32420  20.79212  77.94010  1.000 53.66208  ? 104 PRO A O   1 
ATOM   789  C CB  . PRO A 1 104 ? -2.36836  23.70047  78.44814  1.000 48.26773  ? 104 PRO A CB  1 
ATOM   790  C CG  . PRO A 1 104 ? -1.20292  23.88947  79.37716  1.000 57.73683  ? 104 PRO A CG  1 
ATOM   791  C CD  . PRO A 1 104 ? -1.62451  23.23681  80.66013  1.000 51.55488  ? 104 PRO A CD  1 
ATOM   792  N N   . ASN A 1 105 ? -3.36708  20.82162  76.98035  1.000 46.29274  ? 105 ASN A N   1 
ATOM   793  C CA  . ASN A 1 105 ? -3.07012  19.78947  75.99442  1.000 40.66451  ? 105 ASN A CA  1 
ATOM   794  C C   . ASN A 1 105 ? -3.92858  20.03766  74.75804  1.000 38.25990  ? 105 ASN A C   1 
ATOM   795  O O   . ASN A 1 105 ? -4.69117  21.00661  74.69104  1.000 40.48769  ? 105 ASN A O   1 
ATOM   796  C CB  . ASN A 1 105 ? -3.30905  18.39352  76.57845  1.000 45.13333  ? 105 ASN A CB  1 
ATOM   797  C CG  . ASN A 1 105 ? -2.51079  17.31593  75.86886  1.000 46.44645  ? 105 ASN A CG  1 
ATOM   798  O OD1 . ASN A 1 105 ? -2.29535  17.37729  74.65627  1.000 47.53195  ? 105 ASN A OD1 1 
ATOM   799  N ND2 . ASN A 1 105 ? -2.06574  16.32041  76.62471  1.000 31.15507  ? 105 ASN A ND2 1 
ATOM   800  N N   . ILE A 1 106 ? -3.79732  19.15445  73.76863  1.000 44.77290  ? 106 ILE A N   1 
ATOM   801  C CA  . ILE A 1 106 ? -4.52715  19.26630  72.50715  1.000 42.32246  ? 106 ILE A CA  1 
ATOM   802  C C   . ILE A 1 106 ? -5.00428  17.88288  72.08491  1.000 41.53763  ? 106 ILE A C   1 
ATOM   803  O O   . ILE A 1 106 ? -4.20241  16.94747  71.98191  1.000 36.61292  ? 106 ILE A O   1 
ATOM   804  C CB  . ILE A 1 106 ? -3.67043  19.88438  71.38309  1.000 34.66995  ? 106 ILE A CB  1 
ATOM   805  C CG1 . ILE A 1 106 ? -3.12472  21.25508  71.79025  1.000 34.18183  ? 106 ILE A CG1 1 
ATOM   806  C CG2 . ILE A 1 106 ? -4.48934  19.99616  70.10106  1.000 35.21729  ? 106 ILE A CG2 1 
ATOM   807  C CD1 . ILE A 1 106 ? -2.26691  21.90497  70.72005  1.000 36.82459  ? 106 ILE A CD1 1 
ATOM   808  N N   . LEU A 1 107 ? -6.30341  17.75759  71.82200  1.000 40.71778  ? 107 LEU A N   1 
ATOM   809  C CA  . LEU A 1 107 ? -6.86001  16.53967  71.25197  1.000 36.04660  ? 107 LEU A CA  1 
ATOM   810  C C   . LEU A 1 107 ? -6.76261  16.59385  69.73059  1.000 42.16356  ? 107 LEU A C   1 
ATOM   811  O O   . LEU A 1 107 ? -7.04778  17.62126  69.10737  1.000 40.37346  ? 107 LEU A O   1 
ATOM   812  C CB  . LEU A 1 107 ? -8.31358  16.34700  71.69079  1.000 35.54591  ? 107 LEU A CB  1 
ATOM   813  C CG  . LEU A 1 107 ? -8.58134  15.24200  72.72185  1.000 58.31025  ? 107 LEU A CG  1 
ATOM   814  C CD1 . LEU A 1 107 ? -7.70484  15.40494  73.95576  1.000 40.26314  ? 107 LEU A CD1 1 
ATOM   815  C CD2 . LEU A 1 107 ? -10.05038 15.20175  73.11499  1.000 45.02241  ? 107 LEU A CD2 1 
ATOM   816  N N   . ILE A 1 108 ? -6.34160  15.48272  69.13805  1.000 41.53734  ? 108 ILE A N   1 
ATOM   817  C CA  . ILE A 1 108 ? -6.09163  15.39107  67.70521  1.000 39.14733  ? 108 ILE A CA  1 
ATOM   818  C C   . ILE A 1 108 ? -6.98502  14.29426  67.14686  1.000 39.93467  ? 108 ILE A C   1 
ATOM   819  O O   . ILE A 1 108 ? -6.94437  13.15107  67.61896  1.000 44.17882  ? 108 ILE A O   1 
ATOM   820  C CB  . ILE A 1 108 ? -4.61086  15.10864  67.40484  1.000 38.99237  ? 108 ILE A CB  1 
ATOM   821  C CG1 . ILE A 1 108 ? -3.73981  16.25194  67.93062  1.000 41.69143  ? 108 ILE A CG1 1 
ATOM   822  C CG2 . ILE A 1 108 ? -4.38874  14.91736  65.92007  1.000 30.53223  ? 108 ILE A CG2 1 
ATOM   823  C CD1 . ILE A 1 108 ? -2.25891  16.00933  67.79228  1.000 36.19276  ? 108 ILE A CD1 1 
ATOM   824  N N   . CYS A 1 109 ? -7.79973  14.64311  66.15575  1.000 32.64345  ? 109 CYS A N   1 
ATOM   825  C CA  . CYS A 1 109 ? -8.69144  13.69696  65.49532  1.000 34.73017  ? 109 CYS A CA  1 
ATOM   826  C C   . CYS A 1 109 ? -8.26138  13.58610  64.04067  1.000 35.07142  ? 109 CYS A C   1 
ATOM   827  O O   . CYS A 1 109 ? -8.46815  14.51682  63.25397  1.000 32.26972  ? 109 CYS A O   1 
ATOM   828  C CB  . CYS A 1 109 ? -10.14945 14.13785  65.60742  1.000 39.94546  ? 109 CYS A CB  1 
ATOM   829  S SG  . CYS A 1 109 ? -11.32809 13.02619  64.80226  1.000 46.84707  ? 109 CYS A SG  1 
ATOM   830  N N   . LEU A 1 110 ? -7.65319  12.45843  63.69324  1.000 35.92421  ? 110 LEU A N   1 
ATOM   831  C CA  . LEU A 1 110 ? -7.21932  12.19465  62.33051  1.000 31.63035  ? 110 LEU A CA  1 
ATOM   832  C C   . LEU A 1 110 ? -8.32051  11.44169  61.60007  1.000 36.21886  ? 110 LEU A C   1 
ATOM   833  O O   . LEU A 1 110 ? -8.74040  10.36657  62.04095  1.000 36.02152  ? 110 LEU A O   1 
ATOM   834  C CB  . LEU A 1 110 ? -5.92206  11.38787  62.32457  1.000 35.48279  ? 110 LEU A CB  1 
ATOM   835  C CG  . LEU A 1 110 ? -5.48957  10.73602  61.00499  1.000 43.57786  ? 110 LEU A CG  1 
ATOM   836  C CD1 . LEU A 1 110 ? -5.08723  11.77738  59.96874  1.000 27.28860  ? 110 LEU A CD1 1 
ATOM   837  C CD2 . LEU A 1 110 ? -4.35261  9.75107   61.24532  1.000 33.56239  ? 110 LEU A CD2 1 
ATOM   838  N N   . VAL A 1 111 ? -8.79583  12.01245  60.49964  1.000 35.68760  ? 111 VAL A N   1 
ATOM   839  C CA  . VAL A 1 111 ? -9.70129  11.33271  59.58165  1.000 37.00408  ? 111 VAL A CA  1 
ATOM   840  C C   . VAL A 1 111 ? -8.88451  10.98543  58.34622  1.000 37.52436  ? 111 VAL A C   1 
ATOM   841  O O   . VAL A 1 111 ? -8.45863  11.87908  57.60453  1.000 35.93990  ? 111 VAL A O   1 
ATOM   842  C CB  . VAL A 1 111 ? -10.92151 12.19564  59.22969  1.000 35.55930  ? 111 VAL A CB  1 
ATOM   843  C CG1 . VAL A 1 111 ? -11.94753 11.37711  58.46419  1.000 30.21734  ? 111 VAL A CG1 1 
ATOM   844  C CG2 . VAL A 1 111 ? -11.54209 12.76597  60.49262  1.000 42.51025  ? 111 VAL A CG2 1 
ATOM   845  N N   . ASP A 1 112 ? -8.65077  9.69465   58.12940  1.000 40.89798  ? 112 ASP A N   1 
ATOM   846  C CA  . ASP A 1 112 ? -7.80037  9.21509   57.05089  1.000 32.75690  ? 112 ASP A CA  1 
ATOM   847  C C   . ASP A 1 112 ? -8.63405  8.51111   55.98363  1.000 35.80905  ? 112 ASP A C   1 
ATOM   848  O O   . ASP A 1 112 ? -9.78530  8.12898   56.21204  1.000 40.86731  ? 112 ASP A O   1 
ATOM   849  C CB  . ASP A 1 112 ? -6.72327  8.26848   57.60001  1.000 36.69366  ? 112 ASP A CB  1 
ATOM   850  C CG  . ASP A 1 112 ? -5.47907  8.21338   56.72480  1.000 33.47024  ? 112 ASP A CG  1 
ATOM   851  O OD1 . ASP A 1 112 ? -5.48163  8.81698   55.63098  1.000 35.29522  ? 112 ASP A OD1 1 
ATOM   852  O OD2 . ASP A 1 112 ? -4.49241  7.56098   57.13331  1.000 43.83548  ? 112 ASP A OD2 1 
ATOM   853  N N   . ASN A 1 113 ? -8.02797  8.34547   54.80627  1.000 34.09458  ? 113 ASN A N   1 
ATOM   854  C CA  . ASN A 1 113 ? -8.65880  7.68936   53.65692  1.000 33.77410  ? 113 ASN A CA  1 
ATOM   855  C C   . ASN A 1 113 ? -9.99932  8.33807   53.31309  1.000 31.02208  ? 113 ASN A C   1 
ATOM   856  O O   . ASN A 1 113 ? -11.03416 7.67846   53.20438  1.000 40.57619  ? 113 ASN A O   1 
ATOM   857  C CB  . ASN A 1 113 ? -8.81964  6.18691   53.89757  1.000 33.45395  ? 113 ASN A CB  1 
ATOM   858  C CG  . ASN A 1 113 ? -9.27496  5.44432   52.65027  1.000 48.39930  ? 113 ASN A CG  1 
ATOM   859  O OD1 . ASN A 1 113 ? -10.34946 4.84634   52.63062  1.000 54.11945  ? 113 ASN A OD1 1 
ATOM   860  N ND2 . ASN A 1 113 ? -8.46935  5.50353   51.59466  1.000 49.93412  ? 113 ASN A ND2 1 
ATOM   861  N N   . ILE A 1 114 ? -9.97427  9.65419   53.14493  1.000 30.71183  ? 114 ILE A N   1 
ATOM   862  C CA  . ILE A 1 114 ? -11.17091 10.41714  52.81543  1.000 30.39416  ? 114 ILE A CA  1 
ATOM   863  C C   . ILE A 1 114 ? -11.30426 10.48224  51.30288  1.000 35.63278  ? 114 ILE A C   1 
ATOM   864  O O   . ILE A 1 114 ? -10.40853 10.98392  50.61509  1.000 38.02312  ? 114 ILE A O   1 
ATOM   865  C CB  . ILE A 1 114 ? -11.11368 11.83065  53.40809  1.000 27.86083  ? 114 ILE A CB  1 
ATOM   866  C CG1 . ILE A 1 114 ? -10.92039 11.77704  54.92103  1.000 25.76509  ? 114 ILE A CG1 1 
ATOM   867  C CG2 . ILE A 1 114 ? -12.37244 12.61004  53.03325  1.000 29.09934  ? 114 ILE A CG2 1 
ATOM   868  C CD1 . ILE A 1 114 ? -10.65837 13.13850  55.52499  1.000 27.93638  ? 114 ILE A CD1 1 
ATOM   869  N N   . PHE A 1 115 ? -12.41502 9.97734   50.78358  1.000 41.72425  ? 115 PHE A N   1 
ATOM   870  C CA  . PHE A 1 115 ? -12.76059 10.28964  49.40442  1.000 43.94016  ? 115 PHE A CA  1 
ATOM   871  C C   . PHE A 1 115 ? -14.24990 10.06799  49.17525  1.000 44.36296  ? 115 PHE A C   1 
ATOM   872  O O   . PHE A 1 115 ? -14.79669 9.03822   49.59335  1.000 39.85766  ? 115 PHE A O   1 
ATOM   873  C CB  . PHE A 1 115 ? -11.94047 9.46755   48.41144  1.000 33.33690  ? 115 PHE A CB  1 
ATOM   874  C CG  . PHE A 1 115 ? -11.89406 10.07654  47.04787  1.000 34.04395  ? 115 PHE A CG  1 
ATOM   875  C CD1 . PHE A 1 115 ? -11.03798 11.13418  46.78062  1.000 30.71770  ? 115 PHE A CD1 1 
ATOM   876  C CD2 . PHE A 1 115 ? -12.73254 9.62094   46.04141  1.000 34.36605  ? 115 PHE A CD2 1 
ATOM   877  C CE1 . PHE A 1 115 ? -11.00231 11.71441  45.52272  1.000 29.54944  ? 115 PHE A CE1 1 
ATOM   878  C CE2 . PHE A 1 115 ? -12.70337 10.19331  44.78675  1.000 35.36688  ? 115 PHE A CE2 1 
ATOM   879  C CZ  . PHE A 1 115 ? -11.83673 11.24290  44.52712  1.000 41.99838  ? 115 PHE A CZ  1 
ATOM   880  N N   . PRO A 1 116 ? -14.94867 11.02146  48.53686  1.000 36.43716  ? 116 PRO A N   1 
ATOM   881  C CA  . PRO A 1 116 ? -14.41956 12.31170  48.07357  1.000 34.94260  ? 116 PRO A CA  1 
ATOM   882  C C   . PRO A 1 116 ? -14.12092 13.27625  49.22522  1.000 40.01530  ? 116 PRO A C   1 
ATOM   883  O O   . PRO A 1 116 ? -14.55211 13.02352  50.35409  1.000 36.66902  ? 116 PRO A O   1 
ATOM   884  C CB  . PRO A 1 116 ? -15.55212 12.84850  47.19174  1.000 41.73045  ? 116 PRO A CB  1 
ATOM   885  C CG  . PRO A 1 116 ? -16.78394 12.24276  47.76762  1.000 41.22186  ? 116 PRO A CG  1 
ATOM   886  C CD  . PRO A 1 116 ? -16.37646 10.86606  48.20914  1.000 42.71758  ? 116 PRO A CD  1 
ATOM   887  N N   . PRO A 1 117 ? -13.38297 14.35891  48.95028  1.000 31.90652  ? 117 PRO A N   1 
ATOM   888  C CA  . PRO A 1 117 ? -13.07589 15.32861  50.01324  1.000 33.06165  ? 117 PRO A CA  1 
ATOM   889  C C   . PRO A 1 117 ? -14.28404 16.14508  50.45048  1.000 38.83567  ? 117 PRO A C   1 
ATOM   890  O O   . PRO A 1 117 ? -14.36353 17.34991  50.18412  1.000 33.89086  ? 117 PRO A O   1 
ATOM   891  C CB  . PRO A 1 117 ? -12.00099 16.21743  49.37473  1.000 34.81298  ? 117 PRO A CB  1 
ATOM   892  C CG  . PRO A 1 117 ? -12.23921 16.09478  47.90754  1.000 35.12180  ? 117 PRO A CG  1 
ATOM   893  C CD  . PRO A 1 117 ? -12.68417 14.67890  47.69448  1.000 38.05235  ? 117 PRO A CD  1 
ATOM   894  N N   . VAL A 1 118 ? -15.22959 15.49018  51.12555  1.000 31.47531  ? 118 VAL A N   1 
ATOM   895  C CA  . VAL A 1 118 ? -16.42290 16.12624  51.68059  1.000 36.13913  ? 118 VAL A CA  1 
ATOM   896  C C   . VAL A 1 118 ? -16.66656 15.46736  53.02999  1.000 37.24795  ? 118 VAL A C   1 
ATOM   897  O O   . VAL A 1 118 ? -17.05450 14.29551  53.08453  1.000 43.97528  ? 118 VAL A O   1 
ATOM   898  C CB  . VAL A 1 118 ? -17.65809 15.96548  50.77939  1.000 45.01155  ? 118 VAL A CB  1 
ATOM   899  C CG1 . VAL A 1 118 ? -18.89999 16.48824  51.48426  1.000 48.17157  ? 118 VAL A CG1 1 
ATOM   900  C CG2 . VAL A 1 118 ? -17.46080 16.67152  49.44421  1.000 34.02915  ? 118 VAL A CG2 1 
ATOM   901  N N   . VAL A 1 119 ? -16.44465 16.20237  54.11739  1.000 31.95127  ? 119 VAL A N   1 
ATOM   902  C CA  . VAL A 1 119 ? -16.47374 15.58451  55.43672  1.000 38.88298  ? 119 VAL A CA  1 
ATOM   903  C C   . VAL A 1 119 ? -16.99525 16.58682  56.45725  1.000 38.26809  ? 119 VAL A C   1 
ATOM   904  O O   . VAL A 1 119 ? -16.87042 17.80160  56.28494  1.000 38.92313  ? 119 VAL A O   1 
ATOM   905  C CB  . VAL A 1 119 ? -15.07125 15.04488  55.82250  1.000 37.17533  ? 119 VAL A CB  1 
ATOM   906  C CG1 . VAL A 1 119 ? -14.16768 16.16396  56.33189  1.000 41.34899  ? 119 VAL A CG1 1 
ATOM   907  C CG2 . VAL A 1 119 ? -15.18091 13.92019  56.83739  1.000 31.57867  ? 119 VAL A CG2 1 
ATOM   908  N N   . ASN A 1 120 ? -17.61078 16.06218  57.51618  1.000 42.02078  ? 120 ASN A N   1 
ATOM   909  C CA  . ASN A 1 120 ? -17.98106 16.83305  58.69863  1.000 48.57298  ? 120 ASN A CA  1 
ATOM   910  C C   . ASN A 1 120 ? -17.19725 16.29777  59.88692  1.000 44.63457  ? 120 ASN A C   1 
ATOM   911  O O   . ASN A 1 120 ? -17.28120 15.10503  60.19817  1.000 41.39266  ? 120 ASN A O   1 
ATOM   912  C CB  . ASN A 1 120 ? -19.47880 16.73546  58.99019  1.000 62.08017  ? 120 ASN A CB  1 
ATOM   913  C CG  . ASN A 1 120 ? -20.31767 17.58484  58.06726  1.000 57.38343  ? 120 ASN A CG  1 
ATOM   914  O OD1 . ASN A 1 120 ? -19.83794 18.55033  57.46773  1.000 50.10165  ? 120 ASN A OD1 1 
ATOM   915  N ND2 . ASN A 1 120 ? -21.59105 17.22904  57.95379  1.000 74.40924  ? 120 ASN A ND2 1 
ATOM   916  N N   . ILE A 1 121 ? -16.44663 17.17139  60.55181  1.000 40.84490  ? 121 ILE A N   1 
ATOM   917  C CA  . ILE A 1 121 ? -15.72942 16.82003  61.77245  1.000 46.11780  ? 121 ILE A CA  1 
ATOM   918  C C   . ILE A 1 121 ? -16.18201 17.76673  62.87215  1.000 51.88024  ? 121 ILE A C   1 
ATOM   919  O O   . ILE A 1 121 ? -15.98781 18.98467  62.77023  1.000 50.85514  ? 121 ILE A O   1 
ATOM   920  C CB  . ILE A 1 121 ? -14.20787 16.88586  61.58918  1.000 47.95549  ? 121 ILE A CB  1 
ATOM   921  C CG1 . ILE A 1 121 ? -13.78971 16.08055  60.36158  1.000 43.17368  ? 121 ILE A CG1 1 
ATOM   922  C CG2 . ILE A 1 121 ? -13.50813 16.35972  62.83273  1.000 41.55166  ? 121 ILE A CG2 1 
ATOM   923  C CD1 . ILE A 1 121 ? -12.33841 16.23109  60.02945  1.000 31.34001  ? 121 ILE A CD1 1 
ATOM   924  N N   . THR A 1 122 ? -16.78234 17.20967  63.92007  1.000 50.73392  ? 122 THR A N   1 
ATOM   925  C CA  . THR A 1 122 ? -17.32153 17.98894  65.02456  1.000 52.99468  ? 122 THR A CA  1 
ATOM   926  C C   . THR A 1 122 ? -16.93259 17.33884  66.34402  1.000 43.69542  ? 122 THR A C   1 
ATOM   927  O O   . THR A 1 122 ? -17.02627 16.11683  66.49541  1.000 49.24256  ? 122 THR A O   1 
ATOM   928  C CB  . THR A 1 122 ? -18.85255 18.10902  64.92828  1.000 58.80671  ? 122 THR A CB  1 
ATOM   929  O OG1 . THR A 1 122 ? -19.42372 16.80656  64.75797  1.000 65.87009  ? 122 THR A OG1 1 
ATOM   930  C CG2 . THR A 1 122 ? -19.25424 18.99168  63.74611  1.000 49.53624  ? 122 THR A CG2 1 
ATOM   931  N N   . TRP A 1 123 ? -16.49373 18.16143  67.29346  1.000 36.55682  ? 123 TRP A N   1 
ATOM   932  C CA  . TRP A 1 123 ? -16.12620 17.69033  68.62153  1.000 48.83690  ? 123 TRP A CA  1 
ATOM   933  C C   . TRP A 1 123 ? -17.32297 17.74185  69.56333  1.000 51.00622  ? 123 TRP A C   1 
ATOM   934  O O   . TRP A 1 123 ? -18.10701 18.69489  69.54709  1.000 56.32802  ? 123 TRP A O   1 
ATOM   935  C CB  . TRP A 1 123 ? -14.98477 18.52914  69.19691  1.000 44.99333  ? 123 TRP A CB  1 
ATOM   936  C CG  . TRP A 1 123 ? -13.67060 18.32636  68.51590  1.000 46.96423  ? 123 TRP A CG  1 
ATOM   937  C CD1 . TRP A 1 123 ? -13.15583 19.06333  67.49006  1.000 47.20938  ? 123 TRP A CD1 1 
ATOM   938  C CD2 . TRP A 1 123 ? -12.69453 17.32144  68.81872  1.000 52.75741  ? 123 TRP A CD2 1 
ATOM   939  N NE1 . TRP A 1 123 ? -11.91884 18.57891  67.13502  1.000 51.71595  ? 123 TRP A NE1 1 
ATOM   940  C CE2 . TRP A 1 123 ? -11.61297 17.51039  67.93612  1.000 44.49620  ? 123 TRP A CE2 1 
ATOM   941  C CE3 . TRP A 1 123 ? -12.63244 16.27911  69.74833  1.000 46.93304  ? 123 TRP A CE3 1 
ATOM   942  C CZ2 . TRP A 1 123 ? -10.48182 16.69977  67.95814  1.000 33.29424  ? 123 TRP A CZ2 1 
ATOM   943  C CZ3 . TRP A 1 123 ? -11.51102 15.47325  69.76570  1.000 45.56702  ? 123 TRP A CZ3 1 
ATOM   944  C CH2 . TRP A 1 123 ? -10.45023 15.68818  68.87669  1.000 44.00057  ? 123 TRP A CH2 1 
ATOM   945  N N   . LEU A 1 124 ? -17.45064 16.71382  70.39267  1.000 43.69132  ? 124 LEU A N   1 
ATOM   946  C CA  . LEU A 1 124 ? -18.50993 16.62855  71.38494  1.000 48.39263  ? 124 LEU A CA  1 
ATOM   947  C C   . LEU A 1 124 ? -17.90868 16.49981  72.77651  1.000 58.60912  ? 124 LEU A C   1 
ATOM   948  O O   . LEU A 1 124 ? -16.88383 15.83533  72.96336  1.000 50.08803  ? 124 LEU A O   1 
ATOM   949  C CB  . LEU A 1 124 ? -19.42525 15.43739  71.11263  1.000 39.84054  ? 124 LEU A CB  1 
ATOM   950  C CG  . LEU A 1 124 ? -20.12523 15.46394  69.75800  1.000 56.67063  ? 124 LEU A CG  1 
ATOM   951  C CD1 . LEU A 1 124 ? -20.79037 14.12785  69.48963  1.000 48.92890  ? 124 LEU A CD1 1 
ATOM   952  C CD2 . LEU A 1 124 ? -21.13514 16.59892  69.71510  1.000 45.46967  ? 124 LEU A CD2 1 
ATOM   953  N N   . SER A 1 125 ? -18.55125 17.14206  73.74933  1.000 58.35227  ? 125 SER A N   1 
ATOM   954  C CA  . SER A 1 125 ? -18.23525 16.96156  75.16248  1.000 62.17849  ? 125 SER A CA  1 
ATOM   955  C C   . SER A 1 125 ? -19.54922 16.77992  75.90233  1.000 66.17437  ? 125 SER A C   1 
ATOM   956  O O   . SER A 1 125 ? -20.36266 17.70959  75.96414  1.000 58.53307  ? 125 SER A O   1 
ATOM   957  C CB  . SER A 1 125 ? -17.45282 18.14530  75.72720  1.000 61.15727  ? 125 SER A CB  1 
ATOM   958  O OG  . SER A 1 125 ? -17.14092 17.93414  77.09491  1.000 62.05562  ? 125 SER A OG  1 
ATOM   959  N N   . ASN A 1 126 ? -19.75251 15.58498  76.45531  1.000 62.90531  ? 126 ASN A N   1 
ATOM   960  C CA  . ASN A 1 126 ? -20.99937 15.24504  77.13650  1.000 81.75884  ? 126 ASN A CA  1 
ATOM   961  C C   . ASN A 1 126 ? -22.20322 15.54109  76.24547  1.000 88.88384  ? 126 ASN A C   1 
ATOM   962  O O   . ASN A 1 126 ? -23.20638 16.11393  76.67861  1.000 97.86041  ? 126 ASN A O   1 
ATOM   963  C CB  . ASN A 1 126 ? -21.11184 15.97827  78.47361  1.000 75.46846  ? 126 ASN A CB  1 
ATOM   964  N N   . GLY A 1 127 ? -22.09688 15.15042  74.97627  1.000 72.73422  ? 127 GLY A N   1 
ATOM   965  C CA  . GLY A 1 127 ? -23.14406 15.39075  74.00836  1.000 67.00981  ? 127 GLY A CA  1 
ATOM   966  C C   . GLY A 1 127 ? -23.22056 16.80470  73.47334  1.000 72.60917  ? 127 GLY A C   1 
ATOM   967  O O   . GLY A 1 127 ? -23.77456 17.00975  72.38422  1.000 75.57060  ? 127 GLY A O   1 
ATOM   968  N N   . HIS A 1 128 ? -22.68260 17.78879  74.19215  1.000 79.70639  ? 128 HIS A N   1 
ATOM   969  C CA  . HIS A 1 128 ? -22.70537 19.16724  73.72224  1.000 76.45383  ? 128 HIS A CA  1 
ATOM   970  C C   . HIS A 1 128 ? -21.63136 19.38639  72.66396  1.000 66.57775  ? 128 HIS A C   1 
ATOM   971  O O   . HIS A 1 128 ? -20.52982 18.83575  72.75048  1.000 55.74286  ? 128 HIS A O   1 
ATOM   972  C CB  . HIS A 1 128 ? -22.49117 20.14057  74.88250  1.000 67.73713  ? 128 HIS A CB  1 
ATOM   973  C CG  . HIS A 1 128 ? -23.60907 20.15544  75.87714  1.000 88.82029  ? 128 HIS A CG  1 
ATOM   974  N ND1 . HIS A 1 128 ? -24.10131 19.00817  76.46085  1.000 92.76154  ? 128 HIS A ND1 1 
ATOM   975  C CD2 . HIS A 1 128 ? -24.33184 21.17912  76.39135  1.000 87.46236  ? 128 HIS A CD2 1 
ATOM   976  C CE1 . HIS A 1 128 ? -25.07921 19.32385  77.29133  1.000 105.91349 ? 128 HIS A CE1 1 
ATOM   977  N NE2 . HIS A 1 128 ? -25.23881 20.63501  77.26824  1.000 105.92859 ? 128 HIS A NE2 1 
ATOM   978  N N   . SER A 1 129 ? -21.95666 20.19497  71.65962  1.000 57.56642  ? 129 SER A N   1 
ATOM   979  C CA  . SER A 1 129 ? -21.00353 20.49775  70.60245  1.000 55.87454  ? 129 SER A CA  1 
ATOM   980  C C   . SER A 1 129 ? -20.01824 21.55636  71.08577  1.000 67.34903  ? 129 SER A C   1 
ATOM   981  O O   . SER A 1 129 ? -20.42069 22.59219  71.62656  1.000 66.74032  ? 129 SER A O   1 
ATOM   982  C CB  . SER A 1 129 ? -21.73350 20.97330  69.34704  1.000 46.06470  ? 129 SER A CB  1 
ATOM   983  O OG  . SER A 1 129 ? -20.90609 20.84535  68.20594  1.000 79.60555  ? 129 SER A OG  1 
ATOM   984  N N   . VAL A 1 130 ? -18.72770 21.29588  70.88810  1.000 58.14961  ? 130 VAL A N   1 
ATOM   985  C CA  . VAL A 1 130 ? -17.66575 22.20034  71.31184  1.000 53.83526  ? 130 VAL A CA  1 
ATOM   986  C C   . VAL A 1 130 ? -17.14993 22.95755  70.09831  1.000 46.37939  ? 130 VAL A C   1 
ATOM   987  O O   . VAL A 1 130 ? -16.74460 22.34819  69.10174  1.000 62.63696  ? 130 VAL A O   1 
ATOM   988  C CB  . VAL A 1 130 ? -16.52428 21.43688  72.00216  1.000 57.51096  ? 130 VAL A CB  1 
ATOM   989  C CG1 . VAL A 1 130 ? -15.52042 22.41829  72.60041  1.000 51.81667  ? 130 VAL A CG1 1 
ATOM   990  C CG2 . VAL A 1 130 ? -17.07633 20.50786  73.06438  1.000 49.94491  ? 130 VAL A CG2 1 
ATOM   991  N N   . THR A 1 131 ? -17.14694 24.28102  70.18550  1.000 61.31012  ? 131 THR A N   1 
ATOM   992  C CA  . THR A 1 131 ? -16.69823 25.13373  69.09094  1.000 55.42334  ? 131 THR A CA  1 
ATOM   993  C C   . THR A 1 131 ? -15.45477 25.93948  69.42533  1.000 48.55990  ? 131 THR A C   1 
ATOM   994  O O   . THR A 1 131 ? -14.58003 26.09290  68.56935  1.000 55.68226  ? 131 THR A O   1 
ATOM   995  C CB  . THR A 1 131 ? -17.82450 26.08925  68.66890  1.000 66.76962  ? 131 THR A CB  1 
ATOM   996  O OG1 . THR A 1 131 ? -18.32496 26.78382  69.81880  1.000 68.57680  ? 131 THR A OG1 1 
ATOM   997  C CG2 . THR A 1 131 ? -18.96110 25.31567  68.01638  1.000 61.05828  ? 131 THR A CG2 1 
ATOM   998  N N   . GLU A 1 132 ? -15.34615 26.45444  70.64749  1.000 57.25397  ? 132 GLU A N   1 
ATOM   999  C CA  . GLU A 1 132 ? -14.16519 27.21254  71.03483  1.000 57.08682  ? 132 GLU A CA  1 
ATOM   1000 C C   . GLU A 1 132 ? -12.94626 26.29944  71.11651  1.000 55.23192  ? 132 GLU A C   1 
ATOM   1001 O O   . GLU A 1 132 ? -13.03002 25.16095  71.58627  1.000 56.94209  ? 132 GLU A O   1 
ATOM   1002 C CB  . GLU A 1 132 ? -14.39564 27.90782  72.37618  1.000 51.86343  ? 132 GLU A CB  1 
ATOM   1003 N N   . GLY A 1 133 ? -11.80749 26.80509  70.64794  1.000 47.45901  ? 133 GLY A N   1 
ATOM   1004 C CA  . GLY A 1 133 ? -10.58349 26.03033  70.67620  1.000 43.97457  ? 133 GLY A CA  1 
ATOM   1005 C C   . GLY A 1 133 ? -10.52217 24.89412  69.68162  1.000 47.34674  ? 133 GLY A C   1 
ATOM   1006 O O   . GLY A 1 133 ? -9.78662  23.93208  69.90415  1.000 48.71765  ? 133 GLY A O   1 
ATOM   1007 N N   . VAL A 1 134 ? -11.28026 24.97033  68.59141  1.000 40.40058  ? 134 VAL A N   1 
ATOM   1008 C CA  . VAL A 1 134 ? -11.30067 23.93827  67.56242  1.000 44.18762  ? 134 VAL A CA  1 
ATOM   1009 C C   . VAL A 1 134 ? -10.69860 24.51931  66.29435  1.000 45.14304  ? 134 VAL A C   1 
ATOM   1010 O O   . VAL A 1 134 ? -11.03845 25.63956  65.89532  1.000 50.51777  ? 134 VAL A O   1 
ATOM   1011 C CB  . VAL A 1 134 ? -12.72269 23.41588  67.29532  1.000 47.29164  ? 134 VAL A CB  1 
ATOM   1012 C CG1 . VAL A 1 134 ? -12.69650 22.38421  66.17597  1.000 38.75702  ? 134 VAL A CG1 1 
ATOM   1013 C CG2 . VAL A 1 134 ? -13.32084 22.82013  68.55817  1.000 42.11016  ? 134 VAL A CG2 1 
ATOM   1014 N N   . SER A 1 135 ? -9.79875  23.76328  65.67143  1.000 40.56647  ? 135 SER A N   1 
ATOM   1015 C CA  . SER A 1 135 ? -9.21197  24.14469  64.39786  1.000 36.27074  ? 135 SER A CA  1 
ATOM   1016 C C   . SER A 1 135 ? -8.97566  22.87435  63.59641  1.000 39.32261  ? 135 SER A C   1 
ATOM   1017 O O   . SER A 1 135 ? -9.10615  21.75957  64.11233  1.000 37.35347  ? 135 SER A O   1 
ATOM   1018 C CB  . SER A 1 135 ? -7.91465  24.93828  64.59117  1.000 33.51545  ? 135 SER A CB  1 
ATOM   1019 O OG  . SER A 1 135 ? -6.92661  24.16004  65.24766  1.000 38.43463  ? 135 SER A OG  1 
ATOM   1020 N N   . GLU A 1 136 ? -8.63388  23.04506  62.32118  1.000 36.41572  ? 136 GLU A N   1 
ATOM   1021 C CA  . GLU A 1 136 ? -8.38563  21.87645  61.49113  1.000 42.44979  ? 136 GLU A CA  1 
ATOM   1022 C C   . GLU A 1 136 ? -7.47539  22.24585  60.33070  1.000 35.68737  ? 136 GLU A C   1 
ATOM   1023 O O   . GLU A 1 136 ? -7.33472  23.41543  59.96499  1.000 35.31915  ? 136 GLU A O   1 
ATOM   1024 C CB  . GLU A 1 136 ? -9.69201  21.26484  60.97425  1.000 37.63412  ? 136 GLU A CB  1 
ATOM   1025 C CG  . GLU A 1 136 ? -10.35213 22.05076  59.85780  1.000 44.88433  ? 136 GLU A CG  1 
ATOM   1026 C CD  . GLU A 1 136 ? -11.62120 21.38630  59.35218  1.000 49.19119  ? 136 GLU A CD  1 
ATOM   1027 O OE1 . GLU A 1 136 ? -12.23705 20.60380  60.11000  1.000 52.37322  ? 136 GLU A OE1 1 
ATOM   1028 O OE2 . GLU A 1 136 ? -12.00166 21.64636  58.19335  1.000 46.73933  ? 136 GLU A OE2 1 
ATOM   1029 N N   . THR A 1 137 ? -6.84744  21.22044  59.77045  1.000 30.86473  ? 137 THR A N   1 
ATOM   1030 C CA  . THR A 1 137 ? -6.05933  21.35456  58.56311  1.000 37.06215  ? 137 THR A CA  1 
ATOM   1031 C C   . THR A 1 137 ? -6.97223  21.39037  57.34143  1.000 39.27577  ? 137 THR A C   1 
ATOM   1032 O O   . THR A 1 137 ? -8.17300  21.10814  57.41765  1.000 34.58855  ? 137 THR A O   1 
ATOM   1033 C CB  . THR A 1 137 ? -5.08164  20.18956  58.43269  1.000 33.43042  ? 137 THR A CB  1 
ATOM   1034 O OG1 . THR A 1 137 ? -5.81969  18.98110  58.20471  1.000 30.78734  ? 137 THR A OG1 1 
ATOM   1035 C CG2 . THR A 1 137 ? -4.26764  20.03786  59.69808  1.000 32.03802  ? 137 THR A CG2 1 
ATOM   1036 N N   . SER A 1 138 ? -6.38415  21.73954  56.19919  1.000 33.12706  ? 138 SER A N   1 
ATOM   1037 C CA  . SER A 1 138 ? -7.04693  21.52321  54.92311  1.000 28.64512  ? 138 SER A CA  1 
ATOM   1038 C C   . SER A 1 138 ? -7.09745  20.02840  54.61866  1.000 30.23519  ? 138 SER A C   1 
ATOM   1039 O O   . SER A 1 138 ? -6.65666  19.18458  55.40430  1.000 30.34135  ? 138 SER A O   1 
ATOM   1040 C CB  . SER A 1 138 ? -6.31341  22.25543  53.79708  1.000 26.66806  ? 138 SER A CB  1 
ATOM   1041 O OG  . SER A 1 138 ? -6.19737  23.64384  54.04830  1.000 41.11140  ? 138 SER A OG  1 
ATOM   1042 N N   . PHE A 1 139 ? -7.62399  19.69547  53.44755  1.000 29.68440  ? 139 PHE A N   1 
ATOM   1043 C CA  . PHE A 1 139 ? -7.49458  18.33562  52.94703  1.000 32.50845  ? 139 PHE A CA  1 
ATOM   1044 C C   . PHE A 1 139 ? -6.05728  18.11932  52.48640  1.000 26.48193  ? 139 PHE A C   1 
ATOM   1045 O O   . PHE A 1 139 ? -5.57876  18.80989  51.58056  1.000 34.00482  ? 139 PHE A O   1 
ATOM   1046 C CB  . PHE A 1 139 ? -8.48208  18.09132  51.80953  1.000 33.99537  ? 139 PHE A CB  1 
ATOM   1047 C CG  . PHE A 1 139 ? -9.90450  17.92676  52.26785  1.000 33.70078  ? 139 PHE A CG  1 
ATOM   1048 C CD1 . PHE A 1 139 ? -10.33009 16.73321  52.83081  1.000 29.56657  ? 139 PHE A CD1 1 
ATOM   1049 C CD2 . PHE A 1 139 ? -10.81546 18.96027  52.13458  1.000 34.12121  ? 139 PHE A CD2 1 
ATOM   1050 C CE1 . PHE A 1 139 ? -11.63563 16.57150  53.25138  1.000 36.78911  ? 139 PHE A CE1 1 
ATOM   1051 C CE2 . PHE A 1 139 ? -12.12512 18.80496  52.55253  1.000 34.70740  ? 139 PHE A CE2 1 
ATOM   1052 C CZ  . PHE A 1 139 ? -12.53560 17.60880  53.11073  1.000 29.63844  ? 139 PHE A CZ  1 
ATOM   1053 N N   . LEU A 1 140 ? -5.36089  17.18858  53.13392  1.000 25.98436  ? 140 LEU A N   1 
ATOM   1054 C CA  . LEU A 1 140 ? -3.97526  16.87659  52.82172  1.000 23.51848  ? 140 LEU A CA  1 
ATOM   1055 C C   . LEU A 1 140 ? -3.92190  15.63824  51.93581  1.000 30.28564  ? 140 LEU A C   1 
ATOM   1056 O O   . LEU A 1 140 ? -4.62281  14.65250  52.18604  1.000 27.44389  ? 140 LEU A O   1 
ATOM   1057 C CB  . LEU A 1 140 ? -3.16071  16.65834  54.10145  1.000 27.95405  ? 140 LEU A CB  1 
ATOM   1058 C CG  . LEU A 1 140 ? -3.23243  17.79205  55.13968  1.000 32.69102  ? 140 LEU A CG  1 
ATOM   1059 C CD1 . LEU A 1 140 ? -2.35648  17.51139  56.34699  1.000 40.75153  ? 140 LEU A CD1 1 
ATOM   1060 C CD2 . LEU A 1 140 ? -2.86121  19.13687  54.53617  1.000 36.13422  ? 140 LEU A CD2 1 
ATOM   1061 N N   . SER A 1 141 ? -3.08354  15.69773  50.90130  1.000 28.24701  ? 141 SER A N   1 
ATOM   1062 C CA  . SER A 1 141 ? -3.07320  14.69862  49.84374  1.000 24.90173  ? 141 SER A CA  1 
ATOM   1063 C C   . SER A 1 141 ? -2.39065  13.41028  50.29102  1.000 27.75734  ? 141 SER A C   1 
ATOM   1064 O O   . SER A 1 141 ? -1.54840  13.39340  51.19152  1.000 29.72077  ? 141 SER A O   1 
ATOM   1065 C CB  . SER A 1 141 ? -2.36035  15.23294  48.60328  1.000 31.11810  ? 141 SER A CB  1 
ATOM   1066 O OG  . SER A 1 141 ? -0.95804  15.24853  48.81103  1.000 28.77042  ? 141 SER A OG  1 
ATOM   1067 N N   . LYS A 1 142 ? -2.77025  12.31989  49.63135  1.000 23.76712  ? 142 LYS A N   1 
ATOM   1068 C CA  . LYS A 1 142 ? -2.12247  11.02948  49.78272  1.000 31.91951  ? 142 LYS A CA  1 
ATOM   1069 C C   . LYS A 1 142 ? -1.78035  10.49413  48.39945  1.000 28.94977  ? 142 LYS A C   1 
ATOM   1070 O O   . LYS A 1 142 ? -2.41780  10.84363  47.40200  1.000 38.11545  ? 142 LYS A O   1 
ATOM   1071 C CB  . LYS A 1 142 ? -3.00931  10.03868  50.54694  1.000 25.25865  ? 142 LYS A CB  1 
ATOM   1072 C CG  . LYS A 1 142 ? -3.59020  10.61749  51.82283  1.000 24.98855  ? 142 LYS A CG  1 
ATOM   1073 C CD  . LYS A 1 142 ? -3.58848  9.59864   52.94074  1.000 37.53172  ? 142 LYS A CD  1 
ATOM   1074 C CE  . LYS A 1 142 ? -4.33691  8.34409   52.56104  1.000 30.36945  ? 142 LYS A CE  1 
ATOM   1075 N NZ  . LYS A 1 142 ? -4.02119  7.24943   53.51283  1.000 38.99576  ? 142 LYS A NZ  1 
ATOM   1076 N N   . SER A 1 143 ? -0.75563  9.64036   48.34646  1.000 28.13283  ? 143 SER A N   1 
ATOM   1077 C CA  . SER A 1 143 ? -0.24703  9.17128   47.06323  1.000 25.53872  ? 143 SER A CA  1 
ATOM   1078 C C   . SER A 1 143 ? -1.23788  8.27501   46.33162  1.000 32.87131  ? 143 SER A C   1 
ATOM   1079 O O   . SER A 1 143 ? -1.08460  8.06659   45.12256  1.000 28.40329  ? 143 SER A O   1 
ATOM   1080 C CB  . SER A 1 143 ? 1.07512   8.43024   47.25439  1.000 26.80192  ? 143 SER A CB  1 
ATOM   1081 O OG  . SER A 1 143 ? 0.85942   7.16050   47.84338  1.000 38.83666  ? 143 SER A OG  1 
ATOM   1082 N N   . ASP A 1 144 ? -2.23664  7.73197   47.02526  1.000 26.60129  ? 144 ASP A N   1 
ATOM   1083 C CA  . ASP A 1 144 ? -3.31199  7.01325   46.35897  1.000 21.47983  ? 144 ASP A CA  1 
ATOM   1084 C C   . ASP A 1 144 ? -4.47277  7.92829   45.98620  1.000 24.62692  ? 144 ASP A C   1 
ATOM   1085 O O   . ASP A 1 144 ? -5.53150  7.43548   45.58214  1.000 32.71056  ? 144 ASP A O   1 
ATOM   1086 C CB  . ASP A 1 144 ? -3.79913  5.84492   47.22707  1.000 21.93684  ? 144 ASP A CB  1 
ATOM   1087 C CG  . ASP A 1 144 ? -4.52941  6.29374   48.48609  1.000 28.93677  ? 144 ASP A CG  1 
ATOM   1088 O OD1 . ASP A 1 144 ? -4.60003  7.51082   48.76881  1.000 38.32857  ? 144 ASP A OD1 1 
ATOM   1089 O OD2 . ASP A 1 144 ? -5.04094  5.40949   49.20424  1.000 35.25299  ? 144 ASP A OD2 1 
ATOM   1090 N N   . HIS A 1 145 ? -4.29645  9.24252   46.14323  1.000 24.92596  ? 145 HIS A N   1 
ATOM   1091 C CA  . HIS A 1 145 ? -5.20621  10.30067  45.70162  1.000 31.89330  ? 145 HIS A CA  1 
ATOM   1092 C C   . HIS A 1 145 ? -6.45632  10.42724  46.56328  1.000 32.24612  ? 145 HIS A C   1 
ATOM   1093 O O   . HIS A 1 145 ? -7.34224  11.22770  46.23799  1.000 36.54843  ? 145 HIS A O   1 
ATOM   1094 C CB  . HIS A 1 145 ? -5.58729  10.13195  44.22678  1.000 23.93845  ? 145 HIS A CB  1 
ATOM   1095 C CG  . HIS A 1 145 ? -4.40871  9.85845   43.34582  1.000 31.70831  ? 145 HIS A CG  1 
ATOM   1096 N ND1 . HIS A 1 145 ? -3.20833  10.52220  43.48863  1.000 25.60804  ? 145 HIS A ND1 1 
ATOM   1097 C CD2 . HIS A 1 145 ? -4.22684  8.96246   42.34707  1.000 28.80379  ? 145 HIS A CD2 1 
ATOM   1098 C CE1 . HIS A 1 145 ? -2.34517  10.06296  42.59999  1.000 30.99640  ? 145 HIS A CE1 1 
ATOM   1099 N NE2 . HIS A 1 145 ? -2.93857  9.11733   41.89341  1.000 36.78916  ? 145 HIS A NE2 1 
ATOM   1100 N N   . SER A 1 146 ? -6.55100  9.67867   47.65924  1.000 28.71921  ? 146 SER A N   1 
ATOM   1101 C CA  . SER A 1 146 ? -7.49789  10.00875  48.71175  1.000 32.54809  ? 146 SER A CA  1 
ATOM   1102 C C   . SER A 1 146 ? -6.90318  11.12523  49.56862  1.000 29.60672  ? 146 SER A C   1 
ATOM   1103 O O   . SER A 1 146 ? -5.80815  11.62281  49.29965  1.000 26.31474  ? 146 SER A O   1 
ATOM   1104 C CB  . SER A 1 146 ? -7.83517  8.77024   49.54315  1.000 29.47643  ? 146 SER A CB  1 
ATOM   1105 O OG  . SER A 1 146 ? -6.70363  8.32868   50.27947  1.000 38.64964  ? 146 SER A OG  1 
ATOM   1106 N N   . PHE A 1 147 ? -7.61954  11.52635  50.61850  1.000 24.72342  ? 147 PHE A N   1 
ATOM   1107 C CA  . PHE A 1 147 ? -7.18634  12.62517  51.47020  1.000 22.58664  ? 147 PHE A CA  1 
ATOM   1108 C C   . PHE A 1 147 ? -7.24256  12.22014  52.93516  1.000 31.37413  ? 147 PHE A C   1 
ATOM   1109 O O   . PHE A 1 147 ? -7.86742  11.22243  53.30901  1.000 25.89834  ? 147 PHE A O   1 
ATOM   1110 C CB  . PHE A 1 147 ? -8.04375  13.88263  51.26087  1.000 24.06431  ? 147 PHE A CB  1 
ATOM   1111 C CG  . PHE A 1 147 ? -7.91413  14.47472  49.89251  1.000 30.12124  ? 147 PHE A CG  1 
ATOM   1112 C CD1 . PHE A 1 147 ? -8.66774  13.98116  48.83476  1.000 29.70089  ? 147 PHE A CD1 1 
ATOM   1113 C CD2 . PHE A 1 147 ? -7.03013  15.51653  49.65782  1.000 28.13784  ? 147 PHE A CD2 1 
ATOM   1114 C CE1 . PHE A 1 147 ? -8.53818  14.51546  47.55810  1.000 31.58680  ? 147 PHE A CE1 1 
ATOM   1115 C CE2 . PHE A 1 147 ? -6.89593  16.05879  48.38670  1.000 33.01692  ? 147 PHE A CE2 1 
ATOM   1116 C CZ  . PHE A 1 147 ? -7.65266  15.55684  47.33307  1.000 26.38608  ? 147 PHE A CZ  1 
ATOM   1117 N N   . PHE A 1 148 ? -6.55999  13.00621  53.76577  1.000 26.49582  ? 148 PHE A N   1 
ATOM   1118 C CA  . PHE A 1 148 ? -6.77779  12.96592  55.20212  1.000 31.32451  ? 148 PHE A CA  1 
ATOM   1119 C C   . PHE A 1 148 ? -6.92408  14.38836  55.71891  1.000 33.03896  ? 148 PHE A C   1 
ATOM   1120 O O   . PHE A 1 148 ? -6.60528  15.36287  55.03115  1.000 26.79523  ? 148 PHE A O   1 
ATOM   1121 C CB  . PHE A 1 148 ? -5.66455  12.20792  55.95836  1.000 30.74202  ? 148 PHE A CB  1 
ATOM   1122 C CG  . PHE A 1 148 ? -4.31479  12.87756  55.94148  1.000 24.48462  ? 148 PHE A CG  1 
ATOM   1123 C CD1 . PHE A 1 148 ? -3.45947  12.72441  54.86005  1.000 31.52262  ? 148 PHE A CD1 1 
ATOM   1124 C CD2 . PHE A 1 148 ? -3.87332  13.59813  57.03905  1.000 26.67330  ? 148 PHE A CD2 1 
ATOM   1125 C CE1 . PHE A 1 148 ? -2.20287  13.31118  54.85789  1.000 28.54109  ? 148 PHE A CE1 1 
ATOM   1126 C CE2 . PHE A 1 148 ? -2.61985  14.18756  57.04814  1.000 29.05790  ? 148 PHE A CE2 1 
ATOM   1127 C CZ  . PHE A 1 148 ? -1.78176  14.04608  55.95543  1.000 32.01943  ? 148 PHE A CZ  1 
ATOM   1128 N N   . LYS A 1 149 ? -7.45298  14.49326  56.93230  1.000 31.30647  ? 149 LYS A N   1 
ATOM   1129 C CA  . LYS A 1 149 ? -7.74400  15.78340  57.53498  1.000 29.74352  ? 149 LYS A CA  1 
ATOM   1130 C C   . LYS A 1 149 ? -7.68347  15.61278  59.04013  1.000 36.08702  ? 149 LYS A C   1 
ATOM   1131 O O   . LYS A 1 149 ? -8.13269  14.59434  59.57596  1.000 36.14554  ? 149 LYS A O   1 
ATOM   1132 C CB  . LYS A 1 149 ? -9.11987  16.32021  57.10684  1.000 32.20910  ? 149 LYS A CB  1 
ATOM   1133 C CG  . LYS A 1 149 ? -9.43555  17.72385  57.62611  1.000 35.82985  ? 149 LYS A CG  1 
ATOM   1134 C CD  . LYS A 1 149 ? -10.88281 18.10938  57.34812  1.000 36.01993  ? 149 LYS A CD  1 
ATOM   1135 C CE  . LYS A 1 149 ? -11.02619 18.94221  56.08357  1.000 34.61192  ? 149 LYS A CE  1 
ATOM   1136 N NZ  . LYS A 1 149 ? -10.78280 20.38549  56.34372  1.000 39.38465  ? 149 LYS A NZ  1 
ATOM   1137 N N   . ILE A 1 150 ? -7.12263  16.60985  59.71275  1.000 32.14462  ? 150 ILE A N   1 
ATOM   1138 C CA  . ILE A 1 150 ? -6.85719  16.54430  61.14122  1.000 33.75343  ? 150 ILE A CA  1 
ATOM   1139 C C   . ILE A 1 150 ? -7.54493  17.72175  61.81041  1.000 35.29947  ? 150 ILE A C   1 
ATOM   1140 O O   . ILE A 1 150 ? -7.34528  18.87262  61.40818  1.000 29.18617  ? 150 ILE A O   1 
ATOM   1141 C CB  . ILE A 1 150 ? -5.34631  16.54753  61.42734  1.000 24.66426  ? 150 ILE A CB  1 
ATOM   1142 C CG1 . ILE A 1 150 ? -4.70930  15.26775  60.87712  1.000 23.93875  ? 150 ILE A CG1 1 
ATOM   1143 C CG2 . ILE A 1 150 ? -5.08418  16.70632  62.91503  1.000 30.34694  ? 150 ILE A CG2 1 
ATOM   1144 C CD1 . ILE A 1 150 ? -3.20161  15.29600  60.86139  1.000 26.67027  ? 150 ILE A CD1 1 
ATOM   1145 N N   . SER A 1 151 ? -8.36185  17.43269  62.81696  1.000 27.86190  ? 151 SER A N   1 
ATOM   1146 C CA  . SER A 1 151 ? -9.00449  18.45966  63.61832  1.000 40.71116  ? 151 SER A CA  1 
ATOM   1147 C C   . SER A 1 151 ? -8.38451  18.47963  65.00833  1.000 36.18740  ? 151 SER A C   1 
ATOM   1148 O O   . SER A 1 151 ? -7.97689  17.44381  65.54107  1.000 36.66369  ? 151 SER A O   1 
ATOM   1149 C CB  . SER A 1 151 ? -10.51415 18.22786  63.72217  1.000 35.01069  ? 151 SER A CB  1 
ATOM   1150 O OG  . SER A 1 151 ? -11.14326 19.30276  64.39643  1.000 41.30519  ? 151 SER A OG  1 
ATOM   1151 N N   . TYR A 1 152 ? -8.31285  19.67184  65.58857  1.000 32.47127  ? 152 TYR A N   1 
ATOM   1152 C CA  . TYR A 1 152 ? -7.69645  19.87327  66.88815  1.000 34.58324  ? 152 TYR A CA  1 
ATOM   1153 C C   . TYR A 1 152 ? -8.70675  20.46597  67.85885  1.000 44.40911  ? 152 TYR A C   1 
ATOM   1154 O O   . TYR A 1 152 ? -9.61586  21.20322  67.46610  1.000 43.15152  ? 152 TYR A O   1 
ATOM   1155 C CB  . TYR A 1 152 ? -6.47977  20.80089  66.79043  1.000 40.28825  ? 152 TYR A CB  1 
ATOM   1156 C CG  . TYR A 1 152 ? -5.46906  20.38135  65.75350  1.000 44.62161  ? 152 TYR A CG  1 
ATOM   1157 C CD1 . TYR A 1 152 ? -5.54957  20.85186  64.44876  1.000 35.39913  ? 152 TYR A CD1 1 
ATOM   1158 C CD2 . TYR A 1 152 ? -4.43306  19.51378  66.07783  1.000 38.61317  ? 152 TYR A CD2 1 
ATOM   1159 C CE1 . TYR A 1 152 ? -4.63173  20.46979  63.49974  1.000 28.80970  ? 152 TYR A CE1 1 
ATOM   1160 C CE2 . TYR A 1 152 ? -3.50817  19.12600  65.13473  1.000 31.11387  ? 152 TYR A CE2 1 
ATOM   1161 C CZ  . TYR A 1 152 ? -3.61061  19.60732  63.84947  1.000 32.96113  ? 152 TYR A CZ  1 
ATOM   1162 O OH  . TYR A 1 152 ? -2.69135  19.22267  62.91089  1.000 29.47508  ? 152 TYR A OH  1 
ATOM   1163 N N   . LEU A 1 153 ? -8.53219  20.13733  69.13581  1.000 46.91314  ? 153 LEU A N   1 
ATOM   1164 C CA  . LEU A 1 153 ? -9.34834  20.69367  70.21395  1.000 38.67752  ? 153 LEU A CA  1 
ATOM   1165 C C   . LEU A 1 153 ? -8.42794  20.93316  71.40571  1.000 43.32102  ? 153 LEU A C   1 
ATOM   1166 O O   . LEU A 1 153 ? -8.03082  19.98294  72.08866  1.000 37.42960  ? 153 LEU A O   1 
ATOM   1167 C CB  . LEU A 1 153 ? -10.49781 19.76558  70.58315  1.000 51.83330  ? 153 LEU A CB  1 
ATOM   1168 C CG  . LEU A 1 153 ? -11.22649 20.13375  71.87815  1.000 48.06663  ? 153 LEU A CG  1 
ATOM   1169 C CD1 . LEU A 1 153 ? -12.08876 21.36281  71.68124  1.000 44.61723  ? 153 LEU A CD1 1 
ATOM   1170 C CD2 . LEU A 1 153 ? -12.05490 18.96640  72.37958  1.000 53.79446  ? 153 LEU A CD2 1 
ATOM   1171 N N   . THR A 1 154 ? -8.06850  22.19441  71.63532  1.000 36.67582  ? 154 THR A N   1 
ATOM   1172 C CA  . THR A 1 154 ? -7.35871  22.53722  72.85702  1.000 46.81652  ? 154 THR A CA  1 
ATOM   1173 C C   . THR A 1 154 ? -8.28295  22.33714  74.04633  1.000 42.03429  ? 154 THR A C   1 
ATOM   1174 O O   . THR A 1 154 ? -9.49457  22.55302  73.96277  1.000 42.43953  ? 154 THR A O   1 
ATOM   1175 C CB  . THR A 1 154 ? -6.85754  23.98037  72.82123  1.000 41.43505  ? 154 THR A CB  1 
ATOM   1176 O OG1 . THR A 1 154 ? -7.95992  24.86688  72.59473  1.000 59.65858  ? 154 THR A OG1 1 
ATOM   1177 C CG2 . THR A 1 154 ? -5.82777  24.15741  71.71780  1.000 38.59451  ? 154 THR A CG2 1 
ATOM   1178 N N   . LEU A 1 155 ? -7.70754  21.89572  75.15632  1.000 48.47025  ? 155 LEU A N   1 
ATOM   1179 C CA  . LEU A 1 155 ? -8.52510  21.53868  76.30372  1.000 51.48997  ? 155 LEU A CA  1 
ATOM   1180 C C   . LEU A 1 155 ? -7.65988  21.51440  77.55106  1.000 55.44477  ? 155 LEU A C   1 
ATOM   1181 O O   . LEU A 1 155 ? -6.42730  21.50576  77.48672  1.000 51.70536  ? 155 LEU A O   1 
ATOM   1182 C CB  . LEU A 1 155 ? -9.20148  20.17847  76.11124  1.000 49.77225  ? 155 LEU A CB  1 
ATOM   1183 C CG  . LEU A 1 155 ? -8.33049  18.97379  76.47599  1.000 42.19393  ? 155 LEU A CG  1 
ATOM   1184 C CD1 . LEU A 1 155 ? -9.18104  17.73898  76.68301  1.000 52.56886  ? 155 LEU A CD1 1 
ATOM   1185 C CD2 . LEU A 1 155 ? -7.28236  18.71667  75.41229  1.000 41.81822  ? 155 LEU A CD2 1 
ATOM   1186 N N   . LEU A 1 156 ? -8.34005  21.50695  78.69322  1.000 63.03927  ? 156 LEU A N   1 
ATOM   1187 C CA  . LEU A 1 156 ? -7.74172  21.20975  79.98738  1.000 44.29918  ? 156 LEU A CA  1 
ATOM   1188 C C   . LEU A 1 156 ? -8.32938  19.88549  80.45385  1.000 48.66592  ? 156 LEU A C   1 
ATOM   1189 O O   . LEU A 1 156 ? -9.48956  19.84430  80.89370  1.000 51.69210  ? 156 LEU A O   1 
ATOM   1190 C CB  . LEU A 1 156 ? -8.04134  22.32437  80.99218  1.000 45.62205  ? 156 LEU A CB  1 
ATOM   1191 C CG  . LEU A 1 156 ? -6.86707  22.84630  81.81507  1.000 58.29170  ? 156 LEU A CG  1 
ATOM   1192 C CD1 . LEU A 1 156 ? -5.72138  23.21409  80.90237  1.000 50.36484  ? 156 LEU A CD1 1 
ATOM   1193 C CD2 . LEU A 1 156 ? -7.29939  24.04777  82.63915  1.000 59.56917  ? 156 LEU A CD2 1 
ATOM   1194 N N   . PRO A 1 157 ? -7.59973  18.77605  80.34534  1.000 52.00481  ? 157 PRO A N   1 
ATOM   1195 C CA  . PRO A 1 157 ? -8.18810  17.47341  80.68303  1.000 61.29688  ? 157 PRO A CA  1 
ATOM   1196 C C   . PRO A 1 157 ? -8.55906  17.39240  82.15637  1.000 68.94108  ? 157 PRO A C   1 
ATOM   1197 O O   . PRO A 1 157 ? -7.73719  17.64701  83.04042  1.000 62.81067  ? 157 PRO A O   1 
ATOM   1198 C CB  . PRO A 1 157 ? -7.08131  16.47685  80.31639  1.000 50.76220  ? 157 PRO A CB  1 
ATOM   1199 C CG  . PRO A 1 157 ? -5.82913  17.27072  80.34256  1.000 51.35252  ? 157 PRO A CG  1 
ATOM   1200 C CD  . PRO A 1 157 ? -6.20678  18.64980  79.88851  1.000 53.79611  ? 157 PRO A CD  1 
ATOM   1201 N N   . SER A 1 158 ? -9.81675  17.04183  82.40892  1.000 60.76909  ? 158 SER A N   1 
ATOM   1202 C CA  . SER A 1 158 ? -10.35899 16.91620  83.75029  1.000 67.54134  ? 158 SER A CA  1 
ATOM   1203 C C   . SER A 1 158 ? -10.89839 15.50738  83.95677  1.000 67.86055  ? 158 SER A C   1 
ATOM   1204 O O   . SER A 1 158 ? -11.28607 14.82103  83.00610  1.000 63.71819  ? 158 SER A O   1 
ATOM   1205 C CB  . SER A 1 158 ? -11.46354 17.94763  83.99740  1.000 75.75817  ? 158 SER A CB  1 
ATOM   1206 O OG  . SER A 1 158 ? -11.01670 19.24520  83.64684  1.000 74.93840  ? 158 SER A OG  1 
ATOM   1207 N N   . ALA A 1 159 ? -10.92933 15.09239  85.22657  1.000 68.31410  ? 159 ALA A N   1 
ATOM   1208 C CA  . ALA A 1 159 ? -11.22312 13.70514  85.56893  1.000 56.85314  ? 159 ALA A CA  1 
ATOM   1209 C C   . ALA A 1 159 ? -12.63229 13.27989  85.17621  1.000 65.43269  ? 159 ALA A C   1 
ATOM   1210 O O   . ALA A 1 159 ? -12.86846 12.08334  84.97482  1.000 66.79521  ? 159 ALA A O   1 
ATOM   1211 C CB  . ALA A 1 159 ? -11.01549 13.48606  87.06760  1.000 69.19973  ? 159 ALA A CB  1 
ATOM   1212 N N   . GLU A 1 160 ? -13.56914 14.21951  85.05679  1.000 59.60221  ? 160 GLU A N   1 
ATOM   1213 C CA  . GLU A 1 160 ? -14.96287 13.91353  84.75298  1.000 63.92772  ? 160 GLU A CA  1 
ATOM   1214 C C   . GLU A 1 160 ? -15.43794 14.63514  83.49316  1.000 74.28304  ? 160 GLU A C   1 
ATOM   1215 O O   . GLU A 1 160 ? -16.58708 15.07480  83.40635  1.000 79.40959  ? 160 GLU A O   1 
ATOM   1216 C CB  . GLU A 1 160 ? -15.85765 14.26003  85.94044  1.000 64.04179  ? 160 GLU A CB  1 
ATOM   1217 N N   . GLU A 1 161 ? -14.55654 14.77278  82.49907  1.000 67.40915  ? 161 GLU A N   1 
ATOM   1218 C CA  . GLU A 1 161 ? -14.89903 15.41907  81.23152  1.000 62.15627  ? 161 GLU A CA  1 
ATOM   1219 C C   . GLU A 1 161 ? -14.26921 14.62544  80.09401  1.000 54.21166  ? 161 GLU A C   1 
ATOM   1220 O O   . GLU A 1 161 ? -13.04621 14.64774  79.92601  1.000 67.88497  ? 161 GLU A O   1 
ATOM   1221 C CB  . GLU A 1 161 ? -14.42999 16.87577  81.20373  1.000 62.23174  ? 161 GLU A CB  1 
ATOM   1222 C CG  . GLU A 1 161 ? -14.77658 17.65667  82.46578  1.000 77.44576  ? 161 GLU A CG  1 
ATOM   1223 C CD  . GLU A 1 161 ? -14.69942 19.15827  82.28462  1.000 86.85578  ? 161 GLU A CD  1 
ATOM   1224 O OE1 . GLU A 1 161 ? -14.38525 19.61297  81.16329  1.000 87.99176  ? 161 GLU A OE1 1 
ATOM   1225 O OE2 . GLU A 1 161 ? -14.96078 19.88373  83.26940  1.000 88.05798  ? 161 GLU A OE2 1 
ATOM   1226 N N   . SER A 1 162 ? -15.09835 13.93595  79.31321  1.000 55.28270  ? 162 SER A N   1 
ATOM   1227 C CA  . SER A 1 162 ? -14.66028 13.14328  78.17001  1.000 54.62322  ? 162 SER A CA  1 
ATOM   1228 C C   . SER A 1 162 ? -15.16418 13.75801  76.86731  1.000 49.98051  ? 162 SER A C   1 
ATOM   1229 O O   . SER A 1 162 ? -16.03454 14.63311  76.85720  1.000 49.86705  ? 162 SER A O   1 
ATOM   1230 C CB  . SER A 1 162 ? -15.14415 11.69531  78.29562  1.000 48.15753  ? 162 SER A CB  1 
ATOM   1231 O OG  . SER A 1 162 ? -16.55862 11.63840  78.29562  1.000 58.60725  ? 162 SER A OG  1 
ATOM   1232 N N   . TYR A 1 163 ? -14.60933 13.27710  75.75260  1.000 63.44388  ? 163 TYR A N   1 
ATOM   1233 C CA  . TYR A 1 163 ? -14.84326 13.88858  74.44957  1.000 48.43335  ? 163 TYR A CA  1 
ATOM   1234 C C   . TYR A 1 163 ? -15.05366 12.82396  73.37921  1.000 54.31087  ? 163 TYR A C   1 
ATOM   1235 O O   . TYR A 1 163 ? -14.62704 11.67355  73.51385  1.000 51.76008  ? 163 TYR A O   1 
ATOM   1236 C CB  . TYR A 1 163 ? -13.67979 14.80546  74.04689  1.000 41.15972  ? 163 TYR A CB  1 
ATOM   1237 C CG  . TYR A 1 163 ? -13.47555 15.96307  74.99144  1.000 48.83325  ? 163 TYR A CG  1 
ATOM   1238 C CD1 . TYR A 1 163 ? -12.69856 15.82362  76.13565  1.000 49.37301  ? 163 TYR A CD1 1 
ATOM   1239 C CD2 . TYR A 1 163 ? -14.06625 17.19484  74.74697  1.000 44.05936  ? 163 TYR A CD2 1 
ATOM   1240 C CE1 . TYR A 1 163 ? -12.51707 16.88075  77.01046  1.000 55.12717  ? 163 TYR A CE1 1 
ATOM   1241 C CE2 . TYR A 1 163 ? -13.88571 18.25859  75.61545  1.000 55.35735  ? 163 TYR A CE2 1 
ATOM   1242 C CZ  . TYR A 1 163 ? -13.11011 18.09598  76.74493  1.000 54.59781  ? 163 TYR A CZ  1 
ATOM   1243 O OH  . TYR A 1 163 ? -12.93024 19.14960  77.61218  1.000 79.03080  ? 163 TYR A OH  1 
ATOM   1244 N N   . ASP A 1 164 ? -15.71335 13.23825  72.29781  1.000 49.66787  ? 164 ASP A N   1 
ATOM   1245 C CA  . ASP A 1 164 ? -15.98513 12.38491  71.14724  1.000 49.33677  ? 164 ASP A CA  1 
ATOM   1246 C C   . ASP A 1 164 ? -15.69695 13.16218  69.87300  1.000 54.59523  ? 164 ASP A C   1 
ATOM   1247 O O   . ASP A 1 164 ? -16.15092 14.30051  69.72197  1.000 51.47114  ? 164 ASP A O   1 
ATOM   1248 C CB  . ASP A 1 164 ? -17.44346 11.90624  71.13261  1.000 53.93942  ? 164 ASP A CB  1 
ATOM   1249 C CG  . ASP A 1 164 ? -17.73380 10.86687  72.19728  1.000 69.21510  ? 164 ASP A CG  1 
ATOM   1250 O OD1 . ASP A 1 164 ? -17.30171 9.70586   72.02927  1.000 62.42061  ? 164 ASP A OD1 1 
ATOM   1251 O OD2 . ASP A 1 164 ? -18.39311 11.21500  73.20253  1.000 62.27669  ? 164 ASP A OD2 1 
ATOM   1252 N N   . CYS A 1 165 ? -14.94750 12.55437  68.96051  1.000 50.34561  ? 165 CYS A N   1 
ATOM   1253 C CA  . CYS A 1 165 ? -14.80136 13.09566  67.61817  1.000 47.37548  ? 165 CYS A CA  1 
ATOM   1254 C C   . CYS A 1 165 ? -15.90259 12.50249  66.75177  1.000 44.65248  ? 165 CYS A C   1 
ATOM   1255 O O   . CYS A 1 165 ? -15.99101 11.27832  66.61404  1.000 43.87059  ? 165 CYS A O   1 
ATOM   1256 C CB  . CYS A 1 165 ? -13.42673 12.78467  67.02783  1.000 44.81377  ? 165 CYS A CB  1 
ATOM   1257 S SG  . CYS A 1 165 ? -13.13611 13.67073  65.47950  1.000 60.17418  ? 165 CYS A SG  1 
ATOM   1258 N N   . LYS A 1 166 ? -16.74361 13.36537  66.18300  1.000 35.87904  ? 166 LYS A N   1 
ATOM   1259 C CA  . LYS A 1 166 ? -17.86695 12.95198  65.34905  1.000 54.76658  ? 166 LYS A CA  1 
ATOM   1260 C C   . LYS A 1 166 ? -17.54335 13.25151  63.89021  1.000 46.26395  ? 166 LYS A C   1 
ATOM   1261 O O   . LYS A 1 166 ? -17.26701 14.40351  63.53542  1.000 42.31302  ? 166 LYS A O   1 
ATOM   1262 C CB  . LYS A 1 166 ? -19.15195 13.66434  65.77158  1.000 44.00450  ? 166 LYS A CB  1 
ATOM   1263 C CG  . LYS A 1 166 ? -20.38843 13.19437  65.02826  1.000 41.85064  ? 166 LYS A CG  1 
ATOM   1264 C CD  . LYS A 1 166 ? -21.63907 13.91694  65.50770  1.000 58.89778  ? 166 LYS A CD  1 
ATOM   1265 C CE  . LYS A 1 166 ? -22.88073 13.42452  64.77528  1.000 69.17159  ? 166 LYS A CE  1 
ATOM   1266 N NZ  . LYS A 1 166 ? -24.08077 14.23513  65.11422  1.000 74.74464  ? 166 LYS A NZ  1 
ATOM   1267 N N   . VAL A 1 167 ? -17.58436 12.22157  63.04942  1.000 33.92268  ? 167 VAL A N   1 
ATOM   1268 C CA  . VAL A 1 167 ? -17.25087 12.34532  61.63612  1.000 47.97759  ? 167 VAL A CA  1 
ATOM   1269 C C   . VAL A 1 167 ? -18.43806 11.87329  60.80714  1.000 43.89730  ? 167 VAL A C   1 
ATOM   1270 O O   . VAL A 1 167 ? -19.02302 10.81911  61.08427  1.000 45.21660  ? 167 VAL A O   1 
ATOM   1271 C CB  . VAL A 1 167 ? -15.97815 11.55573  61.28333  1.000 46.02649  ? 167 VAL A CB  1 
ATOM   1272 C CG1 . VAL A 1 167 ? -14.77617 12.14278  62.01180  1.000 41.11879  ? 167 VAL A CG1 1 
ATOM   1273 C CG2 . VAL A 1 167 ? -16.14485 10.11474  61.66586  1.000 44.56721  ? 167 VAL A CG2 1 
ATOM   1274 N N   . GLU A 1 168 ? -18.79905 12.66139  59.80095  1.000 46.14907  ? 168 GLU A N   1 
ATOM   1275 C CA  . GLU A 1 168 ? -19.89511 12.34096  58.89853  1.000 53.01125  ? 168 GLU A CA  1 
ATOM   1276 C C   . GLU A 1 168 ? -19.34695 12.28606  57.48371  1.000 43.39731  ? 168 GLU A C   1 
ATOM   1277 O O   . GLU A 1 168 ? -18.69093 13.23193  57.03399  1.000 42.74706  ? 168 GLU A O   1 
ATOM   1278 C CB  . GLU A 1 168 ? -21.01798 13.37762  58.99498  1.000 55.79567  ? 168 GLU A CB  1 
ATOM   1279 C CG  . GLU A 1 168 ? -21.49046 13.66304  60.41415  1.000 63.34006  ? 168 GLU A CG  1 
ATOM   1280 C CD  . GLU A 1 168 ? -22.32701 14.92228  60.49535  1.000 64.34540  ? 168 GLU A CD  1 
ATOM   1281 O OE1 . GLU A 1 168 ? -23.35933 14.99507  59.79697  1.000 75.15800  ? 168 GLU A OE1 1 
ATOM   1282 O OE2 . GLU A 1 168 ? -21.94331 15.84697  61.24158  1.000 64.90170  ? 168 GLU A OE2 1 
ATOM   1283 N N   . HIS A 1 169 ? -19.61222 11.18349  56.78789  1.000 45.31871  ? 169 HIS A N   1 
ATOM   1284 C CA  . HIS A 1 169 ? -19.08459 10.99373  55.44537  1.000 50.60540  ? 169 HIS A CA  1 
ATOM   1285 C C   . HIS A 1 169 ? -19.99987 10.05585  54.67003  1.000 46.29544  ? 169 HIS A C   1 
ATOM   1286 O O   . HIS A 1 169 ? -20.52553 9.08906   55.22915  1.000 47.41766  ? 169 HIS A O   1 
ATOM   1287 C CB  . HIS A 1 169 ? -17.65505 10.43854  55.49214  1.000 45.66840  ? 169 HIS A CB  1 
ATOM   1288 C CG  . HIS A 1 169 ? -16.93959 10.50457  54.17998  1.000 41.11640  ? 169 HIS A CG  1 
ATOM   1289 N ND1 . HIS A 1 169 ? -17.02456 9.50547   53.23456  1.000 40.36649  ? 169 HIS A ND1 1 
ATOM   1290 C CD2 . HIS A 1 169 ? -16.12849 11.45279  53.65378  1.000 35.68698  ? 169 HIS A CD2 1 
ATOM   1291 C CE1 . HIS A 1 169 ? -16.29554 9.83476   52.18295  1.000 45.84192  ? 169 HIS A CE1 1 
ATOM   1292 N NE2 . HIS A 1 169 ? -15.74100 11.01168  52.41223  1.000 37.59062  ? 169 HIS A NE2 1 
ATOM   1293 N N   . TRP A 1 170 ? -20.17460 10.34540  53.37516  1.000 42.30689  ? 170 TRP A N   1 
ATOM   1294 C CA  . TRP A 1 170 ? -21.05499 9.53407   52.53508  1.000 46.29644  ? 170 TRP A CA  1 
ATOM   1295 C C   . TRP A 1 170 ? -20.63855 8.06691   52.51745  1.000 47.43153  ? 170 TRP A C   1 
ATOM   1296 O O   . TRP A 1 170 ? -21.48639 7.18463   52.34503  1.000 64.28676  ? 170 TRP A O   1 
ATOM   1297 C CB  . TRP A 1 170 ? -21.08444 10.09060  51.11073  1.000 39.07841  ? 170 TRP A CB  1 
ATOM   1298 C CG  . TRP A 1 170 ? -21.58988 11.49308  51.05191  1.000 42.13936  ? 170 TRP A CG  1 
ATOM   1299 C CD1 . TRP A 1 170 ? -22.50143 12.06739  51.88925  1.000 43.87704  ? 170 TRP A CD1 1 
ATOM   1300 C CD2 . TRP A 1 170 ? -21.19607 12.51424  50.12491  1.000 40.35163  ? 170 TRP A CD2 1 
ATOM   1301 N NE1 . TRP A 1 170 ? -22.70584 13.37832  51.53688  1.000 47.10782  ? 170 TRP A NE1 1 
ATOM   1302 C CE2 . TRP A 1 170 ? -21.91596 13.67807  50.45735  1.000 42.84510  ? 170 TRP A CE2 1 
ATOM   1303 C CE3 . TRP A 1 170 ? -20.30510 12.55717  49.04775  1.000 50.10111  ? 170 TRP A CE3 1 
ATOM   1304 C CZ2 . TRP A 1 170 ? -21.77324 14.87230  49.75151  1.000 49.45848  ? 170 TRP A CZ2 1 
ATOM   1305 C CZ3 . TRP A 1 170 ? -20.16661 13.74362  48.34593  1.000 48.26680  ? 170 TRP A CZ3 1 
ATOM   1306 C CH2 . TRP A 1 170 ? -20.89831 14.88429  48.70057  1.000 48.45814  ? 170 TRP A CH2 1 
ATOM   1307 N N   . GLY A 1 171 ? -19.35049 7.78059   52.69947  1.000 49.32363  ? 171 GLY A N   1 
ATOM   1308 C CA  . GLY A 1 171 ? -18.91204 6.39795   52.76995  1.000 43.44355  ? 171 GLY A CA  1 
ATOM   1309 C C   . GLY A 1 171 ? -19.23365 5.71210   54.08079  1.000 41.10787  ? 171 GLY A C   1 
ATOM   1310 O O   . GLY A 1 171 ? -18.96662 4.51232   54.21012  1.000 59.27338  ? 171 GLY A O   1 
ATOM   1311 N N   . LEU A 1 172 ? -19.78647 6.44070   55.04856  1.000 44.37735  ? 172 LEU A N   1 
ATOM   1312 C CA  . LEU A 1 172 ? -20.19366 5.87316   56.32317  1.000 58.33450  ? 172 LEU A CA  1 
ATOM   1313 C C   . LEU A 1 172 ? -21.69287 5.61418   56.32182  1.000 64.43692  ? 172 LEU A C   1 
ATOM   1314 O O   . LEU A 1 172 ? -22.47019 6.41913   55.80169  1.000 59.60397  ? 172 LEU A O   1 
ATOM   1315 C CB  . LEU A 1 172 ? -19.83599 6.80941   57.47485  1.000 50.79540  ? 172 LEU A CB  1 
ATOM   1316 C CG  . LEU A 1 172 ? -18.35781 7.04882   57.73524  1.000 36.39333  ? 172 LEU A CG  1 
ATOM   1317 C CD1 . LEU A 1 172 ? -18.18930 8.05002   58.86912  1.000 36.11533  ? 172 LEU A CD1 1 
ATOM   1318 C CD2 . LEU A 1 172 ? -17.68014 5.73278   58.06295  1.000 41.71212  ? 172 LEU A CD2 1 
ATOM   1319 N N   . ASP A 1 173 ? -22.09298 4.48533   56.91271  1.000 65.19113  ? 173 ASP A N   1 
ATOM   1320 C CA  . ASP A 1 173 ? -23.51551 4.19892   57.06657  1.000 58.14135  ? 173 ASP A CA  1 
ATOM   1321 C C   . ASP A 1 173 ? -24.15380 5.13106   58.08860  1.000 63.16241  ? 173 ASP A C   1 
ATOM   1322 O O   . ASP A 1 173 ? -25.25234 5.65375   57.86540  1.000 66.55936  ? 173 ASP A O   1 
ATOM   1323 C CB  . ASP A 1 173 ? -23.71568 2.73951   57.47300  1.000 60.56714  ? 173 ASP A CB  1 
ATOM   1324 C CG  . ASP A 1 173 ? -23.23041 1.76543   56.41533  1.000 77.55055  ? 173 ASP A CG  1 
ATOM   1325 O OD1 . ASP A 1 173 ? -23.27867 2.10857   55.21264  1.000 77.40177  ? 173 ASP A OD1 1 
ATOM   1326 O OD2 . ASP A 1 173 ? -22.80754 0.65170   56.79102  1.000 70.84757  ? 173 ASP A OD2 1 
ATOM   1327 N N   . LYS A 1 174 ? -23.48280 5.34801   59.20842  1.000 56.91771  ? 174 LYS A N   1 
ATOM   1328 C CA  . LYS A 1 174 ? -23.91809 6.25080   60.26004  1.000 61.61920  ? 174 LYS A CA  1 
ATOM   1329 C C   . LYS A 1 174 ? -22.73679 7.10887   60.67082  1.000 59.39917  ? 174 LYS A C   1 
ATOM   1330 O O   . LYS A 1 174 ? -21.58167 6.75047   60.41004  1.000 49.42953  ? 174 LYS A O   1 
ATOM   1331 C CB  . LYS A 1 174 ? -24.45531 5.47488   61.47294  1.000 54.37822  ? 174 LYS A CB  1 
ATOM   1332 N N   . PRO A 1 175 ? -22.98361 8.25978   61.29567  1.000 54.48108  ? 175 PRO A N   1 
ATOM   1333 C CA  . PRO A 1 175 ? -21.87242 9.04745   61.83563  1.000 43.12772  ? 175 PRO A CA  1 
ATOM   1334 C C   . PRO A 1 175 ? -21.02495 8.20143   62.77367  1.000 56.98375  ? 175 PRO A C   1 
ATOM   1335 O O   . PRO A 1 175 ? -21.54295 7.43827   63.59290  1.000 56.12746  ? 175 PRO A O   1 
ATOM   1336 C CB  . PRO A 1 175 ? -22.57450 10.19000  62.57466  1.000 51.56127  ? 175 PRO A CB  1 
ATOM   1337 C CG  . PRO A 1 175 ? -23.87258 10.33581  61.87998  1.000 50.55980  ? 175 PRO A CG  1 
ATOM   1338 C CD  . PRO A 1 175 ? -24.27669 8.94568   61.47244  1.000 59.82985  ? 175 PRO A CD  1 
ATOM   1339 N N   . LEU A 1 176 ? -19.71039 8.31804   62.62681  1.000 53.32968  ? 176 LEU A N   1 
ATOM   1340 C CA  . LEU A 1 176 ? -18.75997 7.57552   63.44064  1.000 55.33407  ? 176 LEU A CA  1 
ATOM   1341 C C   . LEU A 1 176 ? -18.29155 8.45159   64.59673  1.000 55.44524  ? 176 LEU A C   1 
ATOM   1342 O O   . LEU A 1 176 ? -17.94718 9.62234   64.39741  1.000 45.90789  ? 176 LEU A O   1 
ATOM   1343 C CB  . LEU A 1 176 ? -17.56912 7.11763   62.59833  1.000 45.45462  ? 176 LEU A CB  1 
ATOM   1344 C CG  . LEU A 1 176 ? -16.59861 6.11856   63.22648  1.000 61.21416  ? 176 LEU A CG  1 
ATOM   1345 C CD1 . LEU A 1 176 ? -16.94875 4.69514   62.82399  1.000 55.49067  ? 176 LEU A CD1 1 
ATOM   1346 C CD2 . LEU A 1 176 ? -15.17614 6.44377   62.83396  1.000 58.05604  ? 176 LEU A CD2 1 
ATOM   1347 N N   . LEU A 1 177 ? -18.29413 7.88867   65.80199  1.000 50.06661  ? 177 LEU A N   1 
ATOM   1348 C CA  . LEU A 1 177 ? -17.85303 8.58965   66.99990  1.000 53.29717  ? 177 LEU A CA  1 
ATOM   1349 C C   . LEU A 1 177 ? -16.62650 7.88969   67.56343  1.000 51.02983  ? 177 LEU A C   1 
ATOM   1350 O O   . LEU A 1 177 ? -16.62938 6.66637   67.74364  1.000 48.62779  ? 177 LEU A O   1 
ATOM   1351 C CB  . LEU A 1 177 ? -18.96228 8.65398   68.05642  1.000 48.04425  ? 177 LEU A CB  1 
ATOM   1352 C CG  . LEU A 1 177 ? -19.87076 9.88588   68.01775  1.000 55.00761  ? 177 LEU A CG  1 
ATOM   1353 C CD1 . LEU A 1 177 ? -20.70120 9.92541   66.74178  1.000 51.85226  ? 177 LEU A CD1 1 
ATOM   1354 C CD2 . LEU A 1 177 ? -20.76758 9.93691   69.24001  1.000 47.18286  ? 177 LEU A CD2 1 
ATOM   1355 N N   . LYS A 1 178 ? -15.57816 8.66339   67.82627  1.000 50.11818  ? 178 LYS A N   1 
ATOM   1356 C CA  . LYS A 1 178 ? -14.35462 8.15319   68.43389  1.000 53.48597  ? 178 LYS A CA  1 
ATOM   1357 C C   . LYS A 1 178 ? -14.19972 8.82812   69.78881  1.000 47.97146  ? 178 LYS A C   1 
ATOM   1358 O O   . LYS A 1 178 ? -14.00797 10.04664  69.86312  1.000 44.88841  ? 178 LYS A O   1 
ATOM   1359 C CB  . LYS A 1 178 ? -13.14328 8.40937   67.54122  1.000 55.13143  ? 178 LYS A CB  1 
ATOM   1360 C CG  . LYS A 1 178 ? -12.24408 7.19852   67.37540  1.000 44.45621  ? 178 LYS A CG  1 
ATOM   1361 C CD  . LYS A 1 178 ? -13.00064 6.03807   66.74744  1.000 44.93006  ? 178 LYS A CD  1 
ATOM   1362 C CE  . LYS A 1 178 ? -12.06614 4.87724   66.43501  1.000 55.71973  ? 178 LYS A CE  1 
ATOM   1363 N NZ  . LYS A 1 178 ? -12.75251 3.80259   65.66442  1.000 56.15754  ? 178 LYS A NZ  1 
ATOM   1364 N N   . HIS A 1 179 ? -14.29104 8.03832   70.85137  1.000 47.33438  ? 179 HIS A N   1 
ATOM   1365 C CA  . HIS A 1 179 ? -14.27987 8.55229   72.21099  1.000 49.18965  ? 179 HIS A CA  1 
ATOM   1366 C C   . HIS A 1 179 ? -12.85238 8.71150   72.71579  1.000 41.60293  ? 179 HIS A C   1 
ATOM   1367 O O   . HIS A 1 179 ? -11.94026 7.99201   72.30117  1.000 48.69464  ? 179 HIS A O   1 
ATOM   1368 C CB  . HIS A 1 179 ? -15.06354 7.61779   73.13718  1.000 47.06534  ? 179 HIS A CB  1 
ATOM   1369 C CG  . HIS A 1 179 ? -15.27462 8.16327   74.51367  1.000 54.71414  ? 179 HIS A CG  1 
ATOM   1370 N ND1 . HIS A 1 179 ? -14.51627 7.76850   75.59481  1.000 65.73825  ? 179 HIS A ND1 1 
ATOM   1371 C CD2 . HIS A 1 179 ? -16.15945 9.07151   74.98629  1.000 56.12262  ? 179 HIS A CD2 1 
ATOM   1372 C CE1 . HIS A 1 179 ? -14.92316 8.41230   76.67398  1.000 69.75912  ? 179 HIS A CE1 1 
ATOM   1373 N NE2 . HIS A 1 179 ? -15.91926 9.20896   76.33168  1.000 62.52573  ? 179 HIS A NE2 1 
ATOM   1374 N N   . TRP A 1 180 ? -12.66793 9.67274   73.61782  1.000 55.53818  ? 180 TRP A N   1 
ATOM   1375 C CA  . TRP A 1 180 ? -11.39336 9.88712   74.29054  1.000 49.63879  ? 180 TRP A CA  1 
ATOM   1376 C C   . TRP A 1 180 ? -11.65778 10.22904  75.74919  1.000 58.87099  ? 180 TRP A C   1 
ATOM   1377 O O   . TRP A 1 180 ? -12.44832 11.13096  76.04232  1.000 58.37439  ? 180 TRP A O   1 
ATOM   1378 C CB  . TRP A 1 180 ? -10.59005 11.00847  73.61822  1.000 47.62743  ? 180 TRP A CB  1 
ATOM   1379 C CG  . TRP A 1 180 ? -9.26881  11.29536  74.27894  1.000 49.57882  ? 180 TRP A CG  1 
ATOM   1380 C CD1 . TRP A 1 180 ? -8.05295  10.77656  73.93873  1.000 37.15657  ? 180 TRP A CD1 1 
ATOM   1381 C CD2 . TRP A 1 180 ? -9.03265  12.17120  75.39012  1.000 49.55670  ? 180 TRP A CD2 1 
ATOM   1382 N NE1 . TRP A 1 180 ? -7.07817  11.27206  74.76726  1.000 38.19987  ? 180 TRP A NE1 1 
ATOM   1383 C CE2 . TRP A 1 180 ? -7.65264  12.13081  75.66668  1.000 46.31845  ? 180 TRP A CE2 1 
ATOM   1384 C CE3 . TRP A 1 180 ? -9.85420  12.98290  76.17764  1.000 50.18568  ? 180 TRP A CE3 1 
ATOM   1385 C CZ2 . TRP A 1 180 ? -7.07667  12.86971  76.69565  1.000 40.95863  ? 180 TRP A CZ2 1 
ATOM   1386 C CZ3 . TRP A 1 180 ? -9.27994  13.71662  77.19614  1.000 49.25893  ? 180 TRP A CZ3 1 
ATOM   1387 C CH2 . TRP A 1 180 ? -7.90610  13.65419  77.44817  1.000 44.36594  ? 180 TRP A CH2 1 
ATOM   1388 N N   . GLU A 1 181 ? -11.00034 9.50909   76.65808  1.000 61.75466  ? 181 GLU A N   1 
ATOM   1389 C CA  . GLU A 1 181 ? -11.09248 9.78038   78.08452  1.000 58.33643  ? 181 GLU A CA  1 
ATOM   1390 C C   . GLU A 1 181 ? -9.69317  9.92993   78.66556  1.000 60.72076  ? 181 GLU A C   1 
ATOM   1391 O O   . GLU A 1 181 ? -8.75187  9.27560   78.19842  1.000 54.57922  ? 181 GLU A O   1 
ATOM   1392 C CB  . GLU A 1 181 ? -11.84524 8.66100   78.82379  1.000 51.34091  ? 181 GLU A CB  1 
ATOM   1393 N N   . PRO A 1 182 ? -9.51530  10.80247  79.66888  1.000 69.00086  ? 182 PRO A N   1 
ATOM   1394 C CA  . PRO A 1 182 ? -8.22061  10.93205  80.34666  1.000 65.27587  ? 182 PRO A CA  1 
ATOM   1395 C C   . PRO A 1 182 ? -8.03463  9.89114   81.44643  1.000 50.83819  ? 182 PRO A C   1 
ATOM   1396 O O   . PRO A 1 182 ? -7.54912  8.79615   81.15874  1.000 66.08867  ? 182 PRO A O   1 
ATOM   1397 C CB  . PRO A 1 182 ? -8.27513  12.34333  80.93267  1.000 59.05024  ? 182 PRO A CB  1 
ATOM   1398 C CG  . PRO A 1 182 ? -9.72987  12.58023  81.17753  1.000 64.25856  ? 182 PRO A CG  1 
ATOM   1399 C CD  . PRO A 1 182 ? -10.47313 11.83968  80.09477  1.000 60.84614  ? 182 PRO A CD  1 
ATOM   1400 N N   . SER B 2 3   ? -26.63688 8.72929   48.52078  1.000 61.56291  ? 3   SER B N   1 
ATOM   1401 C CA  . SER B 2 3   ? -25.63303 9.77025   48.71940  1.000 69.28643  ? 3   SER B CA  1 
ATOM   1402 C C   . SER B 2 3   ? -25.49654 10.63544  47.46518  1.000 63.45437  ? 3   SER B C   1 
ATOM   1403 O O   . SER B 2 3   ? -25.70169 10.14784  46.35237  1.000 55.54992  ? 3   SER B O   1 
ATOM   1404 C CB  . SER B 2 3   ? -24.27980 9.15081   49.08344  1.000 61.23314  ? 3   SER B CB  1 
ATOM   1405 O OG  . SER B 2 3   ? -23.61718 8.65707   47.93165  1.000 64.32560  ? 3   SER B OG  1 
ATOM   1406 N N   . PRO B 2 4   ? -25.15966 11.91599  47.64072  1.000 46.35683  ? 4   PRO B N   1 
ATOM   1407 C CA  . PRO B 2 4   ? -24.94090 12.77878  46.47504  1.000 48.02662  ? 4   PRO B CA  1 
ATOM   1408 C C   . PRO B 2 4   ? -23.78016 12.26786  45.63724  1.000 57.13363  ? 4   PRO B C   1 
ATOM   1409 O O   . PRO B 2 4   ? -22.83898 11.65457  46.14560  1.000 57.94238  ? 4   PRO B O   1 
ATOM   1410 C CB  . PRO B 2 4   ? -24.62161 14.14687  47.09224  1.000 45.71503  ? 4   PRO B CB  1 
ATOM   1411 C CG  . PRO B 2 4   ? -25.11255 14.07055  48.49627  1.000 48.68498  ? 4   PRO B CG  1 
ATOM   1412 C CD  . PRO B 2 4   ? -24.95824 12.64080  48.90621  1.000 48.32025  ? 4   PRO B CD  1 
ATOM   1413 N N   . GLU B 2 5   ? -23.85876 12.51373  44.33583  1.000 50.32149  ? 5   GLU B N   1 
ATOM   1414 C CA  . GLU B 2 5   ? -22.77548 12.14551  43.44201  1.000 50.98174  ? 5   GLU B CA  1 
ATOM   1415 C C   . GLU B 2 5   ? -21.79315 13.30194  43.33109  1.000 55.41022  ? 5   GLU B C   1 
ATOM   1416 O O   . GLU B 2 5   ? -22.18699 14.47283  43.30426  1.000 50.33199  ? 5   GLU B O   1 
ATOM   1417 C CB  . GLU B 2 5   ? -23.30419 11.75501  42.06173  1.000 48.75939  ? 5   GLU B CB  1 
ATOM   1418 C CG  . GLU B 2 5   ? -23.98045 12.87049  41.29740  1.000 59.04182  ? 5   GLU B CG  1 
ATOM   1419 C CD  . GLU B 2 5   ? -24.19663 12.51125  39.84135  1.000 64.00236  ? 5   GLU B CD  1 
ATOM   1420 O OE1 . GLU B 2 5   ? -23.95399 11.33832  39.47738  1.000 56.84718  ? 5   GLU B OE1 1 
ATOM   1421 O OE2 . GLU B 2 5   ? -24.59867 13.40161  39.06222  1.000 72.37589  ? 5   GLU B OE2 1 
ATOM   1422 N N   . ASP B 2 6   ? -20.50889 12.96706  43.28840  1.000 47.25237  ? 6   ASP B N   1 
ATOM   1423 C CA  . ASP B 2 6   ? -19.45649 13.96666  43.23375  1.000 54.10733  ? 6   ASP B CA  1 
ATOM   1424 C C   . ASP B 2 6   ? -18.48517 13.62769  42.11479  1.000 41.06409  ? 6   ASP B C   1 
ATOM   1425 O O   . ASP B 2 6   ? -18.18488 12.45480  41.87072  1.000 43.20695  ? 6   ASP B O   1 
ATOM   1426 C CB  . ASP B 2 6   ? -18.70757 14.06278  44.56501  1.000 39.25973  ? 6   ASP B CB  1 
ATOM   1427 C CG  . ASP B 2 6   ? -17.88612 15.32460  44.66806  1.000 37.32554  ? 6   ASP B CG  1 
ATOM   1428 O OD1 . ASP B 2 6   ? -18.02873 16.18983  43.77856  1.000 43.84468  ? 6   ASP B OD1 1 
ATOM   1429 O OD2 . ASP B 2 6   ? -17.09877 15.45579  45.62773  1.000 45.66350  ? 6   ASP B OD2 1 
ATOM   1430 N N   . PHE B 2 7   ? -18.00169 14.66024  41.43333  1.000 36.93037  ? 7   PHE B N   1 
ATOM   1431 C CA  . PHE B 2 7   ? -17.01438 14.51239  40.37236  1.000 37.88340  ? 7   PHE B CA  1 
ATOM   1432 C C   . PHE B 2 7   ? -15.78677 15.31558  40.76671  1.000 37.44800  ? 7   PHE B C   1 
ATOM   1433 O O   . PHE B 2 7   ? -15.87886 16.53115  40.96814  1.000 34.88940  ? 7   PHE B O   1 
ATOM   1434 C CB  . PHE B 2 7   ? -17.57211 14.98172  39.02821  1.000 45.97684  ? 7   PHE B CB  1 
ATOM   1435 C CG  . PHE B 2 7   ? -18.76673 14.20148  38.56774  1.000 44.94771  ? 7   PHE B CG  1 
ATOM   1436 C CD1 . PHE B 2 7   ? -18.61044 12.97679  37.93964  1.000 43.70212  ? 7   PHE B CD1 1 
ATOM   1437 C CD2 . PHE B 2 7   ? -20.04672 14.68733  38.76887  1.000 43.56304  ? 7   PHE B CD2 1 
ATOM   1438 C CE1 . PHE B 2 7   ? -19.70985 12.25492  37.51439  1.000 53.82691  ? 7   PHE B CE1 1 
ATOM   1439 C CE2 . PHE B 2 7   ? -21.15014 13.96942  38.34491  1.000 48.13318  ? 7   PHE B CE2 1 
ATOM   1440 C CZ  . PHE B 2 7   ? -20.97983 12.75044  37.71872  1.000 50.46675  ? 7   PHE B CZ  1 
ATOM   1441 N N   . VAL B 2 8   ? -14.64729 14.63734  40.88179  1.000 39.55388  ? 8   VAL B N   1 
ATOM   1442 C CA  . VAL B 2 8   ? -13.45317 15.19735  41.50064  1.000 40.55575  ? 8   VAL B CA  1 
ATOM   1443 C C   . VAL B 2 8   ? -12.33320 15.26996  40.47403  1.000 36.19166  ? 8   VAL B C   1 
ATOM   1444 O O   . VAL B 2 8   ? -12.11238 14.32653  39.70590  1.000 31.22131  ? 8   VAL B O   1 
ATOM   1445 C CB  . VAL B 2 8   ? -13.01524 14.36707  42.72613  1.000 41.87368  ? 8   VAL B CB  1 
ATOM   1446 C CG1 . VAL B 2 8   ? -11.73151 14.93259  43.33286  1.000 34.35538  ? 8   VAL B CG1 1 
ATOM   1447 C CG2 . VAL B 2 8   ? -14.13668 14.31949  43.76026  1.000 35.18602  ? 8   VAL B CG2 1 
ATOM   1448 N N   . TYR B 2 9   ? -11.62877 16.39649  40.46971  1.000 31.17551  ? 9   TYR B N   1 
ATOM   1449 C CA  . TYR B 2 9   ? -10.42853 16.59522  39.67091  1.000 29.57998  ? 9   TYR B CA  1 
ATOM   1450 C C   . TYR B 2 9   ? -9.30634  17.03853  40.59983  1.000 39.62535  ? 9   TYR B C   1 
ATOM   1451 O O   . TYR B 2 9   ? -9.50132  17.92887  41.43513  1.000 34.12645  ? 9   TYR B O   1 
ATOM   1452 C CB  . TYR B 2 9   ? -10.66639 17.64209  38.57965  1.000 27.77545  ? 9   TYR B CB  1 
ATOM   1453 C CG  . TYR B 2 9   ? -9.57918  17.74201  37.53228  1.000 35.76412  ? 9   TYR B CG  1 
ATOM   1454 C CD1 . TYR B 2 9   ? -8.36896  18.36335  37.80913  1.000 26.70500  ? 9   TYR B CD1 1 
ATOM   1455 C CD2 . TYR B 2 9   ? -9.77903  17.24358  36.25313  1.000 41.11532  ? 9   TYR B CD2 1 
ATOM   1456 C CE1 . TYR B 2 9   ? -7.37806  18.46479  36.84785  1.000 32.35788  ? 9   TYR B CE1 1 
ATOM   1457 C CE2 . TYR B 2 9   ? -8.79516  17.34245  35.28367  1.000 49.91442  ? 9   TYR B CE2 1 
ATOM   1458 C CZ  . TYR B 2 9   ? -7.59814  17.95151  35.58555  1.000 33.22797  ? 9   TYR B CZ  1 
ATOM   1459 O OH  . TYR B 2 9   ? -6.62353  18.05050  34.62369  1.000 37.12008  ? 9   TYR B OH  1 
ATOM   1460 N N   . GLN B 2 10  ? -8.14356  16.40959  40.46791  1.000 34.17356  ? 10  GLN B N   1 
ATOM   1461 C CA  . GLN B 2 10  ? -6.95673  16.80300  41.20975  1.000 34.56427  ? 10  GLN B CA  1 
ATOM   1462 C C   . GLN B 2 10  ? -5.83445  17.08526  40.22489  1.000 28.83383  ? 10  GLN B C   1 
ATOM   1463 O O   . GLN B 2 10  ? -5.71383  16.40590  39.20008  1.000 29.64228  ? 10  GLN B O   1 
ATOM   1464 C CB  . GLN B 2 10  ? -6.51676  15.71842  42.20276  1.000 22.77350  ? 10  GLN B CB  1 
ATOM   1465 C CG  . GLN B 2 10  ? -7.62810  15.19263  43.08737  1.000 34.63406  ? 10  GLN B CG  1 
ATOM   1466 C CD  . GLN B 2 10  ? -7.13430  14.17156  44.09770  1.000 29.78984  ? 10  GLN B CD  1 
ATOM   1467 O OE1 . GLN B 2 10  ? -6.19327  14.42932  44.84521  1.000 30.12463  ? 10  GLN B OE1 1 
ATOM   1468 N NE2 . GLN B 2 10  ? -7.76885  13.00510  44.12358  1.000 29.93374  ? 10  GLN B NE2 1 
ATOM   1469 N N   . PHE B 2 11  ? -5.02500  18.09667  40.53232  1.000 27.54371  ? 11  PHE B N   1 
ATOM   1470 C CA  . PHE B 2 11  ? -3.79637  18.36741  39.79588  1.000 29.04988  ? 11  PHE B CA  1 
ATOM   1471 C C   . PHE B 2 11  ? -2.66399  18.55520  40.79537  1.000 27.65123  ? 11  PHE B C   1 
ATOM   1472 O O   . PHE B 2 11  ? -2.72283  19.45076  41.64485  1.000 24.53055  ? 11  PHE B O   1 
ATOM   1473 C CB  . PHE B 2 11  ? -3.93692  19.59830  38.89673  1.000 26.77787  ? 11  PHE B CB  1 
ATOM   1474 C CG  . PHE B 2 11  ? -2.66545  19.97337  38.20463  1.000 26.11929  ? 11  PHE B CG  1 
ATOM   1475 C CD1 . PHE B 2 11  ? -2.06515  19.09494  37.31037  1.000 25.97853  ? 11  PHE B CD1 1 
ATOM   1476 C CD2 . PHE B 2 11  ? -2.05586  21.19180  38.45879  1.000 25.97191  ? 11  PHE B CD2 1 
ATOM   1477 C CE1 . PHE B 2 11  ? -0.87913  19.42592  36.67605  1.000 20.92440  ? 11  PHE B CE1 1 
ATOM   1478 C CE2 . PHE B 2 11  ? -0.86788  21.53352  37.82431  1.000 34.73547  ? 11  PHE B CE2 1 
ATOM   1479 C CZ  . PHE B 2 11  ? -0.27975  20.64865  36.93000  1.000 24.92732  ? 11  PHE B CZ  1 
ATOM   1480 N N   . LYS B 2 12  ? -1.63931  17.71394  40.69500  1.000 26.33982  ? 12  LYS B N   1 
ATOM   1481 C CA  . LYS B 2 12  ? -0.53442  17.69481  41.64530  1.000 29.83651  ? 12  LYS B CA  1 
ATOM   1482 C C   . LYS B 2 12  ? 0.76920   17.98771  40.91685  1.000 25.67927  ? 12  LYS B C   1 
ATOM   1483 O O   . LYS B 2 12  ? 1.20279   17.20157  40.06920  1.000 24.71945  ? 12  LYS B O   1 
ATOM   1484 C CB  . LYS B 2 12  ? -0.45390  16.34537  42.36042  1.000 29.51232  ? 12  LYS B CB  1 
ATOM   1485 C CG  . LYS B 2 12  ? -1.69202  15.99071  43.17226  1.000 26.20681  ? 12  LYS B CG  1 
ATOM   1486 C CD  . LYS B 2 12  ? -1.57102  14.58452  43.73636  1.000 31.57728  ? 12  LYS B CD  1 
ATOM   1487 C CE  . LYS B 2 12  ? -2.66888  14.27910  44.74058  1.000 22.62178  ? 12  LYS B CE  1 
ATOM   1488 N NZ  . LYS B 2 12  ? -2.46415  12.94665  45.36984  1.000 31.06432  ? 12  LYS B NZ  1 
ATOM   1489 N N   . GLY B 2 13  ? 1.38539   19.11972  41.24318  1.000 29.94066  ? 13  GLY B N   1 
ATOM   1490 C CA  . GLY B 2 13  ? 2.71379   19.42981  40.75152  1.000 29.73220  ? 13  GLY B CA  1 
ATOM   1491 C C   . GLY B 2 13  ? 3.77883   19.06669  41.76676  1.000 26.37248  ? 13  GLY B C   1 
ATOM   1492 O O   . GLY B 2 13  ? 4.06673   19.84857  42.67541  1.000 22.89407  ? 13  GLY B O   1 
ATOM   1493 N N   . MET B 2 14  ? 4.37118   17.88716  41.62772  1.000 22.30200  ? 14  MET B N   1 
ATOM   1494 C CA  . MET B 2 14  ? 5.18180   17.29640  42.68158  1.000 26.93608  ? 14  MET B CA  1 
ATOM   1495 C C   . MET B 2 14  ? 6.66015   17.30978  42.31438  1.000 30.98683  ? 14  MET B C   1 
ATOM   1496 O O   . MET B 2 14  ? 7.02778   17.11135  41.15092  1.000 19.94442  ? 14  MET B O   1 
ATOM   1497 C CB  . MET B 2 14  ? 4.73142   15.86222  42.97041  1.000 19.84910  ? 14  MET B CB  1 
ATOM   1498 C CG  . MET B 2 14  ? 3.24082   15.74914  43.23750  1.000 25.26243  ? 14  MET B CG  1 
ATOM   1499 S SD  . MET B 2 14  ? 2.74704   14.09669  43.74770  1.000 32.28229  ? 14  MET B SD  1 
ATOM   1500 C CE  . MET B 2 14  ? 3.53409   13.97326  45.35063  1.000 22.09627  ? 14  MET B CE  1 
ATOM   1501 N N   . CYS B 2 15  ? 7.50031   17.53744  43.32106  1.000 25.76426  ? 15  CYS B N   1 
ATOM   1502 C CA  . CYS B 2 15  ? 8.94521   17.51776  43.17504  1.000 27.24526  ? 15  CYS B CA  1 
ATOM   1503 C C   . CYS B 2 15  ? 9.52885   16.47267  44.11101  1.000 22.22301  ? 15  CYS B C   1 
ATOM   1504 O O   . CYS B 2 15  ? 9.08476   16.33216  45.25251  1.000 25.43856  ? 15  CYS B O   1 
ATOM   1505 C CB  . CYS B 2 15  ? 9.55670   18.88426  43.49108  1.000 22.54624  ? 15  CYS B CB  1 
ATOM   1506 S SG  . CYS B 2 15  ? 8.97859   20.24371  42.45596  1.000 34.00902  ? 15  CYS B SG  1 
ATOM   1507 N N   . TYR B 2 16  ? 10.53421  15.75257  43.63045  1.000 26.35307  ? 16  TYR B N   1 
ATOM   1508 C CA  . TYR B 2 16  ? 11.24628  14.76776  44.42991  1.000 24.93505  ? 16  TYR B CA  1 
ATOM   1509 C C   . TYR B 2 16  ? 12.71301  15.16670  44.49055  1.000 28.04495  ? 16  TYR B C   1 
ATOM   1510 O O   . TYR B 2 16  ? 13.31173  15.50436  43.46224  1.000 23.73794  ? 16  TYR B O   1 
ATOM   1511 C CB  . TYR B 2 16  ? 11.08089  13.36334  43.84216  1.000 20.57668  ? 16  TYR B CB  1 
ATOM   1512 C CG  . TYR B 2 16  ? 9.64029   12.92657  43.75293  1.000 25.62501  ? 16  TYR B CG  1 
ATOM   1513 C CD1 . TYR B 2 16  ? 8.84726   13.28032  42.65986  1.000 23.03972  ? 16  TYR B CD1 1 
ATOM   1514 C CD2 . TYR B 2 16  ? 9.06071   12.17291  44.76907  1.000 32.40953  ? 16  TYR B CD2 1 
ATOM   1515 C CE1 . TYR B 2 16  ? 7.51520   12.88675  42.58438  1.000 26.30756  ? 16  TYR B CE1 1 
ATOM   1516 C CE2 . TYR B 2 16  ? 7.73485   11.77105  44.69910  1.000 28.38716  ? 16  TYR B CE2 1 
ATOM   1517 C CZ  . TYR B 2 16  ? 6.96643   12.13042  43.60819  1.000 24.03932  ? 16  TYR B CZ  1 
ATOM   1518 O OH  . TYR B 2 16  ? 5.65183   11.72883  43.55138  1.000 24.64494  ? 16  TYR B OH  1 
ATOM   1519 N N   . PHE B 2 17  ? 13.27905  15.14993  45.69551  1.000 23.39555  ? 17  PHE B N   1 
ATOM   1520 C CA  . PHE B 2 17  ? 14.66443  15.53878  45.91434  1.000 23.53959  ? 17  PHE B CA  1 
ATOM   1521 C C   . PHE B 2 17  ? 15.38277  14.43131  46.66500  1.000 28.87475  ? 17  PHE B C   1 
ATOM   1522 O O   . PHE B 2 17  ? 14.85024  13.89317  47.64209  1.000 28.46039  ? 17  PHE B O   1 
ATOM   1523 C CB  . PHE B 2 17  ? 14.76937  16.84427  46.71459  1.000 25.27812  ? 17  PHE B CB  1 
ATOM   1524 C CG  . PHE B 2 17  ? 13.87713  17.94871  46.22093  1.000 24.90916  ? 17  PHE B CG  1 
ATOM   1525 C CD1 . PHE B 2 17  ? 14.34557  18.88276  45.31188  1.000 25.54092  ? 17  PHE B CD1 1 
ATOM   1526 C CD2 . PHE B 2 17  ? 12.58303  18.07459  46.69492  1.000 25.17575  ? 17  PHE B CD2 1 
ATOM   1527 C CE1 . PHE B 2 17  ? 13.53538  19.91338  44.87386  1.000 23.76073  ? 17  PHE B CE1 1 
ATOM   1528 C CE2 . PHE B 2 17  ? 11.76678  19.10292  46.26159  1.000 29.76496  ? 17  PHE B CE2 1 
ATOM   1529 C CZ  . PHE B 2 17  ? 12.24309  20.02340  45.34917  1.000 32.86923  ? 17  PHE B CZ  1 
ATOM   1530 N N   . THR B 2 18  ? 16.59494  14.11102  46.22236  1.000 23.03148  ? 18  THR B N   1 
ATOM   1531 C CA  . THR B 2 18  ? 17.44553  13.15263  46.91058  1.000 32.09631  ? 18  THR B CA  1 
ATOM   1532 C C   . THR B 2 18  ? 18.87497  13.67684  46.90141  1.000 30.04224  ? 18  THR B C   1 
ATOM   1533 O O   . THR B 2 18  ? 19.33157  14.22960  45.89446  1.000 30.71406  ? 18  THR B O   1 
ATOM   1534 C CB  . THR B 2 18  ? 17.36250  11.76470  46.25438  1.000 32.45189  ? 18  THR B CB  1 
ATOM   1535 O OG1 . THR B 2 18  ? 15.99898  11.32123  46.25462  1.000 31.07540  ? 18  THR B OG1 1 
ATOM   1536 C CG2 . THR B 2 18  ? 18.20488  10.75455  47.01457  1.000 27.84471  ? 18  THR B CG2 1 
ATOM   1537 N N   . ASN B 2 19  ? 19.56359  13.52670  48.03734  1.000 27.74589  ? 19  ASN B N   1 
ATOM   1538 C CA  . ASN B 2 19  ? 20.95677  13.95107  48.19511  1.000 36.08763  ? 19  ASN B CA  1 
ATOM   1539 C C   . ASN B 2 19  ? 21.10493  15.44932  47.92284  1.000 37.08526  ? 19  ASN B C   1 
ATOM   1540 O O   . ASN B 2 19  ? 21.87306  15.88615  47.06122  1.000 31.81123  ? 19  ASN B O   1 
ATOM   1541 C CB  . ASN B 2 19  ? 21.88725  13.12855  47.29404  1.000 38.32232  ? 19  ASN B CB  1 
ATOM   1542 C CG  . ASN B 2 19  ? 22.28127  11.80562  47.91663  1.000 44.03124  ? 19  ASN B CG  1 
ATOM   1543 O OD1 . ASN B 2 19  ? 21.72847  11.40290  48.93752  1.000 37.56187  ? 19  ASN B OD1 1 
ATOM   1544 N ND2 . ASN B 2 19  ? 23.24453  11.12014  47.30276  1.000 68.12243  ? 19  ASN B ND2 1 
ATOM   1545 N N   . GLY B 2 20  ? 20.35898  16.23725  48.69157  1.000 25.59129  ? 20  GLY B N   1 
ATOM   1546 C CA  . GLY B 2 20  ? 20.25651  17.65410  48.41126  1.000 21.67381  ? 20  GLY B CA  1 
ATOM   1547 C C   . GLY B 2 20  ? 19.52683  17.87758  47.10378  1.000 34.84266  ? 20  GLY B C   1 
ATOM   1548 O O   . GLY B 2 20  ? 18.36852  17.47407  46.95924  1.000 31.98110  ? 20  GLY B O   1 
ATOM   1549 N N   . THR B 2 21  ? 20.19532  18.50382  46.13604  1.000 28.37751  ? 21  THR B N   1 
ATOM   1550 C CA  . THR B 2 21  ? 19.65845  18.65750  44.79064  1.000 28.61876  ? 21  THR B CA  1 
ATOM   1551 C C   . THR B 2 21  ? 20.43589  17.83790  43.76698  1.000 31.87588  ? 21  THR B C   1 
ATOM   1552 O O   . THR B 2 21  ? 20.38788  18.14127  42.57080  1.000 34.47317  ? 21  THR B O   1 
ATOM   1553 C CB  . THR B 2 21  ? 19.63593  20.13146  44.37546  1.000 32.42697  ? 21  THR B CB  1 
ATOM   1554 O OG1 . THR B 2 21  ? 20.91272  20.73030  44.62784  1.000 40.66354  ? 21  THR B OG1 1 
ATOM   1555 C CG2 . THR B 2 21  ? 18.55986  20.88743  45.13588  1.000 27.17371  ? 21  THR B CG2 1 
ATOM   1556 N N   . GLU B 2 22  ? 21.15704  16.80772  44.21467  1.000 36.12874  ? 22  GLU B N   1 
ATOM   1557 C CA  . GLU B 2 22  ? 21.87083  15.93949  43.28190  1.000 37.20435  ? 22  GLU B CA  1 
ATOM   1558 C C   . GLU B 2 22  ? 20.90305  15.26423  42.31953  1.000 34.91315  ? 22  GLU B C   1 
ATOM   1559 O O   . GLU B 2 22  ? 21.13426  15.23349  41.10616  1.000 32.80200  ? 22  GLU B O   1 
ATOM   1560 C CB  . GLU B 2 22  ? 22.67007  14.89462  44.05295  1.000 37.89547  ? 22  GLU B CB  1 
ATOM   1561 C CG  . GLU B 2 22  ? 24.08410  14.70514  43.57042  1.000 49.93612  ? 22  GLU B CG  1 
ATOM   1562 C CD  . GLU B 2 22  ? 24.85676  13.76901  44.46754  1.000 59.70574  ? 22  GLU B CD  1 
ATOM   1563 O OE1 . GLU B 2 22  ? 24.71053  12.53837  44.30787  1.000 64.78925  ? 22  GLU B OE1 1 
ATOM   1564 O OE2 . GLU B 2 22  ? 25.58885  14.26834  45.34962  1.000 68.22721  ? 22  GLU B OE2 1 
ATOM   1565 N N   . ARG B 2 23  ? 19.81426  14.71157  42.84987  1.000 33.44990  ? 23  ARG B N   1 
ATOM   1566 C CA  . ARG B 2 23  ? 18.72500  14.16351  42.05475  1.000 30.47526  ? 23  ARG B CA  1 
ATOM   1567 C C   . ARG B 2 23  ? 17.47206  14.97947  42.33616  1.000 30.43425  ? 23  ARG B C   1 
ATOM   1568 O O   . ARG B 2 23  ? 16.98634  15.00423  43.47262  1.000 36.28042  ? 23  ARG B O   1 
ATOM   1569 C CB  . ARG B 2 23  ? 18.48110  12.68933  42.38045  1.000 28.29352  ? 23  ARG B CB  1 
ATOM   1570 C CG  . ARG B 2 23  ? 19.65469  11.77028  42.11132  1.000 38.58802  ? 23  ARG B CG  1 
ATOM   1571 C CD  . ARG B 2 23  ? 19.20930  10.54792  41.30778  1.000 70.41712  ? 23  ARG B CD  1 
ATOM   1572 N NE  . ARG B 2 23  ? 20.18599  9.46436   41.34398  1.000 61.98668  ? 23  ARG B NE  1 
ATOM   1573 C CZ  . ARG B 2 23  ? 21.33635  9.46459   40.68208  1.000 70.15276  ? 23  ARG B CZ  1 
ATOM   1574 N NH1 . ARG B 2 23  ? 21.70753  10.49431  39.93705  1.000 65.74834  ? 23  ARG B NH1 1 
ATOM   1575 N NH2 . ARG B 2 23  ? 22.13949  8.40806   40.77640  1.000 65.55901  ? 23  ARG B NH2 1 
ATOM   1576 N N   . VAL B 2 24  ? 16.95975  15.65586  41.31169  1.000 32.90191  ? 24  VAL B N   1 
ATOM   1577 C CA  . VAL B 2 24  ? 15.70174  16.38996  41.39523  1.000 24.39651  ? 24  VAL B CA  1 
ATOM   1578 C C   . VAL B 2 24  ? 14.80044  15.89514  40.27821  1.000 30.45344  ? 24  VAL B C   1 
ATOM   1579 O O   . VAL B 2 24  ? 15.22085  15.82467  39.11737  1.000 40.09697  ? 24  VAL B O   1 
ATOM   1580 C CB  . VAL B 2 24  ? 15.90553  17.91156  41.28881  1.000 24.62475  ? 24  VAL B CB  1 
ATOM   1581 C CG1 . VAL B 2 24  ? 14.58554  18.62911  41.50890  1.000 17.79147  ? 24  VAL B CG1 1 
ATOM   1582 C CG2 . VAL B 2 24  ? 16.94900  18.38313  42.28237  1.000 28.06289  ? 24  VAL B CG2 1 
ATOM   1583 N N   . ARG B 2 25  ? 13.56738  15.55966  40.62502  1.000 27.36866  ? 25  ARG B N   1 
ATOM   1584 C CA  . ARG B 2 25  ? 12.62676  14.98970  39.67738  1.000 17.45213  ? 25  ARG B CA  1 
ATOM   1585 C C   . ARG B 2 25  ? 11.28218  15.67485  39.84850  1.000 20.55742  ? 25  ARG B C   1 
ATOM   1586 O O   . ARG B 2 25  ? 10.81790  15.87012  40.97618  1.000 23.85574  ? 25  ARG B O   1 
ATOM   1587 C CB  . ARG B 2 25  ? 12.49927  13.48041  39.88601  1.000 25.46667  ? 25  ARG B CB  1 
ATOM   1588 C CG  . ARG B 2 25  ? 11.57293  12.77157  38.92560  1.000 23.17571  ? 25  ARG B CG  1 
ATOM   1589 C CD  . ARG B 2 25  ? 11.67281  11.27114  39.14008  1.000 20.35125  ? 25  ARG B CD  1 
ATOM   1590 N NE  . ARG B 2 25  ? 10.78238  10.52094  38.26499  1.000 33.69162  ? 25  ARG B NE  1 
ATOM   1591 C CZ  . ARG B 2 25  ? 10.51551  9.23078   38.40932  1.000 36.90458  ? 25  ARG B CZ  1 
ATOM   1592 N NH1 . ARG B 2 25  ? 11.07243  8.51517   39.37443  1.000 32.38395  ? 25  ARG B NH1 1 
ATOM   1593 N NH2 . ARG B 2 25  ? 9.66051   8.64676   37.57271  1.000 28.06802  ? 25  ARG B NH2 1 
ATOM   1594 N N   . LEU B 2 26  ? 10.67321  16.05085  38.73121  1.000 20.23749  ? 26  LEU B N   1 
ATOM   1595 C CA  . LEU B 2 26  ? 9.35996   16.66989  38.71097  1.000 17.93950  ? 26  LEU B CA  1 
ATOM   1596 C C   . LEU B 2 26  ? 8.37111   15.68085  38.12087  1.000 23.55491  ? 26  LEU B C   1 
ATOM   1597 O O   . LEU B 2 26  ? 8.61222   15.12832  37.04325  1.000 24.33896  ? 26  LEU B O   1 
ATOM   1598 C CB  . LEU B 2 26  ? 9.38368   17.96132  37.88871  1.000 27.96203  ? 26  LEU B CB  1 
ATOM   1599 C CG  . LEU B 2 26  ? 8.10797   18.78598  37.70230  1.000 25.18890  ? 26  LEU B CG  1 
ATOM   1600 C CD1 . LEU B 2 26  ? 8.48045   20.25570  37.63727  1.000 25.43573  ? 26  LEU B CD1 1 
ATOM   1601 C CD2 . LEU B 2 26  ? 7.34701   18.38626  36.44058  1.000 31.24211  ? 26  LEU B CD2 1 
ATOM   1602 N N   . VAL B 2 27  ? 7.26329   15.45975  38.81686  1.000 16.04822  ? 27  VAL B N   1 
ATOM   1603 C CA  . VAL B 2 27  ? 6.17290   14.65202  38.29465  1.000 21.80319  ? 27  VAL B CA  1 
ATOM   1604 C C   . VAL B 2 27  ? 4.88872   15.45209  38.45595  1.000 23.17603  ? 27  VAL B C   1 
ATOM   1605 O O   . VAL B 2 27  ? 4.44203   15.70369  39.57604  1.000 28.13128  ? 27  VAL B O   1 
ATOM   1606 C CB  . VAL B 2 27  ? 6.06743   13.28515  38.98502  1.000 23.98405  ? 27  VAL B CB  1 
ATOM   1607 C CG1 . VAL B 2 27  ? 4.99964   12.45043  38.30535  1.000 22.11502  ? 27  VAL B CG1 1 
ATOM   1608 C CG2 . VAL B 2 27  ? 7.41749   12.55992  38.97361  1.000 19.82627  ? 27  VAL B CG2 1 
ATOM   1609 N N   . SER B 2 28  ? 4.29911   15.85214  37.34487  1.000 26.02758  ? 28  SER B N   1 
ATOM   1610 C CA  . SER B 2 28  ? 3.00648   16.52940  37.32156  1.000 24.28363  ? 28  SER B CA  1 
ATOM   1611 C C   . SER B 2 28  ? 1.91459   15.49668  37.03591  1.000 27.10685  ? 28  SER B C   1 
ATOM   1612 O O   . SER B 2 28  ? 2.01881   14.73112  36.06936  1.000 28.19004  ? 28  SER B O   1 
ATOM   1613 C CB  . SER B 2 28  ? 2.98912   17.63355  36.25561  1.000 25.55540  ? 28  SER B CB  1 
ATOM   1614 O OG  . SER B 2 28  ? 1.75775   17.66307  35.57159  1.000 48.10068  ? 28  SER B OG  1 
ATOM   1615 N N   . ARG B 2 29  ? 0.86710   15.47840  37.86746  1.000 24.23383  ? 29  ARG B N   1 
ATOM   1616 C CA  . ARG B 2 29  ? -0.16609  14.44697  37.81281  1.000 23.35604  ? 29  ARG B CA  1 
ATOM   1617 C C   . ARG B 2 29  ? -1.54711  15.06627  37.65991  1.000 26.96814  ? 29  ARG B C   1 
ATOM   1618 O O   . ARG B 2 29  ? -1.94253  15.91806  38.46019  1.000 30.74102  ? 29  ARG B O   1 
ATOM   1619 C CB  . ARG B 2 29  ? -0.14686  13.58018  39.07357  1.000 24.24023  ? 29  ARG B CB  1 
ATOM   1620 C CG  . ARG B 2 29  ? 1.23140   13.16732  39.53604  1.000 25.42494  ? 29  ARG B CG  1 
ATOM   1621 C CD  . ARG B 2 29  ? 1.14439   12.22867  40.72901  1.000 29.23259  ? 29  ARG B CD  1 
ATOM   1622 N NE  . ARG B 2 29  ? 2.46160   11.86613  41.23987  1.000 29.94368  ? 29  ARG B NE  1 
ATOM   1623 C CZ  . ARG B 2 29  ? 3.13606   10.78565  40.87129  1.000 36.89377  ? 29  ARG B CZ  1 
ATOM   1624 N NH1 . ARG B 2 29  ? 2.63448   9.91916   40.00575  1.000 25.94834  ? 29  ARG B NH1 1 
ATOM   1625 N NH2 . ARG B 2 29  ? 4.34480   10.56920  41.38303  1.000 25.80668  ? 29  ARG B NH2 1 
ATOM   1626 N N   . SER B 2 30  ? -2.28777  14.60879  36.65582  1.000 30.46187  ? 30  SER B N   1 
ATOM   1627 C CA  . SER B 2 30  ? -3.68158  14.98710  36.44629  1.000 25.84917  ? 30  SER B CA  1 
ATOM   1628 C C   . SER B 2 30  ? -4.55718  13.78739  36.78875  1.000 32.04662  ? 30  SER B C   1 
ATOM   1629 O O   . SER B 2 30  ? -4.37950  12.70381  36.22105  1.000 32.88323  ? 30  SER B O   1 
ATOM   1630 C CB  . SER B 2 30  ? -3.91726  15.44003  35.00528  1.000 29.95072  ? 30  SER B CB  1 
ATOM   1631 O OG  . SER B 2 30  ? -3.07891  16.53202  34.67258  1.000 27.33568  ? 30  SER B OG  1 
ATOM   1632 N N   . ILE B 2 31  ? -5.49663  13.97684  37.71334  1.000 28.68666  ? 31  ILE B N   1 
ATOM   1633 C CA  . ILE B 2 31  ? -6.24143  12.87117  38.30527  1.000 31.87553  ? 31  ILE B CA  1 
ATOM   1634 C C   . ILE B 2 31  ? -7.73493  13.14496  38.19134  1.000 36.63115  ? 31  ILE B C   1 
ATOM   1635 O O   . ILE B 2 31  ? -8.21104  14.21233  38.59442  1.000 37.48707  ? 31  ILE B O   1 
ATOM   1636 C CB  . ILE B 2 31  ? -5.84076  12.64808  39.77649  1.000 29.07202  ? 31  ILE B CB  1 
ATOM   1637 C CG1 . ILE B 2 31  ? -4.35657  12.27985  39.86129  1.000 25.49596  ? 31  ILE B CG1 1 
ATOM   1638 C CG2 . ILE B 2 31  ? -6.70837  11.56210  40.41354  1.000 29.93515  ? 31  ILE B CG2 1 
ATOM   1639 C CD1 . ILE B 2 31  ? -3.63656  12.89585  41.02023  1.000 29.72038  ? 31  ILE B CD1 1 
ATOM   1640 N N   . TYR B 2 32  ? -8.46866  12.18053  37.64297  1.000 30.95332  ? 32  TYR B N   1 
ATOM   1641 C CA  . TYR B 2 32  ? -9.92376  12.21900  37.60165  1.000 28.35847  ? 32  TYR B CA  1 
ATOM   1642 C C   . TYR B 2 32  ? -10.45728 11.30521  38.69683  1.000 35.48731  ? 32  TYR B C   1 
ATOM   1643 O O   . TYR B 2 32  ? -10.20104 10.09503  38.67848  1.000 34.65998  ? 32  TYR B O   1 
ATOM   1644 C CB  . TYR B 2 32  ? -10.45157 11.78872  36.23494  1.000 29.16183  ? 32  TYR B CB  1 
ATOM   1645 C CG  . TYR B 2 32  ? -11.95551 11.84521  36.14120  1.000 28.47332  ? 32  TYR B CG  1 
ATOM   1646 C CD1 . TYR B 2 32  ? -12.61997 13.06072  36.08909  1.000 30.96969  ? 32  TYR B CD1 1 
ATOM   1647 C CD2 . TYR B 2 32  ? -12.71153 10.68240  36.10294  1.000 34.53683  ? 32  TYR B CD2 1 
ATOM   1648 C CE1 . TYR B 2 32  ? -13.99669 13.11716  36.00696  1.000 43.73066  ? 32  TYR B CE1 1 
ATOM   1649 C CE2 . TYR B 2 32  ? -14.08684 10.72860  36.01850  1.000 40.02283  ? 32  TYR B CE2 1 
ATOM   1650 C CZ  . TYR B 2 32  ? -14.72406 11.94809  35.97294  1.000 37.31707  ? 32  TYR B CZ  1 
ATOM   1651 O OH  . TYR B 2 32  ? -16.09557 11.99644  35.88775  1.000 54.20186  ? 32  TYR B OH  1 
ATOM   1652 N N   . ASN B 2 33  ? -11.20162 11.88699  39.63980  1.000 31.90139  ? 33  ASN B N   1 
ATOM   1653 C CA  . ASN B 2 33  ? -11.56879 11.21216  40.88072  1.000 41.10510  ? 33  ASN B CA  1 
ATOM   1654 C C   . ASN B 2 33  ? -10.30998 10.71856  41.58159  1.000 29.57735  ? 33  ASN B C   1 
ATOM   1655 O O   . ASN B 2 33  ? -9.55669  11.52522  42.13296  1.000 36.41047  ? 33  ASN B O   1 
ATOM   1656 C CB  . ASN B 2 33  ? -12.55220 10.07173  40.61318  1.000 37.46220  ? 33  ASN B CB  1 
ATOM   1657 C CG  . ASN B 2 33  ? -13.89579 10.57620  40.12171  1.000 41.63667  ? 33  ASN B CG  1 
ATOM   1658 O OD1 . ASN B 2 33  ? -14.39100 11.60847  40.58355  1.000 40.80044  ? 33  ASN B OD1 1 
ATOM   1659 N ND2 . ASN B 2 33  ? -14.48462 9.86313   39.17043  1.000 38.21539  ? 33  ASN B ND2 1 
ATOM   1660 N N   . ARG B 2 34  ? -10.06132 9.40854   41.56182  1.000 36.67827  ? 34  ARG B N   1 
ATOM   1661 C CA  . ARG B 2 34  ? -8.82286  8.85390   42.09586  1.000 34.05607  ? 34  ARG B CA  1 
ATOM   1662 C C   . ARG B 2 34  ? -7.98453  8.16814   41.02804  1.000 35.09429  ? 34  ARG B C   1 
ATOM   1663 O O   . ARG B 2 34  ? -7.00554  7.49246   41.36604  1.000 39.66159  ? 34  ARG B O   1 
ATOM   1664 C CB  . ARG B 2 34  ? -9.11720  7.88115   43.24186  1.000 43.21231  ? 34  ARG B CB  1 
ATOM   1665 C CG  . ARG B 2 34  ? -9.39799  8.58623   44.56081  1.000 39.27499  ? 34  ARG B CG  1 
ATOM   1666 C CD  . ARG B 2 34  ? -9.87114  7.62794   45.62373  1.000 35.50093  ? 34  ARG B CD  1 
ATOM   1667 N NE  . ARG B 2 34  ? -8.78583  7.12740   46.45452  1.000 37.80177  ? 34  ARG B NE  1 
ATOM   1668 C CZ  . ARG B 2 34  ? -8.55413  5.84422   46.69104  1.000 52.58722  ? 34  ARG B CZ  1 
ATOM   1669 N NH1 . ARG B 2 34  ? -9.29701  4.89656   46.14369  1.000 39.25148  ? 34  ARG B NH1 1 
ATOM   1670 N NH2 . ARG B 2 34  ? -7.56302  5.50469   47.51155  1.000 54.49243  ? 34  ARG B NH2 1 
ATOM   1671 N N   . GLU B 2 35  ? -8.33351  8.33142   39.75373  1.000 39.42713  ? 35  GLU B N   1 
ATOM   1672 C CA  . GLU B 2 35  ? -7.58537  7.75436   38.64387  1.000 35.26818  ? 35  GLU B CA  1 
ATOM   1673 C C   . GLU B 2 35  ? -6.65173  8.81164   38.06538  1.000 37.18978  ? 35  GLU B C   1 
ATOM   1674 O O   . GLU B 2 35  ? -7.11514  9.82838   37.53553  1.000 36.22419  ? 35  GLU B O   1 
ATOM   1675 C CB  . GLU B 2 35  ? -8.53027  7.22776   37.55979  1.000 41.24354  ? 35  GLU B CB  1 
ATOM   1676 C CG  . GLU B 2 35  ? -7.81706  6.55233   36.38174  1.000 59.06911  ? 35  GLU B CG  1 
ATOM   1677 C CD  . GLU B 2 35  ? -8.76721  5.97833   35.32544  1.000 74.42654  ? 35  GLU B CD  1 
ATOM   1678 O OE1 . GLU B 2 35  ? -9.35370  6.75485   34.53707  1.000 64.40512  ? 35  GLU B OE1 1 
ATOM   1679 O OE2 . GLU B 2 35  ? -8.91483  4.73789   35.27543  1.000 92.41745  ? 35  GLU B OE2 1 
ATOM   1680 N N   . GLU B 2 36  ? -5.34374  8.57841   38.17790  1.000 34.37807  ? 36  GLU B N   1 
ATOM   1681 C CA  . GLU B 2 36  ? -4.37076  9.38366   37.44832  1.000 37.23542  ? 36  GLU B CA  1 
ATOM   1682 C C   . GLU B 2 36  ? -4.46597  9.05903   35.96090  1.000 28.46495  ? 36  GLU B C   1 
ATOM   1683 O O   . GLU B 2 36  ? -4.34106  7.89551   35.56619  1.000 30.91776  ? 36  GLU B O   1 
ATOM   1684 C CB  . GLU B 2 36  ? -2.96272  9.11028   37.96698  1.000 25.64520  ? 36  GLU B CB  1 
ATOM   1685 C CG  . GLU B 2 36  ? -1.89087  9.97219   37.32245  1.000 28.98589  ? 36  GLU B CG  1 
ATOM   1686 C CD  . GLU B 2 36  ? -0.49526  9.67109   37.84805  1.000 36.76589  ? 36  GLU B CD  1 
ATOM   1687 O OE1 . GLU B 2 36  ? -0.36112  8.81076   38.74395  1.000 51.06042  ? 36  GLU B OE1 1 
ATOM   1688 O OE2 . GLU B 2 36  ? 0.47026   10.29568  37.36233  1.000 36.27107  ? 36  GLU B OE2 1 
ATOM   1689 N N   . ILE B 2 37  ? -4.69726  10.07350  35.13165  1.000 27.79945  ? 37  ILE B N   1 
ATOM   1690 C CA  . ILE B 2 37  ? -4.92977  9.87220   33.70868  1.000 36.16706  ? 37  ILE B CA  1 
ATOM   1691 C C   . ILE B 2 37  ? -3.78893  10.42119  32.85901  1.000 31.45049  ? 37  ILE B C   1 
ATOM   1692 O O   . ILE B 2 37  ? -3.46393  9.84686   31.81849  1.000 33.25814  ? 37  ILE B O   1 
ATOM   1693 C CB  . ILE B 2 37  ? -6.28493  10.47422  33.27205  1.000 35.77112  ? 37  ILE B CB  1 
ATOM   1694 C CG1 . ILE B 2 37  ? -6.29881  11.99358  33.45415  1.000 29.21150  ? 37  ILE B CG1 1 
ATOM   1695 C CG2 . ILE B 2 37  ? -7.42174  9.83099   34.05075  1.000 32.29768  ? 37  ILE B CG2 1 
ATOM   1696 C CD1 . ILE B 2 37  ? -7.55013  12.65666  32.93826  1.000 35.78890  ? 37  ILE B CD1 1 
ATOM   1697 N N   . VAL B 2 38  ? -3.17940  11.53483  33.26881  1.000 35.83825  ? 38  VAL B N   1 
ATOM   1698 C CA  . VAL B 2 38  ? -2.06089  12.12515  32.54504  1.000 33.63284  ? 38  VAL B CA  1 
ATOM   1699 C C   . VAL B 2 38  ? -0.95348  12.43301  33.53801  1.000 31.28413  ? 38  VAL B C   1 
ATOM   1700 O O   . VAL B 2 38  ? -1.20761  12.80748  34.68621  1.000 28.57457  ? 38  VAL B O   1 
ATOM   1701 C CB  . VAL B 2 38  ? -2.43755  13.41234  31.77694  1.000 31.30726  ? 38  VAL B CB  1 
ATOM   1702 C CG1 . VAL B 2 38  ? -1.41572  13.68297  30.67919  1.000 31.30802  ? 38  VAL B CG1 1 
ATOM   1703 C CG2 . VAL B 2 38  ? -3.83660  13.32909  31.20644  1.000 40.67371  ? 38  VAL B CG2 1 
ATOM   1704 N N   . ARG B 2 39  ? 0.28422   12.30125  33.07396  1.000 31.38209  ? 39  ARG B N   1 
ATOM   1705 C CA  . ARG B 2 39  ? 1.46778   12.48546  33.89673  1.000 24.51765  ? 39  ARG B CA  1 
ATOM   1706 C C   . ARG B 2 39  ? 2.56253   13.13818  33.06332  1.000 28.71928  ? 39  ARG B C   1 
ATOM   1707 O O   . ARG B 2 39  ? 2.77102   12.77054  31.90367  1.000 31.08903  ? 39  ARG B O   1 
ATOM   1708 C CB  . ARG B 2 39  ? 1.94912   11.13561  34.45531  1.000 21.28400  ? 39  ARG B CB  1 
ATOM   1709 C CG  . ARG B 2 39  ? 3.36111   11.13869  34.98307  1.000 32.72051  ? 39  ARG B CG  1 
ATOM   1710 C CD  . ARG B 2 39  ? 3.83568   9.72653   35.29872  1.000 27.20696  ? 39  ARG B CD  1 
ATOM   1711 N NE  . ARG B 2 39  ? 3.01716   9.09550   36.32678  1.000 27.57838  ? 39  ARG B NE  1 
ATOM   1712 C CZ  . ARG B 2 39  ? 3.32816   7.96355   36.94259  1.000 26.68274  ? 39  ARG B CZ  1 
ATOM   1713 N NH1 . ARG B 2 39  ? 4.45127   7.31500   36.67433  1.000 26.93099  ? 39  ARG B NH1 1 
ATOM   1714 N NH2 . ARG B 2 39  ? 2.49250   7.47043   37.85132  1.000 30.28711  ? 39  ARG B NH2 1 
ATOM   1715 N N   . PHE B 2 40  ? 3.24573   14.12174  33.64063  1.000 25.11668  ? 40  PHE B N   1 
ATOM   1716 C CA  . PHE B 2 40  ? 4.48644   14.63257  33.06473  1.000 31.26887  ? 40  PHE B CA  1 
ATOM   1717 C C   . PHE B 2 40  ? 5.61642   14.31415  34.03034  1.000 25.03122  ? 40  PHE B C   1 
ATOM   1718 O O   . PHE B 2 40  ? 5.67616   14.87450  35.12958  1.000 22.49205  ? 40  PHE B O   1 
ATOM   1719 C CB  . PHE B 2 40  ? 4.44133   16.13248  32.78169  1.000 18.30085  ? 40  PHE B CB  1 
ATOM   1720 C CG  . PHE B 2 40  ? 5.70296   16.64636  32.14327  1.000 26.90565  ? 40  PHE B CG  1 
ATOM   1721 C CD1 . PHE B 2 40  ? 6.79675   17.01502  32.92348  1.000 26.28111  ? 40  PHE B CD1 1 
ATOM   1722 C CD2 . PHE B 2 40  ? 5.81413   16.72730  30.75764  1.000 25.63596  ? 40  PHE B CD2 1 
ATOM   1723 C CE1 . PHE B 2 40  ? 7.97158   17.46713  32.33538  1.000 23.08028  ? 40  PHE B CE1 1 
ATOM   1724 C CE2 . PHE B 2 40  ? 6.98468   17.18374  30.16243  1.000 20.51910  ? 40  PHE B CE2 1 
ATOM   1725 C CZ  . PHE B 2 40  ? 8.06381   17.55439  30.95326  1.000 25.48781  ? 40  PHE B CZ  1 
ATOM   1726 N N   . ASP B 2 41  ? 6.51162   13.43115  33.60972  1.000 20.69173  ? 41  ASP B N   1 
ATOM   1727 C CA  . ASP B 2 41  ? 7.67121   13.02239  34.38845  1.000 17.63477  ? 41  ASP B CA  1 
ATOM   1728 C C   . ASP B 2 41  ? 8.89760   13.61308  33.70589  1.000 21.89428  ? 41  ASP B C   1 
ATOM   1729 O O   . ASP B 2 41  ? 9.17768   13.29569  32.54574  1.000 28.12015  ? 41  ASP B O   1 
ATOM   1730 C CB  . ASP B 2 41  ? 7.72853   11.49417  34.46922  1.000 20.47211  ? 41  ASP B CB  1 
ATOM   1731 C CG  . ASP B 2 41  ? 8.95416   10.96105  35.20149  1.000 22.05342  ? 41  ASP B CG  1 
ATOM   1732 O OD1 . ASP B 2 41  ? 9.85970   11.73228  35.58628  1.000 25.52989  ? 41  ASP B OD1 1 
ATOM   1733 O OD2 . ASP B 2 41  ? 9.00482   9.72680   35.38791  1.000 27.69376  ? 41  ASP B OD2 1 
ATOM   1734 N N   . SER B 2 42  ? 9.61436   14.48559  34.41793  1.000 23.70573  ? 42  SER B N   1 
ATOM   1735 C CA  . SER B 2 42  ? 10.73929  15.18401  33.80634  1.000 23.62565  ? 42  SER B CA  1 
ATOM   1736 C C   . SER B 2 42  ? 11.82420  14.22317  33.33053  1.000 22.08502  ? 42  SER B C   1 
ATOM   1737 O O   . SER B 2 42  ? 12.59483  14.57767  32.43482  1.000 23.88214  ? 42  SER B O   1 
ATOM   1738 C CB  . SER B 2 42  ? 11.31654  16.21870  34.77965  1.000 18.81041  ? 42  SER B CB  1 
ATOM   1739 O OG  . SER B 2 42  ? 12.00196  15.60188  35.85337  1.000 21.01129  ? 42  SER B OG  1 
ATOM   1740 N N   . ASP B 2 43  ? 11.89183  13.00993  33.88487  1.000 22.51190  ? 43  ASP B N   1 
ATOM   1741 C CA  . ASP B 2 43  ? 12.79590  12.00898  33.32424  1.000 23.51728  ? 43  ASP B CA  1 
ATOM   1742 C C   . ASP B 2 43  ? 12.37584  11.62912  31.91293  1.000 22.03645  ? 43  ASP B C   1 
ATOM   1743 O O   . ASP B 2 43  ? 13.22098  11.33751  31.05702  1.000 32.30036  ? 43  ASP B O   1 
ATOM   1744 C CB  . ASP B 2 43  ? 12.83462  10.75986  34.20430  1.000 27.70539  ? 43  ASP B CB  1 
ATOM   1745 C CG  . ASP B 2 43  ? 13.42010  11.02057  35.57753  1.000 30.66204  ? 43  ASP B CG  1 
ATOM   1746 O OD1 . ASP B 2 43  ? 14.03211  12.09572  35.78758  1.000 24.51995  ? 43  ASP B OD1 1 
ATOM   1747 O OD2 . ASP B 2 43  ? 13.26301  10.13600  36.44866  1.000 26.01138  ? 43  ASP B OD2 1 
ATOM   1748 N N   . VAL B 2 44  ? 11.07089  11.62307  31.65500  1.000 24.61113  ? 44  VAL B N   1 
ATOM   1749 C CA  . VAL B 2 44  ? 10.56230  11.22161  30.34956  1.000 21.81891  ? 44  VAL B CA  1 
ATOM   1750 C C   . VAL B 2 44  ? 10.59845  12.38707  29.36957  1.000 23.34893  ? 44  VAL B C   1 
ATOM   1751 O O   . VAL B 2 44  ? 10.94151  12.21071  28.19544  1.000 24.07327  ? 44  VAL B O   1 
ATOM   1752 C CB  . VAL B 2 44  ? 9.14845   10.64452  30.50714  1.000 23.07317  ? 44  VAL B CB  1 
ATOM   1753 C CG1 . VAL B 2 44  ? 8.56574   10.29050  29.15283  1.000 19.35667  ? 44  VAL B CG1 1 
ATOM   1754 C CG2 . VAL B 2 44  ? 9.19049   9.42141   31.42559  1.000 16.19945  ? 44  VAL B CG2 1 
ATOM   1755 N N   . GLY B 2 45  ? 10.25594  13.59088  29.82862  1.000 20.14926  ? 45  GLY B N   1 
ATOM   1756 C CA  . GLY B 2 45  ? 10.34073  14.77106  28.99512  1.000 25.88930  ? 45  GLY B CA  1 
ATOM   1757 C C   . GLY B 2 45  ? 9.14138   15.05994  28.11680  1.000 21.50337  ? 45  GLY B C   1 
ATOM   1758 O O   . GLY B 2 45  ? 9.22713   15.95068  27.26506  1.000 29.70324  ? 45  GLY B O   1 
ATOM   1759 N N   . GLU B 2 46  ? 8.03123   14.34508  28.29119  1.000 22.27331  ? 46  GLU B N   1 
ATOM   1760 C CA  . GLU B 2 46  ? 6.80115   14.64372  27.56833  1.000 27.93198  ? 46  GLU B CA  1 
ATOM   1761 C C   . GLU B 2 46  ? 5.63699   14.07948  28.36615  1.000 27.57506  ? 46  GLU B C   1 
ATOM   1762 O O   . GLU B 2 46  ? 5.82563   13.25953  29.26750  1.000 29.40535  ? 46  GLU B O   1 
ATOM   1763 C CB  . GLU B 2 46  ? 6.81520   14.06289  26.14804  1.000 21.81090  ? 46  GLU B CB  1 
ATOM   1764 C CG  . GLU B 2 46  ? 6.80688   12.53950  26.10708  1.000 29.90539  ? 46  GLU B CG  1 
ATOM   1765 C CD  . GLU B 2 46  ? 6.70178   11.99050  24.69751  1.000 38.52300  ? 46  GLU B CD  1 
ATOM   1766 O OE1 . GLU B 2 46  ? 6.98361   12.74536  23.74172  1.000 34.64117  ? 46  GLU B OE1 1 
ATOM   1767 O OE2 . GLU B 2 46  ? 6.33080   10.80586  24.54622  1.000 34.52419  ? 46  GLU B OE2 1 
ATOM   1768 N N   . PHE B 2 47  ? 4.43076   14.53200  28.03076  1.000 26.01213  ? 47  PHE B N   1 
ATOM   1769 C CA  . PHE B 2 47  ? 3.24114   14.01757  28.69522  1.000 22.88527  ? 47  PHE B CA  1 
ATOM   1770 C C   . PHE B 2 47  ? 2.97587   12.57981  28.27320  1.000 21.69658  ? 47  PHE B C   1 
ATOM   1771 O O   . PHE B 2 47  ? 3.14580   12.21408  27.10793  1.000 32.13624  ? 47  PHE B O   1 
ATOM   1772 C CB  . PHE B 2 47  ? 2.02655   14.88455  28.37450  1.000 23.55493  ? 47  PHE B CB  1 
ATOM   1773 C CG  . PHE B 2 47  ? 2.05264   16.23246  29.03171  1.000 20.93797  ? 47  PHE B CG  1 
ATOM   1774 C CD1 . PHE B 2 47  ? 1.61678   16.38851  30.33980  1.000 29.37624  ? 47  PHE B CD1 1 
ATOM   1775 C CD2 . PHE B 2 47  ? 2.51125   17.34283  28.34456  1.000 20.84424  ? 47  PHE B CD2 1 
ATOM   1776 C CE1 . PHE B 2 47  ? 1.63843   17.63124  30.94958  1.000 27.47002  ? 47  PHE B CE1 1 
ATOM   1777 C CE2 . PHE B 2 47  ? 2.53380   18.58582  28.94425  1.000 26.94009  ? 47  PHE B CE2 1 
ATOM   1778 C CZ  . PHE B 2 47  ? 2.09723   18.73121  30.25059  1.000 27.40709  ? 47  PHE B CZ  1 
ATOM   1779 N N   . ARG B 2 48  ? 2.55798   11.75914  29.22833  1.000 26.80463  ? 48  ARG B N   1 
ATOM   1780 C CA  . ARG B 2 48  ? 2.25720   10.35882  28.96721  1.000 28.30441  ? 48  ARG B CA  1 
ATOM   1781 C C   . ARG B 2 48  ? 0.87173   10.03389  29.50177  1.000 26.93568  ? 48  ARG B C   1 
ATOM   1782 O O   . ARG B 2 48  ? 0.55311   10.35268  30.65276  1.000 26.91590  ? 48  ARG B O   1 
ATOM   1783 C CB  . ARG B 2 48  ? 3.31107   9.43873   29.60028  1.000 31.73210  ? 48  ARG B CB  1 
ATOM   1784 C CG  . ARG B 2 48  ? 4.67230   9.48117   28.91111  1.000 26.25819  ? 48  ARG B CG  1 
ATOM   1785 C CD  . ARG B 2 48  ? 4.60150   8.85748   27.52213  1.000 28.07531  ? 48  ARG B CD  1 
ATOM   1786 N NE  . ARG B 2 48  ? 5.82154   9.07015   26.74765  1.000 29.44409  ? 48  ARG B NE  1 
ATOM   1787 C CZ  . ARG B 2 48  ? 6.90231   8.30172   26.81760  1.000 30.04492  ? 48  ARG B CZ  1 
ATOM   1788 N NH1 . ARG B 2 48  ? 6.96072   7.25933   27.63197  1.000 17.99327  ? 48  ARG B NH1 1 
ATOM   1789 N NH2 . ARG B 2 48  ? 7.95102   8.58450   26.04959  1.000 27.24225  ? 48  ARG B NH2 1 
ATOM   1790 N N   . ALA B 2 49  ? 0.04802   9.41514   28.66258  1.000 28.28095  ? 49  ALA B N   1 
ATOM   1791 C CA  . ALA B 2 49  ? -1.28562  9.01078   29.08795  1.000 31.22380  ? 49  ALA B CA  1 
ATOM   1792 C C   . ALA B 2 49  ? -1.18518  7.79478   29.99610  1.000 28.43638  ? 49  ALA B C   1 
ATOM   1793 O O   . ALA B 2 49  ? -0.70371  6.73775   29.57564  1.000 30.14168  ? 49  ALA B O   1 
ATOM   1794 C CB  . ALA B 2 49  ? -2.15922  8.70222   27.87627  1.000 24.39095  ? 49  ALA B CB  1 
ATOM   1795 N N   . VAL B 2 50  ? -1.63295  7.94177   31.24244  1.000 29.33423  ? 50  VAL B N   1 
ATOM   1796 C CA  . VAL B 2 50  ? -1.64827  6.80166   32.15241  1.000 29.34825  ? 50  VAL B CA  1 
ATOM   1797 C C   . VAL B 2 50  ? -2.84427  5.90418   31.86412  1.000 32.98564  ? 50  VAL B C   1 
ATOM   1798 O O   . VAL B 2 50  ? -2.74708  4.67618   31.95317  1.000 42.60001  ? 50  VAL B O   1 
ATOM   1799 C CB  . VAL B 2 50  ? -1.63166  7.28539   33.61352  1.000 34.69452  ? 50  VAL B CB  1 
ATOM   1800 C CG1 . VAL B 2 50  ? -1.58121  6.10560   34.56429  1.000 24.28954  ? 50  VAL B CG1 1 
ATOM   1801 C CG2 . VAL B 2 50  ? -0.45039  8.20146   33.84041  1.000 25.46406  ? 50  VAL B CG2 1 
ATOM   1802 N N   . THR B 2 51  ? -3.98692  6.49434   31.51916  1.000 33.23684  ? 51  THR B N   1 
ATOM   1803 C CA  . THR B 2 51  ? -5.15289  5.74800   31.06971  1.000 28.58126  ? 51  THR B CA  1 
ATOM   1804 C C   . THR B 2 51  ? -5.70967  6.40241   29.81309  1.000 32.90932  ? 51  THR B C   1 
ATOM   1805 O O   . THR B 2 51  ? -5.39486  7.55283   29.49408  1.000 32.16076  ? 51  THR B O   1 
ATOM   1806 C CB  . THR B 2 51  ? -6.25665  5.67685   32.14232  1.000 29.58526  ? 51  THR B CB  1 
ATOM   1807 O OG1 . THR B 2 51  ? -6.81645  6.98041   32.34444  1.000 34.88513  ? 51  THR B OG1 1 
ATOM   1808 C CG2 . THR B 2 51  ? -5.70448  5.15476   33.45996  1.000 32.21180  ? 51  THR B CG2 1 
ATOM   1809 N N   . LEU B 2 52  ? -6.55986  5.64895   29.10917  1.000 34.58378  ? 52  LEU B N   1 
ATOM   1810 C CA  . LEU B 2 52  ? -7.19053  6.15188   27.89255  1.000 37.01096  ? 52  LEU B CA  1 
ATOM   1811 C C   . LEU B 2 52  ? -7.87365  7.49975   28.10711  1.000 33.35845  ? 52  LEU B C   1 
ATOM   1812 O O   . LEU B 2 52  ? -7.91085  8.33091   27.19318  1.000 42.83222  ? 52  LEU B O   1 
ATOM   1813 C CB  . LEU B 2 52  ? -8.19940  5.12296   27.37959  1.000 38.62860  ? 52  LEU B CB  1 
ATOM   1814 C CG  . LEU B 2 52  ? -9.07761  5.53264   26.19990  1.000 41.54255  ? 52  LEU B CG  1 
ATOM   1815 C CD1 . LEU B 2 52  ? -8.24902  5.69425   24.93931  1.000 28.51008  ? 52  LEU B CD1 1 
ATOM   1816 C CD2 . LEU B 2 52  ? -10.16607 4.50541   26.00460  1.000 38.06066  ? 52  LEU B CD2 1 
ATOM   1817 N N   . LEU B 2 53  ? -8.41184  7.73950   29.30500  1.000 43.60563  ? 53  LEU B N   1 
ATOM   1818 C CA  . LEU B 2 53  ? -9.08586  9.00591   29.57170  1.000 34.57165  ? 53  LEU B CA  1 
ATOM   1819 C C   . LEU B 2 53  ? -8.14485  10.19264  29.39717  1.000 42.69163  ? 53  LEU B C   1 
ATOM   1820 O O   . LEU B 2 53  ? -8.59273  11.29563  29.05769  1.000 32.78600  ? 53  LEU B O   1 
ATOM   1821 C CB  . LEU B 2 53  ? -9.67624  8.98934   30.98232  1.000 34.12203  ? 53  LEU B CB  1 
ATOM   1822 C CG  . LEU B 2 53  ? -10.74621 10.02594  31.32682  1.000 49.85519  ? 53  LEU B CG  1 
ATOM   1823 C CD1 . LEU B 2 53  ? -11.95165 9.87077   30.41435  1.000 40.07425  ? 53  LEU B CD1 1 
ATOM   1824 C CD2 . LEU B 2 53  ? -11.15623 9.89210   32.78925  1.000 41.65220  ? 53  LEU B CD2 1 
ATOM   1825 N N   . GLY B 2 54  ? -6.84459  9.98635   29.60486  1.000 36.13829  ? 54  GLY B N   1 
ATOM   1826 C CA  . GLY B 2 54  ? -5.85860  11.03377  29.46531  1.000 27.57965  ? 54  GLY B CA  1 
ATOM   1827 C C   . GLY B 2 54  ? -5.12211  11.09344  28.14454  1.000 28.54286  ? 54  GLY B C   1 
ATOM   1828 O O   . GLY B 2 54  ? -4.23235  11.93603  27.98733  1.000 31.38515  ? 54  GLY B O   1 
ATOM   1829 N N   . LEU B 2 55  ? -5.46451  10.22853  27.18209  1.000 36.40846  ? 55  LEU B N   1 
ATOM   1830 C CA  . LEU B 2 55  ? -4.74554  10.22679  25.90854  1.000 38.08373  ? 55  LEU B CA  1 
ATOM   1831 C C   . LEU B 2 55  ? -4.95037  11.51134  25.11025  1.000 33.72226  ? 55  LEU B C   1 
ATOM   1832 O O   . LEU B 2 55  ? -3.95483  12.06514  24.61495  1.000 33.27816  ? 55  LEU B O   1 
ATOM   1833 C CB  . LEU B 2 55  ? -5.12928  8.98754   25.09480  1.000 34.56592  ? 55  LEU B CB  1 
ATOM   1834 C CG  . LEU B 2 55  ? -4.37268  8.77375   23.78402  1.000 36.39209  ? 55  LEU B CG  1 
ATOM   1835 C CD1 . LEU B 2 55  ? -2.87787  8.94034   23.98183  1.000 25.24443  ? 55  LEU B CD1 1 
ATOM   1836 C CD2 . LEU B 2 55  ? -4.68222  7.39385   23.22657  1.000 33.14970  ? 55  LEU B CD2 1 
ATOM   1837 N N   . PRO B 2 56  ? -6.17581  12.03034  24.93273  1.000 39.42404  ? 56  PRO B N   1 
ATOM   1838 C CA  . PRO B 2 56  ? -6.30843  13.29296  24.18072  1.000 33.79774  ? 56  PRO B CA  1 
ATOM   1839 C C   . PRO B 2 56  ? -5.51498  14.44128  24.77950  1.000 30.11723  ? 56  PRO B C   1 
ATOM   1840 O O   . PRO B 2 56  ? -4.87472  15.19871  24.04026  1.000 34.88185  ? 56  PRO B O   1 
ATOM   1841 C CB  . PRO B 2 56  ? -7.81933  13.56493  24.22338  1.000 35.18249  ? 56  PRO B CB  1 
ATOM   1842 C CG  . PRO B 2 56  ? -8.43580  12.23464  24.42306  1.000 32.72559  ? 56  PRO B CG  1 
ATOM   1843 C CD  . PRO B 2 56  ? -7.49491  11.48500  25.30591  1.000 34.01862  ? 56  PRO B CD  1 
ATOM   1844 N N   . ALA B 2 57  ? -5.53509  14.59500  26.10350  1.000 30.57717  ? 57  ALA B N   1 
ATOM   1845 C CA  . ALA B 2 57  ? -4.78362  15.68455  26.71538  1.000 33.58085  ? 57  ALA B CA  1 
ATOM   1846 C C   . ALA B 2 57  ? -3.28615  15.50540  26.50089  1.000 31.87813  ? 57  ALA B C   1 
ATOM   1847 O O   . ALA B 2 57  ? -2.58579  16.46086  26.13939  1.000 30.71008  ? 57  ALA B O   1 
ATOM   1848 C CB  . ALA B 2 57  ? -5.11520  15.78164  28.20510  1.000 30.27742  ? 57  ALA B CB  1 
ATOM   1849 N N   . ALA B 2 58  ? -2.78477  14.28299  26.70013  1.000 30.14797  ? 58  ALA B N   1 
ATOM   1850 C CA  . ALA B 2 58  ? -1.36306  14.01571  26.51317  1.000 27.15203  ? 58  ALA B CA  1 
ATOM   1851 C C   . ALA B 2 58  ? -0.92460  14.34721  25.09466  1.000 30.88960  ? 58  ALA B C   1 
ATOM   1852 O O   . ALA B 2 58  ? 0.09334   15.01537  24.88823  1.000 32.54058  ? 58  ALA B O   1 
ATOM   1853 C CB  . ALA B 2 58  ? -1.05821  12.55643  26.84378  1.000 27.50296  ? 58  ALA B CB  1 
ATOM   1854 N N   . GLU B 2 59  ? -1.69227  13.89989  24.10070  1.000 33.73064  ? 59  GLU B N   1 
ATOM   1855 C CA  . GLU B 2 59  ? -1.35177  14.20585  22.71482  1.000 38.50300  ? 59  GLU B CA  1 
ATOM   1856 C C   . GLU B 2 59  ? -1.47571  15.69823  22.42885  1.000 30.84789  ? 59  GLU B C   1 
ATOM   1857 O O   . GLU B 2 59  ? -0.63505  16.27399  21.72962  1.000 38.21141  ? 59  GLU B O   1 
ATOM   1858 C CB  . GLU B 2 59  ? -2.24056  13.40145  21.76602  1.000 38.46630  ? 59  GLU B CB  1 
ATOM   1859 C CG  . GLU B 2 59  ? -2.03703  11.90265  21.86170  1.000 42.29043  ? 59  GLU B CG  1 
ATOM   1860 C CD  . GLU B 2 59  ? -1.79876  11.25789  20.49979  1.000 73.99359  ? 59  GLU B CD  1 
ATOM   1861 O OE1 . GLU B 2 59  ? -2.68281  11.36808  19.61535  1.000 62.69024  ? 59  GLU B OE1 1 
ATOM   1862 O OE2 . GLU B 2 59  ? -0.71744  10.65144  20.31188  1.000 62.39191  ? 59  GLU B OE2 1 
ATOM   1863 N N   . TYR B 2 60  ? -2.51092  16.34210  22.96712  1.000 26.41526  ? 60  TYR B N   1 
ATOM   1864 C CA  . TYR B 2 60  ? -2.73211  17.75773  22.69143  1.000 33.31358  ? 60  TYR B CA  1 
ATOM   1865 C C   . TYR B 2 60  ? -1.59957  18.61024  23.25687  1.000 38.56716  ? 60  TYR B C   1 
ATOM   1866 O O   . TYR B 2 60  ? -1.01223  19.43603  22.54659  1.000 36.94164  ? 60  TYR B O   1 
ATOM   1867 C CB  . TYR B 2 60  ? -4.08989  18.17999  23.26122  1.000 31.99426  ? 60  TYR B CB  1 
ATOM   1868 C CG  . TYR B 2 60  ? -4.38389  19.66358  23.20104  1.000 40.70367  ? 60  TYR B CG  1 
ATOM   1869 C CD1 . TYR B 2 60  ? -4.14635  20.39895  22.04409  1.000 37.21116  ? 60  TYR B CD1 1 
ATOM   1870 C CD2 . TYR B 2 60  ? -4.92784  20.32312  24.29804  1.000 42.37825  ? 60  TYR B CD2 1 
ATOM   1871 C CE1 . TYR B 2 60  ? -4.42408  21.75760  21.99217  1.000 44.25676  ? 60  TYR B CE1 1 
ATOM   1872 C CE2 . TYR B 2 60  ? -5.21164  21.67477  24.25421  1.000 53.78035  ? 60  TYR B CE2 1 
ATOM   1873 C CZ  . TYR B 2 60  ? -4.95838  22.38739  23.10049  1.000 60.87920  ? 60  TYR B CZ  1 
ATOM   1874 O OH  . TYR B 2 60  ? -5.24334  23.73355  23.06166  1.000 62.20372  ? 60  TYR B OH  1 
ATOM   1875 N N   . TRP B 2 61  ? -1.27027  18.41110  24.53590  1.000 33.66570  ? 61  TRP B N   1 
ATOM   1876 C CA  . TRP B 2 61  ? -0.19830  19.18338  25.15889  1.000 36.76523  ? 61  TRP B CA  1 
ATOM   1877 C C   . TRP B 2 61  ? 1.15276   18.88673  24.51785  1.000 33.50227  ? 61  TRP B C   1 
ATOM   1878 O O   . TRP B 2 61  ? 1.96539   19.79821  24.32567  1.000 34.95106  ? 61  TRP B O   1 
ATOM   1879 C CB  . TRP B 2 61  ? -0.14806  18.89249  26.65813  1.000 31.82534  ? 61  TRP B CB  1 
ATOM   1880 C CG  . TRP B 2 61  ? -1.37662  19.30668  27.40444  1.000 37.72994  ? 61  TRP B CG  1 
ATOM   1881 C CD1 . TRP B 2 61  ? -2.22435  20.33143  27.08951  1.000 34.45252  ? 61  TRP B CD1 1 
ATOM   1882 C CD2 . TRP B 2 61  ? -1.90430  18.69858  28.59182  1.000 34.61935  ? 61  TRP B CD2 1 
ATOM   1883 N NE1 . TRP B 2 61  ? -3.24089  20.40240  28.01170  1.000 31.34062  ? 61  TRP B NE1 1 
ATOM   1884 C CE2 . TRP B 2 61  ? -3.06709  19.41149  28.94395  1.000 38.40289  ? 61  TRP B CE2 1 
ATOM   1885 C CE3 . TRP B 2 61  ? -1.50498  17.62015  29.39137  1.000 32.00757  ? 61  TRP B CE3 1 
ATOM   1886 C CZ2 . TRP B 2 61  ? -3.83296  19.08376  30.06394  1.000 30.01953  ? 61  TRP B CZ2 1 
ATOM   1887 C CZ3 . TRP B 2 61  ? -2.26730  17.29706  30.50473  1.000 32.84899  ? 61  TRP B CZ3 1 
ATOM   1888 C CH2 . TRP B 2 61  ? -3.41617  18.02538  30.82905  1.000 30.79795  ? 61  TRP B CH2 1 
ATOM   1889 N N   . ASN B 2 62  ? 1.41387   17.61880  24.18358  1.000 29.91459  ? 62  ASN B N   1 
ATOM   1890 C CA  . ASN B 2 62  ? 2.69637   17.26530  23.58179  1.000 28.93485  ? 62  ASN B CA  1 
ATOM   1891 C C   . ASN B 2 62  ? 2.87755   17.90439  22.20935  1.000 40.13982  ? 62  ASN B C   1 
ATOM   1892 O O   . ASN B 2 62  ? 4.01449   18.13705  21.78278  1.000 35.77343  ? 62  ASN B O   1 
ATOM   1893 C CB  . ASN B 2 62  ? 2.83313   15.74522  23.47872  1.000 22.42139  ? 62  ASN B CB  1 
ATOM   1894 C CG  . ASN B 2 62  ? 3.25511   15.10650  24.78991  1.000 26.75667  ? 62  ASN B CG  1 
ATOM   1895 O OD1 . ASN B 2 62  ? 3.79357   15.77331  25.67132  1.000 32.70913  ? 62  ASN B OD1 1 
ATOM   1896 N ND2 . ASN B 2 62  ? 3.01597   13.80859  24.92325  1.000 25.92197  ? 62  ASN B ND2 1 
ATOM   1897 N N   . SER B 2 63  ? 1.78152   18.19445  21.50250  1.000 27.07427  ? 63  SER B N   1 
ATOM   1898 C CA  . SER B 2 63  ? 1.89641   18.81288  20.18859  1.000 40.58432  ? 63  SER B CA  1 
ATOM   1899 C C   . SER B 2 63  ? 2.24820   20.29334  20.26202  1.000 38.28133  ? 63  SER B C   1 
ATOM   1900 O O   . SER B 2 63  ? 2.53106   20.89690  19.22206  1.000 54.39497  ? 63  SER B O   1 
ATOM   1901 C CB  . SER B 2 63  ? 0.59315   18.63361  19.40886  1.000 35.68164  ? 63  SER B CB  1 
ATOM   1902 O OG  . SER B 2 63  ? -0.43388  19.43224  19.96142  1.000 34.77662  ? 63  SER B OG  1 
ATOM   1903 N N   . GLN B 2 64  ? 2.23438   20.89065  21.45067  1.000 43.03728  ? 64  GLN B N   1 
ATOM   1904 C CA  . GLN B 2 64  ? 2.50277   22.31691  21.62409  1.000 41.71284  ? 64  GLN B CA  1 
ATOM   1905 C C   . GLN B 2 64  ? 3.94256   22.49883  22.09037  1.000 45.78015  ? 64  GLN B C   1 
ATOM   1906 O O   . GLN B 2 64  ? 4.26020   22.27871  23.26144  1.000 43.78313  ? 64  GLN B O   1 
ATOM   1907 C CB  . GLN B 2 64  ? 1.51927   22.92776  22.61137  1.000 44.15565  ? 64  GLN B CB  1 
ATOM   1908 C CG  . GLN B 2 64  ? 0.33789   23.58734  21.95166  1.000 46.72373  ? 64  GLN B CG  1 
ATOM   1909 C CD  . GLN B 2 64  ? -0.88334  23.54772  22.82961  1.000 66.76195  ? 64  GLN B CD  1 
ATOM   1910 O OE1 . GLN B 2 64  ? -1.46798  22.48509  23.03952  1.000 52.60710  ? 64  GLN B OE1 1 
ATOM   1911 N NE2 . GLN B 2 64  ? -1.27342  24.70222  23.36346  1.000 79.20477  ? 64  GLN B NE2 1 
ATOM   1912 N N   . LYS B 2 65  ? 4.80893   22.92121  21.16719  1.000 48.22192  ? 65  LYS B N   1 
ATOM   1913 C CA  . LYS B 2 65  ? 6.22341   23.09444  21.48275  1.000 45.67902  ? 65  LYS B CA  1 
ATOM   1914 C C   . LYS B 2 65  ? 6.41926   23.98320  22.70491  1.000 39.84088  ? 65  LYS B C   1 
ATOM   1915 O O   . LYS B 2 65  ? 7.17674   23.63996  23.61909  1.000 43.24762  ? 65  LYS B O   1 
ATOM   1916 C CB  . LYS B 2 65  ? 6.96333   23.67608  20.27567  1.000 41.96529  ? 65  LYS B CB  1 
ATOM   1917 N N   . ASP B 2 66  ? 5.73179   25.12790  22.74474  1.000 45.97978  ? 66  ASP B N   1 
ATOM   1918 C CA  . ASP B 2 66  ? 5.95026   26.07583  23.83465  1.000 37.35358  ? 66  ASP B CA  1 
ATOM   1919 C C   . ASP B 2 66  ? 5.56069   25.48154  25.18559  1.000 32.52433  ? 66  ASP B C   1 
ATOM   1920 O O   . ASP B 2 66  ? 6.21459   25.74908  26.19956  1.000 34.33738  ? 66  ASP B O   1 
ATOM   1921 C CB  . ASP B 2 66  ? 5.18209   27.37291  23.57084  1.000 49.85366  ? 66  ASP B CB  1 
ATOM   1922 C CG  . ASP B 2 66  ? 3.68840   27.14810  23.38811  1.000 51.60239  ? 66  ASP B CG  1 
ATOM   1923 O OD1 . ASP B 2 66  ? 3.27361   25.98134  23.22353  1.000 57.82736  ? 66  ASP B OD1 1 
ATOM   1924 O OD2 . ASP B 2 66  ? 2.92764   28.14275  23.41386  1.000 69.79729  ? 66  ASP B OD2 1 
ATOM   1925 N N   . ILE B 2 67  ? 4.49943   24.67491  25.22813  1.000 38.06561  ? 67  ILE B N   1 
ATOM   1926 C CA  . ILE B 2 67  ? 4.11830   24.05987  26.49561  1.000 38.45399  ? 67  ILE B CA  1 
ATOM   1927 C C   . ILE B 2 67  ? 5.14852   23.02189  26.91283  1.000 33.91966  ? 67  ILE B C   1 
ATOM   1928 O O   . ILE B 2 67  ? 5.55840   22.96583  28.07947  1.000 37.09156  ? 67  ILE B O   1 
ATOM   1929 C CB  . ILE B 2 67  ? 2.71174   23.44736  26.40189  1.000 38.18040  ? 67  ILE B CB  1 
ATOM   1930 C CG1 . ILE B 2 67  ? 1.65678   24.54837  26.29206  1.000 41.62273  ? 67  ILE B CG1 1 
ATOM   1931 C CG2 . ILE B 2 67  ? 2.43818   22.56315  27.61317  1.000 32.04214  ? 67  ILE B CG2 1 
ATOM   1932 C CD1 . ILE B 2 67  ? 0.24244   24.01700  26.28957  1.000 48.48307  ? 67  ILE B CD1 1 
ATOM   1933 N N   . LEU B 2 68  ? 5.58406   22.18998  25.96582  1.000 31.85569  ? 68  LEU B N   1 
ATOM   1934 C CA  . LEU B 2 68  ? 6.55912   21.14594  26.26259  1.000 32.35641  ? 68  LEU B CA  1 
ATOM   1935 C C   . LEU B 2 68  ? 7.83989   21.73158  26.84968  1.000 30.08395  ? 68  LEU B C   1 
ATOM   1936 O O   . LEU B 2 68  ? 8.32525   21.27553  27.89115  1.000 35.30260  ? 68  LEU B O   1 
ATOM   1937 C CB  . LEU B 2 68  ? 6.85241   20.35754  24.98939  1.000 30.87282  ? 68  LEU B CB  1 
ATOM   1938 C CG  . LEU B 2 68  ? 7.19370   18.87645  25.10583  1.000 38.50708  ? 68  LEU B CG  1 
ATOM   1939 C CD1 . LEU B 2 68  ? 6.35069   18.21392  26.17956  1.000 24.45853  ? 68  LEU B CD1 1 
ATOM   1940 C CD2 . LEU B 2 68  ? 6.95707   18.21111  23.75206  1.000 33.50996  ? 68  LEU B CD2 1 
ATOM   1941 N N   . GLU B 2 69  ? 8.39271   22.75911  26.20144  1.000 28.09476  ? 69  GLU B N   1 
ATOM   1942 C CA  . GLU B 2 69  ? 9.63423   23.35644  26.68151  1.000 33.21954  ? 69  GLU B CA  1 
ATOM   1943 C C   . GLU B 2 69  ? 9.46208   23.99058  28.05343  1.000 31.55664  ? 69  GLU B C   1 
ATOM   1944 O O   . GLU B 2 69  ? 10.38823  23.95788  28.87365  1.000 34.21319  ? 69  GLU B O   1 
ATOM   1945 C CB  . GLU B 2 69  ? 10.14296  24.38595  25.67401  1.000 37.38646  ? 69  GLU B CB  1 
ATOM   1946 C CG  . GLU B 2 69  ? 10.57092  23.76231  24.35870  1.000 42.52426  ? 69  GLU B CG  1 
ATOM   1947 C CD  . GLU B 2 69  ? 11.46907  22.54638  24.55414  1.000 46.15413  ? 69  GLU B CD  1 
ATOM   1948 O OE1 . GLU B 2 69  ? 12.47128  22.64614  25.29723  1.000 48.09406  ? 69  GLU B OE1 1 
ATOM   1949 O OE2 . GLU B 2 69  ? 11.16488  21.48384  23.97144  1.000 50.48234  ? 69  GLU B OE2 1 
ATOM   1950 N N   . ARG B 2 70  ? 8.29159   24.56612  28.32389  1.000 28.18201  ? 70  ARG B N   1 
ATOM   1951 C CA  . ARG B 2 70  ? 8.03185   25.09894  29.65324  1.000 30.79355  ? 70  ARG B CA  1 
ATOM   1952 C C   . ARG B 2 70  ? 8.01727   23.98332  30.69265  1.000 33.73624  ? 70  ARG B C   1 
ATOM   1953 O O   . ARG B 2 70  ? 8.61888   24.11815  31.76479  1.000 28.84588  ? 70  ARG B O   1 
ATOM   1954 C CB  . ARG B 2 70  ? 6.71178   25.86673  29.65555  1.000 39.74124  ? 70  ARG B CB  1 
ATOM   1955 C CG  . ARG B 2 70  ? 6.75223   27.19338  30.39395  1.000 47.51491  ? 70  ARG B CG  1 
ATOM   1956 C CD  . ARG B 2 70  ? 5.36334   27.81008  30.46826  1.000 64.13807  ? 70  ARG B CD  1 
ATOM   1957 N NE  . ARG B 2 70  ? 4.49284   27.07355  31.37763  1.000 72.97219  ? 70  ARG B NE  1 
ATOM   1958 C CZ  . ARG B 2 70  ? 3.16884   27.06648  31.30802  1.000 70.60346  ? 70  ARG B CZ  1 
ATOM   1959 N NH1 . ARG B 2 70  ? 2.52297   27.71878  30.35448  1.000 68.66192  ? 70  ARG B NH1 1 
ATOM   1960 N NH2 . ARG B 2 70  ? 2.47598   26.38127  32.21332  1.000 63.79793  ? 70  ARG B NH2 1 
ATOM   1961 N N   . LYS B 2 71  ? 7.35590   22.86421  30.38667  1.000 29.04866  ? 71  LYS B N   1 
ATOM   1962 C CA  . LYS B 2 71  ? 7.31697   21.75967  31.33945  1.000 33.03569  ? 71  LYS B CA  1 
ATOM   1963 C C   . LYS B 2 71  ? 8.68409   21.11408  31.50669  1.000 30.96438  ? 71  LYS B C   1 
ATOM   1964 O O   . LYS B 2 71  ? 9.02008   20.66221  32.60694  1.000 27.36888  ? 71  LYS B O   1 
ATOM   1965 C CB  . LYS B 2 71  ? 6.29283   20.71249  30.90703  1.000 24.90417  ? 71  LYS B CB  1 
ATOM   1966 C CG  . LYS B 2 71  ? 4.87321   21.22568  30.86884  1.000 33.32456  ? 71  LYS B CG  1 
ATOM   1967 C CD  . LYS B 2 71  ? 4.38876   21.58826  32.25598  1.000 27.21341  ? 71  LYS B CD  1 
ATOM   1968 C CE  . LYS B 2 71  ? 4.38274   20.36024  33.16333  1.000 36.27071  ? 71  LYS B CE  1 
ATOM   1969 N NZ  . LYS B 2 71  ? 3.06593   20.16652  33.84432  1.000 44.17259  ? 71  LYS B NZ  1 
ATOM   1970 N N   . ARG B 2 72  ? 9.48653   21.06556  30.43993  1.000 26.05359  ? 72  ARG B N   1 
ATOM   1971 C CA  . ARG B 2 72  ? 10.81770  20.47794  30.55647  1.000 23.48801  ? 72  ARG B CA  1 
ATOM   1972 C C   . ARG B 2 72  ? 11.72668  21.31420  31.44691  1.000 24.61411  ? 72  ARG B C   1 
ATOM   1973 O O   . ARG B 2 72  ? 12.58083  20.76469  32.14931  1.000 30.76650  ? 72  ARG B O   1 
ATOM   1974 C CB  . ARG B 2 72  ? 11.43230  20.29332  29.17029  1.000 26.42668  ? 72  ARG B CB  1 
ATOM   1975 C CG  . ARG B 2 72  ? 10.78376  19.17527  28.38629  1.000 28.59714  ? 72  ARG B CG  1 
ATOM   1976 C CD  . ARG B 2 72  ? 11.20935  19.16034  26.93705  1.000 23.39781  ? 72  ARG B CD  1 
ATOM   1977 N NE  . ARG B 2 72  ? 10.77392  17.93055  26.29310  1.000 32.42422  ? 72  ARG B NE  1 
ATOM   1978 C CZ  . ARG B 2 72  ? 10.92079  17.65996  25.00480  1.000 37.82689  ? 72  ARG B CZ  1 
ATOM   1979 N NH1 . ARG B 2 72  ? 11.47840  18.52605  24.17542  1.000 25.80687  ? 72  ARG B NH1 1 
ATOM   1980 N NH2 . ARG B 2 72  ? 10.49366  16.49124  24.53688  1.000 28.55571  ? 72  ARG B NH2 1 
ATOM   1981 N N   . ALA B 2 73  ? 11.55266  22.62752  31.44944  1.000 22.12456  ? 73  ALA B N   1 
ATOM   1982 C CA  . ALA B 2 73  ? 12.35492  23.48663  32.30234  1.000 25.56152  ? 73  ALA B CA  1 
ATOM   1983 C C   . ALA B 2 73  ? 11.79847  23.61914  33.71927  1.000 31.85519  ? 73  ALA B C   1 
ATOM   1984 O O   . ALA B 2 73  ? 12.45804  24.22559  34.57344  1.000 27.00831  ? 73  ALA B O   1 
ATOM   1985 C CB  . ALA B 2 73  ? 12.48876  24.87246  31.65842  1.000 24.72248  ? 73  ALA B CB  1 
ATOM   1986 N N   . ALA B 2 74  ? 10.62265  23.04974  34.00267  1.000 22.93637  ? 74  ALA B N   1 
ATOM   1987 C CA  . ALA B 2 74  ? 9.96656   23.32238  35.28076  1.000 24.67236  ? 74  ALA B CA  1 
ATOM   1988 C C   . ALA B 2 74  ? 10.67809  22.65816  36.45862  1.000 33.57086  ? 74  ALA B C   1 
ATOM   1989 O O   . ALA B 2 74  ? 10.57200  23.14261  37.59432  1.000 27.75134  ? 74  ALA B O   1 
ATOM   1990 C CB  . ALA B 2 74  ? 8.50773   22.88048  35.22308  1.000 26.36892  ? 74  ALA B CB  1 
ATOM   1991 N N   . VAL B 2 75  ? 11.40369  21.55925  36.22218  1.000 25.54544  ? 75  VAL B N   1 
ATOM   1992 C CA  . VAL B 2 75  ? 12.14860  20.92547  37.31035  1.000 31.54293  ? 75  VAL B CA  1 
ATOM   1993 C C   . VAL B 2 75  ? 13.20188  21.87728  37.86056  1.000 25.97748  ? 75  VAL B C   1 
ATOM   1994 O O   . VAL B 2 75  ? 13.43981  21.92633  39.07263  1.000 32.14937  ? 75  VAL B O   1 
ATOM   1995 C CB  . VAL B 2 75  ? 12.77498  19.59426  36.85171  1.000 28.10978  ? 75  VAL B CB  1 
ATOM   1996 C CG1 . VAL B 2 75  ? 13.79290  19.81683  35.72798  1.000 19.41009  ? 75  VAL B CG1 1 
ATOM   1997 C CG2 . VAL B 2 75  ? 13.43492  18.90531  38.02712  1.000 14.53036  ? 75  VAL B CG2 1 
ATOM   1998 N N   . ASP B 2 76  ? 13.84273  22.65563  36.98489  1.000 28.04943  ? 76  ASP B N   1 
ATOM   1999 C CA  . ASP B 2 76  ? 14.81972  23.63225  37.44847  1.000 28.44766  ? 76  ASP B CA  1 
ATOM   2000 C C   . ASP B 2 76  ? 14.15342  24.91874  37.90807  1.000 28.68970  ? 76  ASP B C   1 
ATOM   2001 O O   . ASP B 2 76  ? 14.61106  25.54550  38.86725  1.000 35.87022  ? 76  ASP B O   1 
ATOM   2002 C CB  . ASP B 2 76  ? 15.82380  23.93782  36.34177  1.000 26.39587  ? 76  ASP B CB  1 
ATOM   2003 C CG  . ASP B 2 76  ? 16.51489  22.69508  35.82411  1.000 43.97740  ? 76  ASP B CG  1 
ATOM   2004 O OD1 . ASP B 2 76  ? 16.77524  21.77763  36.63592  1.000 44.27235  ? 76  ASP B OD1 1 
ATOM   2005 O OD2 . ASP B 2 76  ? 16.79045  22.63486  34.60259  1.000 45.00437  ? 76  ASP B OD2 1 
ATOM   2006 N N   . ARG B 2 77  ? 13.07248  25.32357  37.25127  1.000 28.06882  ? 77  ARG B N   1 
ATOM   2007 C CA  . ARG B 2 77  ? 12.47822  26.61148  37.57650  1.000 23.24143  ? 77  ARG B CA  1 
ATOM   2008 C C   . ARG B 2 77  ? 11.59523  26.53588  38.81295  1.000 28.52345  ? 77  ARG B C   1 
ATOM   2009 O O   . ARG B 2 77  ? 11.59528  27.46351  39.62640  1.000 34.28406  ? 77  ARG B O   1 
ATOM   2010 C CB  . ARG B 2 77  ? 11.67777  27.14819  36.39008  1.000 19.63629  ? 77  ARG B CB  1 
ATOM   2011 C CG  . ARG B 2 77  ? 10.66431  28.19299  36.80376  1.000 27.37890  ? 77  ARG B CG  1 
ATOM   2012 C CD  . ARG B 2 77  ? 10.55337  29.28103  35.79730  1.000 23.81546  ? 77  ARG B CD  1 
ATOM   2013 N NE  . ARG B 2 77  ? 9.50101   30.23745  36.11727  1.000 50.39386  ? 77  ARG B NE  1 
ATOM   2014 C CZ  . ARG B 2 77  ? 9.71898   31.45875  36.58606  1.000 53.67807  ? 77  ARG B CZ  1 
ATOM   2015 N NH1 . ARG B 2 77  ? 10.94231  31.88990  36.85428  1.000 57.32791  ? 77  ARG B NH1 1 
ATOM   2016 N NH2 . ARG B 2 77  ? 8.68673   32.27427  36.77577  1.000 48.74762  ? 77  ARG B NH2 1 
ATOM   2017 N N   . VAL B 2 78  ? 10.82905  25.45913  38.97382  1.000 19.99388  ? 78  VAL B N   1 
ATOM   2018 C CA  . VAL B 2 78  ? 9.93053   25.37293  40.11747  1.000 24.83077  ? 78  VAL B CA  1 
ATOM   2019 C C   . VAL B 2 78  ? 10.62472  24.65673  41.26710  1.000 23.28311  ? 78  VAL B C   1 
ATOM   2020 O O   . VAL B 2 78  ? 10.84448  25.24323  42.33319  1.000 33.31941  ? 78  VAL B O   1 
ATOM   2021 C CB  . VAL B 2 78  ? 8.61115   24.67525  39.74386  1.000 32.06940  ? 78  VAL B CB  1 
ATOM   2022 C CG1 . VAL B 2 78  ? 7.71591   24.56526  40.96257  1.000 21.52029  ? 78  VAL B CG1 1 
ATOM   2023 C CG2 . VAL B 2 78  ? 7.90411   25.45436  38.65704  1.000 27.44877  ? 78  VAL B CG2 1 
ATOM   2024 N N   . CYS B 2 79  ? 10.98479  23.38971  41.05013  1.000 25.72363  ? 79  CYS B N   1 
ATOM   2025 C CA  . CYS B 2 79  ? 11.51910  22.56143  42.12862  1.000 29.24687  ? 79  CYS B CA  1 
ATOM   2026 C C   . CYS B 2 79  ? 12.78922  23.15863  42.72563  1.000 23.59560  ? 79  CYS B C   1 
ATOM   2027 O O   . CYS B 2 79  ? 12.91479  23.27514  43.94785  1.000 30.30623  ? 79  CYS B O   1 
ATOM   2028 C CB  . CYS B 2 79  ? 11.77698  21.14330  41.62167  1.000 18.90564  ? 79  CYS B CB  1 
ATOM   2029 S SG  . CYS B 2 79  ? 10.32090  20.33339  40.91840  1.000 26.10428  ? 79  CYS B SG  1 
ATOM   2030 N N   . ARG B 2 80  ? 13.74104  23.55860  41.88316  1.000 20.82355  ? 80  ARG B N   1 
ATOM   2031 C CA  . ARG B 2 80  ? 15.00441  24.05792  42.41890  1.000 20.31913  ? 80  ARG B CA  1 
ATOM   2032 C C   . ARG B 2 80  ? 14.84348  25.42634  43.07480  1.000 25.50910  ? 80  ARG B C   1 
ATOM   2033 O O   . ARG B 2 80  ? 15.47705  25.70404  44.09814  1.000 33.90745  ? 80  ARG B O   1 
ATOM   2034 C CB  . ARG B 2 80  ? 16.05845  24.09764  41.32135  1.000 24.57769  ? 80  ARG B CB  1 
ATOM   2035 C CG  . ARG B 2 80  ? 16.39618  22.71985  40.82804  1.000 32.30104  ? 80  ARG B CG  1 
ATOM   2036 C CD  . ARG B 2 80  ? 17.63580  22.74340  40.00345  1.000 29.89313  ? 80  ARG B CD  1 
ATOM   2037 N NE  . ARG B 2 80  ? 17.90192  21.44190  39.40952  1.000 36.69902  ? 80  ARG B NE  1 
ATOM   2038 C CZ  . ARG B 2 80  ? 18.76854  20.56559  39.89265  1.000 33.23105  ? 80  ARG B CZ  1 
ATOM   2039 N NH1 . ARG B 2 80  ? 19.49314  20.83321  40.96654  1.000 31.63132  ? 80  ARG B NH1 1 
ATOM   2040 N NH2 . ARG B 2 80  ? 18.91399  19.39414  39.28134  1.000 32.74075  ? 80  ARG B NH2 1 
ATOM   2041 N N   . HIS B 2 81  ? 14.00100  26.29322  42.51475  1.000 27.57887  ? 81  HIS B N   1 
ATOM   2042 C CA  . HIS B 2 81  ? 13.74268  27.57102  43.16945  1.000 33.12220  ? 81  HIS B CA  1 
ATOM   2043 C C   . HIS B 2 81  ? 13.11443  27.36196  44.54358  1.000 26.75120  ? 81  HIS B C   1 
ATOM   2044 O O   . HIS B 2 81  ? 13.51672  27.99375  45.52538  1.000 29.81761  ? 81  HIS B O   1 
ATOM   2045 C CB  . HIS B 2 81  ? 12.84387  28.44342  42.29180  1.000 20.46694  ? 81  HIS B CB  1 
ATOM   2046 C CG  . HIS B 2 81  ? 12.33876  29.67778  42.97521  1.000 29.45214  ? 81  HIS B CG  1 
ATOM   2047 N ND1 . HIS B 2 81  ? 12.88903  30.92383  42.76447  1.000 28.51137  ? 81  HIS B ND1 1 
ATOM   2048 C CD2 . HIS B 2 81  ? 11.32614  29.85959  43.85692  1.000 30.39043  ? 81  HIS B CD2 1 
ATOM   2049 C CE1 . HIS B 2 81  ? 12.24192  31.81896  43.49043  1.000 34.43465  ? 81  HIS B CE1 1 
ATOM   2050 N NE2 . HIS B 2 81  ? 11.29046  31.19878  44.16499  1.000 29.88100  ? 81  HIS B NE2 1 
ATOM   2051 N N   . ASN B 2 82  ? 12.11714  26.48027  44.63294  1.000 27.39624  ? 82  ASN B N   1 
ATOM   2052 C CA  . ASN B 2 82  ? 11.41494  26.31466  45.90063  1.000 26.58228  ? 82  ASN B CA  1 
ATOM   2053 C C   . ASN B 2 82  ? 12.27226  25.58336  46.92787  1.000 30.21572  ? 82  ASN B C   1 
ATOM   2054 O O   . ASN B 2 82  ? 12.16289  25.85809  48.12790  1.000 23.35591  ? 82  ASN B O   1 
ATOM   2055 C CB  . ASN B 2 82  ? 10.08884  25.58603  45.67810  1.000 24.57943  ? 82  ASN B CB  1 
ATOM   2056 C CG  . ASN B 2 82  ? 9.02952   26.47524  45.03474  1.000 27.33845  ? 82  ASN B CG  1 
ATOM   2057 O OD1 . ASN B 2 82  ? 9.28794   27.62996  44.69064  1.000 24.05210  ? 82  ASN B OD1 1 
ATOM   2058 N ND2 . ASN B 2 82  ? 7.82974   25.93353  44.86898  1.000 17.32037  ? 82  ASN B ND2 1 
ATOM   2059 N N   . TYR B 2 83  ? 13.14117  24.67226  46.48318  1.000 26.22928  ? 83  TYR B N   1 
ATOM   2060 C CA  . TYR B 2 83  ? 14.02532  23.98697  47.41934  1.000 24.27521  ? 83  TYR B CA  1 
ATOM   2061 C C   . TYR B 2 83  ? 14.93845  24.97385  48.13888  1.000 30.67924  ? 83  TYR B C   1 
ATOM   2062 O O   . TYR B 2 83  ? 15.18547  24.83396  49.34294  1.000 30.06772  ? 83  TYR B O   1 
ATOM   2063 C CB  . TYR B 2 83  ? 14.84621  22.92785  46.68705  1.000 25.25591  ? 83  TYR B CB  1 
ATOM   2064 C CG  . TYR B 2 83  ? 15.55812  21.96019  47.60504  1.000 27.66428  ? 83  TYR B CG  1 
ATOM   2065 C CD1 . TYR B 2 83  ? 14.89426  20.85861  48.13536  1.000 32.76959  ? 83  TYR B CD1 1 
ATOM   2066 C CD2 . TYR B 2 83  ? 16.89474  22.14009  47.93741  1.000 32.43408  ? 83  TYR B CD2 1 
ATOM   2067 C CE1 . TYR B 2 83  ? 15.54215  19.96680  48.97619  1.000 28.38105  ? 83  TYR B CE1 1 
ATOM   2068 C CE2 . TYR B 2 83  ? 17.55050  21.25058  48.77500  1.000 31.12985  ? 83  TYR B CE2 1 
ATOM   2069 C CZ  . TYR B 2 83  ? 16.86760  20.16769  49.29075  1.000 25.63948  ? 83  TYR B CZ  1 
ATOM   2070 O OH  . TYR B 2 83  ? 17.51488  19.28142  50.12277  1.000 26.04559  ? 83  TYR B OH  1 
ATOM   2071 N N   . GLN B 2 84  ? 15.44623  25.98251  47.41915  1.000 25.99890  ? 84  GLN B N   1 
ATOM   2072 C CA  . GLN B 2 84  ? 16.25553  27.01281  48.06314  1.000 30.08265  ? 84  GLN B CA  1 
ATOM   2073 C C   . GLN B 2 84  ? 15.46754  27.72170  49.15563  1.000 31.22228  ? 84  GLN B C   1 
ATOM   2074 O O   . GLN B 2 84  ? 16.02558  28.08567  50.19749  1.000 28.46356  ? 84  GLN B O   1 
ATOM   2075 C CB  . GLN B 2 84  ? 16.76120  28.02129  47.03155  1.000 20.36522  ? 84  GLN B CB  1 
ATOM   2076 C CG  . GLN B 2 84  ? 17.69440  27.43224  45.98526  1.000 36.65762  ? 84  GLN B CG  1 
ATOM   2077 C CD  . GLN B 2 84  ? 18.96137  26.83982  46.58631  1.000 38.00266  ? 84  GLN B CD  1 
ATOM   2078 O OE1 . GLN B 2 84  ? 19.73604  27.53461  47.24091  1.000 44.89565  ? 84  GLN B OE1 1 
ATOM   2079 N NE2 . GLN B 2 84  ? 19.17419  25.54827  46.36391  1.000 45.81144  ? 84  GLN B NE2 1 
ATOM   2080 N N   . LEU B 2 85  ? 14.16710  27.92816  48.93412  1.000 29.56581  ? 85  LEU B N   1 
ATOM   2081 C CA  . LEU B 2 85  ? 13.31918  28.46571  49.99096  1.000 31.39662  ? 85  LEU B CA  1 
ATOM   2082 C C   . LEU B 2 85  ? 13.16155  27.46528  51.12960  1.000 27.91590  ? 85  LEU B C   1 
ATOM   2083 O O   . LEU B 2 85  ? 13.09348  27.85519  52.30060  1.000 29.67574  ? 85  LEU B O   1 
ATOM   2084 C CB  . LEU B 2 85  ? 11.95226  28.85419  49.42789  1.000 26.30917  ? 85  LEU B CB  1 
ATOM   2085 C CG  . LEU B 2 85  ? 11.91603  29.84372  48.26323  1.000 30.79402  ? 85  LEU B CG  1 
ATOM   2086 C CD1 . LEU B 2 85  ? 10.48910  30.29480  48.00822  1.000 23.17926  ? 85  LEU B CD1 1 
ATOM   2087 C CD2 . LEU B 2 85  ? 12.82203  31.03927  48.51611  1.000 28.69903  ? 85  LEU B CD2 1 
ATOM   2088 N N   . GLU B 2 86  ? 13.09785  26.17114  50.80789  1.000 27.14071  ? 86  GLU B N   1 
ATOM   2089 C CA  . GLU B 2 86  ? 12.98460  25.16026  51.85320  1.000 26.28846  ? 86  GLU B CA  1 
ATOM   2090 C C   . GLU B 2 86  ? 14.24944  25.10033  52.70376  1.000 31.10104  ? 86  GLU B C   1 
ATOM   2091 O O   . GLU B 2 86  ? 14.17647  24.87204  53.91763  1.000 29.97634  ? 86  GLU B O   1 
ATOM   2092 C CB  . GLU B 2 86  ? 12.68694  23.79182  51.23872  1.000 23.51764  ? 86  GLU B CB  1 
ATOM   2093 C CG  . GLU B 2 86  ? 11.51895  23.74911  50.24196  1.000 28.65100  ? 86  GLU B CG  1 
ATOM   2094 C CD  . GLU B 2 86  ? 10.15801  24.06655  50.85233  1.000 29.65708  ? 86  GLU B CD  1 
ATOM   2095 O OE1 . GLU B 2 86  ? 10.05098  24.20463  52.08674  1.000 28.78621  ? 86  GLU B OE1 1 
ATOM   2096 O OE2 . GLU B 2 86  ? 9.17905   24.17525  50.08393  1.000 32.21781  ? 86  GLU B OE2 1 
ATOM   2097 N N   . LEU B 2 87  ? 15.41859  25.31083  52.08307  1.000 31.78789  ? 87  LEU B N   1 
ATOM   2098 C CA  . LEU B 2 87  ? 16.68507  25.29204  52.81380  1.000 27.23074  ? 87  LEU B CA  1 
ATOM   2099 C C   . LEU B 2 87  ? 16.73278  26.36065  53.89525  1.000 30.71928  ? 87  LEU B C   1 
ATOM   2100 O O   . LEU B 2 87  ? 17.38782  26.16818  54.92473  1.000 39.65597  ? 87  LEU B O   1 
ATOM   2101 C CB  . LEU B 2 87  ? 17.85725  25.48060  51.84672  1.000 27.27373  ? 87  LEU B CB  1 
ATOM   2102 C CG  . LEU B 2 87  ? 18.29722  24.27841  51.01182  1.000 31.40989  ? 87  LEU B CG  1 
ATOM   2103 C CD1 . LEU B 2 87  ? 19.27050  24.72340  49.93278  1.000 31.97346  ? 87  LEU B CD1 1 
ATOM   2104 C CD2 . LEU B 2 87  ? 18.93665  23.22215  51.89646  1.000 26.75037  ? 87  LEU B CD2 1 
ATOM   2105 N N   . ARG B 2 88  ? 16.05152  27.48498  53.68305  1.000 29.44383  ? 88  ARG B N   1 
ATOM   2106 C CA  . ARG B 2 88  ? 15.99904  28.57471  54.64879  1.000 35.21733  ? 88  ARG B CA  1 
ATOM   2107 C C   . ARG B 2 88  ? 14.88990  28.41587  55.68541  1.000 36.63743  ? 88  ARG B C   1 
ATOM   2108 O O   . ARG B 2 88  ? 14.87391  29.16179  56.66999  1.000 39.54719  ? 88  ARG B O   1 
ATOM   2109 C CB  . ARG B 2 88  ? 15.80015  29.91020  53.92199  1.000 36.49052  ? 88  ARG B CB  1 
ATOM   2110 C CG  . ARG B 2 88  ? 16.87151  30.25228  52.90628  1.000 52.17716  ? 88  ARG B CG  1 
ATOM   2111 C CD  . ARG B 2 88  ? 16.33288  31.23843  51.87634  1.000 50.34091  ? 88  ARG B CD  1 
ATOM   2112 N NE  . ARG B 2 88  ? 15.53412  32.28682  52.49992  1.000 54.47315  ? 88  ARG B NE  1 
ATOM   2113 C CZ  . ARG B 2 88  ? 14.94919  33.27599  51.83841  1.000 53.32736  ? 88  ARG B CZ  1 
ATOM   2114 N NH1 . ARG B 2 88  ? 15.05590  33.38566  50.52381  1.000 59.98639  ? 88  ARG B NH1 1 
ATOM   2115 N NH2 . ARG B 2 88  ? 14.24247  34.17963  52.51307  1.000 58.44162  ? 88  ARG B NH2 1 
ATOM   2116 N N   . THR B 2 89  ? 13.95717  27.48498  55.48811  1.000 35.51682  ? 89  THR B N   1 
ATOM   2117 C CA  . THR B 2 89  ? 12.77546  27.41559  56.34002  1.000 27.18608  ? 89  THR B CA  1 
ATOM   2118 C C   . THR B 2 89  ? 12.50020  25.98950  56.80644  1.000 33.63993  ? 89  THR B C   1 
ATOM   2119 O O   . THR B 2 89  ? 12.99930  25.56801  57.85639  1.000 29.47808  ? 89  THR B O   1 
ATOM   2120 C CB  . THR B 2 89  ? 11.55335  27.97163  55.59704  1.000 31.06854  ? 89  THR B CB  1 
ATOM   2121 O OG1 . THR B 2 89  ? 11.38044  27.26736  54.36150  1.000 28.16278  ? 89  THR B OG1 1 
ATOM   2122 C CG2 . THR B 2 89  ? 11.72477  29.45447  55.29722  1.000 24.53755  ? 89  THR B CG2 1 
ATOM   2123 N N   . THR B 2 90  ? 11.71033  25.24486  56.02278  1.000 28.76932  ? 90  THR B N   1 
ATOM   2124 C CA  . THR B 2 90  ? 11.30758  23.89414  56.40743  1.000 24.55032  ? 90  THR B CA  1 
ATOM   2125 C C   . THR B 2 90  ? 12.50357  23.00859  56.73550  1.000 26.37126  ? 90  THR B C   1 
ATOM   2126 O O   . THR B 2 90  ? 12.49265  22.28584  57.73989  1.000 27.93124  ? 90  THR B O   1 
ATOM   2127 C CB  . THR B 2 90  ? 10.48367  23.25556  55.28872  1.000 26.27626  ? 90  THR B CB  1 
ATOM   2128 O OG1 . THR B 2 90  ? 11.24783  23.25783  54.07421  1.000 26.78898  ? 90  THR B OG1 1 
ATOM   2129 C CG2 . THR B 2 90  ? 9.18123   24.01303  55.08420  1.000 21.38339  ? 90  THR B CG2 1 
ATOM   2130 N N   . LEU B 2 91  ? 13.54326  23.04252  55.89738  1.000 26.76150  ? 91  LEU B N   1 
ATOM   2131 C CA  . LEU B 2 91  ? 14.68898  22.16451  56.11096  1.000 28.78723  ? 91  LEU B CA  1 
ATOM   2132 C C   . LEU B 2 91  ? 15.57336  22.61995  57.26191  1.000 29.34510  ? 91  LEU B C   1 
ATOM   2133 O O   . LEU B 2 91  ? 16.48258  21.87989  57.64823  1.000 31.62585  ? 91  LEU B O   1 
ATOM   2134 C CB  . LEU B 2 91  ? 15.51332  22.04726  54.82716  1.000 23.44771  ? 91  LEU B CB  1 
ATOM   2135 C CG  . LEU B 2 91  ? 14.80496  21.27572  53.71291  1.000 25.49184  ? 91  LEU B CG  1 
ATOM   2136 C CD1 . LEU B 2 91  ? 15.61731  21.26499  52.43018  1.000 31.26050  ? 91  LEU B CD1 1 
ATOM   2137 C CD2 . LEU B 2 91  ? 14.49950  19.84825  54.17311  1.000 26.06206  ? 91  LEU B CD2 1 
ATOM   2138 N N   . GLN B 2 92  ? 15.32840  23.80365  57.81889  1.000 27.17308  ? 92  GLN B N   1 
ATOM   2139 C CA  . GLN B 2 92  ? 16.03559  24.27631  58.99803  1.000 27.35979  ? 92  GLN B CA  1 
ATOM   2140 C C   . GLN B 2 92  ? 15.22461  24.10575  60.27341  1.000 39.48693  ? 92  GLN B C   1 
ATOM   2141 O O   . GLN B 2 92  ? 15.71981  24.43188  61.35633  1.000 43.77356  ? 92  GLN B O   1 
ATOM   2142 C CB  . GLN B 2 92  ? 16.42169  25.74927  58.83221  1.000 30.24604  ? 92  GLN B CB  1 
ATOM   2143 C CG  . GLN B 2 92  ? 17.80838  25.97401  58.24718  1.000 53.56235  ? 92  GLN B CG  1 
ATOM   2144 C CD  . GLN B 2 92  ? 18.24886  27.42332  58.35405  1.000 72.94152  ? 92  GLN B CD  1 
ATOM   2145 O OE1 . GLN B 2 92  ? 17.56355  28.24616  58.96404  1.000 71.19144  ? 92  GLN B OE1 1 
ATOM   2146 N NE2 . GLN B 2 92  ? 19.39653  27.74321  57.76187  1.000 74.38966  ? 92  GLN B NE2 1 
ATOM   2147 N N   . ARG B 2 93  ? 13.99705  23.60686  60.17311  1.000 30.44971  ? 93  ARG B N   1 
ATOM   2148 C CA  . ARG B 2 93  ? 13.14112  23.46297  61.34058  1.000 30.71750  ? 93  ARG B CA  1 
ATOM   2149 C C   . ARG B 2 93  ? 13.66019  22.34822  62.24629  1.000 40.16591  ? 93  ARG B C   1 
ATOM   2150 O O   . ARG B 2 93  ? 13.78122  21.19281  61.82232  1.000 27.87854  ? 93  ARG B O   1 
ATOM   2151 C CB  . ARG B 2 93  ? 11.70992  23.18663  60.89594  1.000 30.18258  ? 93  ARG B CB  1 
ATOM   2152 C CG  . ARG B 2 93  ? 10.72625  23.00581  62.02298  1.000 30.58675  ? 93  ARG B CG  1 
ATOM   2153 C CD  . ARG B 2 93  ? 9.32289   22.91417  61.46434  1.000 25.69549  ? 93  ARG B CD  1 
ATOM   2154 N NE  . ARG B 2 93  ? 8.36828   22.45347  62.46108  1.000 30.09123  ? 93  ARG B NE  1 
ATOM   2155 C CZ  . ARG B 2 93  ? 7.81931   23.23748  63.37541  1.000 27.24559  ? 93  ARG B CZ  1 
ATOM   2156 N NH1 . ARG B 2 93  ? 8.14043   24.51810  63.46583  1.000 25.86773  ? 93  ARG B NH1 1 
ATOM   2157 N NH2 . ARG B 2 93  ? 6.91983   22.72730  64.21275  1.000 20.10441  ? 93  ARG B NH2 1 
ATOM   2158 N N   . ARG B 2 94  ? 13.96925  22.70303  63.49442  1.000 39.06801  ? 94  ARG B N   1 
ATOM   2159 C CA  . ARG B 2 94  ? 14.46567  21.76950  64.50068  1.000 31.68574  ? 94  ARG B CA  1 
ATOM   2160 C C   . ARG B 2 94  ? 13.63009  21.94233  65.76064  1.000 34.39398  ? 94  ARG B C   1 
ATOM   2161 O O   . ARG B 2 94  ? 13.74444  22.96094  66.45002  1.000 43.05111  ? 94  ARG B O   1 
ATOM   2162 C CB  . ARG B 2 94  ? 15.94398  22.01340  64.80288  1.000 32.70453  ? 94  ARG B CB  1 
ATOM   2163 C CG  . ARG B 2 94  ? 16.87404  21.80312  63.62745  1.000 34.11143  ? 94  ARG B CG  1 
ATOM   2164 C CD  . ARG B 2 94  ? 16.97687  20.33970  63.26306  1.000 30.41275  ? 94  ARG B CD  1 
ATOM   2165 N NE  . ARG B 2 94  ? 18.06998  20.10935  62.32955  1.000 47.25435  ? 94  ARG B NE  1 
ATOM   2166 C CZ  . ARG B 2 94  ? 17.96012  20.22318  61.01410  1.000 53.00544  ? 94  ARG B CZ  1 
ATOM   2167 N NH1 . ARG B 2 94  ? 16.80987  20.54155  60.44323  1.000 40.08354  ? 94  ARG B NH1 1 
ATOM   2168 N NH2 . ARG B 2 94  ? 19.03115  20.01637  60.25314  1.000 48.37307  ? 94  ARG B NH2 1 
ATOM   2169 N N   . VAL B 2 95  ? 12.79216  20.95763  66.06019  1.000 29.90421  ? 95  VAL B N   1 
ATOM   2170 C CA  . VAL B 2 95  ? 11.96310  20.96261  67.25943  1.000 28.53176  ? 95  VAL B CA  1 
ATOM   2171 C C   . VAL B 2 95  ? 12.37621  19.75492  68.08411  1.000 34.01960  ? 95  VAL B C   1 
ATOM   2172 O O   . VAL B 2 95  ? 12.18149  18.60940  67.65684  1.000 35.25677  ? 95  VAL B O   1 
ATOM   2173 C CB  . VAL B 2 95  ? 10.46531  20.93063  66.93023  1.000 27.04788  ? 95  VAL B CB  1 
ATOM   2174 C CG1 . VAL B 2 95  ? 9.63946   20.86054  68.20726  1.000 27.43943  ? 95  VAL B CG1 1 
ATOM   2175 C CG2 . VAL B 2 95  ? 10.08026  22.15886  66.11815  1.000 25.35010  ? 95  VAL B CG2 1 
ATOM   2176 N N   . GLU B 2 96  ? 12.95642  20.00787  69.25474  1.000 38.24003  ? 96  GLU B N   1 
ATOM   2177 C CA  . GLU B 2 96  ? 13.48628  18.92962  70.07489  1.000 31.03580  ? 96  GLU B CA  1 
ATOM   2178 C C   . GLU B 2 96  ? 12.35075  18.09293  70.66012  1.000 25.80729  ? 96  GLU B C   1 
ATOM   2179 O O   . GLU B 2 96  ? 11.33793  18.63871  71.11211  1.000 27.93159  ? 96  GLU B O   1 
ATOM   2180 C CB  . GLU B 2 96  ? 14.34599  19.48502  71.20628  1.000 44.47319  ? 96  GLU B CB  1 
ATOM   2181 C CG  . GLU B 2 96  ? 15.49216  20.36934  70.76207  1.000 49.03690  ? 96  GLU B CG  1 
ATOM   2182 C CD  . GLU B 2 96  ? 16.24432  20.94706  71.94025  1.000 51.70860  ? 96  GLU B CD  1 
ATOM   2183 O OE1 . GLU B 2 96  ? 16.74969  20.15889  72.76478  1.000 61.71807  ? 96  GLU B OE1 1 
ATOM   2184 O OE2 . GLU B 2 96  ? 16.30943  22.18832  72.05515  1.000 72.79854  ? 96  GLU B OE2 1 
ATOM   2185 N N   . PRO B 2 97  ? 12.48654  16.77354  70.66576  1.000 25.29347  ? 97  PRO B N   1 
ATOM   2186 C CA  . PRO B 2 97  ? 11.43081  15.92952  71.23289  1.000 33.06472  ? 97  PRO B CA  1 
ATOM   2187 C C   . PRO B 2 97  ? 11.35479  16.03369  72.74883  1.000 37.01582  ? 97  PRO B C   1 
ATOM   2188 O O   . PRO B 2 97  ? 12.35696  16.21885  73.44383  1.000 38.60482  ? 97  PRO B O   1 
ATOM   2189 C CB  . PRO B 2 97  ? 11.83278  14.51487  70.79897  1.000 26.49690  ? 97  PRO B CB  1 
ATOM   2190 C CG  . PRO B 2 97  ? 13.29717  14.60491  70.50215  1.000 32.65428  ? 97  PRO B CG  1 
ATOM   2191 C CD  . PRO B 2 97  ? 13.52555  15.98987  69.97878  1.000 27.46463  ? 97  PRO B CD  1 
ATOM   2192 N N   . THR B 2 98  ? 10.13299  15.91346  73.25444  1.000 36.90461  ? 98  THR B N   1 
ATOM   2193 C CA  . THR B 2 98  ? 9.87140   15.75467  74.67626  1.000 24.37706  ? 98  THR B CA  1 
ATOM   2194 C C   . THR B 2 98  ? 9.75491   14.26344  74.96329  1.000 27.63196  ? 98  THR B C   1 
ATOM   2195 O O   . THR B 2 98  ? 8.91552   13.57890  74.36846  1.000 32.41918  ? 98  THR B O   1 
ATOM   2196 C CB  . THR B 2 98  ? 8.59537   16.49278  75.07680  1.000 38.35691  ? 98  THR B CB  1 
ATOM   2197 O OG1 . THR B 2 98  ? 8.75772   17.89394  74.81615  1.000 43.70727  ? 98  THR B OG1 1 
ATOM   2198 C CG2 . THR B 2 98  ? 8.28317   16.27957  76.55493  1.000 21.97163  ? 98  THR B CG2 1 
ATOM   2199 N N   . VAL B 2 99  ? 10.60530  13.76311  75.85548  1.000 27.02659  ? 99  VAL B N   1 
ATOM   2200 C CA  . VAL B 2 99  ? 10.70245  12.33983  76.15793  1.000 37.81257  ? 99  VAL B CA  1 
ATOM   2201 C C   . VAL B 2 99  ? 10.14915  12.10209  77.55642  1.000 32.77234  ? 99  VAL B C   1 
ATOM   2202 O O   . VAL B 2 99  ? 10.55946  12.76628  78.51564  1.000 31.02002  ? 99  VAL B O   1 
ATOM   2203 C CB  . VAL B 2 99  ? 12.15310  11.83976  76.04100  1.000 34.14432  ? 99  VAL B CB  1 
ATOM   2204 C CG1 . VAL B 2 99  ? 12.21845  10.33021  76.21408  1.000 25.37555  ? 99  VAL B CG1 1 
ATOM   2205 C CG2 . VAL B 2 99  ? 12.73589  12.25553  74.70788  1.000 23.49705  ? 99  VAL B CG2 1 
ATOM   2206 N N   . THR B 2 100 ? 9.23457   11.13884  77.66974  1.000 30.98482  ? 100 THR B N   1 
ATOM   2207 C CA  . THR B 2 100 ? 8.47421   10.88510  78.88681  1.000 27.73709  ? 100 THR B CA  1 
ATOM   2208 C C   . THR B 2 100 ? 8.27604   9.38607   79.04803  1.000 26.28646  ? 100 THR B C   1 
ATOM   2209 O O   . THR B 2 100 ? 7.88947   8.70762   78.09414  1.000 29.36738  ? 100 THR B O   1 
ATOM   2210 C CB  . THR B 2 100 ? 7.11641   11.60222  78.82831  1.000 31.06433  ? 100 THR B CB  1 
ATOM   2211 O OG1 . THR B 2 100 ? 7.26861   12.95066  79.28675  1.000 44.09751  ? 100 THR B OG1 1 
ATOM   2212 C CG2 . THR B 2 100 ? 6.07363   10.89189  79.67297  1.000 42.00348  ? 100 THR B CG2 1 
ATOM   2213 N N   . ILE B 2 101 ? 8.54585   8.86786   80.24376  1.000 29.65943  ? 101 ILE B N   1 
ATOM   2214 C CA  . ILE B 2 101 ? 8.30871   7.46403   80.56227  1.000 35.35848  ? 101 ILE B CA  1 
ATOM   2215 C C   . ILE B 2 101 ? 7.14017   7.38144   81.53026  1.000 34.04224  ? 101 ILE B C   1 
ATOM   2216 O O   . ILE B 2 101 ? 7.05098   8.16897   82.47836  1.000 42.47978  ? 101 ILE B O   1 
ATOM   2217 C CB  . ILE B 2 101 ? 9.54979   6.77826   81.16393  1.000 32.56115  ? 101 ILE B CB  1 
ATOM   2218 C CG1 . ILE B 2 101 ? 10.74772  6.89712   80.22414  1.000 29.10335  ? 101 ILE B CG1 1 
ATOM   2219 C CG2 . ILE B 2 101 ? 9.25683   5.31427   81.44825  1.000 28.50320  ? 101 ILE B CG2 1 
ATOM   2220 C CD1 . ILE B 2 101 ? 11.99918  6.23572   80.76675  1.000 27.40468  ? 101 ILE B CD1 1 
ATOM   2221 N N   . SER B 2 102 ? 6.23741   6.43054   81.28571  1.000 36.88061  ? 102 SER B N   1 
ATOM   2222 C CA  . SER B 2 102 ? 5.15526   6.17532   82.21206  1.000 42.32802  ? 102 SER B CA  1 
ATOM   2223 C C   . SER B 2 102 ? 4.87180   4.68144   82.17453  1.000 38.63862  ? 102 SER B C   1 
ATOM   2224 O O   . SER B 2 102 ? 4.80055   4.10593   81.07741  1.000 45.33895  ? 102 SER B O   1 
ATOM   2225 C CB  . SER B 2 102 ? 3.88976   6.96148   81.87550  1.000 33.62506  ? 102 SER B CB  1 
ATOM   2226 O OG  . SER B 2 102 ? 3.41296   6.62418   80.58796  1.000 60.21977  ? 102 SER B OG  1 
ATOM   2227 N N   . PRO B 2 103 ? 4.72206   4.03543   83.32449  1.000 47.39624  ? 103 PRO B N   1 
ATOM   2228 C CA  . PRO B 2 103 ? 4.43036   2.60072   83.34143  1.000 45.22623  ? 103 PRO B CA  1 
ATOM   2229 C C   . PRO B 2 103 ? 2.97918   2.33219   82.96379  1.000 59.88060  ? 103 PRO B C   1 
ATOM   2230 O O   . PRO B 2 103 ? 2.13307   3.22616   82.93039  1.000 58.57128  ? 103 PRO B O   1 
ATOM   2231 C CB  . PRO B 2 103 ? 4.71407   2.20061   84.79161  1.000 46.28549  ? 103 PRO B CB  1 
ATOM   2232 C CG  . PRO B 2 103 ? 4.43576   3.44488   85.57109  1.000 46.27604  ? 103 PRO B CG  1 
ATOM   2233 C CD  . PRO B 2 103 ? 4.83683   4.59544   84.68324  1.000 52.02264  ? 103 PRO B CD  1 
ATOM   2234 N N   . SER B 2 104 ? 2.70613   1.06549   82.67270  1.000 61.13690  ? 104 SER B N   1 
ATOM   2235 C CA  . SER B 2 104 ? 1.38291   0.63704   82.24347  1.000 68.70747  ? 104 SER B CA  1 
ATOM   2236 C C   . SER B 2 104 ? 1.15536   -0.78302  82.74954  1.000 78.53352  ? 104 SER B C   1 
ATOM   2237 O O   . SER B 2 104 ? 1.92606   -1.30099  83.56402  1.000 80.58302  ? 104 SER B O   1 
ATOM   2238 C CB  . SER B 2 104 ? 1.25638   0.74621   80.71866  1.000 58.43258  ? 104 SER B CB  1 
ATOM   2239 O OG  . SER B 2 104 ? -0.04026  0.38191   80.28613  1.000 65.04221  ? 104 SER B OG  1 
ATOM   2240 N N   . ARG B 2 105 ? 0.08743   -1.41395  82.26675  1.000 84.77768  ? 105 ARG B N   1 
ATOM   2241 C CA  . ARG B 2 105 ? -0.22264  -2.78858  82.63318  1.000 83.63168  ? 105 ARG B CA  1 
ATOM   2242 C C   . ARG B 2 105 ? -1.13552  -3.37743  81.56870  1.000 87.78288  ? 105 ARG B C   1 
ATOM   2243 O O   . ARG B 2 105 ? -1.99871  -2.67929  81.03121  1.000 104.10174 ? 105 ARG B O   1 
ATOM   2244 C CB  . ARG B 2 105 ? -0.88447  -2.87133  84.01645  1.000 68.35189  ? 105 ARG B CB  1 
ATOM   2245 N N   . THR B 2 106 ? -0.93604  -4.65607  81.26715  1.000 90.80221  ? 106 THR B N   1 
ATOM   2246 C CA  . THR B 2 106 ? -1.75726  -5.34176  80.27409  1.000 88.03097  ? 106 THR B CA  1 
ATOM   2247 C C   . THR B 2 106 ? -2.33115  -6.64544  80.82261  1.000 95.99557  ? 106 THR B C   1 
ATOM   2248 O O   . THR B 2 106 ? -2.70468  -6.72892  81.99375  1.000 97.95157  ? 106 THR B O   1 
ATOM   2249 C CB  . THR B 2 106 ? -0.95672  -5.64343  78.99702  1.000 82.34837  ? 106 THR B CB  1 
ATOM   2250 O OG1 . THR B 2 106 ? 0.33303   -6.15751  79.35149  1.000 77.29363  ? 106 THR B OG1 1 
ATOM   2251 C CG2 . THR B 2 106 ? -0.79145  -4.38271  78.16034  1.000 79.73833  ? 106 THR B CG2 1 
ATOM   2252 N N   . HIS B 2 112 ? 3.22595   -3.75853  87.75401  1.000 84.60593  ? 112 HIS B N   1 
ATOM   2253 C CA  . HIS B 2 112 ? 3.66184   -3.13306  86.50846  1.000 81.58833  ? 112 HIS B CA  1 
ATOM   2254 C C   . HIS B 2 112 ? 4.37932   -4.13041  85.59932  1.000 66.99631  ? 112 HIS B C   1 
ATOM   2255 O O   . HIS B 2 112 ? 5.16404   -4.95514  86.06580  1.000 62.27348  ? 112 HIS B O   1 
ATOM   2256 C CB  . HIS B 2 112 ? 4.57746   -1.94035  86.79996  1.000 70.03735  ? 112 HIS B CB  1 
ATOM   2257 C CG  . HIS B 2 112 ? 3.85518   -0.72821  87.30088  1.000 74.76425  ? 112 HIS B CG  1 
ATOM   2258 N ND1 . HIS B 2 112 ? 4.44311   0.19386   88.14115  1.000 77.08677  ? 112 HIS B ND1 1 
ATOM   2259 C CD2 . HIS B 2 112 ? 2.59814   -0.27956  87.07015  1.000 72.78209  ? 112 HIS B CD2 1 
ATOM   2260 C CE1 . HIS B 2 112 ? 3.57720   1.15471   88.41140  1.000 75.58630  ? 112 HIS B CE1 1 
ATOM   2261 N NE2 . HIS B 2 112 ? 2.44979   0.89100   87.77449  1.000 64.93833  ? 112 HIS B NE2 1 
ATOM   2262 N N   . ASN B 2 113 ? 4.10157   -4.04823  84.29315  1.000 67.72536  ? 113 ASN B N   1 
ATOM   2263 C CA  . ASN B 2 113 ? 4.78504   -4.91489  83.33901  1.000 59.12334  ? 113 ASN B CA  1 
ATOM   2264 C C   . ASN B 2 113 ? 4.99206   -4.25726  81.97843  1.000 49.54737  ? 113 ASN B C   1 
ATOM   2265 O O   . ASN B 2 113 ? 5.32239   -4.96764  81.01925  1.000 39.47403  ? 113 ASN B O   1 
ATOM   2266 C CB  . ASN B 2 113 ? 4.01339   -6.22746  83.15006  1.000 50.58076  ? 113 ASN B CB  1 
ATOM   2267 C CG  . ASN B 2 113 ? 2.75878   -6.04979  82.31622  1.000 65.85410  ? 113 ASN B CG  1 
ATOM   2268 O OD1 . ASN B 2 113 ? 2.11903   -4.99832  82.35262  1.000 72.90122  ? 113 ASN B OD1 1 
ATOM   2269 N ND2 . ASN B 2 113 ? 2.40226   -7.07855  81.55554  1.000 58.57706  ? 113 ASN B ND2 1 
ATOM   2270 N N   . LEU B 2 114 ? 4.82244   -2.94236  81.85411  1.000 48.25284  ? 114 LEU B N   1 
ATOM   2271 C CA  . LEU B 2 114 ? 4.92245   -2.28032  80.56150  1.000 52.46043  ? 114 LEU B CA  1 
ATOM   2272 C C   . LEU B 2 114 ? 5.37742   -0.84150  80.75887  1.000 44.31886  ? 114 LEU B C   1 
ATOM   2273 O O   . LEU B 2 114 ? 4.76783   -0.09934  81.53327  1.000 40.89904  ? 114 LEU B O   1 
ATOM   2274 C CB  . LEU B 2 114 ? 3.57419   -2.32138  79.83396  1.000 59.80401  ? 114 LEU B CB  1 
ATOM   2275 C CG  . LEU B 2 114 ? 3.51526   -1.69519  78.44248  1.000 61.95071  ? 114 LEU B CG  1 
ATOM   2276 C CD1 . LEU B 2 114 ? 4.47500   -2.40876  77.50531  1.000 49.17582  ? 114 LEU B CD1 1 
ATOM   2277 C CD2 . LEU B 2 114 ? 2.09302   -1.74068  77.90719  1.000 60.57293  ? 114 LEU B CD2 1 
ATOM   2278 N N   . LEU B 2 115 ? 6.43875   -0.45145  80.05748  1.000 41.54051  ? 115 LEU B N   1 
ATOM   2279 C CA  . LEU B 2 115 ? 6.93381   0.92059   80.06520  1.000 43.01628  ? 115 LEU B CA  1 
ATOM   2280 C C   . LEU B 2 115 ? 6.63921   1.57410   78.72372  1.000 42.40136  ? 115 LEU B C   1 
ATOM   2281 O O   . LEU B 2 115 ? 6.94861   1.00557   77.67240  1.000 32.84577  ? 115 LEU B O   1 
ATOM   2282 C CB  . LEU B 2 115 ? 8.43753   0.97030   80.34244  1.000 33.60571  ? 115 LEU B CB  1 
ATOM   2283 C CG  . LEU B 2 115 ? 8.85335   0.65790   81.77777  1.000 41.41636  ? 115 LEU B CG  1 
ATOM   2284 C CD1 . LEU B 2 115 ? 10.36159  0.78826   81.93402  1.000 30.02720  ? 115 LEU B CD1 1 
ATOM   2285 C CD2 . LEU B 2 115 ? 8.12178   1.56547   82.75916  1.000 34.33233  ? 115 LEU B CD2 1 
ATOM   2286 N N   . VAL B 2 116 ? 6.05931   2.76763   78.75952  1.000 35.76482  ? 116 VAL B N   1 
ATOM   2287 C CA  . VAL B 2 116 ? 5.74549   3.51767   77.55188  1.000 34.82285  ? 116 VAL B CA  1 
ATOM   2288 C C   . VAL B 2 116 ? 6.63500   4.74909   77.52109  1.000 31.15240  ? 116 VAL B C   1 
ATOM   2289 O O   . VAL B 2 116 ? 6.50466   5.64567   78.36569  1.000 31.49137  ? 116 VAL B O   1 
ATOM   2290 C CB  . VAL B 2 116 ? 4.26517   3.90869   77.48333  1.000 36.38563  ? 116 VAL B CB  1 
ATOM   2291 C CG1 . VAL B 2 116 ? 4.00863   4.75476   76.23744  1.000 34.08711  ? 116 VAL B CG1 1 
ATOM   2292 C CG2 . VAL B 2 116 ? 3.39409   2.66911   77.48659  1.000 35.84975  ? 116 VAL B CG2 1 
ATOM   2293 N N   . CYS B 2 117 ? 7.53590   4.79944   76.54458  1.000 30.63901  ? 117 CYS B N   1 
ATOM   2294 C CA  . CYS B 2 117 ? 8.33317   5.99237   76.30054  1.000 33.01651  ? 117 CYS B CA  1 
ATOM   2295 C C   . CYS B 2 117 ? 7.62505   6.82973   75.24328  1.000 31.26467  ? 117 CYS B C   1 
ATOM   2296 O O   . CYS B 2 117 ? 7.55495   6.43710   74.07299  1.000 28.60472  ? 117 CYS B O   1 
ATOM   2297 C CB  . CYS B 2 117 ? 9.74975   5.63208   75.86491  1.000 39.30613  ? 117 CYS B CB  1 
ATOM   2298 S SG  . CYS B 2 117 ? 10.78798  7.09364   75.67483  1.000 36.12714  ? 117 CYS B SG  1 
ATOM   2299 N N   . SER B 2 118 ? 7.08799   7.97309   75.66285  1.000 31.00168  ? 118 SER B N   1 
ATOM   2300 C CA  . SER B 2 118 ? 6.40732   8.90267   74.77053  1.000 26.97897  ? 118 SER B CA  1 
ATOM   2301 C C   . SER B 2 118 ? 7.41396   9.92122   74.25581  1.000 32.58041  ? 118 SER B C   1 
ATOM   2302 O O   . SER B 2 118 ? 8.02384   10.64937  75.04551  1.000 25.21768  ? 118 SER B O   1 
ATOM   2303 C CB  . SER B 2 118 ? 5.25867   9.61261   75.48577  1.000 24.89070  ? 118 SER B CB  1 
ATOM   2304 O OG  . SER B 2 118 ? 4.24490   8.69689   75.85830  1.000 37.99983  ? 118 SER B OG  1 
ATOM   2305 N N   . VAL B 2 119 ? 7.58661   9.96680   72.93983  1.000 24.78586  ? 119 VAL B N   1 
ATOM   2306 C CA  . VAL B 2 119 ? 8.49318   10.89975  72.28612  1.000 27.33164  ? 119 VAL B CA  1 
ATOM   2307 C C   . VAL B 2 119 ? 7.61465   11.82626  71.45771  1.000 29.06704  ? 119 VAL B C   1 
ATOM   2308 O O   . VAL B 2 119 ? 7.15910   11.45880  70.36769  1.000 30.33281  ? 119 VAL B O   1 
ATOM   2309 C CB  . VAL B 2 119 ? 9.53617   10.17515  71.42592  1.000 25.14498  ? 119 VAL B CB  1 
ATOM   2310 C CG1 . VAL B 2 119 ? 10.55335  11.15593  70.89010  1.000 26.72589  ? 119 VAL B CG1 1 
ATOM   2311 C CG2 . VAL B 2 119 ? 10.21837  9.07370   72.23080  1.000 23.33470  ? 119 VAL B CG2 1 
ATOM   2312 N N   . THR B 2 120 ? 7.36526   13.02752  71.97117  1.000 26.74708  ? 120 THR B N   1 
ATOM   2313 C CA  . THR B 2 120 ? 6.32886   13.89465  71.43345  1.000 32.07347  ? 120 THR B CA  1 
ATOM   2314 C C   . THR B 2 120 ? 6.90983   15.19228  70.88722  1.000 29.71278  ? 120 THR B C   1 
ATOM   2315 O O   . THR B 2 120 ? 7.95264   15.67241  71.34651  1.000 23.71463  ? 120 THR B O   1 
ATOM   2316 C CB  . THR B 2 120 ? 5.27459   14.21796  72.50788  1.000 30.83409  ? 120 THR B CB  1 
ATOM   2317 O OG1 . THR B 2 120 ? 5.91762   14.79296  73.65310  1.000 33.17786  ? 120 THR B OG1 1 
ATOM   2318 C CG2 . THR B 2 120 ? 4.53254   12.95530  72.92396  1.000 24.62196  ? 120 THR B CG2 1 
ATOM   2319 N N   . ASP B 2 121 ? 6.21698   15.73840  69.88212  1.000 30.29632  ? 121 ASP B N   1 
ATOM   2320 C CA  . ASP B 2 121 ? 6.43309   17.09557  69.36886  1.000 32.22561  ? 121 ASP B CA  1 
ATOM   2321 C C   . ASP B 2 121 ? 7.87452   17.32072  68.90622  1.000 31.00410  ? 121 ASP B C   1 
ATOM   2322 O O   . ASP B 2 121 ? 8.59324   18.17802  69.42214  1.000 37.03977  ? 121 ASP B O   1 
ATOM   2323 C CB  . ASP B 2 121 ? 6.02960   18.13841  70.41816  1.000 29.36226  ? 121 ASP B CB  1 
ATOM   2324 C CG  . ASP B 2 121 ? 4.53512   18.14049  70.68967  1.000 45.07393  ? 121 ASP B CG  1 
ATOM   2325 O OD1 . ASP B 2 121 ? 3.76678   17.71449  69.79386  1.000 33.29772  ? 121 ASP B OD1 1 
ATOM   2326 O OD2 . ASP B 2 121 ? 4.12929   18.56571  71.79469  1.000 51.55890  ? 121 ASP B OD2 1 
ATOM   2327 N N   . PHE B 2 122 ? 8.28580   16.54987  67.90296  1.000 28.53211  ? 122 PHE B N   1 
ATOM   2328 C CA  . PHE B 2 122 ? 9.59418   16.74424  67.29682  1.000 33.72371  ? 122 PHE B CA  1 
ATOM   2329 C C   . PHE B 2 122 ? 9.45568   16.91922  65.79049  1.000 28.91055  ? 122 PHE B C   1 
ATOM   2330 O O   . PHE B 2 122 ? 8.47247   16.49837  65.17803  1.000 26.60280  ? 122 PHE B O   1 
ATOM   2331 C CB  . PHE B 2 122 ? 10.55366  15.58568  67.61208  1.000 30.12141  ? 122 PHE B CB  1 
ATOM   2332 C CG  . PHE B 2 122 ? 10.04795  14.23616  67.19287  1.000 29.89272  ? 122 PHE B CG  1 
ATOM   2333 C CD1 . PHE B 2 122 ? 10.31113  13.74404  65.91961  1.000 21.36034  ? 122 PHE B CD1 1 
ATOM   2334 C CD2 . PHE B 2 122 ? 9.33404   13.44705  68.07936  1.000 22.94980  ? 122 PHE B CD2 1 
ATOM   2335 C CE1 . PHE B 2 122 ? 9.85909   12.49582  65.53448  1.000 22.96298  ? 122 PHE B CE1 1 
ATOM   2336 C CE2 . PHE B 2 122 ? 8.87659   12.19287  67.70175  1.000 24.22295  ? 122 PHE B CE2 1 
ATOM   2337 C CZ  . PHE B 2 122 ? 9.13844   11.71648  66.42651  1.000 22.12023  ? 122 PHE B CZ  1 
ATOM   2338 N N   . TYR B 2 123 ? 10.46230  17.57240  65.20394  1.000 26.18110  ? 123 TYR B N   1 
ATOM   2339 C CA  . TYR B 2 123 ? 10.54579  17.77585  63.76750  1.000 25.98928  ? 123 TYR B CA  1 
ATOM   2340 C C   . TYR B 2 123 ? 12.01035  17.98852  63.43465  1.000 30.04327  ? 123 TYR B C   1 
ATOM   2341 O O   . TYR B 2 123 ? 12.68677  18.72834  64.16205  1.000 35.98663  ? 123 TYR B O   1 
ATOM   2342 C CB  . TYR B 2 123 ? 9.71234   18.97717  63.30135  1.000 27.04156  ? 123 TYR B CB  1 
ATOM   2343 C CG  . TYR B 2 123 ? 9.57687   19.05024  61.79645  1.000 31.10493  ? 123 TYR B CG  1 
ATOM   2344 C CD1 . TYR B 2 123 ? 10.54568  19.67936  61.01936  1.000 29.38119  ? 123 TYR B CD1 1 
ATOM   2345 C CD2 . TYR B 2 123 ? 8.49441   18.46679  61.14828  1.000 24.18179  ? 123 TYR B CD2 1 
ATOM   2346 C CE1 . TYR B 2 123 ? 10.43568  19.73432  59.63925  1.000 20.61301  ? 123 TYR B CE1 1 
ATOM   2347 C CE2 . TYR B 2 123 ? 8.37298   18.51933  59.77170  1.000 23.32409  ? 123 TYR B CE2 1 
ATOM   2348 C CZ  . TYR B 2 123 ? 9.34743   19.15252  59.02061  1.000 25.45028  ? 123 TYR B CZ  1 
ATOM   2349 O OH  . TYR B 2 123 ? 9.22826   19.20343  57.64838  1.000 28.38196  ? 123 TYR B OH  1 
ATOM   2350 N N   . PRO B 2 124 ? 12.53792  17.37957  62.35741  1.000 29.53849  ? 124 PRO B N   1 
ATOM   2351 C CA  . PRO B 2 124 ? 11.80610  16.54632  61.39346  1.000 27.10960  ? 124 PRO B CA  1 
ATOM   2352 C C   . PRO B 2 124 ? 11.55255  15.11932  61.87116  1.000 24.64005  ? 124 PRO B C   1 
ATOM   2353 O O   . PRO B 2 124 ? 11.76795  14.81313  63.04002  1.000 26.86426  ? 124 PRO B O   1 
ATOM   2354 C CB  . PRO B 2 124 ? 12.72359  16.55299  60.16206  1.000 20.77316  ? 124 PRO B CB  1 
ATOM   2355 C CG  . PRO B 2 124 ? 14.08620  16.68368  60.72930  1.000 23.34946  ? 124 PRO B CG  1 
ATOM   2356 C CD  . PRO B 2 124 ? 13.94952  17.55630  61.96812  1.000 30.12406  ? 124 PRO B CD  1 
ATOM   2357 N N   . ALA B 2 125 ? 11.10444  14.26513  60.94543  1.000 27.53272  ? 125 ALA B N   1 
ATOM   2358 C CA  . ALA B 2 125 ? 10.62386  12.92997  61.28332  1.000 27.76908  ? 125 ALA B CA  1 
ATOM   2359 C C   . ALA B 2 125 ? 11.74036  11.97405  61.67860  1.000 22.51247  ? 125 ALA B C   1 
ATOM   2360 O O   . ALA B 2 125 ? 11.49988  11.04152  62.44985  1.000 38.19370  ? 125 ALA B O   1 
ATOM   2361 C CB  . ALA B 2 125 ? 9.84850   12.34603  60.10199  1.000 22.14828  ? 125 ALA B CB  1 
ATOM   2362 N N   . GLN B 2 126 ? 12.94228  12.16591  61.15226  1.000 27.53796  ? 126 GLN B N   1 
ATOM   2363 C CA  . GLN B 2 126 ? 14.02838  11.22719  61.39085  1.000 26.69393  ? 126 GLN B CA  1 
ATOM   2364 C C   . GLN B 2 126 ? 14.33691  11.16461  62.87788  1.000 36.85510  ? 126 GLN B C   1 
ATOM   2365 O O   . GLN B 2 126 ? 14.62164  12.18828  63.50599  1.000 32.19897  ? 126 GLN B O   1 
ATOM   2366 C CB  . GLN B 2 126 ? 15.26600  11.64960  60.59994  1.000 43.29999  ? 126 GLN B CB  1 
ATOM   2367 C CG  . GLN B 2 126 ? 16.42660  10.66814  60.65553  1.000 64.47142  ? 126 GLN B CG  1 
ATOM   2368 C CD  . GLN B 2 126 ? 17.65814  11.17795  59.91796  1.000 83.22724  ? 126 GLN B CD  1 
ATOM   2369 O OE1 . GLN B 2 126 ? 17.93229  12.37922  59.89712  1.000 94.12703  ? 126 GLN B OE1 1 
ATOM   2370 N NE2 . GLN B 2 126 ? 18.39832  10.26378  59.29678  1.000 67.66335  ? 126 GLN B NE2 1 
ATOM   2371 N N   . ILE B 2 127 ? 14.26325  9.96189   63.44456  1.000 36.81572  ? 127 ILE B N   1 
ATOM   2372 C CA  . ILE B 2 127 ? 14.41887  9.78341   64.88091  1.000 39.20799  ? 127 ILE B CA  1 
ATOM   2373 C C   . ILE B 2 127 ? 14.76367  8.32647   65.13798  1.000 36.16762  ? 127 ILE B C   1 
ATOM   2374 O O   . ILE B 2 127 ? 14.34898  7.43401   64.39254  1.000 29.05379  ? 127 ILE B O   1 
ATOM   2375 C CB  . ILE B 2 127 ? 13.13602  10.21776  65.63621  1.000 32.67584  ? 127 ILE B CB  1 
ATOM   2376 C CG1 . ILE B 2 127 ? 13.43785  10.47033  67.11282  1.000 36.25667  ? 127 ILE B CG1 1 
ATOM   2377 C CG2 . ILE B 2 127 ? 12.04975  9.17003   65.49291  1.000 23.09897  ? 127 ILE B CG2 1 
ATOM   2378 C CD1 . ILE B 2 127 ? 12.45582  11.40532  67.78024  1.000 32.94135  ? 127 ILE B CD1 1 
ATOM   2379 N N   . LYS B 2 128 ? 15.54267  8.08859   66.19095  1.000 31.13567  ? 128 LYS B N   1 
ATOM   2380 C CA  . LYS B 2 128 ? 15.88302  6.74169   66.63256  1.000 39.06838  ? 128 LYS B CA  1 
ATOM   2381 C C   . LYS B 2 128 ? 15.62950  6.64964   68.13138  1.000 31.30408  ? 128 LYS B C   1 
ATOM   2382 O O   . LYS B 2 128 ? 16.18857  7.43374   68.90617  1.000 29.01953  ? 128 LYS B O   1 
ATOM   2383 C CB  . LYS B 2 128 ? 17.34003  6.40116   66.29769  1.000 35.28778  ? 128 LYS B CB  1 
ATOM   2384 C CG  . LYS B 2 128 ? 17.67723  4.92497   66.45759  1.000 35.73425  ? 128 LYS B CG  1 
ATOM   2385 C CD  . LYS B 2 128 ? 16.58283  4.06307   65.83618  1.000 64.16663  ? 128 LYS B CD  1 
ATOM   2386 C CE  . LYS B 2 128 ? 16.82880  2.57887   66.06620  1.000 68.28558  ? 128 LYS B CE  1 
ATOM   2387 N NZ  . LYS B 2 128 ? 15.57318  1.78018   65.93697  1.000 58.95172  ? 128 LYS B NZ  1 
ATOM   2388 N N   . VAL B 2 129 ? 14.78002  5.70600   68.53430  1.000 34.30129  ? 129 VAL B N   1 
ATOM   2389 C CA  . VAL B 2 129 ? 14.41074  5.50518   69.93160  1.000 30.13482  ? 129 VAL B CA  1 
ATOM   2390 C C   . VAL B 2 129 ? 14.81434  4.09608   70.33792  1.000 30.79499  ? 129 VAL B C   1 
ATOM   2391 O O   . VAL B 2 129 ? 14.42797  3.12423   69.67931  1.000 39.13223  ? 129 VAL B O   1 
ATOM   2392 C CB  . VAL B 2 129 ? 12.90401  5.72079   70.16392  1.000 30.72663  ? 129 VAL B CB  1 
ATOM   2393 C CG1 . VAL B 2 129 ? 12.56300  5.54038   71.64380  1.000 25.01527  ? 129 VAL B CG1 1 
ATOM   2394 C CG2 . VAL B 2 129 ? 12.47535  7.09377   69.66668  1.000 20.77484  ? 129 VAL B CG2 1 
ATOM   2395 N N   . ARG B 2 130 ? 15.58233  3.98792   71.42457  1.000 26.38450  ? 130 ARG B N   1 
ATOM   2396 C CA  . ARG B 2 130 ? 16.05060  2.70857   71.94084  1.000 35.91438  ? 130 ARG B CA  1 
ATOM   2397 C C   . ARG B 2 130 ? 15.71682  2.56912   73.41936  1.000 37.26156  ? 130 ARG B C   1 
ATOM   2398 O O   . ARG B 2 130 ? 15.74008  3.54293   74.18003  1.000 30.30813  ? 130 ARG B O   1 
ATOM   2399 C CB  . ARG B 2 130 ? 17.56117  2.53906   71.76703  1.000 39.06769  ? 130 ARG B CB  1 
ATOM   2400 C CG  . ARG B 2 130 ? 18.01566  2.39817   70.33721  1.000 39.05540  ? 130 ARG B CG  1 
ATOM   2401 C CD  . ARG B 2 130 ? 19.52579  2.45896   70.25927  1.000 49.36430  ? 130 ARG B CD  1 
ATOM   2402 N NE  . ARG B 2 130 ? 19.96510  3.10028   69.02796  1.000 52.45305  ? 130 ARG B NE  1 
ATOM   2403 C CZ  . ARG B 2 130 ? 21.14220  3.68658   68.86931  1.000 60.62059  ? 130 ARG B CZ  1 
ATOM   2404 N NH1 . ARG B 2 130 ? 22.04250  3.70189   69.83926  1.000 70.32768  ? 130 ARG B NH1 1 
ATOM   2405 N NH2 . ARG B 2 130 ? 21.41779  4.28347   67.71341  1.000 66.98260  ? 130 ARG B NH2 1 
ATOM   2406 N N   . TRP B 2 131 ? 15.42720  1.33534   73.81811  1.000 31.92396  ? 131 TRP B N   1 
ATOM   2407 C CA  . TRP B 2 131 ? 15.24211  0.97905   75.21506  1.000 33.51943  ? 131 TRP B CA  1 
ATOM   2408 C C   . TRP B 2 131 ? 16.49402  0.28783   75.74499  1.000 39.21118  ? 131 TRP B C   1 
ATOM   2409 O O   . TRP B 2 131 ? 17.10580  -0.53012  75.05069  1.000 34.56090  ? 131 TRP B O   1 
ATOM   2410 C CB  . TRP B 2 131 ? 14.02773  0.06399   75.38719  1.000 25.53592  ? 131 TRP B CB  1 
ATOM   2411 C CG  . TRP B 2 131 ? 12.74588  0.78894   75.66900  1.000 35.42078  ? 131 TRP B CG  1 
ATOM   2412 C CD1 . TRP B 2 131 ? 11.64820  0.87429   74.85557  1.000 30.43135  ? 131 TRP B CD1 1 
ATOM   2413 C CD2 . TRP B 2 131 ? 12.42557  1.52649   76.85385  1.000 28.46522  ? 131 TRP B CD2 1 
ATOM   2414 N NE1 . TRP B 2 131 ? 10.66436  1.61650   75.46576  1.000 32.26707  ? 131 TRP B NE1 1 
ATOM   2415 C CE2 . TRP B 2 131 ? 11.11715  2.03014   76.69254  1.000 32.00091  ? 131 TRP B CE2 1 
ATOM   2416 C CE3 . TRP B 2 131 ? 13.12002  1.81249   78.03547  1.000 29.73407  ? 131 TRP B CE3 1 
ATOM   2417 C CZ2 . TRP B 2 131 ? 10.49001  2.80592   77.66900  1.000 30.96772  ? 131 TRP B CZ2 1 
ATOM   2418 C CZ3 . TRP B 2 131 ? 12.49656  2.57993   79.00425  1.000 27.55045  ? 131 TRP B CZ3 1 
ATOM   2419 C CH2 . TRP B 2 131 ? 11.19409  3.06914   78.81400  1.000 37.19788  ? 131 TRP B CH2 1 
ATOM   2420 N N   . PHE B 2 132 ? 16.86915  0.62641   76.97963  1.000 33.11013  ? 132 PHE B N   1 
ATOM   2421 C CA  . PHE B 2 132 ? 17.98699  0.00824   77.68270  1.000 31.31543  ? 132 PHE B CA  1 
ATOM   2422 C C   . PHE B 2 132 ? 17.53782  -0.45586  79.05979  1.000 31.73228  ? 132 PHE B C   1 
ATOM   2423 O O   . PHE B 2 132 ? 16.79031  0.24715   79.74659  1.000 26.73708  ? 132 PHE B O   1 
ATOM   2424 C CB  . PHE B 2 132 ? 19.15951  0.97794   77.84625  1.000 33.04702  ? 132 PHE B CB  1 
ATOM   2425 C CG  . PHE B 2 132 ? 19.87765  1.27984   76.57207  1.000 37.44444  ? 132 PHE B CG  1 
ATOM   2426 C CD1 . PHE B 2 132 ? 19.37314  2.20973   75.67747  1.000 41.45459  ? 132 PHE B CD1 1 
ATOM   2427 C CD2 . PHE B 2 132 ? 21.06560  0.64120   76.26939  1.000 43.68134  ? 132 PHE B CD2 1 
ATOM   2428 C CE1 . PHE B 2 132 ? 20.04097  2.48955   74.49519  1.000 41.52265  ? 132 PHE B CE1 1 
ATOM   2429 C CE2 . PHE B 2 132 ? 21.73520  0.91555   75.09353  1.000 46.65246  ? 132 PHE B CE2 1 
ATOM   2430 C CZ  . PHE B 2 132 ? 21.22110  1.84164   74.20549  1.000 43.77453  ? 132 PHE B CZ  1 
ATOM   2431 N N   . ARG B 2 133 ? 18.00095  -1.63781  79.46032  1.000 28.94518  ? 133 ARG B N   1 
ATOM   2432 C CA  . ARG B 2 133 ? 17.79907  -2.15518  80.81003  1.000 29.64406  ? 133 ARG B CA  1 
ATOM   2433 C C   . ARG B 2 133 ? 19.17368  -2.36233  81.43106  1.000 31.44460  ? 133 ARG B C   1 
ATOM   2434 O O   . ARG B 2 133 ? 19.91967  -3.25113  81.00762  1.000 35.86957  ? 133 ARG B O   1 
ATOM   2435 C CB  . ARG B 2 133 ? 16.99758  -3.45548  80.79285  1.000 31.60598  ? 133 ARG B CB  1 
ATOM   2436 C CG  . ARG B 2 133 ? 16.78727  -4.07621  82.16176  1.000 33.97504  ? 133 ARG B CG  1 
ATOM   2437 C CD  . ARG B 2 133 ? 16.49143  -5.55904  82.05289  1.000 40.75258  ? 133 ARG B CD  1 
ATOM   2438 N NE  . ARG B 2 133 ? 17.13033  -6.31254  83.12686  1.000 52.52304  ? 133 ARG B NE  1 
ATOM   2439 C CZ  . ARG B 2 133 ? 16.49646  -6.81168  84.18048  1.000 59.95551  ? 133 ARG B CZ  1 
ATOM   2440 N NH1 . ARG B 2 133 ? 15.18802  -6.68121  84.32665  1.000 65.25057  ? 133 ARG B NH1 1 
ATOM   2441 N NH2 . ARG B 2 133 ? 17.19286  -7.46183  85.11005  1.000 68.82412  ? 133 ARG B NH2 1 
ATOM   2442 N N   . ASN B 2 134 ? 19.51192  -1.53331  82.42152  1.000 30.33308  ? 134 ASN B N   1 
ATOM   2443 C CA  . ASN B 2 134 ? 20.81543  -1.59035  83.08977  1.000 36.49043  ? 134 ASN B CA  1 
ATOM   2444 C C   . ASN B 2 134 ? 21.95733  -1.45308  82.08120  1.000 40.59833  ? 134 ASN B C   1 
ATOM   2445 O O   . ASN B 2 134 ? 22.90967  -2.23810  82.07745  1.000 37.51906  ? 134 ASN B O   1 
ATOM   2446 C CB  . ASN B 2 134 ? 20.96454  -2.87719  83.90745  1.000 33.69854  ? 134 ASN B CB  1 
ATOM   2447 C CG  . ASN B 2 134 ? 19.92845  -2.99636  85.00922  1.000 34.78625  ? 134 ASN B CG  1 
ATOM   2448 O OD1 . ASN B 2 134 ? 19.54170  -2.00400  85.63149  1.000 26.53805  ? 134 ASN B OD1 1 
ATOM   2449 N ND2 . ASN B 2 134 ? 19.47401  -4.21753  85.25702  1.000 31.98541  ? 134 ASN B ND2 1 
ATOM   2450 N N   . ASP B 2 135 ? 21.83624  -0.45034  81.20516  1.000 37.80247  ? 135 ASP B N   1 
ATOM   2451 C CA  . ASP B 2 135 ? 22.81712  -0.06532  80.18983  1.000 33.75274  ? 135 ASP B CA  1 
ATOM   2452 C C   . ASP B 2 135 ? 22.96735  -1.08846  79.07398  1.000 36.96509  ? 135 ASP B C   1 
ATOM   2453 O O   . ASP B 2 135 ? 23.87663  -0.96073  78.24876  1.000 40.35256  ? 135 ASP B O   1 
ATOM   2454 C CB  . ASP B 2 135 ? 24.19689  0.21060   80.79847  1.000 33.49994  ? 135 ASP B CB  1 
ATOM   2455 C CG  . ASP B 2 135 ? 24.18540  1.37510   81.76322  1.000 39.15013  ? 135 ASP B CG  1 
ATOM   2456 O OD1 . ASP B 2 135 ? 23.63533  2.44309   81.40800  1.000 36.48741  ? 135 ASP B OD1 1 
ATOM   2457 O OD2 . ASP B 2 135 ? 24.72230  1.21562   82.88122  1.000 41.70267  ? 135 ASP B OD2 1 
ATOM   2458 N N   . GLN B 2 136 ? 22.11021  -2.09869  79.02164  1.000 38.33228  ? 136 GLN B N   1 
ATOM   2459 C CA  . GLN B 2 136 ? 22.12050  -3.09085  77.95584  1.000 33.03119  ? 136 GLN B CA  1 
ATOM   2460 C C   . GLN B 2 136 ? 20.85778  -2.91026  77.12240  1.000 39.01909  ? 136 GLN B C   1 
ATOM   2461 O O   . GLN B 2 136 ? 19.74549  -2.95302  77.66258  1.000 34.78694  ? 136 GLN B O   1 
ATOM   2462 C CB  . GLN B 2 136 ? 22.19713  -4.50324  78.53268  1.000 35.29582  ? 136 GLN B CB  1 
ATOM   2463 C CG  . GLN B 2 136 ? 22.18194  -5.59960  77.48542  1.000 39.31775  ? 136 GLN B CG  1 
ATOM   2464 C CD  . GLN B 2 136 ? 22.25243  -6.98999  78.09193  1.000 48.68040  ? 136 GLN B CD  1 
ATOM   2465 O OE1 . GLN B 2 136 ? 21.72249  -7.24134  79.18111  1.000 50.31131  ? 136 GLN B OE1 1 
ATOM   2466 N NE2 . GLN B 2 136 ? 22.91908  -7.90122  77.39167  1.000 39.74599  ? 136 GLN B NE2 1 
ATOM   2467 N N   . GLU B 2 137 ? 21.02771  -2.70764  75.81493  1.000 37.55370  ? 137 GLU B N   1 
ATOM   2468 C CA  . GLU B 2 137 ? 19.88710  -2.39883  74.96350  1.000 35.19191  ? 137 GLU B CA  1 
ATOM   2469 C C   . GLU B 2 137 ? 18.92002  -3.57169  74.91015  1.000 34.59942  ? 137 GLU B C   1 
ATOM   2470 O O   . GLU B 2 137 ? 19.32542  -4.71892  74.70822  1.000 38.90126  ? 137 GLU B O   1 
ATOM   2471 C CB  . GLU B 2 137 ? 20.33736  -2.03470  73.54893  1.000 41.14882  ? 137 GLU B CB  1 
ATOM   2472 C CG  . GLU B 2 137 ? 19.14974  -1.85237  72.59710  1.000 47.08340  ? 137 GLU B CG  1 
ATOM   2473 C CD  . GLU B 2 137 ? 19.53762  -1.37107  71.20895  1.000 50.97740  ? 137 GLU B CD  1 
ATOM   2474 O OE1 . GLU B 2 137 ? 20.74879  -1.27901  70.91387  1.000 54.62165  ? 137 GLU B OE1 1 
ATOM   2475 O OE2 . GLU B 2 137 ? 18.61900  -1.08221  70.41094  1.000 48.86941  ? 137 GLU B OE2 1 
ATOM   2476 N N   . GLU B 2 138 ? 17.63802  -3.27684  75.11299  1.000 41.79239  ? 138 GLU B N   1 
ATOM   2477 C CA  . GLU B 2 138 ? 16.57732  -4.26266  74.97125  1.000 43.08607  ? 138 GLU B CA  1 
ATOM   2478 C C   . GLU B 2 138 ? 16.09320  -4.25236  73.52937  1.000 51.86993  ? 138 GLU B C   1 
ATOM   2479 O O   . GLU B 2 138 ? 15.83513  -3.18404  72.96533  1.000 47.54144  ? 138 GLU B O   1 
ATOM   2480 C CB  . GLU B 2 138 ? 15.41208  -3.95938  75.91769  1.000 41.44176  ? 138 GLU B CB  1 
ATOM   2481 C CG  . GLU B 2 138 ? 15.68513  -4.20981  77.39667  1.000 49.70573  ? 138 GLU B CG  1 
ATOM   2482 C CD  . GLU B 2 138 ? 15.44793  -5.65538  77.81058  1.000 60.65534  ? 138 GLU B CD  1 
ATOM   2483 O OE1 . GLU B 2 138 ? 16.11130  -6.55720  77.25567  1.000 57.92079  ? 138 GLU B OE1 1 
ATOM   2484 O OE2 . GLU B 2 138 ? 14.59115  -5.88822  78.69216  1.000 69.28438  ? 138 GLU B OE2 1 
ATOM   2485 N N   . THR B 2 139 ? 15.98487  -5.43416  72.93452  1.000 60.44315  ? 139 THR B N   1 
ATOM   2486 C CA  . THR B 2 139 ? 15.44857  -5.57644  71.58575  1.000 49.83135  ? 139 THR B CA  1 
ATOM   2487 C C   . THR B 2 139 ? 14.19557  -6.43333  71.53482  1.000 52.06839  ? 139 THR B C   1 
ATOM   2488 O O   . THR B 2 139 ? 13.27304  -6.12296  70.77762  1.000 69.14780  ? 139 THR B O   1 
ATOM   2489 C CB  . THR B 2 139 ? 16.51339  -6.15923  70.64754  1.000 44.73248  ? 139 THR B CB  1 
ATOM   2490 O OG1 . THR B 2 139 ? 17.10531  -7.31814  71.24752  1.000 54.90816  ? 139 THR B OG1 1 
ATOM   2491 C CG2 . THR B 2 139 ? 17.59675  -5.12479  70.37989  1.000 52.96356  ? 139 THR B CG2 1 
ATOM   2492 N N   . ALA B 2 140 ? 14.13058  -7.49554  72.33162  1.000 52.74367  ? 140 ALA B N   1 
ATOM   2493 C CA  . ALA B 2 140 ? 12.91474  -8.28485  72.44717  1.000 48.87781  ? 140 ALA B CA  1 
ATOM   2494 C C   . ALA B 2 140 ? 11.96866  -7.64173  73.45255  1.000 61.46323  ? 140 ALA B C   1 
ATOM   2495 O O   . ALA B 2 140 ? 12.39497  -7.13244  74.49394  1.000 67.65008  ? 140 ALA B O   1 
ATOM   2496 C CB  . ALA B 2 140 ? 13.24228  -9.71553  72.87464  1.000 59.40451  ? 140 ALA B CB  1 
ATOM   2497 N N   . GLY B 2 141 ? 10.67716  -7.67356  73.14002  1.000 49.71124  ? 141 GLY B N   1 
ATOM   2498 C CA  . GLY B 2 141 ? 9.68590   -7.03146  73.97100  1.000 37.99447  ? 141 GLY B CA  1 
ATOM   2499 C C   . GLY B 2 141 ? 9.48931   -5.55615  73.70431  1.000 36.81259  ? 141 GLY B C   1 
ATOM   2500 O O   . GLY B 2 141 ? 8.72637   -4.90992  74.43179  1.000 45.28388  ? 141 GLY B O   1 
ATOM   2501 N N   . VAL B 2 142 ? 10.15165  -5.00051  72.69596  1.000 45.02603  ? 142 VAL B N   1 
ATOM   2502 C CA  . VAL B 2 142 ? 9.96207   -3.60578  72.31520  1.000 41.59053  ? 142 VAL B CA  1 
ATOM   2503 C C   . VAL B 2 142 ? 8.90635   -3.54726  71.21950  1.000 49.97495  ? 142 VAL B C   1 
ATOM   2504 O O   . VAL B 2 142 ? 9.05173   -4.18427  70.17035  1.000 60.09776  ? 142 VAL B O   1 
ATOM   2505 C CB  . VAL B 2 142 ? 11.27805  -2.96917  71.84539  1.000 37.91848  ? 142 VAL B CB  1 
ATOM   2506 C CG1 . VAL B 2 142 ? 11.02072  -1.57878  71.29701  1.000 38.29006  ? 142 VAL B CG1 1 
ATOM   2507 C CG2 . VAL B 2 142 ? 12.27312  -2.91126  72.98334  1.000 39.51634  ? 142 VAL B CG2 1 
ATOM   2508 N N   . VAL B 2 143 ? 7.84130   -2.78783  71.46268  1.000 50.69470  ? 143 VAL B N   1 
ATOM   2509 C CA  . VAL B 2 143 ? 6.76594   -2.59580  70.49599  1.000 49.67267  ? 143 VAL B CA  1 
ATOM   2510 C C   . VAL B 2 143 ? 6.53141   -1.10219  70.34449  1.000 43.98739  ? 143 VAL B C   1 
ATOM   2511 O O   . VAL B 2 143 ? 6.22415   -0.41409  71.32553  1.000 48.64656  ? 143 VAL B O   1 
ATOM   2512 C CB  . VAL B 2 143 ? 5.46667   -3.30152  70.91560  1.000 52.79091  ? 143 VAL B CB  1 
ATOM   2513 C CG1 . VAL B 2 143 ? 4.35136   -2.95036  69.94643  1.000 38.57131  ? 143 VAL B CG1 1 
ATOM   2514 C CG2 . VAL B 2 143 ? 5.67592   -4.80884  70.97253  1.000 56.98307  ? 143 VAL B CG2 1 
ATOM   2515 N N   . SER B 2 144 ? 6.65726   -0.60725  69.12145  1.000 39.57214  ? 144 SER B N   1 
ATOM   2516 C CA  . SER B 2 144 ? 6.53937   0.81032   68.82921  1.000 40.86523  ? 144 SER B CA  1 
ATOM   2517 C C   . SER B 2 144 ? 5.32509   1.06648   67.94934  1.000 39.12217  ? 144 SER B C   1 
ATOM   2518 O O   . SER B 2 144 ? 5.01243   0.26944   67.06109  1.000 41.42439  ? 144 SER B O   1 
ATOM   2519 C CB  . SER B 2 144 ? 7.80289   1.32290   68.13146  1.000 38.88184  ? 144 SER B CB  1 
ATOM   2520 O OG  . SER B 2 144 ? 7.62876   2.65445   67.68414  1.000 46.45471  ? 144 SER B OG  1 
ATOM   2521 N N   . THR B 2 145 ? 4.63638   2.17640   68.20436  1.000 37.65246  ? 145 THR B N   1 
ATOM   2522 C CA  . THR B 2 145 ? 3.65897   2.66785   67.25087  1.000 35.99815  ? 145 THR B CA  1 
ATOM   2523 C C   . THR B 2 145 ? 4.37918   3.09113   65.97603  1.000 29.72441  ? 145 THR B C   1 
ATOM   2524 O O   . THR B 2 145 ? 5.60026   3.25695   65.96749  1.000 36.74259  ? 145 THR B O   1 
ATOM   2525 C CB  . THR B 2 145 ? 2.88976   3.86424   67.81049  1.000 31.30949  ? 145 THR B CB  1 
ATOM   2526 O OG1 . THR B 2 145 ? 3.76061   5.00161   67.87488  1.000 29.99887  ? 145 THR B OG1 1 
ATOM   2527 C CG2 . THR B 2 145 ? 2.32661   3.56491   69.18735  1.000 31.55571  ? 145 THR B CG2 1 
ATOM   2528 N N   . PRO B 2 146 ? 3.65487   3.27466   64.88145  1.000 35.53935  ? 146 PRO B N   1 
ATOM   2529 C CA  . PRO B 2 146 ? 4.26020   3.94504   63.72962  1.000 40.19000  ? 146 PRO B CA  1 
ATOM   2530 C C   . PRO B 2 146 ? 4.56280   5.39643   64.06741  1.000 34.13541  ? 146 PRO B C   1 
ATOM   2531 O O   . PRO B 2 146 ? 4.11275   5.95129   65.07269  1.000 33.89668  ? 146 PRO B O   1 
ATOM   2532 C CB  . PRO B 2 146 ? 3.21614   3.83114   62.61597  1.000 29.43320  ? 146 PRO B CB  1 
ATOM   2533 C CG  . PRO B 2 146 ? 2.02384   3.18899   63.20877  1.000 41.55273  ? 146 PRO B CG  1 
ATOM   2534 C CD  . PRO B 2 146 ? 2.25847   2.86828   64.64218  1.000 46.48627  ? 146 PRO B CD  1 
ATOM   2535 N N   . LEU B 2 147 ? 5.37590   6.00332   63.21583  1.000 33.68832  ? 147 LEU B N   1 
ATOM   2536 C CA  . LEU B 2 147 ? 5.55186   7.44285   63.26998  1.000 29.93502  ? 147 LEU B CA  1 
ATOM   2537 C C   . LEU B 2 147 ? 4.19801   8.11324   63.09072  1.000 31.09980  ? 147 LEU B C   1 
ATOM   2538 O O   . LEU B 2 147 ? 3.44588   7.77938   62.17163  1.000 35.77479  ? 147 LEU B O   1 
ATOM   2539 C CB  . LEU B 2 147 ? 6.52676   7.88506   62.18515  1.000 29.46436  ? 147 LEU B CB  1 
ATOM   2540 C CG  . LEU B 2 147 ? 6.94679   9.34526   62.19623  1.000 34.45641  ? 147 LEU B CG  1 
ATOM   2541 C CD1 . LEU B 2 147 ? 7.42368   9.73364   63.58316  1.000 24.90273  ? 147 LEU B CD1 1 
ATOM   2542 C CD2 . LEU B 2 147 ? 8.04269   9.53287   61.17638  1.000 41.57574  ? 147 LEU B CD2 1 
ATOM   2543 N N   . ILE B 2 148 ? 3.87501   9.03745   63.98835  1.000 31.01962  ? 148 ILE B N   1 
ATOM   2544 C CA  . ILE B 2 148 ? 2.56103   9.66491   64.03756  1.000 28.99691  ? 148 ILE B CA  1 
ATOM   2545 C C   . ILE B 2 148 ? 2.70553   11.12174  63.62634  1.000 33.01798  ? 148 ILE B C   1 
ATOM   2546 O O   . ILE B 2 148 ? 3.42595   11.89275  64.27399  1.000 26.71569  ? 148 ILE B O   1 
ATOM   2547 C CB  . ILE B 2 148 ? 1.92953   9.54581   65.43047  1.000 29.43759  ? 148 ILE B CB  1 
ATOM   2548 C CG1 . ILE B 2 148 ? 1.68749   8.07643   65.77066  1.000 33.18999  ? 148 ILE B CG1 1 
ATOM   2549 C CG2 . ILE B 2 148 ? 0.63562   10.33462  65.48921  1.000 29.47392  ? 148 ILE B CG2 1 
ATOM   2550 C CD1 . ILE B 2 148 ? 1.26065   7.85494   67.19869  1.000 33.93467  ? 148 ILE B CD1 1 
ATOM   2551 N N   . ARG B 2 149 ? 2.01526   11.49494  62.55231  1.000 37.90190  ? 149 ARG B N   1 
ATOM   2552 C CA  . ARG B 2 149 ? 2.02985   12.85926  62.03947  1.000 29.59701  ? 149 ARG B CA  1 
ATOM   2553 C C   . ARG B 2 149 ? 0.90884   13.63470  62.72083  1.000 26.03058  ? 149 ARG B C   1 
ATOM   2554 O O   . ARG B 2 149 ? -0.27248  13.33709  62.51752  1.000 26.63002  ? 149 ARG B O   1 
ATOM   2555 C CB  . ARG B 2 149 ? 1.86691   12.86017  60.51991  1.000 21.83175  ? 149 ARG B CB  1 
ATOM   2556 C CG  . ARG B 2 149 ? 1.88159   14.24282  59.89076  1.000 27.29096  ? 149 ARG B CG  1 
ATOM   2557 C CD  . ARG B 2 149 ? 1.53217   14.18028  58.41694  1.000 38.89411  ? 149 ARG B CD  1 
ATOM   2558 N NE  . ARG B 2 149 ? 2.50145   13.39697  57.65867  1.000 27.00363  ? 149 ARG B NE  1 
ATOM   2559 C CZ  . ARG B 2 149 ? 3.64655   13.87780  57.19756  1.000 27.18965  ? 149 ARG B CZ  1 
ATOM   2560 N NH1 . ARG B 2 149 ? 4.00223   15.13711  57.40728  1.000 29.44160  ? 149 ARG B NH1 1 
ATOM   2561 N NH2 . ARG B 2 149 ? 4.45922   13.07543  56.51896  1.000 19.65694  ? 149 ARG B NH2 1 
ATOM   2562 N N   . ASN B 2 150 ? 1.27496   14.61858  63.54437  1.000 27.26207  ? 150 ASN B N   1 
ATOM   2563 C CA  . ASN B 2 150 ? 0.25714   15.41625  64.21718  1.000 32.41584  ? 150 ASN B CA  1 
ATOM   2564 C C   . ASN B 2 150 ? -0.44252  16.37275  63.26029  1.000 30.98745  ? 150 ASN B C   1 
ATOM   2565 O O   . ASN B 2 150 ? -1.57509  16.78220  63.53358  1.000 33.21208  ? 150 ASN B O   1 
ATOM   2566 C CB  . ASN B 2 150 ? 0.86523   16.20560  65.38127  1.000 25.14899  ? 150 ASN B CB  1 
ATOM   2567 C CG  . ASN B 2 150 ? 1.41611   15.31212  66.48242  1.000 33.88910  ? 150 ASN B CG  1 
ATOM   2568 O OD1 . ASN B 2 150 ? 0.87609   14.24166  66.76834  1.000 25.41970  ? 150 ASN B OD1 1 
ATOM   2569 N ND2 . ASN B 2 150 ? 2.50206   15.75673  67.11075  1.000 33.59695  ? 150 ASN B ND2 1 
ATOM   2570 N N   . GLY B 2 151 ? 0.19830   16.73055  62.14684  1.000 27.39014  ? 151 GLY B N   1 
ATOM   2571 C CA  . GLY B 2 151 ? -0.37617  17.64949  61.18975  1.000 26.38631  ? 151 GLY B CA  1 
ATOM   2572 C C   . GLY B 2 151 ? -0.00913  19.09817  61.40951  1.000 27.46395  ? 151 GLY B C   1 
ATOM   2573 O O   . GLY B 2 151 ? -0.30139  19.93406  60.54784  1.000 30.87802  ? 151 GLY B O   1 
ATOM   2574 N N   . ASP B 2 152 ? 0.61245   19.42314  62.53884  1.000 30.02725  ? 152 ASP B N   1 
ATOM   2575 C CA  . ASP B 2 152 ? 1.01838   20.78289  62.86446  1.000 26.82269  ? 152 ASP B CA  1 
ATOM   2576 C C   . ASP B 2 152 ? 2.52991   20.95368  62.76277  1.000 26.22477  ? 152 ASP B C   1 
ATOM   2577 O O   . ASP B 2 152 ? 3.12406   21.71596  63.52807  1.000 27.55041  ? 152 ASP B O   1 
ATOM   2578 C CB  . ASP B 2 152 ? 0.53477   21.16059  64.26511  1.000 27.21121  ? 152 ASP B CB  1 
ATOM   2579 C CG  . ASP B 2 152 ? 1.10328   20.24974  65.34759  1.000 34.52410  ? 152 ASP B CG  1 
ATOM   2580 O OD1 . ASP B 2 152 ? 1.86125   19.31082  65.01652  1.000 27.69182  ? 152 ASP B OD1 1 
ATOM   2581 O OD2 . ASP B 2 152 ? 0.78948   20.47007  66.53523  1.000 39.24008  ? 152 ASP B OD2 1 
ATOM   2582 N N   . TRP B 2 153 ? 3.15914   20.21987  61.84193  1.000 24.78930  ? 153 TRP B N   1 
ATOM   2583 C CA  . TRP B 2 153 ? 4.60623   20.23655  61.63761  1.000 25.64752  ? 153 TRP B CA  1 
ATOM   2584 C C   . TRP B 2 153 ? 5.36333   19.69615  62.84618  1.000 22.36109  ? 153 TRP B C   1 
ATOM   2585 O O   . TRP B 2 153 ? 6.49249   20.11073  63.11875  1.000 22.44038  ? 153 TRP B O   1 
ATOM   2586 C CB  . TRP B 2 153 ? 5.10438   21.63793  61.26746  1.000 20.96332  ? 153 TRP B CB  1 
ATOM   2587 C CG  . TRP B 2 153 ? 4.57355   22.07422  59.94915  1.000 30.49632  ? 153 TRP B CG  1 
ATOM   2588 C CD1 . TRP B 2 153 ? 3.32845   22.56637  59.69108  1.000 20.55216  ? 153 TRP B CD1 1 
ATOM   2589 C CD2 . TRP B 2 153 ? 5.26082   22.03594  58.69069  1.000 24.38160  ? 153 TRP B CD2 1 
ATOM   2590 N NE1 . TRP B 2 153 ? 3.19873   22.84510  58.35201  1.000 28.06319  ? 153 TRP B NE1 1 
ATOM   2591 C CE2 . TRP B 2 153 ? 4.37072   22.53037  57.71550  1.000 31.30549  ? 153 TRP B CE2 1 
ATOM   2592 C CE3 . TRP B 2 153 ? 6.54290   21.63911  58.29627  1.000 24.64374  ? 153 TRP B CE3 1 
ATOM   2593 C CZ2 . TRP B 2 153 ? 4.71936   22.63708  56.37038  1.000 19.14605  ? 153 TRP B CZ2 1 
ATOM   2594 C CZ3 . TRP B 2 153 ? 6.88763   21.74236  56.95731  1.000 36.06930  ? 153 TRP B CZ3 1 
ATOM   2595 C CH2 . TRP B 2 153 ? 5.97755   22.23972  56.01108  1.000 23.94085  ? 153 TRP B CH2 1 
ATOM   2596 N N   . THR B 2 154 ? 4.74527   18.77625  63.58309  1.000 20.36932  ? 154 THR B N   1 
ATOM   2597 C CA  . THR B 2 154 ? 5.43228   17.99547  64.60129  1.000 26.64649  ? 154 THR B CA  1 
ATOM   2598 C C   . THR B 2 154 ? 4.99422   16.54529  64.47983  1.000 30.97097  ? 154 THR B C   1 
ATOM   2599 O O   . THR B 2 154 ? 3.91587   16.23943  63.96452  1.000 28.92464  ? 154 THR B O   1 
ATOM   2600 C CB  . THR B 2 154 ? 5.14769   18.48258  66.02950  1.000 29.38771  ? 154 THR B CB  1 
ATOM   2601 O OG1 . THR B 2 154 ? 3.79662   18.16153  66.38307  1.000 27.48735  ? 154 THR B OG1 1 
ATOM   2602 C CG2 . THR B 2 154 ? 5.36036   19.98473  66.15162  1.000 28.36271  ? 154 THR B CG2 1 
ATOM   2603 N N   . PHE B 2 155 ? 5.84625   15.65564  64.96695  1.000 24.16924  ? 155 PHE B N   1 
ATOM   2604 C CA  . PHE B 2 155 ? 5.57316   14.23052  65.01244  1.000 23.35213  ? 155 PHE B CA  1 
ATOM   2605 C C   . PHE B 2 155 ? 5.59086   13.74618  66.45515  1.000 33.65833  ? 155 PHE B C   1 
ATOM   2606 O O   . PHE B 2 155 ? 6.03970   14.44389  67.37150  1.000 27.13289  ? 155 PHE B O   1 
ATOM   2607 C CB  . PHE B 2 155 ? 6.60760   13.44055  64.20170  1.000 28.97216  ? 155 PHE B CB  1 
ATOM   2608 C CG  . PHE B 2 155 ? 6.55461   13.70118  62.72838  1.000 29.97796  ? 155 PHE B CG  1 
ATOM   2609 C CD1 . PHE B 2 155 ? 5.71053   12.96477  61.91415  1.000 25.04019  ? 155 PHE B CD1 1 
ATOM   2610 C CD2 . PHE B 2 155 ? 7.35573   14.67020  62.15494  1.000 26.50877  ? 155 PHE B CD2 1 
ATOM   2611 C CE1 . PHE B 2 155 ? 5.66337   13.19166  60.55809  1.000 24.93459  ? 155 PHE B CE1 1 
ATOM   2612 C CE2 . PHE B 2 155 ? 7.31063   14.90198  60.79752  1.000 31.51279  ? 155 PHE B CE2 1 
ATOM   2613 C CZ  . PHE B 2 155 ? 6.46487   14.15987  59.99871  1.000 28.66752  ? 155 PHE B CZ  1 
ATOM   2614 N N   . GLN B 2 156 ? 5.10705   12.52100  66.64396  1.000 29.46735  ? 156 GLN B N   1 
ATOM   2615 C CA  . GLN B 2 156 ? 5.28467   11.82653  67.90681  1.000 24.19165  ? 156 GLN B CA  1 
ATOM   2616 C C   . GLN B 2 156 ? 5.36196   10.33453  67.63566  1.000 25.44940  ? 156 GLN B C   1 
ATOM   2617 O O   . GLN B 2 156 ? 5.00444   9.85893   66.55676  1.000 25.48006  ? 156 GLN B O   1 
ATOM   2618 C CB  . GLN B 2 156 ? 4.16549   12.13991  68.89975  1.000 23.24694  ? 156 GLN B CB  1 
ATOM   2619 C CG  . GLN B 2 156 ? 2.76402   11.75587  68.45383  1.000 29.74562  ? 156 GLN B CG  1 
ATOM   2620 C CD  . GLN B 2 156 ? 1.74594   12.03228  69.54590  1.000 31.32302  ? 156 GLN B CD  1 
ATOM   2621 O OE1 . GLN B 2 156 ? 1.88549   11.54704  70.66562  1.000 40.28527  ? 156 GLN B OE1 1 
ATOM   2622 N NE2 . GLN B 2 156 ? 0.73898   12.83760  69.23688  1.000 25.52305  ? 156 GLN B NE2 1 
ATOM   2623 N N   . ILE B 2 157 ? 5.85200   9.59768   68.62974  1.000 28.00914  ? 157 ILE B N   1 
ATOM   2624 C CA  . ILE B 2 157 ? 5.95497   8.14991   68.52207  1.000 26.51922  ? 157 ILE B CA  1 
ATOM   2625 C C   . ILE B 2 157 ? 6.02240   7.58305   69.93095  1.000 26.71691  ? 157 ILE B C   1 
ATOM   2626 O O   . ILE B 2 157 ? 6.58247   8.20025   70.83953  1.000 29.62359  ? 157 ILE B O   1 
ATOM   2627 C CB  . ILE B 2 157 ? 7.17494   7.72720   67.66132  1.000 23.95128  ? 157 ILE B CB  1 
ATOM   2628 C CG1 . ILE B 2 157 ? 7.09260   6.23694   67.32286  1.000 30.16742  ? 157 ILE B CG1 1 
ATOM   2629 C CG2 . ILE B 2 157 ? 8.49222   8.05156   68.37082  1.000 22.45925  ? 157 ILE B CG2 1 
ATOM   2630 C CD1 . ILE B 2 157 ? 8.21718   5.74343   66.44989  1.000 23.49621  ? 157 ILE B CD1 1 
ATOM   2631 N N   . LEU B 2 158 ? 5.42782   6.41062   70.11267  1.000 26.78087  ? 158 LEU B N   1 
ATOM   2632 C CA  . LEU B 2 158 ? 5.40025   5.71461   71.38939  1.000 31.01367  ? 158 LEU B CA  1 
ATOM   2633 C C   . LEU B 2 158 ? 6.14544   4.40101   71.22990  1.000 34.10573  ? 158 LEU B C   1 
ATOM   2634 O O   . LEU B 2 158 ? 5.93856   3.68296   70.24500  1.000 34.80255  ? 158 LEU B O   1 
ATOM   2635 C CB  . LEU B 2 158 ? 3.96301   5.45361   71.85261  1.000 25.79815  ? 158 LEU B CB  1 
ATOM   2636 C CG  . LEU B 2 158 ? 3.17796   6.51257   72.63319  1.000 39.22419  ? 158 LEU B CG  1 
ATOM   2637 C CD1 . LEU B 2 158 ? 3.21675   7.88690   71.97934  1.000 36.10636  ? 158 LEU B CD1 1 
ATOM   2638 C CD2 . LEU B 2 158 ? 1.74244   6.04066   72.77873  1.000 35.67587  ? 158 LEU B CD2 1 
ATOM   2639 N N   . VAL B 2 159 ? 7.01505   4.09458   72.18875  1.000 25.76880  ? 159 VAL B N   1 
ATOM   2640 C CA  . VAL B 2 159 ? 7.82872   2.88502   72.15684  1.000 31.86128  ? 159 VAL B CA  1 
ATOM   2641 C C   . VAL B 2 159 ? 7.60028   2.14132   73.46617  1.000 35.09227  ? 159 VAL B C   1 
ATOM   2642 O O   . VAL B 2 159 ? 8.07341   2.57771   74.52393  1.000 32.63526  ? 159 VAL B O   1 
ATOM   2643 C CB  . VAL B 2 159 ? 9.31782   3.19307   71.94663  1.000 29.63685  ? 159 VAL B CB  1 
ATOM   2644 C CG1 . VAL B 2 159 ? 10.11429  1.90395   71.81979  1.000 32.28576  ? 159 VAL B CG1 1 
ATOM   2645 C CG2 . VAL B 2 159 ? 9.49794   4.05837   70.71535  1.000 23.83231  ? 159 VAL B CG2 1 
ATOM   2646 N N   . MET B 2 160 ? 6.87429   1.02566   73.39852  1.000 39.12796  ? 160 MET B N   1 
ATOM   2647 C CA  . MET B 2 160 ? 6.58209   0.21355   74.57173  1.000 35.48070  ? 160 MET B CA  1 
ATOM   2648 C C   . MET B 2 160 ? 7.66127   -0.84313  74.77612  1.000 40.75500  ? 160 MET B C   1 
ATOM   2649 O O   . MET B 2 160 ? 8.19583   -1.39801  73.81227  1.000 42.10103  ? 160 MET B O   1 
ATOM   2650 C CB  . MET B 2 160 ? 5.21547   -0.46617  74.44212  1.000 37.75151  ? 160 MET B CB  1 
ATOM   2651 C CG  . MET B 2 160 ? 4.00812   0.43600   74.71323  1.000 53.45476  ? 160 MET B CG  1 
ATOM   2652 S SD  . MET B 2 160 ? 3.62438   1.61292   73.39469  1.000 75.80923  ? 160 MET B SD  1 
ATOM   2653 C CE  . MET B 2 160 ? 3.11873   0.51130   72.07378  1.000 51.81247  ? 160 MET B CE  1 
ATOM   2654 N N   . LEU B 2 161 ? 7.97258   -1.11809  76.04243  1.000 30.34262  ? 161 LEU B N   1 
ATOM   2655 C CA  . LEU B 2 161 ? 8.89467   -2.18107  76.42256  1.000 33.95777  ? 161 LEU B CA  1 
ATOM   2656 C C   . LEU B 2 161 ? 8.18916   -3.11239  77.39690  1.000 40.26750  ? 161 LEU B C   1 
ATOM   2657 O O   . LEU B 2 161 ? 7.75739   -2.67893  78.47064  1.000 45.74466  ? 161 LEU B O   1 
ATOM   2658 C CB  . LEU B 2 161 ? 10.16843  -1.61298  77.05573  1.000 33.11096  ? 161 LEU B CB  1 
ATOM   2659 C CG  . LEU B 2 161 ? 11.09319  -2.64408  77.71127  1.000 34.65013  ? 161 LEU B CG  1 
ATOM   2660 C CD1 . LEU B 2 161 ? 11.68414  -3.57159  76.66102  1.000 30.16595  ? 161 LEU B CD1 1 
ATOM   2661 C CD2 . LEU B 2 161 ? 12.19786  -1.97573  78.53776  1.000 32.92669  ? 161 LEU B CD2 1 
ATOM   2662 N N   . GLU B 2 162 ? 8.05729   -4.38007  77.01777  1.000 34.08747  ? 162 GLU B N   1 
ATOM   2663 C CA  . GLU B 2 162 ? 7.56775   -5.38804  77.94706  1.000 41.53664  ? 162 GLU B CA  1 
ATOM   2664 C C   . GLU B 2 162 ? 8.66864   -5.71161  78.94556  1.000 40.93513  ? 162 GLU B C   1 
ATOM   2665 O O   . GLU B 2 162 ? 9.80405   -6.00465  78.55913  1.000 44.22984  ? 162 GLU B O   1 
ATOM   2666 C CB  . GLU B 2 162 ? 7.13403   -6.64624  77.19570  1.000 48.15064  ? 162 GLU B CB  1 
ATOM   2667 N N   . MET B 2 163 ? 8.34508   -5.64062  80.23076  1.000 33.77548  ? 163 MET B N   1 
ATOM   2668 C CA  . MET B 2 163 ? 9.37287   -5.71369  81.25259  1.000 44.62784  ? 163 MET B CA  1 
ATOM   2669 C C   . MET B 2 163 ? 8.87115   -6.50643  82.44757  1.000 39.44840  ? 163 MET B C   1 
ATOM   2670 O O   . MET B 2 163 ? 7.68672   -6.47519  82.78598  1.000 45.31645  ? 163 MET B O   1 
ATOM   2671 C CB  . MET B 2 163 ? 9.80085   -4.30936  81.70645  1.000 34.35198  ? 163 MET B CB  1 
ATOM   2672 C CG  . MET B 2 163 ? 8.66640   -3.49541  82.31380  1.000 32.13956  ? 163 MET B CG  1 
ATOM   2673 S SD  . MET B 2 163 ? 9.24151   -2.40467  83.62307  1.000 51.22184  ? 163 MET B SD  1 
ATOM   2674 C CE  . MET B 2 163 ? 7.69566   -1.81653  84.31119  1.000 50.06953  ? 163 MET B CE  1 
ATOM   2675 N N   . THR B 2 164 ? 9.79050   -7.22891  83.07515  1.000 47.06567  ? 164 THR B N   1 
ATOM   2676 C CA  . THR B 2 164 ? 9.57420   -7.80663  84.40090  1.000 48.63808  ? 164 THR B CA  1 
ATOM   2677 C C   . THR B 2 164 ? 10.64456  -7.21824  85.31004  1.000 38.87725  ? 164 THR B C   1 
ATOM   2678 O O   . THR B 2 164 ? 11.78011  -7.72301  85.35268  1.000 37.59252  ? 164 THR B O   1 
ATOM   2679 C CB  . THR B 2 164 ? 9.63998   -9.33405  84.37039  1.000 51.99611  ? 164 THR B CB  1 
ATOM   2680 O OG1 . THR B 2 164 ? 10.69042  -9.75439  83.49232  1.000 56.16980  ? 164 THR B OG1 1 
ATOM   2681 C CG2 . THR B 2 164 ? 8.31493   -9.91385  83.88439  1.000 53.46407  ? 164 THR B CG2 1 
ATOM   2682 N N   . PRO B 2 165 ? 10.33980  -6.14985  86.04644  1.000 40.33434  ? 165 PRO B N   1 
ATOM   2683 C CA  . PRO B 2 165 ? 11.40055  -5.37015  86.70131  1.000 46.97503  ? 165 PRO B CA  1 
ATOM   2684 C C   . PRO B 2 165 ? 11.82915  -5.95197  88.04332  1.000 49.21098  ? 165 PRO B C   1 
ATOM   2685 O O   . PRO B 2 165 ? 10.99626  -6.31875  88.87762  1.000 42.33604  ? 165 PRO B O   1 
ATOM   2686 C CB  . PRO B 2 165 ? 10.76389  -3.98669  86.87654  1.000 47.89657  ? 165 PRO B CB  1 
ATOM   2687 C CG  . PRO B 2 165 ? 9.26374   -4.20902  86.76595  1.000 48.77830  ? 165 PRO B CG  1 
ATOM   2688 C CD  . PRO B 2 165 ? 8.99691   -5.61153  86.31263  1.000 40.35836  ? 165 PRO B CD  1 
ATOM   2689 N N   . GLN B 2 166 ? 13.14696  -6.03241  88.23504  1.000 37.52706  ? 166 GLN B N   1 
ATOM   2690 C CA  . GLN B 2 166 ? 13.75086  -6.29180  89.53197  1.000 39.67874  ? 166 GLN B CA  1 
ATOM   2691 C C   . GLN B 2 166 ? 14.00437  -4.97059  90.23874  1.000 32.98856  ? 166 GLN B C   1 
ATOM   2692 O O   . GLN B 2 166 ? 14.34814  -3.97284  89.60032  1.000 35.79861  ? 166 GLN B O   1 
ATOM   2693 C CB  . GLN B 2 166 ? 15.07176  -7.04559  89.37870  1.000 40.69620  ? 166 GLN B CB  1 
ATOM   2694 C CG  . GLN B 2 166 ? 14.98040  -8.30944  88.55540  1.000 59.00928  ? 166 GLN B CG  1 
ATOM   2695 C CD  . GLN B 2 166 ? 14.14969  -9.36957  89.23194  1.000 67.43754  ? 166 GLN B CD  1 
ATOM   2696 O OE1 . GLN B 2 166 ? 14.56530  -9.95348  90.23585  1.000 61.32593  ? 166 GLN B OE1 1 
ATOM   2697 N NE2 . GLN B 2 166 ? 12.96091  -9.62232  88.69180  1.000 60.83836  ? 166 GLN B NE2 1 
ATOM   2698 N N   . ARG B 2 167 ? 13.83508  -4.96602  91.55789  1.000 36.31734  ? 167 ARG B N   1 
ATOM   2699 C CA  . ARG B 2 167 ? 14.09072  -3.75221  92.31955  1.000 29.48056  ? 167 ARG B CA  1 
ATOM   2700 C C   . ARG B 2 167 ? 15.53342  -3.31517  92.11068  1.000 29.83499  ? 167 ARG B C   1 
ATOM   2701 O O   . ARG B 2 167 ? 16.46130  -4.11804  92.23704  1.000 35.27913  ? 167 ARG B O   1 
ATOM   2702 C CB  . ARG B 2 167 ? 13.80859  -3.97927  93.80338  1.000 35.86157  ? 167 ARG B CB  1 
ATOM   2703 C CG  . ARG B 2 167 ? 13.83702  -2.70590  94.63072  1.000 37.30562  ? 167 ARG B CG  1 
ATOM   2704 C CD  . ARG B 2 167 ? 13.54085  -2.99820  96.08280  1.000 36.55631  ? 167 ARG B CD  1 
ATOM   2705 N NE  . ARG B 2 167 ? 14.56484  -3.85162  96.66751  1.000 34.44191  ? 167 ARG B NE  1 
ATOM   2706 C CZ  . ARG B 2 167 ? 14.40915  -4.55599  97.77874  1.000 40.01478  ? 167 ARG B CZ  1 
ATOM   2707 N NH1 . ARG B 2 167 ? 13.26181  -4.55956  98.43829  1.000 42.03634  ? 167 ARG B NH1 1 
ATOM   2708 N NH2 . ARG B 2 167 ? 15.42955  -5.27630  98.23749  1.000 40.68588  ? 167 ARG B NH2 1 
ATOM   2709 N N   . GLY B 2 168 ? 15.71586  -2.04509  91.75315  1.000 34.69284  ? 168 GLY B N   1 
ATOM   2710 C CA  . GLY B 2 168 ? 17.01437  -1.49922  91.43723  1.000 21.05542  ? 168 GLY B CA  1 
ATOM   2711 C C   . GLY B 2 168 ? 17.27962  -1.33454  89.95583  1.000 27.41730  ? 168 GLY B C   1 
ATOM   2712 O O   . GLY B 2 168 ? 18.14478  -0.53680  89.58504  1.000 33.09285  ? 168 GLY B O   1 
ATOM   2713 N N   . ASP B 2 169 ? 16.55808  -2.06550  89.10590  1.000 27.32429  ? 169 ASP B N   1 
ATOM   2714 C CA  . ASP B 2 169 ? 16.72686  -1.93897  87.66270  1.000 37.01387  ? 169 ASP B CA  1 
ATOM   2715 C C   . ASP B 2 169 ? 16.46919  -0.51056  87.20556  1.000 31.88256  ? 169 ASP B C   1 
ATOM   2716 O O   . ASP B 2 169 ? 15.50297  0.13324   87.62677  1.000 30.53264  ? 169 ASP B O   1 
ATOM   2717 C CB  . ASP B 2 169 ? 15.77226  -2.87723  86.92053  1.000 32.16615  ? 169 ASP B CB  1 
ATOM   2718 C CG  . ASP B 2 169 ? 16.23657  -4.31832  86.92380  1.000 34.38344  ? 169 ASP B CG  1 
ATOM   2719 O OD1 . ASP B 2 169 ? 17.42570  -4.57342  87.22231  1.000 38.30299  ? 169 ASP B OD1 1 
ATOM   2720 O OD2 . ASP B 2 169 ? 15.40159  -5.19546  86.60746  1.000 38.60076  ? 169 ASP B OD2 1 
ATOM   2721 N N   . VAL B 2 170 ? 17.32677  -0.02164  86.31780  1.000 21.43502  ? 170 VAL B N   1 
ATOM   2722 C CA  . VAL B 2 170 ? 17.15813  1.29434   85.71962  1.000 28.30835  ? 170 VAL B CA  1 
ATOM   2723 C C   . VAL B 2 170 ? 16.88332  1.09992   84.23307  1.000 30.02038  ? 170 VAL B C   1 
ATOM   2724 O O   . VAL B 2 170 ? 17.70954  0.54284   83.49928  1.000 28.56018  ? 170 VAL B O   1 
ATOM   2725 C CB  . VAL B 2 170 ? 18.37742  2.19728   85.97211  1.000 29.09986  ? 170 VAL B CB  1 
ATOM   2726 C CG1 . VAL B 2 170 ? 19.66710  1.47190   85.63552  1.000 40.23014  ? 170 VAL B CG1 1 
ATOM   2727 C CG2 . VAL B 2 170 ? 18.25074  3.50087   85.18282  1.000 27.26812  ? 170 VAL B CG2 1 
ATOM   2728 N N   . TYR B 2 171 ? 15.70504  1.52390   83.79914  1.000 32.69465  ? 171 TYR B N   1 
ATOM   2729 C CA  . TYR B 2 171 ? 15.31295  1.46199   82.40028  1.000 30.98969  ? 171 TYR B CA  1 
ATOM   2730 C C   . TYR B 2 171 ? 15.48892  2.84144   81.78640  1.000 25.27115  ? 171 TYR B C   1 
ATOM   2731 O O   . TYR B 2 171 ? 14.99568  3.83404   82.33155  1.000 28.12935  ? 171 TYR B O   1 
ATOM   2732 C CB  . TYR B 2 171 ? 13.86595  0.98885   82.25894  1.000 22.94608  ? 171 TYR B CB  1 
ATOM   2733 C CG  . TYR B 2 171 ? 13.65292  -0.44594  82.68601  1.000 35.93383  ? 171 TYR B CG  1 
ATOM   2734 C CD1 . TYR B 2 171 ? 13.41886  -0.77494  84.02419  1.000 34.53933  ? 171 TYR B CD1 1 
ATOM   2735 C CD2 . TYR B 2 171 ? 13.69091  -1.47556  81.75450  1.000 27.51977  ? 171 TYR B CD2 1 
ATOM   2736 C CE1 . TYR B 2 171 ? 13.22717  -2.09478  84.41486  1.000 31.85287  ? 171 TYR B CE1 1 
ATOM   2737 C CE2 . TYR B 2 171 ? 13.50004  -2.79414  82.13450  1.000 36.82735  ? 171 TYR B CE2 1 
ATOM   2738 C CZ  . TYR B 2 171 ? 13.26778  -3.09889  83.46015  1.000 39.52828  ? 171 TYR B CZ  1 
ATOM   2739 O OH  . TYR B 2 171 ? 13.08220  -4.41146  83.82214  1.000 41.87538  ? 171 TYR B OH  1 
ATOM   2740 N N   . THR B 2 172 ? 16.20458  2.90222   80.66841  1.000 26.63246  ? 172 THR B N   1 
ATOM   2741 C CA  . THR B 2 172 ? 16.53367  4.16068   80.01501  1.000 36.00240  ? 172 THR B CA  1 
ATOM   2742 C C   . THR B 2 172 ? 15.91912  4.18952   78.62450  1.000 33.47125  ? 172 THR B C   1 
ATOM   2743 O O   . THR B 2 172 ? 16.04748  3.22585   77.86194  1.000 28.10367  ? 172 THR B O   1 
ATOM   2744 C CB  . THR B 2 172 ? 18.04986  4.36271   79.91464  1.000 34.98356  ? 172 THR B CB  1 
ATOM   2745 O OG1 . THR B 2 172 ? 18.63304  4.27236   81.21909  1.000 37.28074  ? 172 THR B OG1 1 
ATOM   2746 C CG2 . THR B 2 172 ? 18.36585  5.73090   79.31874  1.000 29.04844  ? 172 THR B CG2 1 
ATOM   2747 N N   . CYS B 2 173 ? 15.24966  5.29072   78.30574  1.000 31.86305  ? 173 CYS B N   1 
ATOM   2748 C CA  . CYS B 2 173 ? 14.77239  5.56044   76.96027  1.000 26.48072  ? 173 CYS B CA  1 
ATOM   2749 C C   . CYS B 2 173 ? 15.79676  6.45457   76.27235  1.000 31.73404  ? 173 CYS B C   1 
ATOM   2750 O O   . CYS B 2 173 ? 16.09662  7.54853   76.76232  1.000 33.52858  ? 173 CYS B O   1 
ATOM   2751 C CB  . CYS B 2 173 ? 13.39444  6.22006   76.98679  1.000 38.95700  ? 173 CYS B CB  1 
ATOM   2752 S SG  . CYS B 2 173 ? 12.65447  6.38527   75.34630  1.000 41.04324  ? 173 CYS B SG  1 
ATOM   2753 N N   . HIS B 2 174 ? 16.33601  5.98099   75.15060  1.000 28.72364  ? 174 HIS B N   1 
ATOM   2754 C CA  . HIS B 2 174 ? 17.43711  6.62531   74.44284  1.000 33.97539  ? 174 HIS B CA  1 
ATOM   2755 C C   . HIS B 2 174 ? 16.91371  7.16462   73.11911  1.000 33.99722  ? 174 HIS B C   1 
ATOM   2756 O O   . HIS B 2 174 ? 16.41751  6.39652   72.28858  1.000 30.74765  ? 174 HIS B O   1 
ATOM   2757 C CB  . HIS B 2 174 ? 18.57125  5.62671   74.20988  1.000 39.09493  ? 174 HIS B CB  1 
ATOM   2758 C CG  . HIS B 2 174 ? 19.85499  6.24778   73.75505  1.000 39.85197  ? 174 HIS B CG  1 
ATOM   2759 N ND1 . HIS B 2 174 ? 20.15504  6.44995   72.42461  1.000 36.99971  ? 174 HIS B ND1 1 
ATOM   2760 C CD2 . HIS B 2 174 ? 20.92849  6.68789   74.45399  1.000 35.63904  ? 174 HIS B CD2 1 
ATOM   2761 C CE1 . HIS B 2 174 ? 21.35149  6.99965   72.32341  1.000 38.48980  ? 174 HIS B CE1 1 
ATOM   2762 N NE2 . HIS B 2 174 ? 21.84216  7.15573   73.54068  1.000 51.04035  ? 174 HIS B NE2 1 
ATOM   2763 N N   . VAL B 2 175 ? 17.02647  8.47538   72.91849  1.000 27.67205  ? 175 VAL B N   1 
ATOM   2764 C CA  . VAL B 2 175 ? 16.39920  9.14271   71.78182  1.000 28.97953  ? 175 VAL B CA  1 
ATOM   2765 C C   . VAL B 2 175 ? 17.45007  9.95672   71.04342  1.000 37.11669  ? 175 VAL B C   1 
ATOM   2766 O O   . VAL B 2 175 ? 18.11699  10.80837  71.64491  1.000 32.88655  ? 175 VAL B O   1 
ATOM   2767 C CB  . VAL B 2 175 ? 15.23166  10.04308  72.21812  1.000 30.50002  ? 175 VAL B CB  1 
ATOM   2768 C CG1 . VAL B 2 175 ? 14.66183  10.78173  71.01877  1.000 24.45136  ? 175 VAL B CG1 1 
ATOM   2769 C CG2 . VAL B 2 175 ? 14.15496  9.21625   72.91219  1.000 26.68827  ? 175 VAL B CG2 1 
ATOM   2770 N N   . GLU B 2 176 ? 17.58624  9.70505   69.74275  1.000 31.48617  ? 176 GLU B N   1 
ATOM   2771 C CA  . GLU B 2 176 ? 18.47922  10.45752  68.87346  1.000 34.64389  ? 176 GLU B CA  1 
ATOM   2772 C C   . GLU B 2 176 ? 17.66242  11.19242  67.82095  1.000 33.85297  ? 176 GLU B C   1 
ATOM   2773 O O   . GLU B 2 176 ? 16.73590  10.62770  67.22973  1.000 40.93023  ? 176 GLU B O   1 
ATOM   2774 C CB  . GLU B 2 176 ? 19.50776  9.53819   68.20839  1.000 39.67189  ? 176 GLU B CB  1 
ATOM   2775 C CG  . GLU B 2 176 ? 20.51092  8.95344   69.19509  1.000 46.29297  ? 176 GLU B CG  1 
ATOM   2776 C CD  . GLU B 2 176 ? 21.36461  7.85350   68.60046  1.000 47.32097  ? 176 GLU B CD  1 
ATOM   2777 O OE1 . GLU B 2 176 ? 21.04181  7.36698   67.49532  1.000 63.45517  ? 176 GLU B OE1 1 
ATOM   2778 O OE2 . GLU B 2 176 ? 22.36336  7.47467   69.24594  1.000 67.79325  ? 176 GLU B OE2 1 
ATOM   2779 N N   . HIS B 2 177 ? 18.00617  12.45908  67.59244  1.000 36.99361  ? 177 HIS B N   1 
ATOM   2780 C CA  . HIS B 2 177 ? 17.21719  13.29956  66.71879  1.000 29.91205  ? 177 HIS B CA  1 
ATOM   2781 C C   . HIS B 2 177 ? 18.11490  14.38908  66.15500  1.000 31.53057  ? 177 HIS B C   1 
ATOM   2782 O O   . HIS B 2 177 ? 18.99359  14.88103  66.87554  1.000 34.49668  ? 177 HIS B O   1 
ATOM   2783 C CB  . HIS B 2 177 ? 16.03517  13.91909  67.47181  1.000 23.26845  ? 177 HIS B CB  1 
ATOM   2784 C CG  . HIS B 2 177 ? 15.06714  14.63402  66.58658  1.000 31.78433  ? 177 HIS B CG  1 
ATOM   2785 N ND1 . HIS B 2 177 ? 15.04839  16.00560  66.45912  1.000 34.31792  ? 177 HIS B ND1 1 
ATOM   2786 C CD2 . HIS B 2 177 ? 14.09464  14.16576  65.76967  1.000 27.13017  ? 177 HIS B CD2 1 
ATOM   2787 C CE1 . HIS B 2 177 ? 14.10230  16.35174  65.60578  1.000 24.69697  ? 177 HIS B CE1 1 
ATOM   2788 N NE2 . HIS B 2 177 ? 13.50882  15.25395  65.17326  1.000 26.06830  ? 177 HIS B NE2 1 
ATOM   2789 N N   . PRO B 2 178 ? 17.92958  14.78341  64.89043  1.000 36.25568  ? 178 PRO B N   1 
ATOM   2790 C CA  . PRO B 2 178 ? 18.82225  15.79823  64.29858  1.000 30.26588  ? 178 PRO B CA  1 
ATOM   2791 C C   . PRO B 2 178 ? 18.87042  17.11112  65.06253  1.000 30.75910  ? 178 PRO B C   1 
ATOM   2792 O O   . PRO B 2 178 ? 19.82658  17.87309  64.88652  1.000 45.95564  ? 178 PRO B O   1 
ATOM   2793 C CB  . PRO B 2 178 ? 18.24405  15.99184  62.89052  1.000 30.98294  ? 178 PRO B CB  1 
ATOM   2794 C CG  . PRO B 2 178 ? 17.59942  14.67641  62.57880  1.000 28.63168  ? 178 PRO B CG  1 
ATOM   2795 C CD  . PRO B 2 178 ? 17.03028  14.18661  63.88486  1.000 25.07221  ? 178 PRO B CD  1 
ATOM   2796 N N   . SER B 2 179 ? 17.88491  17.40448  65.90373  1.000 35.87188  ? 179 SER B N   1 
ATOM   2797 C CA  . SER B 2 179 ? 17.91505  18.62437  66.69865  1.000 38.70386  ? 179 SER B CA  1 
ATOM   2798 C C   . SER B 2 179 ? 18.76803  18.49645  67.95140  1.000 38.60803  ? 179 SER B C   1 
ATOM   2799 O O   . SER B 2 179 ? 18.88989  19.47447  68.69485  1.000 36.27146  ? 179 SER B O   1 
ATOM   2800 C CB  . SER B 2 179 ? 16.49829  19.01881  67.10876  1.000 37.65367  ? 179 SER B CB  1 
ATOM   2801 O OG  . SER B 2 179 ? 16.01127  18.11413  68.08499  1.000 30.57245  ? 179 SER B OG  1 
ATOM   2802 N N   . LEU B 2 180 ? 19.34472  17.32578  68.20826  1.000 36.70886  ? 180 LEU B N   1 
ATOM   2803 C CA  . LEU B 2 180 ? 20.04600  17.03769  69.45395  1.000 44.53436  ? 180 LEU B CA  1 
ATOM   2804 C C   . LEU B 2 180 ? 21.54342  16.96172  69.19536  1.000 43.13143  ? 180 LEU B C   1 
ATOM   2805 O O   . LEU B 2 180 ? 21.99451  16.16158  68.36835  1.000 45.86362  ? 180 LEU B O   1 
ATOM   2806 C CB  . LEU B 2 180 ? 19.55188  15.72620  70.06145  1.000 37.97150  ? 180 LEU B CB  1 
ATOM   2807 C CG  . LEU B 2 180 ? 18.06097  15.68225  70.36774  1.000 31.12506  ? 180 LEU B CG  1 
ATOM   2808 C CD1 . LEU B 2 180 ? 17.65732  14.30315  70.84980  1.000 30.74796  ? 180 LEU B CD1 1 
ATOM   2809 C CD2 . LEU B 2 180 ? 17.72295  16.74441  71.39580  1.000 32.37344  ? 180 LEU B CD2 1 
ATOM   2810 N N   . GLN B 2 181 ? 22.31297  17.78406  69.91051  1.000 47.33347  ? 181 GLN B N   1 
ATOM   2811 C CA  . GLN B 2 181 ? 23.76267  17.66024  69.83780  1.000 45.57749  ? 181 GLN B CA  1 
ATOM   2812 C C   . GLN B 2 181 ? 24.25281  16.38544  70.51241  1.000 43.53505  ? 181 GLN B C   1 
ATOM   2813 O O   . GLN B 2 181 ? 25.34828  15.91208  70.19770  1.000 49.68185  ? 181 GLN B O   1 
ATOM   2814 C CB  . GLN B 2 181 ? 24.42726  18.88615  70.46117  1.000 48.74234  ? 181 GLN B CB  1 
ATOM   2815 N N   . SER B 2 182 ? 23.46099  15.81646  71.41815  1.000 41.97839  ? 182 SER B N   1 
ATOM   2816 C CA  . SER B 2 182 ? 23.75987  14.54733  72.06471  1.000 46.61114  ? 182 SER B CA  1 
ATOM   2817 C C   . SER B 2 182 ? 22.43926  13.89307  72.43808  1.000 43.26082  ? 182 SER B C   1 
ATOM   2818 O O   . SER B 2 182 ? 21.44459  14.59715  72.65467  1.000 43.81387  ? 182 SER B O   1 
ATOM   2819 C CB  . SER B 2 182 ? 24.64463  14.73971  73.30804  1.000 35.48491  ? 182 SER B CB  1 
ATOM   2820 O OG  . SER B 2 182 ? 24.04073  15.62404  74.23579  1.000 59.83488  ? 182 SER B OG  1 
ATOM   2821 N N   . PRO B 2 183 ? 22.39040  12.56117  72.52058  1.000 38.95160  ? 183 PRO B N   1 
ATOM   2822 C CA  . PRO B 2 183 ? 21.10698  11.87981  72.73902  1.000 37.02902  ? 183 PRO B CA  1 
ATOM   2823 C C   . PRO B 2 183 ? 20.44265  12.29294  74.04481  1.000 31.20813  ? 183 PRO B C   1 
ATOM   2824 O O   . PRO B 2 183 ? 21.10338  12.68813  75.00535  1.000 34.93744  ? 183 PRO B O   1 
ATOM   2825 C CB  . PRO B 2 183 ? 21.49158  10.39643  72.76612  1.000 40.73769  ? 183 PRO B CB  1 
ATOM   2826 C CG  . PRO B 2 183 ? 22.81472  10.32205  72.09105  1.000 41.06111  ? 183 PRO B CG  1 
ATOM   2827 C CD  . PRO B 2 183 ? 23.50688  11.60911  72.39264  1.000 31.71473  ? 183 PRO B CD  1 
ATOM   2828 N N   . ILE B 2 184 ? 19.11202  12.20707  74.06266  1.000 31.93859  ? 184 ILE B N   1 
ATOM   2829 C CA  . ILE B 2 184 ? 18.32800  12.40604  75.27839  1.000 25.22368  ? 184 ILE B CA  1 
ATOM   2830 C C   . ILE B 2 184 ? 18.13208  11.05657  75.95719  1.000 30.30166  ? 184 ILE B C   1 
ATOM   2831 O O   . ILE B 2 184 ? 17.78827  10.06398  75.30316  1.000 30.78273  ? 184 ILE B O   1 
ATOM   2832 C CB  . ILE B 2 184 ? 16.97215  13.06224  74.96685  1.000 26.38948  ? 184 ILE B CB  1 
ATOM   2833 C CG1 . ILE B 2 184 ? 17.14220  14.54299  74.62239  1.000 37.92330  ? 184 ILE B CG1 1 
ATOM   2834 C CG2 . ILE B 2 184 ? 16.02251  12.90562  76.14133  1.000 25.47083  ? 184 ILE B CG2 1 
ATOM   2835 C CD1 . ILE B 2 184 ? 15.86933  15.18860  74.09240  1.000 31.27286  ? 184 ILE B CD1 1 
ATOM   2836 N N   . THR B 2 185 ? 18.36452  11.01233  77.26619  1.000 32.24035  ? 185 THR B N   1 
ATOM   2837 C CA  . THR B 2 185 ? 18.12119  9.82167   78.06855  1.000 31.17675  ? 185 THR B CA  1 
ATOM   2838 C C   . THR B 2 185 ? 17.19042  10.18070  79.21601  1.000 31.90072  ? 185 THR B C   1 
ATOM   2839 O O   . THR B 2 185 ? 17.44577  11.13675  79.95315  1.000 31.92113  ? 185 THR B O   1 
ATOM   2840 C CB  . THR B 2 185 ? 19.42119  9.22498   78.62118  1.000 36.27824  ? 185 THR B CB  1 
ATOM   2841 O OG1 . THR B 2 185 ? 20.16395  10.23891  79.30828  1.000 38.36503  ? 185 THR B OG1 1 
ATOM   2842 C CG2 . THR B 2 185 ? 20.26811  8.63160   77.49996  1.000 27.06548  ? 185 THR B CG2 1 
ATOM   2843 N N   . VAL B 2 186 ? 16.10763  9.42378   79.34724  1.000 33.49951  ? 186 VAL B N   1 
ATOM   2844 C CA  . VAL B 2 186 ? 15.19287  9.50862   80.47597  1.000 21.59804  ? 186 VAL B CA  1 
ATOM   2845 C C   . VAL B 2 186 ? 15.19619  8.14696   81.15493  1.000 28.00868  ? 186 VAL B C   1 
ATOM   2846 O O   . VAL B 2 186 ? 15.17749  7.11175   80.48138  1.000 28.51638  ? 186 VAL B O   1 
ATOM   2847 C CB  . VAL B 2 186 ? 13.77171  9.91180   80.02373  1.000 27.58549  ? 186 VAL B CB  1 
ATOM   2848 C CG1 . VAL B 2 186 ? 12.77976  9.79938   81.16363  1.000 26.35515  ? 186 VAL B CG1 1 
ATOM   2849 C CG2 . VAL B 2 186 ? 13.77012  11.32751  79.46753  1.000 26.27727  ? 186 VAL B CG2 1 
ATOM   2850 N N   . GLU B 2 187 ? 15.24382  8.14060   82.48038  1.000 28.27839  ? 187 GLU B N   1 
ATOM   2851 C CA  . GLU B 2 187 ? 15.37551  6.90449   83.23644  1.000 27.78849  ? 187 GLU B CA  1 
ATOM   2852 C C   . GLU B 2 187 ? 14.11847  6.62784   84.04446  1.000 30.56795  ? 187 GLU B C   1 
ATOM   2853 O O   . GLU B 2 187 ? 13.49563  7.54703   84.58626  1.000 26.07677  ? 187 GLU B O   1 
ATOM   2854 C CB  . GLU B 2 187 ? 16.57761  6.95913   84.17873  1.000 28.06512  ? 187 GLU B CB  1 
ATOM   2855 C CG  . GLU B 2 187 ? 17.89068  7.24236   83.49282  1.000 34.97994  ? 187 GLU B CG  1 
ATOM   2856 C CD  . GLU B 2 187 ? 19.03184  7.31013   84.47825  1.000 60.52165  ? 187 GLU B CD  1 
ATOM   2857 O OE1 . GLU B 2 187 ? 18.76590  7.57353   85.67490  1.000 39.71385  ? 187 GLU B OE1 1 
ATOM   2858 O OE2 . GLU B 2 187 ? 20.18759  7.08883   84.05861  1.000 63.35307  ? 187 GLU B OE2 1 
ATOM   2859 N N   . TRP B 2 188 ? 13.76024  5.35227   84.12985  1.000 21.55574  ? 188 TRP B N   1 
ATOM   2860 C CA  . TRP B 2 188 ? 12.71535  4.89095   85.03086  1.000 24.80939  ? 188 TRP B CA  1 
ATOM   2861 C C   . TRP B 2 188 ? 13.31599  3.78906   85.88369  1.000 25.05194  ? 188 TRP B C   1 
ATOM   2862 O O   . TRP B 2 188 ? 13.73685  2.75750   85.35274  1.000 27.76222  ? 188 TRP B O   1 
ATOM   2863 C CB  . TRP B 2 188 ? 11.49052  4.38711   84.26039  1.000 22.21995  ? 188 TRP B CB  1 
ATOM   2864 C CG  . TRP B 2 188 ? 10.35185  4.00546   85.15372  1.000 29.95642  ? 188 TRP B CG  1 
ATOM   2865 C CD1 . TRP B 2 188 ? 9.33895   4.81413   85.58767  1.000 33.46683  ? 188 TRP B CD1 1 
ATOM   2866 C CD2 . TRP B 2 188 ? 10.11584  2.72030   85.73335  1.000 21.16286  ? 188 TRP B CD2 1 
ATOM   2867 N NE1 . TRP B 2 188 ? 8.48344   4.10746   86.39799  1.000 33.37750  ? 188 TRP B NE1 1 
ATOM   2868 C CE2 . TRP B 2 188 ? 8.93920   2.81963   86.50468  1.000 31.94812  ? 188 TRP B CE2 1 
ATOM   2869 C CE3 . TRP B 2 188 ? 10.77990  1.49064   85.66707  1.000 28.98825  ? 188 TRP B CE3 1 
ATOM   2870 C CZ2 . TRP B 2 188 ? 8.41530   1.73722   87.21023  1.000 30.25710  ? 188 TRP B CZ2 1 
ATOM   2871 C CZ3 . TRP B 2 188 ? 10.25915  0.41612   86.36425  1.000 31.86439  ? 188 TRP B CZ3 1 
ATOM   2872 C CH2 . TRP B 2 188 ? 9.08615   0.54605   87.12688  1.000 39.29155  ? 188 TRP B CH2 1 
ATOM   2873 N N   . ARG B 2 189 ? 13.36841  4.00968   87.19425  1.000 26.25337  ? 189 ARG B N   1 
ATOM   2874 C CA  . ARG B 2 189 ? 14.06011  3.11641   88.11718  1.000 23.94956  ? 189 ARG B CA  1 
ATOM   2875 C C   . ARG B 2 189 ? 13.04546  2.32904   88.93585  1.000 27.63654  ? 189 ARG B C   1 
ATOM   2876 O O   . ARG B 2 189 ? 12.19803  2.91871   89.61610  1.000 29.72978  ? 189 ARG B O   1 
ATOM   2877 C CB  . ARG B 2 189 ? 14.99150  3.90933   89.02829  1.000 23.55922  ? 189 ARG B CB  1 
ATOM   2878 C CG  . ARG B 2 189 ? 16.11722  4.58972   88.28985  1.000 25.66988  ? 189 ARG B CG  1 
ATOM   2879 C CD  . ARG B 2 189 ? 16.89972  5.53669   89.18537  1.000 28.29241  ? 189 ARG B CD  1 
ATOM   2880 N NE  . ARG B 2 189 ? 18.03646  6.10319   88.47075  1.000 39.00973  ? 189 ARG B NE  1 
ATOM   2881 C CZ  . ARG B 2 189 ? 19.19799  5.48094   88.30606  1.000 50.09944  ? 189 ARG B CZ  1 
ATOM   2882 N NH1 . ARG B 2 189 ? 19.41329  4.27442   88.80827  1.000 51.23927  ? 189 ARG B NH1 1 
ATOM   2883 N NH2 . ARG B 2 189 ? 20.16932  6.08439   87.62349  1.000 36.59163  ? 189 ARG B NH2 1 
ATOM   2884 N N   . ALA B 2 190 ? 13.14555  1.00247   88.88112  1.000 22.84179  ? 190 ALA B N   1 
ATOM   2885 C CA  . ALA B 2 190 ? 12.20771  0.13806   89.58876  1.000 23.07204  ? 190 ALA B CA  1 
ATOM   2886 C C   . ALA B 2 190 ? 12.45182  0.20618   91.09269  1.000 30.29296  ? 190 ALA B C   1 
ATOM   2887 O O   . ALA B 2 190 ? 13.55559  -0.08203  91.56682  1.000 30.05647  ? 190 ALA B O   1 
ATOM   2888 C CB  . ALA B 2 190 ? 12.33456  -1.30029  89.09568  1.000 20.97243  ? 190 ALA B CB  1 
ATOM   2889 N N   . GLN B 2 191 ? 11.41352  0.56470   91.84262  1.000 31.04437  ? 191 GLN B N   1 
ATOM   2890 C CA  . GLN B 2 191 ? 11.49251  0.64745   93.29135  1.000 31.77525  ? 191 GLN B CA  1 
ATOM   2891 C C   . GLN B 2 191 ? 11.06104  -0.63758  93.98795  1.000 36.97532  ? 191 GLN B C   1 
ATOM   2892 O O   . GLN B 2 191 ? 11.28063  -0.77209  95.19522  1.000 34.00497  ? 191 GLN B O   1 
ATOM   2893 C CB  . GLN B 2 191 ? 10.64646  1.82503   93.78054  1.000 27.62533  ? 191 GLN B CB  1 
ATOM   2894 C CG  . GLN B 2 191 ? 11.02523  3.13490   93.11153  1.000 19.72767  ? 191 GLN B CG  1 
ATOM   2895 C CD  . GLN B 2 191 ? 12.49267  3.47911   93.32054  1.000 28.91007  ? 191 GLN B CD  1 
ATOM   2896 O OE1 . GLN B 2 191 ? 12.92126  3.74348   94.43983  1.000 32.54362  ? 191 GLN B OE1 1 
ATOM   2897 N NE2 . GLN B 2 191 ? 13.26885  3.46117   92.24615  1.000 26.12940  ? 191 GLN B NE2 1 
ATOM   2898 N N   . SER B 2 192 ? 10.46922  -1.58301  93.26178  1.000 36.05410  ? 192 SER B N   1 
ATOM   2899 C CA  . SER B 2 192 ? 10.08265  -2.86846  93.82809  1.000 38.98126  ? 192 SER B CA  1 
ATOM   2900 C C   . SER B 2 192 ? 10.16712  -3.92820  92.73945  1.000 37.83965  ? 192 SER B C   1 
ATOM   2901 O O   . SER B 2 192 ? 10.24178  -3.61403  91.54898  1.000 40.65586  ? 192 SER B O   1 
ATOM   2902 C CB  . SER B 2 192 ? 8.67273   -2.82298  94.42792  1.000 27.05777  ? 192 SER B CB  1 
ATOM   2903 O OG  . SER B 2 192 ? 7.77162   -2.16277  93.55951  1.000 38.56622  ? 192 SER B OG  1 
ATOM   2904 N N   . THR B 2 193 ? 10.15973  -5.19311  93.15865  1.000 36.44994  ? 193 THR B N   1 
ATOM   2905 C CA  . THR B 2 193 ? 10.25037  -6.30662  92.22255  1.000 46.15286  ? 193 THR B CA  1 
ATOM   2906 C C   . THR B 2 193 ? 8.85206   -6.72104  91.78442  1.000 48.17895  ? 193 THR B C   1 
ATOM   2907 O O   . THR B 2 193 ? 7.97836   -6.96253  92.62366  1.000 46.02490  ? 193 THR B O   1 
ATOM   2908 C CB  . THR B 2 193 ? 10.98575  -7.49711  92.84322  1.000 39.18004  ? 193 THR B CB  1 
ATOM   2909 O OG1 . THR B 2 193 ? 12.33643  -7.12643  93.14727  1.000 40.73010  ? 193 THR B OG1 1 
ATOM   2910 C CG2 . THR B 2 193 ? 11.00496  -8.67078  91.87387  1.000 35.54287  ? 193 THR B CG2 1 
ATOM   2911 N N   . GLY B 2 194 ? 8.64434   -6.79271  90.47160  1.000 56.42067  ? 194 GLY B N   1 
ATOM   2912 C CA  . GLY B 2 194 ? 7.36191   -7.19270  89.92164  1.000 63.27967  ? 194 GLY B CA  1 
ATOM   2913 C C   . GLY B 2 194 ? 7.21195   -8.69563  89.78210  1.000 70.89103  ? 194 GLY B C   1 
ATOM   2914 O O   . GLY B 2 194 ? 6.77051   -9.37598  90.70965  1.000 80.20519  ? 194 GLY B O   1 
ATOM   2915 N N   . ALA C 3 1   ? 11.63097  35.18779  47.71185  1.000 68.69735  ? -1  ALA C N   1 
ATOM   2916 C CA  . ALA C 3 1   ? 10.61448  35.54970  48.68867  1.000 42.98999  ? -1  ALA C CA  1 
ATOM   2917 C C   . ALA C 3 1   ? 9.23864   35.07466  48.22840  1.000 44.57223  ? -1  ALA C C   1 
ATOM   2918 O O   . ALA C 3 1   ? 8.21552   35.45667  48.79593  1.000 46.06092  ? -1  ALA C O   1 
ATOM   2919 C CB  . ALA C 3 1   ? 10.61143  37.05510  48.92260  1.000 47.65850  ? -1  ALA C CB  1 
ATOM   2920 N N   . THR C 3 2   ? 9.22359   34.23282  47.19638  1.000 36.53997  ? 0   THR C N   1 
ATOM   2921 C CA  . THR C 3 2   ? 7.97857   33.72327  46.63563  1.000 40.22071  ? 0   THR C CA  1 
ATOM   2922 C C   . THR C 3 2   ? 8.14288   32.28436  46.16640  1.000 40.06911  ? 0   THR C C   1 
ATOM   2923 O O   . THR C 3 2   ? 9.01869   31.99015  45.34170  1.000 33.75798  ? 0   THR C O   1 
ATOM   2924 C CB  . THR C 3 2   ? 7.50869   34.58890  45.46279  1.000 41.36190  ? 0   THR C CB  1 
ATOM   2925 O OG1 . THR C 3 2   ? 6.91022   35.79152  45.95847  1.000 56.63556  ? 0   THR C OG1 1 
ATOM   2926 C CG2 . THR C 3 2   ? 6.49661   33.83841  44.60871  1.000 38.48913  ? 0   THR C CG2 1 
ATOM   2927 N N   . PRO C 3 3   ? 7.31682   31.36442  46.65310  1.000 35.32811  ? 1   PRO C N   1 
ATOM   2928 C CA  . PRO C 3 3   ? 7.30866   30.01766  46.07394  1.000 35.29220  ? 1   PRO C CA  1 
ATOM   2929 C C   . PRO C 3 3   ? 6.65666   30.02291  44.70008  1.000 37.04618  ? 1   PRO C C   1 
ATOM   2930 O O   . PRO C 3 3   ? 5.64937   30.69813  44.47146  1.000 36.67805  ? 1   PRO C O   1 
ATOM   2931 C CB  . PRO C 3 3   ? 6.50064   29.18823  47.08124  1.000 30.04943  ? 1   PRO C CB  1 
ATOM   2932 C CG  . PRO C 3 3   ? 5.84521   30.16286  48.00855  1.000 30.25096  ? 1   PRO C CG  1 
ATOM   2933 C CD  . PRO C 3 3   ? 6.26546   31.55780  47.66211  1.000 39.57900  ? 1   PRO C CD  1 
ATOM   2934 N N   . LEU C 3 4   ? 7.25510   29.27349  43.77768  1.000 30.34531  ? 2   LEU C N   1 
ATOM   2935 C CA  . LEU C 3 4   ? 6.69301   29.10491  42.44750  1.000 30.40579  ? 2   LEU C CA  1 
ATOM   2936 C C   . LEU C 3 4   ? 5.75767   27.90134  42.42804  1.000 30.05762  ? 2   LEU C C   1 
ATOM   2937 O O   . LEU C 3 4   ? 5.80750   27.02320  43.29345  1.000 29.73542  ? 2   LEU C O   1 
ATOM   2938 C CB  . LEU C 3 4   ? 7.79890   28.94146  41.40013  1.000 30.45109  ? 2   LEU C CB  1 
ATOM   2939 C CG  . LEU C 3 4   ? 8.81395   30.08780  41.30811  1.000 37.25176  ? 2   LEU C CG  1 
ATOM   2940 C CD1 . LEU C 3 4   ? 9.68994   29.97185  40.06571  1.000 30.87678  ? 2   LEU C CD1 1 
ATOM   2941 C CD2 . LEU C 3 4   ? 8.10813   31.43044  41.33770  1.000 31.18046  ? 2   LEU C CD2 1 
ATOM   2942 N N   . LEU C 3 5   ? 4.88474   27.87705  41.43320  1.000 30.13003  ? 3   LEU C N   1 
ATOM   2943 C CA  . LEU C 3 5   ? 3.90307   26.81587  41.30837  1.000 29.83148  ? 3   LEU C CA  1 
ATOM   2944 C C   . LEU C 3 5   ? 3.96319   26.22988  39.90900  1.000 29.77434  ? 3   LEU C C   1 
ATOM   2945 O O   . LEU C 3 5   ? 4.55819   26.79677  38.98974  1.000 31.80484  ? 3   LEU C O   1 
ATOM   2946 C CB  . LEU C 3 5   ? 2.48394   27.31891  41.59918  1.000 29.95344  ? 3   LEU C CB  1 
ATOM   2947 C CG  . LEU C 3 5   ? 1.87258   28.28312  40.58433  1.000 30.31640  ? 3   LEU C CG  1 
ATOM   2948 C CD1 . LEU C 3 5   ? 0.35544   28.16019  40.59236  1.000 30.28309  ? 3   LEU C CD1 1 
ATOM   2949 C CD2 . LEU C 3 5   ? 2.29157   29.71416  40.89501  1.000 41.54738  ? 3   LEU C CD2 1 
ATOM   2950 N N   . MET C 3 6   ? 3.33005   25.07940  39.75581  1.000 33.15167  ? 4   MET C N   1 
ATOM   2951 C CA  . MET C 3 6   ? 3.13714   24.47563  38.45099  1.000 29.49908  ? 4   MET C CA  1 
ATOM   2952 C C   . MET C 3 6   ? 1.74219   24.81485  37.95804  1.000 30.83470  ? 4   MET C C   1 
ATOM   2953 O O   . MET C 3 6   ? 0.76104   24.65291  38.69155  1.000 29.40924  ? 4   MET C O   1 
ATOM   2954 C CB  . MET C 3 6   ? 3.35360   22.96957  38.52126  1.000 28.93645  ? 4   MET C CB  1 
ATOM   2955 C CG  . MET C 3 6   ? 4.79497   22.65368  38.85478  1.000 31.75517  ? 4   MET C CG  1 
ATOM   2956 S SD  . MET C 3 6   ? 5.17696   20.90700  38.96427  1.000 43.19571  ? 4   MET C SD  1 
ATOM   2957 C CE  . MET C 3 6   ? 6.28827   20.92750  40.37344  1.000 28.22172  ? 4   MET C CE  1 
ATOM   2958 N N   . GLN C 3 7   ? 1.66393   25.31414  36.73113  1.000 35.29271  ? 5   GLN C N   1 
ATOM   2959 C CA  . GLN C 3 7   ? 0.40622   25.77508  36.17172  1.000 35.37304  ? 5   GLN C CA  1 
ATOM   2960 C C   . GLN C 3 7   ? -0.35942  24.62030  35.55036  1.000 29.64779  ? 5   GLN C C   1 
ATOM   2961 O O   . GLN C 3 7   ? 0.22197   23.74262  34.90586  1.000 37.07358  ? 5   GLN C O   1 
ATOM   2962 C CB  . GLN C 3 7   ? 0.65055   26.86846  35.13495  1.000 38.90221  ? 5   GLN C CB  1 
ATOM   2963 C CG  . GLN C 3 7   ? 1.06327   28.18986  35.75914  1.000 52.37324  ? 5   GLN C CG  1 
ATOM   2964 C CD  . GLN C 3 7   ? 1.45276   29.22048  34.72846  1.000 72.01890  ? 5   GLN C CD  1 
ATOM   2965 O OE1 . GLN C 3 7   ? 2.08859   28.89815  33.72521  1.000 68.85004  ? 5   GLN C OE1 1 
ATOM   2966 N NE2 . GLN C 3 7   ? 1.06791   30.47095  34.96460  1.000 76.69313  ? 5   GLN C NE2 1 
ATOM   2967 N N   . ALA C 3 8   ? -1.67069  24.62587  35.76195  1.000 33.76166  ? 6   ALA C N   1 
ATOM   2968 C CA  . ALA C 3 8   ? -2.54702  23.62648  35.17381  1.000 31.87374  ? 6   ALA C CA  1 
ATOM   2969 C C   . ALA C 3 8   ? -2.83657  23.97852  33.71897  1.000 33.75292  ? 6   ALA C C   1 
ATOM   2970 O O   . ALA C 3 8   ? -2.96216  25.15467  33.36288  1.000 29.98549  ? 6   ALA C O   1 
ATOM   2971 C CB  . ALA C 3 8   ? -3.84682  23.53319  35.97376  1.000 30.01874  ? 6   ALA C CB  1 
ATOM   2972 N N   . LEU C 3 9   ? -2.93382  22.94707  32.87172  1.000 32.08646  ? 7   LEU C N   1 
ATOM   2973 C CA  . LEU C 3 9   ? -3.15764  23.16914  31.45220  1.000 29.54313  ? 7   LEU C CA  1 
ATOM   2974 C C   . LEU C 3 9   ? -4.58099  22.79742  31.06212  1.000 40.65674  ? 7   LEU C C   1 
ATOM   2975 O O   . LEU C 3 9   ? -5.08308  21.74586  31.47788  1.000 36.25994  ? 7   LEU C O   1 
ATOM   2976 C CB  . LEU C 3 9   ? -2.18019  22.35288  30.60381  1.000 30.89708  ? 7   LEU C CB  1 
ATOM   2977 C CG  . LEU C 3 9   ? -0.70616  22.66389  30.83916  1.000 41.70368  ? 7   LEU C CG  1 
ATOM   2978 C CD1 . LEU C 3 9   ? 0.14565   21.59859  30.19232  1.000 31.27882  ? 7   LEU C CD1 1 
ATOM   2979 C CD2 . LEU C 3 9   ? -0.37045  24.04127  30.29334  1.000 30.76287  ? 7   LEU C CD2 1 
ATOM   2980 N N   . PRO C 3 10  ? -5.24845  23.62954  30.26487  1.000 48.20150  ? 8   PRO C N   1 
ATOM   2981 C CA  . PRO C 3 10  ? -6.61065  23.30011  29.83868  1.000 35.62068  ? 8   PRO C CA  1 
ATOM   2982 C C   . PRO C 3 10  ? -6.60711  22.12172  28.88458  1.000 36.60801  ? 8   PRO C C   1 
ATOM   2983 O O   . PRO C 3 10  ? -5.67914  21.93339  28.09554  1.000 38.45016  ? 8   PRO C O   1 
ATOM   2984 C CB  . PRO C 3 10  ? -7.08945  24.57743  29.13195  1.000 40.45808  ? 8   PRO C CB  1 
ATOM   2985 C CG  . PRO C 3 10  ? -6.08309  25.63541  29.47082  1.000 35.17869  ? 8   PRO C CG  1 
ATOM   2986 C CD  . PRO C 3 10  ? -4.79345  24.91300  29.70754  1.000 39.55451  ? 8   PRO C CD  1 
ATOM   2987 N N   . MET C 3 11  ? -7.66499  21.32005  28.96807  1.000 43.77690  ? 9   MET C N   1 
ATOM   2988 C CA  . MET C 3 11  ? -7.87889  20.22188  28.02622  1.000 56.65652  ? 9   MET C CA  1 
ATOM   2989 C C   . MET C 3 11  ? -8.72690  20.72218  26.85588  1.000 66.37216  ? 9   MET C C   1 
ATOM   2990 O O   . MET C 3 11  ? -9.89564  20.37029  26.68075  1.000 73.39409  ? 9   MET C O   1 
ATOM   2991 C CB  . MET C 3 11  ? -8.52195  19.03641  28.73091  1.000 42.40742  ? 9   MET C CB  1 
ATOM   2992 C CG  . MET C 3 11  ? -7.61138  18.38110  29.73852  1.000 38.98212  ? 9   MET C CG  1 
ATOM   2993 S SD  . MET C 3 11  ? -8.43392  17.02909  30.58946  1.000 56.07996  ? 9   MET C SD  1 
ATOM   2994 C CE  . MET C 3 11  ? -7.05200  16.32477  31.49363  1.000 46.68134  ? 9   MET C CE  1 
ATOM   2995 N N   . GLY C 3 12  ? -8.09915  21.56835  26.04493  1.000 76.74263  ? 10  GLY C N   1 
ATOM   2996 C CA  . GLY C 3 12  ? -8.75848  22.18181  24.90691  1.000 76.11453  ? 10  GLY C CA  1 
ATOM   2997 C C   . GLY C 3 12  ? -8.91509  23.68380  25.05623  1.000 78.23796  ? 10  GLY C C   1 
ATOM   2998 O O   . GLY C 3 12  ? -7.93506  24.43058  25.01697  1.000 80.30826  ? 10  GLY C O   1 
ATOM   2999 N N   . LYS D 4 4   ? -0.27025  -10.87510 21.25639  1.000 40.97051  ? 2   LYS D N   1 
ATOM   3000 C CA  . LYS D 4 4   ? -1.62792  -10.35520 21.13557  1.000 45.43833  ? 2   LYS D CA  1 
ATOM   3001 C C   . LYS D 4 4   ? -1.66747  -8.83027  21.20941  1.000 50.30790  ? 2   LYS D C   1 
ATOM   3002 O O   . LYS D 4 4   ? -2.50797  -8.19946  20.56095  1.000 48.85406  ? 2   LYS D O   1 
ATOM   3003 C CB  . LYS D 4 4   ? -2.53754  -10.95176 22.21707  1.000 57.35689  ? 2   LYS D CB  1 
ATOM   3004 C CG  . LYS D 4 4   ? -3.34550  -12.15753 21.74998  1.000 73.96331  ? 2   LYS D CG  1 
ATOM   3005 C CD  . LYS D 4 4   ? -4.20334  -11.81593 20.53253  1.000 60.57727  ? 2   LYS D CD  1 
ATOM   3006 C CE  . LYS D 4 4   ? -5.23916  -10.74908 20.86542  1.000 73.30748  ? 2   LYS D CE  1 
ATOM   3007 N NZ  . LYS D 4 4   ? -5.98406  -10.27334 19.66486  1.000 47.51906  ? 2   LYS D NZ  1 
ATOM   3008 N N   . GLU D 4 5   ? -0.76482  -8.23809  21.99779  1.000 33.49795  ? 3   GLU D N   1 
ATOM   3009 C CA  . GLU D 4 5   ? -0.71723  -6.78112  22.09278  1.000 36.02097  ? 3   GLU D CA  1 
ATOM   3010 C C   . GLU D 4 5   ? -0.38224  -6.15214  20.74563  1.000 41.01721  ? 3   GLU D C   1 
ATOM   3011 O O   . GLU D 4 5   ? -1.07381  -5.23806  20.28643  1.000 38.02532  ? 3   GLU D O   1 
ATOM   3012 C CB  . GLU D 4 5   ? 0.29507   -6.35005  23.14651  1.000 29.42034  ? 3   GLU D CB  1 
ATOM   3013 C CG  . GLU D 4 5   ? -0.19754  -6.49834  24.56211  1.000 60.48700  ? 3   GLU D CG  1 
ATOM   3014 C CD  . GLU D 4 5   ? 0.91035   -6.30932  25.56834  1.000 71.92247  ? 3   GLU D CD  1 
ATOM   3015 O OE1 . GLU D 4 5   ? 1.81630   -7.16881  25.61735  1.000 72.25623  ? 3   GLU D OE1 1 
ATOM   3016 O OE2 . GLU D 4 5   ? 0.88411   -5.29320  26.29478  1.000 77.30006  ? 3   GLU D OE2 1 
ATOM   3017 N N   . VAL D 4 6   ? 0.67591   -6.62807  20.09685  1.000 32.65700  ? 4   VAL D N   1 
ATOM   3018 C CA  . VAL D 4 6   ? 1.07484   -6.14649  18.77980  1.000 37.37310  ? 4   VAL D CA  1 
ATOM   3019 C C   . VAL D 4 6   ? 1.04839   -7.32378  17.81516  1.000 35.44003  ? 4   VAL D C   1 
ATOM   3020 O O   . VAL D 4 6   ? 1.72793   -8.33365  18.03818  1.000 35.92934  ? 4   VAL D O   1 
ATOM   3021 C CB  . VAL D 4 6   ? 2.46052   -5.48564  18.80396  1.000 37.23693  ? 4   VAL D CB  1 
ATOM   3022 C CG1 . VAL D 4 6   ? 2.89115   -5.11789  17.38918  1.000 32.39261  ? 4   VAL D CG1 1 
ATOM   3023 C CG2 . VAL D 4 6   ? 2.43484   -4.25430  19.69756  1.000 32.07615  ? 4   VAL D CG2 1 
ATOM   3024 N N   . GLU D 4 7   ? 0.27029   -7.19044  16.74322  1.000 32.61959  ? 5   GLU D N   1 
ATOM   3025 C CA  . GLU D 4 7   ? 0.12734   -8.23354  15.73448  1.000 43.67747  ? 5   GLU D CA  1 
ATOM   3026 C C   . GLU D 4 7   ? 0.44045   -7.64116  14.36540  1.000 39.37668  ? 5   GLU D C   1 
ATOM   3027 O O   . GLU D 4 7   ? -0.18413  -6.65783  13.95370  1.000 41.08621  ? 5   GLU D O   1 
ATOM   3028 C CB  . GLU D 4 7   ? -1.28632  -8.82737  15.76236  1.000 37.57118  ? 5   GLU D CB  1 
ATOM   3029 C CG  . GLU D 4 7   ? -1.38310  -10.24016 15.21273  1.000 62.95062  ? 5   GLU D CG  1 
ATOM   3030 C CD  . GLU D 4 7   ? -1.10944  -11.29501 16.26720  1.000 71.75531  ? 5   GLU D CD  1 
ATOM   3031 O OE1 . GLU D 4 7   ? -1.78072  -11.26713 17.32264  1.000 62.97155  ? 5   GLU D OE1 1 
ATOM   3032 O OE2 . GLU D 4 7   ? -0.21946  -12.14565 16.04171  1.000 68.88285  ? 5   GLU D OE2 1 
ATOM   3033 N N   . GLN D 4 8   ? 1.40521   -8.23104  13.66742  1.000 36.33609  ? 6   GLN D N   1 
ATOM   3034 C CA  . GLN D 4 8   ? 1.77456   -7.82410  12.31810  1.000 37.46242  ? 6   GLN D CA  1 
ATOM   3035 C C   . GLN D 4 8   ? 1.37787   -8.89696  11.31235  1.000 39.73461  ? 6   GLN D C   1 
ATOM   3036 O O   . GLN D 4 8   ? 1.04134   -10.02837 11.67265  1.000 42.56703  ? 6   GLN D O   1 
ATOM   3037 C CB  . GLN D 4 8   ? 3.28035   -7.56226  12.20817  1.000 26.98942  ? 6   GLN D CB  1 
ATOM   3038 C CG  . GLN D 4 8   ? 3.81244   -6.45381  13.06614  1.000 30.28381  ? 6   GLN D CG  1 
ATOM   3039 C CD  . GLN D 4 8   ? 5.27824   -6.18057  12.78945  1.000 36.32082  ? 6   GLN D CD  1 
ATOM   3040 O OE1 . GLN D 4 8   ? 6.11656   -6.25393  13.68996  1.000 26.16282  ? 6   GLN D OE1 1 
ATOM   3041 N NE2 . GLN D 4 8   ? 5.59606   -5.85767  11.53544  1.000 31.50386  ? 6   GLN D NE2 1 
ATOM   3042 N N   . ASP D 4 9   ? 1.42873   -8.52156  10.03527  1.000 34.96541  ? 7   ASP D N   1 
ATOM   3043 C CA  . ASP D 4 9   ? 1.28640   -9.49485  8.96269   1.000 41.69886  ? 7   ASP D CA  1 
ATOM   3044 C C   . ASP D 4 9   ? 2.29429   -10.62431 9.16864   1.000 43.52551  ? 7   ASP D C   1 
ATOM   3045 O O   . ASP D 4 9   ? 3.49100   -10.35628 9.36101   1.000 34.51994  ? 7   ASP D O   1 
ATOM   3046 C CB  . ASP D 4 9   ? 1.50184   -8.83953  7.59338   1.000 34.38557  ? 7   ASP D CB  1 
ATOM   3047 C CG  . ASP D 4 9   ? 0.49860   -7.73240  7.30392   1.000 36.97596  ? 7   ASP D CG  1 
ATOM   3048 O OD1 . ASP D 4 9   ? -0.70663  -7.92941  7.56874   1.000 61.68928  ? 7   ASP D OD1 1 
ATOM   3049 O OD2 . ASP D 4 9   ? 0.91976   -6.65911  6.81932   1.000 39.43286  ? 7   ASP D OD2 1 
ATOM   3050 N N   . PRO D 4 10  ? 1.86123   -11.87990 9.15518   1.000 48.82861  ? 8   PRO D N   1 
ATOM   3051 C CA  . PRO D 4 10  ? 2.75656   -12.98135 9.53602   1.000 47.29449  ? 8   PRO D CA  1 
ATOM   3052 C C   . PRO D 4 10  ? 3.83294   -13.28737 8.50926   1.000 49.99195  ? 8   PRO D C   1 
ATOM   3053 O O   . PRO D 4 10  ? 5.01094   -12.96464 8.69796   1.000 46.90896  ? 8   PRO D O   1 
ATOM   3054 C CB  . PRO D 4 10  ? 1.80229   -14.17692 9.68262   1.000 47.22019  ? 8   PRO D CB  1 
ATOM   3055 C CG  . PRO D 4 10  ? 0.41779   -13.59499 9.71418   1.000 43.21664  ? 8   PRO D CG  1 
ATOM   3056 C CD  . PRO D 4 10  ? 0.48267   -12.33693 8.91989   1.000 44.22212  ? 8   PRO D CD  1 
ATOM   3057 N N   . GLY D 4 11  ? 3.41691   -13.92740 7.41954   1.000 71.67760  ? 9   GLY D N   1 
ATOM   3058 C CA  . GLY D 4 11  ? 4.32021   -14.56061 6.49085   1.000 52.86797  ? 9   GLY D CA  1 
ATOM   3059 C C   . GLY D 4 11  ? 5.26280   -13.60393 5.80022   1.000 54.19878  ? 9   GLY D C   1 
ATOM   3060 O O   . GLY D 4 11  ? 5.10620   -12.37956 5.85457   1.000 56.28894  ? 9   GLY D O   1 
ATOM   3061 N N   . PRO D 4 12  ? 6.27866   -14.15925 5.14354   1.000 53.30890  ? 10  PRO D N   1 
ATOM   3062 C CA  . PRO D 4 12  ? 7.21563   -13.32104 4.38913   1.000 42.16526  ? 10  PRO D CA  1 
ATOM   3063 C C   . PRO D 4 12  ? 6.54067   -12.69958 3.17808   1.000 40.68654  ? 10  PRO D C   1 
ATOM   3064 O O   . PRO D 4 12  ? 5.68635   -13.31050 2.53597   1.000 42.92880  ? 10  PRO D O   1 
ATOM   3065 C CB  . PRO D 4 12  ? 8.31706   -14.30410 3.96830   1.000 47.45915  ? 10  PRO D CB  1 
ATOM   3066 C CG  . PRO D 4 12  ? 8.14856   -15.49657 4.86049   1.000 54.87985  ? 10  PRO D CG  1 
ATOM   3067 C CD  . PRO D 4 12  ? 6.68728   -15.57252 5.16630   1.000 52.91860  ? 10  PRO D CD  1 
ATOM   3068 N N   . PHE D 4 13  ? 6.92525   -11.46905 2.87243   1.000 43.70682  ? 11  PHE D N   1 
ATOM   3069 C CA  . PHE D 4 13  ? 6.48156   -10.81524 1.65203   1.000 35.36506  ? 11  PHE D CA  1 
ATOM   3070 C C   . PHE D 4 13  ? 7.54829   -11.02105 0.58502   1.000 46.48295  ? 11  PHE D C   1 
ATOM   3071 O O   . PHE D 4 13  ? 8.69239   -10.57998 0.74826   1.000 43.53290  ? 11  PHE D O   1 
ATOM   3072 C CB  . PHE D 4 13  ? 6.22240   -9.32471  1.87434   1.000 34.88761  ? 11  PHE D CB  1 
ATOM   3073 C CG  . PHE D 4 13  ? 5.00644   -9.03268  2.70823   1.000 40.53405  ? 11  PHE D CG  1 
ATOM   3074 C CD1 . PHE D 4 13  ? 4.13987   -10.04720 3.08360   1.000 32.54643  ? 11  PHE D CD1 1 
ATOM   3075 C CD2 . PHE D 4 13  ? 4.72806   -7.73564  3.11366   1.000 35.01958  ? 11  PHE D CD2 1 
ATOM   3076 C CE1 . PHE D 4 13  ? 3.02663   -9.77216  3.85326   1.000 36.78619  ? 11  PHE D CE1 1 
ATOM   3077 C CE2 . PHE D 4 13  ? 3.61627   -7.45584  3.87711   1.000 29.61959  ? 11  PHE D CE2 1 
ATOM   3078 C CZ  . PHE D 4 13  ? 2.76370   -8.47420  4.24704   1.000 34.94345  ? 11  PHE D CZ  1 
ATOM   3079 N N   . ASN D 4 14  ? 7.18057   -11.70532 -0.49255  1.000 41.28286  ? 12  ASN D N   1 
ATOM   3080 C CA  . ASN D 4 14  ? 8.03983   -11.84952 -1.66000  1.000 40.70825  ? 12  ASN D CA  1 
ATOM   3081 C C   . ASN D 4 14  ? 7.50016   -10.91943 -2.73526  1.000 32.67412  ? 12  ASN D C   1 
ATOM   3082 O O   . ASN D 4 14  ? 6.41545   -11.14308 -3.27941  1.000 35.49734  ? 12  ASN D O   1 
ATOM   3083 C CB  . ASN D 4 14  ? 8.09598   -13.29966 -2.12638  1.000 38.05884  ? 12  ASN D CB  1 
ATOM   3084 C CG  . ASN D 4 14  ? 8.85994   -14.18024 -1.15630  1.000 48.57759  ? 12  ASN D CG  1 
ATOM   3085 O OD1 . ASN D 4 14  ? 10.08508  -14.10272 -1.07027  1.000 56.27512  ? 12  ASN D OD1 1 
ATOM   3086 N ND2 . ASN D 4 14  ? 8.14061   -15.00992 -0.40891  1.000 47.68681  ? 12  ASN D ND2 1 
ATOM   3087 N N   . VAL D 4 15  ? 8.25388   -9.86837  -3.02347  1.000 37.25844  ? 13  VAL D N   1 
ATOM   3088 C CA  . VAL D 4 15  ? 7.75910   -8.75126  -3.81614  1.000 33.77721  ? 13  VAL D CA  1 
ATOM   3089 C C   . VAL D 4 15  ? 8.71396   -8.51819  -4.98017  1.000 42.71237  ? 13  VAL D C   1 
ATOM   3090 O O   . VAL D 4 15  ? 9.93919   -8.56509  -4.79522  1.000 39.39793  ? 13  VAL D O   1 
ATOM   3091 C CB  . VAL D 4 15  ? 7.60028   -7.50475  -2.93033  1.000 34.42594  ? 13  VAL D CB  1 
ATOM   3092 C CG1 . VAL D 4 15  ? 7.62246   -6.23260  -3.74791  1.000 33.58501  ? 13  VAL D CG1 1 
ATOM   3093 C CG2 . VAL D 4 15  ? 6.31570   -7.60788  -2.12572  1.000 37.56773  ? 13  VAL D CG2 1 
ATOM   3094 N N   . PRO D 4 16  ? 8.20896   -8.30379  -6.19131  1.000 33.81928  ? 14  PRO D N   1 
ATOM   3095 C CA  . PRO D 4 16  ? 9.09574   -7.95318  -7.30260  1.000 32.21767  ? 14  PRO D CA  1 
ATOM   3096 C C   . PRO D 4 16  ? 9.55719   -6.51217  -7.18118  1.000 39.87888  ? 14  PRO D C   1 
ATOM   3097 O O   . PRO D 4 16  ? 8.81548   -5.63543  -6.72662  1.000 33.29351  ? 14  PRO D O   1 
ATOM   3098 C CB  . PRO D 4 16  ? 8.21356   -8.14254  -8.54413  1.000 23.39754  ? 14  PRO D CB  1 
ATOM   3099 C CG  . PRO D 4 16  ? 6.92042   -8.72781  -8.05452  1.000 28.51470  ? 14  PRO D CG  1 
ATOM   3100 C CD  . PRO D 4 16  ? 6.80399   -8.37658  -6.61328  1.000 36.60001  ? 14  PRO D CD  1 
ATOM   3101 N N   . GLU D 4 17  ? 10.79768  -6.27365  -7.60158  1.000 26.65816  ? 15  GLU D N   1 
ATOM   3102 C CA  . GLU D 4 17  ? 11.33801  -4.92123  -7.58458  1.000 30.45343  ? 15  GLU D CA  1 
ATOM   3103 C C   . GLU D 4 17  ? 10.42523  -3.96737  -8.34561  1.000 31.09727  ? 15  GLU D C   1 
ATOM   3104 O O   . GLU D 4 17  ? 9.94065   -4.28021  -9.43620  1.000 43.47071  ? 15  GLU D O   1 
ATOM   3105 C CB  . GLU D 4 17  ? 12.73925  -4.90087  -8.19165  1.000 31.12112  ? 15  GLU D CB  1 
ATOM   3106 C CG  . GLU D 4 17  ? 13.64022  -3.87289  -7.54163  1.000 47.41784  ? 15  GLU D CG  1 
ATOM   3107 C CD  . GLU D 4 17  ? 14.97056  -3.72410  -8.24043  1.000 56.70839  ? 15  GLU D CD  1 
ATOM   3108 O OE1 . GLU D 4 17  ? 15.09300  -4.17548  -9.40179  1.000 50.30814  ? 15  GLU D OE1 1 
ATOM   3109 O OE2 . GLU D 4 17  ? 15.89450  -3.15236  -7.61929  1.000 55.15584  ? 15  GLU D OE2 1 
ATOM   3110 N N   . GLY D 4 18  ? 10.17657  -2.80083  -7.75397  1.000 36.10901  ? 16  GLY D N   1 
ATOM   3111 C CA  . GLY D 4 18  ? 9.31290   -1.79915  -8.33860  1.000 39.33982  ? 16  GLY D CA  1 
ATOM   3112 C C   . GLY D 4 18  ? 7.88929   -1.79720  -7.81344  1.000 37.25104  ? 16  GLY D C   1 
ATOM   3113 O O   . GLY D 4 18  ? 7.17223   -0.80902  -8.01419  1.000 39.39717  ? 16  GLY D O   1 
ATOM   3114 N N   . ALA D 4 19  ? 7.46341   -2.86913  -7.15005  1.000 32.32385  ? 17  ALA D N   1 
ATOM   3115 C CA  . ALA D 4 19  ? 6.11129   -2.95470  -6.62197  1.000 34.82453  ? 17  ALA D CA  1 
ATOM   3116 C C   . ALA D 4 19  ? 5.97246   -2.13703  -5.34100  1.000 34.28627  ? 17  ALA D C   1 
ATOM   3117 O O   . ALA D 4 19  ? 6.94415   -1.87090  -4.62893  1.000 33.78292  ? 17  ALA D O   1 
ATOM   3118 C CB  . ALA D 4 19  ? 5.73318   -4.40951  -6.34705  1.000 25.69136  ? 17  ALA D CB  1 
ATOM   3119 N N   . THR D 4 20  ? 4.73891   -1.73477  -5.05603  1.000 34.17079  ? 18  THR D N   1 
ATOM   3120 C CA  . THR D 4 20  ? 4.41029   -1.07822  -3.80065  1.000 32.46728  ? 18  THR D CA  1 
ATOM   3121 C C   . THR D 4 20  ? 4.01027   -2.13350  -2.77781  1.000 36.61481  ? 18  THR D C   1 
ATOM   3122 O O   . THR D 4 20  ? 3.31374   -3.09837  -3.10690  1.000 35.76260  ? 18  THR D O   1 
ATOM   3123 C CB  . THR D 4 20  ? 3.28242   -0.06140  -3.99988  1.000 30.19164  ? 18  THR D CB  1 
ATOM   3124 O OG1 . THR D 4 20  ? 3.74331   0.99637   -4.85015  1.000 37.59143  ? 18  THR D OG1 1 
ATOM   3125 C CG2 . THR D 4 20  ? 2.83294   0.52951   -2.67133  1.000 39.33021  ? 18  THR D CG2 1 
ATOM   3126 N N   . VAL D 4 21  ? 4.47706   -1.95834  -1.54213  1.000 36.50669  ? 19  VAL D N   1 
ATOM   3127 C CA  . VAL D 4 21  ? 4.26926   -2.92236  -0.46699  1.000 30.55688  ? 19  VAL D CA  1 
ATOM   3128 C C   . VAL D 4 21  ? 3.47653   -2.25667  0.64945   1.000 35.65365  ? 19  VAL D C   1 
ATOM   3129 O O   . VAL D 4 21  ? 3.72003   -1.09376  0.99206   1.000 32.32103  ? 19  VAL D O   1 
ATOM   3130 C CB  . VAL D 4 21  ? 5.60788   -3.46813  0.07215   1.000 33.90950  ? 19  VAL D CB  1 
ATOM   3131 C CG1 . VAL D 4 21  ? 5.36346   -4.56431  1.10108   1.000 38.86968  ? 19  VAL D CG1 1 
ATOM   3132 C CG2 . VAL D 4 21  ? 6.46205   -3.98391  -1.07158  1.000 43.10439  ? 19  VAL D CG2 1 
ATOM   3133 N N   . ALA D 4 22  ? 2.53340   -2.99939  1.22184   1.000 31.51112  ? 20  ALA D N   1 
ATOM   3134 C CA  . ALA D 4 22  ? 1.71257   -2.51908  2.32434   1.000 31.52828  ? 20  ALA D CA  1 
ATOM   3135 C C   . ALA D 4 22  ? 1.90716   -3.44131  3.51889   1.000 27.31083  ? 20  ALA D C   1 
ATOM   3136 O O   . ALA D 4 22  ? 1.57331   -4.62868  3.44973   1.000 35.75367  ? 20  ALA D O   1 
ATOM   3137 C CB  . ALA D 4 22  ? 0.23743   -2.45959  1.92271   1.000 36.20826  ? 20  ALA D CB  1 
ATOM   3138 N N   . PHE D 4 23  ? 2.45206   -2.89893  4.60361   1.000 34.72954  ? 21  PHE D N   1 
ATOM   3139 C CA  . PHE D 4 23  ? 2.56136   -3.60400  5.87649   1.000 26.33054  ? 21  PHE D CA  1 
ATOM   3140 C C   . PHE D 4 23  ? 1.43188   -3.15750  6.79292   1.000 27.99319  ? 21  PHE D C   1 
ATOM   3141 O O   . PHE D 4 23  ? 1.16522   -1.95648  6.90900   1.000 29.84988  ? 21  PHE D O   1 
ATOM   3142 C CB  . PHE D 4 23  ? 3.89662   -3.31426  6.55889   1.000 21.73272  ? 21  PHE D CB  1 
ATOM   3143 C CG  . PHE D 4 23  ? 5.09371   -3.81153  5.81051   1.000 26.43789  ? 21  PHE D CG  1 
ATOM   3144 C CD1 . PHE D 4 23  ? 5.70194   -3.02820  4.84410   1.000 23.07661  ? 21  PHE D CD1 1 
ATOM   3145 C CD2 . PHE D 4 23  ? 5.63526   -5.04858  6.09993   1.000 28.52547  ? 21  PHE D CD2 1 
ATOM   3146 C CE1 . PHE D 4 23  ? 6.81819   -3.48454  4.17156   1.000 28.96783  ? 21  PHE D CE1 1 
ATOM   3147 C CE2 . PHE D 4 23  ? 6.74837   -5.50647  5.43143   1.000 21.24980  ? 21  PHE D CE2 1 
ATOM   3148 C CZ  . PHE D 4 23  ? 7.34191   -4.72608  4.46907   1.000 26.40149  ? 21  PHE D CZ  1 
ATOM   3149 N N   . ASN D 4 24  ? 0.79101   -4.10986  7.46431   1.000 31.02571  ? 22  ASN D N   1 
ATOM   3150 C CA  . ASN D 4 24  ? -0.26690  -3.78561  8.40954   1.000 31.11165  ? 22  ASN D CA  1 
ATOM   3151 C C   . ASN D 4 24  ? 0.04981   -4.34231  9.78955   1.000 31.50693  ? 22  ASN D C   1 
ATOM   3152 O O   . ASN D 4 24  ? 0.72972   -5.36286  9.92832   1.000 38.50580  ? 22  ASN D O   1 
ATOM   3153 C CB  . ASN D 4 24  ? -1.62205  -4.30659  7.92921   1.000 29.58837  ? 22  ASN D CB  1 
ATOM   3154 C CG  . ASN D 4 24  ? -2.17481  -3.48582  6.79076   1.000 28.57394  ? 22  ASN D CG  1 
ATOM   3155 O OD1 . ASN D 4 24  ? -1.98936  -3.82032  5.62406   1.000 37.66023  ? 22  ASN D OD1 1 
ATOM   3156 N ND2 . ASN D 4 24  ? -2.82924  -2.38558  7.12175   1.000 26.40156  ? 22  ASN D ND2 1 
ATOM   3157 N N   . CYS D 4 25  ? -0.46676  -3.65649  10.80789  1.000 37.40124  ? 23  CYS D N   1 
ATOM   3158 C CA  . CYS D 4 25  ? -0.20478  -3.98461  12.20105  1.000 36.07146  ? 23  CYS D CA  1 
ATOM   3159 C C   . CYS D 4 25  ? -1.37741  -3.50285  13.04517  1.000 33.15574  ? 23  CYS D C   1 
ATOM   3160 O O   . CYS D 4 25  ? -1.89372  -2.40393  12.82594  1.000 37.12866  ? 23  CYS D O   1 
ATOM   3161 C CB  . CYS D 4 25  ? 1.10863   -3.34154  12.67225  1.000 31.55703  ? 23  CYS D CB  1 
ATOM   3162 S SG  . CYS D 4 25  ? 1.38523   -3.33848  14.45889  1.000 39.20830  ? 23  CYS D SG  1 
ATOM   3163 N N   . THR D 4 26  ? -1.79675  -4.32816  14.00321  1.000 31.44996  ? 24  THR D N   1 
ATOM   3164 C CA  . THR D 4 26  ? -2.89148  -3.99722  14.90882  1.000 29.56941  ? 24  THR D CA  1 
ATOM   3165 C C   . THR D 4 26  ? -2.41904  -4.06023  16.35354  1.000 31.03346  ? 24  THR D C   1 
ATOM   3166 O O   . THR D 4 26  ? -1.60473  -4.91433  16.71793  1.000 32.02961  ? 24  THR D O   1 
ATOM   3167 C CB  . THR D 4 26  ? -4.08650  -4.94071  14.72517  1.000 31.42997  ? 24  THR D CB  1 
ATOM   3168 O OG1 . THR D 4 26  ? -3.64459  -6.30400  14.75745  1.000 47.01400  ? 24  THR D OG1 1 
ATOM   3169 C CG2 . THR D 4 26  ? -4.77395  -4.66746  13.40802  1.000 37.54315  ? 24  THR D CG2 1 
ATOM   3170 N N   . TYR D 4 27  ? -2.93868  -3.15596  17.17360  1.000 30.74472  ? 25  TYR D N   1 
ATOM   3171 C CA  . TYR D 4 27  ? -2.60994  -3.09887  18.58817  1.000 28.62109  ? 25  TYR D CA  1 
ATOM   3172 C C   . TYR D 4 27  ? -3.89303  -3.18017  19.40372  1.000 35.74993  ? 25  TYR D C   1 
ATOM   3173 O O   . TYR D 4 27  ? -4.92675  -2.63771  19.00268  1.000 35.48156  ? 25  TYR D O   1 
ATOM   3174 C CB  . TYR D 4 27  ? -1.82725  -1.81753  18.92167  1.000 28.08488  ? 25  TYR D CB  1 
ATOM   3175 C CG  . TYR D 4 27  ? -2.59133  -0.52558  18.69943  1.000 27.82952  ? 25  TYR D CG  1 
ATOM   3176 C CD1 . TYR D 4 27  ? -2.59123  0.10816   17.46115  1.000 26.53069  ? 25  TYR D CD1 1 
ATOM   3177 C CD2 . TYR D 4 27  ? -3.30278  0.06378   19.73461  1.000 29.26995  ? 25  TYR D CD2 1 
ATOM   3178 C CE1 . TYR D 4 27  ? -3.28428  1.29640   17.26390  1.000 32.40926  ? 25  TYR D CE1 1 
ATOM   3179 C CE2 . TYR D 4 27  ? -3.99826  1.24322   19.54933  1.000 29.09889  ? 25  TYR D CE2 1 
ATOM   3180 C CZ  . TYR D 4 27  ? -3.98895  1.85753   18.31562  1.000 31.25685  ? 25  TYR D CZ  1 
ATOM   3181 O OH  . TYR D 4 27  ? -4.68393  3.03341   18.13882  1.000 36.39885  ? 25  TYR D OH  1 
ATOM   3182 N N   . SER D 4 28  ? -3.82436  -3.85938  20.55017  1.000 36.50147  ? 26  SER D N   1 
ATOM   3183 C CA  . SER D 4 28  ? -5.01594  -4.10522  21.35565  1.000 39.06186  ? 26  SER D CA  1 
ATOM   3184 C C   . SER D 4 28  ? -5.30947  -3.00294  22.36482  1.000 41.76347  ? 26  SER D C   1 
ATOM   3185 O O   . SER D 4 28  ? -6.48366  -2.74028  22.65043  1.000 40.61601  ? 26  SER D O   1 
ATOM   3186 C CB  . SER D 4 28  ? -4.88764  -5.43454  22.10150  1.000 28.66515  ? 26  SER D CB  1 
ATOM   3187 O OG  . SER D 4 28  ? -3.69278  -5.46076  22.85951  1.000 57.50964  ? 26  SER D OG  1 
ATOM   3188 N N   . ASN D 4 29  ? -4.28485  -2.35545  22.91813  1.000 33.88644  ? 27  ASN D N   1 
ATOM   3189 C CA  . ASN D 4 29  ? -4.49036  -1.37711  23.98527  1.000 36.52789  ? 27  ASN D CA  1 
ATOM   3190 C C   . ASN D 4 29  ? -4.87699  -0.03502  23.37702  1.000 35.62138  ? 27  ASN D C   1 
ATOM   3191 O O   . ASN D 4 29  ? -4.04724  0.63833   22.75702  1.000 39.41559  ? 27  ASN D O   1 
ATOM   3192 C CB  . ASN D 4 29  ? -3.23809  -1.24403  24.84844  1.000 33.07009  ? 27  ASN D CB  1 
ATOM   3193 C CG  . ASN D 4 29  ? -3.32332  -0.08384  25.83218  1.000 42.37280  ? 27  ASN D CG  1 
ATOM   3194 O OD1 . ASN D 4 29  ? -4.40444  0.28015   26.29976  1.000 37.70322  ? 27  ASN D OD1 1 
ATOM   3195 N ND2 . ASN D 4 29  ? -2.17510  0.50659   26.14415  1.000 41.25677  ? 27  ASN D ND2 1 
ATOM   3196 N N   . SER D 4 30  ? -6.13584  0.36111   23.57539  1.000 39.33382  ? 28  SER D N   1 
ATOM   3197 C CA  . SER D 4 30  ? -6.61132  1.64376   23.06795  1.000 33.60171  ? 28  SER D CA  1 
ATOM   3198 C C   . SER D 4 30  ? -5.80763  2.81252   23.62660  1.000 32.82119  ? 28  SER D C   1 
ATOM   3199 O O   . SER D 4 30  ? -5.69288  3.85267   22.97089  1.000 41.41199  ? 28  SER D O   1 
ATOM   3200 C CB  . SER D 4 30  ? -8.09216  1.81711   23.40826  1.000 28.45593  ? 28  SER D CB  1 
ATOM   3201 O OG  . SER D 4 30  ? -8.84313  0.70462   22.95787  1.000 46.02777  ? 28  SER D OG  1 
ATOM   3202 N N   . ALA D 4 31  ? -5.24756  2.66931   24.82916  1.000 34.42277  ? 29  ALA D N   1 
ATOM   3203 C CA  . ALA D 4 31  ? -4.49199  3.75970   25.43730  1.000 37.26687  ? 29  ALA D CA  1 
ATOM   3204 C C   . ALA D 4 31  ? -3.11621  3.95477   24.82091  1.000 28.31426  ? 29  ALA D C   1 
ATOM   3205 O O   . ALA D 4 31  ? -2.39135  4.84995   25.26453  1.000 33.63852  ? 29  ALA D O   1 
ATOM   3206 C CB  . ALA D 4 31  ? -4.34627  3.52377   26.93990  1.000 28.27072  ? 29  ALA D CB  1 
ATOM   3207 N N   . SER D 4 32  ? -2.73947  3.15362   23.82777  1.000 32.11213  ? 36  SER D N   1 
ATOM   3208 C CA  . SER D 4 32  ? -1.42273  3.28063   23.22055  1.000 27.71903  ? 36  SER D CA  1 
ATOM   3209 C C   . SER D 4 32  ? -1.23443  4.68074   22.65763  1.000 30.71792  ? 36  SER D C   1 
ATOM   3210 O O   . SER D 4 32  ? -2.11328  5.21566   21.97403  1.000 29.48158  ? 36  SER D O   1 
ATOM   3211 C CB  . SER D 4 32  ? -1.24900  2.23303   22.12663  1.000 23.25005  ? 36  SER D CB  1 
ATOM   3212 O OG  . SER D 4 32  ? -1.38718  0.93240   22.67153  1.000 37.03223  ? 36  SER D OG  1 
ATOM   3213 N N   . GLN D 4 33  ? -0.08319  5.27627   22.95633  1.000 27.24213  ? 37  GLN D N   1 
ATOM   3214 C CA  . GLN D 4 33  ? 0.14470   6.69244   22.70902  1.000 29.80642  ? 37  GLN D CA  1 
ATOM   3215 C C   . GLN D 4 33  ? 0.97073   6.95495   21.45641  1.000 24.71089  ? 37  GLN D C   1 
ATOM   3216 O O   . GLN D 4 33  ? 0.61733   7.82013   20.65139  1.000 39.58852  ? 37  GLN D O   1 
ATOM   3217 C CB  . GLN D 4 33  ? 0.83025   7.32213   23.92790  1.000 21.58633  ? 37  GLN D CB  1 
ATOM   3218 C CG  . GLN D 4 33  ? 0.95712   8.83421   23.85215  1.000 27.32476  ? 37  GLN D CG  1 
ATOM   3219 C CD  . GLN D 4 33  ? 1.47191   9.44168   25.14199  1.000 33.98650  ? 37  GLN D CD  1 
ATOM   3220 O OE1 . GLN D 4 33  ? 1.23484   8.91573   26.23597  1.000 32.99130  ? 37  GLN D OE1 1 
ATOM   3221 N NE2 . GLN D 4 33  ? 2.18643   10.55431  25.02171  1.000 31.29982  ? 37  GLN D NE2 1 
ATOM   3222 N N   . SER D 4 34  ? 2.07121   6.23187   21.27817  1.000 30.19796  ? 38  SER D N   1 
ATOM   3223 C CA  . SER D 4 34  ? 3.00938   6.50227   20.20162  1.000 27.53762  ? 38  SER D CA  1 
ATOM   3224 C C   . SER D 4 34  ? 3.30171   5.22363   19.43584  1.000 25.23489  ? 38  SER D C   1 
ATOM   3225 O O   . SER D 4 34  ? 3.23679   4.11583   19.98084  1.000 26.46979  ? 38  SER D O   1 
ATOM   3226 C CB  . SER D 4 34  ? 4.31075   7.11045   20.73279  1.000 35.38130  ? 38  SER D CB  1 
ATOM   3227 O OG  . SER D 4 34  ? 4.06511   8.38981   21.28627  1.000 37.75205  ? 38  SER D OG  1 
ATOM   3228 N N   . PHE D 4 35  ? 3.62187   5.39338   18.15785  1.000 24.49438  ? 39  PHE D N   1 
ATOM   3229 C CA  . PHE D 4 35  ? 3.74431   4.27816   17.23553  1.000 28.28649  ? 39  PHE D CA  1 
ATOM   3230 C C   . PHE D 4 35  ? 4.91418   4.53427   16.29970  1.000 25.91891  ? 39  PHE D C   1 
ATOM   3231 O O   . PHE D 4 35  ? 5.13106   5.66602   15.86101  1.000 29.84754  ? 39  PHE D O   1 
ATOM   3232 C CB  . PHE D 4 35  ? 2.43722   4.08159   16.45103  1.000 24.60190  ? 39  PHE D CB  1 
ATOM   3233 C CG  . PHE D 4 35  ? 1.21179   4.03824   17.32662  1.000 23.81546  ? 39  PHE D CG  1 
ATOM   3234 C CD1 . PHE D 4 35  ? 0.76407   2.83986   17.85595  1.000 26.79024  ? 39  PHE D CD1 1 
ATOM   3235 C CD2 . PHE D 4 35  ? 0.52097   5.19960   17.63834  1.000 28.64244  ? 39  PHE D CD2 1 
ATOM   3236 C CE1 . PHE D 4 35  ? -0.35749  2.79387   18.66830  1.000 33.66539  ? 39  PHE D CE1 1 
ATOM   3237 C CE2 . PHE D 4 35  ? -0.60155  5.16240   18.45596  1.000 36.08257  ? 39  PHE D CE2 1 
ATOM   3238 C CZ  . PHE D 4 35  ? -1.04105  3.95748   18.96769  1.000 30.66371  ? 39  PHE D CZ  1 
ATOM   3239 N N   . PHE D 4 36  ? 5.67250   3.48118   16.00828  1.000 18.80698  ? 40  PHE D N   1 
ATOM   3240 C CA  . PHE D 4 36  ? 6.87855   3.59940   15.20737  1.000 21.76772  ? 40  PHE D CA  1 
ATOM   3241 C C   . PHE D 4 36  ? 7.01555   2.37683   14.31417  1.000 25.88170  ? 40  PHE D C   1 
ATOM   3242 O O   . PHE D 4 36  ? 6.52179   1.29087   14.62353  1.000 21.43771  ? 40  PHE D O   1 
ATOM   3243 C CB  . PHE D 4 36  ? 8.14115   3.73167   16.07770  1.000 25.12330  ? 40  PHE D CB  1 
ATOM   3244 C CG  . PHE D 4 36  ? 8.01106   4.72415   17.19147  1.000 24.22480  ? 40  PHE D CG  1 
ATOM   3245 C CD1 . PHE D 4 36  ? 7.53157   4.33471   18.42830  1.000 21.52507  ? 40  PHE D CD1 1 
ATOM   3246 C CD2 . PHE D 4 36  ? 8.36472   6.04511   17.00156  1.000 28.31391  ? 40  PHE D CD2 1 
ATOM   3247 C CE1 . PHE D 4 36  ? 7.40458   5.24721   19.46054  1.000 28.18329  ? 40  PHE D CE1 1 
ATOM   3248 C CE2 . PHE D 4 36  ? 8.24430   6.96117   18.02568  1.000 30.98572  ? 40  PHE D CE2 1 
ATOM   3249 C CZ  . PHE D 4 36  ? 7.76188   6.56326   19.25882  1.000 23.36584  ? 40  PHE D CZ  1 
ATOM   3250 N N   . TRP D 4 37  ? 7.70549   2.56719   13.19790  1.000 21.02033  ? 41  TRP D N   1 
ATOM   3251 C CA  . TRP D 4 37  ? 8.19620   1.46425   12.39040  1.000 25.95460  ? 41  TRP D CA  1 
ATOM   3252 C C   . TRP D 4 37  ? 9.71367   1.39872   12.50003  1.000 24.74100  ? 41  TRP D C   1 
ATOM   3253 O O   . TRP D 4 37  ? 10.40054  2.42370   12.42534  1.000 24.68087  ? 41  TRP D O   1 
ATOM   3254 C CB  . TRP D 4 37  ? 7.77263   1.60617   10.92451  1.000 15.38606  ? 41  TRP D CB  1 
ATOM   3255 C CG  . TRP D 4 37  ? 6.34366   1.21716   10.68440  1.000 19.84125  ? 41  TRP D CG  1 
ATOM   3256 C CD1 . TRP D 4 37  ? 5.27243   2.05495   10.56641  1.000 20.94046  ? 41  TRP D CD1 1 
ATOM   3257 C CD2 . TRP D 4 37  ? 5.83358   -0.11044  10.53364  1.000 17.84504  ? 41  TRP D CD2 1 
ATOM   3258 N NE1 . TRP D 4 37  ? 4.12473   1.32975   10.34914  1.000 24.17558  ? 41  TRP D NE1 1 
ATOM   3259 C CE2 . TRP D 4 37  ? 4.44274   -0.00227  10.32314  1.000 22.56894  ? 41  TRP D CE2 1 
ATOM   3260 C CE3 . TRP D 4 37  ? 6.41899   -1.38200  10.54808  1.000 21.88769  ? 41  TRP D CE3 1 
ATOM   3261 C CZ2 . TRP D 4 37  ? 3.62720   -1.11446  10.12984  1.000 20.09755  ? 41  TRP D CZ2 1 
ATOM   3262 C CZ3 . TRP D 4 37  ? 5.60645   -2.48544  10.35651  1.000 25.14867  ? 41  TRP D CZ3 1 
ATOM   3263 C CH2 . TRP D 4 37  ? 4.22470   -2.34273  10.15034  1.000 26.33196  ? 41  TRP D CH2 1 
ATOM   3264 N N   . TYR D 4 38  ? 10.22493  0.19031   12.69925  1.000 22.64120  ? 42  TYR D N   1 
ATOM   3265 C CA  . TYR D 4 38  ? 11.65249  -0.07742  12.72804  1.000 22.97476  ? 42  TYR D CA  1 
ATOM   3266 C C   . TYR D 4 38  ? 11.99997  -1.05912  11.61859  1.000 26.23684  ? 42  TYR D C   1 
ATOM   3267 O O   . TYR D 4 38  ? 11.17755  -1.88793  11.21915  1.000 25.61911  ? 42  TYR D O   1 
ATOM   3268 C CB  . TYR D 4 38  ? 12.09591  -0.65932  14.07371  1.000 21.54493  ? 42  TYR D CB  1 
ATOM   3269 C CG  . TYR D 4 38  ? 12.33152  0.35993   15.16545  1.000 23.29884  ? 42  TYR D CG  1 
ATOM   3270 C CD1 . TYR D 4 38  ? 11.27114  1.00665   15.78637  1.000 19.72951  ? 42  TYR D CD1 1 
ATOM   3271 C CD2 . TYR D 4 38  ? 13.61739  0.65614   15.59097  1.000 23.04411  ? 42  TYR D CD2 1 
ATOM   3272 C CE1 . TYR D 4 38  ? 11.48592  1.92625   16.78409  1.000 23.68633  ? 42  TYR D CE1 1 
ATOM   3273 C CE2 . TYR D 4 38  ? 13.84179  1.57562   16.58800  1.000 22.71049  ? 42  TYR D CE2 1 
ATOM   3274 C CZ  . TYR D 4 38  ? 12.77292  2.20525   17.18659  1.000 29.61124  ? 42  TYR D CZ  1 
ATOM   3275 O OH  . TYR D 4 38  ? 12.99478  3.12212   18.18931  1.000 22.43176  ? 42  TYR D OH  1 
ATOM   3276 N N   . ARG D 4 39  ? 13.23367  -0.96436  11.13837  1.000 21.46314  ? 43  ARG D N   1 
ATOM   3277 C CA  . ARG D 4 39  ? 13.74933  -1.81490  10.07739  1.000 32.11998  ? 43  ARG D CA  1 
ATOM   3278 C C   . ARG D 4 39  ? 14.93527  -2.59660  10.61948  1.000 34.87714  ? 43  ARG D C   1 
ATOM   3279 O O   . ARG D 4 39  ? 15.81206  -2.02306  11.27373  1.000 31.13830  ? 43  ARG D O   1 
ATOM   3280 C CB  . ARG D 4 39  ? 14.16835  -0.97754  8.86373   1.000 35.45947  ? 43  ARG D CB  1 
ATOM   3281 C CG  . ARG D 4 39  ? 14.63149  -1.79004  7.67957   1.000 42.93331  ? 43  ARG D CG  1 
ATOM   3282 C CD  . ARG D 4 39  ? 15.51903  -0.96882  6.76016   1.000 37.16565  ? 43  ARG D CD  1 
ATOM   3283 N NE  . ARG D 4 39  ? 16.55501  -1.80819  6.17212   1.000 51.89937  ? 43  ARG D NE  1 
ATOM   3284 C CZ  . ARG D 4 39  ? 16.77944  -1.93314  4.87284   1.000 43.74995  ? 43  ARG D CZ  1 
ATOM   3285 N NH1 . ARG D 4 39  ? 16.10626  -1.22228  3.98434   1.000 49.02300  ? 43  ARG D NH1 1 
ATOM   3286 N NH2 . ARG D 4 39  ? 17.71095  -2.78680  4.45557   1.000 47.82482  ? 43  ARG D NH2 1 
ATOM   3287 N N   . GLN D 4 40  ? 14.96581  -3.89926  10.35414  1.000 29.12547  ? 44  GLN D N   1 
ATOM   3288 C CA  . GLN D 4 40  ? 16.05003  -4.73628  10.84855  1.000 31.76132  ? 44  GLN D CA  1 
ATOM   3289 C C   . GLN D 4 40  ? 16.51198  -5.66733  9.74322   1.000 32.29453  ? 44  GLN D C   1 
ATOM   3290 O O   . GLN D 4 40  ? 15.73664  -6.49881  9.26188   1.000 35.74342  ? 44  GLN D O   1 
ATOM   3291 C CB  . GLN D 4 40  ? 15.61625  -5.53430  12.07672  1.000 31.37501  ? 44  GLN D CB  1 
ATOM   3292 C CG  . GLN D 4 40  ? 16.73870  -6.32781  12.70585  1.000 35.99757  ? 44  GLN D CG  1 
ATOM   3293 C CD  . GLN D 4 40  ? 16.29486  -7.04717  13.95987  1.000 33.56194  ? 44  GLN D CD  1 
ATOM   3294 O OE1 . GLN D 4 40  ? 15.13969  -7.45051  14.08058  1.000 28.56031  ? 44  GLN D OE1 1 
ATOM   3295 N NE2 . GLN D 4 40  ? 17.20814  -7.19715  14.90816  1.000 35.19280  ? 44  GLN D NE2 1 
ATOM   3296 N N   . ASP D 4 41  ? 17.76868  -5.51851  9.33974   1.000 41.02151  ? 45  ASP D N   1 
ATOM   3297 C CA  . ASP D 4 41  ? 18.37493  -6.45906  8.41475   1.000 40.60303  ? 45  ASP D CA  1 
ATOM   3298 C C   . ASP D 4 41  ? 18.70090  -7.76195  9.13441   1.000 45.75356  ? 45  ASP D C   1 
ATOM   3299 O O   . ASP D 4 41  ? 18.73288  -7.83006  10.36671  1.000 44.64753  ? 45  ASP D O   1 
ATOM   3300 C CB  . ASP D 4 41  ? 19.63911  -5.87060  7.79124   1.000 41.17954  ? 45  ASP D CB  1 
ATOM   3301 C CG  . ASP D 4 41  ? 19.36135  -4.61828  6.98299   1.000 49.22145  ? 45  ASP D CG  1 
ATOM   3302 O OD1 . ASP D 4 41  ? 18.22769  -4.46566  6.47995   1.000 47.57467  ? 45  ASP D OD1 1 
ATOM   3303 O OD2 . ASP D 4 41  ? 20.28322  -3.78537  6.84748   1.000 58.86035  ? 45  ASP D OD2 1 
ATOM   3304 N N   . CYS D 4 42  ? 18.95357  -8.80115  8.34110   1.000 52.76730  ? 46  CYS D N   1 
ATOM   3305 C CA  . CYS D 4 42  ? 19.16196  -10.13660 8.88600   1.000 51.39154  ? 46  CYS D CA  1 
ATOM   3306 C C   . CYS D 4 42  ? 20.35961  -10.15481 9.83098   1.000 40.51480  ? 46  CYS D C   1 
ATOM   3307 O O   . CYS D 4 42  ? 21.41961  -9.60340  9.52175   1.000 40.01489  ? 46  CYS D O   1 
ATOM   3308 C CB  . CYS D 4 42  ? 19.36023  -11.13729 7.74521   1.000 60.11719  ? 46  CYS D CB  1 
ATOM   3309 S SG  . CYS D 4 42  ? 19.15223  -12.87960 8.20287   1.000 64.80853  ? 46  CYS D SG  1 
ATOM   3310 N N   . ARG D 4 43  ? 20.16916  -10.77096 10.99718  1.000 39.00510  ? 47  ARG D N   1 
ATOM   3311 C CA  . ARG D 4 43  ? 21.15821  -10.93623 12.06246  1.000 52.69971  ? 47  ARG D CA  1 
ATOM   3312 C C   . ARG D 4 43  ? 21.77552  -9.61714  12.53795  1.000 50.86175  ? 47  ARG D C   1 
ATOM   3313 O O   . ARG D 4 43  ? 22.76815  -9.63752  13.27966  1.000 55.17126  ? 47  ARG D O   1 
ATOM   3314 C CB  . ARG D 4 43  ? 22.26032  -11.93499 11.65711  1.000 57.51461  ? 47  ARG D CB  1 
ATOM   3315 C CG  . ARG D 4 43  ? 23.43506  -11.36966 10.85901  1.000 71.04191  ? 47  ARG D CG  1 
ATOM   3316 C CD  . ARG D 4 43  ? 24.50439  -12.42632 10.57152  1.000 72.93163  ? 47  ARG D CD  1 
ATOM   3317 N NE  . ARG D 4 43  ? 24.86790  -13.19655 11.75693  1.000 68.21376  ? 47  ARG D NE  1 
ATOM   3318 C CZ  . ARG D 4 43  ? 24.59894  -14.48515 11.92048  1.000 71.35209  ? 47  ARG D CZ  1 
ATOM   3319 N NH1 . ARG D 4 43  ? 23.97958  -15.18431 10.98353  1.000 70.95164  ? 47  ARG D NH1 1 
ATOM   3320 N NH2 . ARG D 4 43  ? 24.96908  -15.08918 13.04748  1.000 62.24570  ? 47  ARG D NH2 1 
ATOM   3321 N N   . LYS D 4 44  ? 21.19388  -8.46681  12.18114  1.000 49.82920  ? 48  LYS D N   1 
ATOM   3322 C CA  . LYS D 4 44  ? 21.70321  -7.16517  12.60067  1.000 41.52690  ? 48  LYS D CA  1 
ATOM   3323 C C   . LYS D 4 44  ? 20.73079  -6.48994  13.56964  1.000 31.36187  ? 48  LYS D C   1 
ATOM   3324 O O   . LYS D 4 44  ? 19.81459  -7.12138  14.10208  1.000 37.95774  ? 48  LYS D O   1 
ATOM   3325 C CB  . LYS D 4 44  ? 21.98213  -6.28759  11.37882  1.000 45.56978  ? 48  LYS D CB  1 
ATOM   3326 C CG  . LYS D 4 44  ? 23.02262  -6.85447  10.42759  1.000 50.88948  ? 48  LYS D CG  1 
ATOM   3327 C CD  . LYS D 4 44  ? 23.94744  -5.76280  9.90259   1.000 54.30110  ? 48  LYS D CD  1 
ATOM   3328 C CE  . LYS D 4 44  ? 24.86393  -6.27203  8.80164   1.000 60.72217  ? 48  LYS D CE  1 
ATOM   3329 N NZ  . LYS D 4 44  ? 25.74230  -5.19012  8.26766   1.000 69.18167  ? 48  LYS D NZ  1 
ATOM   3330 N N   . GLU D 4 45  ? 20.92926  -5.17856  13.79472  1.000 37.55390  ? 49  GLU D N   1 
ATOM   3331 C CA  . GLU D 4 45  ? 20.17160  -4.47970  14.82464  1.000 29.20153  ? 49  GLU D CA  1 
ATOM   3332 C C   . GLU D 4 45  ? 19.00537  -3.69439  14.23837  1.000 29.02237  ? 49  GLU D C   1 
ATOM   3333 O O   . GLU D 4 45  ? 19.01654  -3.31377  13.06389  1.000 36.33831  ? 49  GLU D O   1 
ATOM   3334 C CB  . GLU D 4 45  ? 21.07677  -3.51970  15.59494  1.000 31.02177  ? 49  GLU D CB  1 
ATOM   3335 C CG  . GLU D 4 45  ? 21.21067  -2.14136  14.96921  1.000 33.49452  ? 49  GLU D CG  1 
ATOM   3336 C CD  . GLU D 4 45  ? 22.37337  -2.06032  14.00684  1.000 36.28102  ? 49  GLU D CD  1 
ATOM   3337 O OE1 . GLU D 4 45  ? 22.81134  -3.12261  13.50734  1.000 39.39898  ? 49  GLU D OE1 1 
ATOM   3338 O OE2 . GLU D 4 45  ? 22.85309  -0.93465  13.76079  1.000 43.13116  ? 49  GLU D OE2 1 
ATOM   3339 N N   . PRO D 4 46  ? 17.97968  -3.42046  15.04130  1.000 31.51685  ? 50  PRO D N   1 
ATOM   3340 C CA  . PRO D 4 46  ? 16.85959  -2.61393  14.55458  1.000 31.65783  ? 50  PRO D CA  1 
ATOM   3341 C C   . PRO D 4 46  ? 17.25605  -1.15425  14.40329  1.000 27.93341  ? 50  PRO D C   1 
ATOM   3342 O O   . PRO D 4 46  ? 18.07105  -0.62103  15.15891  1.000 22.65393  ? 50  PRO D O   1 
ATOM   3343 C CB  . PRO D 4 46  ? 15.79517  -2.78302  15.64962  1.000 31.94075  ? 50  PRO D CB  1 
ATOM   3344 C CG  . PRO D 4 46  ? 16.29359  -3.88202  16.54398  1.000 33.84266  ? 50  PRO D CG  1 
ATOM   3345 C CD  . PRO D 4 46  ? 17.77710  -3.85312  16.43431  1.000 29.02549  ? 50  PRO D CD  1 
ATOM   3346 N N   . LYS D 4 47  ? 16.65388  -0.50246  13.41122  1.000 28.23935  ? 51  LYS D N   1 
ATOM   3347 C CA  . LYS D 4 47  ? 16.87909  0.91596   13.16645  1.000 33.43344  ? 51  LYS D CA  1 
ATOM   3348 C C   . LYS D 4 47  ? 15.54135  1.62135   13.01384  1.000 29.70401  ? 51  LYS D C   1 
ATOM   3349 O O   . LYS D 4 47  ? 14.66337  1.14477   12.28853  1.000 26.82235  ? 51  LYS D O   1 
ATOM   3350 C CB  . LYS D 4 47  ? 17.74106  1.13760   11.92190  1.000 24.83653  ? 51  LYS D CB  1 
ATOM   3351 C CG  . LYS D 4 47  ? 19.11599  0.48566   12.01529  1.000 48.58469  ? 51  LYS D CG  1 
ATOM   3352 C CD  . LYS D 4 47  ? 19.97219  0.79261   10.79142  1.000 42.11346  ? 51  LYS D CD  1 
ATOM   3353 C CE  . LYS D 4 47  ? 21.33375  0.11848   10.87505  1.000 54.97737  ? 51  LYS D CE  1 
ATOM   3354 N NZ  . LYS D 4 47  ? 22.30217  0.75858   9.94262   1.000 58.21632  ? 51  LYS D NZ  1 
ATOM   3355 N N   . LEU D 4 48  ? 15.39071  2.75063   13.69992  1.000 22.96987  ? 52  LEU D N   1 
ATOM   3356 C CA  . LEU D 4 48  ? 14.16652  3.53156   13.59951  1.000 25.82967  ? 52  LEU D CA  1 
ATOM   3357 C C   . LEU D 4 48  ? 13.96477  3.99834   12.16446  1.000 27.11814  ? 52  LEU D C   1 
ATOM   3358 O O   . LEU D 4 48  ? 14.83978  4.64317   11.58307  1.000 31.12490  ? 52  LEU D O   1 
ATOM   3359 C CB  . LEU D 4 48  ? 14.22407  4.72351   14.55547  1.000 26.22472  ? 52  LEU D CB  1 
ATOM   3360 C CG  . LEU D 4 48  ? 13.06345  5.72466   14.50735  1.000 34.92064  ? 52  LEU D CG  1 
ATOM   3361 C CD1 . LEU D 4 48  ? 11.74468  5.05471   14.87059  1.000 32.33621  ? 52  LEU D CD1 1 
ATOM   3362 C CD2 . LEU D 4 48  ? 13.33389  6.91953   15.41899  1.000 23.57386  ? 52  LEU D CD2 1 
ATOM   3363 N N   . LEU D 4 49  ? 12.81626  3.64784   11.58773  1.000 31.07767  ? 53  LEU D N   1 
ATOM   3364 C CA  . LEU D 4 49  ? 12.46260  4.04499   10.23089  1.000 25.59758  ? 53  LEU D CA  1 
ATOM   3365 C C   . LEU D 4 49  ? 11.63755  5.32949   10.22455  1.000 34.88646  ? 53  LEU D C   1 
ATOM   3366 O O   . LEU D 4 49  ? 12.03777  6.32442   9.61452   1.000 33.36261  ? 53  LEU D O   1 
ATOM   3367 C CB  . LEU D 4 49  ? 11.70880  2.90356   9.53442   1.000 27.78274  ? 53  LEU D CB  1 
ATOM   3368 C CG  . LEU D 4 49  ? 11.49386  3.01864   8.02192   1.000 34.84733  ? 53  LEU D CG  1 
ATOM   3369 C CD1 . LEU D 4 49  ? 12.82308  2.98956   7.30642   1.000 37.31857  ? 53  LEU D CD1 1 
ATOM   3370 C CD2 . LEU D 4 49  ? 10.59652  1.90472   7.51619   1.000 30.24537  ? 53  LEU D CD2 1 
ATOM   3371 N N   . MET D 4 50  ? 10.49584  5.33617   10.90957  1.000 29.18465  ? 54  MET D N   1 
ATOM   3372 C CA  . MET D 4 50  ? 9.70877   6.55637   11.01660  1.000 28.89816  ? 54  MET D CA  1 
ATOM   3373 C C   . MET D 4 50  ? 8.71809   6.44233   12.16412  1.000 40.94690  ? 54  MET D C   1 
ATOM   3374 O O   . MET D 4 50  ? 8.34249   5.34451   12.58938  1.000 23.37260  ? 54  MET D O   1 
ATOM   3375 C CB  . MET D 4 50  ? 8.96683   6.86624   9.71208   1.000 45.78130  ? 54  MET D CB  1 
ATOM   3376 C CG  . MET D 4 50  ? 8.07167   5.74971   9.20526   1.000 35.79396  ? 54  MET D CG  1 
ATOM   3377 S SD  . MET D 4 50  ? 7.98857   5.79563   7.40122   1.000 58.16050  ? 54  MET D SD  1 
ATOM   3378 C CE  . MET D 4 50  ? 7.51928   7.50173   7.10601   1.000 31.34401  ? 54  MET D CE  1 
ATOM   3379 N N   . SER D 4 51  ? 8.30710   7.60668   12.65766  1.000 29.09353  ? 55  SER D N   1 
ATOM   3380 C CA  . SER D 4 51  ? 7.17166   7.70655   13.55818  1.000 37.55689  ? 55  SER D CA  1 
ATOM   3381 C C   . SER D 4 51  ? 5.87257   7.67717   12.75966  1.000 34.92235  ? 55  SER D C   1 
ATOM   3382 O O   . SER D 4 51  ? 5.84284   8.00715   11.57072  1.000 42.93338  ? 55  SER D O   1 
ATOM   3383 C CB  . SER D 4 51  ? 7.25857   8.98839   14.38699  1.000 44.06513  ? 55  SER D CB  1 
ATOM   3384 O OG  . SER D 4 51  ? 8.53902   9.10581   14.98560  1.000 63.75854  ? 55  SER D OG  1 
ATOM   3385 N N   . VAL D 4 52  ? 4.79400   7.26963   13.42259  1.000 30.06880  ? 56  VAL D N   1 
ATOM   3386 C CA  . VAL D 4 52  ? 3.50301   7.04432   12.78234  1.000 34.97508  ? 56  VAL D CA  1 
ATOM   3387 C C   . VAL D 4 52  ? 2.50782   8.05915   13.32260  1.000 38.34826  ? 56  VAL D C   1 
ATOM   3388 O O   . VAL D 4 52  ? 2.37214   8.21670   14.54059  1.000 49.23221  ? 56  VAL D O   1 
ATOM   3389 C CB  . VAL D 4 52  ? 3.00500   5.61022   13.02480  1.000 32.43423  ? 56  VAL D CB  1 
ATOM   3390 C CG1 . VAL D 4 52  ? 1.68916   5.38454   12.31975  1.000 25.71886  ? 56  VAL D CG1 1 
ATOM   3391 C CG2 . VAL D 4 52  ? 4.04352   4.60745   12.56470  1.000 22.41622  ? 56  VAL D CG2 1 
ATOM   3392 N N   . TYR D 4 53  ? 1.80962   8.74012   12.42209  1.000 43.82150  ? 57  TYR D N   1 
ATOM   3393 C CA  . TYR D 4 53  ? 0.82195   9.73616   12.80341  1.000 48.03782  ? 57  TYR D CA  1 
ATOM   3394 C C   . TYR D 4 53  ? -0.48686  9.45779   12.07829  1.000 48.22532  ? 57  TYR D C   1 
ATOM   3395 O O   . TYR D 4 53  ? -0.52098  8.77275   11.05284  1.000 42.96571  ? 57  TYR D O   1 
ATOM   3396 C CB  . TYR D 4 53  ? 1.30244   11.16329  12.48996  1.000 47.48051  ? 57  TYR D CB  1 
ATOM   3397 C CG  . TYR D 4 53  ? 2.65592   11.50956  13.07939  1.000 61.88870  ? 57  TYR D CG  1 
ATOM   3398 C CD1 . TYR D 4 53  ? 2.82145   11.65885  14.44995  1.000 56.89971  ? 57  TYR D CD1 1 
ATOM   3399 C CD2 . TYR D 4 53  ? 3.76448   11.70219  12.26142  1.000 56.20564  ? 57  TYR D CD2 1 
ATOM   3400 C CE1 . TYR D 4 53  ? 4.05488   11.97970  14.99105  1.000 69.20059  ? 57  TYR D CE1 1 
ATOM   3401 C CE2 . TYR D 4 53  ? 5.00127   12.02454  12.79254  1.000 54.54036  ? 57  TYR D CE2 1 
ATOM   3402 C CZ  . TYR D 4 53  ? 5.14191   12.16078  14.15802  1.000 72.30327  ? 57  TYR D CZ  1 
ATOM   3403 O OH  . TYR D 4 53  ? 6.37217   12.48125  14.69337  1.000 84.44244  ? 57  TYR D OH  1 
ATOM   3404 N N   . SER D 4 54  ? -1.57438  10.00223  12.62929  1.000 47.37853  ? 58  SER D N   1 
ATOM   3405 C CA  . SER D 4 54  ? -2.87392  9.85132   11.98567  1.000 37.49308  ? 58  SER D CA  1 
ATOM   3406 C C   . SER D 4 54  ? -2.93198  10.59581  10.66030  1.000 48.21326  ? 58  SER D C   1 
ATOM   3407 O O   . SER D 4 54  ? -3.55485  10.11159  9.70815   1.000 49.97534  ? 58  SER D O   1 
ATOM   3408 C CB  . SER D 4 54  ? -3.98520  10.33632  12.91507  1.000 35.37261  ? 58  SER D CB  1 
ATOM   3409 O OG  . SER D 4 54  ? -4.13290  9.46918   14.02550  1.000 63.48439  ? 58  SER D OG  1 
ATOM   3410 N N   . SER D 4 55  ? -2.28411  11.76102  10.57414  1.000 53.36582  ? 63  SER D N   1 
ATOM   3411 C CA  . SER D 4 55  ? -2.31103  12.52920  9.33403   1.000 42.48709  ? 63  SER D CA  1 
ATOM   3412 C C   . SER D 4 55  ? -1.62613  11.78331  8.19458   1.000 57.10698  ? 63  SER D C   1 
ATOM   3413 O O   . SER D 4 55  ? -1.97315  11.98338  7.02441   1.000 61.92890  ? 63  SER D O   1 
ATOM   3414 C CB  . SER D 4 55  ? -1.65104  13.89049  9.54589   1.000 43.74662  ? 63  SER D CB  1 
ATOM   3415 O OG  . SER D 4 55  ? -0.24866  13.75760  9.68919   1.000 62.92650  ? 63  SER D OG  1 
ATOM   3416 N N   . GLY D 4 56  ? -0.66030  10.92326  8.50903   1.000 52.85869  ? 64  GLY D N   1 
ATOM   3417 C CA  . GLY D 4 56  ? 0.03901   10.17602  7.48225   1.000 50.25206  ? 64  GLY D CA  1 
ATOM   3418 C C   . GLY D 4 56  ? 1.43770   10.69476  7.22762   1.000 52.90555  ? 64  GLY D C   1 
ATOM   3419 O O   . GLY D 4 56  ? 1.64659   11.54222  6.35344   1.000 67.53965  ? 64  GLY D O   1 
ATOM   3420 N N   . ASN D 4 57  ? 2.40273   10.18961  7.99269   1.000 54.47884  ? 65  ASN D N   1 
ATOM   3421 C CA  . ASN D 4 57  ? 3.79589   10.59519  7.84681   1.000 53.25603  ? 65  ASN D CA  1 
ATOM   3422 C C   . ASN D 4 57  ? 4.36698   10.04852  6.54055   1.000 43.29492  ? 65  ASN D C   1 
ATOM   3423 O O   . ASN D 4 57  ? 4.36289   8.83307   6.31646   1.000 42.86345  ? 65  ASN D O   1 
ATOM   3424 C CB  . ASN D 4 57  ? 4.60407   10.09571  9.04394   1.000 41.90578  ? 65  ASN D CB  1 
ATOM   3425 C CG  . ASN D 4 57  ? 6.07218   10.46399  8.95405   1.000 61.71779  ? 65  ASN D CG  1 
ATOM   3426 O OD1 . ASN D 4 57  ? 6.44746   11.41080  8.25976   1.000 73.62443  ? 65  ASN D OD1 1 
ATOM   3427 N ND2 . ASN D 4 57  ? 6.91372   9.71568   9.66057   1.000 54.44342  ? 65  ASN D ND2 1 
ATOM   3428 N N   . GLU D 4 58  ? 4.86420   10.93950  5.68119   1.000 42.07275  ? 67  GLU D N   1 
ATOM   3429 C CA  . GLU D 4 58  ? 5.43392   10.55562  4.39310   1.000 53.36481  ? 67  GLU D CA  1 
ATOM   3430 C C   . GLU D 4 58  ? 6.86871   11.05297  4.30485   1.000 52.77492  ? 67  GLU D C   1 
ATOM   3431 O O   . GLU D 4 58  ? 7.12040   12.25724  4.41695   1.000 68.87286  ? 67  GLU D O   1 
ATOM   3432 C CB  . GLU D 4 58  ? 4.61365   11.11017  3.22715   1.000 46.42283  ? 67  GLU D CB  1 
ATOM   3433 C CG  . GLU D 4 58  ? 5.15501   10.69138  1.86699   1.000 55.77374  ? 67  GLU D CG  1 
ATOM   3434 C CD  . GLU D 4 58  ? 4.45143   11.37741  0.71248   1.000 72.86105  ? 67  GLU D CD  1 
ATOM   3435 O OE1 . GLU D 4 58  ? 3.76747   12.39657  0.95075   1.000 71.04889  ? 67  GLU D OE1 1 
ATOM   3436 O OE2 . GLU D 4 58  ? 4.58199   10.89491  -0.43435  1.000 80.62268  ? 67  GLU D OE2 1 
ATOM   3437 N N   . ASP D 4 59  ? 7.80248   10.12800  4.08491   1.000 39.80991  ? 68  ASP D N   1 
ATOM   3438 C CA  . ASP D 4 59  ? 9.22706   10.43540  3.96113   1.000 43.08593  ? 68  ASP D CA  1 
ATOM   3439 C C   . ASP D 4 59  ? 9.76159   9.64217   2.76715   1.000 38.45418  ? 68  ASP D C   1 
ATOM   3440 O O   . ASP D 4 59  ? 10.09152  8.45791   2.88525   1.000 43.11825  ? 68  ASP D O   1 
ATOM   3441 C CB  . ASP D 4 59  ? 9.97121   10.11153  5.26300   1.000 50.68282  ? 68  ASP D CB  1 
ATOM   3442 C CG  . ASP D 4 59  ? 11.45176  10.45555  5.19966   1.000 70.22833  ? 68  ASP D CG  1 
ATOM   3443 O OD1 . ASP D 4 59  ? 11.79532  11.51973  4.64285   1.000 68.16924  ? 68  ASP D OD1 1 
ATOM   3444 O OD2 . ASP D 4 59  ? 12.27069  9.66403   5.72283   1.000 74.38515  ? 68  ASP D OD2 1 
ATOM   3445 N N   . GLY D 4 60  ? 9.83012   10.30078  1.61140   1.000 42.33732  ? 74  GLY D N   1 
ATOM   3446 C CA  . GLY D 4 60  ? 10.36429  9.65674   0.41858   1.000 35.52821  ? 74  GLY D CA  1 
ATOM   3447 C C   . GLY D 4 60  ? 9.43520   8.57164   -0.08880  1.000 42.87317  ? 74  GLY D C   1 
ATOM   3448 O O   . GLY D 4 60  ? 8.23888   8.79303   -0.29940  1.000 40.78066  ? 74  GLY D O   1 
ATOM   3449 N N   . ARG D 4 61  ? 9.98266   7.37441   -0.27719  1.000 41.77217  ? 75  ARG D N   1 
ATOM   3450 C CA  . ARG D 4 61  ? 9.19287   6.23966   -0.73117  1.000 37.42389  ? 75  ARG D CA  1 
ATOM   3451 C C   . ARG D 4 61  ? 8.37460   5.59520   0.38220   1.000 38.26825  ? 75  ARG D C   1 
ATOM   3452 O O   . ARG D 4 61  ? 7.66740   4.61621   0.11833   1.000 40.99160  ? 75  ARG D O   1 
ATOM   3453 C CB  . ARG D 4 61  ? 10.11150  5.19933   -1.37616  1.000 35.31160  ? 75  ARG D CB  1 
ATOM   3454 C CG  . ARG D 4 61  ? 10.84476  5.70913   -2.61900  1.000 39.79610  ? 75  ARG D CG  1 
ATOM   3455 C CD  . ARG D 4 61  ? 11.66748  4.62219   -3.29764  1.000 34.14595  ? 75  ARG D CD  1 
ATOM   3456 N NE  . ARG D 4 61  ? 12.67336  4.07367   -2.39753  1.000 34.72123  ? 75  ARG D NE  1 
ATOM   3457 C CZ  . ARG D 4 61  ? 12.57115  2.90192   -1.78559  1.000 36.18392  ? 75  ARG D CZ  1 
ATOM   3458 N NH1 . ARG D 4 61  ? 11.54564  2.09271   -2.00529  1.000 31.49484  ? 75  ARG D NH1 1 
ATOM   3459 N NH2 . ARG D 4 61  ? 13.51597  2.53593   -0.92568  1.000 31.98495  ? 75  ARG D NH2 1 
ATOM   3460 N N   . PHE D 4 62  ? 8.43487   6.11940   1.60302   1.000 34.39357  ? 76  PHE D N   1 
ATOM   3461 C CA  . PHE D 4 62  ? 7.81978   5.48486   2.75830   1.000 38.09039  ? 76  PHE D CA  1 
ATOM   3462 C C   . PHE D 4 62  ? 6.65965   6.31907   3.27951   1.000 32.43073  ? 76  PHE D C   1 
ATOM   3463 O O   . PHE D 4 62  ? 6.75916   7.54456   3.39011   1.000 35.29465  ? 76  PHE D O   1 
ATOM   3464 C CB  . PHE D 4 62  ? 8.84829   5.26508   3.87103   1.000 32.74501  ? 76  PHE D CB  1 
ATOM   3465 C CG  . PHE D 4 62  ? 9.93738   4.31259   3.49334   1.000 35.04752  ? 76  PHE D CG  1 
ATOM   3466 C CD1 . PHE D 4 62  ? 11.02667  4.74699   2.76110   1.000 38.55800  ? 76  PHE D CD1 1 
ATOM   3467 C CD2 . PHE D 4 62  ? 9.86397   2.97842   3.85333   1.000 35.36363  ? 76  PHE D CD2 1 
ATOM   3468 C CE1 . PHE D 4 62  ? 12.02798  3.86847   2.39700   1.000 44.65130  ? 76  PHE D CE1 1 
ATOM   3469 C CE2 . PHE D 4 62  ? 10.86227  2.09666   3.49734   1.000 37.16741  ? 76  PHE D CE2 1 
ATOM   3470 C CZ  . PHE D 4 62  ? 11.94770  2.54268   2.76659   1.000 41.84509  ? 76  PHE D CZ  1 
ATOM   3471 N N   . THR D 4 63  ? 5.55694   5.64342   3.59198   1.000 33.15769  ? 77  THR D N   1 
ATOM   3472 C CA  . THR D 4 63  ? 4.39057   6.27400   4.19192   1.000 32.86013  ? 77  THR D CA  1 
ATOM   3473 C C   . THR D 4 63  ? 3.89975   5.41743   5.34703   1.000 37.14298  ? 77  THR D C   1 
ATOM   3474 O O   . THR D 4 63  ? 3.63226   4.22413   5.17004   1.000 39.74304  ? 77  THR D O   1 
ATOM   3475 C CB  . THR D 4 63  ? 3.26365   6.46448   3.17443   1.000 37.01305  ? 77  THR D CB  1 
ATOM   3476 O OG1 . THR D 4 63  ? 3.67855   7.40108   2.17683   1.000 44.16435  ? 77  THR D OG1 1 
ATOM   3477 C CG2 . THR D 4 63  ? 2.01639   6.99161   3.86698   1.000 29.38378  ? 77  THR D CG2 1 
ATOM   3478 N N   . ALA D 4 64  ? 3.78155   6.02534   6.52272   1.000 35.84300  ? 78  ALA D N   1 
ATOM   3479 C CA  . ALA D 4 64  ? 3.23951   5.36210   7.69765   1.000 30.65386  ? 78  ALA D CA  1 
ATOM   3480 C C   . ALA D 4 64  ? 2.01902   6.12876   8.18119   1.000 34.23119  ? 78  ALA D C   1 
ATOM   3481 O O   . ALA D 4 64  ? 2.01291   7.36370   8.18388   1.000 36.50409  ? 78  ALA D O   1 
ATOM   3482 C CB  . ALA D 4 64  ? 4.28453   5.26048   8.80854   1.000 26.44863  ? 78  ALA D CB  1 
ATOM   3483 N N   . GLN D 4 65  ? 0.97820   5.39605   8.56945   1.000 33.22014  ? 79  GLN D N   1 
ATOM   3484 C CA  . GLN D 4 65  ? -0.26297  6.01756   8.99863   1.000 32.26872  ? 79  GLN D CA  1 
ATOM   3485 C C   . GLN D 4 65  ? -0.86554  5.22955   10.15231  1.000 32.58162  ? 79  GLN D C   1 
ATOM   3486 O O   . GLN D 4 65  ? -0.64285  4.02500   10.29504  1.000 29.75885  ? 79  GLN D O   1 
ATOM   3487 C CB  . GLN D 4 65  ? -1.27114  6.13082   7.84780   1.000 31.57287  ? 79  GLN D CB  1 
ATOM   3488 C CG  . GLN D 4 65  ? -2.32475  7.21623   8.06888   1.000 46.05598  ? 79  GLN D CG  1 
ATOM   3489 C CD  . GLN D 4 65  ? -2.96374  7.69973   6.77636   1.000 52.72342  ? 79  GLN D CD  1 
ATOM   3490 O OE1 . GLN D 4 65  ? -2.54010  7.33091   5.67847   1.000 59.54444  ? 79  GLN D OE1 1 
ATOM   3491 N NE2 . GLN D 4 65  ? -3.98803  8.53413   6.90437   1.000 45.88661  ? 79  GLN D NE2 1 
ATOM   3492 N N   . LEU D 4 66  ? -1.61965  5.94112   10.98156  1.000 33.10334  ? 80  LEU D N   1 
ATOM   3493 C CA  . LEU D 4 66  ? -2.26068  5.40500   12.16823  1.000 33.91722  ? 80  LEU D CA  1 
ATOM   3494 C C   . LEU D 4 66  ? -3.75677  5.65120   12.07395  1.000 36.44651  ? 80  LEU D C   1 
ATOM   3495 O O   . LEU D 4 66  ? -4.18800  6.74231   11.69191  1.000 36.74720  ? 80  LEU D O   1 
ATOM   3496 C CB  . LEU D 4 66  ? -1.70688  6.06982   13.43141  1.000 31.21167  ? 80  LEU D CB  1 
ATOM   3497 C CG  . LEU D 4 66  ? -2.50977  5.91948   14.72455  1.000 38.58598  ? 80  LEU D CG  1 
ATOM   3498 C CD1 . LEU D 4 66  ? -2.37935  4.51033   15.28588  1.000 33.55825  ? 80  LEU D CD1 1 
ATOM   3499 C CD2 . LEU D 4 66  ? -2.06741  6.95511   15.74726  1.000 41.68619  ? 80  LEU D CD2 1 
ATOM   3500 N N   . ASN D 4 67  ? -4.54609  4.63757   12.42129  1.000 33.79411  ? 81  ASN D N   1 
ATOM   3501 C CA  . ASN D 4 67  ? -5.99878  4.77132   12.50989  1.000 41.05725  ? 81  ASN D CA  1 
ATOM   3502 C C   . ASN D 4 67  ? -6.42497  4.30009   13.89867  1.000 35.91461  ? 81  ASN D C   1 
ATOM   3503 O O   . ASN D 4 67  ? -6.52391  3.09581   14.15204  1.000 31.46470  ? 81  ASN D O   1 
ATOM   3504 C CB  . ASN D 4 67  ? -6.69890  3.98032   11.41129  1.000 20.53551  ? 81  ASN D CB  1 
ATOM   3505 C CG  . ASN D 4 67  ? -8.16855  4.33269   11.29105  1.000 40.56943  ? 81  ASN D CG  1 
ATOM   3506 O OD1 . ASN D 4 67  ? -8.79659  4.78101   12.25332  1.000 41.93286  ? 81  ASN D OD1 1 
ATOM   3507 N ND2 . ASN D 4 67  ? -8.72597  4.13499   10.10475  1.000 42.58223  ? 81  ASN D ND2 1 
ATOM   3508 N N   . ARG D 4 68  ? -6.69415  5.25031   14.79426  1.000 35.43835  ? 82  ARG D N   1 
ATOM   3509 C CA  . ARG D 4 68  ? -7.04134  4.89199   16.16426  1.000 35.32203  ? 82  ARG D CA  1 
ATOM   3510 C C   . ARG D 4 68  ? -8.41441  4.24622   16.27553  1.000 45.93587  ? 82  ARG D C   1 
ATOM   3511 O O   . ARG D 4 68  ? -8.67596  3.55267   17.26414  1.000 45.02773  ? 82  ARG D O   1 
ATOM   3512 C CB  . ARG D 4 68  ? -6.98351  6.12490   17.05832  1.000 28.85708  ? 82  ARG D CB  1 
ATOM   3513 C CG  . ARG D 4 68  ? -5.58698  6.66646   17.26332  1.000 38.60668  ? 82  ARG D CG  1 
ATOM   3514 C CD  . ARG D 4 68  ? -5.57245  7.67615   18.39527  1.000 44.70351  ? 82  ARG D CD  1 
ATOM   3515 N NE  . ARG D 4 68  ? -4.21861  8.03596   18.79166  1.000 35.00236  ? 82  ARG D NE  1 
ATOM   3516 C CZ  . ARG D 4 68  ? -3.48101  7.33853   19.64399  1.000 38.33366  ? 82  ARG D CZ  1 
ATOM   3517 N NH1 . ARG D 4 68  ? -3.93261  6.21981   20.19373  1.000 34.22565  ? 82  ARG D NH1 1 
ATOM   3518 N NH2 . ARG D 4 68  ? -2.26209  7.77581   19.95505  1.000 29.70556  ? 82  ARG D NH2 1 
ATOM   3519 N N   . ALA D 4 69  ? -9.29398  4.46066   15.29345  1.000 45.57321  ? 83  ALA D N   1 
ATOM   3520 C CA  . ALA D 4 69  ? -10.63940 3.89784   15.36152  1.000 45.19318  ? 83  ALA D CA  1 
ATOM   3521 C C   . ALA D 4 69  ? -10.61489 2.39040   15.15284  1.000 37.96730  ? 83  ALA D C   1 
ATOM   3522 O O   . ALA D 4 69  ? -11.26819 1.64006   15.88587  1.000 50.87926  ? 83  ALA D O   1 
ATOM   3523 C CB  . ALA D 4 69  ? -11.54037 4.56724   14.32528  1.000 49.44016  ? 83  ALA D CB  1 
ATOM   3524 N N   . SER D 4 70  ? -9.88101  1.93208   14.14403  1.000 32.89993  ? 84  SER D N   1 
ATOM   3525 C CA  . SER D 4 70  ? -9.68519  0.51122   13.90858  1.000 35.90074  ? 84  SER D CA  1 
ATOM   3526 C C   . SER D 4 70  ? -8.45819  -0.03240  14.62202  1.000 29.86491  ? 84  SER D C   1 
ATOM   3527 O O   . SER D 4 70  ? -8.24760  -1.24911  14.61278  1.000 29.35827  ? 84  SER D O   1 
ATOM   3528 C CB  . SER D 4 70  ? -9.56543  0.23537   12.40194  1.000 27.01532  ? 84  SER D CB  1 
ATOM   3529 O OG  . SER D 4 70  ? -8.48464  0.95833   11.83447  1.000 43.65859  ? 84  SER D OG  1 
ATOM   3530 N N   . GLN D 4 71  ? -7.65869  0.83915   15.23658  1.000 31.24296  ? 85  GLN D N   1 
ATOM   3531 C CA  . GLN D 4 71  ? -6.41652  0.45966   15.90855  1.000 37.93075  ? 85  GLN D CA  1 
ATOM   3532 C C   . GLN D 4 71  ? -5.48479  -0.27863  14.93989  1.000 29.37477  ? 85  GLN D C   1 
ATOM   3533 O O   . GLN D 4 71  ? -4.95192  -1.35638  15.22245  1.000 31.66998  ? 85  GLN D O   1 
ATOM   3534 C CB  . GLN D 4 71  ? -6.71069  -0.33765  17.19011  1.000 24.06005  ? 85  GLN D CB  1 
ATOM   3535 C CG  . GLN D 4 71  ? -7.46161  0.52960   18.22641  1.000 34.29450  ? 85  GLN D CG  1 
ATOM   3536 C CD  . GLN D 4 71  ? -7.74353  -0.14254  19.56881  1.000 36.33637  ? 85  GLN D CD  1 
ATOM   3537 O OE1 . GLN D 4 71  ? -8.58923  0.32477   20.33167  1.000 41.20739  ? 85  GLN D OE1 1 
ATOM   3538 N NE2 . GLN D 4 71  ? -7.02774  -1.21888  19.87015  1.000 36.03501  ? 85  GLN D NE2 1 
ATOM   3539 N N   . TYR D 4 72  ? -5.28479  0.34465   13.77960  1.000 29.25111  ? 86  TYR D N   1 
ATOM   3540 C CA  . TYR D 4 72  ? -4.42465  -0.14881  12.71416  1.000 29.23586  ? 86  TYR D CA  1 
ATOM   3541 C C   . TYR D 4 72  ? -3.24401  0.79194   12.52093  1.000 27.05780  ? 86  TYR D C   1 
ATOM   3542 O O   . TYR D 4 72  ? -3.38733  2.01861   12.61166  1.000 25.59825  ? 86  TYR D O   1 
ATOM   3543 C CB  . TYR D 4 72  ? -5.18901  -0.26782  11.38786  1.000 30.61945  ? 86  TYR D CB  1 
ATOM   3544 C CG  . TYR D 4 72  ? -5.61304  -1.67457  11.03823  1.000 36.27301  ? 86  TYR D CG  1 
ATOM   3545 C CD1 . TYR D 4 72  ? -4.77335  -2.51341  10.31982  1.000 34.99057  ? 86  TYR D CD1 1 
ATOM   3546 C CD2 . TYR D 4 72  ? -6.85223  -2.16201  11.42532  1.000 36.83241  ? 86  TYR D CD2 1 
ATOM   3547 C CE1 . TYR D 4 72  ? -5.15513  -3.79802  9.99918   1.000 36.96165  ? 86  TYR D CE1 1 
ATOM   3548 C CE2 . TYR D 4 72  ? -7.24311  -3.44276  11.10932  1.000 35.70055  ? 86  TYR D CE2 1 
ATOM   3549 C CZ  . TYR D 4 72  ? -6.39189  -4.25688  10.39883  1.000 38.49585  ? 86  TYR D CZ  1 
ATOM   3550 O OH  . TYR D 4 72  ? -6.78300  -5.53616  10.09073  1.000 51.80458  ? 86  TYR D OH  1 
ATOM   3551 N N   . ILE D 4 73  ? -2.08154  0.20706   12.25213  1.000 28.07514  ? 87  ILE D N   1 
ATOM   3552 C CA  . ILE D 4 73  ? -0.88895  0.93144   11.83329  1.000 29.91830  ? 87  ILE D CA  1 
ATOM   3553 C C   . ILE D 4 73  ? -0.47828  0.37985   10.47819  1.000 30.19016  ? 87  ILE D C   1 
ATOM   3554 O O   . ILE D 4 73  ? -0.54831  -0.83345  10.25103  1.000 31.75494  ? 87  ILE D O   1 
ATOM   3555 C CB  . ILE D 4 73  ? 0.26110   0.77995   12.85273  1.000 34.65104  ? 87  ILE D CB  1 
ATOM   3556 C CG1 . ILE D 4 73  ? -0.21820  1.13200   14.25693  1.000 39.24692  ? 87  ILE D CG1 1 
ATOM   3557 C CG2 . ILE D 4 73  ? 1.43615   1.65937   12.47940  1.000 31.36065  ? 87  ILE D CG2 1 
ATOM   3558 C CD1 . ILE D 4 73  ? 0.67149   0.56774   15.34150  1.000 44.04102  ? 87  ILE D CD1 1 
ATOM   3559 N N   . SER D 4 74  ? -0.05853  1.26137   9.57563   1.000 23.97322  ? 88  SER D N   1 
ATOM   3560 C CA  . SER D 4 74  ? 0.33541   0.83919   8.24116   1.000 23.26311  ? 88  SER D CA  1 
ATOM   3561 C C   . SER D 4 74  ? 1.68104   1.44337   7.87337   1.000 26.82527  ? 88  SER D C   1 
ATOM   3562 O O   . SER D 4 74  ? 2.05597   2.51803   8.35024   1.000 25.87482  ? 88  SER D O   1 
ATOM   3563 C CB  . SER D 4 74  ? -0.71020  1.23046   7.18513   1.000 25.12758  ? 88  SER D CB  1 
ATOM   3564 O OG  . SER D 4 74  ? -0.64725  2.61450   6.89162   1.000 40.58204  ? 88  SER D OG  1 
ATOM   3565 N N   . LEU D 4 75  ? 2.40662   0.72201   7.02617   1.000 25.74190  ? 89  LEU D N   1 
ATOM   3566 C CA  . LEU D 4 75  ? 3.63096   1.20045   6.40472   1.000 27.39277  ? 89  LEU D CA  1 
ATOM   3567 C C   . LEU D 4 75  ? 3.53501   0.92325   4.91471   1.000 28.90928  ? 89  LEU D C   1 
ATOM   3568 O O   . LEU D 4 75  ? 3.23998   -0.20716  4.51319   1.000 32.27302  ? 89  LEU D O   1 
ATOM   3569 C CB  . LEU D 4 75  ? 4.86736   0.51277   6.98816   1.000 29.08385  ? 89  LEU D CB  1 
ATOM   3570 C CG  . LEU D 4 75  ? 6.18932   0.85281   6.30234   1.000 27.93008  ? 89  LEU D CG  1 
ATOM   3571 C CD1 . LEU D 4 75  ? 6.52265   2.32210   6.49960   1.000 27.57034  ? 89  LEU D CD1 1 
ATOM   3572 C CD2 . LEU D 4 75  ? 7.30809   -0.04141  6.81554   1.000 20.75162  ? 89  LEU D CD2 1 
ATOM   3573 N N   . LEU D 4 76  ? 3.77511   1.94873   4.10119   1.000 32.87593  ? 90  LEU D N   1 
ATOM   3574 C CA  . LEU D 4 76  ? 3.74382   1.82905   2.64975   1.000 34.58220  ? 90  LEU D CA  1 
ATOM   3575 C C   . LEU D 4 76  ? 5.12801   2.10662   2.08661   1.000 33.49006  ? 90  LEU D C   1 
ATOM   3576 O O   . LEU D 4 76  ? 5.75731   3.10924   2.44332   1.000 30.34496  ? 90  LEU D O   1 
ATOM   3577 C CB  . LEU D 4 76  ? 2.72741   2.79109   2.03676   1.000 38.76128  ? 90  LEU D CB  1 
ATOM   3578 C CG  . LEU D 4 76  ? 1.26471   2.46876   2.32976   1.000 32.59638  ? 90  LEU D CG  1 
ATOM   3579 C CD1 . LEU D 4 76  ? 0.37097   3.56458   1.78040   1.000 41.37680  ? 90  LEU D CD1 1 
ATOM   3580 C CD2 . LEU D 4 76  ? 0.89695   1.12390   1.73219   1.000 39.98860  ? 90  LEU D CD2 1 
ATOM   3581 N N   . ILE D 4 77  ? 5.59295   1.21979   1.20920   1.000 32.76984  ? 91  ILE D N   1 
ATOM   3582 C CA  . ILE D 4 77  ? 6.86871   1.36583   0.51574   1.000 37.04326  ? 91  ILE D CA  1 
ATOM   3583 C C   . ILE D 4 77  ? 6.58026   1.39228   -0.98103  1.000 43.15481  ? 91  ILE D C   1 
ATOM   3584 O O   . ILE D 4 77  ? 6.22752   0.36271   -1.57197  1.000 34.25568  ? 91  ILE D O   1 
ATOM   3585 C CB  . ILE D 4 77  ? 7.85224   0.24041   0.86437   1.000 35.71777  ? 91  ILE D CB  1 
ATOM   3586 C CG1 . ILE D 4 77  ? 7.97819   0.08532   2.38001   1.000 36.04807  ? 91  ILE D CG1 1 
ATOM   3587 C CG2 . ILE D 4 77  ? 9.21445   0.52198   0.25741   1.000 29.57720  ? 91  ILE D CG2 1 
ATOM   3588 C CD1 . ILE D 4 77  ? 8.95428   -0.99488  2.79452   1.000 24.89271  ? 91  ILE D CD1 1 
ATOM   3589 N N   . ARG D 4 78  ? 6.72488   2.56534   -1.59181  1.000 36.70355  ? 92  ARG D N   1 
ATOM   3590 C CA  . ARG D 4 78  ? 6.58719   2.70091   -3.03329  1.000 35.85314  ? 92  ARG D CA  1 
ATOM   3591 C C   . ARG D 4 78  ? 7.90054   2.36095   -3.72469  1.000 37.73424  ? 92  ARG D C   1 
ATOM   3592 O O   . ARG D 4 78  ? 8.98867   2.61932   -3.20025  1.000 37.74988  ? 92  ARG D O   1 
ATOM   3593 C CB  . ARG D 4 78  ? 6.16455   4.12411   -3.40651  1.000 23.84442  ? 92  ARG D CB  1 
ATOM   3594 C CG  . ARG D 4 78  ? 4.84162   4.53520   -2.79667  1.000 53.69202  ? 92  ARG D CG  1 
ATOM   3595 C CD  . ARG D 4 78  ? 4.48551   5.99336   -3.08284  1.000 51.92988  ? 92  ARG D CD  1 
ATOM   3596 N NE  . ARG D 4 78  ? 5.33306   6.95160   -2.37829  1.000 56.51488  ? 92  ARG D NE  1 
ATOM   3597 C CZ  . ARG D 4 78  ? 5.25261   7.22082   -1.07959  1.000 65.39465  ? 92  ARG D CZ  1 
ATOM   3598 N NH1 . ARG D 4 78  ? 4.41465   6.57029   -0.28554  1.000 46.53025  ? 92  ARG D NH1 1 
ATOM   3599 N NH2 . ARG D 4 78  ? 6.03956   8.16068   -0.56130  1.000 61.71810  ? 92  ARG D NH2 1 
ATOM   3600 N N   . ASP D 4 79  ? 7.78716   1.77153   -4.91266  1.000 35.54810  ? 93  ASP D N   1 
ATOM   3601 C CA  . ASP D 4 79  ? 8.93243   1.52565   -5.78390  1.000 31.87961  ? 93  ASP D CA  1 
ATOM   3602 C C   . ASP D 4 79  ? 10.02447  0.76299   -5.03520  1.000 38.03333  ? 93  ASP D C   1 
ATOM   3603 O O   . ASP D 4 79  ? 11.15806  1.22214   -4.88278  1.000 38.49377  ? 93  ASP D O   1 
ATOM   3604 C CB  . ASP D 4 79  ? 9.46141   2.84476   -6.35151  1.000 35.86762  ? 93  ASP D CB  1 
ATOM   3605 C CG  . ASP D 4 79  ? 10.13437  2.66924   -7.69196  1.000 62.19568  ? 93  ASP D CG  1 
ATOM   3606 O OD1 . ASP D 4 79  ? 9.50378   2.07570   -8.60086  1.000 64.01961  ? 93  ASP D OD1 1 
ATOM   3607 O OD2 . ASP D 4 79  ? 11.28830  3.13090   -7.84041  1.000 57.74669  ? 93  ASP D OD2 1 
ATOM   3608 N N   . SER D 4 80  ? 9.64460   -0.41818  -4.55109  1.000 38.92020  ? 94  SER D N   1 
ATOM   3609 C CA  . SER D 4 80  ? 10.51612  -1.20425  -3.68763  1.000 31.32208  ? 94  SER D CA  1 
ATOM   3610 C C   . SER D 4 80  ? 11.82031  -1.55960  -4.39340  1.000 39.53948  ? 94  SER D C   1 
ATOM   3611 O O   . SER D 4 80  ? 11.82846  -1.94951  -5.56634  1.000 35.92111  ? 94  SER D O   1 
ATOM   3612 C CB  . SER D 4 80  ? 9.79519   -2.47378  -3.23705  1.000 31.95551  ? 94  SER D CB  1 
ATOM   3613 O OG  . SER D 4 80  ? 9.35735   -3.22504  -4.35373  1.000 38.33953  ? 94  SER D OG  1 
ATOM   3614 N N   . LYS D 4 81  ? 12.92312  -1.42065  -3.66753  1.000 32.03075  ? 95  LYS D N   1 
ATOM   3615 C CA  . LYS D 4 81  ? 14.25651  -1.70960  -4.16545  1.000 33.67368  ? 95  LYS D CA  1 
ATOM   3616 C C   . LYS D 4 81  ? 14.83524  -2.91477  -3.43422  1.000 38.99971  ? 95  LYS D C   1 
ATOM   3617 O O   . LYS D 4 81  ? 14.38723  -3.28033  -2.34242  1.000 35.13161  ? 95  LYS D O   1 
ATOM   3618 C CB  . LYS D 4 81  ? 15.16459  -0.48877  -3.99216  1.000 33.32559  ? 95  LYS D CB  1 
ATOM   3619 C CG  . LYS D 4 81  ? 14.46305  0.81526   -4.32884  1.000 47.18924  ? 95  LYS D CG  1 
ATOM   3620 C CD  . LYS D 4 81  ? 15.44202  1.92510   -4.66504  1.000 59.87527  ? 95  LYS D CD  1 
ATOM   3621 C CE  . LYS D 4 81  ? 14.72184  3.10276   -5.31771  1.000 67.74803  ? 95  LYS D CE  1 
ATOM   3622 N NZ  . LYS D 4 81  ? 13.89201  2.69025   -6.48918  1.000 49.51459  ? 95  LYS D NZ  1 
ATOM   3623 N N   . LEU D 4 82  ? 15.84019  -3.53795  -4.05810  1.000 37.83198  ? 96  LEU D N   1 
ATOM   3624 C CA  . LEU D 4 82  ? 16.48106  -4.70370  -3.45495  1.000 32.34285  ? 96  LEU D CA  1 
ATOM   3625 C C   . LEU D 4 82  ? 16.95781  -4.40390  -2.04372  1.000 30.59559  ? 96  LEU D C   1 
ATOM   3626 O O   . LEU D 4 82  ? 16.84527  -5.24854  -1.14841  1.000 35.05598  ? 96  LEU D O   1 
ATOM   3627 C CB  . LEU D 4 82  ? 17.65973  -5.16537  -4.30887  1.000 33.46490  ? 96  LEU D CB  1 
ATOM   3628 C CG  . LEU D 4 82  ? 17.36038  -5.66105  -5.71386  1.000 52.25679  ? 96  LEU D CG  1 
ATOM   3629 C CD1 . LEU D 4 82  ? 18.62347  -6.23562  -6.31044  1.000 50.51959  ? 96  LEU D CD1 1 
ATOM   3630 C CD2 . LEU D 4 82  ? 16.25189  -6.69141  -5.68281  1.000 43.77075  ? 96  LEU D CD2 1 
ATOM   3631 N N   . SER D 4 83  ? 17.48527  -3.19869  -1.82617  1.000 29.55194  ? 97  SER D N   1 
ATOM   3632 C CA  . SER D 4 83  ? 17.96721  -2.78590  -0.51484  1.000 26.48329  ? 97  SER D CA  1 
ATOM   3633 C C   . SER D 4 83  ? 16.85225  -2.63237  0.51502   1.000 34.22408  ? 97  SER D C   1 
ATOM   3634 O O   . SER D 4 83  ? 17.15296  -2.51543  1.70796   1.000 38.63056  ? 97  SER D O   1 
ATOM   3635 C CB  . SER D 4 83  ? 18.73299  -1.47069  -0.64439  1.000 32.31222  ? 97  SER D CB  1 
ATOM   3636 O OG  . SER D 4 83  ? 17.88940  -0.44797  -1.14712  1.000 41.23620  ? 97  SER D OG  1 
ATOM   3637 N N   . ASP D 4 84  ? 15.58349  -2.61646  0.09751   1.000 24.56028  ? 98  ASP D N   1 
ATOM   3638 C CA  . ASP D 4 84  ? 14.49672  -2.59590  1.06970   1.000 31.14546  ? 98  ASP D CA  1 
ATOM   3639 C C   . ASP D 4 84  ? 14.31553  -3.93341  1.77596   1.000 29.27051  ? 98  ASP D C   1 
ATOM   3640 O O   . ASP D 4 84  ? 13.63376  -3.97799  2.80486   1.000 34.93970  ? 98  ASP D O   1 
ATOM   3641 C CB  . ASP D 4 84  ? 13.17641  -2.19939  0.40397   1.000 28.42902  ? 98  ASP D CB  1 
ATOM   3642 C CG  . ASP D 4 84  ? 13.14175  -0.74196  -0.02637  1.000 32.51265  ? 98  ASP D CG  1 
ATOM   3643 O OD1 . ASP D 4 84  ? 13.71809  0.11289   0.68038   1.000 38.70514  ? 98  ASP D OD1 1 
ATOM   3644 O OD2 . ASP D 4 84  ? 12.52388  -0.45509  -1.07655  1.000 37.54578  ? 98  ASP D OD2 1 
ATOM   3645 N N   . SER D 4 85  ? 14.89815  -5.01265  1.25133   1.000 27.63772  ? 99  SER D N   1 
ATOM   3646 C CA  . SER D 4 85  ? 14.77253  -6.33159  1.85804   1.000 36.42871  ? 99  SER D CA  1 
ATOM   3647 C C   . SER D 4 85  ? 15.24110  -6.30592  3.30505   1.000 31.80244  ? 99  SER D C   1 
ATOM   3648 O O   . SER D 4 85  ? 16.42462  -6.07727  3.57322   1.000 37.06982  ? 99  SER D O   1 
ATOM   3649 C CB  . SER D 4 85  ? 15.57484  -7.36695  1.06783   1.000 32.20417  ? 99  SER D CB  1 
ATOM   3650 O OG  . SER D 4 85  ? 15.18696  -7.38810  -0.28788  1.000 33.76714  ? 99  SER D OG  1 
ATOM   3651 N N   . ALA D 4 86  ? 14.32318  -6.53092  4.23724   1.000 32.10184  ? 100 ALA D N   1 
ATOM   3652 C CA  . ALA D 4 86  ? 14.62147  -6.51909  5.66640   1.000 29.40375  ? 100 ALA D CA  1 
ATOM   3653 C C   . ALA D 4 86  ? 13.37340  -6.99304  6.39202   1.000 29.83627  ? 100 ALA D C   1 
ATOM   3654 O O   . ALA D 4 86  ? 12.36131  -7.32672  5.76800   1.000 32.10441  ? 100 ALA D O   1 
ATOM   3655 C CB  . ALA D 4 86  ? 15.04483  -5.13227  6.15719   1.000 23.00979  ? 100 ALA D CB  1 
ATOM   3656 N N   . THR D 4 87  ? 13.45360  -7.02092  7.71847   1.000 24.26895  ? 101 THR D N   1 
ATOM   3657 C CA  . THR D 4 87  ? 12.29873  -7.27275  8.56847   1.000 28.58394  ? 101 THR D CA  1 
ATOM   3658 C C   . THR D 4 87  ? 11.82132  -5.94317  9.13418   1.000 29.30303  ? 101 THR D C   1 
ATOM   3659 O O   . THR D 4 87  ? 12.62776  -5.15438  9.64170   1.000 30.59379  ? 101 THR D O   1 
ATOM   3660 C CB  . THR D 4 87  ? 12.63709  -8.24246  9.70218   1.000 24.31118  ? 101 THR D CB  1 
ATOM   3661 O OG1 . THR D 4 87  ? 12.99377  -9.51627  9.15386   1.000 37.11776  ? 101 THR D OG1 1 
ATOM   3662 C CG2 . THR D 4 87  ? 11.44691  -8.41879  10.62446  1.000 22.45152  ? 101 THR D CG2 1 
ATOM   3663 N N   . TYR D 4 88  ? 10.51889  -5.69390  9.03697   1.000 28.58558  ? 102 TYR D N   1 
ATOM   3664 C CA  . TYR D 4 88  ? 9.92659   -4.42405  9.43799   1.000 26.42484  ? 102 TYR D CA  1 
ATOM   3665 C C   . TYR D 4 88  ? 9.10366   -4.63239  10.70079  1.000 30.59173  ? 102 TYR D C   1 
ATOM   3666 O O   . TYR D 4 88  ? 8.14992   -5.42019  10.70630  1.000 30.80061  ? 102 TYR D O   1 
ATOM   3667 C CB  . TYR D 4 88  ? 9.08755   -3.84404  8.29962   1.000 29.40767  ? 102 TYR D CB  1 
ATOM   3668 C CG  . TYR D 4 88  ? 9.95872   -3.38146  7.14959   1.000 32.46029  ? 102 TYR D CG  1 
ATOM   3669 C CD1 . TYR D 4 88  ? 10.43960  -4.28425  6.20569   1.000 24.97394  ? 102 TYR D CD1 1 
ATOM   3670 C CD2 . TYR D 4 88  ? 10.33888  -2.04858  7.03668   1.000 29.58256  ? 102 TYR D CD2 1 
ATOM   3671 C CE1 . TYR D 4 88  ? 11.25350  -3.86377  5.16581   1.000 32.79071  ? 102 TYR D CE1 1 
ATOM   3672 C CE2 . TYR D 4 88  ? 11.14849  -1.62013  6.00697   1.000 25.16129  ? 102 TYR D CE2 1 
ATOM   3673 C CZ  . TYR D 4 88  ? 11.60351  -2.52824  5.07087   1.000 25.07598  ? 102 TYR D CZ  1 
ATOM   3674 O OH  . TYR D 4 88  ? 12.41635  -2.09823  4.04450   1.000 37.16001  ? 102 TYR D OH  1 
ATOM   3675 N N   . LEU D 4 89  ? 9.48125   -3.92882  11.76453  1.000 30.27702  ? 103 LEU D N   1 
ATOM   3676 C CA  . LEU D 4 89  ? 8.92540   -4.14033  13.09420  1.000 28.82068  ? 103 LEU D CA  1 
ATOM   3677 C C   . LEU D 4 89  ? 7.93390   -3.03923  13.43923  1.000 27.95533  ? 103 LEU D C   1 
ATOM   3678 O O   . LEU D 4 89  ? 8.25917   -1.84798  13.35510  1.000 27.64389  ? 103 LEU D O   1 
ATOM   3679 C CB  . LEU D 4 89  ? 10.03355  -4.17617  14.14685  1.000 31.72055  ? 103 LEU D CB  1 
ATOM   3680 C CG  . LEU D 4 89  ? 11.20609  -5.11860  13.89463  1.000 34.88634  ? 103 LEU D CG  1 
ATOM   3681 C CD1 . LEU D 4 89  ? 12.31994  -4.81520  14.88093  1.000 32.38577  ? 103 LEU D CD1 1 
ATOM   3682 C CD2 . LEU D 4 89  ? 10.75609  -6.55908  14.01931  1.000 28.15778  ? 103 LEU D CD2 1 
ATOM   3683 N N   . CYS D 4 90  ? 6.73352   -3.44465  13.83370  1.000 25.26740  ? 104 CYS D N   1 
ATOM   3684 C CA  . CYS D 4 90  ? 5.73399   -2.53379  14.36932  1.000 31.49748  ? 104 CYS D CA  1 
ATOM   3685 C C   . CYS D 4 90  ? 5.97856   -2.38012  15.86632  1.000 28.45891  ? 104 CYS D C   1 
ATOM   3686 O O   . CYS D 4 90  ? 6.04804   -3.37762  16.59118  1.000 38.34569  ? 104 CYS D O   1 
ATOM   3687 C CB  . CYS D 4 90  ? 4.33809   -3.07874  14.08920  1.000 22.32307  ? 104 CYS D CB  1 
ATOM   3688 S SG  . CYS D 4 90  ? 2.98324   -2.09996  14.71802  1.000 35.45625  ? 104 CYS D SG  1 
ATOM   3689 N N   . VAL D 4 91  ? 6.13159   -1.14231  16.32842  1.000 23.31680  ? 105 VAL D N   1 
ATOM   3690 C CA  . VAL D 4 91  ? 6.52451   -0.87718  17.70682  1.000 26.91621  ? 105 VAL D CA  1 
ATOM   3691 C C   . VAL D 4 91  ? 5.51255   0.07401   18.32697  1.000 29.97101  ? 105 VAL D C   1 
ATOM   3692 O O   . VAL D 4 91  ? 5.31480   1.18736   17.82753  1.000 32.03354  ? 105 VAL D O   1 
ATOM   3693 C CB  . VAL D 4 91  ? 7.94639   -0.30477  17.79840  1.000 23.37991  ? 105 VAL D CB  1 
ATOM   3694 C CG1 . VAL D 4 91  ? 8.41096   -0.27575  19.24664  1.000 26.23511  ? 105 VAL D CG1 1 
ATOM   3695 C CG2 . VAL D 4 91  ? 8.89222   -1.14672  16.95745  1.000 30.05342  ? 105 VAL D CG2 1 
ATOM   3696 N N   . VAL D 4 92  ? 4.88384   -0.36102  19.41695  1.000 23.83805  ? 106 VAL D N   1 
ATOM   3697 C CA  . VAL D 4 92  ? 3.77030   0.34538   20.03913  1.000 37.92378  ? 106 VAL D CA  1 
ATOM   3698 C C   . VAL D 4 92  ? 4.15866   0.70521   21.46783  1.000 32.77938  ? 106 VAL D C   1 
ATOM   3699 O O   . VAL D 4 92  ? 4.64821   -0.14693  22.22006  1.000 26.96690  ? 106 VAL D O   1 
ATOM   3700 C CB  . VAL D 4 92  ? 2.48227   -0.49999  20.00932  1.000 30.50028  ? 106 VAL D CB  1 
ATOM   3701 C CG1 . VAL D 4 92  ? 1.36648   0.21078   20.73616  1.000 31.92776  ? 106 VAL D CG1 1 
ATOM   3702 C CG2 . VAL D 4 92  ? 2.07543   -0.78297  18.56845  1.000 28.37221  ? 106 VAL D CG2 1 
ATOM   3703 N N   . MET D 4 93  ? 3.94122   1.96484   21.83739  1.000 29.92335  ? 107 MET D N   1 
ATOM   3704 C CA  . MET D 4 93  ? 4.32628   2.49085   23.14247  1.000 33.21922  ? 107 MET D CA  1 
ATOM   3705 C C   . MET D 4 93  ? 3.07450   2.83873   23.93748  1.000 33.38730  ? 107 MET D C   1 
ATOM   3706 O O   . MET D 4 93  ? 2.25728   3.65002   23.48908  1.000 34.02865  ? 107 MET D O   1 
ATOM   3707 C CB  . MET D 4 93  ? 5.21530   3.72491   22.98941  1.000 26.97258  ? 107 MET D CB  1 
ATOM   3708 C CG  . MET D 4 93  ? 5.73452   4.28625   24.29543  1.000 26.79798  ? 107 MET D CG  1 
ATOM   3709 S SD  . MET D 4 93  ? 6.36919   5.96735   24.13623  1.000 37.44090  ? 107 MET D SD  1 
ATOM   3710 C CE  . MET D 4 93  ? 4.85812   6.90515   24.34666  1.000 32.00459  ? 107 MET D CE  1 
ATOM   3711 N N   . GLY D 4 94  ? 2.92876   2.22293   25.10961  1.000 39.39049  ? 108 GLY D N   1 
ATOM   3712 C CA  . GLY D 4 94  ? 1.89635   2.57996   26.06496  1.000 29.19101  ? 108 GLY D CA  1 
ATOM   3713 C C   . GLY D 4 94  ? 2.53337   3.01904   27.36659  1.000 33.26348  ? 108 GLY D C   1 
ATOM   3714 O O   . GLY D 4 94  ? 3.75484   3.17935   27.42481  1.000 35.96884  ? 108 GLY D O   1 
ATOM   3715 N N   . PHE D 4 95  ? 1.73925   3.21314   28.41898  1.000 34.11883  ? 109 PHE D N   1 
ATOM   3716 C CA  . PHE D 4 95  ? 2.29970   3.66764   29.68773  1.000 31.45249  ? 109 PHE D CA  1 
ATOM   3717 C C   . PHE D 4 95  ? 3.24561   2.62373   30.27319  1.000 30.71069  ? 109 PHE D C   1 
ATOM   3718 O O   . PHE D 4 95  ? 2.82310   1.52027   30.63271  1.000 42.22782  ? 109 PHE D O   1 
ATOM   3719 C CB  . PHE D 4 95  ? 1.18515   4.00306   30.68280  1.000 35.56771  ? 109 PHE D CB  1 
ATOM   3720 C CG  . PHE D 4 95  ? 1.68403   4.55086   31.99062  1.000 41.48964  ? 109 PHE D CG  1 
ATOM   3721 C CD1 . PHE D 4 95  ? 2.30760   5.78769   32.04317  1.000 33.87784  ? 109 PHE D CD1 1 
ATOM   3722 C CD2 . PHE D 4 95  ? 1.52435   3.83484   33.16876  1.000 27.66373  ? 109 PHE D CD2 1 
ATOM   3723 C CE1 . PHE D 4 95  ? 2.77624   6.29656   33.24675  1.000 33.46203  ? 109 PHE D CE1 1 
ATOM   3724 C CE2 . PHE D 4 95  ? 1.98842   4.34053   34.37097  1.000 38.26312  ? 109 PHE D CE2 1 
ATOM   3725 C CZ  . PHE D 4 95  ? 2.61351   5.57178   34.41031  1.000 32.37949  ? 109 PHE D CZ  1 
ATOM   3726 N N   . GLN D 4 96  ? 4.53241   2.96065   30.33597  1.000 32.87247  ? 110 GLN D N   1 
ATOM   3727 C CA  . GLN D 4 96  ? 5.56603   2.09608   30.91520  1.000 57.55902  ? 110 GLN D CA  1 
ATOM   3728 C C   . GLN D 4 96  ? 5.65766   0.74133   30.21145  1.000 44.42222  ? 110 GLN D C   1 
ATOM   3729 O O   . GLN D 4 96  ? 5.92463   -0.28524  30.83895  1.000 45.72505  ? 110 GLN D O   1 
ATOM   3730 C CB  . GLN D 4 96  ? 5.35182   1.90522   32.41771  1.000 48.83530  ? 110 GLN D CB  1 
ATOM   3731 C CG  . GLN D 4 96  ? 5.78962   3.08484   33.26261  1.000 43.84814  ? 110 GLN D CG  1 
ATOM   3732 C CD  . GLN D 4 96  ? 5.44281   2.89525   34.71856  1.000 60.51500  ? 110 GLN D CD  1 
ATOM   3733 O OE1 . GLN D 4 96  ? 4.85338   1.88220   35.09725  1.000 64.97208  ? 110 GLN D OE1 1 
ATOM   3734 N NE2 . GLN D 4 96  ? 5.80104   3.86955   35.54713  1.000 61.85115  ? 110 GLN D NE2 1 
ATOM   3735 N N   . LYS D 4 97  ? 5.45312   0.73134   28.89693  1.000 42.24378  ? 111 LYS D N   1 
ATOM   3736 C CA  . LYS D 4 97  ? 5.62896   -0.50325  28.13590  1.000 36.48320  ? 111 LYS D CA  1 
ATOM   3737 C C   . LYS D 4 97  ? 5.84412   -0.15572  26.67250  1.000 38.07709  ? 111 LYS D C   1 
ATOM   3738 O O   . LYS D 4 97  ? 5.00379   0.51652   26.06853  1.000 33.13419  ? 111 LYS D O   1 
ATOM   3739 C CB  . LYS D 4 97  ? 4.42610   -1.42324  28.30579  1.000 32.03647  ? 111 LYS D CB  1 
ATOM   3740 C CG  . LYS D 4 97  ? 4.71399   -2.87473  27.96982  1.000 36.84168  ? 111 LYS D CG  1 
ATOM   3741 C CD  . LYS D 4 97  ? 3.67148   -3.80535  28.58301  1.000 53.79546  ? 111 LYS D CD  1 
ATOM   3742 C CE  . LYS D 4 97  ? 3.67654   -5.17223  27.91093  1.000 60.90391  ? 111 LYS D CE  1 
ATOM   3743 N NZ  . LYS D 4 97  ? 5.05944   -5.66538  27.65992  1.000 69.04297  ? 111 LYS D NZ  1 
ATOM   3744 N N   . LEU D 4 98  ? 6.96740   -0.60744  26.11238  1.000 36.78381  ? 112 LEU D N   1 
ATOM   3745 C CA  . LEU D 4 98  ? 7.30929   -0.42387  24.70590  1.000 28.92784  ? 112 LEU D CA  1 
ATOM   3746 C C   . LEU D 4 98  ? 7.39772   -1.80258  24.06275  1.000 31.56187  ? 112 LEU D C   1 
ATOM   3747 O O   . LEU D 4 98  ? 8.30968   -2.57632  24.37451  1.000 29.24356  ? 112 LEU D O   1 
ATOM   3748 C CB  . LEU D 4 98  ? 8.62670   0.33359   24.55867  1.000 21.91583  ? 112 LEU D CB  1 
ATOM   3749 C CG  . LEU D 4 98  ? 9.08984   0.60314   23.12390  1.000 29.29145  ? 112 LEU D CG  1 
ATOM   3750 C CD1 . LEU D 4 98  ? 8.13666   1.56086   22.41967  1.000 22.20056  ? 112 LEU D CD1 1 
ATOM   3751 C CD2 . LEU D 4 98  ? 10.50784  1.14480   23.10769  1.000 29.47640  ? 112 LEU D CD2 1 
ATOM   3752 N N   . VAL D 4 99  ? 6.47057   -2.10246  23.15373  1.000 24.94905  ? 113 VAL D N   1 
ATOM   3753 C CA  . VAL D 4 99  ? 6.29639   -3.45007  22.61573  1.000 33.87094  ? 113 VAL D CA  1 
ATOM   3754 C C   . VAL D 4 99  ? 6.79792   -3.49474  21.17759  1.000 32.67856  ? 113 VAL D C   1 
ATOM   3755 O O   . VAL D 4 99  ? 6.26890   -2.80141  20.29858  1.000 30.75073  ? 113 VAL D O   1 
ATOM   3756 C CB  . VAL D 4 99  ? 4.83277   -3.90839  22.69374  1.000 33.85778  ? 113 VAL D CB  1 
ATOM   3757 C CG1 . VAL D 4 99  ? 4.71244   -5.35542  22.22543  1.000 27.03989  ? 113 VAL D CG1 1 
ATOM   3758 C CG2 . VAL D 4 99  ? 4.31131   -3.75636  24.11298  1.000 32.48233  ? 113 VAL D CG2 1 
ATOM   3759 N N   . PHE D 4 100 ? 7.80208   -4.33340  20.93962  1.000 32.93658  ? 114 PHE D N   1 
ATOM   3760 C CA  . PHE D 4 100 ? 8.30768   -4.60234  19.60053  1.000 28.31469  ? 114 PHE D CA  1 
ATOM   3761 C C   . PHE D 4 100 ? 7.53571   -5.76671  18.99252  1.000 34.95308  ? 114 PHE D C   1 
ATOM   3762 O O   . PHE D 4 100 ? 7.49523   -6.85968  19.56946  1.000 28.73502  ? 114 PHE D O   1 
ATOM   3763 C CB  . PHE D 4 100 ? 9.80455   -4.91733  19.64292  1.000 29.55690  ? 114 PHE D CB  1 
ATOM   3764 C CG  . PHE D 4 100 ? 10.67918  -3.69683  19.72742  1.000 31.85289  ? 114 PHE D CG  1 
ATOM   3765 C CD1 . PHE D 4 100 ? 10.89828  -3.06189  20.94194  1.000 23.15742  ? 114 PHE D CD1 1 
ATOM   3766 C CD2 . PHE D 4 100 ? 11.28150  -3.18303  18.58921  1.000 24.43514  ? 114 PHE D CD2 1 
ATOM   3767 C CE1 . PHE D 4 100 ? 11.70126  -1.93963  21.01759  1.000 26.70266  ? 114 PHE D CE1 1 
ATOM   3768 C CE2 . PHE D 4 100 ? 12.08558  -2.05793  18.65857  1.000 30.14454  ? 114 PHE D CE2 1 
ATOM   3769 C CZ  . PHE D 4 100 ? 12.29592  -1.43596  19.87465  1.000 33.82406  ? 114 PHE D CZ  1 
ATOM   3770 N N   . GLY D 4 101 ? 6.92443   -5.53240  17.83384  1.000 36.27262  ? 115 GLY D N   1 
ATOM   3771 C CA  . GLY D 4 101 ? 6.30218   -6.61754  17.10590  1.000 17.93414  ? 115 GLY D CA  1 
ATOM   3772 C C   . GLY D 4 101 ? 7.31841   -7.64518  16.64767  1.000 26.99111  ? 115 GLY D C   1 
ATOM   3773 O O   . GLY D 4 101 ? 8.52470   -7.40060  16.61938  1.000 29.19531  ? 115 GLY D O   1 
ATOM   3774 N N   . THR D 4 102 ? 6.81412   -8.82483  16.27826  1.000 26.75384  ? 116 THR D N   1 
ATOM   3775 C CA  . THR D 4 102 ? 7.70206   -9.88668  15.81771  1.000 34.70606  ? 116 THR D CA  1 
ATOM   3776 C C   . THR D 4 102 ? 8.24038   -9.62717  14.41555  1.000 32.85691  ? 116 THR D C   1 
ATOM   3777 O O   . THR D 4 102 ? 9.26793   -10.20760 14.04614  1.000 38.96477  ? 116 THR D O   1 
ATOM   3778 C CB  . THR D 4 102 ? 6.98868   -11.24020 15.86585  1.000 46.34667  ? 116 THR D CB  1 
ATOM   3779 O OG1 . THR D 4 102 ? 5.64814   -11.09934 15.38260  1.000 56.30347  ? 116 THR D OG1 1 
ATOM   3780 C CG2 . THR D 4 102 ? 6.95560   -11.77030 17.28617  1.000 37.79539  ? 116 THR D CG2 1 
ATOM   3781 N N   . GLY D 4 103 ? 7.58120   -8.78207  13.63586  1.000 28.13459  ? 117 GLY D N   1 
ATOM   3782 C CA  . GLY D 4 103 ? 8.12962   -8.31985  12.37490  1.000 34.66913  ? 117 GLY D CA  1 
ATOM   3783 C C   . GLY D 4 103 ? 7.54658   -9.04113  11.17357  1.000 36.02032  ? 117 GLY D C   1 
ATOM   3784 O O   . GLY D 4 103 ? 7.14462   -10.20755 11.24248  1.000 40.77998  ? 117 GLY D O   1 
ATOM   3785 N N   . THR D 4 104 ? 7.49295   -8.33247  10.04970  1.000 36.62622  ? 118 THR D N   1 
ATOM   3786 C CA  . THR D 4 104 ? 7.14889   -8.91268  8.75768   1.000 35.45513  ? 118 THR D CA  1 
ATOM   3787 C C   . THR D 4 104 ? 8.38285   -8.85463  7.86758   1.000 28.84152  ? 118 THR D C   1 
ATOM   3788 O O   . THR D 4 104 ? 8.92376   -7.77047  7.62311   1.000 31.04390  ? 118 THR D O   1 
ATOM   3789 C CB  . THR D 4 104 ? 5.98338   -8.16727  8.11055   1.000 28.62975  ? 118 THR D CB  1 
ATOM   3790 O OG1 . THR D 4 104 ? 4.87908   -8.12962  9.02285   1.000 30.98507  ? 118 THR D OG1 1 
ATOM   3791 C CG2 . THR D 4 104 ? 5.55745   -8.87037  6.83423   1.000 36.89942  ? 118 THR D CG2 1 
ATOM   3792 N N   . ARG D 4 105 ? 8.83281   -10.01088 7.39285   1.000 26.86867  ? 119 ARG D N   1 
ATOM   3793 C CA  . ARG D 4 105 ? 10.03505  -10.04882 6.57240   1.000 34.84020  ? 119 ARG D CA  1 
ATOM   3794 C C   . ARG D 4 105 ? 9.70601   -9.73008  5.11980   1.000 34.94202  ? 119 ARG D C   1 
ATOM   3795 O O   . ARG D 4 105 ? 8.71954   -10.22069 4.56617   1.000 36.78898  ? 119 ARG D O   1 
ATOM   3796 C CB  . ARG D 4 105 ? 10.72175  -11.40878 6.66952   1.000 33.61957  ? 119 ARG D CB  1 
ATOM   3797 C CG  . ARG D 4 105 ? 12.18979  -11.37350 6.25522   1.000 37.29321  ? 119 ARG D CG  1 
ATOM   3798 C CD  . ARG D 4 105 ? 12.88690  -12.66637 6.62887   1.000 56.61173  ? 119 ARG D CD  1 
ATOM   3799 N NE  . ARG D 4 105 ? 12.29682  -13.80445 5.93556   1.000 70.12987  ? 119 ARG D NE  1 
ATOM   3800 C CZ  . ARG D 4 105 ? 12.85887  -14.42535 4.90796   1.000 83.41033  ? 119 ARG D CZ  1 
ATOM   3801 N NH1 . ARG D 4 105 ? 14.05158  -14.07208 4.45629   1.000 85.88421  ? 119 ARG D NH1 1 
ATOM   3802 N NH2 . ARG D 4 105 ? 12.20943  -15.42680 4.32042   1.000 73.89283  ? 119 ARG D NH2 1 
ATOM   3803 N N   . LEU D 4 106 ? 10.54045  -8.89186  4.51122   1.000 35.20412  ? 120 LEU D N   1 
ATOM   3804 C CA  . LEU D 4 106 ? 10.36684  -8.43741  3.14008   1.000 28.91468  ? 120 LEU D CA  1 
ATOM   3805 C C   . LEU D 4 106 ? 11.56358  -8.88156  2.31432   1.000 35.13660  ? 120 LEU D C   1 
ATOM   3806 O O   . LEU D 4 106 ? 12.71165  -8.61605  2.68516   1.000 31.65697  ? 120 LEU D O   1 
ATOM   3807 C CB  . LEU D 4 106 ? 10.22425  -6.91323  3.07105   1.000 30.18881  ? 120 LEU D CB  1 
ATOM   3808 C CG  . LEU D 4 106 ? 10.27118  -6.31045  1.66078   1.000 36.65539  ? 120 LEU D CG  1 
ATOM   3809 C CD1 . LEU D 4 106 ? 9.04711   -6.73255  0.85571   1.000 31.29918  ? 120 LEU D CD1 1 
ATOM   3810 C CD2 . LEU D 4 106 ? 10.40219  -4.78910  1.69124   1.000 22.82576  ? 120 LEU D CD2 1 
ATOM   3811 N N   . LEU D 4 107 ? 11.29344  -9.55268  1.19826   1.000 35.72705  ? 121 LEU D N   1 
ATOM   3812 C CA  . LEU D 4 107 ? 12.33056  -9.97189  0.26256   1.000 37.95638  ? 121 LEU D CA  1 
ATOM   3813 C C   . LEU D 4 107 ? 11.97268  -9.43424  -1.11765  1.000 36.24299  ? 121 LEU D C   1 
ATOM   3814 O O   . LEU D 4 107 ? 11.02882  -9.91577  -1.75132  1.000 39.18115  ? 121 LEU D O   1 
ATOM   3815 C CB  . LEU D 4 107 ? 12.47796  -11.49219 0.24434   1.000 37.36705  ? 121 LEU D CB  1 
ATOM   3816 C CG  . LEU D 4 107 ? 13.56677  -12.00332 -0.70173  1.000 64.07258  ? 121 LEU D CG  1 
ATOM   3817 C CD1 . LEU D 4 107 ? 14.93199  -11.43093 -0.31882  1.000 56.12572  ? 121 LEU D CD1 1 
ATOM   3818 C CD2 . LEU D 4 107 ? 13.59989  -13.52478 -0.73099  1.000 67.69747  ? 121 LEU D CD2 1 
ATOM   3819 N N   . VAL D 4 108 ? 12.71463  -8.43045  -1.57203  1.000 35.83219  ? 122 VAL D N   1 
ATOM   3820 C CA  . VAL D 4 108 ? 12.50905  -7.83264  -2.88501  1.000 32.32491  ? 122 VAL D CA  1 
ATOM   3821 C C   . VAL D 4 108 ? 13.37494  -8.58342  -3.88653  1.000 39.73117  ? 122 VAL D C   1 
ATOM   3822 O O   . VAL D 4 108 ? 14.59812  -8.65024  -3.73060  1.000 43.35651  ? 122 VAL D O   1 
ATOM   3823 C CB  . VAL D 4 108 ? 12.85453  -6.33628  -2.87363  1.000 35.64213  ? 122 VAL D CB  1 
ATOM   3824 C CG1 . VAL D 4 108 ? 12.51841  -5.70258  -4.20699  1.000 32.25484  ? 122 VAL D CG1 1 
ATOM   3825 C CG2 . VAL D 4 108 ? 12.13227  -5.62583  -1.73483  1.000 29.70269  ? 122 VAL D CG2 1 
ATOM   3826 N N   . SER D 4 109 ? 12.73864  -9.15789  -4.91977  1.000 45.58317  ? 123 SER D N   1 
ATOM   3827 C CA  . SER D 4 109 ? 13.47576  -9.87852  -5.94616  1.000 36.92289  ? 123 SER D CA  1 
ATOM   3828 C C   . SER D 4 109 ? 13.65584  -9.02055  -7.19424  1.000 40.73523  ? 123 SER D C   1 
ATOM   3829 O O   . SER D 4 109 ? 12.78423  -8.21330  -7.53574  1.000 42.02359  ? 123 SER D O   1 
ATOM   3830 C CB  . SER D 4 109 ? 12.75645  -11.17660 -6.32045  1.000 41.08703  ? 123 SER D CB  1 
ATOM   3831 O OG  . SER D 4 109 ? 13.00766  -12.17961 -5.34951  1.000 63.31159  ? 123 SER D OG  1 
ATOM   3832 N N   . PRO D 4 110 ? 14.77843  -9.17727  -7.89191  1.000 39.78274  ? 124 PRO D N   1 
ATOM   3833 C CA  . PRO D 4 110 ? 15.03231  -8.36161  -9.08180  1.000 48.52403  ? 124 PRO D CA  1 
ATOM   3834 C C   . PRO D 4 110 ? 14.26563  -8.86910  -10.28898 1.000 40.06415  ? 124 PRO D C   1 
ATOM   3835 O O   . PRO D 4 110 ? 13.91338  -10.04630 -10.38818 1.000 44.21511  ? 124 PRO D O   1 
ATOM   3836 C CB  . PRO D 4 110 ? 16.54064  -8.52173  -9.29344  1.000 43.83285  ? 124 PRO D CB  1 
ATOM   3837 C CG  . PRO D 4 110 ? 16.79468  -9.92030  -8.83362  1.000 48.07944  ? 124 PRO D CG  1 
ATOM   3838 C CD  . PRO D 4 110 ? 15.86772  -10.14046 -7.65088  1.000 37.13915  ? 124 PRO D CD  1 
ATOM   3839 N N   . ASN D 4 111 ? 14.01954  -7.95382  -11.22304 1.000 36.47933  ? 125 ASN D N   1 
ATOM   3840 C CA  . ASN D 4 111 ? 13.32161  -8.27989  -12.46495 1.000 50.24623  ? 125 ASN D CA  1 
ATOM   3841 C C   . ASN D 4 111 ? 14.37389  -8.55504  -13.53133 1.000 43.56469  ? 125 ASN D C   1 
ATOM   3842 O O   . ASN D 4 111 ? 14.87825  -7.64407  -14.18860 1.000 54.77910  ? 125 ASN D O   1 
ATOM   3843 C CB  . ASN D 4 111 ? 12.38178  -7.14944  -12.86494 1.000 62.31550  ? 125 ASN D CB  1 
ATOM   3844 N N   . ILE D 4 112 ? 14.71390  -9.83112  -13.70273 1.000 44.72391  ? 126 ILE D N   1 
ATOM   3845 C CA  . ILE D 4 112 ? 15.73653  -10.22561 -14.66989 1.000 51.49092  ? 126 ILE D CA  1 
ATOM   3846 C C   . ILE D 4 112 ? 15.15684  -10.05768 -16.07181 1.000 59.46469  ? 126 ILE D C   1 
ATOM   3847 O O   . ILE D 4 112 ? 14.27981  -10.82113 -16.48768 1.000 54.21240  ? 126 ILE D O   1 
ATOM   3848 C CB  . ILE D 4 112 ? 16.21627  -11.66180 -14.43273 1.000 56.79348  ? 126 ILE D CB  1 
ATOM   3849 C CG1 . ILE D 4 112 ? 16.54464  -11.88423 -12.95302 1.000 46.62752  ? 126 ILE D CG1 1 
ATOM   3850 C CG2 . ILE D 4 112 ? 17.44124  -11.95286 -15.28149 1.000 54.24348  ? 126 ILE D CG2 1 
ATOM   3851 C CD1 . ILE D 4 112 ? 17.62490  -10.96747 -12.42103 1.000 35.83907  ? 126 ILE D CD1 1 
ATOM   3852 N N   . GLN D 4 113 ? 15.64857  -9.05761  -16.80638 1.000 61.56969  ? 127 GLN D N   1 
ATOM   3853 C CA  . GLN D 4 113 ? 15.06940  -8.73728  -18.10814 1.000 67.37250  ? 127 GLN D CA  1 
ATOM   3854 C C   . GLN D 4 113 ? 15.28689  -9.87250  -19.10409 1.000 75.72805  ? 127 GLN D C   1 
ATOM   3855 O O   . GLN D 4 113 ? 14.33203  -10.39849 -19.68750 1.000 72.89040  ? 127 GLN D O   1 
ATOM   3856 C CB  . GLN D 4 113 ? 15.65890  -7.42716  -18.63525 1.000 51.84085  ? 127 GLN D CB  1 
ATOM   3857 N N   . ASN D 4 114 ? 16.54302  -10.26965 -19.31017 1.000 74.89818  ? 128 ASN D N   1 
ATOM   3858 C CA  . ASN D 4 114 ? 16.88891  -11.33175 -20.25376 1.000 68.26120  ? 128 ASN D CA  1 
ATOM   3859 C C   . ASN D 4 114 ? 17.57737  -12.46257 -19.50245 1.000 59.49441  ? 128 ASN D C   1 
ATOM   3860 O O   . ASN D 4 114 ? 18.80648  -12.44826 -19.32557 1.000 66.33328  ? 128 ASN D O   1 
ATOM   3861 C CB  . ASN D 4 114 ? 17.76716  -10.79709 -21.38190 1.000 71.53575  ? 128 ASN D CB  1 
ATOM   3862 C CG  . ASN D 4 114 ? 17.08114  -9.70382  -22.18003 1.000 83.44299  ? 128 ASN D CG  1 
ATOM   3863 O OD1 . ASN D 4 114 ? 16.14583  -9.96454  -22.93950 1.000 75.66717  ? 128 ASN D OD1 1 
ATOM   3864 N ND2 . ASN D 4 114 ? 17.54343  -8.47059  -22.01083 1.000 82.12032  ? 128 ASN D ND2 1 
ATOM   3865 N N   . PRO D 4 115 ? 16.82438  -13.46155 -19.04151 1.000 55.10435  ? 129 PRO D N   1 
ATOM   3866 C CA  . PRO D 4 115 ? 17.44663  -14.59127 -18.34543 1.000 57.65970  ? 129 PRO D CA  1 
ATOM   3867 C C   . PRO D 4 115 ? 18.37985  -15.35502 -19.26895 1.000 68.76397  ? 129 PRO D C   1 
ATOM   3868 O O   . PRO D 4 115 ? 18.14886  -15.46278 -20.47437 1.000 73.79150  ? 129 PRO D O   1 
ATOM   3869 C CB  . PRO D 4 115 ? 16.25234  -15.45727 -17.92569 1.000 52.79547  ? 129 PRO D CB  1 
ATOM   3870 C CG  . PRO D 4 115 ? 15.05938  -14.56109 -18.02267 1.000 62.40191  ? 129 PRO D CG  1 
ATOM   3871 C CD  . PRO D 4 115 ? 15.36135  -13.59700 -19.12159 1.000 56.99000  ? 129 PRO D CD  1 
ATOM   3872 N N   . ASP D 4 116 ? 19.44907  -15.88671 -18.68380 1.000 62.54412  ? 130 ASP D N   1 
ATOM   3873 C CA  . ASP D 4 116 ? 20.42008  -16.70768 -19.40904 1.000 52.16297  ? 130 ASP D CA  1 
ATOM   3874 C C   . ASP D 4 116 ? 20.87861  -17.84385 -18.49872 1.000 58.87505  ? 130 ASP D C   1 
ATOM   3875 O O   . ASP D 4 116 ? 22.07006  -17.98754 -18.20289 1.000 53.50442  ? 130 ASP D O   1 
ATOM   3876 C CB  . ASP D 4 116 ? 21.59351  -15.84719 -19.87909 1.000 55.91183  ? 130 ASP D CB  1 
ATOM   3877 C CG  . ASP D 4 116 ? 22.49823  -16.56716 -20.85525 1.000 68.09254  ? 130 ASP D CG  1 
ATOM   3878 O OD1 . ASP D 4 116 ? 22.18955  -17.72030 -21.22387 1.000 68.37716  ? 130 ASP D OD1 1 
ATOM   3879 O OD2 . ASP D 4 116 ? 23.52235  -15.97282 -21.25464 1.000 70.35381  ? 130 ASP D OD2 1 
ATOM   3880 N N   . PRO D 4 117 ? 19.94507  -18.68153 -18.03835 1.000 51.38469  ? 131 PRO D N   1 
ATOM   3881 C CA  . PRO D 4 117 ? 20.28560  -19.66188 -17.00054 1.000 58.22368  ? 131 PRO D CA  1 
ATOM   3882 C C   . PRO D 4 117 ? 21.32870  -20.65573 -17.48312 1.000 63.23814  ? 131 PRO D C   1 
ATOM   3883 O O   . PRO D 4 117 ? 21.25092  -21.17771 -18.59615 1.000 78.06296  ? 131 PRO D O   1 
ATOM   3884 C CB  . PRO D 4 117 ? 18.94663  -20.34850 -16.70622 1.000 61.65452  ? 131 PRO D CB  1 
ATOM   3885 C CG  . PRO D 4 117 ? 18.14776  -20.15742 -17.93912 1.000 55.65628  ? 131 PRO D CG  1 
ATOM   3886 C CD  . PRO D 4 117 ? 18.54235  -18.81255 -18.47199 1.000 56.03511  ? 131 PRO D CD  1 
ATOM   3887 N N   . ALA D 4 118 ? 22.31092  -20.91474 -16.62464 1.000 64.29546  ? 132 ALA D N   1 
ATOM   3888 C CA  . ALA D 4 118 ? 23.41861  -21.78884 -16.97387 1.000 55.26093  ? 132 ALA D CA  1 
ATOM   3889 C C   . ALA D 4 118 ? 24.03475  -22.34259 -15.69963 1.000 62.72740  ? 132 ALA D C   1 
ATOM   3890 O O   . ALA D 4 118 ? 23.88383  -21.77499 -14.61463 1.000 58.22282  ? 132 ALA D O   1 
ATOM   3891 C CB  . ALA D 4 118 ? 24.47292  -21.05133 -17.80376 1.000 59.18475  ? 132 ALA D CB  1 
ATOM   3892 N N   . VAL D 4 119 ? 24.73591  -23.46173 -15.85206 1.000 59.99188  ? 133 VAL D N   1 
ATOM   3893 C CA  . VAL D 4 119 ? 25.43881  -24.12255 -14.76065 1.000 50.79609  ? 133 VAL D CA  1 
ATOM   3894 C C   . VAL D 4 119 ? 26.90534  -24.21600 -15.15422 1.000 55.75938  ? 133 VAL D C   1 
ATOM   3895 O O   . VAL D 4 119 ? 27.25445  -24.91515 -16.11425 1.000 58.33894  ? 133 VAL D O   1 
ATOM   3896 C CB  . VAL D 4 119 ? 24.86151  -25.51064 -14.45854 1.000 58.65674  ? 133 VAL D CB  1 
ATOM   3897 C CG1 . VAL D 4 119 ? 25.70314  -26.21010 -13.40612 1.000 53.90954  ? 133 VAL D CG1 1 
ATOM   3898 C CG2 . VAL D 4 119 ? 23.41997  -25.39314 -14.00369 1.000 49.90156  ? 133 VAL D CG2 1 
ATOM   3899 N N   . TYR D 4 120 ? 27.76305  -23.51689 -14.41809 1.000 49.98238  ? 134 TYR D N   1 
ATOM   3900 C CA  . TYR D 4 120 ? 29.18974  -23.49102 -14.69184 1.000 50.59939  ? 134 TYR D CA  1 
ATOM   3901 C C   . TYR D 4 120 ? 29.95533  -24.21032 -13.58857 1.000 55.35402  ? 134 TYR D C   1 
ATOM   3902 O O   . TYR D 4 120 ? 29.53498  -24.23778 -12.42835 1.000 48.90975  ? 134 TYR D O   1 
ATOM   3903 C CB  . TYR D 4 120 ? 29.70560  -22.05423 -14.81763 1.000 45.49020  ? 134 TYR D CB  1 
ATOM   3904 C CG  . TYR D 4 120 ? 28.96324  -21.20350 -15.81843 1.000 52.12137  ? 134 TYR D CG  1 
ATOM   3905 C CD1 . TYR D 4 120 ? 28.96058  -21.52758 -17.16772 1.000 63.15457  ? 134 TYR D CD1 1 
ATOM   3906 C CD2 . TYR D 4 120 ? 28.28684  -20.05815 -15.41869 1.000 48.21659  ? 134 TYR D CD2 1 
ATOM   3907 C CE1 . TYR D 4 120 ? 28.28768  -20.74408 -18.08943 1.000 60.96731  ? 134 TYR D CE1 1 
ATOM   3908 C CE2 . TYR D 4 120 ? 27.61291  -19.26915 -16.33339 1.000 59.49585  ? 134 TYR D CE2 1 
ATOM   3909 C CZ  . TYR D 4 120 ? 27.61741  -19.61687 -17.66714 1.000 62.37521  ? 134 TYR D CZ  1 
ATOM   3910 O OH  . TYR D 4 120 ? 26.95136  -18.83582 -18.58455 1.000 52.54710  ? 134 TYR D OH  1 
ATOM   3911 N N   . GLN D 4 121 ? 31.08852  -24.79295 -13.96294 1.000 52.65889  ? 135 GLN D N   1 
ATOM   3912 C CA  . GLN D 4 121 ? 31.99029  -25.43591 -13.02119 1.000 46.19957  ? 135 GLN D CA  1 
ATOM   3913 C C   . GLN D 4 121 ? 33.19897  -24.53541 -12.81358 1.000 55.16816  ? 135 GLN D C   1 
ATOM   3914 O O   . GLN D 4 121 ? 33.75952  -24.01066 -13.78098 1.000 42.34702  ? 135 GLN D O   1 
ATOM   3915 C CB  . GLN D 4 121 ? 32.41753  -26.81574 -13.52200 1.000 55.39538  ? 135 GLN D CB  1 
ATOM   3916 C CG  . GLN D 4 121 ? 33.18078  -27.63451 -12.49193 1.000 57.87982  ? 135 GLN D CG  1 
ATOM   3917 C CD  . GLN D 4 121 ? 33.00348  -29.13059 -12.68284 1.000 77.63317  ? 135 GLN D CD  1 
ATOM   3918 O OE1 . GLN D 4 121 ? 32.27080  -29.57530 -13.56856 1.000 75.14528  ? 135 GLN D OE1 1 
ATOM   3919 N NE2 . GLN D 4 121 ? 33.67020  -29.91557 -11.84514 1.000 82.59280  ? 135 GLN D NE2 1 
ATOM   3920 N N   . LEU D 4 122 ? 33.58480  -24.34469 -11.55466 1.000 57.22790  ? 136 LEU D N   1 
ATOM   3921 C CA  . LEU D 4 122 ? 34.65611  -23.42964 -11.18723 1.000 51.27492  ? 136 LEU D CA  1 
ATOM   3922 C C   . LEU D 4 122 ? 35.73674  -24.20245 -10.44817 1.000 55.72213  ? 136 LEU D C   1 
ATOM   3923 O O   . LEU D 4 122 ? 35.44106  -24.93067 -9.49639  1.000 62.19942  ? 136 LEU D O   1 
ATOM   3924 C CB  . LEU D 4 122 ? 34.13084  -22.27911 -10.31799 1.000 55.40760  ? 136 LEU D CB  1 
ATOM   3925 C CG  . LEU D 4 122 ? 33.26716  -21.18988 -10.97228 1.000 58.31714  ? 136 LEU D CG  1 
ATOM   3926 C CD1 . LEU D 4 122 ? 31.87476  -21.69261 -11.32353 1.000 54.54760  ? 136 LEU D CD1 1 
ATOM   3927 C CD2 . LEU D 4 122 ? 33.17708  -19.95463 -10.07987 1.000 42.81380  ? 136 LEU D CD2 1 
ATOM   3928 N N   . ARG D 4 123 ? 36.98155  -24.04384 -10.88346 1.000 54.68697  ? 137 ARG D N   1 
ATOM   3929 C CA  . ARG D 4 123 ? 38.09021  -24.78950 -10.30734 1.000 66.46340  ? 137 ARG D CA  1 
ATOM   3930 C C   . ARG D 4 123 ? 38.75707  -23.98977 -9.19429  1.000 64.82980  ? 137 ARG D C   1 
ATOM   3931 O O   . ARG D 4 123 ? 38.80380  -22.75687 -9.22753  1.000 58.63415  ? 137 ARG D O   1 
ATOM   3932 C CB  . ARG D 4 123 ? 39.11720  -25.15118 -11.38467 1.000 49.17318  ? 137 ARG D CB  1 
ATOM   3933 N N   . ASP D 4 124 ? 39.26760  -24.71217 -8.19925  1.000 73.98293  ? 138 ASP D N   1 
ATOM   3934 C CA  . ASP D 4 124 ? 39.96612  -24.08619 -7.08416  1.000 53.64118  ? 138 ASP D CA  1 
ATOM   3935 C C   . ASP D 4 124 ? 41.24522  -23.41680 -7.57254  1.000 62.13617  ? 138 ASP D C   1 
ATOM   3936 O O   . ASP D 4 124 ? 41.97248  -23.96317 -8.40746  1.000 79.59398  ? 138 ASP D O   1 
ATOM   3937 C CB  . ASP D 4 124 ? 40.28962  -25.13276 -6.01515  1.000 57.55908  ? 138 ASP D CB  1 
ATOM   3938 C CG  . ASP D 4 124 ? 40.76276  -24.51919 -4.70118  1.000 75.84857  ? 138 ASP D CG  1 
ATOM   3939 O OD1 . ASP D 4 124 ? 41.26455  -23.37358 -4.69723  1.000 75.16331  ? 138 ASP D OD1 1 
ATOM   3940 O OD2 . ASP D 4 124 ? 40.63725  -25.19755 -3.65971  1.000 77.52341  ? 138 ASP D OD2 1 
ATOM   3941 N N   . SER D 4 125 ? 41.51927  -22.22088 -7.04339  1.000 52.17382  ? 139 SER D N   1 
ATOM   3942 C CA  . SER D 4 125 ? 42.73391  -21.51164 -7.43127  1.000 66.29137  ? 139 SER D CA  1 
ATOM   3943 C C   . SER D 4 125 ? 43.98282  -22.21002 -6.90806  1.000 68.05573  ? 139 SER D C   1 
ATOM   3944 O O   . SER D 4 125 ? 45.04919  -22.11090 -7.52489  1.000 81.28930  ? 139 SER D O   1 
ATOM   3945 C CB  . SER D 4 125 ? 42.68361  -20.06388 -6.93818  1.000 55.90064  ? 139 SER D CB  1 
ATOM   3946 O OG  . SER D 4 125 ? 42.61804  -20.00722 -5.52301  1.000 66.22255  ? 139 SER D OG  1 
ATOM   3947 N N   . LYS D 4 126 ? 43.87192  -22.92327 -5.78770  1.000 71.05459  ? 140 LYS D N   1 
ATOM   3948 C CA  . LYS D 4 126 ? 45.01540  -23.61350 -5.20389  1.000 78.53578  ? 140 LYS D CA  1 
ATOM   3949 C C   . LYS D 4 126 ? 44.82865  -25.12605 -5.24833  1.000 86.27540  ? 140 LYS D C   1 
ATOM   3950 O O   . LYS D 4 126 ? 44.77170  -25.77811 -4.20023  1.000 99.88054  ? 140 LYS D O   1 
ATOM   3951 C CB  . LYS D 4 126 ? 45.23838  -23.14826 -3.76270  1.000 59.91795  ? 140 LYS D CB  1 
ATOM   3952 N N   . SER D 4 127 ? 44.73368  -25.68453 -6.45332  1.000 81.53393  ? 141 SER D N   1 
ATOM   3953 C CA  . SER D 4 127 ? 44.55934  -27.12421 -6.65751  1.000 95.29828  ? 141 SER D CA  1 
ATOM   3954 C C   . SER D 4 127 ? 43.32097  -27.66447 -5.94363  1.000 89.05966  ? 141 SER D C   1 
ATOM   3955 O O   . SER D 4 127 ? 42.77913  -28.70535 -6.32131  1.000 92.01152  ? 141 SER D O   1 
ATOM   3956 C CB  . SER D 4 127 ? 45.80514  -27.88844 -6.19503  1.000 96.42365  ? 141 SER D CB  1 
ATOM   3957 N N   . ASP D 4 129 ? 41.77398  -30.29401 -7.92270  1.000 83.50635  ? 143 ASP D N   1 
ATOM   3958 C CA  . ASP D 4 129 ? 40.74605  -31.32766 -7.97838  1.000 87.25297  ? 143 ASP D CA  1 
ATOM   3959 C C   . ASP D 4 129 ? 39.40836  -30.80799 -7.45451  1.000 86.20066  ? 143 ASP D C   1 
ATOM   3960 O O   . ASP D 4 129 ? 38.34600  -31.19858 -7.94486  1.000 75.47242  ? 143 ASP D O   1 
ATOM   3961 C CB  . ASP D 4 129 ? 41.18096  -32.55969 -7.17967  1.000 75.59754  ? 143 ASP D CB  1 
ATOM   3962 N N   . LYS D 4 130 ? 39.46949  -29.92396 -6.45953  1.000 79.64723  ? 144 LYS D N   1 
ATOM   3963 C CA  . LYS D 4 130 ? 38.25833  -29.37580 -5.86121  1.000 75.89717  ? 144 LYS D CA  1 
ATOM   3964 C C   . LYS D 4 130 ? 37.55763  -28.42463 -6.82629  1.000 73.24682  ? 144 LYS D C   1 
ATOM   3965 O O   . LYS D 4 130 ? 38.20392  -27.68373 -7.57366  1.000 73.00447  ? 144 LYS D O   1 
ATOM   3966 C CB  . LYS D 4 130 ? 38.59514  -28.64832 -4.55978  1.000 59.87078  ? 144 LYS D CB  1 
ATOM   3967 N N   . SER D 4 131 ? 36.22501  -28.44492 -6.80670  1.000 65.82244  ? 145 SER D N   1 
ATOM   3968 C CA  . SER D 4 131 ? 35.44778  -27.56326 -7.66888  1.000 65.77391  ? 145 SER D CA  1 
ATOM   3969 C C   . SER D 4 131 ? 34.04288  -27.40717 -7.10321  1.000 59.33573  ? 145 SER D C   1 
ATOM   3970 O O   . SER D 4 131 ? 33.54965  -28.26394 -6.36366  1.000 55.28336  ? 145 SER D O   1 
ATOM   3971 C CB  . SER D 4 131 ? 35.39264  -28.08646 -9.11126  1.000 57.59431  ? 145 SER D CB  1 
ATOM   3972 O OG  . SER D 4 131 ? 34.78407  -29.36348 -9.17483  1.000 61.92786  ? 145 SER D OG  1 
ATOM   3973 N N   . VAL D 4 132 ? 33.40935  -26.28888 -7.46267  1.000 60.90060  ? 146 VAL D N   1 
ATOM   3974 C CA  . VAL D 4 132 ? 32.02107  -26.00727 -7.12414  1.000 51.98521  ? 146 VAL D CA  1 
ATOM   3975 C C   . VAL D 4 132 ? 31.25064  -25.76087 -8.41599  1.000 54.20695  ? 146 VAL D C   1 
ATOM   3976 O O   . VAL D 4 132 ? 31.82459  -25.46589 -9.46868  1.000 53.29801  ? 146 VAL D O   1 
ATOM   3977 C CB  . VAL D 4 132 ? 31.87581  -24.80134 -6.16898  1.000 50.32877  ? 146 VAL D CB  1 
ATOM   3978 C CG1 . VAL D 4 132 ? 32.63355  -25.04582 -4.87887  1.000 44.17797  ? 146 VAL D CG1 1 
ATOM   3979 C CG2 . VAL D 4 132 ? 32.36375  -23.52939 -6.83682  1.000 42.07648  ? 146 VAL D CG2 1 
ATOM   3980 N N   . CYS D 4 133 ? 29.93063  -25.89044 -8.32572  1.000 47.00617  ? 147 CYS D N   1 
ATOM   3981 C CA  . CYS D 4 133 ? 29.03776  -25.65340 -9.45121  1.000 46.55639  ? 147 CYS D CA  1 
ATOM   3982 C C   . CYS D 4 133 ? 28.24233  -24.38307 -9.19404  1.000 48.13405  ? 147 CYS D C   1 
ATOM   3983 O O   . CYS D 4 133 ? 27.69058  -24.19954 -8.10341  1.000 53.38390  ? 147 CYS D O   1 
ATOM   3984 C CB  . CYS D 4 133 ? 28.09278  -26.83556 -9.66846  1.000 53.87081  ? 147 CYS D CB  1 
ATOM   3985 S SG  . CYS D 4 133 ? 28.91957  -28.43206 -9.75343  1.000 66.23722  ? 147 CYS D SG  1 
ATOM   3986 N N   . LEU D 4 134 ? 28.18753  -23.51164 -10.19375 1.000 47.63800  ? 148 LEU D N   1 
ATOM   3987 C CA  . LEU D 4 134 ? 27.51733  -22.22073 -10.07794 1.000 44.38173  ? 148 LEU D CA  1 
ATOM   3988 C C   . LEU D 4 134 ? 26.33627  -22.19856 -11.03888 1.000 44.47189  ? 148 LEU D C   1 
ATOM   3989 O O   . LEU D 4 134 ? 26.50833  -21.99318 -12.24469 1.000 56.23070  ? 148 LEU D O   1 
ATOM   3990 C CB  . LEU D 4 134 ? 28.47988  -21.07448 -10.36690 1.000 43.52360  ? 148 LEU D CB  1 
ATOM   3991 C CG  . LEU D 4 134 ? 27.86236  -19.67588 -10.40376 1.000 47.56127  ? 148 LEU D CG  1 
ATOM   3992 C CD1 . LEU D 4 134 ? 27.48691  -19.21246 -9.00348  1.000 34.66127  ? 148 LEU D CD1 1 
ATOM   3993 C CD2 . LEU D 4 134 ? 28.80637  -18.69227 -11.07619 1.000 41.21746  ? 148 LEU D CD2 1 
ATOM   3994 N N   . PHE D 4 135 ? 25.14195  -22.42505 -10.50672 1.000 44.14643  ? 149 PHE D N   1 
ATOM   3995 C CA  . PHE D 4 135 ? 23.91936  -22.13072 -11.23859 1.000 48.04228  ? 149 PHE D CA  1 
ATOM   3996 C C   . PHE D 4 135 ? 23.67007  -20.63183 -11.13750 1.000 54.66341  ? 149 PHE D C   1 
ATOM   3997 O O   . PHE D 4 135 ? 23.54962  -20.09515 -10.03203 1.000 47.26483  ? 149 PHE D O   1 
ATOM   3998 C CB  . PHE D 4 135 ? 22.75255  -22.92600 -10.66203 1.000 41.38840  ? 149 PHE D CB  1 
ATOM   3999 C CG  . PHE D 4 135 ? 21.46871  -22.75738 -11.41466 1.000 62.43719  ? 149 PHE D CG  1 
ATOM   4000 C CD1 . PHE D 4 135 ? 21.47228  -22.46663 -12.77008 1.000 60.28047  ? 149 PHE D CD1 1 
ATOM   4001 C CD2 . PHE D 4 135 ? 20.25151  -22.88275 -10.76124 1.000 63.93155  ? 149 PHE D CD2 1 
ATOM   4002 C CE1 . PHE D 4 135 ? 20.28723  -22.31094 -13.46413 1.000 56.23587  ? 149 PHE D CE1 1 
ATOM   4003 C CE2 . PHE D 4 135 ? 19.06204  -22.72717 -11.44803 1.000 58.01972  ? 149 PHE D CE2 1 
ATOM   4004 C CZ  . PHE D 4 135 ? 19.08010  -22.44070 -12.80261 1.000 52.01355  ? 149 PHE D CZ  1 
ATOM   4005 N N   . THR D 4 136 ? 23.61594  -19.94912 -12.27825 1.000 51.23615  ? 150 THR D N   1 
ATOM   4006 C CA  . THR D 4 136 ? 23.56005  -18.49559 -12.27498 1.000 45.43386  ? 150 THR D CA  1 
ATOM   4007 C C   . THR D 4 136 ? 22.68836  -17.99157 -13.41354 1.000 54.25894  ? 150 THR D C   1 
ATOM   4008 O O   . THR D 4 136 ? 22.23852  -18.75105 -14.27398 1.000 55.11278  ? 150 THR D O   1 
ATOM   4009 C CB  . THR D 4 136 ? 24.95390  -17.87156 -12.39676 1.000 51.47351  ? 150 THR D CB  1 
ATOM   4010 O OG1 . THR D 4 136 ? 24.83265  -16.44370 -12.41924 1.000 37.27742  ? 150 THR D OG1 1 
ATOM   4011 C CG2 . THR D 4 136 ? 25.61665  -18.32403 -13.68350 1.000 44.64675  ? 150 THR D CG2 1 
ATOM   4012 N N   . ASP D 4 137 ? 22.45898  -16.67903 -13.39531 1.000 49.94784  ? 151 ASP D N   1 
ATOM   4013 C CA  . ASP D 4 137 ? 21.76654  -15.93923 -14.44550 1.000 47.98657  ? 151 ASP D CA  1 
ATOM   4014 C C   . ASP D 4 137 ? 20.36503  -16.47407 -14.72524 1.000 51.91402  ? 151 ASP D C   1 
ATOM   4015 O O   . ASP D 4 137 ? 19.80178  -16.21065 -15.79275 1.000 55.32952  ? 151 ASP D O   1 
ATOM   4016 C CB  . ASP D 4 137 ? 22.59378  -15.91337 -15.73385 1.000 43.91705  ? 151 ASP D CB  1 
ATOM   4017 C CG  . ASP D 4 137 ? 23.93388  -15.22385 -15.54528 1.000 55.82650  ? 151 ASP D CG  1 
ATOM   4018 O OD1 . ASP D 4 137 ? 24.01137  -14.32549 -14.67954 1.000 58.21998  ? 151 ASP D OD1 1 
ATOM   4019 O OD2 . ASP D 4 137 ? 24.90908  -15.57495 -16.24543 1.000 55.11740  ? 151 ASP D OD2 1 
ATOM   4020 N N   . PHE D 4 138 ? 19.76526  -17.20633 -13.78773 1.000 52.37670  ? 152 PHE D N   1 
ATOM   4021 C CA  . PHE D 4 138 ? 18.39783  -17.66387 -13.96977 1.000 54.51746  ? 152 PHE D CA  1 
ATOM   4022 C C   . PHE D 4 138 ? 17.43099  -16.56259 -13.53504 1.000 58.04526  ? 152 PHE D C   1 
ATOM   4023 O O   . PHE D 4 138 ? 17.83316  -15.44557 -13.20647 1.000 58.12100  ? 152 PHE D O   1 
ATOM   4024 C CB  . PHE D 4 138 ? 18.17207  -18.98430 -13.23341 1.000 54.65471  ? 152 PHE D CB  1 
ATOM   4025 C CG  . PHE D 4 138 ? 18.51892  -18.94468 -11.77278 1.000 57.32241  ? 152 PHE D CG  1 
ATOM   4026 C CD1 . PHE D 4 138 ? 19.76130  -19.37329 -11.32522 1.000 51.40144  ? 152 PHE D CD1 1 
ATOM   4027 C CD2 . PHE D 4 138 ? 17.59499  -18.49039 -10.84905 1.000 57.81288  ? 152 PHE D CD2 1 
ATOM   4028 C CE1 . PHE D 4 138 ? 20.07410  -19.33699 -9.98309  1.000 49.50869  ? 152 PHE D CE1 1 
ATOM   4029 C CE2 . PHE D 4 138 ? 17.90234  -18.44827 -9.51007  1.000 50.87627  ? 152 PHE D CE2 1 
ATOM   4030 C CZ  . PHE D 4 138 ? 19.14048  -18.86972 -9.07399  1.000 55.60361  ? 152 PHE D CZ  1 
ATOM   4031 N N   . ASP D 4 139 ? 16.14191  -16.88022 -13.52706 1.000 56.98295  ? 153 ASP D N   1 
ATOM   4032 C CA  . ASP D 4 139 ? 15.04551  -15.93326 -13.36817 1.000 62.53938  ? 153 ASP D CA  1 
ATOM   4033 C C   . ASP D 4 139 ? 14.52432  -15.93248 -11.93449 1.000 65.98042  ? 153 ASP D C   1 
ATOM   4034 O O   . ASP D 4 139 ? 14.53656  -16.96042 -11.25143 1.000 60.67893  ? 153 ASP D O   1 
ATOM   4035 C CB  . ASP D 4 139 ? 13.91601  -16.29328 -14.34118 1.000 59.50812  ? 153 ASP D CB  1 
ATOM   4036 C CG  . ASP D 4 139 ? 12.59000  -15.69875 -13.95825 1.000 70.53461  ? 153 ASP D CG  1 
ATOM   4037 O OD1 . ASP D 4 139 ? 12.42911  -14.46662 -14.08560 1.000 74.79464  ? 153 ASP D OD1 1 
ATOM   4038 O OD2 . ASP D 4 139 ? 11.69053  -16.46047 -13.53577 1.000 77.14563  ? 153 ASP D OD2 1 
ATOM   4039 N N   . SER D 4 140 ? 14.05204  -14.76393 -11.48208 1.000 61.87946  ? 154 SER D N   1 
ATOM   4040 C CA  . SER D 4 140 ? 13.67427  -14.62450 -10.07585 1.000 57.59690  ? 154 SER D CA  1 
ATOM   4041 C C   . SER D 4 140 ? 12.53437  -15.55490 -9.67093  1.000 55.96889  ? 154 SER D C   1 
ATOM   4042 O O   . SER D 4 140 ? 12.40054  -15.86640 -8.48209  1.000 66.55151  ? 154 SER D O   1 
ATOM   4043 C CB  . SER D 4 140 ? 13.29199  -13.17295 -9.75138  1.000 49.67459  ? 154 SER D CB  1 
ATOM   4044 O OG  . SER D 4 140 ? 14.43366  -12.33869 -9.68815  1.000 43.84716  ? 154 SER D OG  1 
ATOM   4045 N N   . GLN D 4 141 ? 11.72191  -16.01640 -10.62078 1.000 66.99440  ? 155 GLN D N   1 
ATOM   4046 C CA  . GLN D 4 141 ? 10.64506  -16.95473 -10.31961 1.000 72.41467  ? 155 GLN D CA  1 
ATOM   4047 C C   . GLN D 4 141 ? 11.13511  -18.38636 -10.14044 1.000 64.35806  ? 155 GLN D C   1 
ATOM   4048 O O   . GLN D 4 141 ? 10.31836  -19.27480 -9.87531  1.000 74.04484  ? 155 GLN D O   1 
ATOM   4049 C CB  . GLN D 4 141 ? 9.57546   -16.91534 -11.41752 1.000 72.46194  ? 155 GLN D CB  1 
ATOM   4050 N N   . THR D 4 142 ? 12.43492  -18.63162 -10.27102 1.000 63.63511  ? 156 THR D N   1 
ATOM   4051 C CA  . THR D 4 142 ? 12.99701  -19.96271 -10.09193 1.000 65.80963  ? 156 THR D CA  1 
ATOM   4052 C C   . THR D 4 142 ? 13.38396  -20.16983 -8.63359  1.000 56.00108  ? 156 THR D C   1 
ATOM   4053 O O   . THR D 4 142 ? 14.08290  -19.33893 -8.04469  1.000 57.98633  ? 156 THR D O   1 
ATOM   4054 C CB  . THR D 4 142 ? 14.21718  -20.15859 -10.99155 1.000 64.09954  ? 156 THR D CB  1 
ATOM   4055 O OG1 . THR D 4 142 ? 13.87362  -19.81330 -12.33820 1.000 64.68659  ? 156 THR D OG1 1 
ATOM   4056 C CG2 . THR D 4 142 ? 14.68876  -21.60306 -10.94700 1.000 62.77573  ? 156 THR D CG2 1 
ATOM   4057 N N   . ASN D 4 143 ? 12.92245  -21.27442 -8.05913  1.000 63.80686  ? 157 ASN D N   1 
ATOM   4058 C CA  . ASN D 4 143 ? 13.24287  -21.65442 -6.69363  1.000 65.97644  ? 157 ASN D CA  1 
ATOM   4059 C C   . ASN D 4 143 ? 14.36764  -22.68113 -6.69335  1.000 66.52839  ? 157 ASN D C   1 
ATOM   4060 O O   . ASN D 4 143 ? 14.47136  -23.51415 -7.59685  1.000 74.13671  ? 157 ASN D O   1 
ATOM   4061 C CB  . ASN D 4 143 ? 12.01297  -22.22774 -5.98324  1.000 54.69269  ? 157 ASN D CB  1 
ATOM   4062 N N   . VAL D 4 144 ? 15.21526  -22.60901 -5.67066  1.000 63.68954  ? 158 VAL D N   1 
ATOM   4063 C CA  . VAL D 4 144 ? 16.30730  -23.55555 -5.47011  1.000 68.73668  ? 158 VAL D CA  1 
ATOM   4064 C C   . VAL D 4 144 ? 16.01655  -24.35373 -4.20697  1.000 66.26048  ? 158 VAL D C   1 
ATOM   4065 O O   . VAL D 4 144 ? 15.77494  -23.77375 -3.14140  1.000 78.46769  ? 158 VAL D O   1 
ATOM   4066 C CB  . VAL D 4 144 ? 17.66512  -22.83908 -5.36846  1.000 69.59801  ? 158 VAL D CB  1 
ATOM   4067 C CG1 . VAL D 4 144 ? 18.79917  -23.85199 -5.32853  1.000 57.77204  ? 158 VAL D CG1 1 
ATOM   4068 C CG2 . VAL D 4 144 ? 17.84292  -21.86741 -6.52676  1.000 66.24004  ? 158 VAL D CG2 1 
ATOM   4069 N N   . SER D 4 145 ? 16.03862  -25.67847 -4.32331  1.000 67.96089  ? 159 SER D N   1 
ATOM   4070 C CA  . SER D 4 145 ? 15.72736  -26.56826 -3.21099  1.000 72.74542  ? 159 SER D CA  1 
ATOM   4071 C C   . SER D 4 145 ? 17.02210  -27.04363 -2.56623  1.000 72.95540  ? 159 SER D C   1 
ATOM   4072 O O   . SER D 4 145 ? 17.88759  -27.60433 -3.24794  1.000 72.79294  ? 159 SER D O   1 
ATOM   4073 C CB  . SER D 4 145 ? 14.90808  -27.76772 -3.68213  1.000 77.20426  ? 159 SER D CB  1 
ATOM   4074 O OG  . SER D 4 145 ? 15.73232  -28.69718 -4.36429  1.000 86.85440  ? 159 SER D OG  1 
ATOM   4075 N N   . GLN D 4 146 ? 17.14944  -26.82439 -1.25837  1.000 83.50428  ? 160 GLN D N   1 
ATOM   4076 C CA  . GLN D 4 146 ? 18.29301  -27.35022 -0.52503  1.000 84.45326  ? 160 GLN D CA  1 
ATOM   4077 C C   . GLN D 4 146 ? 18.31591  -28.86858 -0.63290  1.000 83.97743  ? 160 GLN D C   1 
ATOM   4078 O O   . GLN D 4 146 ? 17.29087  -29.53084 -0.44530  1.000 84.47387  ? 160 GLN D O   1 
ATOM   4079 C CB  . GLN D 4 146 ? 18.23388  -26.91757 0.94061   1.000 58.35322  ? 160 GLN D CB  1 
ATOM   4080 N N   . SER D 4 147 ? 19.48802  -29.41453 -0.94994  1.000 82.93087  ? 161 SER D N   1 
ATOM   4081 C CA  . SER D 4 147 ? 19.61062  -30.84409 -1.19834  1.000 85.14921  ? 161 SER D CA  1 
ATOM   4082 C C   . SER D 4 147 ? 19.21763  -31.65386 0.03221   1.000 95.10371  ? 161 SER D C   1 
ATOM   4083 O O   . SER D 4 147 ? 19.44032  -31.24400 1.17505   1.000 96.56864  ? 161 SER D O   1 
ATOM   4084 C CB  . SER D 4 147 ? 21.04064  -31.19315 -1.60926  1.000 87.07517  ? 161 SER D CB  1 
ATOM   4085 O OG  . SER D 4 147 ? 21.20949  -32.59765 -1.69132  1.000 92.49041  ? 161 SER D OG  1 
ATOM   4086 N N   . LYS D 4 148 ? 18.62082  -32.81884 -0.21712  1.000 95.23902  ? 162 LYS D N   1 
ATOM   4087 C CA  . LYS D 4 148 ? 18.26175  -33.76165 0.83214   1.000 90.75096  ? 162 LYS D CA  1 
ATOM   4088 C C   . LYS D 4 148 ? 19.28423  -34.87995 0.98726   1.000 98.25786  ? 162 LYS D C   1 
ATOM   4089 O O   . LYS D 4 148 ? 19.06430  -35.79780 1.78430   1.000 96.60466  ? 162 LYS D O   1 
ATOM   4090 C CB  . LYS D 4 148 ? 16.87393  -34.35226 0.56065   1.000 75.67793  ? 162 LYS D CB  1 
ATOM   4091 N N   . ASP D 4 149 ? 20.38719  -34.82714 0.24300   1.000 96.20058  ? 163 ASP D N   1 
ATOM   4092 C CA  . ASP D 4 149 ? 21.49976  -35.75270 0.40401   1.000 85.66089  ? 163 ASP D CA  1 
ATOM   4093 C C   . ASP D 4 149 ? 22.55276  -35.12731 1.30901   1.000 92.07433  ? 163 ASP D C   1 
ATOM   4094 O O   . ASP D 4 149 ? 22.87614  -33.94306 1.17681   1.000 100.57863 ? 163 ASP D O   1 
ATOM   4095 C CB  . ASP D 4 149 ? 22.11823  -36.11516 -0.94774  1.000 79.13553  ? 163 ASP D CB  1 
ATOM   4096 N N   . SER D 4 150 ? 23.08792  -35.93239 2.22901   1.000 96.47152  ? 164 SER D N   1 
ATOM   4097 C CA  . SER D 4 150 ? 23.99582  -35.42156 3.24952   1.000 84.55511  ? 164 SER D CA  1 
ATOM   4098 C C   . SER D 4 150 ? 25.37576  -35.07053 2.70769   1.000 89.80951  ? 164 SER D C   1 
ATOM   4099 O O   . SER D 4 150 ? 26.13824  -34.39529 3.40852   1.000 92.29734  ? 164 SER D O   1 
ATOM   4100 C CB  . SER D 4 150 ? 24.13459  -36.44281 4.38144   1.000 80.95081  ? 164 SER D CB  1 
ATOM   4101 N N   . ASP D 4 151 ? 25.71418  -35.49671 1.48986   1.000 72.82676  ? 165 ASP D N   1 
ATOM   4102 C CA  . ASP D 4 151 ? 27.05481  -35.30523 0.95394   1.000 77.57043  ? 165 ASP D CA  1 
ATOM   4103 C C   . ASP D 4 151 ? 27.15418  -34.18208 -0.07325  1.000 84.49696  ? 165 ASP D C   1 
ATOM   4104 O O   . ASP D 4 151 ? 28.27198  -33.76152 -0.39263  1.000 78.63865  ? 165 ASP D O   1 
ATOM   4105 C CB  . ASP D 4 151 ? 27.56349  -36.60996 0.32709   1.000 83.72219  ? 165 ASP D CB  1 
ATOM   4106 N N   . VAL D 4 152 ? 26.03430  -33.68732 -0.59832  1.000 78.82586  ? 166 VAL D N   1 
ATOM   4107 C CA  . VAL D 4 152 ? 26.03604  -32.60766 -1.58055  1.000 74.98909  ? 166 VAL D CA  1 
ATOM   4108 C C   . VAL D 4 152 ? 25.31157  -31.40426 -0.98887  1.000 70.89185  ? 166 VAL D C   1 
ATOM   4109 O O   . VAL D 4 152 ? 24.17814  -31.52482 -0.50843  1.000 72.44352  ? 166 VAL D O   1 
ATOM   4110 C CB  . VAL D 4 152 ? 25.39789  -33.04227 -2.91357  1.000 77.41896  ? 166 VAL D CB  1 
ATOM   4111 C CG1 . VAL D 4 152 ? 24.04869  -33.70182 -2.68247  1.000 77.24698  ? 166 VAL D CG1 1 
ATOM   4112 C CG2 . VAL D 4 152 ? 25.26645  -31.85042 -3.85278  1.000 73.03485  ? 166 VAL D CG2 1 
ATOM   4113 N N   . TYR D 4 153 ? 25.96761  -30.24823 -1.02747  1.000 58.58642  ? 167 TYR D N   1 
ATOM   4114 C CA  . TYR D 4 153 ? 25.46447  -29.02434 -0.42204  1.000 58.66721  ? 167 TYR D CA  1 
ATOM   4115 C C   . TYR D 4 153 ? 24.97524  -28.07046 -1.50385  1.000 56.16014  ? 167 TYR D C   1 
ATOM   4116 O O   . TYR D 4 153 ? 25.56804  -27.98623 -2.58308  1.000 54.67501  ? 167 TYR D O   1 
ATOM   4117 C CB  . TYR D 4 153 ? 26.55238  -28.35161 0.42168   1.000 46.93111  ? 167 TYR D CB  1 
ATOM   4118 C CG  . TYR D 4 153 ? 27.19639  -29.28212 1.42598   1.000 59.60585  ? 167 TYR D CG  1 
ATOM   4119 C CD1 . TYR D 4 153 ? 26.68249  -29.41236 2.71300   1.000 73.74317  ? 167 TYR D CD1 1 
ATOM   4120 C CD2 . TYR D 4 153 ? 28.30869  -30.04185 1.08486   1.000 57.19089  ? 167 TYR D CD2 1 
ATOM   4121 C CE1 . TYR D 4 153 ? 27.26211  -30.26971 3.63373   1.000 64.72586  ? 167 TYR D CE1 1 
ATOM   4122 C CE2 . TYR D 4 153 ? 28.89477  -30.90086 1.99622   1.000 67.51915  ? 167 TYR D CE2 1 
ATOM   4123 C CZ  . TYR D 4 153 ? 28.36855  -31.01123 3.26975   1.000 76.08853  ? 167 TYR D CZ  1 
ATOM   4124 O OH  . TYR D 4 153 ? 28.95061  -31.86430 4.18195   1.000 68.00253  ? 167 TYR D OH  1 
ATOM   4125 N N   . ILE D 4 154 ? 23.89304  -27.35179 -1.20666  1.000 50.00145  ? 168 ILE D N   1 
ATOM   4126 C CA  . ILE D 4 154 ? 23.28183  -26.40741 -2.13727  1.000 50.69654  ? 168 ILE D CA  1 
ATOM   4127 C C   . ILE D 4 154 ? 22.86148  -25.17260 -1.35220  1.000 45.19901  ? 168 ILE D C   1 
ATOM   4128 O O   . ILE D 4 154 ? 22.05598  -25.27400 -0.42028  1.000 51.15696  ? 168 ILE D O   1 
ATOM   4129 C CB  . ILE D 4 154 ? 22.06946  -27.01345 -2.86693  1.000 63.15576  ? 168 ILE D CB  1 
ATOM   4130 C CG1 . ILE D 4 154 ? 22.52548  -28.03054 -3.91426  1.000 65.10231  ? 168 ILE D CG1 1 
ATOM   4131 C CG2 . ILE D 4 154 ? 21.22427  -25.92211 -3.50376  1.000 66.37534  ? 168 ILE D CG2 1 
ATOM   4132 C CD1 . ILE D 4 154 ? 21.39899  -28.86095 -4.48189  1.000 76.87454  ? 168 ILE D CD1 1 
ATOM   4133 N N   . THR D 4 155 ? 23.40076  -24.01208 -1.72242  1.000 46.14078  ? 169 THR D N   1 
ATOM   4134 C CA  . THR D 4 155 ? 23.03198  -22.76407 -1.07312  1.000 37.41379  ? 169 THR D CA  1 
ATOM   4135 C C   . THR D 4 155 ? 21.71883  -22.23400 -1.64116  1.000 42.87459  ? 169 THR D C   1 
ATOM   4136 O O   . THR D 4 155 ? 21.23791  -22.67168 -2.68871  1.000 53.18550  ? 169 THR D O   1 
ATOM   4137 C CB  . THR D 4 155 ? 24.12282  -21.71112 -1.25247  1.000 40.47557  ? 169 THR D CB  1 
ATOM   4138 O OG1 . THR D 4 155 ? 24.09951  -21.22397 -2.60345  1.000 47.72690  ? 169 THR D OG1 1 
ATOM   4139 C CG2 . THR D 4 155 ? 25.48944  -22.29831 -0.94878  1.000 37.81973  ? 169 THR D CG2 1 
ATOM   4140 N N   . ASP D 4 156 ? 21.14226  -21.26309 -0.93907  1.000 49.29997  ? 170 ASP D N   1 
ATOM   4141 C CA  . ASP D 4 156 ? 19.92205  -20.62457 -1.40382  1.000 42.89812  ? 170 ASP D CA  1 
ATOM   4142 C C   . ASP D 4 156 ? 20.23449  -19.67915 -2.56397  1.000 48.03049  ? 170 ASP D C   1 
ATOM   4143 O O   . ASP D 4 156 ? 21.38565  -19.50510 -2.97413  1.000 55.10861  ? 170 ASP D O   1 
ATOM   4144 C CB  . ASP D 4 156 ? 19.24845  -19.87313 -0.25792  1.000 36.19906  ? 170 ASP D CB  1 
ATOM   4145 N N   . LYS D 4 157 ? 19.18590  -19.06300 -3.10306  1.000 58.97895  ? 171 LYS D N   1 
ATOM   4146 C CA  . LYS D 4 157 ? 19.36275  -18.01705 -4.10025  1.000 46.98760  ? 171 LYS D CA  1 
ATOM   4147 C C   . LYS D 4 157 ? 20.11686  -16.83772 -3.50471  1.000 42.56740  ? 171 LYS D C   1 
ATOM   4148 O O   . LYS D 4 157 ? 20.02973  -16.55248 -2.30896  1.000 45.82736  ? 171 LYS D O   1 
ATOM   4149 C CB  . LYS D 4 157 ? 18.01197  -17.53336 -4.62357  1.000 46.60913  ? 171 LYS D CB  1 
ATOM   4150 C CG  . LYS D 4 157 ? 17.56372  -18.16084 -5.91157  1.000 65.49137  ? 171 LYS D CG  1 
ATOM   4151 C CD  . LYS D 4 157 ? 16.30398  -17.47522 -6.40494  1.000 64.07649  ? 171 LYS D CD  1 
ATOM   4152 C CE  . LYS D 4 157 ? 15.20812  -17.53426 -5.35412  1.000 42.95001  ? 171 LYS D CE  1 
ATOM   4153 N NZ  . LYS D 4 157 ? 13.93182  -16.95338 -5.85903  1.000 68.64134  ? 171 LYS D NZ  1 
ATOM   4154 N N   . CYS D 4 158 ? 20.84749  -16.13467 -4.36146  1.000 43.98393  ? 172 CYS D N   1 
ATOM   4155 C CA  . CYS D 4 158 ? 21.60677  -14.97031 -3.93563  1.000 38.62507  ? 172 CYS D CA  1 
ATOM   4156 C C   . CYS D 4 158 ? 21.61459  -13.95998 -5.07147  1.000 41.86259  ? 172 CYS D C   1 
ATOM   4157 O O   . CYS D 4 158 ? 21.97286  -14.30203 -6.20218  1.000 41.75926  ? 172 CYS D O   1 
ATOM   4158 C CB  . CYS D 4 158 ? 23.03521  -15.36482 -3.54494  1.000 49.06495  ? 172 CYS D CB  1 
ATOM   4159 S SG  . CYS D 4 158 ? 23.74618  -14.35075 -2.24033  1.000 54.03641  ? 172 CYS D SG  1 
ATOM   4160 N N   . VAL D 4 159 ? 21.22420  -12.72596 -4.76919  1.000 38.78046  ? 173 VAL D N   1 
ATOM   4161 C CA  . VAL D 4 159 ? 21.11593  -11.66908 -5.76518  1.000 32.58889  ? 173 VAL D CA  1 
ATOM   4162 C C   . VAL D 4 159 ? 22.30941  -10.73836 -5.61909  1.000 34.33801  ? 173 VAL D C   1 
ATOM   4163 O O   . VAL D 4 159 ? 22.47702  -10.09229 -4.57741  1.000 40.54321  ? 173 VAL D O   1 
ATOM   4164 C CB  . VAL D 4 159 ? 19.80578  -10.88528 -5.60995  1.000 43.96398  ? 173 VAL D CB  1 
ATOM   4165 C CG1 . VAL D 4 159 ? 19.66836  -9.88206  -6.73423  1.000 41.88576  ? 173 VAL D CG1 1 
ATOM   4166 C CG2 . VAL D 4 159 ? 18.61321  -11.82904 -5.54978  1.000 43.94586  ? 173 VAL D CG2 1 
ATOM   4167 N N   . LEU D 4 160 ? 23.12763  -10.64439 -6.66261  1.000 38.21212  ? 174 LEU D N   1 
ATOM   4168 C CA  . LEU D 4 160 ? 24.22855  -9.69476  -6.68594  1.000 41.91437  ? 174 LEU D CA  1 
ATOM   4169 C C   . LEU D 4 160 ? 23.91462  -8.55910  -7.65275  1.000 49.57828  ? 174 LEU D C   1 
ATOM   4170 O O   . LEU D 4 160 ? 23.11080  -8.69628  -8.57875  1.000 40.95083  ? 174 LEU D O   1 
ATOM   4171 C CB  . LEU D 4 160 ? 25.55065  -10.37896 -7.05699  1.000 35.99534  ? 174 LEU D CB  1 
ATOM   4172 C CG  . LEU D 4 160 ? 25.78390  -10.92928 -8.46393  1.000 49.96901  ? 174 LEU D CG  1 
ATOM   4173 C CD1 . LEU D 4 160 ? 26.31818  -9.85034  -9.39178  1.000 44.51130  ? 174 LEU D CD1 1 
ATOM   4174 C CD2 . LEU D 4 160 ? 26.74530  -12.11021 -8.41116  1.000 47.00151  ? 174 LEU D CD2 1 
ATOM   4175 N N   . ASP D 4 161 ? 24.57044  -7.42586  -7.42739  1.000 53.08101  ? 175 ASP D N   1 
ATOM   4176 C CA  . ASP D 4 161 ? 24.26744  -6.19009  -8.13933  1.000 46.77522  ? 175 ASP D CA  1 
ATOM   4177 C C   . ASP D 4 161 ? 25.57367  -5.57350  -8.62110  1.000 52.00737  ? 175 ASP D C   1 
ATOM   4178 O O   . ASP D 4 161 ? 26.34378  -5.03720  -7.81792  1.000 46.15353  ? 175 ASP D O   1 
ATOM   4179 C CB  . ASP D 4 161 ? 23.50364  -5.22376  -7.23201  1.000 53.02370  ? 175 ASP D CB  1 
ATOM   4180 C CG  . ASP D 4 161 ? 22.79755  -4.12089  -8.00156  1.000 56.32532  ? 175 ASP D CG  1 
ATOM   4181 O OD1 . ASP D 4 161 ? 23.31827  -3.68104  -9.04924  1.000 62.32805  ? 175 ASP D OD1 1 
ATOM   4182 O OD2 . ASP D 4 161 ? 21.71354  -3.69204  -7.55098  1.000 60.61886  ? 175 ASP D OD2 1 
ATOM   4183 N N   . MET D 4 162 ? 25.82397  -5.64764  -9.92720  1.000 45.90463  ? 176 MET D N   1 
ATOM   4184 C CA  . MET D 4 162 ? 26.97518  -4.97567  -10.53140 1.000 52.00070  ? 176 MET D CA  1 
ATOM   4185 C C   . MET D 4 162 ? 26.54660  -3.54519  -10.82211 1.000 49.29151  ? 176 MET D C   1 
ATOM   4186 O O   . MET D 4 162 ? 25.99699  -3.24015  -11.88120 1.000 59.14128  ? 176 MET D O   1 
ATOM   4187 C CB  . MET D 4 162 ? 27.44277  -5.71018  -11.78133 1.000 46.29949  ? 176 MET D CB  1 
ATOM   4188 C CG  . MET D 4 162 ? 27.81445  -7.16173  -11.51426 1.000 43.99630  ? 176 MET D CG  1 
ATOM   4189 S SD  . MET D 4 162 ? 28.19988  -8.11134  -12.99160 1.000 61.91230  ? 176 MET D SD  1 
ATOM   4190 C CE  . MET D 4 162 ? 29.87242  -7.56885  -13.32657 1.000 40.13914  ? 176 MET D CE  1 
ATOM   4191 N N   . ARG D 4 163 ? 26.80591  -2.65856  -9.85697  1.000 51.17998  ? 177 ARG D N   1 
ATOM   4192 C CA  . ARG D 4 163 ? 26.21217  -1.32421  -9.87737  1.000 60.04969  ? 177 ARG D CA  1 
ATOM   4193 C C   . ARG D 4 163 ? 26.67447  -0.52169  -11.08868 1.000 56.96490  ? 177 ARG D C   1 
ATOM   4194 O O   . ARG D 4 163 ? 25.85949  0.09380   -11.78586 1.000 64.74324  ? 177 ARG D O   1 
ATOM   4195 C CB  . ARG D 4 163 ? 26.54330  -0.58872  -8.57736  1.000 53.05418  ? 177 ARG D CB  1 
ATOM   4196 N N   . SER D 4 164 ? 27.98061  -0.52441  -11.36343 1.000 52.00773  ? 178 SER D N   1 
ATOM   4197 C CA  . SER D 4 164 ? 28.50476  0.25609   -12.47958 1.000 61.37965  ? 178 SER D CA  1 
ATOM   4198 C C   . SER D 4 164 ? 27.93786  -0.19161  -13.82193 1.000 70.74839  ? 178 SER D C   1 
ATOM   4199 O O   . SER D 4 164 ? 28.03218  0.55674   -14.80106 1.000 77.17410  ? 178 SER D O   1 
ATOM   4200 C CB  . SER D 4 164 ? 30.03388  0.17499   -12.50577 1.000 41.33666  ? 178 SER D CB  1 
ATOM   4201 N N   . MET D 4 165 ? 27.34419  -1.38351  -13.88842 1.000 57.87506  ? 179 MET D N   1 
ATOM   4202 C CA  . MET D 4 165 ? 26.80995  -1.92928  -15.12753 1.000 54.19045  ? 179 MET D CA  1 
ATOM   4203 C C   . MET D 4 165 ? 25.29406  -2.05337  -15.12693 1.000 56.47812  ? 179 MET D C   1 
ATOM   4204 O O   . MET D 4 165 ? 24.72886  -2.51597  -16.12378 1.000 66.53032  ? 179 MET D O   1 
ATOM   4205 C CB  . MET D 4 165 ? 27.43134  -3.30074  -15.40727 1.000 49.15908  ? 179 MET D CB  1 
ATOM   4206 C CG  . MET D 4 165 ? 28.90895  -3.24970  -15.73861 1.000 53.03831  ? 179 MET D CG  1 
ATOM   4207 S SD  . MET D 4 165 ? 29.60129  -4.88974  -16.01558 1.000 81.43195  ? 179 MET D SD  1 
ATOM   4208 C CE  . MET D 4 165 ? 28.26071  -5.66121  -16.91624 1.000 69.62748  ? 179 MET D CE  1 
ATOM   4209 N N   . ASP D 4 166 ? 24.62464  -1.65866  -14.04113 1.000 64.56769  ? 180 ASP D N   1 
ATOM   4210 C CA  . ASP D 4 166 ? 23.16930  -1.78025  -13.92020 1.000 65.95863  ? 180 ASP D CA  1 
ATOM   4211 C C   . ASP D 4 166 ? 22.70601  -3.19479  -14.26412 1.000 59.38263  ? 180 ASP D C   1 
ATOM   4212 O O   . ASP D 4 166 ? 21.70567  -3.39516  -14.95733 1.000 67.92321  ? 180 ASP D O   1 
ATOM   4213 C CB  . ASP D 4 166 ? 22.45347  -0.74214  -14.78967 1.000 54.49448  ? 180 ASP D CB  1 
ATOM   4214 N N   . PHE D 4 167 ? 23.45050  -4.18696  -13.77726 1.000 49.39824  ? 181 PHE D N   1 
ATOM   4215 C CA  . PHE D 4 167 ? 23.18891  -5.59245  -14.06221 1.000 51.62924  ? 181 PHE D CA  1 
ATOM   4216 C C   . PHE D 4 167 ? 23.03914  -6.34685  -12.74948 1.000 53.51477  ? 181 PHE D C   1 
ATOM   4217 O O   . PHE D 4 167 ? 23.96529  -6.36789  -11.93114 1.000 55.05999  ? 181 PHE D O   1 
ATOM   4218 C CB  . PHE D 4 167 ? 24.31401  -6.19655  -14.90665 1.000 50.16372  ? 181 PHE D CB  1 
ATOM   4219 C CG  . PHE D 4 167 ? 24.10544  -7.64500  -15.25708 1.000 46.45954  ? 181 PHE D CG  1 
ATOM   4220 C CD1 . PHE D 4 167 ? 23.27116  -8.00666  -16.30113 1.000 46.44158  ? 181 PHE D CD1 1 
ATOM   4221 C CD2 . PHE D 4 167 ? 24.75483  -8.64388  -14.54954 1.000 53.53832  ? 181 PHE D CD2 1 
ATOM   4222 C CE1 . PHE D 4 167 ? 23.08178  -9.33751  -16.62774 1.000 60.19221  ? 181 PHE D CE1 1 
ATOM   4223 C CE2 . PHE D 4 167 ? 24.57125  -9.97715  -14.87225 1.000 54.19595  ? 181 PHE D CE2 1 
ATOM   4224 C CZ  . PHE D 4 167 ? 23.73433  -10.32460 -15.91111 1.000 50.99281  ? 181 PHE D CZ  1 
ATOM   4225 N N   . LYS D 4 168 ? 21.87731  -6.95815  -12.54994 1.000 45.86463  ? 182 LYS D N   1 
ATOM   4226 C CA  . LYS D 4 168 ? 21.63591  -7.84466  -11.42351 1.000 43.84156  ? 182 LYS D CA  1 
ATOM   4227 C C   . LYS D 4 168 ? 21.55776  -9.28017  -11.92475 1.000 50.86212  ? 182 LYS D C   1 
ATOM   4228 O O   . LYS D 4 168 ? 21.14433  -9.53347  -13.05920 1.000 55.83498  ? 182 LYS D O   1 
ATOM   4229 C CB  . LYS D 4 168 ? 20.34291  -7.47021  -10.68849 1.000 36.36084  ? 182 LYS D CB  1 
ATOM   4230 C CG  . LYS D 4 168 ? 20.37905  -6.09499  -10.03783 1.000 43.27659  ? 182 LYS D CG  1 
ATOM   4231 C CD  . LYS D 4 168 ? 19.03818  -5.38804  -10.14687 1.000 57.20498  ? 182 LYS D CD  1 
ATOM   4232 C CE  . LYS D 4 168 ? 19.12634  -3.94971  -9.65456  1.000 61.33560  ? 182 LYS D CE  1 
ATOM   4233 N NZ  . LYS D 4 168 ? 17.93599  -3.14466  -10.05710 1.000 62.27416  ? 182 LYS D NZ  1 
ATOM   4234 N N   . SER D 4 169 ? 21.97162  -10.22180 -11.07896 1.000 43.96346  ? 183 SER D N   1 
ATOM   4235 C CA  . SER D 4 169 ? 21.89545  -11.62622 -11.44868 1.000 38.04906  ? 183 SER D CA  1 
ATOM   4236 C C   . SER D 4 169 ? 21.69529  -12.48095 -10.20580 1.000 40.85110  ? 183 SER D C   1 
ATOM   4237 O O   . SER D 4 169 ? 22.20170  -12.16850 -9.12526  1.000 40.61632  ? 183 SER D O   1 
ATOM   4238 C CB  . SER D 4 169 ? 23.14674  -12.08406 -12.20786 1.000 41.58551  ? 183 SER D CB  1 
ATOM   4239 O OG  . SER D 4 169 ? 24.31006  -11.95269 -11.41204 1.000 48.17964  ? 183 SER D OG  1 
ATOM   4240 N N   . ASN D 4 170 ? 20.94145  -13.56114 -10.38072 1.000 40.12179  ? 184 ASN D N   1 
ATOM   4241 C CA  . ASN D 4 170 ? 20.75279  -14.58664 -9.36824  1.000 34.15423  ? 184 ASN D CA  1 
ATOM   4242 C C   . ASN D 4 170 ? 21.81048  -15.67568 -9.52813  1.000 44.48266  ? 184 ASN D C   1 
ATOM   4243 O O   . ASN D 4 170 ? 22.33672  -15.89909 -10.62057 1.000 40.33425  ? 184 ASN D O   1 
ATOM   4244 C CB  . ASN D 4 170 ? 19.35058  -15.19614 -9.47909  1.000 38.77973  ? 184 ASN D CB  1 
ATOM   4245 C CG  . ASN D 4 170 ? 18.25163  -14.20177 -9.14488  1.000 40.87057  ? 184 ASN D CG  1 
ATOM   4246 O OD1 . ASN D 4 170 ? 18.35529  -13.45879 -8.17582  1.000 56.06016  ? 184 ASN D OD1 1 
ATOM   4247 N ND2 . ASN D 4 170 ? 17.19236  -14.18722 -9.94529  1.000 42.07871  ? 184 ASN D ND2 1 
ATOM   4248 N N   . SER D 4 171 ? 22.12716  -16.35066 -8.42451  1.000 42.72359  ? 185 SER D N   1 
ATOM   4249 C CA  . SER D 4 171 ? 23.05121  -17.47544 -8.49155  1.000 42.84742  ? 185 SER D CA  1 
ATOM   4250 C C   . SER D 4 171 ? 22.88088  -18.35235 -7.26271  1.000 41.92780  ? 185 SER D C   1 
ATOM   4251 O O   . SER D 4 171 ? 22.42603  -17.90174 -6.20927  1.000 45.42080  ? 185 SER D O   1 
ATOM   4252 C CB  . SER D 4 171 ? 24.51002  -17.02088 -8.61256  1.000 39.34933  ? 185 SER D CB  1 
ATOM   4253 O OG  . SER D 4 171 ? 24.96898  -16.44741 -7.40558  1.000 43.30635  ? 185 SER D OG  1 
ATOM   4254 N N   . ALA D 4 172 ? 23.25193  -19.62012 -7.42410  1.000 43.16898  ? 186 ALA D N   1 
ATOM   4255 C CA  . ALA D 4 172 ? 23.29094  -20.58680 -6.33888  1.000 43.38001  ? 186 ALA D CA  1 
ATOM   4256 C C   . ALA D 4 172 ? 24.52644  -21.45344 -6.52061  1.000 42.40239  ? 186 ALA D C   1 
ATOM   4257 O O   . ALA D 4 172 ? 24.92316  -21.74564 -7.65120  1.000 51.82513  ? 186 ALA D O   1 
ATOM   4258 C CB  . ALA D 4 172 ? 22.02538  -21.45575 -6.30319  1.000 37.79876  ? 186 ALA D CB  1 
ATOM   4259 N N   . VAL D 4 173 ? 25.13815  -21.85299 -5.41178  1.000 37.46533  ? 187 VAL D N   1 
ATOM   4260 C CA  . VAL D 4 173 ? 26.38068  -22.61346 -5.43006  1.000 43.40698  ? 187 VAL D CA  1 
ATOM   4261 C C   . VAL D 4 173 ? 26.10329  -24.00552 -4.88324  1.000 44.80357  ? 187 VAL D C   1 
ATOM   4262 O O   . VAL D 4 173 ? 25.34368  -24.16825 -3.92133  1.000 47.50459  ? 187 VAL D O   1 
ATOM   4263 C CB  . VAL D 4 173 ? 27.48528  -21.90364 -4.61875  1.000 47.05143  ? 187 VAL D CB  1 
ATOM   4264 C CG1 . VAL D 4 173 ? 28.79885  -22.67290 -4.69426  1.000 48.66876  ? 187 VAL D CG1 1 
ATOM   4265 C CG2 . VAL D 4 173 ? 27.67116  -20.47025 -5.10928  1.000 38.22300  ? 187 VAL D CG2 1 
ATOM   4266 N N   . ALA D 4 174 ? 26.70306  -25.01072 -5.51077  1.000 47.87925  ? 188 ALA D N   1 
ATOM   4267 C CA  . ALA D 4 174 ? 26.60980  -26.38024 -5.03510  1.000 45.21279  ? 188 ALA D CA  1 
ATOM   4268 C C   . ALA D 4 174 ? 27.98158  -27.02660 -5.11131  1.000 51.55047  ? 188 ALA D C   1 
ATOM   4269 O O   . ALA D 4 174 ? 28.73468  -26.78787 -6.05973  1.000 52.65974  ? 188 ALA D O   1 
ATOM   4270 C CB  . ALA D 4 174 ? 25.60318  -27.19990 -5.84871  1.000 47.66095  ? 188 ALA D CB  1 
ATOM   4271 N N   . TRP D 4 175 ? 28.30305  -27.83842 -4.10692  1.000 47.14077  ? 189 TRP D N   1 
ATOM   4272 C CA  . TRP D 4 175 ? 29.54110  -28.60144 -4.11345  1.000 56.85512  ? 189 TRP D CA  1 
ATOM   4273 C C   . TRP D 4 175 ? 29.31608  -29.90955 -3.36900  1.000 59.01402  ? 189 TRP D C   1 
ATOM   4274 O O   . TRP D 4 175 ? 28.26589  -30.13150 -2.75972  1.000 53.58787  ? 189 TRP D O   1 
ATOM   4275 C CB  . TRP D 4 175 ? 30.69039  -27.81106 -3.48775  1.000 53.02990  ? 189 TRP D CB  1 
ATOM   4276 C CG  . TRP D 4 175 ? 30.52813  -27.64265 -2.02737  1.000 49.13326  ? 189 TRP D CG  1 
ATOM   4277 C CD1 . TRP D 4 175 ? 31.09483  -28.40252 -1.04985  1.000 55.97484  ? 189 TRP D CD1 1 
ATOM   4278 C CD2 . TRP D 4 175 ? 29.72675  -26.66184 -1.36292  1.000 54.76771  ? 189 TRP D CD2 1 
ATOM   4279 N NE1 . TRP D 4 175 ? 30.70491  -27.95012 0.18687   1.000 57.58330  ? 189 TRP D NE1 1 
ATOM   4280 C CE2 . TRP D 4 175 ? 29.86343  -26.88140 0.02212   1.000 56.52878  ? 189 TRP D CE2 1 
ATOM   4281 C CE3 . TRP D 4 175 ? 28.91135  -25.61492 -1.80335  1.000 51.47043  ? 189 TRP D CE3 1 
ATOM   4282 C CZ2 . TRP D 4 175 ? 29.21495  -26.09393 0.97099   1.000 44.46604  ? 189 TRP D CZ2 1 
ATOM   4283 C CZ3 . TRP D 4 175 ? 28.26789  -24.83370 -0.85772  1.000 46.83400  ? 189 TRP D CZ3 1 
ATOM   4284 C CH2 . TRP D 4 175 ? 28.42355  -25.07891 0.51184   1.000 52.89930  ? 189 TRP D CH2 1 
ATOM   4285 N N   . SER D 4 176 ? 30.32514  -30.77557 -3.42460  1.000 61.80081  ? 190 SER D N   1 
ATOM   4286 C CA  . SER D 4 176 ? 30.26900  -32.09160 -2.80337  1.000 68.96388  ? 190 SER D CA  1 
ATOM   4287 C C   . SER D 4 176 ? 31.67210  -32.67285 -2.72842  1.000 67.97027  ? 190 SER D C   1 
ATOM   4288 O O   . SER D 4 176 ? 32.53215  -32.36184 -3.55769  1.000 62.83426  ? 190 SER D O   1 
ATOM   4289 C CB  . SER D 4 176 ? 29.35434  -33.04287 -3.57867  1.000 69.78247  ? 190 SER D CB  1 
ATOM   4290 O OG  . SER D 4 176 ? 29.70831  -34.39025 -3.32121  1.000 77.89291  ? 190 SER D OG  1 
ATOM   4291 N N   . ASN D 4 177 ? 31.88712  -33.52599 -1.72697  1.000 74.74110  ? 191 ASN D N   1 
ATOM   4292 C CA  . ASN D 4 177 ? 33.13391  -34.26889 -1.60642  1.000 69.43666  ? 191 ASN D CA  1 
ATOM   4293 C C   . ASN D 4 177 ? 33.11584  -35.57940 -2.38018  1.000 78.11010  ? 191 ASN D C   1 
ATOM   4294 O O   . ASN D 4 177 ? 34.18460  -36.14133 -2.64475  1.000 80.52274  ? 191 ASN D O   1 
ATOM   4295 C CB  . ASN D 4 177 ? 33.43972  -34.55526 -0.13277  1.000 61.89931  ? 191 ASN D CB  1 
ATOM   4296 N N   . LYS D 4 178 ? 31.93485  -36.07018 -2.74996  1.000 76.48097  ? 192 LYS D N   1 
ATOM   4297 C CA  . LYS D 4 178 ? 31.82837  -37.33237 -3.46787  1.000 81.02151  ? 192 LYS D CA  1 
ATOM   4298 C C   . LYS D 4 178 ? 32.41248  -37.20664 -4.86994  1.000 85.50712  ? 192 LYS D C   1 
ATOM   4299 O O   . LYS D 4 178 ? 32.17810  -36.22025 -5.57341  1.000 86.34398  ? 192 LYS D O   1 
ATOM   4300 C CB  . LYS D 4 178 ? 30.36681  -37.77583 -3.54337  1.000 62.86378  ? 192 LYS D CB  1 
ATOM   4301 N N   . SER D 4 179 ? 33.18021  -38.22262 -5.27355  1.000 87.31546  ? 193 SER D N   1 
ATOM   4302 C CA  . SER D 4 179 ? 33.82162  -38.21397 -6.58307  1.000 83.83250  ? 193 SER D CA  1 
ATOM   4303 C C   . SER D 4 179 ? 32.83340  -38.44435 -7.72162  1.000 85.92424  ? 193 SER D C   1 
ATOM   4304 O O   . SER D 4 179 ? 33.10345  -38.02662 -8.85391  1.000 80.87422  ? 193 SER D O   1 
ATOM   4305 C CB  . SER D 4 179 ? 34.92924  -39.26920 -6.62575  1.000 75.14997  ? 193 SER D CB  1 
ATOM   4306 N N   . ASP D 4 180 ? 31.70362  -39.09748 -7.45302  1.000 79.80879  ? 194 ASP D N   1 
ATOM   4307 C CA  . ASP D 4 180 ? 30.67275  -39.30006 -8.46391  1.000 89.93237  ? 194 ASP D CA  1 
ATOM   4308 C C   . ASP D 4 180 ? 29.85713  -38.04254 -8.73434  1.000 92.42304  ? 194 ASP D C   1 
ATOM   4309 O O   . ASP D 4 180 ? 28.98005  -38.06579 -9.60518  1.000 87.88523  ? 194 ASP D O   1 
ATOM   4310 C CB  . ASP D 4 180 ? 29.73608  -40.43835 -8.04321  1.000 80.03747  ? 194 ASP D CB  1 
ATOM   4311 N N   . PHE D 4 181 ? 30.12661  -36.95496 -8.01710  1.000 101.12204 ? 195 PHE D N   1 
ATOM   4312 C CA  . PHE D 4 181 ? 29.36010  -35.72534 -8.15835  1.000 92.01831  ? 195 PHE D CA  1 
ATOM   4313 C C   . PHE D 4 181 ? 29.79876  -34.96635 -9.40453  1.000 76.06509  ? 195 PHE D C   1 
ATOM   4314 O O   . PHE D 4 181 ? 30.99555  -34.75517 -9.62520  1.000 82.59240  ? 195 PHE D O   1 
ATOM   4315 C CB  . PHE D 4 181 ? 29.53499  -34.85928 -6.90979  1.000 88.21587  ? 195 PHE D CB  1 
ATOM   4316 C CG  . PHE D 4 181 ? 29.00943  -33.45831 -7.05315  1.000 74.80509  ? 195 PHE D CG  1 
ATOM   4317 C CD1 . PHE D 4 181 ? 27.65918  -33.18883 -6.90244  1.000 70.12063  ? 195 PHE D CD1 1 
ATOM   4318 C CD2 . PHE D 4 181 ? 29.87318  -32.40616 -7.31295  1.000 75.89513  ? 195 PHE D CD2 1 
ATOM   4319 C CE1 . PHE D 4 181 ? 27.17978  -31.89886 -7.02350  1.000 74.13772  ? 195 PHE D CE1 1 
ATOM   4320 C CE2 . PHE D 4 181 ? 29.40068  -31.11722 -7.43449  1.000 63.25306  ? 195 PHE D CE2 1 
ATOM   4321 C CZ  . PHE D 4 181 ? 28.05274  -30.86228 -7.28910  1.000 65.88561  ? 195 PHE D CZ  1 
ATOM   4322 N N   . ALA D 4 182 ? 28.82504  -34.55700 -10.21655 1.000 73.14878  ? 196 ALA D N   1 
ATOM   4323 C CA  . ALA D 4 182 ? 29.07622  -33.77033 -11.41470 1.000 76.86091  ? 196 ALA D CA  1 
ATOM   4324 C C   . ALA D 4 182 ? 28.07671  -32.62640 -11.47667 1.000 74.98956  ? 196 ALA D C   1 
ATOM   4325 O O   . ALA D 4 182 ? 26.93724  -32.75491 -11.02107 1.000 76.09537  ? 196 ALA D O   1 
ATOM   4326 C CB  . ALA D 4 182 ? 28.97836  -34.62050 -12.68601 1.000 72.44214  ? 196 ALA D CB  1 
ATOM   4327 N N   . CYS D 4 183 ? 28.51241  -31.50392 -12.05668 1.000 72.69906  ? 197 CYS D N   1 
ATOM   4328 C CA  . CYS D 4 183 ? 27.65239  -30.32568 -12.11340 1.000 70.77120  ? 197 CYS D CA  1 
ATOM   4329 C C   . CYS D 4 183 ? 26.39420  -30.57973 -12.93410 1.000 82.74756  ? 197 CYS D C   1 
ATOM   4330 O O   . CYS D 4 183 ? 25.37522  -29.91201 -12.72288 1.000 79.26382  ? 197 CYS D O   1 
ATOM   4331 C CB  . CYS D 4 183 ? 28.41962  -29.13003 -12.67965 1.000 61.26817  ? 197 CYS D CB  1 
ATOM   4332 S SG  . CYS D 4 183 ? 29.74681  -28.51540 -11.61233 1.000 79.63745  ? 197 CYS D SG  1 
ATOM   4333 N N   . ALA D 4 184 ? 26.43817  -31.53555 -13.86774 1.000 84.60341  ? 198 ALA D N   1 
ATOM   4334 C CA  . ALA D 4 184 ? 25.24445  -31.85479 -14.64512 1.000 80.08262  ? 198 ALA D CA  1 
ATOM   4335 C C   . ALA D 4 184 ? 24.13128  -32.38498 -13.75060 1.000 83.51585  ? 198 ALA D C   1 
ATOM   4336 O O   . ALA D 4 184 ? 22.95313  -32.07300 -13.96238 1.000 78.56891  ? 198 ALA D O   1 
ATOM   4337 C CB  . ALA D 4 184 ? 25.58319  -32.86428 -15.73959 1.000 79.82721  ? 198 ALA D CB  1 
ATOM   4338 N N   . ASN D 4 185 ? 24.48660  -33.17824 -12.73917 1.000 92.81507  ? 199 ASN D N   1 
ATOM   4339 C CA  . ASN D 4 185 ? 23.52784  -33.73123 -11.79284 1.000 92.70321  ? 199 ASN D CA  1 
ATOM   4340 C C   . ASN D 4 185 ? 23.38796  -32.89137 -10.52974 1.000 88.22087  ? 199 ASN D C   1 
ATOM   4341 O O   . ASN D 4 185 ? 22.60400  -33.25371 -9.64685  1.000 89.87732  ? 199 ASN D O   1 
ATOM   4342 C CB  . ASN D 4 185 ? 23.92599  -35.16324 -11.41431 1.000 77.03135  ? 199 ASN D CB  1 
ATOM   4343 N N   . ALA D 4 186 ? 24.11777  -31.77843 -10.42485 1.000 90.74941  ? 200 ALA D N   1 
ATOM   4344 C CA  . ALA D 4 186 ? 24.13764  -31.01052 -9.18295  1.000 88.28945  ? 200 ALA D CA  1 
ATOM   4345 C C   . ALA D 4 186 ? 22.76783  -30.41764 -8.87739  1.000 80.64890  ? 200 ALA D C   1 
ATOM   4346 O O   . ALA D 4 186 ? 22.16540  -30.71094 -7.83839  1.000 78.31151  ? 200 ALA D O   1 
ATOM   4347 C CB  . ALA D 4 186 ? 25.19812  -29.91193 -9.26525  1.000 78.79736  ? 200 ALA D CB  1 
ATOM   4348 N N   . PHE D 4 187 ? 22.25965  -29.57617 -9.77748  1.000 79.52306  ? 201 PHE D N   1 
ATOM   4349 C CA  . PHE D 4 187 ? 20.97482  -28.90750 -9.58730  1.000 80.22814  ? 201 PHE D CA  1 
ATOM   4350 C C   . PHE D 4 187 ? 19.89869  -29.71846 -10.30287 1.000 99.20444  ? 201 PHE D C   1 
ATOM   4351 O O   . PHE D 4 187 ? 19.42029  -29.36414 -11.38127 1.000 101.53747 ? 201 PHE D O   1 
ATOM   4352 C CB  . PHE D 4 187 ? 21.03973  -27.47230 -10.09592 1.000 72.23782  ? 201 PHE D CB  1 
ATOM   4353 C CG  . PHE D 4 187 ? 22.11732  -26.65456 -9.45064  1.000 69.42534  ? 201 PHE D CG  1 
ATOM   4354 C CD1 . PHE D 4 187 ? 21.86908  -25.96643 -8.27793  1.000 66.78546  ? 201 PHE D CD1 1 
ATOM   4355 C CD2 . PHE D 4 187 ? 23.38124  -26.58106 -10.01129 1.000 72.54387  ? 201 PHE D CD2 1 
ATOM   4356 C CE1 . PHE D 4 187 ? 22.85860  -25.21375 -7.67617  1.000 53.44401  ? 201 PHE D CE1 1 
ATOM   4357 C CE2 . PHE D 4 187 ? 24.37667  -25.83121 -9.41464  1.000 70.22197  ? 201 PHE D CE2 1 
ATOM   4358 C CZ  . PHE D 4 187 ? 24.11363  -25.14548 -8.24580  1.000 63.66451  ? 201 PHE D CZ  1 
ATOM   4359 N N   . ASN D 4 188 ? 19.51622  -30.83277 -9.68065  1.000 104.23560 ? 202 ASN D N   1 
ATOM   4360 C CA  . ASN D 4 188 ? 18.47435  -31.69706 -10.21690 1.000 100.63749 ? 202 ASN D CA  1 
ATOM   4361 C C   . ASN D 4 188 ? 17.17976  -31.65372 -9.42265  1.000 104.30690 ? 202 ASN D C   1 
ATOM   4362 O O   . ASN D 4 188 ? 16.10937  -31.84854 -10.00349 1.000 108.53499 ? 202 ASN D O   1 
ATOM   4363 C CB  . ASN D 4 188 ? 18.97180  -33.14520 -10.29086 1.000 102.76927 ? 202 ASN D CB  1 
ATOM   4364 C CG  . ASN D 4 188 ? 19.86283  -33.39129 -11.49422 1.000 104.28362 ? 202 ASN D CG  1 
ATOM   4365 O OD1 . ASN D 4 188 ? 20.14632  -32.47469 -12.26946 1.000 97.31712  ? 202 ASN D OD1 1 
ATOM   4366 N ND2 . ASN D 4 188 ? 20.31176  -34.63190 -11.65584 1.000 104.96612 ? 202 ASN D ND2 1 
ATOM   4367 N N   . ASN D 4 189 ? 17.24928  -31.40970 -8.11151  1.000 103.34198 ? 203 ASN D N   1 
ATOM   4368 C CA  . ASN D 4 189 ? 16.03342  -31.21899 -7.32931  1.000 100.88645 ? 203 ASN D CA  1 
ATOM   4369 C C   . ASN D 4 189 ? 15.49620  -29.80305 -7.48898  1.000 99.21010  ? 203 ASN D C   1 
ATOM   4370 O O   . ASN D 4 189 ? 14.27837  -29.59550 -7.50315  1.000 91.37028  ? 203 ASN D O   1 
ATOM   4371 C CB  . ASN D 4 189 ? 16.29737  -31.53115 -5.85613  1.000 89.96287  ? 203 ASN D CB  1 
ATOM   4372 N N   . SER D 4 190 ? 16.38522  -28.82417 -7.61860  1.000 91.02529  ? 204 SER D N   1 
ATOM   4373 C CA  . SER D 4 190 ? 15.98037  -27.44438 -7.85519  1.000 86.42832  ? 204 SER D CA  1 
ATOM   4374 C C   . SER D 4 190 ? 15.51040  -27.25776 -9.29592  1.000 103.77152 ? 204 SER D C   1 
ATOM   4375 O O   . SER D 4 190 ? 15.89895  -28.01206 -10.19027 1.000 105.60259 ? 204 SER D O   1 
ATOM   4376 C CB  . SER D 4 190 ? 17.13204  -26.48753 -7.54833  1.000 73.68043  ? 204 SER D CB  1 
ATOM   4377 N N   . ILE D 4 192 ? 14.59703  -26.72439 -12.38802 1.000 97.56453  ? 206 ILE D N   1 
ATOM   4378 C CA  . ILE D 4 192 ? 15.58949  -26.27746 -13.35857 1.000 89.67816  ? 206 ILE D CA  1 
ATOM   4379 C C   . ILE D 4 192 ? 14.89977  -25.93085 -14.66820 1.000 88.14819  ? 206 ILE D C   1 
ATOM   4380 O O   . ILE D 4 192 ? 13.91922  -26.57516 -15.04540 1.000 95.44378  ? 206 ILE D O   1 
ATOM   4381 C CB  . ILE D 4 192 ? 16.67861  -27.33982 -13.57768 1.000 75.45501  ? 206 ILE D CB  1 
ATOM   4382 N N   . PRO D 4 193 ? 15.40196  -24.91477 -15.36361 1.000 87.76567  ? 207 PRO D N   1 
ATOM   4383 C CA  . PRO D 4 193 ? 14.79524  -24.53359 -16.64193 1.000 89.24817  ? 207 PRO D CA  1 
ATOM   4384 C C   . PRO D 4 193 ? 15.34142  -25.36391 -17.79154 1.000 88.98410  ? 207 PRO D C   1 
ATOM   4385 O O   . PRO D 4 193 ? 16.50256  -25.77990 -17.79859 1.000 86.66784  ? 207 PRO D O   1 
ATOM   4386 C CB  . PRO D 4 193 ? 15.18158  -23.05669 -16.79116 1.000 81.86426  ? 207 PRO D CB  1 
ATOM   4387 N N   . GLU D 4 194 ? 14.47290  -25.60365 -18.77683 1.000 92.30325  ? 208 GLU D N   1 
ATOM   4388 C CA  . GLU D 4 194 ? 14.85272  -26.38708 -19.94634 1.000 81.17561  ? 208 GLU D CA  1 
ATOM   4389 C C   . GLU D 4 194 ? 15.83627  -25.65676 -20.85209 1.000 70.91666  ? 208 GLU D C   1 
ATOM   4390 O O   . GLU D 4 194 ? 16.39282  -26.27781 -21.76408 1.000 78.74613  ? 208 GLU D O   1 
ATOM   4391 C CB  . GLU D 4 194 ? 13.60601  -26.77681 -20.74133 1.000 89.49284  ? 208 GLU D CB  1 
ATOM   4392 N N   . ASP D 4 195 ? 16.06181  -24.36582 -20.62806 1.000 76.83203  ? 209 ASP D N   1 
ATOM   4393 C CA  . ASP D 4 195 ? 17.02855  -23.59576 -21.39443 1.000 82.24500  ? 209 ASP D CA  1 
ATOM   4394 C C   . ASP D 4 195 ? 18.37735  -23.48710 -20.69581 1.000 80.23305  ? 209 ASP D C   1 
ATOM   4395 O O   . ASP D 4 195 ? 19.24886  -22.75294 -21.17306 1.000 84.72934  ? 209 ASP D O   1 
ATOM   4396 C CB  . ASP D 4 195 ? 16.47788  -22.19555 -21.67791 1.000 78.37487  ? 209 ASP D CB  1 
ATOM   4397 N N   . THR D 4 196 ? 18.56990  -24.20310 -19.58851 1.000 79.12517  ? 210 THR D N   1 
ATOM   4398 C CA  . THR D 4 196 ? 19.80305  -24.08616 -18.82059 1.000 80.41081  ? 210 THR D CA  1 
ATOM   4399 C C   . THR D 4 196 ? 20.98549  -24.62266 -19.61754 1.000 71.12958  ? 210 THR D C   1 
ATOM   4400 O O   . THR D 4 196 ? 20.95431  -25.74979 -20.11834 1.000 77.75275  ? 210 THR D O   1 
ATOM   4401 C CB  . THR D 4 196 ? 19.68091  -24.82761 -17.48806 1.000 69.48407  ? 210 THR D CB  1 
ATOM   4402 O OG1 . THR D 4 196 ? 18.60230  -24.26997 -16.72640 1.000 69.75727  ? 210 THR D OG1 1 
ATOM   4403 C CG2 . THR D 4 196 ? 20.96702  -24.69419 -16.68751 1.000 64.42580  ? 210 THR D CG2 1 
ATOM   4404 N N   . PHE D 4 197 ? 22.03192  -23.80865 -19.71915 1.000 66.28912  ? 211 PHE D N   1 
ATOM   4405 C CA  . PHE D 4 197 ? 23.22218  -24.12926 -20.49455 1.000 66.83719  ? 211 PHE D CA  1 
ATOM   4406 C C   . PHE D 4 197 ? 24.20126  -24.94620 -19.65514 1.000 78.31667  ? 211 PHE D C   1 
ATOM   4407 O O   . PHE D 4 197 ? 24.55652  -24.54832 -18.53955 1.000 77.03753  ? 211 PHE D O   1 
ATOM   4408 C CB  . PHE D 4 197 ? 23.87575  -22.83534 -20.98517 1.000 64.83019  ? 211 PHE D CB  1 
ATOM   4409 C CG  . PHE D 4 197 ? 25.16201  -23.04125 -21.71904 1.000 71.39082  ? 211 PHE D CG  1 
ATOM   4410 C CD1 . PHE D 4 197 ? 25.25294  -23.98324 -22.73125 1.000 75.50922  ? 211 PHE D CD1 1 
ATOM   4411 C CD2 . PHE D 4 197 ? 26.27426  -22.27501 -21.41615 1.000 65.99835  ? 211 PHE D CD2 1 
ATOM   4412 C CE1 . PHE D 4 197 ? 26.43618  -24.17034 -23.41584 1.000 75.28314  ? 211 PHE D CE1 1 
ATOM   4413 C CE2 . PHE D 4 197 ? 27.46178  -22.45421 -22.09659 1.000 75.36925  ? 211 PHE D CE2 1 
ATOM   4414 C CZ  . PHE D 4 197 ? 27.54242  -23.40417 -23.10118 1.000 85.11583  ? 211 PHE D CZ  1 
ATOM   4415 N N   . PHE D 4 198 ? 24.63502  -26.09034 -20.19788 1.000 80.21865  ? 212 PHE D N   1 
ATOM   4416 C CA  . PHE D 4 198 ? 25.56913  -27.00190 -19.53688 1.000 76.30097  ? 212 PHE D CA  1 
ATOM   4417 C C   . PHE D 4 198 ? 26.80852  -27.14833 -20.41271 1.000 83.37942  ? 212 PHE D C   1 
ATOM   4418 O O   . PHE D 4 198 ? 26.95193  -28.14404 -21.13914 1.000 84.42102  ? 212 PHE D O   1 
ATOM   4419 C CB  . PHE D 4 198 ? 24.93225  -28.36706 -19.27927 1.000 74.74782  ? 212 PHE D CB  1 
ATOM   4420 C CG  . PHE D 4 198 ? 23.94915  -28.38145 -18.14318 1.000 80.51137  ? 212 PHE D CG  1 
ATOM   4421 C CD1 . PHE D 4 198 ? 22.62334  -28.04110 -18.34909 1.000 79.56568  ? 212 PHE D CD1 1 
ATOM   4422 C CD2 . PHE D 4 198 ? 24.35003  -28.75163 -16.86963 1.000 77.55351  ? 212 PHE D CD2 1 
ATOM   4423 C CE1 . PHE D 4 198 ? 21.71782  -28.06145 -17.30428 1.000 76.49337  ? 212 PHE D CE1 1 
ATOM   4424 C CE2 . PHE D 4 198 ? 23.44867  -28.77288 -15.82070 1.000 73.57062  ? 212 PHE D CE2 1 
ATOM   4425 C CZ  . PHE D 4 198 ? 22.13155  -28.42643 -16.03841 1.000 73.10097  ? 212 PHE D CZ  1 
ATOM   4426 N N   . PRO D 4 199 ? 27.73240  -26.17662 -20.36959 1.000 80.43765  ? 213 PRO D N   1 
ATOM   4427 C CA  . PRO D 4 199 ? 28.96073  -26.23407 -21.17125 1.000 79.88092  ? 213 PRO D CA  1 
ATOM   4428 C C   . PRO D 4 199 ? 29.85920  -27.41376 -20.80718 1.000 85.48800  ? 213 PRO D C   1 
ATOM   4429 O O   . PRO D 4 199 ? 30.68885  -27.80376 -21.62911 1.000 90.78641  ? 213 PRO D O   1 
ATOM   4430 C CB  . PRO D 4 199 ? 29.65416  -24.90763 -20.84566 1.000 80.12259  ? 213 PRO D CB  1 
ATOM   4431 C CG  . PRO D 4 199 ? 29.07966  -24.48229 -19.53720 1.000 73.88972  ? 213 PRO D CG  1 
ATOM   4432 C CD  . PRO D 4 199 ? 27.66383  -24.95435 -19.55173 1.000 70.57123  ? 213 PRO D CD  1 
ATOM   4433 N N   . GLY E 5 2   ? 28.03101  5.84399   16.63437  1.000 63.56734  ? 3   GLY E N   1 
ATOM   4434 C CA  . GLY E 5 2   ? 26.81829  5.69241   17.41702  1.000 42.42758  ? 3   GLY E CA  1 
ATOM   4435 C C   . GLY E 5 2   ? 27.01657  4.95862   18.73146  1.000 47.21288  ? 3   GLY E C   1 
ATOM   4436 O O   . GLY E 5 2   ? 27.86101  5.33112   19.54712  1.000 48.12172  ? 3   GLY E O   1 
ATOM   4437 N N   . VAL E 5 3   ? 26.22868  3.91181   18.93970  1.000 41.77567  ? 4   VAL E N   1 
ATOM   4438 C CA  . VAL E 5 3   ? 26.28493  3.12310   20.16408  1.000 34.59777  ? 4   VAL E CA  1 
ATOM   4439 C C   . VAL E 5 3   ? 27.35798  2.05250   20.00662  1.000 26.79582  ? 4   VAL E C   1 
ATOM   4440 O O   . VAL E 5 3   ? 27.42694  1.37209   18.97699  1.000 38.76895  ? 4   VAL E O   1 
ATOM   4441 C CB  . VAL E 5 3   ? 24.91214  2.50239   20.47484  1.000 31.84963  ? 4   VAL E CB  1 
ATOM   4442 C CG1 . VAL E 5 3   ? 24.97800  1.64775   21.71641  1.000 25.62553  ? 4   VAL E CG1 1 
ATOM   4443 C CG2 . VAL E 5 3   ? 23.87689  3.59340   20.64787  1.000 24.85236  ? 4   VAL E CG2 1 
ATOM   4444 N N   . THR E 5 4   ? 28.20168  1.90706   21.02209  1.000 28.62130  ? 5   THR E N   1 
ATOM   4445 C CA  . THR E 5 4   ? 29.32796  0.98098   20.99295  1.000 37.93013  ? 5   THR E CA  1 
ATOM   4446 C C   . THR E 5 4   ? 29.09259  -0.13827  21.99908  1.000 32.64814  ? 5   THR E C   1 
ATOM   4447 O O   . THR E 5 4   ? 28.95656  0.12517   23.19971  1.000 27.53890  ? 5   THR E O   1 
ATOM   4448 C CB  . THR E 5 4   ? 30.63404  1.70897   21.30934  1.000 37.78266  ? 5   THR E CB  1 
ATOM   4449 O OG1 . THR E 5 4   ? 30.81231  2.79230   20.38947  1.000 49.39528  ? 5   THR E OG1 1 
ATOM   4450 C CG2 . THR E 5 4   ? 31.81252  0.75723   21.19913  1.000 45.56156  ? 5   THR E CG2 1 
ATOM   4451 N N   . GLN E 5 5   ? 29.06156  -1.37949  21.51381  1.000 26.45320  ? 6   GLN E N   1 
ATOM   4452 C CA  . GLN E 5 5   ? 28.91993  -2.55743  22.36051  1.000 28.74775  ? 6   GLN E CA  1 
ATOM   4453 C C   . GLN E 5 5   ? 30.16239  -3.43260  22.26902  1.000 26.70475  ? 6   GLN E C   1 
ATOM   4454 O O   . GLN E 5 5   ? 30.69447  -3.65851  21.17849  1.000 30.49114  ? 6   GLN E O   1 
ATOM   4455 C CB  . GLN E 5 5   ? 27.69198  -3.37958  21.96767  1.000 23.50118  ? 6   GLN E CB  1 
ATOM   4456 C CG  . GLN E 5 5   ? 26.38205  -2.68622  22.24271  1.000 22.96776  ? 6   GLN E CG  1 
ATOM   4457 C CD  . GLN E 5 5   ? 25.19667  -3.60457  22.06192  1.000 22.38778  ? 6   GLN E CD  1 
ATOM   4458 O OE1 . GLN E 5 5   ? 24.36719  -3.39436  21.18220  1.000 25.36917  ? 6   GLN E OE1 1 
ATOM   4459 N NE2 . GLN E 5 5   ? 25.11096  -4.63737  22.89597  1.000 21.57771  ? 6   GLN E NE2 1 
ATOM   4460 N N   . THR E 5 6   ? 30.62017  -3.92612  23.41639  1.000 27.03316  ? 7   THR E N   1 
ATOM   4461 C CA  . THR E 5 6   ? 31.73462  -4.86043  23.48620  1.000 33.92685  ? 7   THR E CA  1 
ATOM   4462 C C   . THR E 5 6   ? 31.43335  -5.91397  24.54112  1.000 29.75303  ? 7   THR E C   1 
ATOM   4463 O O   . THR E 5 6   ? 30.70514  -5.63886  25.50178  1.000 31.44657  ? 7   THR E O   1 
ATOM   4464 C CB  . THR E 5 6   ? 33.06658  -4.16943  23.83324  1.000 37.25805  ? 7   THR E CB  1 
ATOM   4465 O OG1 . THR E 5 6   ? 32.94611  -3.49224  25.09015  1.000 31.09690  ? 7   THR E OG1 1 
ATOM   4466 C CG2 . THR E 5 6   ? 33.47892  -3.17852  22.74673  1.000 33.19106  ? 7   THR E CG2 1 
ATOM   4467 N N   . PRO E 5 7   ? 31.94710  -7.14530  24.37014  1.000 36.66594  ? 8   PRO E N   1 
ATOM   4468 C CA  . PRO E 5 7   ? 32.59151  -7.60727  23.13476  1.000 25.61427  ? 8   PRO E CA  1 
ATOM   4469 C C   . PRO E 5 7   ? 31.54963  -7.83749  22.05060  1.000 34.70888  ? 8   PRO E C   1 
ATOM   4470 O O   . PRO E 5 7   ? 30.37674  -8.01528  22.38222  1.000 27.07391  ? 8   PRO E O   1 
ATOM   4471 C CB  . PRO E 5 7   ? 33.26168  -8.92105  23.54951  1.000 23.42413  ? 8   PRO E CB  1 
ATOM   4472 C CG  . PRO E 5 7   ? 32.45286  -9.40257  24.70930  1.000 33.14874  ? 8   PRO E CG  1 
ATOM   4473 C CD  . PRO E 5 7   ? 31.98758  -8.16804  25.43244  1.000 26.70631  ? 8   PRO E CD  1 
ATOM   4474 N N   . ARG E 5 8   ? 31.96061  -7.80947  20.78154  1.000 28.11784  ? 9   ARG E N   1 
ATOM   4475 C CA  . ARG E 5 8   ? 31.00238  -7.99206  19.69683  1.000 31.48938  ? 9   ARG E CA  1 
ATOM   4476 C C   . ARG E 5 8   ? 30.62674  -9.45632  19.52087  1.000 28.53471  ? 9   ARG E C   1 
ATOM   4477 O O   . ARG E 5 8   ? 29.48424  -9.76352  19.16604  1.000 30.43821  ? 9   ARG E O   1 
ATOM   4478 C CB  . ARG E 5 8   ? 31.57154  -7.41579  18.39890  1.000 28.30443  ? 9   ARG E CB  1 
ATOM   4479 C CG  . ARG E 5 8   ? 31.86242  -5.91773  18.49808  1.000 43.38375  ? 9   ARG E CG  1 
ATOM   4480 C CD  . ARG E 5 8   ? 32.69993  -5.39836  17.33767  1.000 48.24318  ? 9   ARG E CD  1 
ATOM   4481 N NE  . ARG E 5 8   ? 32.05928  -5.61634  16.04615  1.000 52.83432  ? 9   ARG E NE  1 
ATOM   4482 C CZ  . ARG E 5 8   ? 32.51085  -6.44640  15.11451  1.000 63.27844  ? 9   ARG E CZ  1 
ATOM   4483 N NH1 . ARG E 5 8   ? 33.62652  -7.13761  15.28612  1.000 48.46868  ? 9   ARG E NH1 1 
ATOM   4484 N NH2 . ARG E 5 8   ? 31.82964  -6.58044  13.97884  1.000 46.78225  ? 9   ARG E NH2 1 
ATOM   4485 N N   . TYR E 5 9   ? 31.56510  -10.36031 19.77212  1.000 24.78026  ? 10  TYR E N   1 
ATOM   4486 C CA  . TYR E 5 9   ? 31.33487  -11.79204 19.70842  1.000 26.92176  ? 10  TYR E CA  1 
ATOM   4487 C C   . TYR E 5 9   ? 31.98301  -12.43685 20.91704  1.000 23.74320  ? 10  TYR E C   1 
ATOM   4488 O O   . TYR E 5 9   ? 33.01491  -11.97025 21.40741  1.000 29.68848  ? 10  TYR E O   1 
ATOM   4489 C CB  . TYR E 5 9   ? 31.92218  -12.41715 18.44539  1.000 25.28616  ? 10  TYR E CB  1 
ATOM   4490 C CG  . TYR E 5 9   ? 31.31479  -11.93395 17.15428  1.000 28.01653  ? 10  TYR E CG  1 
ATOM   4491 C CD1 . TYR E 5 9   ? 31.67683  -10.70952 16.60726  1.000 28.45466  ? 10  TYR E CD1 1 
ATOM   4492 C CD2 . TYR E 5 9   ? 30.39915  -12.71630 16.46539  1.000 26.43114  ? 10  TYR E CD2 1 
ATOM   4493 C CE1 . TYR E 5 9   ? 31.12659  -10.26893 15.42117  1.000 35.34620  ? 10  TYR E CE1 1 
ATOM   4494 C CE2 . TYR E 5 9   ? 29.84927  -12.28728 15.27419  1.000 31.95415  ? 10  TYR E CE2 1 
ATOM   4495 C CZ  . TYR E 5 9   ? 30.21807  -11.06413 14.75623  1.000 31.01562  ? 10  TYR E CZ  1 
ATOM   4496 O OH  . TYR E 5 9   ? 29.67777  -10.63049 13.57038  1.000 47.05938  ? 10  TYR E OH  1 
ATOM   4497 N N   . LEU E 5 10  ? 31.38480  -13.52647 21.38269  1.000 29.75242  ? 11  LEU E N   1 
ATOM   4498 C CA  . LEU E 5 10  ? 31.87639  -14.16835 22.59237  1.000 28.28649  ? 11  LEU E CA  1 
ATOM   4499 C C   . LEU E 5 10  ? 31.37494  -15.60008 22.63001  1.000 27.51911  ? 11  LEU E C   1 
ATOM   4500 O O   . LEU E 5 10  ? 30.19460  -15.85420 22.36836  1.000 29.48248  ? 11  LEU E O   1 
ATOM   4501 C CB  . LEU E 5 10  ? 31.41580  -13.39458 23.83498  1.000 21.64930  ? 11  LEU E CB  1 
ATOM   4502 C CG  . LEU E 5 10  ? 32.10678  -13.67785 25.17117  1.000 43.35413  ? 11  LEU E CG  1 
ATOM   4503 C CD1 . LEU E 5 10  ? 33.62590  -13.72513 25.02757  1.000 32.32720  ? 11  LEU E CD1 1 
ATOM   4504 C CD2 . LEU E 5 10  ? 31.70887  -12.60946 26.16465  1.000 39.54559  ? 11  LEU E CD2 1 
ATOM   4505 N N   . ILE E 5 11  ? 32.27172  -16.52797 22.94185  1.000 29.12498  ? 12  ILE E N   1 
ATOM   4506 C CA  . ILE E 5 11  ? 31.91558  -17.91779 23.19444  1.000 30.98971  ? 12  ILE E CA  1 
ATOM   4507 C C   . ILE E 5 11  ? 32.13695  -18.18281 24.67706  1.000 25.87519  ? 12  ILE E C   1 
ATOM   4508 O O   . ILE E 5 11  ? 33.24421  -17.98132 25.19020  1.000 26.97388  ? 12  ILE E O   1 
ATOM   4509 C CB  . ILE E 5 11  ? 32.73914  -18.88262 22.32930  1.000 29.56612  ? 12  ILE E CB  1 
ATOM   4510 C CG1 . ILE E 5 11  ? 32.55532  -18.56641 20.84247  1.000 35.91500  ? 12  ILE E CG1 1 
ATOM   4511 C CG2 . ILE E 5 11  ? 32.35071  -20.31974 22.63022  1.000 23.29677  ? 12  ILE E CG2 1 
ATOM   4512 C CD1 . ILE E 5 11  ? 33.54630  -19.27661 19.94133  1.000 33.71230  ? 12  ILE E CD1 1 
ATOM   4513 N N   . LYS E 5 12  ? 31.08804  -18.61160 25.36949  1.000 26.84620  ? 13  LYS E N   1 
ATOM   4514 C CA  . LYS E 5 12  ? 31.19329  -19.03306 26.75780  1.000 20.54833  ? 13  LYS E CA  1 
ATOM   4515 C C   . LYS E 5 12  ? 30.67474  -20.45929 26.87842  1.000 25.35926  ? 13  LYS E C   1 
ATOM   4516 O O   . LYS E 5 12  ? 30.03597  -20.98610 25.96680  1.000 25.80118  ? 13  LYS E O   1 
ATOM   4517 C CB  . LYS E 5 12  ? 30.40877  -18.10039 27.69404  1.000 27.39390  ? 13  LYS E CB  1 
ATOM   4518 C CG  . LYS E 5 12  ? 30.74701  -16.61722 27.57234  1.000 30.55231  ? 13  LYS E CG  1 
ATOM   4519 C CD  . LYS E 5 12  ? 32.19946  -16.33276 27.92249  1.000 28.57365  ? 13  LYS E CD  1 
ATOM   4520 C CE  . LYS E 5 12  ? 32.44311  -16.40988 29.41663  1.000 31.55672  ? 13  LYS E CE  1 
ATOM   4521 N NZ  . LYS E 5 12  ? 33.83766  -16.02141 29.75659  1.000 38.41461  ? 13  LYS E NZ  1 
ATOM   4522 N N   . THR E 5 13  ? 30.95009  -21.09907 28.01232  1.000 30.90604  ? 14  THR E N   1 
ATOM   4523 C CA  . THR E 5 13  ? 30.36635  -22.40377 28.28676  1.000 27.29181  ? 14  THR E CA  1 
ATOM   4524 C C   . THR E 5 13  ? 29.28434  -22.28632 29.35276  1.000 27.98991  ? 14  THR E C   1 
ATOM   4525 O O   . THR E 5 13  ? 29.21561  -21.30953 30.10496  1.000 33.73492  ? 14  THR E O   1 
ATOM   4526 C CB  . THR E 5 13  ? 31.42230  -23.43544 28.71881  1.000 33.60821  ? 14  THR E CB  1 
ATOM   4527 O OG1 . THR E 5 13  ? 32.09799  -22.99070 29.90044  1.000 36.18134  ? 14  THR E OG1 1 
ATOM   4528 C CG2 . THR E 5 13  ? 32.43528  -23.66058 27.60843  1.000 36.35686  ? 14  THR E CG2 1 
ATOM   4529 N N   . ARG E 5 14  ? 28.42412  -23.29879 29.39547  1.000 29.77948  ? 15  ARG E N   1 
ATOM   4530 C CA  . ARG E 5 14  ? 27.34877  -23.33274 30.37477  1.000 31.51780  ? 15  ARG E CA  1 
ATOM   4531 C C   . ARG E 5 14  ? 27.91177  -23.28681 31.79170  1.000 26.15183  ? 15  ARG E C   1 
ATOM   4532 O O   . ARG E 5 14  ? 28.87701  -23.98218 32.11650  1.000 32.01841  ? 15  ARG E O   1 
ATOM   4533 C CB  . ARG E 5 14  ? 26.50743  -24.58974 30.16487  1.000 30.57450  ? 15  ARG E CB  1 
ATOM   4534 C CG  . ARG E 5 14  ? 25.39740  -24.77519 31.17545  1.000 32.92726  ? 15  ARG E CG  1 
ATOM   4535 C CD  . ARG E 5 14  ? 24.72971  -26.11616 30.97334  1.000 53.52832  ? 15  ARG E CD  1 
ATOM   4536 N NE  . ARG E 5 14  ? 25.70120  -27.19740 31.07399  1.000 56.04264  ? 15  ARG E NE  1 
ATOM   4537 C CZ  . ARG E 5 14  ? 25.98818  -27.84379 32.19377  1.000 72.04654  ? 15  ARG E CZ  1 
ATOM   4538 N NH1 . ARG E 5 14  ? 25.37717  -27.55832 33.33046  1.000 64.24808  ? 15  ARG E NH1 1 
ATOM   4539 N NH2 . ARG E 5 14  ? 26.90664  -28.80458 32.17027  1.000 70.19331  ? 15  ARG E NH2 1 
ATOM   4540 N N   . GLY E 5 15  ? 27.31119  -22.44850 32.62947  1.000 26.10780  ? 16  GLY E N   1 
ATOM   4541 C CA  . GLY E 5 15  ? 27.77389  -22.24895 33.98298  1.000 25.13712  ? 16  GLY E CA  1 
ATOM   4542 C C   . GLY E 5 15  ? 28.72760  -21.08656 34.17117  1.000 27.64721  ? 16  GLY E C   1 
ATOM   4543 O O   . GLY E 5 15  ? 28.98253  -20.69336 35.31585  1.000 33.04704  ? 16  GLY E O   1 
ATOM   4544 N N   . GLN E 5 16  ? 29.26045  -20.52314 33.09199  1.000 26.61422  ? 17  GLN E N   1 
ATOM   4545 C CA  . GLN E 5 16  ? 30.18337  -19.40657 33.20650  1.000 31.07033  ? 17  GLN E CA  1 
ATOM   4546 C C   . GLN E 5 16  ? 29.42681  -18.08279 33.31441  1.000 26.90073  ? 17  GLN E C   1 
ATOM   4547 O O   . GLN E 5 16  ? 28.22107  -17.99512 33.07324  1.000 27.65456  ? 17  GLN E O   1 
ATOM   4548 C CB  . GLN E 5 16  ? 31.13668  -19.37507 32.01528  1.000 25.38209  ? 17  GLN E CB  1 
ATOM   4549 C CG  . GLN E 5 16  ? 32.13664  -20.51617 31.98823  1.000 28.13923  ? 17  GLN E CG  1 
ATOM   4550 C CD  . GLN E 5 16  ? 33.16380  -20.33965 30.88879  1.000 31.16980  ? 17  GLN E CD  1 
ATOM   4551 O OE1 . GLN E 5 16  ? 32.86021  -19.80457 29.81903  1.000 28.43985  ? 17  GLN E OE1 1 
ATOM   4552 N NE2 . GLN E 5 16  ? 34.39006  -20.77262 31.15056  1.000 34.51527  ? 17  GLN E NE2 1 
ATOM   4553 N N   . GLN E 5 17  ? 30.15646  -17.04119 33.68744  1.000 25.39853  ? 18  GLN E N   1 
ATOM   4554 C CA  . GLN E 5 17  ? 29.61384  -15.70034 33.80641  1.000 32.61899  ? 18  GLN E CA  1 
ATOM   4555 C C   . GLN E 5 17  ? 30.11771  -14.83965 32.65836  1.000 32.80948  ? 18  GLN E C   1 
ATOM   4556 O O   . GLN E 5 17  ? 31.17404  -15.09970 32.07580  1.000 28.41069  ? 18  GLN E O   1 
ATOM   4557 C CB  . GLN E 5 17  ? 30.01008  -15.06664 35.13920  1.000 26.43129  ? 18  GLN E CB  1 
ATOM   4558 C CG  . GLN E 5 17  ? 31.50597  -14.95809 35.30389  1.000 42.35924  ? 18  GLN E CG  1 
ATOM   4559 C CD  . GLN E 5 17  ? 31.89672  -14.25593 36.58060  1.000 54.37626  ? 18  GLN E CD  1 
ATOM   4560 O OE1 . GLN E 5 17  ? 31.06311  -13.62289 37.23642  1.000 62.07134  ? 18  GLN E OE1 1 
ATOM   4561 N NE2 . GLN E 5 17  ? 33.17030  -14.36289 36.94618  1.000 49.79994  ? 18  GLN E NE2 1 
ATOM   4562 N N   . VAL E 5 18  ? 29.35501  -13.79138 32.35448  1.000 22.96908  ? 19  VAL E N   1 
ATOM   4563 C CA  . VAL E 5 18  ? 29.67769  -12.89628 31.25589  1.000 23.48798  ? 19  VAL E CA  1 
ATOM   4564 C C   . VAL E 5 18  ? 29.23118  -11.49248 31.62980  1.000 23.78981  ? 19  VAL E C   1 
ATOM   4565 O O   . VAL E 5 18  ? 28.23828  -11.30643 32.33603  1.000 26.34381  ? 19  VAL E O   1 
ATOM   4566 C CB  . VAL E 5 18  ? 29.01093  -13.37130 29.94296  1.000 27.30217  ? 19  VAL E CB  1 
ATOM   4567 C CG1 . VAL E 5 18  ? 27.48074  -13.28821 30.04933  1.000 22.71288  ? 19  VAL E CG1 1 
ATOM   4568 C CG2 . VAL E 5 18  ? 29.51342  -12.57093 28.77968  1.000 23.40397  ? 19  VAL E CG2 1 
ATOM   4569 N N   . THR E 5 19  ? 29.97666  -10.49953 31.15029  1.000 23.60547  ? 20  THR E N   1 
ATOM   4570 C CA  . THR E 5 19  ? 29.64339  -9.09421  31.34293  1.000 18.65760  ? 20  THR E CA  1 
ATOM   4571 C C   . THR E 5 19  ? 29.76091  -8.37594  30.00773  1.000 20.04067  ? 20  THR E C   1 
ATOM   4572 O O   . THR E 5 19  ? 30.82657  -8.38380  29.38371  1.000 24.60994  ? 20  THR E O   1 
ATOM   4573 C CB  . THR E 5 19  ? 30.55492  -8.44607  32.38828  1.000 30.09420  ? 20  THR E CB  1 
ATOM   4574 O OG1 . THR E 5 19  ? 30.40707  -9.13596  33.63475  1.000 36.30584  ? 20  THR E OG1 1 
ATOM   4575 C CG2 . THR E 5 19  ? 30.19043  -6.97254  32.58923  1.000 19.45144  ? 20  THR E CG2 1 
ATOM   4576 N N   . LEU E 5 20  ? 28.66695  -7.76981  29.56787  1.000 27.84965  ? 21  LEU E N   1 
ATOM   4577 C CA  . LEU E 5 20  ? 28.61936  -7.02852  28.32000  1.000 29.47656  ? 21  LEU E CA  1 
ATOM   4578 C C   . LEU E 5 20  ? 28.57335  -5.53580  28.61931  1.000 29.34004  ? 21  LEU E C   1 
ATOM   4579 O O   . LEU E 5 20  ? 27.97746  -5.10594  29.60829  1.000 26.42219  ? 21  LEU E O   1 
ATOM   4580 C CB  . LEU E 5 20  ? 27.39811  -7.43605  27.49292  1.000 21.44755  ? 21  LEU E CB  1 
ATOM   4581 C CG  . LEU E 5 20  ? 27.20715  -8.93763  27.27246  1.000 24.15032  ? 21  LEU E CG  1 
ATOM   4582 C CD1 . LEU E 5 20  ? 25.92122  -9.18519  26.49619  1.000 15.82066  ? 21  LEU E CD1 1 
ATOM   4583 C CD2 . LEU E 5 20  ? 28.39615  -9.55435  26.54771  1.000 23.09010  ? 21  LEU E CD2 1 
ATOM   4584 N N   . SER E 5 21  ? 29.19906  -4.74251  27.75849  1.000 27.94596  ? 22  SER E N   1 
ATOM   4585 C CA  . SER E 5 21  ? 29.30075  -3.31054  27.98193  1.000 30.44094  ? 22  SER E CA  1 
ATOM   4586 C C   . SER E 5 21  ? 28.66674  -2.54739  26.82673  1.000 31.66565  ? 22  SER E C   1 
ATOM   4587 O O   . SER E 5 21  ? 28.68086  -2.99693  25.67591  1.000 26.31828  ? 22  SER E O   1 
ATOM   4588 C CB  . SER E 5 21  ? 30.76184  -2.88249  28.16516  1.000 32.39429  ? 22  SER E CB  1 
ATOM   4589 O OG  . SER E 5 21  ? 30.84065  -1.52651  28.57419  1.000 39.94955  ? 22  SER E OG  1 
ATOM   4590 N N   . CYS E 5 22  ? 28.11160  -1.38052  27.15136  1.000 30.21880  ? 23  CYS E N   1 
ATOM   4591 C CA  . CYS E 5 22  ? 27.40682  -0.54425  26.18729  1.000 29.28411  ? 23  CYS E CA  1 
ATOM   4592 C C   . CYS E 5 22  ? 27.73365  0.90882   26.48610  1.000 37.33140  ? 23  CYS E C   1 
ATOM   4593 O O   . CYS E 5 22  ? 27.47443  1.38766   27.59461  1.000 34.86548  ? 23  CYS E O   1 
ATOM   4594 C CB  . CYS E 5 22  ? 25.89222  -0.78630  26.25921  1.000 33.74413  ? 23  CYS E CB  1 
ATOM   4595 S SG  . CYS E 5 22  ? 24.82562  0.32667   25.27300  1.000 32.44705  ? 23  CYS E SG  1 
ATOM   4596 N N   . SER E 5 23  ? 28.30848  1.60542   25.50747  1.000 31.11081  ? 24  SER E N   1 
ATOM   4597 C CA  . SER E 5 23  ? 28.49499  3.04357   25.62032  1.000 32.90336  ? 24  SER E CA  1 
ATOM   4598 C C   . SER E 5 23  ? 27.43326  3.73970   24.78436  1.000 32.44274  ? 24  SER E C   1 
ATOM   4599 O O   . SER E 5 23  ? 27.45374  3.62253   23.54800  1.000 26.22035  ? 24  SER E O   1 
ATOM   4600 C CB  . SER E 5 23  ? 29.89231  3.45692   25.16590  1.000 29.00548  ? 24  SER E CB  1 
ATOM   4601 O OG  . SER E 5 23  ? 30.86657  3.00636   26.08905  1.000 38.29892  ? 24  SER E OG  1 
ATOM   4602 N N   . PRO E 5 24  ? 26.49812  4.46026   25.39299  1.000 24.18664  ? 25  PRO E N   1 
ATOM   4603 C CA  . PRO E 5 24  ? 25.41203  5.06633   24.62082  1.000 24.89695  ? 25  PRO E CA  1 
ATOM   4604 C C   . PRO E 5 24  ? 25.92006  6.21957   23.76999  1.000 23.80695  ? 25  PRO E C   1 
ATOM   4605 O O   . PRO E 5 24  ? 27.07105  6.65092   23.86610  1.000 27.42350  ? 25  PRO E O   1 
ATOM   4606 C CB  . PRO E 5 24  ? 24.44541  5.54898   25.70573  1.000 18.27386  ? 25  PRO E CB  1 
ATOM   4607 C CG  . PRO E 5 24  ? 25.32451  5.84547   26.86420  1.000 25.48469  ? 25  PRO E CG  1 
ATOM   4608 C CD  . PRO E 5 24  ? 26.42465  4.81500   26.82123  1.000 23.74860  ? 25  PRO E CD  1 
ATOM   4609 N N   . ILE E 5 25  ? 25.02919  6.71227   22.90712  1.000 25.26063  ? 26  ILE E N   1 
ATOM   4610 C CA  . ILE E 5 25  ? 25.32265  7.92210   22.15383  1.000 25.78776  ? 26  ILE E CA  1 
ATOM   4611 C C   . ILE E 5 25  ? 25.62425  9.04750   23.13090  1.000 28.30473  ? 26  ILE E C   1 
ATOM   4612 O O   . ILE E 5 25  ? 24.95441  9.19842   24.16079  1.000 37.44121  ? 26  ILE E O   1 
ATOM   4613 C CB  . ILE E 5 25  ? 24.15030  8.26241   21.21741  1.000 32.68247  ? 26  ILE E CB  1 
ATOM   4614 C CG1 . ILE E 5 25  ? 24.16723  7.32296   20.00566  1.000 36.72335  ? 26  ILE E CG1 1 
ATOM   4615 C CG2 . ILE E 5 25  ? 24.19644  9.72856   20.78289  1.000 24.43068  ? 26  ILE E CG2 1 
ATOM   4616 C CD1 . ILE E 5 25  ? 22.95438  7.42843   19.12209  1.000 27.71980  ? 26  ILE E CD1 1 
ATOM   4617 N N   . SER E 5 26  ? 26.67119  9.81339   22.83267  1.000 27.20791  ? 27  SER E N   1 
ATOM   4618 C CA  . SER E 5 26  ? 27.13978  10.87113  23.72099  1.000 32.02176  ? 27  SER E CA  1 
ATOM   4619 C C   . SER E 5 26  ? 26.00885  11.82408  24.07138  1.000 28.09763  ? 27  SER E C   1 
ATOM   4620 O O   . SER E 5 26  ? 25.37249  12.39835  23.18525  1.000 35.88172  ? 27  SER E O   1 
ATOM   4621 C CB  . SER E 5 26  ? 28.29044  11.63143  23.05625  1.000 32.03671  ? 27  SER E CB  1 
ATOM   4622 O OG  . SER E 5 26  ? 28.86449  12.57095  23.94422  1.000 40.13008  ? 27  SER E OG  1 
ATOM   4623 N N   . GLY E 5 27  ? 25.75544  11.98276  25.36996  1.000 29.78161  ? 28  GLY E N   1 
ATOM   4624 C CA  . GLY E 5 27  ? 24.67538  12.80273  25.86009  1.000 26.67909  ? 28  GLY E CA  1 
ATOM   4625 C C   . GLY E 5 27  ? 23.41249  12.03949  26.20283  1.000 28.05492  ? 28  GLY E C   1 
ATOM   4626 O O   . GLY E 5 27  ? 22.56755  12.56733  26.93277  1.000 36.17559  ? 28  GLY E O   1 
ATOM   4627 N N   . HIS E 5 28  ? 23.25641  10.82127  25.69514  1.000 28.54092  ? 29  HIS E N   1 
ATOM   4628 C CA  . HIS E 5 28  ? 22.09878  10.01696  26.05456  1.000 22.80057  ? 29  HIS E CA  1 
ATOM   4629 C C   . HIS E 5 28  ? 22.21982  9.52948   27.49168  1.000 27.31225  ? 29  HIS E C   1 
ATOM   4630 O O   . HIS E 5 28  ? 23.31583  9.21868   27.96878  1.000 30.05523  ? 29  HIS E O   1 
ATOM   4631 C CB  . HIS E 5 28  ? 21.95319  8.83243   25.10134  1.000 23.80907  ? 29  HIS E CB  1 
ATOM   4632 C CG  . HIS E 5 28  ? 21.33913  9.19405   23.78439  1.000 30.91944  ? 29  HIS E CG  1 
ATOM   4633 N ND1 . HIS E 5 28  ? 20.72983  8.26627   22.96460  1.000 28.27482  ? 29  HIS E ND1 1 
ATOM   4634 C CD2 . HIS E 5 28  ? 21.23528  10.38535  23.14707  1.000 30.75715  ? 29  HIS E CD2 1 
ATOM   4635 C CE1 . HIS E 5 28  ? 20.27968  8.87031   21.87816  1.000 31.88261  ? 29  HIS E CE1 1 
ATOM   4636 N NE2 . HIS E 5 28  ? 20.57394  10.15633  21.96302  1.000 24.30798  ? 29  HIS E NE2 1 
ATOM   4637 N N   . ARG E 5 29  ? 21.08129  9.46655   28.18911  1.000 28.26029  ? 37  ARG E N   1 
ATOM   4638 C CA  . ARG E 5 29  ? 21.07301  9.05729   29.58568  1.000 28.24010  ? 37  ARG E CA  1 
ATOM   4639 C C   . ARG E 5 29  ? 20.35410  7.74089   29.83949  1.000 23.80631  ? 37  ARG E C   1 
ATOM   4640 O O   . ARG E 5 29  ? 20.56099  7.13757   30.89560  1.000 28.88880  ? 37  ARG E O   1 
ATOM   4641 C CB  . ARG E 5 29  ? 20.44757  10.15678  30.45885  1.000 25.87361  ? 37  ARG E CB  1 
ATOM   4642 C CG  . ARG E 5 29  ? 21.26235  11.45708  30.47631  1.000 33.14047  ? 37  ARG E CG  1 
ATOM   4643 C CD  . ARG E 5 29  ? 21.27097  12.13537  31.84988  1.000 54.19805  ? 37  ARG E CD  1 
ATOM   4644 N NE  . ARG E 5 29  ? 22.18253  11.49532  32.79591  1.000 69.59707  ? 37  ARG E NE  1 
ATOM   4645 C CZ  . ARG E 5 29  ? 23.44131  11.86534  33.00458  1.000 77.11912  ? 37  ARG E CZ  1 
ATOM   4646 N NH1 . ARG E 5 29  ? 23.98739  12.87245  32.34165  1.000 77.47521  ? 37  ARG E NH1 1 
ATOM   4647 N NH2 . ARG E 5 29  ? 24.17123  11.20881  33.90315  1.000 79.20541  ? 37  ARG E NH2 1 
ATOM   4648 N N   . SER E 5 30  ? 19.54237  7.26966   28.90358  1.000 28.07972  ? 38  SER E N   1 
ATOM   4649 C CA  . SER E 5 30  ? 18.78928  6.03331   29.06377  1.000 29.09848  ? 38  SER E CA  1 
ATOM   4650 C C   . SER E 5 30  ? 19.42251  4.94019   28.21176  1.000 28.53493  ? 38  SER E C   1 
ATOM   4651 O O   . SER E 5 30  ? 19.58840  5.11122   27.00135  1.000 28.42996  ? 38  SER E O   1 
ATOM   4652 C CB  . SER E 5 30  ? 17.32431  6.23642   28.67804  1.000 25.79373  ? 38  SER E CB  1 
ATOM   4653 O OG  . SER E 5 30  ? 16.62565  5.00579   28.65998  1.000 26.48576  ? 38  SER E OG  1 
ATOM   4654 N N   . VAL E 5 31  ? 19.77467  3.82506   28.84590  1.000 27.01335  ? 39  VAL E N   1 
ATOM   4655 C CA  . VAL E 5 31  ? 20.28797  2.64313   28.16640  1.000 21.78752  ? 39  VAL E CA  1 
ATOM   4656 C C   . VAL E 5 31  ? 19.33819  1.48451   28.44191  1.000 31.93747  ? 39  VAL E C   1 
ATOM   4657 O O   . VAL E 5 31  ? 19.00504  1.20564   29.60251  1.000 24.90862  ? 39  VAL E O   1 
ATOM   4658 C CB  . VAL E 5 31  ? 21.71747  2.29511   28.62495  1.000 31.81773  ? 39  VAL E CB  1 
ATOM   4659 C CG1 . VAL E 5 31  ? 22.17776  1.00240   27.97816  1.000 30.35625  ? 39  VAL E CG1 1 
ATOM   4660 C CG2 . VAL E 5 31  ? 22.67508  3.41658   28.29225  1.000 24.64102  ? 39  VAL E CG2 1 
ATOM   4661 N N   . SER E 5 32  ? 18.90093  0.81740   27.37787  1.000 29.77925  ? 40  SER E N   1 
ATOM   4662 C CA  . SER E 5 32  ? 18.05351  -0.36000  27.47608  1.000 25.20793  ? 40  SER E CA  1 
ATOM   4663 C C   . SER E 5 32  ? 18.81100  -1.56370  26.93892  1.000 25.00739  ? 40  SER E C   1 
ATOM   4664 O O   . SER E 5 32  ? 19.65276  -1.43279  26.04792  1.000 21.40809  ? 40  SER E O   1 
ATOM   4665 C CB  . SER E 5 32  ? 16.74115  -0.18042  26.68712  1.000 23.29334  ? 40  SER E CB  1 
ATOM   4666 O OG  . SER E 5 32  ? 15.98626  0.92119   27.15778  1.000 30.65991  ? 40  SER E OG  1 
ATOM   4667 N N   . TRP E 5 33  ? 18.50839  -2.73929  27.48059  1.000 27.38170  ? 41  TRP E N   1 
ATOM   4668 C CA  . TRP E 5 33  ? 19.07177  -3.98926  26.98955  1.000 20.53117  ? 41  TRP E CA  1 
ATOM   4669 C C   . TRP E 5 33  ? 17.95010  -4.87277  26.46661  1.000 24.04724  ? 41  TRP E C   1 
ATOM   4670 O O   . TRP E 5 33  ? 16.90313  -5.00698  27.11048  1.000 24.27421  ? 41  TRP E O   1 
ATOM   4671 C CB  . TRP E 5 33  ? 19.84924  -4.72415  28.08014  1.000 21.12297  ? 41  TRP E CB  1 
ATOM   4672 C CG  . TRP E 5 33  ? 21.15979  -4.08867  28.45508  1.000 26.08561  ? 41  TRP E CG  1 
ATOM   4673 C CD1 . TRP E 5 33  ? 21.37891  -3.19509  29.46071  1.000 19.09503  ? 41  TRP E CD1 1 
ATOM   4674 C CD2 . TRP E 5 33  ? 22.43283  -4.31736  27.83813  1.000 19.17051  ? 41  TRP E CD2 1 
ATOM   4675 N NE1 . TRP E 5 33  ? 22.70571  -2.84923  29.50756  1.000 27.16151  ? 41  TRP E NE1 1 
ATOM   4676 C CE2 . TRP E 5 33  ? 23.37587  -3.52789  28.52301  1.000 25.60636  ? 41  TRP E CE2 1 
ATOM   4677 C CE3 . TRP E 5 33  ? 22.86629  -5.11212  26.77140  1.000 22.87911  ? 41  TRP E CE3 1 
ATOM   4678 C CZ2 . TRP E 5 33  ? 24.72769  -3.50811  28.17665  1.000 22.47629  ? 41  TRP E CZ2 1 
ATOM   4679 C CZ3 . TRP E 5 33  ? 24.21231  -5.09106  26.42902  1.000 24.29894  ? 41  TRP E CZ3 1 
ATOM   4680 C CH2 . TRP E 5 33  ? 25.12486  -4.29357  27.13042  1.000 21.53260  ? 41  TRP E CH2 1 
ATOM   4681 N N   . TYR E 5 34  ? 18.17270  -5.46855  25.30255  1.000 18.72162  ? 42  TYR E N   1 
ATOM   4682 C CA  . TYR E 5 34  ? 17.23087  -6.39384  24.70403  1.000 23.14729  ? 42  TYR E CA  1 
ATOM   4683 C C   . TYR E 5 34  ? 17.95750  -7.67040  24.31900  1.000 23.12102  ? 42  TYR E C   1 
ATOM   4684 O O   . TYR E 5 34  ? 19.14737  -7.65521  23.98998  1.000 22.42657  ? 42  TYR E O   1 
ATOM   4685 C CB  . TYR E 5 34  ? 16.54874  -5.78686  23.46662  1.000 21.56585  ? 42  TYR E CB  1 
ATOM   4686 C CG  . TYR E 5 34  ? 15.54388  -4.70973  23.79038  1.000 24.34187  ? 42  TYR E CG  1 
ATOM   4687 C CD1 . TYR E 5 34  ? 15.94782  -3.40251  24.02581  1.000 23.09315  ? 42  TYR E CD1 1 
ATOM   4688 C CD2 . TYR E 5 34  ? 14.18880  -5.00123  23.86323  1.000 22.23907  ? 42  TYR E CD2 1 
ATOM   4689 C CE1 . TYR E 5 34  ? 15.02705  -2.41497  24.33116  1.000 17.10272  ? 42  TYR E CE1 1 
ATOM   4690 C CE2 . TYR E 5 34  ? 13.26556  -4.02499  24.16775  1.000 17.32791  ? 42  TYR E CE2 1 
ATOM   4691 C CZ  . TYR E 5 34  ? 13.68690  -2.73203  24.40066  1.000 19.34739  ? 42  TYR E CZ  1 
ATOM   4692 O OH  . TYR E 5 34  ? 12.75863  -1.75678  24.69881  1.000 18.40021  ? 42  TYR E OH  1 
ATOM   4693 N N   . GLN E 5 35  ? 17.22837  -8.77661  24.36616  1.000 22.13866  ? 43  GLN E N   1 
ATOM   4694 C CA  . GLN E 5 35  ? 17.72008  -10.06241 23.89942  1.000 20.67833  ? 43  GLN E CA  1 
ATOM   4695 C C   . GLN E 5 35  ? 17.01208  -10.41272 22.59871  1.000 27.18984  ? 43  GLN E C   1 
ATOM   4696 O O   . GLN E 5 35  ? 15.77945  -10.33262 22.51309  1.000 26.87195  ? 43  GLN E O   1 
ATOM   4697 C CB  . GLN E 5 35  ? 17.48900  -11.15543 24.94182  1.000 25.70558  ? 43  GLN E CB  1 
ATOM   4698 C CG  . GLN E 5 35  ? 18.10866  -12.48708 24.58200  1.000 24.87365  ? 43  GLN E CG  1 
ATOM   4699 C CD  . GLN E 5 35  ? 17.47072  -13.63457 25.33009  1.000 26.17755  ? 43  GLN E CD  1 
ATOM   4700 O OE1 . GLN E 5 35  ? 16.29779  -13.93703 25.12395  1.000 34.75042  ? 43  GLN E OE1 1 
ATOM   4701 N NE2 . GLN E 5 35  ? 18.23476  -14.27395 26.21641  1.000 26.54492  ? 43  GLN E NE2 1 
ATOM   4702 N N   . GLN E 5 36  ? 17.79431  -10.78897 21.59022  1.000 23.53063  ? 44  GLN E N   1 
ATOM   4703 C CA  . GLN E 5 36  ? 17.28808  -11.13463 20.26608  1.000 27.24289  ? 44  GLN E CA  1 
ATOM   4704 C C   . GLN E 5 36  ? 17.60944  -12.59738 19.99464  1.000 33.08202  ? 44  GLN E C   1 
ATOM   4705 O O   . GLN E 5 36  ? 18.78067  -12.96094 19.84141  1.000 35.39170  ? 44  GLN E O   1 
ATOM   4706 C CB  . GLN E 5 36  ? 17.90427  -10.23618 19.19920  1.000 29.86528  ? 44  GLN E CB  1 
ATOM   4707 C CG  . GLN E 5 36  ? 17.66643  -10.71200 17.78240  1.000 43.87611  ? 44  GLN E CG  1 
ATOM   4708 C CD  . GLN E 5 36  ? 16.44783  -10.08101 17.16871  1.000 38.04011  ? 44  GLN E CD  1 
ATOM   4709 O OE1 . GLN E 5 36  ? 16.51483  -8.97287  16.63999  1.000 44.94176  ? 44  GLN E OE1 1 
ATOM   4710 N NE2 . GLN E 5 36  ? 15.31942  -10.77603 17.24051  1.000 41.81878  ? 44  GLN E NE2 1 
ATOM   4711 N N   . THR E 5 37  ? 16.57180  -13.42734 19.93129  1.000 36.66072  ? 45  THR E N   1 
ATOM   4712 C CA  . THR E 5 37  ? 16.64697  -14.83991 19.59977  1.000 44.88023  ? 45  THR E CA  1 
ATOM   4713 C C   . THR E 5 37  ? 15.77650  -15.14685 18.38489  1.000 42.52811  ? 45  THR E C   1 
ATOM   4714 O O   . THR E 5 37  ? 14.77126  -14.47062 18.14795  1.000 44.54851  ? 45  THR E O   1 
ATOM   4715 C CB  . THR E 5 37  ? 16.17793  -15.71413 20.76849  1.000 39.08039  ? 45  THR E CB  1 
ATOM   4716 O OG1 . THR E 5 37  ? 14.81619  -15.39380 21.07434  1.000 47.77283  ? 45  THR E OG1 1 
ATOM   4717 C CG2 . THR E 5 37  ? 17.03411  -15.47516 21.99572  1.000 33.43577  ? 45  THR E CG2 1 
ATOM   4718 N N   . PRO E 5 38  ? 16.12537  -16.16722 17.60393  1.000 56.28463  ? 46  PRO E N   1 
ATOM   4719 C CA  . PRO E 5 38  ? 15.24531  -16.57453 16.50038  1.000 48.57263  ? 46  PRO E CA  1 
ATOM   4720 C C   . PRO E 5 38  ? 13.94895  -17.16365 17.03797  1.000 60.88294  ? 46  PRO E C   1 
ATOM   4721 O O   . PRO E 5 38  ? 13.96237  -18.03716 17.90818  1.000 62.36271  ? 46  PRO E O   1 
ATOM   4722 C CB  . PRO E 5 38  ? 16.07555  -17.62258 15.74931  1.000 51.33141  ? 46  PRO E CB  1 
ATOM   4723 C CG  . PRO E 5 38  ? 17.50029  -17.38483 16.20186  1.000 57.50730  ? 46  PRO E CG  1 
ATOM   4724 C CD  . PRO E 5 38  ? 17.38481  -16.92978 17.61555  1.000 42.89369  ? 46  PRO E CD  1 
ATOM   4725 N N   . GLY E 5 39  ? 12.82366  -16.66787 16.52301  1.000 61.17839  ? 47  GLY E N   1 
ATOM   4726 C CA  . GLY E 5 39  ? 11.51654  -17.18966 16.85579  1.000 67.97069  ? 47  GLY E CA  1 
ATOM   4727 C C   . GLY E 5 39  ? 10.79202  -16.45389 17.96553  1.000 65.23399  ? 47  GLY E C   1 
ATOM   4728 O O   . GLY E 5 39  ? 9.57175   -16.61099 18.10086  1.000 54.68374  ? 47  GLY E O   1 
ATOM   4729 N N   . GLN E 5 40  ? 11.50496  -15.66367 18.76648  1.000 66.49735  ? 48  GLN E N   1 
ATOM   4730 C CA  . GLN E 5 40  ? 10.87760  -14.89053 19.82628  1.000 73.92197  ? 48  GLN E CA  1 
ATOM   4731 C C   . GLN E 5 40  ? 10.87644  -13.39215 19.56954  1.000 71.71440  ? 48  GLN E C   1 
ATOM   4732 O O   . GLN E 5 40  ? 10.04622  -12.68522 20.15081  1.000 72.35976  ? 48  GLN E O   1 
ATOM   4733 C CB  . GLN E 5 40  ? 11.57004  -15.16676 21.16919  1.000 58.76410  ? 48  GLN E CB  1 
ATOM   4734 C CG  . GLN E 5 40  ? 10.87627  -16.21280 22.02809  1.000 65.33422  ? 48  GLN E CG  1 
ATOM   4735 C CD  . GLN E 5 40  ? 9.76316   -15.62091 22.87358  1.000 73.34879  ? 48  GLN E CD  1 
ATOM   4736 O OE1 . GLN E 5 40  ? 8.91077   -14.88577 22.37408  1.000 73.99183  ? 48  GLN E OE1 1 
ATOM   4737 N NE2 . GLN E 5 40  ? 9.77513   -15.92809 24.16712  1.000 72.00276  ? 48  GLN E NE2 1 
ATOM   4738 N N   . GLY E 5 41  ? 11.76359  -12.89530 18.71195  1.000 45.88374  ? 49  GLY E N   1 
ATOM   4739 C CA  . GLY E 5 41  ? 11.86645  -11.46690 18.50697  1.000 51.79135  ? 49  GLY E CA  1 
ATOM   4740 C C   . GLY E 5 41  ? 12.61643  -10.77986 19.63765  1.000 51.16201  ? 49  GLY E C   1 
ATOM   4741 O O   . GLY E 5 41  ? 13.39355  -11.39408 20.38361  1.000 46.63736  ? 49  GLY E O   1 
ATOM   4742 N N   . LEU E 5 42  ? 12.36824  -9.47526  19.76191  1.000 30.95896  ? 50  LEU E N   1 
ATOM   4743 C CA  . LEU E 5 42  ? 13.06254  -8.65310  20.74157  1.000 32.67340  ? 50  LEU E CA  1 
ATOM   4744 C C   . LEU E 5 42  ? 12.39244  -8.76966  22.10571  1.000 34.41402  ? 50  LEU E C   1 
ATOM   4745 O O   . LEU E 5 42  ? 11.18517  -8.53624  22.23868  1.000 33.68747  ? 50  LEU E O   1 
ATOM   4746 C CB  . LEU E 5 42  ? 13.09790  -7.19044  20.29324  1.000 23.55060  ? 50  LEU E CB  1 
ATOM   4747 C CG  . LEU E 5 42  ? 14.36942  -6.68219  19.60207  1.000 29.51636  ? 50  LEU E CG  1 
ATOM   4748 C CD1 . LEU E 5 42  ? 14.51369  -5.17293  19.76299  1.000 30.58948  ? 50  LEU E CD1 1 
ATOM   4749 C CD2 . LEU E 5 42  ? 15.60226  -7.37781  20.14082  1.000 37.91799  ? 50  LEU E CD2 1 
ATOM   4750 N N   . GLN E 5 43  ? 13.18556  -9.12076  23.11867  1.000 22.61753  ? 51  GLN E N   1 
ATOM   4751 C CA  . GLN E 5 43  ? 12.71764  -9.27036  24.49055  1.000 26.00181  ? 51  GLN E CA  1 
ATOM   4752 C C   . GLN E 5 43  ? 13.41049  -8.24626  25.37731  1.000 24.60842  ? 51  GLN E C   1 
ATOM   4753 O O   . GLN E 5 43  ? 14.63725  -8.12516  25.34829  1.000 22.54485  ? 51  GLN E O   1 
ATOM   4754 C CB  . GLN E 5 43  ? 12.98236  -10.68576 25.01198  1.000 29.50540  ? 51  GLN E CB  1 
ATOM   4755 C CG  . GLN E 5 43  ? 12.20470  -11.77232 24.28733  1.000 35.40356  ? 51  GLN E CG  1 
ATOM   4756 C CD  . GLN E 5 43  ? 10.70401  -11.56755 24.37648  1.000 48.07894  ? 51  GLN E CD  1 
ATOM   4757 O OE1 . GLN E 5 43  ? 10.01166  -11.53131 23.35831  1.000 52.71457  ? 51  GLN E OE1 1 
ATOM   4758 N NE2 . GLN E 5 43  ? 10.19230  -11.43244 25.59907  1.000 46.93813  ? 51  GLN E NE2 1 
ATOM   4759 N N   . PHE E 5 44  ? 12.62236  -7.52789  26.17087  1.000 26.53974  ? 52  PHE E N   1 
ATOM   4760 C CA  . PHE E 5 44  ? 13.13103  -6.46897  27.03295  1.000 23.51669  ? 52  PHE E CA  1 
ATOM   4761 C C   . PHE E 5 44  ? 13.77009  -7.05421  28.28740  1.000 24.99723  ? 52  PHE E C   1 
ATOM   4762 O O   . PHE E 5 44  ? 13.14736  -7.85107  28.99725  1.000 24.94082  ? 52  PHE E O   1 
ATOM   4763 C CB  . PHE E 5 44  ? 11.98536  -5.52696  27.41100  1.000 28.99023  ? 52  PHE E CB  1 
ATOM   4764 C CG  . PHE E 5 44  ? 12.39384  -4.36900  28.28629  1.000 24.17517  ? 52  PHE E CG  1 
ATOM   4765 C CD1 . PHE E 5 44  ? 13.32017  -3.43647  27.84380  1.000 21.72429  ? 52  PHE E CD1 1 
ATOM   4766 C CD2 . PHE E 5 44  ? 11.81516  -4.18959  29.53143  1.000 18.82294  ? 52  PHE E CD2 1 
ATOM   4767 C CE1 . PHE E 5 44  ? 13.67568  -2.36259  28.63143  1.000 18.23541  ? 52  PHE E CE1 1 
ATOM   4768 C CE2 . PHE E 5 44  ? 12.16884  -3.11757  30.32683  1.000 18.89445  ? 52  PHE E CE2 1 
ATOM   4769 C CZ  . PHE E 5 44  ? 13.10065  -2.20155  29.87326  1.000 25.22359  ? 52  PHE E CZ  1 
ATOM   4770 N N   . LEU E 5 45  ? 15.01094  -6.65313  28.56420  1.000 20.32396  ? 53  LEU E N   1 
ATOM   4771 C CA  . LEU E 5 45  ? 15.69156  -7.04831  29.80821  1.000 25.60715  ? 53  LEU E CA  1 
ATOM   4772 C C   . LEU E 5 45  ? 15.45540  -6.00187  30.89391  1.000 21.98802  ? 53  LEU E C   1 
ATOM   4773 O O   . LEU E 5 45  ? 14.78789  -6.27136  31.89623  1.000 23.78860  ? 53  LEU E O   1 
ATOM   4774 C CB  . LEU E 5 45  ? 17.18765  -7.25633  29.55886  1.000 23.81378  ? 53  LEU E CB  1 
ATOM   4775 C CG  . LEU E 5 45  ? 17.60543  -8.59690  28.94343  1.000 34.30920  ? 53  LEU E CG  1 
ATOM   4776 C CD1 . LEU E 5 45  ? 18.86640  -8.45367  28.12114  1.000 22.51437  ? 53  LEU E CD1 1 
ATOM   4777 C CD2 . LEU E 5 45  ? 17.82056  -9.62954  30.02976  1.000 26.50401  ? 53  LEU E CD2 1 
ATOM   4778 N N   . PHE E 5 46  ? 15.99492  -4.80210  30.69792  1.000 22.01611  ? 54  PHE E N   1 
ATOM   4779 C CA  . PHE E 5 46  ? 15.85296  -3.71059  31.65056  1.000 22.02267  ? 54  PHE E CA  1 
ATOM   4780 C C   . PHE E 5 46  ? 16.30920  -2.41170  30.99315  1.000 27.50781  ? 54  PHE E C   1 
ATOM   4781 O O   . PHE E 5 46  ? 17.01545  -2.41895  29.97686  1.000 21.54795  ? 54  PHE E O   1 
ATOM   4782 C CB  . PHE E 5 46  ? 16.64485  -3.96987  32.94920  1.000 26.67786  ? 54  PHE E CB  1 
ATOM   4783 C CG  . PHE E 5 46  ? 17.79231  -4.94548  32.79884  1.000 28.85109  ? 54  PHE E CG  1 
ATOM   4784 C CD1 . PHE E 5 46  ? 18.87460  -4.65133  31.97597  1.000 18.16988  ? 54  PHE E CD1 1 
ATOM   4785 C CD2 . PHE E 5 46  ? 17.79860  -6.14608  33.50797  1.000 20.31888  ? 54  PHE E CD2 1 
ATOM   4786 C CE1 . PHE E 5 46  ? 19.93263  -5.53779  31.84397  1.000 23.15082  ? 54  PHE E CE1 1 
ATOM   4787 C CE2 . PHE E 5 46  ? 18.85345  -7.03898  33.38451  1.000 20.99079  ? 54  PHE E CE2 1 
ATOM   4788 C CZ  . PHE E 5 46  ? 19.92537  -6.73457  32.54931  1.000 23.97640  ? 54  PHE E CZ  1 
ATOM   4789 N N   . GLU E 5 47  ? 15.88625  -1.29525  31.59037  1.000 25.51849  ? 55  GLU E N   1 
ATOM   4790 C CA  . GLU E 5 47  ? 16.29457  0.04338   31.18497  1.000 23.23092  ? 55  GLU E CA  1 
ATOM   4791 C C   . GLU E 5 47  ? 16.94944  0.73583   32.37138  1.000 23.76889  ? 55  GLU E C   1 
ATOM   4792 O O   . GLU E 5 47  ? 16.43322  0.67362   33.49024  1.000 34.71818  ? 55  GLU E O   1 
ATOM   4793 C CB  . GLU E 5 47  ? 15.10021  0.87206   30.68216  1.000 25.07803  ? 55  GLU E CB  1 
ATOM   4794 C CG  . GLU E 5 47  ? 15.42196  2.35360   30.44354  1.000 24.87666  ? 55  GLU E CG  1 
ATOM   4795 C CD  . GLU E 5 47  ? 14.20612  3.19276   30.05680  1.000 30.41423  ? 55  GLU E CD  1 
ATOM   4796 O OE1 . GLU E 5 47  ? 13.07626  2.65438   30.02343  1.000 36.95017  ? 55  GLU E OE1 1 
ATOM   4797 O OE2 . GLU E 5 47  ? 14.38555  4.40172   29.78139  1.000 27.51439  ? 55  GLU E OE2 1 
ATOM   4798 N N   . TYR E 5 48  ? 18.07907  1.39202   32.12554  1.000 30.44633  ? 56  TYR E N   1 
ATOM   4799 C CA  . TYR E 5 48  ? 18.79660  2.13370   33.15013  1.000 24.88188  ? 56  TYR E CA  1 
ATOM   4800 C C   . TYR E 5 48  ? 18.76652  3.61815   32.82293  1.000 27.06834  ? 56  TYR E C   1 
ATOM   4801 O O   . TYR E 5 48  ? 18.89973  4.01663   31.66111  1.000 24.61037  ? 56  TYR E O   1 
ATOM   4802 C CB  . TYR E 5 48  ? 20.23524  1.62141   33.29124  1.000 20.92636  ? 56  TYR E CB  1 
ATOM   4803 C CG  . TYR E 5 48  ? 20.23611  0.29540   33.99812  1.000 23.27223  ? 56  TYR E CG  1 
ATOM   4804 C CD1 . TYR E 5 48  ? 19.96835  -0.88124  33.30808  1.000 23.88413  ? 56  TYR E CD1 1 
ATOM   4805 C CD2 . TYR E 5 48  ? 20.42418  0.22308   35.37285  1.000 32.79086  ? 56  TYR E CD2 1 
ATOM   4806 C CE1 . TYR E 5 48  ? 19.92310  -2.10052  33.96472  1.000 29.92575  ? 56  TYR E CE1 1 
ATOM   4807 C CE2 . TYR E 5 48  ? 20.38003  -0.98990  36.03704  1.000 28.81868  ? 56  TYR E CE2 1 
ATOM   4808 C CZ  . TYR E 5 48  ? 20.12635  -2.14712  35.32867  1.000 25.93391  ? 56  TYR E CZ  1 
ATOM   4809 O OH  . TYR E 5 48  ? 20.07869  -3.34620  35.99025  1.000 36.57643  ? 56  TYR E OH  1 
ATOM   4810 N N   . PHE E 5 49  ? 18.55513  4.42493   33.85378  1.000 26.42046  ? 57  PHE E N   1 
ATOM   4811 C CA  . PHE E 5 49  ? 18.47096  5.87053   33.71980  1.000 25.06057  ? 57  PHE E CA  1 
ATOM   4812 C C   . PHE E 5 49  ? 18.94586  6.48281   35.02675  1.000 27.15212  ? 57  PHE E C   1 
ATOM   4813 O O   . PHE E 5 49  ? 18.52049  6.04867   36.10306  1.000 26.45990  ? 57  PHE E O   1 
ATOM   4814 C CB  . PHE E 5 49  ? 17.03720  6.31225   33.39786  1.000 20.91441  ? 57  PHE E CB  1 
ATOM   4815 C CG  . PHE E 5 49  ? 16.87627  7.79953   33.25660  1.000 25.97799  ? 57  PHE E CG  1 
ATOM   4816 C CD1 . PHE E 5 49  ? 17.15747  8.42846   32.05639  1.000 29.59241  ? 57  PHE E CD1 1 
ATOM   4817 C CD2 . PHE E 5 49  ? 16.43559  8.56711   34.32292  1.000 22.41385  ? 57  PHE E CD2 1 
ATOM   4818 C CE1 . PHE E 5 49  ? 17.01044  9.79958   31.92202  1.000 26.51484  ? 57  PHE E CE1 1 
ATOM   4819 C CE2 . PHE E 5 49  ? 16.28526  9.93443   34.19868  1.000 23.01255  ? 57  PHE E CE2 1 
ATOM   4820 C CZ  . PHE E 5 49  ? 16.57274  10.55288  32.99553  1.000 28.39766  ? 57  PHE E CZ  1 
ATOM   4821 N N   . SER E 5 50  ? 19.84110  7.46599   34.93114  1.000 29.71381  ? 58  SER E N   1 
ATOM   4822 C CA  . SER E 5 50  ? 20.36704  8.15934   36.10887  1.000 38.54399  ? 58  SER E CA  1 
ATOM   4823 C C   . SER E 5 50  ? 20.97949  7.17285   37.10598  1.000 29.11099  ? 58  SER E C   1 
ATOM   4824 O O   . SER E 5 50  ? 20.82051  7.30874   38.32160  1.000 40.78238  ? 58  SER E O   1 
ATOM   4825 C CB  . SER E 5 50  ? 19.28095  9.01423   36.76913  1.000 34.78547  ? 58  SER E CB  1 
ATOM   4826 O OG  . SER E 5 50  ? 19.83497  9.89267   37.72969  1.000 59.24528  ? 58  SER E OG  1 
ATOM   4827 N N   . GLU E 5 51  ? 21.66583  6.15768   36.57726  1.000 27.21169  ? 63  GLU E N   1 
ATOM   4828 C CA  . GLU E 5 51  ? 22.44231  5.15525   37.30916  1.000 36.14893  ? 63  GLU E CA  1 
ATOM   4829 C C   . GLU E 5 51  ? 21.59405  4.15685   38.08862  1.000 33.77113  ? 63  GLU E C   1 
ATOM   4830 O O   . GLU E 5 51  ? 22.14496  3.38484   38.88307  1.000 32.97934  ? 63  GLU E O   1 
ATOM   4831 C CB  . GLU E 5 51  ? 23.44815  5.80240   38.26650  1.000 28.81074  ? 63  GLU E CB  1 
ATOM   4832 C CG  . GLU E 5 51  ? 24.41259  6.74759   37.58222  1.000 40.18428  ? 63  GLU E CG  1 
ATOM   4833 C CD  . GLU E 5 51  ? 25.30048  7.48075   38.56934  1.000 66.93882  ? 63  GLU E CD  1 
ATOM   4834 O OE1 . GLU E 5 51  ? 25.94175  6.81229   39.41233  1.000 63.16647  ? 63  GLU E OE1 1 
ATOM   4835 O OE2 . GLU E 5 51  ? 25.34548  8.72847   38.50793  1.000 69.50644  ? 63  GLU E OE2 1 
ATOM   4836 N N   . THR E 5 52  ? 20.27725  4.13850   37.89352  1.000 28.49448  ? 64  THR E N   1 
ATOM   4837 C CA  . THR E 5 52  ? 19.41649  3.17225   38.55961  1.000 32.10652  ? 64  THR E CA  1 
ATOM   4838 C C   . THR E 5 52  ? 18.55034  2.47171   37.52345  1.000 35.01821  ? 64  THR E C   1 
ATOM   4839 O O   . THR E 5 52  ? 18.27911  3.01485   36.44940  1.000 30.04020  ? 64  THR E O   1 
ATOM   4840 C CB  . THR E 5 52  ? 18.51965  3.82980   39.62322  1.000 32.17030  ? 64  THR E CB  1 
ATOM   4841 O OG1 . THR E 5 52  ? 17.50304  4.60174   38.97840  1.000 40.94927  ? 64  THR E OG1 1 
ATOM   4842 C CG2 . THR E 5 52  ? 19.33302  4.74969   40.52282  1.000 38.43822  ? 64  THR E CG2 1 
ATOM   4843 N N   . GLN E 5 53  ? 18.12637  1.25442   37.85173  1.000 22.73797  ? 65  GLN E N   1 
ATOM   4844 C CA  . GLN E 5 53  ? 17.24628  0.50117   36.96819  1.000 32.91413  ? 65  GLN E CA  1 
ATOM   4845 C C   . GLN E 5 53  ? 15.84976  1.10908   36.99409  1.000 24.56002  ? 65  GLN E C   1 
ATOM   4846 O O   . GLN E 5 53  ? 15.20913  1.17481   38.04672  1.000 35.27113  ? 65  GLN E O   1 
ATOM   4847 C CB  . GLN E 5 53  ? 17.19977  -0.96586  37.38351  1.000 21.47912  ? 65  GLN E CB  1 
ATOM   4848 C CG  . GLN E 5 53  ? 16.34901  -1.82809  36.47706  1.000 22.43517  ? 65  GLN E CG  1 
ATOM   4849 C CD  . GLN E 5 53  ? 16.33177  -3.28074  36.91399  1.000 27.63549  ? 65  GLN E CD  1 
ATOM   4850 O OE1 . GLN E 5 53  ? 15.36547  -3.74627  37.51809  1.000 40.96989  ? 65  GLN E OE1 1 
ATOM   4851 N NE2 . GLN E 5 53  ? 17.40664  -4.00362  36.61763  1.000 25.12003  ? 65  GLN E NE2 1 
ATOM   4852 N N   . ARG E 5 54  ? 15.37423  1.55277   35.83682  1.000 29.24375  ? 66  ARG E N   1 
ATOM   4853 C CA  . ARG E 5 54  ? 14.06985  2.19444   35.77771  1.000 33.08268  ? 66  ARG E CA  1 
ATOM   4854 C C   . ARG E 5 54  ? 12.94626  1.18950   35.54781  1.000 26.79087  ? 66  ARG E C   1 
ATOM   4855 O O   . ARG E 5 54  ? 11.94787  1.19755   36.27123  1.000 39.24562  ? 66  ARG E O   1 
ATOM   4856 C CB  . ARG E 5 54  ? 14.06375  3.26155   34.68500  1.000 24.06404  ? 66  ARG E CB  1 
ATOM   4857 C CG  . ARG E 5 54  ? 12.82066  4.09958   34.71140  1.000 29.71150  ? 66  ARG E CG  1 
ATOM   4858 C CD  . ARG E 5 54  ? 12.96104  5.28704   33.81823  1.000 36.18127  ? 66  ARG E CD  1 
ATOM   4859 N NE  . ARG E 5 54  ? 11.76092  6.10992   33.84507  1.000 32.36846  ? 66  ARG E NE  1 
ATOM   4860 C CZ  . ARG E 5 54  ? 11.60574  7.18065   34.60868  1.000 27.50562  ? 66  ARG E CZ  1 
ATOM   4861 N NH1 . ARG E 5 54  ? 12.55438  7.57996   35.43963  1.000 26.01607  ? 66  ARG E NH1 1 
ATOM   4862 N NH2 . ARG E 5 54  ? 10.47493  7.87520   34.52641  1.000 32.42313  ? 66  ARG E NH2 1 
ATOM   4863 N N   . ASN E 5 55  ? 13.09376  0.32584   34.54657  1.000 29.16941  ? 67  ASN E N   1 
ATOM   4864 C CA  . ASN E 5 55  ? 12.12816  -0.72185  34.25521  1.000 27.65499  ? 67  ASN E CA  1 
ATOM   4865 C C   . ASN E 5 55  ? 12.85750  -2.04186  34.06292  1.000 31.28657  ? 67  ASN E C   1 
ATOM   4866 O O   . ASN E 5 55  ? 14.06002  -2.08073  33.78377  1.000 23.78944  ? 67  ASN E O   1 
ATOM   4867 C CB  . ASN E 5 55  ? 11.29350  -0.41265  33.00335  1.000 31.79962  ? 67  ASN E CB  1 
ATOM   4868 C CG  . ASN E 5 55  ? 10.38511  0.78826   33.18482  1.000 41.67471  ? 67  ASN E CG  1 
ATOM   4869 O OD1 . ASN E 5 55  ? 10.72554  1.90445   32.78683  1.000 50.95983  ? 67  ASN E OD1 1 
ATOM   4870 N ND2 . ASN E 5 55  ? 9.21759   0.56410   33.78007  1.000 44.41423  ? 67  ASN E ND2 1 
ATOM   4871 N N   . LYS E 5 56  ? 12.10102  -3.12747  34.19678  1.000 28.71208  ? 68  LYS E N   1 
ATOM   4872 C CA  . LYS E 5 56  ? 12.64485  -4.47378  34.14037  1.000 26.15336  ? 68  LYS E CA  1 
ATOM   4873 C C   . LYS E 5 56  ? 11.67395  -5.35175  33.37207  1.000 29.54033  ? 68  LYS E C   1 
ATOM   4874 O O   . LYS E 5 56  ? 10.46037  -5.15259  33.45419  1.000 32.98629  ? 68  LYS E O   1 
ATOM   4875 C CB  . LYS E 5 56  ? 12.87668  -5.02019  35.55715  1.000 30.96729  ? 68  LYS E CB  1 
ATOM   4876 C CG  . LYS E 5 56  ? 13.40741  -6.43644  35.63469  1.000 47.92889  ? 68  LYS E CG  1 
ATOM   4877 C CD  . LYS E 5 56  ? 13.77505  -6.78976  37.07072  1.000 46.15737  ? 68  LYS E CD  1 
ATOM   4878 C CE  . LYS E 5 56  ? 12.60584  -6.54970  38.01328  1.000 46.78891  ? 68  LYS E CE  1 
ATOM   4879 N NZ  . LYS E 5 56  ? 11.46825  -7.45971  37.71637  1.000 57.71868  ? 68  LYS E NZ  1 
ATOM   4880 N N   . GLY E 5 57  ? 12.20541  -6.29670  32.60679  1.000 27.27058  ? 69  GLY E N   1 
ATOM   4881 C CA  . GLY E 5 57  ? 11.39761  -7.27523  31.90589  1.000 27.88814  ? 69  GLY E CA  1 
ATOM   4882 C C   . GLY E 5 57  ? 11.06563  -8.45714  32.78885  1.000 31.81622  ? 69  GLY E C   1 
ATOM   4883 O O   . GLY E 5 57  ? 10.97788  -8.34282  34.01527  1.000 34.97742  ? 69  GLY E O   1 
ATOM   4884 N N   . ASN E 5 58  ? 10.89259  -9.61975  32.16044  1.000 32.16886  ? 70  ASN E N   1 
ATOM   4885 C CA  . ASN E 5 58  ? 10.55098  -10.84414 32.87519  1.000 34.24453  ? 70  ASN E CA  1 
ATOM   4886 C C   . ASN E 5 58  ? 11.69820  -11.85222 32.89414  1.000 32.13952  ? 70  ASN E C   1 
ATOM   4887 O O   . ASN E 5 58  ? 11.45354  -13.05653 33.00334  1.000 39.86575  ? 70  ASN E O   1 
ATOM   4888 C CB  . ASN E 5 58  ? 9.30273   -11.47947 32.26185  1.000 26.66957  ? 70  ASN E CB  1 
ATOM   4889 C CG  . ASN E 5 58  ? 8.24478   -10.45067 31.89893  1.000 57.74121  ? 70  ASN E CG  1 
ATOM   4890 O OD1 . ASN E 5 58  ? 7.87147   -9.61149  32.72091  1.000 66.26032  ? 70  ASN E OD1 1 
ATOM   4891 N ND2 . ASN E 5 58  ? 7.76768   -10.49973 30.65331  1.000 47.01401  ? 70  ASN E ND2 1 
ATOM   4892 N N   . PHE E 5 59  ? 12.94580  -11.38837 32.79322  1.000 26.82868  ? 71  PHE E N   1 
ATOM   4893 C CA  . PHE E 5 59  ? 14.06540  -12.31500 32.74167  1.000 28.39417  ? 71  PHE E CA  1 
ATOM   4894 C C   . PHE E 5 59  ? 14.43889  -12.79025 34.14426  1.000 30.60494  ? 71  PHE E C   1 
ATOM   4895 O O   . PHE E 5 59  ? 14.17438  -12.10190 35.13302  1.000 31.83491  ? 71  PHE E O   1 
ATOM   4896 C CB  . PHE E 5 59  ? 15.27097  -11.66121 32.06625  1.000 24.69427  ? 71  PHE E CB  1 
ATOM   4897 C CG  . PHE E 5 59  ? 15.25097  -11.77698 30.56684  1.000 30.21931  ? 71  PHE E CG  1 
ATOM   4898 C CD1 . PHE E 5 59  ? 14.53973  -10.86614 29.79483  1.000 17.80960  ? 71  PHE E CD1 1 
ATOM   4899 C CD2 . PHE E 5 59  ? 15.92503  -12.81030 29.92992  1.000 30.95289  ? 71  PHE E CD2 1 
ATOM   4900 C CE1 . PHE E 5 59  ? 14.50854  -10.98094 28.41554  1.000 27.54108  ? 71  PHE E CE1 1 
ATOM   4901 C CE2 . PHE E 5 59  ? 15.89630  -12.93480 28.54618  1.000 26.69468  ? 71  PHE E CE2 1 
ATOM   4902 C CZ  . PHE E 5 59  ? 15.18711  -12.01819 27.78812  1.000 29.14287  ? 71  PHE E CZ  1 
ATOM   4903 N N   . PRO E 5 60  ? 15.04572  -13.97095 34.25648  1.000 28.97665  ? 72  PRO E N   1 
ATOM   4904 C CA  . PRO E 5 60  ? 15.41359  -14.48753 35.58002  1.000 28.92896  ? 72  PRO E CA  1 
ATOM   4905 C C   . PRO E 5 60  ? 16.44504  -13.60319 36.26537  1.000 24.82937  ? 72  PRO E C   1 
ATOM   4906 O O   . PRO E 5 60  ? 17.11409  -12.77798 35.64053  1.000 25.01755  ? 72  PRO E O   1 
ATOM   4907 C CB  . PRO E 5 60  ? 15.99060  -15.87809 35.27571  1.000 26.39907  ? 72  PRO E CB  1 
ATOM   4908 C CG  . PRO E 5 60  ? 15.49762  -16.21831 33.89742  1.000 30.76254  ? 72  PRO E CG  1 
ATOM   4909 C CD  . PRO E 5 60  ? 15.40850  -14.90781 33.18095  1.000 19.00093  ? 72  PRO E CD  1 
ATOM   4910 N N   . GLY E 5 61  ? 16.58236  -13.80989 37.57746  1.000 29.38288  ? 74  GLY E N   1 
ATOM   4911 C CA  . GLY E 5 61  ? 17.45485  -12.98339 38.39578  1.000 18.91564  ? 74  GLY E CA  1 
ATOM   4912 C C   . GLY E 5 61  ? 18.92089  -13.04491 38.01888  1.000 29.07198  ? 74  GLY E C   1 
ATOM   4913 O O   . GLY E 5 61  ? 19.67420  -12.11902 38.34399  1.000 27.93947  ? 74  GLY E O   1 
ATOM   4914 N N   . ARG E 5 62  ? 19.35147  -14.11089 37.33957  1.000 30.49048  ? 75  ARG E N   1 
ATOM   4915 C CA  . ARG E 5 62  ? 20.75747  -14.20721 36.96336  1.000 24.88249  ? 75  ARG E CA  1 
ATOM   4916 C C   . ARG E 5 62  ? 21.14049  -13.18810 35.90004  1.000 29.21545  ? 75  ARG E C   1 
ATOM   4917 O O   . ARG E 5 62  ? 22.33530  -12.96293 35.68220  1.000 25.48512  ? 75  ARG E O   1 
ATOM   4918 C CB  . ARG E 5 62  ? 21.08042  -15.61200 36.47305  1.000 22.42515  ? 75  ARG E CB  1 
ATOM   4919 C CG  . ARG E 5 62  ? 20.30692  -16.02034 35.24663  1.000 28.13694  ? 75  ARG E CG  1 
ATOM   4920 C CD  . ARG E 5 62  ? 20.57293  -17.46525 34.95292  1.000 40.47701  ? 75  ARG E CD  1 
ATOM   4921 N NE  . ARG E 5 62  ? 19.58881  -18.01886 34.03900  1.000 29.17867  ? 75  ARG E NE  1 
ATOM   4922 C CZ  . ARG E 5 62  ? 19.79484  -18.13360 32.74024  1.000 30.96754  ? 75  ARG E CZ  1 
ATOM   4923 N NH1 . ARG E 5 62  ? 20.95054  -17.78690 32.20151  1.000 33.31051  ? 75  ARG E NH1 1 
ATOM   4924 N NH2 . ARG E 5 62  ? 18.82028  -18.60491 31.96568  1.000 28.80205  ? 75  ARG E NH2 1 
ATOM   4925 N N   . PHE E 5 63  ? 20.15961  -12.59032 35.22438  1.000 22.50128  ? 76  PHE E N   1 
ATOM   4926 C CA  . PHE E 5 63  ? 20.39939  -11.43167 34.37645  1.000 22.79403  ? 76  PHE E CA  1 
ATOM   4927 C C   . PHE E 5 63  ? 20.36600  -10.18583 35.25060  1.000 24.22706  ? 76  PHE E C   1 
ATOM   4928 O O   . PHE E 5 63  ? 19.37278  -9.93047  35.93742  1.000 29.16091  ? 76  PHE E O   1 
ATOM   4929 C CB  . PHE E 5 63  ? 19.35126  -11.33608 33.26738  1.000 19.27021  ? 76  PHE E CB  1 
ATOM   4930 C CG  . PHE E 5 63  ? 19.41023  -12.46013 32.27301  1.000 17.99426  ? 76  PHE E CG  1 
ATOM   4931 C CD1 . PHE E 5 63  ? 18.80980  -13.68074 32.54474  1.000 19.90067  ? 76  PHE E CD1 1 
ATOM   4932 C CD2 . PHE E 5 63  ? 20.06073  -12.29635 31.05984  1.000 21.15849  ? 76  PHE E CD2 1 
ATOM   4933 C CE1 . PHE E 5 63  ? 18.86522  -14.72091 31.62679  1.000 21.68382  ? 76  PHE E CE1 1 
ATOM   4934 C CE2 . PHE E 5 63  ? 20.11941  -13.33284 30.13542  1.000 21.79391  ? 76  PHE E CE2 1 
ATOM   4935 C CZ  . PHE E 5 63  ? 19.52189  -14.54611 30.41997  1.000 19.44319  ? 76  PHE E CZ  1 
ATOM   4936 N N   . SER E 5 64  ? 21.44955  -9.41990  35.24322  1.000 19.89745  ? 77  SER E N   1 
ATOM   4937 C CA  . SER E 5 64  ? 21.51087  -8.20033  36.02817  1.000 26.49003  ? 77  SER E CA  1 
ATOM   4938 C C   . SER E 5 64  ? 22.23661  -7.14812  35.21109  1.000 26.39092  ? 77  SER E C   1 
ATOM   4939 O O   . SER E 5 64  ? 22.96559  -7.46494  34.26860  1.000 22.34628  ? 77  SER E O   1 
ATOM   4940 C CB  . SER E 5 64  ? 22.21129  -8.41695  37.38121  1.000 20.16572  ? 77  SER E CB  1 
ATOM   4941 O OG  . SER E 5 64  ? 23.60340  -8.64288  37.22021  1.000 23.89261  ? 77  SER E OG  1 
ATOM   4942 N N   . GLY E 5 65  ? 22.03202  -5.88682  35.59027  1.000 23.70130  ? 78  GLY E N   1 
ATOM   4943 C CA  . GLY E 5 65  ? 22.60450  -4.77247  34.86866  1.000 26.92428  ? 78  GLY E CA  1 
ATOM   4944 C C   . GLY E 5 65  ? 23.05722  -3.67726  35.81342  1.000 23.38513  ? 78  GLY E C   1 
ATOM   4945 O O   . GLY E 5 65  ? 22.89639  -3.77283  37.02781  1.000 27.75656  ? 78  GLY E O   1 
ATOM   4946 N N   . ARG E 5 66  ? 23.59571  -2.61714  35.21972  1.000 30.69250  ? 79  ARG E N   1 
ATOM   4947 C CA  . ARG E 5 66  ? 24.26901  -1.55317  35.94579  1.000 25.50679  ? 79  ARG E CA  1 
ATOM   4948 C C   . ARG E 5 66  ? 24.45575  -0.38457  34.99314  1.000 24.80103  ? 79  ARG E C   1 
ATOM   4949 O O   . ARG E 5 66  ? 24.64308  -0.58213  33.78927  1.000 27.33498  ? 79  ARG E O   1 
ATOM   4950 C CB  . ARG E 5 66  ? 25.62558  -2.03350  36.47682  1.000 29.23248  ? 79  ARG E CB  1 
ATOM   4951 C CG  . ARG E 5 66  ? 26.22062  -1.19966  37.58596  1.000 51.99619  ? 79  ARG E CG  1 
ATOM   4952 C CD  . ARG E 5 66  ? 27.56857  -1.76365  38.01333  1.000 62.70224  ? 79  ARG E CD  1 
ATOM   4953 N NE  . ARG E 5 66  ? 27.68785  -3.18206  37.69269  1.000 74.63065  ? 79  ARG E NE  1 
ATOM   4954 C CZ  . ARG E 5 66  ? 28.71015  -3.95113  38.04542  1.000 87.89731  ? 79  ARG E CZ  1 
ATOM   4955 N NH1 . ARG E 5 66  ? 29.71360  -3.48028  38.76915  1.000 69.09227  ? 79  ARG E NH1 1 
ATOM   4956 N NH2 . ARG E 5 66  ? 28.72671  -5.22492  37.66118  1.000 90.98954  ? 79  ARG E NH2 1 
ATOM   4957 N N   . GLN E 5 67  ? 24.40313  0.82845   35.53369  1.000 27.22442  ? 80  GLN E N   1 
ATOM   4958 C CA  . GLN E 5 67  ? 24.73423  2.02141   34.76443  1.000 30.10643  ? 80  GLN E CA  1 
ATOM   4959 C C   . GLN E 5 67  ? 25.63663  2.91483   35.60014  1.000 29.17572  ? 80  GLN E C   1 
ATOM   4960 O O   . GLN E 5 67  ? 25.35551  3.15647   36.77873  1.000 34.52376  ? 80  GLN E O   1 
ATOM   4961 C CB  . GLN E 5 67  ? 23.48425  2.78937   34.32750  1.000 23.61298  ? 80  GLN E CB  1 
ATOM   4962 C CG  . GLN E 5 67  ? 23.79912  3.94846   33.38858  1.000 21.64622  ? 80  GLN E CG  1 
ATOM   4963 C CD  . GLN E 5 67  ? 22.57999  4.76821   33.01776  1.000 27.85096  ? 80  GLN E CD  1 
ATOM   4964 O OE1 . GLN E 5 67  ? 21.69787  5.01064   33.84482  1.000 25.09429  ? 80  GLN E OE1 1 
ATOM   4965 N NE2 . GLN E 5 67  ? 22.52406  5.20255   31.76162  1.000 24.21984  ? 80  GLN E NE2 1 
ATOM   4966 N N   . PHE E 5 68  ? 26.71471  3.39937   34.98644  1.000 24.58507  ? 81  PHE E N   1 
ATOM   4967 C CA  . PHE E 5 68  ? 27.69751  4.23530   35.65299  1.000 25.01649  ? 81  PHE E CA  1 
ATOM   4968 C C   . PHE E 5 68  ? 27.37224  5.71537   35.45113  1.000 32.54352  ? 81  PHE E C   1 
ATOM   4969 O O   . PHE E 5 68  ? 26.43051  6.08423   34.74794  1.000 35.97915  ? 81  PHE E O   1 
ATOM   4970 C CB  . PHE E 5 68  ? 29.09705  3.91228   35.13951  1.000 26.12071  ? 81  PHE E CB  1 
ATOM   4971 C CG  . PHE E 5 68  ? 29.47041  2.47227   35.28057  1.000 29.63345  ? 81  PHE E CG  1 
ATOM   4972 C CD1 . PHE E 5 68  ? 29.99869  1.99267   36.46762  1.000 25.85396  ? 81  PHE E CD1 1 
ATOM   4973 C CD2 . PHE E 5 68  ? 29.29549  1.59376   34.22468  1.000 32.16658  ? 81  PHE E CD2 1 
ATOM   4974 C CE1 . PHE E 5 68  ? 30.34326  0.66401   36.59897  1.000 28.15119  ? 81  PHE E CE1 1 
ATOM   4975 C CE2 . PHE E 5 68  ? 29.64182  0.25957   34.34934  1.000 33.90818  ? 81  PHE E CE2 1 
ATOM   4976 C CZ  . PHE E 5 68  ? 30.16643  -0.20444  35.53847  1.000 38.80182  ? 81  PHE E CZ  1 
ATOM   4977 N N   . SER E 5 69  ? 28.17981  6.58087   36.06741  1.000 31.48712  ? 83  SER E N   1 
ATOM   4978 C CA  . SER E 5 69  ? 27.89400  8.01153   36.05196  1.000 35.97883  ? 83  SER E CA  1 
ATOM   4979 C C   . SER E 5 69  ? 28.09970  8.63943   34.67839  1.000 33.46456  ? 83  SER E C   1 
ATOM   4980 O O   . SER E 5 69  ? 27.50746  9.68623   34.39889  1.000 35.55306  ? 83  SER E O   1 
ATOM   4981 C CB  . SER E 5 69  ? 28.75211  8.73615   37.09578  1.000 38.27638  ? 83  SER E CB  1 
ATOM   4982 O OG  . SER E 5 69  ? 30.13400  8.59108   36.82458  1.000 51.35505  ? 83  SER E OG  1 
ATOM   4983 N N   . ASN E 5 70  ? 28.91631  8.03748   33.81426  1.000 32.93619  ? 84  ASN E N   1 
ATOM   4984 C CA  . ASN E 5 70  ? 29.05080  8.50853   32.44205  1.000 26.92165  ? 84  ASN E CA  1 
ATOM   4985 C C   . ASN E 5 70  ? 28.02646  7.87578   31.50438  1.000 31.51183  ? 84  ASN E C   1 
ATOM   4986 O O   . ASN E 5 70  ? 28.22872  7.88227   30.28435  1.000 32.11430  ? 84  ASN E O   1 
ATOM   4987 C CB  . ASN E 5 70  ? 30.46768  8.25179   31.92725  1.000 30.44052  ? 84  ASN E CB  1 
ATOM   4988 C CG  . ASN E 5 70  ? 30.80898  6.77790   31.85963  1.000 35.48574  ? 84  ASN E CG  1 
ATOM   4989 O OD1 . ASN E 5 70  ? 29.97996  5.91595   32.14954  1.000 45.00481  ? 84  ASN E OD1 1 
ATOM   4990 N ND2 . ASN E 5 70  ? 32.03855  6.47958   31.46685  1.000 39.17763  ? 84  ASN E ND2 1 
ATOM   4991 N N   . SER E 5 71  ? 26.95343  7.30704   32.05688  1.000 28.97988  ? 85  SER E N   1 
ATOM   4992 C CA  . SER E 5 71  ? 25.84655  6.64611   31.36885  1.000 35.84942  ? 85  SER E CA  1 
ATOM   4993 C C   . SER E 5 71  ? 26.24154  5.34266   30.68199  1.000 29.77115  ? 85  SER E C   1 
ATOM   4994 O O   . SER E 5 71  ? 25.36436  4.67623   30.11592  1.000 28.96275  ? 85  SER E O   1 
ATOM   4995 C CB  . SER E 5 71  ? 25.16055  7.56084   30.34277  1.000 25.31149  ? 85  SER E CB  1 
ATOM   4996 O OG  . SER E 5 71  ? 24.49671  8.63170   30.99140  1.000 43.05692  ? 85  SER E OG  1 
ATOM   4997 N N   . ARG E 5 72  ? 27.51613  4.95381   30.69965  1.000 30.73651  ? 86  ARG E N   1 
ATOM   4998 C CA  . ARG E 5 72  ? 27.87670  3.62533   30.22470  1.000 27.78556  ? 86  ARG E CA  1 
ATOM   4999 C C   . ARG E 5 72  ? 27.17359  2.57757   31.08021  1.000 31.10102  ? 86  ARG E C   1 
ATOM   5000 O O   . ARG E 5 72  ? 27.01466  2.74827   32.29255  1.000 29.25592  ? 86  ARG E O   1 
ATOM   5001 C CB  . ARG E 5 72  ? 29.39507  3.42353   30.26775  1.000 33.71059  ? 86  ARG E CB  1 
ATOM   5002 C CG  . ARG E 5 72  ? 29.84864  2.09142   29.67010  1.000 53.57561  ? 86  ARG E CG  1 
ATOM   5003 C CD  . ARG E 5 72  ? 31.36391  1.93121   29.65766  1.000 44.31482  ? 86  ARG E CD  1 
ATOM   5004 N NE  . ARG E 5 72  ? 31.90606  1.75544   30.99948  1.000 51.32686  ? 86  ARG E NE  1 
ATOM   5005 C CZ  . ARG E 5 72  ? 32.06304  0.58293   31.60001  1.000 48.25904  ? 86  ARG E CZ  1 
ATOM   5006 N NH1 . ARG E 5 72  ? 31.74266  -0.55185  31.00068  1.000 49.22304  ? 86  ARG E NH1 1 
ATOM   5007 N NH2 . ARG E 5 72  ? 32.55045  0.54827   32.83528  1.000 42.27197  ? 86  ARG E NH2 1 
ATOM   5008 N N   . SER E 5 73  ? 26.72888  1.49737   30.44395  1.000 23.84939  ? 87  SER E N   1 
ATOM   5009 C CA  . SER E 5 73  ? 25.95761  0.47197   31.12852  1.000 22.56449  ? 87  SER E CA  1 
ATOM   5010 C C   . SER E 5 73  ? 26.58375  -0.89754  30.91522  1.000 26.07222  ? 87  SER E C   1 
ATOM   5011 O O   . SER E 5 73  ? 27.16220  -1.18516  29.86365  1.000 28.35125  ? 87  SER E O   1 
ATOM   5012 C CB  . SER E 5 73  ? 24.50449  0.44904   30.65533  1.000 18.66597  ? 87  SER E CB  1 
ATOM   5013 O OG  . SER E 5 73  ? 23.78945  -0.60614  31.26726  1.000 22.99389  ? 87  SER E OG  1 
ATOM   5014 N N   . GLU E 5 74  ? 26.46249  -1.74195  31.93169  1.000 22.41778  ? 88  GLU E N   1 
ATOM   5015 C CA  . GLU E 5 74  ? 26.95005  -3.10948  31.87130  1.000 23.08243  ? 88  GLU E CA  1 
ATOM   5016 C C   . GLU E 5 74  ? 25.80653  -4.06824  32.13237  1.000 26.45050  ? 88  GLU E C   1 
ATOM   5017 O O   . GLU E 5 74  ? 24.91771  -3.79263  32.94195  1.000 30.95165  ? 88  GLU E O   1 
ATOM   5018 C CB  . GLU E 5 74  ? 28.07075  -3.36883  32.87858  1.000 18.58171  ? 88  GLU E CB  1 
ATOM   5019 C CG  . GLU E 5 74  ? 29.43030  -2.95114  32.37350  1.000 32.78017  ? 88  GLU E CG  1 
ATOM   5020 C CD  . GLU E 5 74  ? 30.54387  -3.24961  33.35749  1.000 30.95157  ? 88  GLU E CD  1 
ATOM   5021 O OE1 . GLU E 5 74  ? 30.24764  -3.60338  34.52067  1.000 41.08367  ? 88  GLU E OE1 1 
ATOM   5022 O OE2 . GLU E 5 74  ? 31.71864  -3.12542  32.95923  1.000 40.22652  ? 88  GLU E OE2 1 
ATOM   5023 N N   . MET E 5 75  ? 25.84289  -5.19148  31.44071  1.000 23.43303  ? 89  MET E N   1 
ATOM   5024 C CA  . MET E 5 75  ? 24.86905  -6.25023  31.60342  1.000 24.43785  ? 89  MET E CA  1 
ATOM   5025 C C   . MET E 5 75  ? 25.62054  -7.51155  31.97825  1.000 24.90584  ? 89  MET E C   1 
ATOM   5026 O O   . MET E 5 75  ? 26.68182  -7.79466  31.41414  1.000 30.85424  ? 89  MET E O   1 
ATOM   5027 C CB  . MET E 5 75  ? 24.08418  -6.45179  30.31652  1.000 28.81120  ? 89  MET E CB  1 
ATOM   5028 C CG  . MET E 5 75  ? 22.99354  -7.45796  30.41567  1.000 41.07219  ? 89  MET E CG  1 
ATOM   5029 S SD  . MET E 5 75  ? 22.71115  -8.10980  28.77053  1.000 38.83110  ? 89  MET E SD  1 
ATOM   5030 C CE  . MET E 5 75  ? 23.12673  -9.83225  29.04691  1.000 37.91402  ? 89  MET E CE  1 
ATOM   5031 N N   . ASN E 5 76  ? 25.08336  -8.26000  32.93501  1.000 22.23614  ? 90  ASN E N   1 
ATOM   5032 C CA  . ASN E 5 76  ? 25.77541  -9.42440  33.46519  1.000 22.17229  ? 90  ASN E CA  1 
ATOM   5033 C C   . ASN E 5 76  ? 24.82624  -10.60930 33.55311  1.000 24.45747  ? 90  ASN E C   1 
ATOM   5034 O O   . ASN E 5 76  ? 23.65614  -10.45633 33.91539  1.000 25.59589  ? 90  ASN E O   1 
ATOM   5035 C CB  . ASN E 5 76  ? 26.37316  -9.11874  34.85048  1.000 26.88360  ? 90  ASN E CB  1 
ATOM   5036 C CG  . ASN E 5 76  ? 26.99904  -10.34077 35.50208  1.000 42.88545  ? 90  ASN E CG  1 
ATOM   5037 O OD1 . ASN E 5 76  ? 26.35867  -11.03473 36.29429  1.000 36.84457  ? 90  ASN E OD1 1 
ATOM   5038 N ND2 . ASN E 5 76  ? 28.25922  -10.60987 35.17071  1.000 34.23394  ? 90  ASN E ND2 1 
ATOM   5039 N N   . VAL E 5 77  ? 25.33547  -11.78565 33.19965  1.000 24.69252  ? 91  VAL E N   1 
ATOM   5040 C CA  . VAL E 5 77  ? 24.66600  -13.06002 33.44387  1.000 24.78994  ? 91  VAL E CA  1 
ATOM   5041 C C   . VAL E 5 77  ? 25.59497  -13.88840 34.32022  1.000 31.22984  ? 91  VAL E C   1 
ATOM   5042 O O   . VAL E 5 77  ? 26.71983  -14.20498 33.91449  1.000 29.11710  ? 91  VAL E O   1 
ATOM   5043 C CB  . VAL E 5 77  ? 24.33133  -13.80097 32.13932  1.000 28.72260  ? 91  VAL E CB  1 
ATOM   5044 C CG1 . VAL E 5 77  ? 23.36282  -14.92936 32.40790  1.000 22.83865  ? 91  VAL E CG1 1 
ATOM   5045 C CG2 . VAL E 5 77  ? 23.75062  -12.84477 31.11481  1.000 21.00242  ? 91  VAL E CG2 1 
ATOM   5046 N N   . SER E 5 78  ? 25.13504  -14.22606 35.52481  1.000 31.36737  ? 92  SER E N   1 
ATOM   5047 C CA  . SER E 5 78  ? 26.01900  -14.84820 36.50632  1.000 28.72925  ? 92  SER E CA  1 
ATOM   5048 C C   . SER E 5 78  ? 26.26031  -16.32389 36.22461  1.000 28.35259  ? 92  SER E C   1 
ATOM   5049 O O   . SER E 5 78  ? 27.33162  -16.84431 36.55421  1.000 30.70674  ? 92  SER E O   1 
ATOM   5050 C CB  . SER E 5 78  ? 25.43793  -14.68171 37.90566  1.000 23.77126  ? 92  SER E CB  1 
ATOM   5051 O OG  . SER E 5 78  ? 24.16247  -15.28790 37.98577  1.000 28.52534  ? 92  SER E OG  1 
ATOM   5052 N N   . THR E 5 79  ? 25.28800  -17.00365 35.62293  1.000 27.52279  ? 93  THR E N   1 
ATOM   5053 C CA  . THR E 5 79  ? 25.38514  -18.43404 35.34955  1.000 30.89638  ? 93  THR E CA  1 
ATOM   5054 C C   . THR E 5 79  ? 24.66924  -18.67556 34.02973  1.000 25.21610  ? 93  THR E C   1 
ATOM   5055 O O   . THR E 5 79  ? 23.43952  -18.60632 33.97177  1.000 42.25237  ? 93  THR E O   1 
ATOM   5056 C CB  . THR E 5 79  ? 24.76266  -19.25597 36.47998  1.000 34.93499  ? 93  THR E CB  1 
ATOM   5057 O OG1 . THR E 5 79  ? 25.50048  -19.04581 37.68904  1.000 37.01701  ? 93  THR E OG1 1 
ATOM   5058 C CG2 . THR E 5 79  ? 24.78305  -20.73168 36.14497  1.000 38.23521  ? 93  THR E CG2 1 
ATOM   5059 N N   . LEU E 5 80  ? 25.42972  -18.95054 32.97815  1.000 29.17264  ? 94  LEU E N   1 
ATOM   5060 C CA  . LEU E 5 80  ? 24.86574  -19.02131 31.63779  1.000 26.25646  ? 94  LEU E CA  1 
ATOM   5061 C C   . LEU E 5 80  ? 24.23920  -20.38283 31.36328  1.000 31.02622  ? 94  LEU E C   1 
ATOM   5062 O O   . LEU E 5 80  ? 24.76035  -21.42570 31.77105  1.000 30.16554  ? 94  LEU E O   1 
ATOM   5063 C CB  . LEU E 5 80  ? 25.94343  -18.72762 30.59561  1.000 26.39149  ? 94  LEU E CB  1 
ATOM   5064 C CG  . LEU E 5 80  ? 26.31200  -17.25143 30.46135  1.000 27.80262  ? 94  LEU E CG  1 
ATOM   5065 C CD1 . LEU E 5 80  ? 27.72340  -17.09557 29.92315  1.000 21.24833  ? 94  LEU E CD1 1 
ATOM   5066 C CD2 . LEU E 5 80  ? 25.30180  -16.55302 29.55971  1.000 27.18179  ? 94  LEU E CD2 1 
ATOM   5067 N N   . GLU E 5 81  ? 23.10644  -20.36000 30.67261  1.000 27.09638  ? 95  GLU E N   1 
ATOM   5068 C CA  . GLU E 5 81  ? 22.47029  -21.55134 30.14090  1.000 28.37175  ? 95  GLU E CA  1 
ATOM   5069 C C   . GLU E 5 81  ? 22.62965  -21.57746 28.62833  1.000 30.20906  ? 95  GLU E C   1 
ATOM   5070 O O   . GLU E 5 81  ? 22.82987  -20.53932 27.98525  1.000 25.44233  ? 95  GLU E O   1 
ATOM   5071 C CB  . GLU E 5 81  ? 20.98189  -21.59997 30.50902  1.000 26.76067  ? 95  GLU E CB  1 
ATOM   5072 C CG  . GLU E 5 81  ? 20.70589  -21.58028 32.00282  1.000 30.19680  ? 95  GLU E CG  1 
ATOM   5073 C CD  . GLU E 5 81  ? 21.28390  -22.78708 32.71928  1.000 36.39181  ? 95  GLU E CD  1 
ATOM   5074 O OE1 . GLU E 5 81  ? 21.36364  -23.86691 32.09698  1.000 39.25466  ? 95  GLU E OE1 1 
ATOM   5075 O OE2 . GLU E 5 81  ? 21.66425  -22.65769 33.90306  1.000 56.58232  ? 95  GLU E OE2 1 
ATOM   5076 N N   . LEU E 5 82  ? 22.53507  -22.78923 28.06998  1.000 26.15440  ? 96  LEU E N   1 
ATOM   5077 C CA  . LEU E 5 82  ? 22.59478  -22.95845 26.62150  1.000 22.84949  ? 96  LEU E CA  1 
ATOM   5078 C C   . LEU E 5 82  ? 21.58629  -22.06474 25.91341  1.000 25.14172  ? 96  LEU E C   1 
ATOM   5079 O O   . LEU E 5 82  ? 21.88340  -21.49241 24.85872  1.000 27.15552  ? 96  LEU E O   1 
ATOM   5080 C CB  . LEU E 5 82  ? 22.34768  -24.42087 26.25703  1.000 26.08222  ? 96  LEU E CB  1 
ATOM   5081 C CG  . LEU E 5 82  ? 23.30234  -25.43051 26.88636  1.000 38.99913  ? 96  LEU E CG  1 
ATOM   5082 C CD1 . LEU E 5 82  ? 22.96741  -26.84037 26.41813  1.000 29.62972  ? 96  LEU E CD1 1 
ATOM   5083 C CD2 . LEU E 5 82  ? 24.74153  -25.06276 26.54818  1.000 29.77069  ? 96  LEU E CD2 1 
ATOM   5084 N N   . GLY E 5 83  ? 20.38878  -21.92921 26.48146  1.000 26.71997  ? 97  GLY E N   1 
ATOM   5085 C CA  . GLY E 5 83  ? 19.35925  -21.09636 25.89603  1.000 16.55929  ? 97  GLY E CA  1 
ATOM   5086 C C   . GLY E 5 83  ? 19.60680  -19.60825 25.99055  1.000 25.89739  ? 97  GLY E C   1 
ATOM   5087 O O   . GLY E 5 83  ? 18.79107  -18.83442 25.48267  1.000 24.00995  ? 97  GLY E O   1 
ATOM   5088 N N   . ASP E 5 84  ? 20.69642  -19.17749 26.62972  1.000 23.01430  ? 98  ASP E N   1 
ATOM   5089 C CA  . ASP E 5 84  ? 21.03269  -17.76084 26.65793  1.000 22.70010  ? 98  ASP E CA  1 
ATOM   5090 C C   . ASP E 5 84  ? 21.76999  -17.30627 25.40684  1.000 31.39748  ? 98  ASP E C   1 
ATOM   5091 O O   . ASP E 5 84  ? 22.05062  -16.10882 25.28032  1.000 31.04203  ? 98  ASP E O   1 
ATOM   5092 C CB  . ASP E 5 84  ? 21.87886  -17.43232 27.88937  1.000 18.79311  ? 98  ASP E CB  1 
ATOM   5093 C CG  . ASP E 5 84  ? 21.13470  -17.65386 29.18889  1.000 26.18980  ? 98  ASP E CG  1 
ATOM   5094 O OD1 . ASP E 5 84  ? 19.88581  -17.58252 29.20374  1.000 30.11815  ? 98  ASP E OD1 1 
ATOM   5095 O OD2 . ASP E 5 84  ? 21.81026  -17.89728 30.20868  1.000 24.88312  ? 98  ASP E OD2 1 
ATOM   5096 N N   . SER E 5 85  ? 22.10175  -18.22681 24.50031  1.000 21.72862  ? 99  SER E N   1 
ATOM   5097 C CA  . SER E 5 85  ? 22.73257  -17.86270 23.23729  1.000 24.15340  ? 99  SER E CA  1 
ATOM   5098 C C   . SER E 5 85  ? 21.81154  -16.94953 22.44856  1.000 23.21008  ? 99  SER E C   1 
ATOM   5099 O O   . SER E 5 85  ? 20.66365  -17.30847 22.16905  1.000 30.35531  ? 99  SER E O   1 
ATOM   5100 C CB  . SER E 5 85  ? 23.05748  -19.11659 22.42809  1.000 18.46037  ? 99  SER E CB  1 
ATOM   5101 O OG  . SER E 5 85  ? 24.01109  -19.92451 23.09431  1.000 25.52211  ? 99  SER E OG  1 
ATOM   5102 N N   . ALA E 5 86  ? 22.30929  -15.76936 22.09165  1.000 21.82051  ? 100 ALA E N   1 
ATOM   5103 C CA  . ALA E 5 86  ? 21.46130  -14.74993 21.48538  1.000 26.29347  ? 100 ALA E CA  1 
ATOM   5104 C C   . ALA E 5 86  ? 22.32312  -13.55753 21.10130  1.000 29.92132  ? 100 ALA E C   1 
ATOM   5105 O O   . ALA E 5 86  ? 23.49089  -13.45427 21.48728  1.000 24.79426  ? 100 ALA E O   1 
ATOM   5106 C CB  . ALA E 5 86  ? 20.34874  -14.29858 22.43485  1.000 19.46315  ? 100 ALA E CB  1 
ATOM   5107 N N   . LEU E 5 87  ? 21.72541  -12.65224 20.33881  1.000 19.86111  ? 101 LEU E N   1 
ATOM   5108 C CA  . LEU E 5 87  ? 22.29833  -11.33298 20.11735  1.000 24.22042  ? 101 LEU E CA  1 
ATOM   5109 C C   . LEU E 5 87  ? 21.77545  -10.40078 21.20799  1.000 26.51155  ? 101 LEU E C   1 
ATOM   5110 O O   . LEU E 5 87  ? 20.56462  -10.17379 21.30689  1.000 22.95718  ? 101 LEU E O   1 
ATOM   5111 C CB  . LEU E 5 87  ? 21.93462  -10.81067 18.72640  1.000 24.67919  ? 101 LEU E CB  1 
ATOM   5112 C CG  . LEU E 5 87  ? 22.51500  -9.44791  18.33520  1.000 29.79839  ? 101 LEU E CG  1 
ATOM   5113 C CD1 . LEU E 5 87  ? 24.03218  -9.52732  18.16605  1.000 22.52793  ? 101 LEU E CD1 1 
ATOM   5114 C CD2 . LEU E 5 87  ? 21.84412  -8.90628  17.07808  1.000 21.14789  ? 101 LEU E CD2 1 
ATOM   5115 N N   . TYR E 5 88  ? 22.67324  -9.87554  22.03629  1.000 19.35316  ? 102 TYR E N   1 
ATOM   5116 C CA  . TYR E 5 88  ? 22.27863  -8.99156  23.12659  1.000 24.71771  ? 102 TYR E CA  1 
ATOM   5117 C C   . TYR E 5 88  ? 22.46664  -7.55021  22.68280  1.000 22.07199  ? 102 TYR E C   1 
ATOM   5118 O O   . TYR E 5 88  ? 23.59684  -7.10474  22.45845  1.000 22.67695  ? 102 TYR E O   1 
ATOM   5119 C CB  . TYR E 5 88  ? 23.06119  -9.29643  24.40578  1.000 15.48124  ? 102 TYR E CB  1 
ATOM   5120 C CG  . TYR E 5 88  ? 22.56978  -10.56979 25.04266  1.000 21.20329  ? 102 TYR E CG  1 
ATOM   5121 C CD1 . TYR E 5 88  ? 21.50282  -10.55587 25.93488  1.000 25.23908  ? 102 TYR E CD1 1 
ATOM   5122 C CD2 . TYR E 5 88  ? 23.13220  -11.79397 24.71460  1.000 14.67895  ? 102 TYR E CD2 1 
ATOM   5123 C CE1 . TYR E 5 88  ? 21.02553  -11.72627 26.49750  1.000 23.41983  ? 102 TYR E CE1 1 
ATOM   5124 C CE2 . TYR E 5 88  ? 22.66137  -12.96991 25.27578  1.000 21.54925  ? 102 TYR E CE2 1 
ATOM   5125 C CZ  . TYR E 5 88  ? 21.60699  -12.92944 26.16152  1.000 19.34576  ? 102 TYR E CZ  1 
ATOM   5126 O OH  . TYR E 5 88  ? 21.13482  -14.09592 26.71847  1.000 21.72083  ? 102 TYR E OH  1 
ATOM   5127 N N   . LEU E 5 89  ? 21.35580  -6.83150  22.55940  1.000 19.05787  ? 103 LEU E N   1 
ATOM   5128 C CA  . LEU E 5 89  ? 21.32487  -5.49306  21.98996  1.000 25.78424  ? 103 LEU E CA  1 
ATOM   5129 C C   . LEU E 5 89  ? 21.10680  -4.46476  23.08626  1.000 28.13861  ? 103 LEU E C   1 
ATOM   5130 O O   . LEU E 5 89  ? 20.25775  -4.65191  23.96314  1.000 27.18217  ? 103 LEU E O   1 
ATOM   5131 C CB  . LEU E 5 89  ? 20.20379  -5.36784  20.94931  1.000 20.93531  ? 103 LEU E CB  1 
ATOM   5132 C CG  . LEU E 5 89  ? 20.36262  -6.14274  19.64213  1.000 24.92177  ? 103 LEU E CG  1 
ATOM   5133 C CD1 . LEU E 5 89  ? 19.02205  -6.32508  18.96142  1.000 27.26763  ? 103 LEU E CD1 1 
ATOM   5134 C CD2 . LEU E 5 89  ? 21.33087  -5.42194  18.72057  1.000 22.23921  ? 103 LEU E CD2 1 
ATOM   5135 N N   . CYS E 5 90  ? 21.86053  -3.37362  23.03277  1.000 26.22058  ? 104 CYS E N   1 
ATOM   5136 C CA  . CYS E 5 90  ? 21.56401  -2.22544  23.87125  1.000 35.80179  ? 104 CYS E CA  1 
ATOM   5137 C C   . CYS E 5 90  ? 21.10850  -1.06434  23.00050  1.000 24.41868  ? 104 CYS E C   1 
ATOM   5138 O O   . CYS E 5 90  ? 21.55254  -0.90595  21.86209  1.000 22.74471  ? 104 CYS E O   1 
ATOM   5139 C CB  . CYS E 5 90  ? 22.75916  -1.80408  24.73260  1.000 29.95874  ? 104 CYS E CB  1 
ATOM   5140 S SG  . CYS E 5 90  ? 23.99978  -0.87404  23.86246  1.000 46.70628  ? 104 CYS E SG  1 
ATOM   5141 N N   . ALA E 5 91  ? 20.19373  -0.27082  23.54309  1.000 23.19687  ? 105 ALA E N   1 
ATOM   5142 C CA  . ALA E 5 91  ? 19.61953  0.86913   22.84842  1.000 28.17762  ? 105 ALA E CA  1 
ATOM   5143 C C   . ALA E 5 91  ? 19.67499  2.07580   23.76795  1.000 26.03594  ? 105 ALA E C   1 
ATOM   5144 O O   . ALA E 5 91  ? 19.44835  1.95269   24.97560  1.000 30.87329  ? 105 ALA E O   1 
ATOM   5145 C CB  . ALA E 5 91  ? 18.16994  0.59293   22.42542  1.000 20.87378  ? 105 ALA E CB  1 
ATOM   5146 N N   . SER E 5 92  ? 19.98570  3.23774   23.20479  1.000 23.91136  ? 106 SER E N   1 
ATOM   5147 C CA  . SER E 5 92  ? 20.07254  4.45725   23.99228  1.000 25.92911  ? 106 SER E CA  1 
ATOM   5148 C C   . SER E 5 92  ? 19.09190  5.49840   23.47013  1.000 27.08076  ? 106 SER E C   1 
ATOM   5149 O O   . SER E 5 92  ? 18.79013  5.54883   22.27597  1.000 25.39308  ? 106 SER E O   1 
ATOM   5150 C CB  . SER E 5 92  ? 21.49862  5.02629   23.98913  1.000 19.08473  ? 106 SER E CB  1 
ATOM   5151 O OG  . SER E 5 92  ? 21.73871  5.84955   22.86479  1.000 33.43409  ? 106 SER E OG  1 
ATOM   5152 N N   . SER E 5 93  ? 18.58147  6.31517   24.38790  1.000 28.42555  ? 107 SER E N   1 
ATOM   5153 C CA  . SER E 5 93  ? 17.75285  7.46232   24.05005  1.000 24.44019  ? 107 SER E CA  1 
ATOM   5154 C C   . SER E 5 93  ? 18.10087  8.59931   24.99592  1.000 31.86792  ? 107 SER E C   1 
ATOM   5155 O O   . SER E 5 93  ? 18.58065  8.36797   26.11304  1.000 25.90207  ? 107 SER E O   1 
ATOM   5156 C CB  . SER E 5 93  ? 16.25614  7.14112   24.14201  1.000 22.46875  ? 107 SER E CB  1 
ATOM   5157 O OG  . SER E 5 93  ? 15.91406  6.70696   25.44563  1.000 22.44268  ? 107 SER E OG  1 
ATOM   5158 N N   . LEU E 5 94  ? 17.86386  9.83178   24.53289  1.000 31.65321  ? 108 LEU E N   1 
ATOM   5159 C CA  . LEU E 5 94  ? 18.16699  11.00308  25.35026  1.000 29.82700  ? 108 LEU E CA  1 
ATOM   5160 C C   . LEU E 5 94  ? 17.48003  10.91366  26.70537  1.000 22.69438  ? 108 LEU E C   1 
ATOM   5161 O O   . LEU E 5 94  ? 18.11635  11.07369  27.75098  1.000 26.17886  ? 108 LEU E O   1 
ATOM   5162 C CB  . LEU E 5 94  ? 17.74923  12.28263  24.62213  1.000 28.55069  ? 108 LEU E CB  1 
ATOM   5163 C CG  . LEU E 5 94  ? 18.00507  13.59905  25.36951  1.000 29.45365  ? 108 LEU E CG  1 
ATOM   5164 C CD1 . LEU E 5 94  ? 19.49202  13.79168  25.69289  1.000 19.46123  ? 108 LEU E CD1 1 
ATOM   5165 C CD2 . LEU E 5 94  ? 17.46942  14.78331  24.57357  1.000 27.59531  ? 108 LEU E CD2 1 
ATOM   5166 N N   . ARG E 5 95  ? 16.18675  10.61936  26.70332  1.000 31.57883  ? 109 ARG E N   1 
ATOM   5167 C CA  . ARG E 5 95  ? 15.37413  10.61294  27.90608  1.000 30.13227  ? 109 ARG E CA  1 
ATOM   5168 C C   . ARG E 5 95  ? 14.85554  9.20734   28.17405  1.000 26.18790  ? 109 ARG E C   1 
ATOM   5169 O O   . ARG E 5 95  ? 14.97808  8.30379   27.34502  1.000 24.41099  ? 109 ARG E O   1 
ATOM   5170 C CB  . ARG E 5 95  ? 14.21078  11.60134  27.77605  1.000 28.94500  ? 109 ARG E CB  1 
ATOM   5171 C CG  . ARG E 5 95  ? 14.65535  13.00613  27.43723  1.000 36.57929  ? 109 ARG E CG  1 
ATOM   5172 C CD  . ARG E 5 95  ? 13.47355  13.90546  27.12571  1.000 47.31452  ? 109 ARG E CD  1 
ATOM   5173 N NE  . ARG E 5 95  ? 13.88535  15.28710  26.90581  1.000 41.82035  ? 109 ARG E NE  1 
ATOM   5174 C CZ  . ARG E 5 95  ? 14.09851  15.82489  25.71287  1.000 41.38141  ? 109 ARG E CZ  1 
ATOM   5175 N NH1 . ARG E 5 95  ? 13.92588  15.12923  24.60058  1.000 36.55986  ? 109 ARG E NH1 1 
ATOM   5176 N NH2 . ARG E 5 95  ? 14.49320  17.09294  25.63445  1.000 45.72424  ? 109 ARG E NH2 1 
ATOM   5177 N N   . ALA E 5 96  ? 14.26976  9.03445   29.35505  1.000 26.86347  ? 110 ALA E N   1 
ATOM   5178 C CA  . ALA E 5 96  ? 13.78376  7.73100   29.78112  1.000 35.48865  ? 110 ALA E CA  1 
ATOM   5179 C C   . ALA E 5 96  ? 12.49647  7.36126   29.05844  1.000 31.69642  ? 110 ALA E C   1 
ATOM   5180 O O   . ALA E 5 96  ? 11.69574  8.22584   28.68986  1.000 19.90718  ? 110 ALA E O   1 
ATOM   5181 C CB  . ALA E 5 96  ? 13.53905  7.70982   31.29086  1.000 20.31143  ? 110 ALA E CB  1 
ATOM   5182 N N   . GLU E 5 97  ? 12.31169  6.05286   28.85891  1.000 26.96317  ? 111 GLU E N   1 
ATOM   5183 C CA  . GLU E 5 97  ? 11.05338  5.49165   28.36551  1.000 24.97596  ? 111 GLU E CA  1 
ATOM   5184 C C   . GLU E 5 97  ? 10.69054  6.04698   26.98954  1.000 24.51634  ? 111 GLU E C   1 
ATOM   5185 O O   . GLU E 5 97  ? 9.51964   6.28209   26.68021  1.000 22.05580  ? 111 GLU E O   1 
ATOM   5186 C CB  . GLU E 5 97  ? 9.92385   5.72379   29.37360  1.000 21.40610  ? 111 GLU E CB  1 
ATOM   5187 C CG  . GLU E 5 97  ? 10.22301  5.13984   30.75499  1.000 29.35895  ? 111 GLU E CG  1 
ATOM   5188 C CD  . GLU E 5 97  ? 9.08283   5.31567   31.75385  1.000 29.46081  ? 111 GLU E CD  1 
ATOM   5189 O OE1 . GLU E 5 97  ? 7.91707   5.47180   31.33396  1.000 42.63697  ? 111 GLU E OE1 1 
ATOM   5190 O OE2 . GLU E 5 97  ? 9.35951   5.29871   32.96768  1.000 38.20384  ? 111 GLU E OE2 1 
ATOM   5191 N N   . SER E 5 98  ? 11.70443  6.25655   26.15419  1.000 25.13639  ? 112 SER E N   1 
ATOM   5192 C CA  . SER E 5 98  ? 11.48144  6.76330   24.80900  1.000 22.83630  ? 112 SER E CA  1 
ATOM   5193 C C   . SER E 5 98  ? 11.18097  5.61997   23.85065  1.000 25.06780  ? 112 SER E C   1 
ATOM   5194 O O   . SER E 5 98  ? 11.72386  4.51969   23.98374  1.000 24.06595  ? 112 SER E O   1 
ATOM   5195 C CB  . SER E 5 98  ? 12.70295  7.53784   24.32176  1.000 23.52510  ? 112 SER E CB  1 
ATOM   5196 O OG  . SER E 5 98  ? 12.68533  7.67316   22.91162  1.000 28.49460  ? 112 SER E OG  1 
ATOM   5197 N N   . GLY E 5 99  ? 10.29652  5.88324   22.88914  1.000 28.52345  ? 113 GLY E N   1 
ATOM   5198 C CA  . GLY E 5 99  ? 10.04310  4.94744   21.80751  1.000 25.09611  ? 113 GLY E CA  1 
ATOM   5199 C C   . GLY E 5 99  ? 11.00789  5.05165   20.64600  1.000 24.86961  ? 113 GLY E C   1 
ATOM   5200 O O   . GLY E 5 99  ? 11.01938  4.17017   19.78317  1.000 30.03757  ? 113 GLY E O   1 
ATOM   5201 N N   . GLU E 5 100 ? 11.82173  6.10620   20.61425  1.000 25.56597  ? 114 GLU E N   1 
ATOM   5202 C CA  . GLU E 5 100 ? 12.82135  6.32855   19.57187  1.000 31.28452  ? 114 GLU E CA  1 
ATOM   5203 C C   . GLU E 5 100 ? 14.17767  5.90121   20.12446  1.000 29.24359  ? 114 GLU E C   1 
ATOM   5204 O O   . GLU E 5 100 ? 14.84021  6.66057   20.83650  1.000 25.97112  ? 114 GLU E O   1 
ATOM   5205 C CB  . GLU E 5 100 ? 12.81810  7.78936   19.13205  1.000 23.96743  ? 114 GLU E CB  1 
ATOM   5206 C CG  . GLU E 5 100 ? 11.48709  8.22123   18.51743  1.000 46.30086  ? 114 GLU E CG  1 
ATOM   5207 C CD  . GLU E 5 100 ? 11.37712  9.72082   18.28039  1.000 48.66685  ? 114 GLU E CD  1 
ATOM   5208 O OE1 . GLU E 5 100 ? 11.45201  10.49332  19.25898  1.000 46.19543  ? 114 GLU E OE1 1 
ATOM   5209 O OE2 . GLU E 5 100 ? 11.20605  10.12441  17.11120  1.000 53.89961  ? 114 GLU E OE2 1 
ATOM   5210 N N   . LEU E 5 101 ? 14.58811  4.68209   19.78584  1.000 23.82003  ? 115 LEU E N   1 
ATOM   5211 C CA  . LEU E 5 101 ? 15.78899  4.06346   20.32001  1.000 21.33028  ? 115 LEU E CA  1 
ATOM   5212 C C   . LEU E 5 101 ? 16.87743  3.98010   19.25585  1.000 25.82877  ? 115 LEU E C   1 
ATOM   5213 O O   . LEU E 5 101 ? 16.60201  3.81169   18.06447  1.000 30.58838  ? 115 LEU E O   1 
ATOM   5214 C CB  . LEU E 5 101 ? 15.48521  2.65971   20.84839  1.000 21.18772  ? 115 LEU E CB  1 
ATOM   5215 C CG  . LEU E 5 101 ? 14.42893  2.59112   21.94959  1.000 25.75280  ? 115 LEU E CG  1 
ATOM   5216 C CD1 . LEU E 5 101 ? 14.16733  1.14773   22.33839  1.000 28.55811  ? 115 LEU E CD1 1 
ATOM   5217 C CD2 . LEU E 5 101 ? 14.87911  3.40270   23.15641  1.000 23.28100  ? 115 LEU E CD2 1 
ATOM   5218 N N   . PHE E 5 102 ? 18.12271  4.08106   19.70463  1.000 19.89275  ? 116 PHE E N   1 
ATOM   5219 C CA  . PHE E 5 102 ? 19.29383  3.94822   18.84661  1.000 27.71202  ? 116 PHE E CA  1 
ATOM   5220 C C   . PHE E 5 102 ? 20.06552  2.71963   19.30828  1.000 19.01531  ? 116 PHE E C   1 
ATOM   5221 O O   . PHE E 5 102 ? 20.63194  2.71227   20.40669  1.000 20.42624  ? 116 PHE E O   1 
ATOM   5222 C CB  . PHE E 5 102 ? 20.14699  5.21388   18.89693  1.000 28.57232  ? 116 PHE E CB  1 
ATOM   5223 C CG  . PHE E 5 102 ? 19.44563  6.42808   18.35582  1.000 50.01114  ? 116 PHE E CG  1 
ATOM   5224 C CD1 . PHE E 5 102 ? 18.48782  7.09312   19.11366  1.000 44.32652  ? 116 PHE E CD1 1 
ATOM   5225 C CD2 . PHE E 5 102 ? 19.73170  6.89870   17.08300  1.000 56.92921  ? 116 PHE E CD2 1 
ATOM   5226 C CE1 . PHE E 5 102 ? 17.83234  8.20617   18.61157  1.000 49.56725  ? 116 PHE E CE1 1 
ATOM   5227 C CE2 . PHE E 5 102 ? 19.08056  8.01230   16.57608  1.000 60.22207  ? 116 PHE E CE2 1 
ATOM   5228 C CZ  . PHE E 5 102 ? 18.13076  8.66676   17.34184  1.000 50.08842  ? 116 PHE E CZ  1 
ATOM   5229 N N   . PHE E 5 103 ? 20.07362  1.68187   18.47823  1.000 19.95630  ? 117 PHE E N   1 
ATOM   5230 C CA  . PHE E 5 103 ? 20.63190  0.39331   18.85655  1.000 24.07598  ? 117 PHE E CA  1 
ATOM   5231 C C   . PHE E 5 103 ? 22.09908  0.29461   18.46980  1.000 27.72932  ? 117 PHE E C   1 
ATOM   5232 O O   . PHE E 5 103 ? 22.51237  0.79539   17.42197  1.000 33.19791  ? 117 PHE E O   1 
ATOM   5233 C CB  . PHE E 5 103 ? 19.86294  -0.74611  18.18892  1.000 20.70234  ? 117 PHE E CB  1 
ATOM   5234 C CG  . PHE E 5 103 ? 18.54883  -1.06143  18.83698  1.000 22.42732  ? 117 PHE E CG  1 
ATOM   5235 C CD1 . PHE E 5 103 ? 17.38725  -0.42110  18.42674  1.000 25.63786  ? 117 PHE E CD1 1 
ATOM   5236 C CD2 . PHE E 5 103 ? 18.46678  -2.02092  19.83736  1.000 17.74268  ? 117 PHE E CD2 1 
ATOM   5237 C CE1 . PHE E 5 103 ? 16.16751  -0.71946  19.01178  1.000 18.68750  ? 117 PHE E CE1 1 
ATOM   5238 C CE2 . PHE E 5 103 ? 17.25317  -2.31907  20.42981  1.000 18.43487  ? 117 PHE E CE2 1 
ATOM   5239 C CZ  . PHE E 5 103 ? 16.10064  -1.66304  20.01806  1.000 21.30796  ? 117 PHE E CZ  1 
ATOM   5240 N N   . GLY E 5 104 ? 22.88179  -0.36205  19.32557  1.000 29.89991  ? 118 GLY E N   1 
ATOM   5241 C CA  . GLY E 5 104 ? 24.20782  -0.80130  18.95598  1.000 26.17516  ? 118 GLY E CA  1 
ATOM   5242 C C   . GLY E 5 104 ? 24.13919  -2.01564  18.05049  1.000 28.73889  ? 118 GLY E C   1 
ATOM   5243 O O   . GLY E 5 104 ? 23.07257  -2.54951  17.75151  1.000 23.83893  ? 118 GLY E O   1 
ATOM   5244 N N   . GLU E 5 105 ? 25.31114  -2.45946  17.59982  1.000 29.44374  ? 119 GLU E N   1 
ATOM   5245 C CA  . GLU E 5 105 ? 25.36065  -3.60543  16.70052  1.000 32.24071  ? 119 GLU E CA  1 
ATOM   5246 C C   . GLU E 5 105 ? 25.22491  -4.93397  17.42543  1.000 31.59986  ? 119 GLU E C   1 
ATOM   5247 O O   . GLU E 5 105 ? 25.15202  -5.97686  16.76593  1.000 32.75515  ? 119 GLU E O   1 
ATOM   5248 C CB  . GLU E 5 105 ? 26.65527  -3.58631  15.89386  1.000 28.45225  ? 119 GLU E CB  1 
ATOM   5249 C CG  . GLU E 5 105 ? 26.65415  -2.55134  14.79701  1.000 42.86525  ? 119 GLU E CG  1 
ATOM   5250 C CD  . GLU E 5 105 ? 27.96497  -2.50938  14.04272  1.000 60.39552  ? 119 GLU E CD  1 
ATOM   5251 O OE1 . GLU E 5 105 ? 29.02986  -2.62690  14.69113  1.000 65.24959  ? 119 GLU E OE1 1 
ATOM   5252 O OE2 . GLU E 5 105 ? 27.92836  -2.36500  12.80092  1.000 58.42453  ? 119 GLU E OE2 1 
ATOM   5253 N N   . GLY E 5 106 ? 25.20254  -4.92254  18.75088  1.000 25.64975  ? 120 GLY E N   1 
ATOM   5254 C CA  . GLY E 5 106 ? 24.93172  -6.11540  19.51928  1.000 25.75856  ? 120 GLY E CA  1 
ATOM   5255 C C   . GLY E 5 106 ? 26.18516  -6.88422  19.90352  1.000 34.30060  ? 120 GLY E C   1 
ATOM   5256 O O   . GLY E 5 106 ? 27.24581  -6.76657  19.29160  1.000 32.51922  ? 120 GLY E O   1 
ATOM   5257 N N   . SER E 5 107 ? 26.04109  -7.67586  20.96110  1.000 25.90957  ? 121 SER E N   1 
ATOM   5258 C CA  . SER E 5 107 ? 27.01530  -8.67837  21.36403  1.000 25.60468  ? 121 SER E CA  1 
ATOM   5259 C C   . SER E 5 107 ? 26.44724  -10.04594 21.01480  1.000 26.69288  ? 121 SER E C   1 
ATOM   5260 O O   . SER E 5 107 ? 25.38823  -10.42656 21.52559  1.000 32.97196  ? 121 SER E O   1 
ATOM   5261 C CB  . SER E 5 107 ? 27.30666  -8.58829  22.86236  1.000 23.77496  ? 121 SER E CB  1 
ATOM   5262 O OG  . SER E 5 107 ? 28.00387  -7.40017  23.17663  1.000 29.66492  ? 121 SER E OG  1 
ATOM   5263 N N   . ARG E 5 108 ? 27.13838  -10.77828 20.14894  1.000 26.45088  ? 122 ARG E N   1 
ATOM   5264 C CA  . ARG E 5 108 ? 26.67765  -12.10030 19.72920  1.000 32.61665  ? 122 ARG E CA  1 
ATOM   5265 C C   . ARG E 5 108 ? 27.28535  -13.12088 20.68208  1.000 29.93115  ? 122 ARG E C   1 
ATOM   5266 O O   . ARG E 5 108 ? 28.46884  -13.45938 20.58595  1.000 27.91506  ? 122 ARG E O   1 
ATOM   5267 C CB  . ARG E 5 108 ? 27.04538  -12.37874 18.27518  1.000 22.93970  ? 122 ARG E CB  1 
ATOM   5268 C CG  . ARG E 5 108 ? 26.27773  -13.54749 17.65916  1.000 36.80276  ? 122 ARG E CG  1 
ATOM   5269 C CD  . ARG E 5 108 ? 26.22428  -13.46663 16.12252  1.000 44.62020  ? 122 ARG E CD  1 
ATOM   5270 N NE  . ARG E 5 108 ? 25.29981  -12.45213 15.62134  1.000 51.56113  ? 122 ARG E NE  1 
ATOM   5271 C CZ  . ARG E 5 108 ? 23.97726  -12.57915 15.60011  1.000 64.25298  ? 122 ARG E CZ  1 
ATOM   5272 N NH1 . ARG E 5 108 ? 23.37433  -13.64911 16.09818  1.000 49.54346  ? 122 ARG E NH1 1 
ATOM   5273 N NH2 . ARG E 5 108 ? 23.23906  -11.60347 15.07496  1.000 60.74187  ? 122 ARG E NH2 1 
ATOM   5274 N N   . LEU E 5 109 ? 26.46978  -13.60118 21.61285  1.000 23.14038  ? 123 LEU E N   1 
ATOM   5275 C CA  . LEU E 5 109 ? 26.90240  -14.52993 22.64582  1.000 29.04156  ? 123 LEU E CA  1 
ATOM   5276 C C   . LEU E 5 109 ? 26.43594  -15.93211 22.28222  1.000 28.65868  ? 123 LEU E C   1 
ATOM   5277 O O   . LEU E 5 109 ? 25.23143  -16.18555 22.17899  1.000 27.15929  ? 123 LEU E O   1 
ATOM   5278 C CB  . LEU E 5 109 ? 26.34920  -14.12276 24.01114  1.000 25.54708  ? 123 LEU E CB  1 
ATOM   5279 C CG  . LEU E 5 109 ? 26.52597  -15.14296 25.14282  1.000 20.12839  ? 123 LEU E CG  1 
ATOM   5280 C CD1 . LEU E 5 109 ? 27.99059  -15.35321 25.44274  1.000 19.23724  ? 123 LEU E CD1 1 
ATOM   5281 C CD2 . LEU E 5 109 ? 25.79106  -14.68662 26.38666  1.000 23.23764  ? 123 LEU E CD2 1 
ATOM   5282 N N   . THR E 5 110 ? 27.38607  -16.83395 22.08755  1.000 29.29064  ? 124 THR E N   1 
ATOM   5283 C CA  . THR E 5 110 ? 27.09879  -18.24478 21.88820  1.000 27.95276  ? 124 THR E CA  1 
ATOM   5284 C C   . THR E 5 110 ? 27.54756  -18.98465 23.13874  1.000 26.64033  ? 124 THR E C   1 
ATOM   5285 O O   . THR E 5 110 ? 28.71709  -18.89551 23.53104  1.000 27.58845  ? 124 THR E O   1 
ATOM   5286 C CB  . THR E 5 110 ? 27.80116  -18.78745 20.64089  1.000 31.83055  ? 124 THR E CB  1 
ATOM   5287 O OG1 . THR E 5 110 ? 27.26264  -18.15373 19.47414  1.000 33.31665  ? 124 THR E OG1 1 
ATOM   5288 C CG2 . THR E 5 110 ? 27.59998  -20.28800 20.52550  1.000 30.17851  ? 124 THR E CG2 1 
ATOM   5289 N N   . VAL E 5 111 ? 26.61461  -19.68212 23.77544  1.000 25.80401  ? 125 VAL E N   1 
ATOM   5290 C CA  . VAL E 5 111 ? 26.89566  -20.47936 24.96129  1.000 28.94047  ? 125 VAL E CA  1 
ATOM   5291 C C   . VAL E 5 111 ? 26.93875  -21.93907 24.53593  1.000 33.28228  ? 125 VAL E C   1 
ATOM   5292 O O   . VAL E 5 111 ? 25.98781  -22.44346 23.92691  1.000 26.77856  ? 125 VAL E O   1 
ATOM   5293 C CB  . VAL E 5 111 ? 25.84265  -20.25107 26.05466  1.000 31.08164  ? 125 VAL E CB  1 
ATOM   5294 C CG1 . VAL E 5 111 ? 26.21014  -21.02543 27.30852  1.000 19.64612  ? 125 VAL E CG1 1 
ATOM   5295 C CG2 . VAL E 5 111 ? 25.69939  -18.76342 26.34438  1.000 27.97422  ? 125 VAL E CG2 1 
ATOM   5296 N N   . LEU E 5 112 ? 28.03837  -22.61748 24.85149  1.000 31.90524  ? 126 LEU E N   1 
ATOM   5297 C CA  . LEU E 5 112 ? 28.25095  -23.99972 24.45609  1.000 31.22947  ? 126 LEU E CA  1 
ATOM   5298 C C   . LEU E 5 112 ? 28.39135  -24.88561 25.68647  1.000 26.77079  ? 126 LEU E C   1 
ATOM   5299 O O   . LEU E 5 112 ? 28.74885  -24.42872 26.77340  1.000 29.97271  ? 126 LEU E O   1 
ATOM   5300 C CB  . LEU E 5 112 ? 29.50248  -24.13243 23.57924  1.000 29.10227  ? 126 LEU E CB  1 
ATOM   5301 C CG  . LEU E 5 112 ? 29.48867  -23.33563 22.27728  1.000 32.05957  ? 126 LEU E CG  1 
ATOM   5302 C CD1 . LEU E 5 112 ? 30.77069  -23.57299 21.49142  1.000 28.94731  ? 126 LEU E CD1 1 
ATOM   5303 C CD2 . LEU E 5 112 ? 28.25963  -23.70173 21.44980  1.000 30.08896  ? 126 LEU E CD2 1 
ATOM   5304 N N   . GLU E 5 113 ? 28.10527  -26.17257 25.51081  1.000 32.09808  ? 127 GLU E N   1 
ATOM   5305 C CA  . GLU E 5 113 ? 28.43644  -27.11696 26.56731  1.000 29.45778  ? 127 GLU E CA  1 
ATOM   5306 C C   . GLU E 5 113 ? 29.93612  -27.37108 26.64546  1.000 33.08118  ? 127 GLU E C   1 
ATOM   5307 O O   . GLU E 5 113 ? 30.44761  -27.67720 27.72673  1.000 34.75736  ? 127 GLU E O   1 
ATOM   5308 C CB  . GLU E 5 113 ? 27.69998  -28.43812 26.35118  1.000 27.30515  ? 127 GLU E CB  1 
ATOM   5309 C CG  . GLU E 5 113 ? 27.87259  -29.42822 27.49173  1.000 25.12847  ? 127 GLU E CG  1 
ATOM   5310 C CD  . GLU E 5 113 ? 27.32618  -28.89195 28.80166  1.000 44.93505  ? 127 GLU E CD  1 
ATOM   5311 O OE1 . GLU E 5 113 ? 26.14878  -28.46937 28.82542  1.000 47.55694  ? 127 GLU E OE1 1 
ATOM   5312 O OE2 . GLU E 5 113 ? 28.07706  -28.87721 29.80258  1.000 54.50431  ? 127 GLU E OE2 1 
ATOM   5313 N N   . ASP E 5 114 ? 30.65253  -27.20181 25.53649  1.000 38.23362  ? 128 ASP E N   1 
ATOM   5314 C CA  . ASP E 5 114 ? 32.01331  -27.69810 25.40730  1.000 38.92807  ? 128 ASP E CA  1 
ATOM   5315 C C   . ASP E 5 114 ? 32.71505  -26.94698 24.28221  1.000 35.64560  ? 128 ASP E C   1 
ATOM   5316 O O   . ASP E 5 114 ? 32.12116  -26.70241 23.23115  1.000 45.56239  ? 128 ASP E O   1 
ATOM   5317 C CB  . ASP E 5 114 ? 31.98883  -29.20685 25.13016  1.000 43.32357  ? 128 ASP E CB  1 
ATOM   5318 C CG  . ASP E 5 114 ? 33.35806  -29.78108 24.87443  1.000 53.88915  ? 128 ASP E CG  1 
ATOM   5319 O OD1 . ASP E 5 114 ? 34.36219  -29.15232 25.27105  1.000 51.22050  ? 128 ASP E OD1 1 
ATOM   5320 O OD2 . ASP E 5 114 ? 33.42724  -30.87105 24.26839  1.000 73.68125  ? 128 ASP E OD2 1 
ATOM   5321 N N   . LEU E 5 115 ? 33.98153  -26.59885 24.50292  1.000 42.23561  ? 129 LEU E N   1 
ATOM   5322 C CA  . LEU E 5 115 ? 34.75395  -25.84366 23.52344  1.000 31.76220  ? 129 LEU E CA  1 
ATOM   5323 C C   . LEU E 5 115 ? 35.49139  -26.72185 22.52165  1.000 41.94705  ? 129 LEU E C   1 
ATOM   5324 O O   . LEU E 5 115 ? 36.07520  -26.18788 21.57186  1.000 42.29212  ? 129 LEU E O   1 
ATOM   5325 C CB  . LEU E 5 115 ? 35.76453  -24.93166 24.22943  1.000 30.57718  ? 129 LEU E CB  1 
ATOM   5326 C CG  . LEU E 5 115 ? 35.14507  -23.87066 25.14076  1.000 32.04154  ? 129 LEU E CG  1 
ATOM   5327 C CD1 . LEU E 5 115 ? 36.21828  -23.01008 25.78623  1.000 29.19027  ? 129 LEU E CD1 1 
ATOM   5328 C CD2 . LEU E 5 115 ? 34.15869  -23.00826 24.36928  1.000 31.01977  ? 129 LEU E CD2 1 
ATOM   5329 N N   . ASN E 5 116 ? 35.48957  -28.04417 22.70585  1.000 42.80400  ? 130 ASN E N   1 
ATOM   5330 C CA  . ASN E 5 116 ? 36.07847  -28.93891 21.71676  1.000 49.25614  ? 130 ASN E CA  1 
ATOM   5331 C C   . ASN E 5 116 ? 35.32953  -28.91746 20.39277  1.000 46.94073  ? 130 ASN E C   1 
ATOM   5332 O O   . ASN E 5 116 ? 35.79617  -29.52267 19.42217  1.000 53.22139  ? 130 ASN E O   1 
ATOM   5333 C CB  . ASN E 5 116 ? 36.11352  -30.37070 22.24897  1.000 61.45006  ? 130 ASN E CB  1 
ATOM   5334 C CG  . ASN E 5 116 ? 36.70128  -30.45913 23.63715  1.000 68.08308  ? 130 ASN E CG  1 
ATOM   5335 O OD1 . ASN E 5 116 ? 36.16831  -31.15203 24.50368  1.000 68.94964  ? 130 ASN E OD1 1 
ATOM   5336 N ND2 . ASN E 5 116 ? 37.80525  -29.75092 23.86135  1.000 65.99420  ? 130 ASN E ND2 1 
ATOM   5337 N N   . LYS E 5 117 ? 34.18389  -28.24923 20.33328  1.000 46.07485  ? 131 LYS E N   1 
ATOM   5338 C CA  . LYS E 5 117 ? 33.38065  -28.17210 19.12665  1.000 43.26847  ? 131 LYS E CA  1 
ATOM   5339 C C   . LYS E 5 117 ? 33.68225  -26.93387 18.29095  1.000 43.51614  ? 131 LYS E C   1 
ATOM   5340 O O   . LYS E 5 117 ? 33.08320  -26.76422 17.22530  1.000 44.51583  ? 131 LYS E O   1 
ATOM   5341 C CB  . LYS E 5 117 ? 31.89335  -28.20616 19.50016  1.000 57.79999  ? 131 LYS E CB  1 
ATOM   5342 C CG  . LYS E 5 117 ? 31.46906  -29.48014 20.22956  1.000 53.06475  ? 131 LYS E CG  1 
ATOM   5343 C CD  . LYS E 5 117 ? 30.69906  -29.17318 21.50756  1.000 59.06631  ? 131 LYS E CD  1 
ATOM   5344 C CE  . LYS E 5 117 ? 29.34144  -28.52832 21.22496  1.000 67.51619  ? 131 LYS E CE  1 
ATOM   5345 N NZ  . LYS E 5 117 ? 28.60627  -28.16706 22.48834  1.000 37.96841  ? 131 LYS E NZ  1 
ATOM   5346 N N   . VAL E 5 118 ? 34.59734  -26.07514 18.73690  1.000 36.55488  ? 132 VAL E N   1 
ATOM   5347 C CA  . VAL E 5 118 ? 34.87315  -24.80801 18.06800  1.000 43.12194  ? 132 VAL E CA  1 
ATOM   5348 C C   . VAL E 5 118 ? 35.93966  -25.02302 16.99731  1.000 33.48330  ? 132 VAL E C   1 
ATOM   5349 O O   . VAL E 5 118 ? 37.01695  -25.56239 17.27883  1.000 39.86961  ? 132 VAL E O   1 
ATOM   5350 C CB  . VAL E 5 118 ? 35.31023  -23.73949 19.08622  1.000 31.46913  ? 132 VAL E CB  1 
ATOM   5351 C CG1 . VAL E 5 118 ? 35.53648  -22.40002 18.40123  1.000 28.83339  ? 132 VAL E CG1 1 
ATOM   5352 C CG2 . VAL E 5 118 ? 34.26801  -23.60145 20.18236  1.000 25.48411  ? 132 VAL E CG2 1 
ATOM   5353 N N   . PHE E 5 119 ? 35.64163  -24.59125 15.76412  1.000 28.96990  ? 133 PHE E N   1 
ATOM   5354 C CA  . PHE E 5 119 ? 36.54227  -24.75472 14.60956  1.000 45.90785  ? 133 PHE E CA  1 
ATOM   5355 C C   . PHE E 5 119 ? 36.57362  -23.47639 13.77897  1.000 33.93789  ? 133 PHE E C   1 
ATOM   5356 O O   . PHE E 5 119 ? 35.50849  -22.90099 13.48803  1.000 30.86396  ? 133 PHE E O   1 
ATOM   5357 C CB  . PHE E 5 119 ? 36.12297  -25.92197 13.71118  1.000 35.53637  ? 133 PHE E CB  1 
ATOM   5358 C CG  . PHE E 5 119 ? 36.29381  -27.26910 14.33886  1.000 39.31073  ? 133 PHE E CG  1 
ATOM   5359 C CD1 . PHE E 5 119 ? 37.47728  -27.96941 14.19208  1.000 39.20609  ? 133 PHE E CD1 1 
ATOM   5360 C CD2 . PHE E 5 119 ? 35.26573  -27.84486 15.06268  1.000 37.48619  ? 133 PHE E CD2 1 
ATOM   5361 C CE1 . PHE E 5 119 ? 37.63704  -29.21857 14.76413  1.000 44.64111  ? 133 PHE E CE1 1 
ATOM   5362 C CE2 . PHE E 5 119 ? 35.41823  -29.09182 15.63716  1.000 51.47879  ? 133 PHE E CE2 1 
ATOM   5363 C CZ  . PHE E 5 119 ? 36.60640  -29.78001 15.48937  1.000 42.45261  ? 133 PHE E CZ  1 
ATOM   5364 N N   . PRO E 5 120 ? 37.75036  -23.02155 13.36408  1.000 35.84018  ? 134 PRO E N   1 
ATOM   5365 C CA  . PRO E 5 120 ? 37.82251  -21.92536 12.39891  1.000 33.55950  ? 134 PRO E CA  1 
ATOM   5366 C C   . PRO E 5 120 ? 37.43156  -22.41324 11.01612  1.000 36.97883  ? 134 PRO E C   1 
ATOM   5367 O O   . PRO E 5 120 ? 37.40017  -23.62668 10.76419  1.000 30.81817  ? 134 PRO E O   1 
ATOM   5368 C CB  . PRO E 5 120 ? 39.30003  -21.51016 12.45094  1.000 26.14859  ? 134 PRO E CB  1 
ATOM   5369 C CG  . PRO E 5 120 ? 40.00611  -22.76466 12.81165  1.000 33.81138  ? 134 PRO E CG  1 
ATOM   5370 C CD  . PRO E 5 120 ? 39.08713  -23.50170 13.75258  1.000 32.09253  ? 134 PRO E CD  1 
ATOM   5371 N N   . PRO E 5 121 ? 37.10920  -21.50977 10.09728  1.000 36.62894  ? 135 PRO E N   1 
ATOM   5372 C CA  . PRO E 5 121 ? 36.75451  -21.93721 8.74401   1.000 40.41961  ? 135 PRO E CA  1 
ATOM   5373 C C   . PRO E 5 121 ? 37.97873  -22.21948 7.88848   1.000 38.58130  ? 135 PRO E C   1 
ATOM   5374 O O   . PRO E 5 121 ? 39.06226  -21.66877 8.09411   1.000 39.91591  ? 135 PRO E O   1 
ATOM   5375 C CB  . PRO E 5 121 ? 35.97964  -20.73459 8.19714   1.000 34.39617  ? 135 PRO E CB  1 
ATOM   5376 C CG  . PRO E 5 121 ? 36.62473  -19.57827 8.87538   1.000 29.95112  ? 135 PRO E CG  1 
ATOM   5377 C CD  . PRO E 5 121 ? 36.92177  -20.05971 10.27483  1.000 32.54631  ? 135 PRO E CD  1 
ATOM   5378 N N   . GLU E 5 122 ? 37.78879  -23.10170 6.91774   1.000 35.27197  ? 136 GLU E N   1 
ATOM   5379 C CA  . GLU E 5 122 ? 38.70677  -23.23415 5.79821   1.000 37.47653  ? 136 GLU E CA  1 
ATOM   5380 C C   . GLU E 5 122 ? 38.12513  -22.44844 4.63335   1.000 36.76346  ? 136 GLU E C   1 
ATOM   5381 O O   . GLU E 5 122 ? 36.92719  -22.54992 4.35222   1.000 42.34523  ? 136 GLU E O   1 
ATOM   5382 C CB  . GLU E 5 122 ? 38.91133  -24.69869 5.41734   1.000 37.60048  ? 136 GLU E CB  1 
ATOM   5383 C CG  . GLU E 5 122 ? 39.43538  -25.55774 6.55087   1.000 58.97728  ? 136 GLU E CG  1 
ATOM   5384 C CD  . GLU E 5 122 ? 40.35278  -26.65911 6.06604   1.000 72.46253  ? 136 GLU E CD  1 
ATOM   5385 O OE1 . GLU E 5 122 ? 41.51292  -26.35573 5.71507   1.000 88.29568  ? 136 GLU E OE1 1 
ATOM   5386 O OE2 . GLU E 5 122 ? 39.91124  -27.82597 6.02584   1.000 77.73864  ? 136 GLU E OE2 1 
ATOM   5387 N N   . VAL E 5 123 ? 38.95728  -21.64744 3.97756   1.000 35.77511  ? 137 VAL E N   1 
ATOM   5388 C CA  . VAL E 5 123 ? 38.49511  -20.72916 2.94634   1.000 42.07268  ? 137 VAL E CA  1 
ATOM   5389 C C   . VAL E 5 123 ? 39.17412  -21.07832 1.62990   1.000 40.55747  ? 137 VAL E C   1 
ATOM   5390 O O   . VAL E 5 123 ? 40.39712  -21.24653 1.57897   1.000 42.86066  ? 137 VAL E O   1 
ATOM   5391 C CB  . VAL E 5 123 ? 38.75791  -19.26524 3.33734   1.000 29.13768  ? 137 VAL E CB  1 
ATOM   5392 C CG1 . VAL E 5 123 ? 38.18314  -18.33410 2.28891   1.000 29.86665  ? 137 VAL E CG1 1 
ATOM   5393 C CG2 . VAL E 5 123 ? 38.13950  -18.97801 4.69068   1.000 41.33910  ? 137 VAL E CG2 1 
ATOM   5394 N N   . ALA E 5 124 ? 38.37722  -21.18945 0.57013   1.000 43.21877  ? 138 ALA E N   1 
ATOM   5395 C CA  . ALA E 5 124 ? 38.87946  -21.47763 -0.76432  1.000 44.94397  ? 138 ALA E CA  1 
ATOM   5396 C C   . ALA E 5 124 ? 38.22862  -20.52842 -1.75630  1.000 41.17688  ? 138 ALA E C   1 
ATOM   5397 O O   . ALA E 5 124 ? 37.05238  -20.18044 -1.61459  1.000 43.49471  ? 138 ALA E O   1 
ATOM   5398 C CB  . ALA E 5 124 ? 38.60157  -22.93034 -1.17294  1.000 32.64307  ? 138 ALA E CB  1 
ATOM   5399 N N   . VAL E 5 125 ? 39.00115  -20.10769 -2.75292  1.000 44.37265  ? 139 VAL E N   1 
ATOM   5400 C CA  . VAL E 5 125 ? 38.51054  -19.28143 -3.84967  1.000 51.62939  ? 139 VAL E CA  1 
ATOM   5401 C C   . VAL E 5 125 ? 38.51565  -20.12148 -5.11946  1.000 47.19523  ? 139 VAL E C   1 
ATOM   5402 O O   . VAL E 5 125 ? 39.52834  -20.74682 -5.45460  1.000 50.60098  ? 139 VAL E O   1 
ATOM   5403 C CB  . VAL E 5 125 ? 39.35874  -18.00963 -4.02230  1.000 49.88809  ? 139 VAL E CB  1 
ATOM   5404 C CG1 . VAL E 5 125 ? 39.00939  -17.31017 -5.32680  1.000 46.72418  ? 139 VAL E CG1 1 
ATOM   5405 C CG2 . VAL E 5 125 ? 39.14368  -17.07420 -2.84477  1.000 45.35197  ? 139 VAL E CG2 1 
ATOM   5406 N N   . PHE E 5 126 ? 37.38714  -20.13618 -5.82159  1.000 47.05778  ? 140 PHE E N   1 
ATOM   5407 C CA  . PHE E 5 126 ? 37.23372  -20.87857 -7.06598  1.000 41.55502  ? 140 PHE E CA  1 
ATOM   5408 C C   . PHE E 5 126 ? 37.19883  -19.89256 -8.22692  1.000 51.95882  ? 140 PHE E C   1 
ATOM   5409 O O   . PHE E 5 126 ? 36.38030  -18.96700 -8.23758  1.000 51.10908  ? 140 PHE E O   1 
ATOM   5410 C CB  . PHE E 5 126 ? 35.97356  -21.74231 -7.02408  1.000 38.71287  ? 140 PHE E CB  1 
ATOM   5411 C CG  . PHE E 5 126 ? 35.98083  -22.74881 -5.90853  1.000 53.56445  ? 140 PHE E CG  1 
ATOM   5412 C CD1 . PHE E 5 126 ? 35.53322  -22.40449 -4.64252  1.000 55.59221  ? 140 PHE E CD1 1 
ATOM   5413 C CD2 . PHE E 5 126 ? 36.45973  -24.03170 -6.11804  1.000 52.52447  ? 140 PHE E CD2 1 
ATOM   5414 C CE1 . PHE E 5 126 ? 35.55116  -23.32386 -3.61171  1.000 51.38154  ? 140 PHE E CE1 1 
ATOM   5415 C CE2 . PHE E 5 126 ? 36.48132  -24.95515 -5.08942  1.000 52.67264  ? 140 PHE E CE2 1 
ATOM   5416 C CZ  . PHE E 5 126 ? 36.02594  -24.60086 -3.83475  1.000 48.83052  ? 140 PHE E CZ  1 
ATOM   5417 N N   . GLU E 5 127 ? 38.08959  -20.09197 -9.19557  1.000 56.41866  ? 141 GLU E N   1 
ATOM   5418 C CA  . GLU E 5 127 ? 38.25794  -19.13814 -10.27572 1.000 57.22339  ? 141 GLU E CA  1 
ATOM   5419 C C   . GLU E 5 127 ? 37.10221  -19.23549 -11.27049 1.000 50.68886  ? 141 GLU E C   1 
ATOM   5420 O O   . GLU E 5 127 ? 36.44554  -20.27324 -11.37593 1.000 56.60482  ? 141 GLU E O   1 
ATOM   5421 C CB  . GLU E 5 127 ? 39.59456  -19.37306 -10.97362 1.000 58.70092  ? 141 GLU E CB  1 
ATOM   5422 C CG  . GLU E 5 127 ? 40.79855  -19.14135 -10.06569 1.000 55.70690  ? 141 GLU E CG  1 
ATOM   5423 C CD  . GLU E 5 127 ? 42.12144  -19.21396 -10.80634 1.000 64.92548  ? 141 GLU E CD  1 
ATOM   5424 O OE1 . GLU E 5 127 ? 42.15020  -19.76510 -11.92932 1.000 71.80982  ? 141 GLU E OE1 1 
ATOM   5425 O OE2 . GLU E 5 127 ? 43.12989  -18.71088 -10.26546 1.000 60.90099  ? 141 GLU E OE2 1 
ATOM   5426 N N   . PRO E 5 128 ? 36.82475  -18.15248 -11.99830 1.000 46.22631  ? 142 PRO E N   1 
ATOM   5427 C CA  . PRO E 5 128 ? 35.67850  -18.15067 -12.91722 1.000 53.30600  ? 142 PRO E CA  1 
ATOM   5428 C C   . PRO E 5 128 ? 35.80024  -19.20740 -14.00410 1.000 61.14394  ? 142 PRO E C   1 
ATOM   5429 O O   . PRO E 5 128 ? 36.89642  -19.62448 -14.38465 1.000 53.93101  ? 142 PRO E O   1 
ATOM   5430 C CB  . PRO E 5 128 ? 35.70691  -16.73941 -13.51650 1.000 51.31859  ? 142 PRO E CB  1 
ATOM   5431 C CG  . PRO E 5 128 ? 36.40907  -15.90983 -12.49228 1.000 55.71484  ? 142 PRO E CG  1 
ATOM   5432 C CD  . PRO E 5 128 ? 37.42633  -16.81483 -11.85833 1.000 50.58605  ? 142 PRO E CD  1 
ATOM   5433 N N   . SER E 5 129 ? 34.64597  -19.63075 -14.51035 1.000 53.47205  ? 143 SER E N   1 
ATOM   5434 C CA  . SER E 5 129 ? 34.59724  -20.57977 -15.61329 1.000 59.63528  ? 143 SER E CA  1 
ATOM   5435 C C   . SER E 5 129 ? 34.91468  -19.87911 -16.92924 1.000 65.01628  ? 143 SER E C   1 
ATOM   5436 O O   . SER E 5 129 ? 34.39590  -18.79160 -17.20498 1.000 59.59586  ? 143 SER E O   1 
ATOM   5437 C CB  . SER E 5 129 ? 33.21893  -21.23682 -15.68782 1.000 62.08168  ? 143 SER E CB  1 
ATOM   5438 O OG  . SER E 5 129 ? 32.95418  -21.71538 -16.99656 1.000 64.09575  ? 143 SER E OG  1 
ATOM   5439 N N   . GLU E 5 130 ? 35.77414  -20.50193 -17.74184 1.000 62.00327  ? 144 GLU E N   1 
ATOM   5440 C CA  . GLU E 5 130 ? 36.02680  -19.96864 -19.07667 1.000 57.42372  ? 144 GLU E CA  1 
ATOM   5441 C C   . GLU E 5 130 ? 34.75127  -19.94781 -19.90489 1.000 57.08323  ? 144 GLU E C   1 
ATOM   5442 O O   . GLU E 5 130 ? 34.55661  -19.04488 -20.72674 1.000 63.37087  ? 144 GLU E O   1 
ATOM   5443 C CB  . GLU E 5 130 ? 37.10947  -20.78698 -19.78224 1.000 66.24260  ? 144 GLU E CB  1 
ATOM   5444 N N   . ALA E 5 131 ? 33.86389  -20.92092 -19.68526 1.000 51.98064  ? 145 ALA E N   1 
ATOM   5445 C CA  . ALA E 5 131 ? 32.57819  -20.92175 -20.37111 1.000 48.30524  ? 145 ALA E CA  1 
ATOM   5446 C C   . ALA E 5 131 ? 31.75733  -19.69121 -20.00892 1.000 63.71939  ? 145 ALA E C   1 
ATOM   5447 O O   . ALA E 5 131 ? 31.15059  -19.06406 -20.88469 1.000 72.18823  ? 145 ALA E O   1 
ATOM   5448 C CB  . ALA E 5 131 ? 31.80998  -22.19786 -20.03627 1.000 50.19305  ? 145 ALA E CB  1 
ATOM   5449 N N   . GLU E 5 132 ? 31.72119  -19.33013 -18.72212 1.000 60.97896  ? 146 GLU E N   1 
ATOM   5450 C CA  . GLU E 5 132 ? 30.98772  -18.13346 -18.32391 1.000 58.97646  ? 146 GLU E CA  1 
ATOM   5451 C C   . GLU E 5 132 ? 31.60949  -16.88216 -18.92556 1.000 50.79274  ? 146 GLU E C   1 
ATOM   5452 O O   . GLU E 5 132 ? 30.89174  -15.97225 -19.35680 1.000 56.36553  ? 146 GLU E O   1 
ATOM   5453 C CB  . GLU E 5 132 ? 30.93744  -18.00938 -16.80161 1.000 53.86022  ? 146 GLU E CB  1 
ATOM   5454 C CG  . GLU E 5 132 ? 30.13075  -16.79962 -16.34128 1.000 53.59336  ? 146 GLU E CG  1 
ATOM   5455 C CD  . GLU E 5 132 ? 30.50737  -16.30634 -14.95357 1.000 65.52149  ? 146 GLU E CD  1 
ATOM   5456 O OE1 . GLU E 5 132 ? 31.43698  -16.87210 -14.33433 1.000 59.90607  ? 146 GLU E OE1 1 
ATOM   5457 O OE2 . GLU E 5 132 ? 29.86799  -15.33968 -14.48442 1.000 54.78350  ? 146 GLU E OE2 1 
ATOM   5458 N N   . ILE E 5 133 ? 32.94227  -16.81687 -18.95770 1.000 53.63944  ? 147 ILE E N   1 
ATOM   5459 C CA  . ILE E 5 133 ? 33.61112  -15.63286 -19.48363 1.000 58.32112  ? 147 ILE E CA  1 
ATOM   5460 C C   . ILE E 5 133 ? 33.32717  -15.46813 -20.97038 1.000 66.70218  ? 147 ILE E C   1 
ATOM   5461 O O   . ILE E 5 133 ? 33.28232  -14.34171 -21.47918 1.000 78.47745  ? 147 ILE E O   1 
ATOM   5462 C CB  . ILE E 5 133 ? 35.12268  -15.70202 -19.20044 1.000 57.87759  ? 147 ILE E CB  1 
ATOM   5463 N N   . SER E 5 134 ? 33.11772  -16.57157 -21.68852 1.000 70.24772  ? 148 SER E N   1 
ATOM   5464 C CA  . SER E 5 134 ? 32.80754  -16.50699 -23.11181 1.000 66.64615  ? 148 SER E CA  1 
ATOM   5465 C C   . SER E 5 134 ? 31.32449  -16.27981 -23.37826 1.000 68.19622  ? 148 SER E C   1 
ATOM   5466 O O   . SER E 5 134 ? 30.96894  -15.49118 -24.26081 1.000 73.23538  ? 148 SER E O   1 
ATOM   5467 C CB  . SER E 5 134 ? 33.26075  -17.79100 -23.81157 1.000 69.39015  ? 148 SER E CB  1 
ATOM   5468 O OG  . SER E 5 134 ? 34.67032  -17.83308 -23.94225 1.000 78.56201  ? 148 SER E OG  1 
ATOM   5469 N N   . HIS E 5 135 ? 30.44989  -16.95478 -22.63089 1.000 64.69049  ? 149 HIS E N   1 
ATOM   5470 C CA  . HIS E 5 135 ? 29.01934  -16.88945 -22.90812 1.000 64.69681  ? 149 HIS E CA  1 
ATOM   5471 C C   . HIS E 5 135 ? 28.39431  -15.58124 -22.43483 1.000 62.18218  ? 149 HIS E C   1 
ATOM   5472 O O   . HIS E 5 135 ? 27.39590  -15.13702 -23.01385 1.000 55.24409  ? 149 HIS E O   1 
ATOM   5473 C CB  . HIS E 5 135 ? 28.31727  -18.08911 -22.26099 1.000 68.06986  ? 149 HIS E CB  1 
ATOM   5474 C CG  . HIS E 5 135 ? 26.84067  -18.15328 -22.51546 1.000 68.12587  ? 149 HIS E CG  1 
ATOM   5475 N ND1 . HIS E 5 135 ? 26.20142  -17.35360 -23.43854 1.000 82.57110  ? 149 HIS E ND1 1 
ATOM   5476 C CD2 . HIS E 5 135 ? 25.87756  -18.92867 -21.96155 1.000 74.73276  ? 149 HIS E CD2 1 
ATOM   5477 C CE1 . HIS E 5 135 ? 24.90931  -17.63078 -23.43991 1.000 88.76969  ? 149 HIS E CE1 1 
ATOM   5478 N NE2 . HIS E 5 135 ? 24.68648  -18.58297 -22.55207 1.000 70.90497  ? 149 HIS E NE2 1 
ATOM   5479 N N   . THR E 5 136 ? 28.95831  -14.94770 -21.40191 1.000 56.49994  ? 150 THR E N   1 
ATOM   5480 C CA  . THR E 5 136 ? 28.34448  -13.77197 -20.79535 1.000 50.78521  ? 150 THR E CA  1 
ATOM   5481 C C   . THR E 5 136 ? 29.24794  -12.55071 -20.72138 1.000 49.19050  ? 150 THR E C   1 
ATOM   5482 O O   . THR E 5 136 ? 28.76123  -11.47711 -20.35101 1.000 54.41892  ? 150 THR E O   1 
ATOM   5483 C CB  . THR E 5 136 ? 27.86352  -14.09052 -19.37077 1.000 55.32206  ? 150 THR E CB  1 
ATOM   5484 O OG1 . THR E 5 136 ? 28.99821  -14.34130 -18.53175 1.000 55.48615  ? 150 THR E OG1 1 
ATOM   5485 C CG2 . THR E 5 136 ? 26.95003  -15.31276 -19.36774 1.000 51.07639  ? 150 THR E CG2 1 
ATOM   5486 N N   . GLN E 5 137 ? 30.53561  -12.67522 -21.04282 1.000 60.72733  ? 151 GLN E N   1 
ATOM   5487 C CA  . GLN E 5 137 ? 31.50790  -11.59688 -20.85738 1.000 60.50584  ? 151 GLN E CA  1 
ATOM   5488 C C   . GLN E 5 137 ? 31.55667  -11.12972 -19.40264 1.000 67.21862  ? 151 GLN E C   1 
ATOM   5489 O O   . GLN E 5 137 ? 31.87703  -9.97304  -19.11730 1.000 67.40159  ? 151 GLN E O   1 
ATOM   5490 C CB  . GLN E 5 137 ? 31.22758  -10.41813 -21.79522 1.000 53.21199  ? 151 GLN E CB  1 
ATOM   5491 N N   . LYS E 5 138 ? 31.24549  -12.03192 -18.47365 1.000 56.56987  ? 152 LYS E N   1 
ATOM   5492 C CA  . LYS E 5 138 ? 31.32941  -11.76790 -17.04614 1.000 62.25248  ? 152 LYS E CA  1 
ATOM   5493 C C   . LYS E 5 138 ? 32.05410  -12.92231 -16.37071 1.000 56.59676  ? 152 LYS E C   1 
ATOM   5494 O O   . LYS E 5 138 ? 32.06192  -14.04943 -16.87493 1.000 53.14958  ? 152 LYS E O   1 
ATOM   5495 C CB  . LYS E 5 138 ? 29.93849  -11.57152 -16.42740 1.000 62.82730  ? 152 LYS E CB  1 
ATOM   5496 C CG  . LYS E 5 138 ? 29.29862  -10.23924 -16.78242 1.000 43.89059  ? 152 LYS E CG  1 
ATOM   5497 C CD  . LYS E 5 138 ? 27.78910  -10.28370 -16.64794 1.000 57.15157  ? 152 LYS E CD  1 
ATOM   5498 C CE  . LYS E 5 138 ? 27.16279  -9.00717  -17.18027 1.000 61.11379  ? 152 LYS E CE  1 
ATOM   5499 N NZ  . LYS E 5 138 ? 27.68058  -8.66418  -18.53900 1.000 86.41643  ? 152 LYS E NZ  1 
ATOM   5500 N N   . ALA E 5 139 ? 32.66877  -12.62926 -15.22533 1.000 51.83122  ? 153 ALA E N   1 
ATOM   5501 C CA  . ALA E 5 139 ? 33.49613  -13.59247 -14.50771 1.000 50.00230  ? 153 ALA E CA  1 
ATOM   5502 C C   . ALA E 5 139 ? 33.08469  -13.61383 -13.04443 1.000 54.84596  ? 153 ALA E C   1 
ATOM   5503 O O   . ALA E 5 139 ? 33.19222  -12.59699 -12.35190 1.000 44.04204  ? 153 ALA E O   1 
ATOM   5504 C CB  . ALA E 5 139 ? 34.97977  -13.24663 -14.64142 1.000 38.45326  ? 153 ALA E CB  1 
ATOM   5505 N N   . THR E 5 140 ? 32.62794  -14.76845 -12.57270 1.000 53.01080  ? 154 THR E N   1 
ATOM   5506 C CA  . THR E 5 140 ? 32.16974  -14.92691 -11.19988 1.000 42.88038  ? 154 THR E CA  1 
ATOM   5507 C C   . THR E 5 140 ? 33.20623  -15.71221 -10.40743 1.000 53.66394  ? 154 THR E C   1 
ATOM   5508 O O   . THR E 5 140 ? 33.51693  -16.85981 -10.74507 1.000 39.77185  ? 154 THR E O   1 
ATOM   5509 C CB  . THR E 5 140 ? 30.81868  -15.63773 -11.14468 1.000 33.92170  ? 154 THR E CB  1 
ATOM   5510 O OG1 . THR E 5 140 ? 29.89478  -14.98078 -12.01638 1.000 49.26712  ? 154 THR E OG1 1 
ATOM   5511 C CG2 . THR E 5 140 ? 30.26810  -15.60468 -9.72370  1.000 47.65965  ? 154 THR E CG2 1 
ATOM   5512 N N   . LEU E 5 141 ? 33.73863  -15.09610 -9.36007  1.000 40.49177  ? 155 LEU E N   1 
ATOM   5513 C CA  . LEU E 5 141 ? 34.53570  -15.81965 -8.38637  1.000 41.55652  ? 155 LEU E CA  1 
ATOM   5514 C C   . LEU E 5 141 ? 33.62005  -16.27990 -7.26203  1.000 41.77304  ? 155 LEU E C   1 
ATOM   5515 O O   . LEU E 5 141 ? 32.70569  -15.55681 -6.85671  1.000 42.30087  ? 155 LEU E O   1 
ATOM   5516 C CB  . LEU E 5 141 ? 35.66908  -14.95029 -7.83374  1.000 45.25542  ? 155 LEU E CB  1 
ATOM   5517 C CG  . LEU E 5 141 ? 36.64512  -14.31587 -8.83149  1.000 49.57945  ? 155 LEU E CG  1 
ATOM   5518 C CD1 . LEU E 5 141 ? 36.16966  -12.93457 -9.27258  1.000 51.57561  ? 155 LEU E CD1 1 
ATOM   5519 C CD2 . LEU E 5 141 ? 38.03842  -14.23436 -8.23901  1.000 45.62755  ? 155 LEU E CD2 1 
ATOM   5520 N N   . VAL E 5 142 ? 33.85109  -17.49745 -6.78118  1.000 41.91595  ? 156 VAL E N   1 
ATOM   5521 C CA  . VAL E 5 142 ? 33.08512  -18.07108 -5.68240  1.000 36.74006  ? 156 VAL E CA  1 
ATOM   5522 C C   . VAL E 5 142 ? 34.03467  -18.33482 -4.52760  1.000 40.87707  ? 156 VAL E C   1 
ATOM   5523 O O   . VAL E 5 142 ? 35.13432  -18.86394 -4.72568  1.000 52.14728  ? 156 VAL E O   1 
ATOM   5524 C CB  . VAL E 5 142 ? 32.36171  -19.36532 -6.09236  1.000 37.16389  ? 156 VAL E CB  1 
ATOM   5525 C CG1 . VAL E 5 142 ? 31.74274  -20.03073 -4.87252  1.000 35.06995  ? 156 VAL E CG1 1 
ATOM   5526 C CG2 . VAL E 5 142 ? 31.30094  -19.06295 -7.11962  1.000 32.78167  ? 156 VAL E CG2 1 
ATOM   5527 N N   . CYS E 5 143 ? 33.60878  -17.96933 -3.32797  1.000 43.31774  ? 157 CYS E N   1 
ATOM   5528 C CA  . CYS E 5 143 ? 34.37630  -18.19877 -2.11760  1.000 34.56180  ? 157 CYS E CA  1 
ATOM   5529 C C   . CYS E 5 143 ? 33.60912  -19.14105 -1.20410  1.000 43.05391  ? 157 CYS E C   1 
ATOM   5530 O O   . CYS E 5 143 ? 32.41834  -18.93218 -0.95002  1.000 37.21568  ? 157 CYS E O   1 
ATOM   5531 C CB  . CYS E 5 143 ? 34.65253  -16.88612 -1.40529  1.000 32.88447  ? 157 CYS E CB  1 
ATOM   5532 S SG  . CYS E 5 143 ? 35.62348  -17.10199 0.06692   1.000 52.06951  ? 157 CYS E SG  1 
ATOM   5533 N N   . LEU E 5 144 ? 34.29098  -20.17055 -0.71182  1.000 40.10886  ? 158 LEU E N   1 
ATOM   5534 C CA  . LEU E 5 144 ? 33.69950  -21.14929 0.19181   1.000 39.26988  ? 158 LEU E CA  1 
ATOM   5535 C C   . LEU E 5 144 ? 34.42501  -21.10537 1.52763   1.000 37.42737  ? 158 LEU E C   1 
ATOM   5536 O O   . LEU E 5 144 ? 35.63742  -21.33255 1.58684   1.000 39.66574  ? 158 LEU E O   1 
ATOM   5537 C CB  . LEU E 5 144 ? 33.76755  -22.56133 -0.39351  1.000 41.60815  ? 158 LEU E CB  1 
ATOM   5538 C CG  . LEU E 5 144 ? 32.51239  -23.10416 -1.07039  1.000 46.13561  ? 158 LEU E CG  1 
ATOM   5539 C CD1 . LEU E 5 144 ? 32.64971  -24.60540 -1.29033  1.000 51.43683  ? 158 LEU E CD1 1 
ATOM   5540 C CD2 . LEU E 5 144 ? 31.29506  -22.79306 -0.22551  1.000 47.96173  ? 158 LEU E CD2 1 
ATOM   5541 N N   . ALA E 5 145 ? 33.68375  -20.81457 2.59050   1.000 39.78811  ? 159 ALA E N   1 
ATOM   5542 C CA  . ALA E 5 145 ? 34.14690  -20.98223 3.96023   1.000 29.16152  ? 159 ALA E CA  1 
ATOM   5543 C C   . ALA E 5 145 ? 33.40621  -22.17619 4.54797   1.000 39.95895  ? 159 ALA E C   1 
ATOM   5544 O O   . ALA E 5 145 ? 32.17129  -22.19620 4.56033   1.000 33.45610  ? 159 ALA E O   1 
ATOM   5545 C CB  . ALA E 5 145 ? 33.89815  -19.71807 4.78157   1.000 30.39855  ? 159 ALA E CB  1 
ATOM   5546 N N   . THR E 5 146 ? 34.14931  -23.17725 5.00953   1.000 34.12335  ? 160 THR E N   1 
ATOM   5547 C CA  . THR E 5 146 ? 33.54626  -24.43992 5.40631   1.000 43.57089  ? 160 THR E CA  1 
ATOM   5548 C C   . THR E 5 146 ? 34.11005  -24.90919 6.74216   1.000 35.40011  ? 160 THR E C   1 
ATOM   5549 O O   . THR E 5 146 ? 35.22335  -24.55598 7.13460   1.000 33.46128  ? 160 THR E O   1 
ATOM   5550 C CB  . THR E 5 146 ? 33.75902  -25.53210 4.33650   1.000 44.39325  ? 160 THR E CB  1 
ATOM   5551 O OG1 . THR E 5 146 ? 35.15791  -25.68668 4.07169   1.000 37.60349  ? 160 THR E OG1 1 
ATOM   5552 C CG2 . THR E 5 146 ? 33.04278  -25.17163 3.03763   1.000 35.96988  ? 160 THR E CG2 1 
ATOM   5553 N N   . GLY E 5 147 ? 33.30605  -25.70493 7.44012   1.000 37.62104  ? 161 GLY E N   1 
ATOM   5554 C CA  . GLY E 5 147 ? 33.71976  -26.37842 8.65895   1.000 36.09347  ? 161 GLY E CA  1 
ATOM   5555 C C   . GLY E 5 147 ? 33.97519  -25.50268 9.86649   1.000 38.28129  ? 161 GLY E C   1 
ATOM   5556 O O   . GLY E 5 147 ? 34.86083  -25.81786 10.66859  1.000 44.05485  ? 161 GLY E O   1 
ATOM   5557 N N   . PHE E 5 148 ? 33.22517  -24.41670 10.02930  1.000 36.08448  ? 162 PHE E N   1 
ATOM   5558 C CA  . PHE E 5 148 ? 33.42110  -23.53989 11.17327  1.000 38.71601  ? 162 PHE E CA  1 
ATOM   5559 C C   . PHE E 5 148 ? 32.26871  -23.66287 12.16105  1.000 36.81176  ? 162 PHE E C   1 
ATOM   5560 O O   . PHE E 5 148 ? 31.13299  -23.97720 11.79273  1.000 35.62607  ? 162 PHE E O   1 
ATOM   5561 C CB  . PHE E 5 148 ? 33.59176  -22.07649 10.74815  1.000 41.23059  ? 162 PHE E CB  1 
ATOM   5562 C CG  . PHE E 5 148 ? 32.41579  -21.50062 10.00876  1.000 34.16555  ? 162 PHE E CG  1 
ATOM   5563 C CD1 . PHE E 5 148 ? 32.34591  -21.57941 8.62567   1.000 36.08245  ? 162 PHE E CD1 1 
ATOM   5564 C CD2 . PHE E 5 148 ? 31.40380  -20.84087 10.69004  1.000 27.11531  ? 162 PHE E CD2 1 
ATOM   5565 C CE1 . PHE E 5 148 ? 31.27968  -21.03596 7.93607   1.000 32.12726  ? 162 PHE E CE1 1 
ATOM   5566 C CE2 . PHE E 5 148 ? 30.33488  -20.29187 10.00686  1.000 30.94566  ? 162 PHE E CE2 1 
ATOM   5567 C CZ  . PHE E 5 148 ? 30.27345  -20.39134 8.62405   1.000 36.00704  ? 162 PHE E CZ  1 
ATOM   5568 N N   . PHE E 5 149 ? 32.58524  -23.42735 13.42682  1.000 32.14898  ? 163 PHE E N   1 
ATOM   5569 C CA  . PHE E 5 149 ? 31.59481  -23.43533 14.49215  1.000 32.69506  ? 163 PHE E CA  1 
ATOM   5570 C C   . PHE E 5 149 ? 32.11634  -22.62822 15.67422  1.000 32.85955  ? 163 PHE E C   1 
ATOM   5571 O O   . PHE E 5 149 ? 33.27223  -22.80594 16.08211  1.000 33.23674  ? 163 PHE E O   1 
ATOM   5572 C CB  . PHE E 5 149 ? 31.26125  -24.86246 14.93084  1.000 30.92034  ? 163 PHE E CB  1 
ATOM   5573 C CG  . PHE E 5 149 ? 30.18524  -24.92632 15.97361  1.000 31.32575  ? 163 PHE E CG  1 
ATOM   5574 C CD1 . PHE E 5 149 ? 28.85177  -24.82438 15.61066  1.000 32.76538  ? 163 PHE E CD1 1 
ATOM   5575 C CD2 . PHE E 5 149 ? 30.50553  -25.05802 17.31823  1.000 27.91822  ? 163 PHE E CD2 1 
ATOM   5576 C CE1 . PHE E 5 149 ? 27.85243  -24.87201 16.56480  1.000 34.45776  ? 163 PHE E CE1 1 
ATOM   5577 C CE2 . PHE E 5 149 ? 29.51619  -25.10341 18.27712  1.000 33.98163  ? 163 PHE E CE2 1 
ATOM   5578 C CZ  . PHE E 5 149 ? 28.18567  -25.01172 17.90167  1.000 45.35771  ? 163 PHE E CZ  1 
ATOM   5579 N N   . PRO E 5 150 ? 31.29948  -21.73724 16.25910  1.000 31.38705  ? 164 PRO E N   1 
ATOM   5580 C CA  . PRO E 5 150 ? 29.91669  -21.45831 15.86836  1.000 29.37341  ? 164 PRO E CA  1 
ATOM   5581 C C   . PRO E 5 150 ? 29.82366  -20.51584 14.68271  1.000 33.51107  ? 164 PRO E C   1 
ATOM   5582 O O   . PRO E 5 150 ? 30.81457  -20.28608 13.99159  1.000 32.17007  ? 164 PRO E O   1 
ATOM   5583 C CB  . PRO E 5 150 ? 29.34038  -20.79482 17.11454  1.000 33.21169  ? 164 PRO E CB  1 
ATOM   5584 C CG  . PRO E 5 150 ? 30.49087  -20.03516 17.64934  1.000 35.13660  ? 164 PRO E CG  1 
ATOM   5585 C CD  . PRO E 5 150 ? 31.69822  -20.92041 17.41673  1.000 32.84378  ? 164 PRO E CD  1 
ATOM   5586 N N   . ASP E 5 151 ? 28.63274  -19.96162 14.46360  1.000 36.04710  ? 165 ASP E N   1 
ATOM   5587 C CA  . ASP E 5 151 ? 28.38666  -19.06716 13.33158  1.000 42.44920  ? 165 ASP E CA  1 
ATOM   5588 C C   . ASP E 5 151 ? 28.84510  -17.65230 13.69638  1.000 38.14891  ? 165 ASP E C   1 
ATOM   5589 O O   . ASP E 5 151 ? 28.05182  -16.72808 13.88817  1.000 45.06637  ? 165 ASP E O   1 
ATOM   5590 C CB  . ASP E 5 151 ? 26.91511  -19.10557 12.94423  1.000 39.51697  ? 165 ASP E CB  1 
ATOM   5591 C CG  . ASP E 5 151 ? 26.62218  -18.31214 11.69298  1.000 50.25501  ? 165 ASP E CG  1 
ATOM   5592 O OD1 . ASP E 5 151 ? 27.58007  -17.95380 10.97506  1.000 53.48832  ? 165 ASP E OD1 1 
ATOM   5593 O OD2 . ASP E 5 151 ? 25.43119  -18.03993 11.43230  1.000 61.63028  ? 165 ASP E OD2 1 
ATOM   5594 N N   . HIS E 5 152 ? 30.16828  -17.50256 13.80603  1.000 30.69334  ? 166 HIS E N   1 
ATOM   5595 C CA  . HIS E 5 152 ? 30.78808  -16.23026 14.16421  1.000 28.36038  ? 166 HIS E CA  1 
ATOM   5596 C C   . HIS E 5 152 ? 31.75891  -15.78502 13.07776  1.000 30.91476  ? 166 HIS E C   1 
ATOM   5597 O O   . HIS E 5 152 ? 32.96472  -15.67599 13.32223  1.000 38.25158  ? 166 HIS E O   1 
ATOM   5598 C CB  . HIS E 5 152 ? 31.52622  -16.33614 15.50486  1.000 25.10170  ? 166 HIS E CB  1 
ATOM   5599 C CG  . HIS E 5 152 ? 30.62495  -16.42768 16.69862  1.000 31.81567  ? 166 HIS E CG  1 
ATOM   5600 N ND1 . HIS E 5 152 ? 31.07399  -16.21669 17.98554  1.000 22.00329  ? 166 HIS E ND1 1 
ATOM   5601 C CD2 . HIS E 5 152 ? 29.30607  -16.71526 16.80360  1.000 28.79214  ? 166 HIS E CD2 1 
ATOM   5602 C CE1 . HIS E 5 152 ? 30.06875  -16.36459 18.83010  1.000 28.83875  ? 166 HIS E CE1 1 
ATOM   5603 N NE2 . HIS E 5 152 ? 28.98529  -16.66962 18.13875  1.000 33.76070  ? 166 HIS E NE2 1 
ATOM   5604 N N   . VAL E 5 153 ? 31.25208  -15.52794 11.87615  1.000 26.88708  ? 167 VAL E N   1 
ATOM   5605 C CA  . VAL E 5 153 ? 32.10051  -15.22422 10.73394  1.000 32.34179  ? 167 VAL E CA  1 
ATOM   5606 C C   . VAL E 5 153 ? 31.62377  -13.94101 10.07413  1.000 32.90607  ? 167 VAL E C   1 
ATOM   5607 O O   . VAL E 5 153 ? 30.43909  -13.59589 10.11850  1.000 31.69585  ? 167 VAL E O   1 
ATOM   5608 C CB  . VAL E 5 153 ? 32.11917  -16.37939 9.71279   1.000 32.06170  ? 167 VAL E CB  1 
ATOM   5609 C CG1 . VAL E 5 153 ? 32.81125  -17.59483 10.29987  1.000 30.63673  ? 167 VAL E CG1 1 
ATOM   5610 C CG2 . VAL E 5 153 ? 30.70736  -16.72655 9.29614   1.000 32.16807  ? 167 VAL E CG2 1 
ATOM   5611 N N   . GLU E 5 154 ? 32.56889  -13.22496 9.46951   1.000 32.19052  ? 168 GLU E N   1 
ATOM   5612 C CA  . GLU E 5 154 ? 32.28445  -12.04862 8.65393   1.000 29.78678  ? 168 GLU E CA  1 
ATOM   5613 C C   . GLU E 5 154 ? 33.11241  -12.17385 7.38555   1.000 32.67544  ? 168 GLU E C   1 
ATOM   5614 O O   . GLU E 5 154 ? 34.34733  -12.12200 7.43758   1.000 29.02588  ? 168 GLU E O   1 
ATOM   5615 C CB  . GLU E 5 154 ? 32.60472  -10.75083 9.39766   1.000 27.13538  ? 168 GLU E CB  1 
ATOM   5616 C CG  . GLU E 5 154 ? 31.61521  -10.41117 10.50723  1.000 34.82159  ? 168 GLU E CG  1 
ATOM   5617 C CD  . GLU E 5 154 ? 32.10407  -9.29261  11.41830  1.000 44.18253  ? 168 GLU E CD  1 
ATOM   5618 O OE1 . GLU E 5 154 ? 33.23507  -8.79900  11.21996  1.000 40.26341  ? 168 GLU E OE1 1 
ATOM   5619 O OE2 . GLU E 5 154 ? 31.35513  -8.91198  12.34150  1.000 43.52624  ? 168 GLU E OE2 1 
ATOM   5620 N N   . LEU E 5 155 ? 32.43531  -12.35675 6.25592   1.000 30.05479  ? 169 LEU E N   1 
ATOM   5621 C CA  . LEU E 5 155 ? 33.09025  -12.55351 4.97227   1.000 25.55372  ? 169 LEU E CA  1 
ATOM   5622 C C   . LEU E 5 155 ? 33.12149  -11.23964 4.20535   1.000 32.23289  ? 169 LEU E C   1 
ATOM   5623 O O   . LEU E 5 155 ? 32.12452  -10.51369 4.15610   1.000 33.37438  ? 169 LEU E O   1 
ATOM   5624 C CB  . LEU E 5 155 ? 32.36797  -13.63061 4.15972   1.000 30.87388  ? 169 LEU E CB  1 
ATOM   5625 C CG  . LEU E 5 155 ? 33.02346  -14.19074 2.89725   1.000 31.31054  ? 169 LEU E CG  1 
ATOM   5626 C CD1 . LEU E 5 155 ? 32.50506  -15.59378 2.62917   1.000 26.25809  ? 169 LEU E CD1 1 
ATOM   5627 C CD2 . LEU E 5 155 ? 32.77811  -13.29925 1.68523   1.000 29.48112  ? 169 LEU E CD2 1 
ATOM   5628 N N   . SER E 5 156 ? 34.27010  -10.94487 3.59971   1.000 29.59984  ? 170 SER E N   1 
ATOM   5629 C CA  . SER E 5 156 ? 34.44504  -9.73234  2.81546   1.000 33.12440  ? 170 SER E CA  1 
ATOM   5630 C C   . SER E 5 156 ? 35.32644  -10.02511 1.60811   1.000 35.73765  ? 170 SER E C   1 
ATOM   5631 O O   . SER E 5 156 ? 36.16121  -10.93310 1.63152   1.000 30.10716  ? 170 SER E O   1 
ATOM   5632 C CB  . SER E 5 156 ? 35.04969  -8.60022  3.66142   1.000 30.34025  ? 170 SER E CB  1 
ATOM   5633 O OG  . SER E 5 156 ? 36.25964  -9.00667  4.27575   1.000 31.11329  ? 170 SER E OG  1 
ATOM   5634 N N   . TRP E 5 157 ? 35.12597  -9.24423  0.55007   1.000 31.40235  ? 171 TRP E N   1 
ATOM   5635 C CA  . TRP E 5 157 ? 35.87495  -9.36704  -0.69423  1.000 34.42166  ? 171 TRP E CA  1 
ATOM   5636 C C   . TRP E 5 157 ? 36.82957  -8.18830  -0.83609  1.000 35.35382  ? 171 TRP E C   1 
ATOM   5637 O O   . TRP E 5 157 ? 36.43863  -7.03625  -0.61913  1.000 36.57749  ? 171 TRP E O   1 
ATOM   5638 C CB  . TRP E 5 157 ? 34.93129  -9.41813  -1.89891  1.000 26.98405  ? 171 TRP E CB  1 
ATOM   5639 C CG  . TRP E 5 157 ? 34.33248  -10.76996 -2.18133  1.000 33.24494  ? 171 TRP E CG  1 
ATOM   5640 C CD1 . TRP E 5 157 ? 33.07651  -11.19340 -1.86188  1.000 30.59415  ? 171 TRP E CD1 1 
ATOM   5641 C CD2 . TRP E 5 157 ? 34.96182  -11.86387 -2.86196  1.000 38.08223  ? 171 TRP E CD2 1 
ATOM   5642 N NE1 . TRP E 5 157 ? 32.88316  -12.48475 -2.29706  1.000 30.43831  ? 171 TRP E NE1 1 
ATOM   5643 C CE2 . TRP E 5 157 ? 34.02614  -12.91763 -2.91510  1.000 43.47650  ? 171 TRP E CE2 1 
ATOM   5644 C CE3 . TRP E 5 157 ? 36.22436  -12.05393 -3.43266  1.000 42.61206  ? 171 TRP E CE3 1 
ATOM   5645 C CZ2 . TRP E 5 157 ? 34.31448  -14.14318 -3.51349  1.000 45.51992  ? 171 TRP E CZ2 1 
ATOM   5646 C CZ3 . TRP E 5 157 ? 36.50934  -13.27257 -4.02718  1.000 34.93652  ? 171 TRP E CZ3 1 
ATOM   5647 C CH2 . TRP E 5 157 ? 35.55889  -14.30014 -4.06361  1.000 36.15375  ? 171 TRP E CH2 1 
ATOM   5648 N N   . TRP E 5 158 ? 38.07212  -8.47196  -1.21869  1.000 37.92098  ? 172 TRP E N   1 
ATOM   5649 C CA  . TRP E 5 158 ? 39.09642  -7.44181  -1.34730  1.000 35.88220  ? 172 TRP E CA  1 
ATOM   5650 C C   . TRP E 5 158 ? 39.72379  -7.52467  -2.72804  1.000 44.72860  ? 172 TRP E C   1 
ATOM   5651 O O   . TRP E 5 158 ? 40.31337  -8.55042  -3.08320  1.000 41.93723  ? 172 TRP E O   1 
ATOM   5652 C CB  . TRP E 5 158 ? 40.15808  -7.59164  -0.25741  1.000 41.31434  ? 172 TRP E CB  1 
ATOM   5653 C CG  . TRP E 5 158 ? 39.62266  -7.30019  1.11138   1.000 44.70825  ? 172 TRP E CG  1 
ATOM   5654 C CD1 . TRP E 5 158 ? 38.85804  -8.12296  1.88421   1.000 33.84432  ? 172 TRP E CD1 1 
ATOM   5655 C CD2 . TRP E 5 158 ? 39.80849  -6.09822  1.86701   1.000 44.89302  ? 172 TRP E CD2 1 
ATOM   5656 N NE1 . TRP E 5 158 ? 38.55544  -7.50963  3.07457   1.000 42.52808  ? 172 TRP E NE1 1 
ATOM   5657 C CE2 . TRP E 5 158 ? 39.12948  -6.26627  3.09077   1.000 41.00840  ? 172 TRP E CE2 1 
ATOM   5658 C CE3 . TRP E 5 158 ? 40.48682  -4.89770  1.62967   1.000 39.78276  ? 172 TRP E CE3 1 
ATOM   5659 C CZ2 . TRP E 5 158 ? 39.10763  -5.28013  4.07417   1.000 37.84615  ? 172 TRP E CZ2 1 
ATOM   5660 C CZ3 . TRP E 5 158 ? 40.46451  -3.91766  2.60798   1.000 38.11590  ? 172 TRP E CZ3 1 
ATOM   5661 C CH2 . TRP E 5 158 ? 39.77916  -4.11520  3.81499   1.000 39.16789  ? 172 TRP E CH2 1 
ATOM   5662 N N   . VAL E 5 159 ? 39.59692  -6.44800  -3.50005  1.000 41.64386  ? 173 VAL E N   1 
ATOM   5663 C CA  . VAL E 5 159 ? 40.15450  -6.36111  -4.84492  1.000 44.05455  ? 173 VAL E CA  1 
ATOM   5664 C C   . VAL E 5 159 ? 41.25090  -5.30549  -4.84124  1.000 47.80517  ? 173 VAL E C   1 
ATOM   5665 O O   . VAL E 5 159 ? 40.98524  -4.12512  -4.57968  1.000 54.45107  ? 173 VAL E O   1 
ATOM   5666 C CB  . VAL E 5 159 ? 39.07986  -6.03126  -5.88967  1.000 44.85968  ? 173 VAL E CB  1 
ATOM   5667 C CG1 . VAL E 5 159 ? 39.73639  -5.72082  -7.23146  1.000 46.70404  ? 173 VAL E CG1 1 
ATOM   5668 C CG2 . VAL E 5 159 ? 38.10403  -7.19025  -6.02150  1.000 39.62660  ? 173 VAL E CG2 1 
ATOM   5669 N N   . ASN E 5 160 ? 42.48034  -5.73298  -5.13177  1.000 45.18274  ? 174 ASN E N   1 
ATOM   5670 C CA  . ASN E 5 160 ? 43.63806  -4.83938  -5.17357  1.000 56.57432  ? 174 ASN E CA  1 
ATOM   5671 C C   . ASN E 5 160 ? 43.80075  -4.07289  -3.86310  1.000 54.02975  ? 174 ASN E C   1 
ATOM   5672 O O   . ASN E 5 160 ? 44.17458  -2.89864  -3.84676  1.000 56.50471  ? 174 ASN E O   1 
ATOM   5673 C CB  . ASN E 5 160 ? 43.54347  -3.88312  -6.36263  1.000 44.96068  ? 174 ASN E CB  1 
ATOM   5674 C CG  . ASN E 5 160 ? 43.57984  -4.61043  -7.68671  1.000 45.81743  ? 174 ASN E CG  1 
ATOM   5675 O OD1 . ASN E 5 160 ? 44.19770  -5.66820  -7.80291  1.000 49.58935  ? 174 ASN E OD1 1 
ATOM   5676 N ND2 . ASN E 5 160 ? 42.91260  -4.05389  -8.69319  1.000 49.09721  ? 174 ASN E ND2 1 
ATOM   5677 N N   . GLY E 5 161 ? 43.50999  -4.74616  -2.75038  1.000 46.95448  ? 175 GLY E N   1 
ATOM   5678 C CA  . GLY E 5 161 ? 43.67352  -4.16280  -1.43902  1.000 45.26587  ? 175 GLY E CA  1 
ATOM   5679 C C   . GLY E 5 161 ? 42.53110  -3.29598  -0.96048  1.000 45.35241  ? 175 GLY E C   1 
ATOM   5680 O O   . GLY E 5 161 ? 42.62954  -2.72636  0.13464   1.000 42.98405  ? 175 GLY E O   1 
ATOM   5681 N N   . LYS E 5 162 ? 41.45577  -3.16868  -1.73421  1.000 38.65788  ? 176 LYS E N   1 
ATOM   5682 C CA  . LYS E 5 162 ? 40.29086  -2.38715  -1.33912  1.000 46.79934  ? 176 LYS E CA  1 
ATOM   5683 C C   . LYS E 5 162 ? 39.08400  -3.30754  -1.23450  1.000 47.95862  ? 176 LYS E C   1 
ATOM   5684 O O   . LYS E 5 162 ? 38.84218  -4.12464  -2.12910  1.000 47.51419  ? 176 LYS E O   1 
ATOM   5685 C CB  . LYS E 5 162 ? 40.01415  -1.25585  -2.33404  1.000 44.17703  ? 176 LYS E CB  1 
ATOM   5686 N N   . GLU E 5 163 ? 38.33717  -3.18186  -0.13955  1.000 50.40935  ? 177 GLU E N   1 
ATOM   5687 C CA  . GLU E 5 163 ? 37.13787  -3.98875  0.03582   1.000 46.53997  ? 177 GLU E CA  1 
ATOM   5688 C C   . GLU E 5 163 ? 36.04658  -3.51780  -0.91632  1.000 46.80785  ? 177 GLU E C   1 
ATOM   5689 O O   . GLU E 5 163 ? 35.74793  -2.32222  -0.99449  1.000 49.40620  ? 177 GLU E O   1 
ATOM   5690 C CB  . GLU E 5 163 ? 36.63797  -3.91944  1.47779   1.000 43.23952  ? 177 GLU E CB  1 
ATOM   5691 C CG  . GLU E 5 163 ? 35.34580  -4.70282  1.67854   1.000 55.37981  ? 177 GLU E CG  1 
ATOM   5692 C CD  . GLU E 5 163 ? 34.80685  -4.64870  3.09630   1.000 43.35561  ? 177 GLU E CD  1 
ATOM   5693 O OE1 . GLU E 5 163 ? 35.39802  -3.94822  3.94678   1.000 55.49883  ? 177 GLU E OE1 1 
ATOM   5694 O OE2 . GLU E 5 163 ? 33.78027  -5.31362  3.35521   1.000 43.17565  ? 177 GLU E OE2 1 
ATOM   5695 N N   . VAL E 5 164 ? 35.44776  -4.45941  -1.63631  1.000 35.41676  ? 178 VAL E N   1 
ATOM   5696 C CA  . VAL E 5 164 ? 34.40519  -4.15010  -2.60071  1.000 36.40412  ? 178 VAL E CA  1 
ATOM   5697 C C   . VAL E 5 164 ? 33.07774  -4.69823  -2.09475  1.000 44.14679  ? 178 VAL E C   1 
ATOM   5698 O O   . VAL E 5 164 ? 33.01785  -5.63027  -1.28600  1.000 44.24699  ? 178 VAL E O   1 
ATOM   5699 C CB  . VAL E 5 164 ? 34.73045  -4.70998  -3.99954  1.000 37.10905  ? 178 VAL E CB  1 
ATOM   5700 C CG1 . VAL E 5 164 ? 36.05876  -4.16298  -4.48887  1.000 37.99588  ? 178 VAL E CG1 1 
ATOM   5701 C CG2 . VAL E 5 164 ? 34.74672  -6.22700  -3.96991  1.000 30.98409  ? 178 VAL E CG2 1 
ATOM   5702 N N   . HIS E 5 165 ? 31.99616  -4.09457  -2.57933  1.000 39.60316  ? 179 HIS E N   1 
ATOM   5703 C CA  . HIS E 5 165 ? 30.65447  -4.55349  -2.25154  1.000 45.45370  ? 179 HIS E CA  1 
ATOM   5704 C C   . HIS E 5 165 ? 29.83903  -4.75590  -3.51791  1.000 43.34817  ? 179 HIS E C   1 
ATOM   5705 O O   . HIS E 5 165 ? 28.90735  -5.56549  -3.53775  1.000 48.84677  ? 179 HIS E O   1 
ATOM   5706 C CB  . HIS E 5 165 ? 29.95358  -3.56282  -1.32434  1.000 43.86515  ? 179 HIS E CB  1 
ATOM   5707 C CG  . HIS E 5 165 ? 30.52027  -3.53355  0.05800   1.000 48.49081  ? 179 HIS E CG  1 
ATOM   5708 N ND1 . HIS E 5 165 ? 31.54718  -2.69048  0.42290   1.000 50.41823  ? 179 HIS E ND1 1 
ATOM   5709 C CD2 . HIS E 5 165 ? 30.21701  -4.25761  1.16045   1.000 53.60478  ? 179 HIS E CD2 1 
ATOM   5710 C CE1 . HIS E 5 165 ? 31.84514  -2.88837  1.69435   1.000 47.06631  ? 179 HIS E CE1 1 
ATOM   5711 N NE2 . HIS E 5 165 ? 31.05319  -3.83463  2.16516   1.000 52.06430  ? 179 HIS E NE2 1 
ATOM   5712 N N   . SER E 5 166 ? 30.18608  -4.02903  -4.57719  1.000 43.37539  ? 180 SER E N   1 
ATOM   5713 C CA  . SER E 5 166 ? 29.43568  -4.11587  -5.82136  1.000 44.55671  ? 180 SER E CA  1 
ATOM   5714 C C   . SER E 5 166 ? 29.69066  -5.45585  -6.50062  1.000 43.42329  ? 180 SER E C   1 
ATOM   5715 O O   . SER E 5 166 ? 30.83847  -5.89311  -6.62952  1.000 41.42130  ? 180 SER E O   1 
ATOM   5716 C CB  . SER E 5 166 ? 29.81662  -2.96615  -6.74969  1.000 39.23920  ? 180 SER E CB  1 
ATOM   5717 O OG  . SER E 5 166 ? 29.11071  -3.06239  -7.97188  1.000 57.97912  ? 180 SER E OG  1 
ATOM   5718 N N   . GLY E 5 167 ? 28.61498  -6.11079  -6.93019  1.000 47.91753  ? 181 GLY E N   1 
ATOM   5719 C CA  . GLY E 5 167 ? 28.74605  -7.40707  -7.56259  1.000 45.64903  ? 181 GLY E CA  1 
ATOM   5720 C C   . GLY E 5 167 ? 29.02261  -8.54543  -6.60970  1.000 44.74441  ? 181 GLY E C   1 
ATOM   5721 O O   . GLY E 5 167 ? 29.45858  -9.61354  -7.04644  1.000 39.61469  ? 181 GLY E O   1 
ATOM   5722 N N   . VAL E 5 168 ? 28.77208  -8.34926  -5.31669  1.000 41.07705  ? 182 VAL E N   1 
ATOM   5723 C CA  . VAL E 5 168 ? 29.01279  -9.35312  -4.28814  1.000 36.74584  ? 182 VAL E CA  1 
ATOM   5724 C C   . VAL E 5 168 ? 27.67388  -9.86826  -3.77996  1.000 37.68897  ? 182 VAL E C   1 
ATOM   5725 O O   . VAL E 5 168 ? 26.73610  -9.08822  -3.57430  1.000 39.07337  ? 182 VAL E O   1 
ATOM   5726 C CB  . VAL E 5 168 ? 29.85034  -8.77552  -3.12679  1.000 44.84532  ? 182 VAL E CB  1 
ATOM   5727 C CG1 . VAL E 5 168 ? 29.95313  -9.77661  -1.98344  1.000 30.50078  ? 182 VAL E CG1 1 
ATOM   5728 C CG2 . VAL E 5 168 ? 31.23585  -8.37360  -3.61078  1.000 34.09261  ? 182 VAL E CG2 1 
ATOM   5729 N N   . CYS E 5 169 ? 27.58133  -11.18247 -3.57758  1.000 35.50165  ? 183 CYS E N   1 
ATOM   5730 C CA  . CYS E 5 169 ? 26.44242  -11.76388 -2.87660  1.000 36.87674  ? 183 CYS E CA  1 
ATOM   5731 C C   . CYS E 5 169 ? 26.93771  -12.84977 -1.93633  1.000 31.22291  ? 183 CYS E C   1 
ATOM   5732 O O   . CYS E 5 169 ? 27.54908  -13.82650 -2.37916  1.000 42.19840  ? 183 CYS E O   1 
ATOM   5733 C CB  . CYS E 5 169 ? 25.40321  -12.33373 -3.84130  1.000 32.56863  ? 183 CYS E CB  1 
ATOM   5734 S SG  . CYS E 5 169 ? 23.79557  -12.48278 -3.03789  1.000 71.29225  ? 183 CYS E SG  1 
ATOM   5735 N N   . THR E 5 170 ? 26.66406  -12.67748 -0.64725  1.000 34.80391  ? 184 THR E N   1 
ATOM   5736 C CA  . THR E 5 170 ? 27.01251  -13.63948 0.38716   1.000 32.57531  ? 184 THR E CA  1 
ATOM   5737 C C   . THR E 5 170 ? 25.73327  -14.24770 0.94558   1.000 32.06482  ? 184 THR E C   1 
ATOM   5738 O O   . THR E 5 170 ? 24.74532  -13.53891 1.16846   1.000 37.60525  ? 184 THR E O   1 
ATOM   5739 C CB  . THR E 5 170 ? 27.82285  -12.97069 1.50912   1.000 29.48522  ? 184 THR E CB  1 
ATOM   5740 O OG1 . THR E 5 170 ? 28.97481  -12.32465 0.95228   1.000 32.18519  ? 184 THR E OG1 1 
ATOM   5741 C CG2 . THR E 5 170 ? 28.28097  -13.99093 2.53601   1.000 32.44116  ? 184 THR E CG2 1 
ATOM   5742 N N   . ASP E 5 171 ? 25.74554  -15.56226 1.14310   1.000 30.29137  ? 185 ASP E N   1 
ATOM   5743 C CA  . ASP E 5 171 ? 24.59378  -16.25920 1.68813   1.000 34.39721  ? 185 ASP E CA  1 
ATOM   5744 C C   . ASP E 5 171 ? 24.16374  -15.61248 3.00012   1.000 38.07695  ? 185 ASP E C   1 
ATOM   5745 O O   . ASP E 5 171 ? 24.98738  -15.48285 3.92032   1.000 41.29458  ? 185 ASP E O   1 
ATOM   5746 C CB  . ASP E 5 171 ? 24.91991  -17.73110 1.91898   1.000 37.95396  ? 185 ASP E CB  1 
ATOM   5747 C CG  . ASP E 5 171 ? 25.48857  -18.39885 0.68941   1.000 46.17927  ? 185 ASP E CG  1 
ATOM   5748 O OD1 . ASP E 5 171 ? 25.09368  -18.01665 -0.43173  1.000 42.13219  ? 185 ASP E OD1 1 
ATOM   5749 O OD2 . ASP E 5 171 ? 26.33490  -19.30513 0.84502   1.000 50.82969  ? 185 ASP E OD2 1 
ATOM   5750 N N   . PRO E 5 172 ? 22.90836  -15.17504 3.12625   1.000 44.82761  ? 186 PRO E N   1 
ATOM   5751 C CA  . PRO E 5 172 ? 22.45719  -14.59192 4.39977   1.000 43.56212  ? 186 PRO E CA  1 
ATOM   5752 C C   . PRO E 5 172 ? 22.52306  -15.55527 5.57376   1.000 42.66048  ? 186 PRO E C   1 
ATOM   5753 O O   . PRO E 5 172 ? 22.63863  -15.09892 6.71717   1.000 40.16633  ? 186 PRO E O   1 
ATOM   5754 C CB  . PRO E 5 172 ? 21.01323  -14.16276 4.10348   1.000 37.71186  ? 186 PRO E CB  1 
ATOM   5755 C CG  . PRO E 5 172 ? 20.61570  -14.94089 2.87804   1.000 37.43086  ? 186 PRO E CG  1 
ATOM   5756 C CD  . PRO E 5 172 ? 21.86801  -15.11602 2.08423   1.000 32.96031  ? 186 PRO E CD  1 
ATOM   5757 N N   . GLN E 5 173 ? 22.46625  -16.86820 5.33808   1.000 40.00286  ? 187 GLN E N   1 
ATOM   5758 C CA  . GLN E 5 173 ? 22.56106  -17.84498 6.41909   1.000 49.19892  ? 187 GLN E CA  1 
ATOM   5759 C C   . GLN E 5 173 ? 23.42830  -19.01982 5.98376   1.000 52.09630  ? 187 GLN E C   1 
ATOM   5760 O O   . GLN E 5 173 ? 23.39259  -19.41623 4.80837   1.000 45.18163  ? 187 GLN E O   1 
ATOM   5761 C CB  . GLN E 5 173 ? 21.17288  -18.35197 6.84642   1.000 52.95894  ? 187 GLN E CB  1 
ATOM   5762 N N   . PRO E 5 174 ? 24.20586  -19.59349 6.89868   1.000 48.24270  ? 188 PRO E N   1 
ATOM   5763 C CA  . PRO E 5 174 ? 25.10298  -20.69173 6.53335   1.000 43.87671  ? 188 PRO E CA  1 
ATOM   5764 C C   . PRO E 5 174 ? 24.35615  -22.00387 6.34442   1.000 46.68014  ? 188 PRO E C   1 
ATOM   5765 O O   . PRO E 5 174 ? 23.21984  -22.17931 6.78210   1.000 53.92287  ? 188 PRO E O   1 
ATOM   5766 C CB  . PRO E 5 174 ? 26.05765  -20.78714 7.73222   1.000 50.93852  ? 188 PRO E CB  1 
ATOM   5767 C CG  . PRO E 5 174 ? 25.74877  -19.59802 8.60286   1.000 50.42455  ? 188 PRO E CG  1 
ATOM   5768 C CD  . PRO E 5 174 ? 24.34083  -19.23151 8.31657   1.000 45.14337  ? 188 PRO E CD  1 
ATOM   5769 N N   . LEU E 5 175 ? 25.02911  -22.93439 5.67515   1.000 44.58722  ? 189 LEU E N   1 
ATOM   5770 C CA  . LEU E 5 175 ? 24.55765  -24.30764 5.56926   1.000 51.77340  ? 189 LEU E CA  1 
ATOM   5771 C C   . LEU E 5 175 ? 25.15108  -25.14524 6.69411   1.000 52.83155  ? 189 LEU E C   1 
ATOM   5772 O O   . LEU E 5 175 ? 26.29078  -24.92680 7.11268   1.000 49.23827  ? 189 LEU E O   1 
ATOM   5773 C CB  . LEU E 5 175 ? 24.93833  -24.91503 4.21813   1.000 38.79124  ? 189 LEU E CB  1 
ATOM   5774 C CG  . LEU E 5 175 ? 24.14009  -24.42258 3.01494   1.000 56.60835  ? 189 LEU E CG  1 
ATOM   5775 C CD1 . LEU E 5 175 ? 24.60644  -25.11269 1.74093   1.000 54.35665  ? 189 LEU E CD1 1 
ATOM   5776 C CD2 . LEU E 5 175 ? 22.65729  -24.65555 3.24708   1.000 46.92055  ? 189 LEU E CD2 1 
ATOM   5777 N N   . LYS E 5 176 ? 24.37445  -26.10646 7.18125   1.000 57.67725  ? 190 LYS E N   1 
ATOM   5778 C CA  . LYS E 5 176 ? 24.84060  -27.01234 8.22177   1.000 54.44408  ? 190 LYS E CA  1 
ATOM   5779 C C   . LYS E 5 176 ? 25.42763  -28.25787 7.56923   1.000 53.43839  ? 190 LYS E C   1 
ATOM   5780 O O   . LYS E 5 176 ? 24.73217  -28.96871 6.83693   1.000 66.25087  ? 190 LYS E O   1 
ATOM   5781 C CB  . LYS E 5 176 ? 23.70320  -27.36804 9.17837   1.000 51.51697  ? 190 LYS E CB  1 
ATOM   5782 C CG  . LYS E 5 176 ? 23.34812  -26.23188 10.13174  1.000 62.67511  ? 190 LYS E CG  1 
ATOM   5783 C CD  . LYS E 5 176 ? 22.03608  -26.46848 10.87581  1.000 57.94347  ? 190 LYS E CD  1 
ATOM   5784 C CE  . LYS E 5 176 ? 22.25393  -27.10150 12.24453  1.000 64.03816  ? 190 LYS E CE  1 
ATOM   5785 N NZ  . LYS E 5 176 ? 21.14824  -26.76645 13.19519  1.000 75.23029  ? 190 LYS E NZ  1 
ATOM   5786 N N   . GLU E 5 177 ? 26.71277  -28.51124 7.82519   1.000 54.74859  ? 191 GLU E N   1 
ATOM   5787 C CA  . GLU E 5 177 ? 27.36884  -29.67874 7.25180   1.000 63.37283  ? 191 GLU E CA  1 
ATOM   5788 C C   . GLU E 5 177 ? 26.79926  -30.98057 7.80133   1.000 72.45233  ? 191 GLU E C   1 
ATOM   5789 O O   . GLU E 5 177 ? 26.97735  -32.03387 7.17954   1.000 72.05943  ? 191 GLU E O   1 
ATOM   5790 C CB  . GLU E 5 177 ? 28.87801  -29.59479 7.49345   1.000 59.81826  ? 191 GLU E CB  1 
ATOM   5791 C CG  . GLU E 5 177 ? 29.50102  -28.31351 6.93915   1.000 56.12808  ? 191 GLU E CG  1 
ATOM   5792 C CD  . GLU E 5 177 ? 31.02125  -28.36036 6.86499   1.000 66.90512  ? 191 GLU E CD  1 
ATOM   5793 O OE1 . GLU E 5 177 ? 31.64885  -29.03956 7.70794   1.000 59.83639  ? 191 GLU E OE1 1 
ATOM   5794 O OE2 . GLU E 5 177 ? 31.58883  -27.71498 5.95453   1.000 70.79881  ? 191 GLU E OE2 1 
ATOM   5795 N N   . GLN E 5 178 ? 26.11392  -30.92644 8.94358   1.000 73.25000  ? 192 GLN E N   1 
ATOM   5796 C CA  . GLN E 5 178 ? 25.35736  -32.06069 9.47148   1.000 65.40241  ? 192 GLN E CA  1 
ATOM   5797 C C   . GLN E 5 178 ? 24.00913  -31.52681 9.93503   1.000 65.36156  ? 192 GLN E C   1 
ATOM   5798 O O   . GLN E 5 178 ? 23.84075  -31.14454 11.10040  1.000 65.65671  ? 192 GLN E O   1 
ATOM   5799 C CB  . GLN E 5 178 ? 26.10696  -32.75774 10.60763  1.000 57.82864  ? 192 GLN E CB  1 
ATOM   5800 N N   . PRO E 5 179 ? 23.01185  -31.50406 9.04494   1.000 68.75942  ? 193 PRO E N   1 
ATOM   5801 C CA  . PRO E 5 179 ? 21.77982  -30.74129 9.32193   1.000 66.82736  ? 193 PRO E CA  1 
ATOM   5802 C C   . PRO E 5 179 ? 21.00543  -31.18560 10.55902  1.000 87.58364  ? 193 PRO E C   1 
ATOM   5803 O O   . PRO E 5 179 ? 20.08822  -30.46312 10.97245  1.000 82.28832  ? 193 PRO E O   1 
ATOM   5804 C CB  . PRO E 5 179 ? 20.94602  -30.95152 8.05000   1.000 59.21101  ? 193 PRO E CB  1 
ATOM   5805 C CG  . PRO E 5 179 ? 21.94308  -31.31102 6.99496   1.000 57.01473  ? 193 PRO E CG  1 
ATOM   5806 C CD  . PRO E 5 179 ? 23.00072  -32.10211 7.69966   1.000 67.46975  ? 193 PRO E CD  1 
ATOM   5807 N N   . ALA E 5 180 ? 21.33164  -32.32953 11.16125  1.000 86.96287  ? 194 ALA E N   1 
ATOM   5808 C CA  . ALA E 5 180 ? 20.59767  -32.79369 12.33409  1.000 85.22266  ? 194 ALA E CA  1 
ATOM   5809 C C   . ALA E 5 180 ? 21.19516  -32.26464 13.63513  1.000 79.91330  ? 194 ALA E C   1 
ATOM   5810 O O   . ALA E 5 180 ? 20.46349  -31.79180 14.51072  1.000 82.87683  ? 194 ALA E O   1 
ATOM   5811 C CB  . ALA E 5 180 ? 20.55474  -34.32434 12.35638  1.000 84.21951  ? 194 ALA E CB  1 
ATOM   5812 N N   . LEU E 5 181 ? 22.51624  -32.33684 13.77307  1.000 80.16705  ? 195 LEU E N   1 
ATOM   5813 C CA  . LEU E 5 181 ? 23.17372  -31.89227 14.99398  1.000 82.66483  ? 195 LEU E CA  1 
ATOM   5814 C C   . LEU E 5 181 ? 23.04994  -30.38126 15.15843  1.000 80.85357  ? 195 LEU E C   1 
ATOM   5815 O O   . LEU E 5 181 ? 23.12077  -29.62573 14.18528  1.000 89.51004  ? 195 LEU E O   1 
ATOM   5816 C CB  . LEU E 5 181 ? 24.65020  -32.29345 14.97361  1.000 70.05421  ? 195 LEU E CB  1 
ATOM   5817 C CG  . LEU E 5 181 ? 24.98575  -33.74397 14.61255  1.000 73.35075  ? 195 LEU E CG  1 
ATOM   5818 C CD1 . LEU E 5 181 ? 26.48904  -33.92186 14.47195  1.000 61.08795  ? 195 LEU E CD1 1 
ATOM   5819 C CD2 . LEU E 5 181 ? 24.42575  -34.71327 15.64441  1.000 74.19964  ? 195 LEU E CD2 1 
ATOM   5820 N N   . ASN E 5 182 ? 22.85653  -29.94018 16.40417  1.000 88.54333  ? 196 ASN E N   1 
ATOM   5821 C CA  . ASN E 5 182 ? 22.90443  -28.51400 16.70359  1.000 88.58462  ? 196 ASN E CA  1 
ATOM   5822 C C   . ASN E 5 182 ? 24.32749  -28.00721 16.87802  1.000 78.27962  ? 196 ASN E C   1 
ATOM   5823 O O   . ASN E 5 182 ? 24.55871  -26.79724 16.77956  1.000 77.03045  ? 196 ASN E O   1 
ATOM   5824 C CB  . ASN E 5 182 ? 22.08954  -28.19866 17.95820  1.000 81.69843  ? 196 ASN E CB  1 
ATOM   5825 C CG  . ASN E 5 182 ? 20.81693  -27.44281 17.64241  1.000 94.75860  ? 196 ASN E CG  1 
ATOM   5826 O OD1 . ASN E 5 182 ? 20.20847  -27.64371 16.59006  1.000 93.46584  ? 196 ASN E OD1 1 
ATOM   5827 N ND2 . ASN E 5 182 ? 20.41402  -26.55686 18.54538  1.000 90.27091  ? 196 ASN E ND2 1 
ATOM   5828 N N   . ASP E 5 183 ? 25.27650  -28.90119 17.13878  1.000 76.16864  ? 197 ASP E N   1 
ATOM   5829 C CA  . ASP E 5 183 ? 26.69200  -28.56826 17.15345  1.000 69.94077  ? 197 ASP E CA  1 
ATOM   5830 C C   . ASP E 5 183 ? 27.32810  -28.68323 15.77324  1.000 68.70932  ? 197 ASP E C   1 
ATOM   5831 O O   . ASP E 5 183 ? 28.55997  -28.67829 15.66906  1.000 71.00082  ? 197 ASP E O   1 
ATOM   5832 C CB  . ASP E 5 183 ? 27.43493  -29.46819 18.14755  1.000 70.18901  ? 197 ASP E CB  1 
ATOM   5833 N N   . SER E 5 184 ? 26.51783  -28.78069 14.71953  1.000 65.62463  ? 198 SER E N   1 
ATOM   5834 C CA  . SER E 5 184 ? 27.04397  -29.00167 13.37983  1.000 45.17278  ? 198 SER E CA  1 
ATOM   5835 C C   . SER E 5 184 ? 27.91346  -27.83841 12.92906  1.000 47.87161  ? 198 SER E C   1 
ATOM   5836 O O   . SER E 5 184 ? 27.57851  -26.66905 13.13634  1.000 37.87542  ? 198 SER E O   1 
ATOM   5837 C CB  . SER E 5 184 ? 25.90416  -29.19404 12.38429  1.000 51.08863  ? 198 SER E CB  1 
ATOM   5838 O OG  . SER E 5 184 ? 26.37722  -29.05385 11.05237  1.000 60.71522  ? 198 SER E OG  1 
ATOM   5839 N N   . ARG E 5 185 ? 29.03463  -28.16894 12.29837  1.000 41.89357  ? 199 ARG E N   1 
ATOM   5840 C CA  . ARG E 5 185 ? 29.85199  -27.15047 11.66871  1.000 37.42525  ? 199 ARG E CA  1 
ATOM   5841 C C   . ARG E 5 185 ? 29.11614  -26.56572 10.46477  1.000 48.04152  ? 199 ARG E C   1 
ATOM   5842 O O   . ARG E 5 185 ? 28.19536  -27.17235 9.90768   1.000 43.56530  ? 199 ARG E O   1 
ATOM   5843 C CB  . ARG E 5 185 ? 31.20375  -27.73708 11.26757  1.000 44.69660  ? 199 ARG E CB  1 
ATOM   5844 C CG  . ARG E 5 185 ? 31.95324  -28.31329 12.45780  1.000 44.32673  ? 199 ARG E CG  1 
ATOM   5845 C CD  . ARG E 5 185 ? 33.09355  -29.22490 12.05214  1.000 44.66437  ? 199 ARG E CD  1 
ATOM   5846 N NE  . ARG E 5 185 ? 34.24103  -28.48104 11.55000  1.000 50.61175  ? 199 ARG E NE  1 
ATOM   5847 C CZ  . ARG E 5 185 ? 35.46543  -28.97936 11.45272  1.000 40.02278  ? 199 ARG E CZ  1 
ATOM   5848 N NH1 . ARG E 5 185 ? 35.73937  -30.21722 11.83145  1.000 51.56013  ? 199 ARG E NH1 1 
ATOM   5849 N NH2 . ARG E 5 185 ? 36.44039  -28.21533 10.97022  1.000 51.55865  ? 199 ARG E NH2 1 
ATOM   5850 N N   . TYR E 5 186 ? 29.52228  -25.36144 10.07800  1.000 48.83418  ? 200 TYR E N   1 
ATOM   5851 C CA  . TYR E 5 186 ? 28.81229  -24.57926 9.08008   1.000 39.23830  ? 200 TYR E CA  1 
ATOM   5852 C C   . TYR E 5 186 ? 29.63461  -24.41868 7.80915   1.000 43.28715  ? 200 TYR E C   1 
ATOM   5853 O O   . TYR E 5 186 ? 30.85796  -24.57731 7.80162   1.000 50.56865  ? 200 TYR E O   1 
ATOM   5854 C CB  . TYR E 5 186 ? 28.46350  -23.18870 9.61321   1.000 32.23418  ? 200 TYR E CB  1 
ATOM   5855 C CG  . TYR E 5 186 ? 27.48140  -23.15979 10.75604  1.000 46.20564  ? 200 TYR E CG  1 
ATOM   5856 C CD1 . TYR E 5 186 ? 26.11250  -23.22920 10.52097  1.000 45.79148  ? 200 TYR E CD1 1 
ATOM   5857 C CD2 . TYR E 5 186 ? 27.91826  -23.02770 12.07041  1.000 29.43609  ? 200 TYR E CD2 1 
ATOM   5858 C CE1 . TYR E 5 186 ? 25.20679  -23.18461 11.56357  1.000 32.78365  ? 200 TYR E CE1 1 
ATOM   5859 C CE2 . TYR E 5 186 ? 27.01972  -22.98525 13.11866  1.000 35.24953  ? 200 TYR E CE2 1 
ATOM   5860 C CZ  . TYR E 5 186 ? 25.66475  -23.06219 12.86002  1.000 31.24892  ? 200 TYR E CZ  1 
ATOM   5861 O OH  . TYR E 5 186 ? 24.76237  -23.02038 13.89915  1.000 29.29171  ? 200 TYR E OH  1 
ATOM   5862 N N   . ALA E 5 187 ? 28.93229  -24.07803 6.73061   1.000 37.39271  ? 201 ALA E N   1 
ATOM   5863 C CA  . ALA E 5 187 ? 29.54119  -23.67530 5.47464   1.000 40.93655  ? 201 ALA E CA  1 
ATOM   5864 C C   . ALA E 5 187 ? 28.84345  -22.42068 4.97073   1.000 38.66573  ? 201 ALA E C   1 
ATOM   5865 O O   . ALA E 5 187 ? 27.63710  -22.24486 5.15983   1.000 38.82297  ? 201 ALA E O   1 
ATOM   5866 C CB  . ALA E 5 187 ? 29.46204  -24.78109 4.41790   1.000 45.42701  ? 201 ALA E CB  1 
ATOM   5867 N N   . LEU E 5 188 ? 29.61509  -21.54634 4.32998   1.000 33.52130  ? 202 LEU E N   1 
ATOM   5868 C CA  . LEU E 5 188 ? 29.10604  -20.28708 3.80441   1.000 30.70347  ? 202 LEU E CA  1 
ATOM   5869 C C   . LEU E 5 188 ? 29.76724  -20.01471 2.46019   1.000 40.68134  ? 202 LEU E C   1 
ATOM   5870 O O   . LEU E 5 188 ? 30.96889  -20.24360 2.29988   1.000 42.98575  ? 202 LEU E O   1 
ATOM   5871 C CB  . LEU E 5 188 ? 29.38151  -19.13221 4.77783   1.000 31.65517  ? 202 LEU E CB  1 
ATOM   5872 C CG  . LEU E 5 188 ? 28.77671  -17.75966 4.48159   1.000 39.75111  ? 202 LEU E CG  1 
ATOM   5873 C CD1 . LEU E 5 188 ? 27.30208  -17.72644 4.85468   1.000 35.74354  ? 202 LEU E CD1 1 
ATOM   5874 C CD2 . LEU E 5 188 ? 29.54555  -16.66646 5.20826   1.000 29.35329  ? 202 LEU E CD2 1 
ATOM   5875 N N   . SER E 5 189 ? 28.98550  -19.53512 1.49373   1.000 36.62411  ? 203 SER E N   1 
ATOM   5876 C CA  . SER E 5 189 ? 29.50708  -19.22326 0.17075   1.000 49.94956  ? 203 SER E CA  1 
ATOM   5877 C C   . SER E 5 189 ? 29.24123  -17.76563 -0.17466  1.000 38.41606  ? 203 SER E C   1 
ATOM   5878 O O   . SER E 5 189 ? 28.33188  -17.12589 0.36066   1.000 33.52264  ? 203 SER E O   1 
ATOM   5879 C CB  . SER E 5 189 ? 28.90229  -20.12584 -0.92171  1.000 47.15887  ? 203 SER E CB  1 
ATOM   5880 O OG  . SER E 5 189 ? 27.62321  -19.66809 -1.33404  1.000 41.05084  ? 203 SER E OG  1 
ATOM   5881 N N   . SER E 5 190 ? 30.05149  -17.25285 -1.09299  1.000 35.24803  ? 204 SER E N   1 
ATOM   5882 C CA  . SER E 5 190 ? 29.90922  -15.88954 -1.57059  1.000 32.96675  ? 204 SER E CA  1 
ATOM   5883 C C   . SER E 5 190 ? 30.34401  -15.83935 -3.02691  1.000 38.99833  ? 204 SER E C   1 
ATOM   5884 O O   . SER E 5 190 ? 31.17243  -16.64060 -3.46887  1.000 40.31581  ? 204 SER E O   1 
ATOM   5885 C CB  . SER E 5 190 ? 30.73687  -14.91903 -0.72449  1.000 26.46990  ? 204 SER E CB  1 
ATOM   5886 O OG  . SER E 5 190 ? 30.44195  -13.57663 -1.05222  1.000 34.36613  ? 204 SER E OG  1 
ATOM   5887 N N   . ARG E 5 191 ? 29.77605  -14.89669 -3.77199  1.000 32.02215  ? 205 ARG E N   1 
ATOM   5888 C CA  . ARG E 5 191 ? 30.14190  -14.68506 -5.16534  1.000 37.51172  ? 205 ARG E CA  1 
ATOM   5889 C C   . ARG E 5 191 ? 30.59366  -13.24386 -5.36715  1.000 46.12157  ? 205 ARG E C   1 
ATOM   5890 O O   . ARG E 5 191 ? 30.01916  -12.31496 -4.79108  1.000 40.31059  ? 205 ARG E O   1 
ATOM   5891 C CB  . ARG E 5 191 ? 28.97247  -14.99836 -6.11689  1.000 35.67125  ? 205 ARG E CB  1 
ATOM   5892 C CG  . ARG E 5 191 ? 28.14663  -16.23064 -5.75656  1.000 35.98128  ? 205 ARG E CG  1 
ATOM   5893 C CD  . ARG E 5 191 ? 26.87979  -15.82676 -5.00734  1.000 47.75071  ? 205 ARG E CD  1 
ATOM   5894 N NE  . ARG E 5 191 ? 25.95649  -16.93430 -4.77435  1.000 41.94290  ? 205 ARG E NE  1 
ATOM   5895 C CZ  . ARG E 5 191 ? 25.79217  -17.53807 -3.60405  1.000 46.16366  ? 205 ARG E CZ  1 
ATOM   5896 N NH1 . ARG E 5 191 ? 26.51711  -17.20652 -2.54784  1.000 50.32773  ? 205 ARG E NH1 1 
ATOM   5897 N NH2 . ARG E 5 191 ? 24.86707  -18.48753 -3.48546  1.000 40.45568  ? 205 ARG E NH2 1 
ATOM   5898 N N   . LEU E 5 192 ? 31.63470  -13.06350 -6.17628  1.000 34.53565  ? 206 LEU E N   1 
ATOM   5899 C CA  . LEU E 5 192 ? 32.04537  -11.74817 -6.64967  1.000 41.14036  ? 206 LEU E CA  1 
ATOM   5900 C C   . LEU E 5 192 ? 32.09585  -11.79817 -8.16856  1.000 49.78275  ? 206 LEU E C   1 
ATOM   5901 O O   . LEU E 5 192 ? 32.89313  -12.54905 -8.74104  1.000 44.63084  ? 206 LEU E O   1 
ATOM   5902 C CB  . LEU E 5 192 ? 33.40230  -11.33879 -6.07269  1.000 36.75427  ? 206 LEU E CB  1 
ATOM   5903 C CG  . LEU E 5 192 ? 34.09564  -10.14421 -6.73812  1.000 41.56964  ? 206 LEU E CG  1 
ATOM   5904 C CD1 . LEU E 5 192 ? 33.24414  -8.88888  -6.65349  1.000 40.56701  ? 206 LEU E CD1 1 
ATOM   5905 C CD2 . LEU E 5 192 ? 35.45611  -9.90282  -6.11215  1.000 43.92970  ? 206 LEU E CD2 1 
ATOM   5906 N N   . ARG E 5 193 ? 31.24021  -11.01565 -8.81811  1.000 47.44403  ? 207 ARG E N   1 
ATOM   5907 C CA  . ARG E 5 193 ? 31.14727  -10.99636 -10.27044 1.000 43.61150  ? 207 ARG E CA  1 
ATOM   5908 C C   . ARG E 5 193 ? 31.72982  -9.69359  -10.79563 1.000 51.92604  ? 207 ARG E C   1 
ATOM   5909 O O   . ARG E 5 193 ? 31.34712  -8.60716  -10.34666 1.000 45.47260  ? 207 ARG E O   1 
ATOM   5910 C CB  . ARG E 5 193 ? 29.70008  -11.16034 -10.73765 1.000 31.23219  ? 207 ARG E CB  1 
ATOM   5911 C CG  . ARG E 5 193 ? 29.58924  -11.66509 -12.16306 1.000 49.68552  ? 207 ARG E CG  1 
ATOM   5912 C CD  . ARG E 5 193 ? 28.17005  -12.07538 -12.51725 1.000 42.33002  ? 207 ARG E CD  1 
ATOM   5913 N NE  . ARG E 5 193 ? 28.15191  -12.93708 -13.69430 1.000 57.10184  ? 207 ARG E NE  1 
ATOM   5914 C CZ  . ARG E 5 193 ? 27.06002  -13.48730 -14.20777 1.000 53.08255  ? 207 ARG E CZ  1 
ATOM   5915 N NH1 . ARG E 5 193 ? 25.86389  -13.26027 -13.69082 1.000 37.86221  ? 207 ARG E NH1 1 
ATOM   5916 N NH2 . ARG E 5 193 ? 27.17269  -14.29303 -15.26050 1.000 45.81440  ? 207 ARG E NH2 1 
ATOM   5917 N N   . VAL E 5 194 ? 32.66440  -9.81093  -11.73573 1.000 52.24940  ? 208 VAL E N   1 
ATOM   5918 C CA  . VAL E 5 194 ? 33.28542  -8.67107  -12.39028 1.000 44.78404  ? 208 VAL E CA  1 
ATOM   5919 C C   . VAL E 5 194 ? 33.15905  -8.86189  -13.89696 1.000 53.62798  ? 208 VAL E C   1 
ATOM   5920 O O   . VAL E 5 194 ? 32.76268  -9.92319  -14.38219 1.000 56.79884  ? 208 VAL E O   1 
ATOM   5921 C CB  . VAL E 5 194 ? 34.76190  -8.49876  -11.98095 1.000 40.73170  ? 208 VAL E CB  1 
ATOM   5922 C CG1 . VAL E 5 194 ? 34.86703  -8.25914  -10.47899 1.000 42.70853  ? 208 VAL E CG1 1 
ATOM   5923 C CG2 . VAL E 5 194 ? 35.56067  -9.72401  -12.38286 1.000 47.88477  ? 208 VAL E CG2 1 
ATOM   5924 N N   . SER E 5 195 ? 33.49137  -7.80967  -14.63924 1.000 64.99433  ? 209 SER E N   1 
ATOM   5925 C CA  . SER E 5 195 ? 33.51598  -7.92591  -16.08966 1.000 61.84290  ? 209 SER E CA  1 
ATOM   5926 C C   . SER E 5 195 ? 34.60482  -8.90540  -16.51451 1.000 62.81531  ? 209 SER E C   1 
ATOM   5927 O O   . SER E 5 195 ? 35.61519  -9.08118  -15.82651 1.000 58.93226  ? 209 SER E O   1 
ATOM   5928 C CB  . SER E 5 195 ? 33.75044  -6.55970  -16.73401 1.000 53.45038  ? 209 SER E CB  1 
ATOM   5929 O OG  . SER E 5 195 ? 35.03591  -6.05225  -16.41386 1.000 62.40168  ? 209 SER E OG  1 
ATOM   5930 N N   . ALA E 5 196 ? 34.38392  -9.56367  -17.65632 1.000 64.27597  ? 210 ALA E N   1 
ATOM   5931 C CA  . ALA E 5 196 ? 35.38576  -10.49395 -18.16745 1.000 65.15403  ? 210 ALA E CA  1 
ATOM   5932 C C   . ALA E 5 196 ? 36.71332  -9.79010  -18.40753 1.000 64.84365  ? 210 ALA E C   1 
ATOM   5933 O O   . ALA E 5 196 ? 37.78286  -10.36309 -18.16852 1.000 55.60644  ? 210 ALA E O   1 
ATOM   5934 C CB  . ALA E 5 196 ? 34.89250  -11.15246 -19.45444 1.000 58.17893  ? 210 ALA E CB  1 
ATOM   5935 N N   . THR E 5 197 ? 36.66394  -8.54163  -18.87411 1.000 68.10971  ? 211 THR E N   1 
ATOM   5936 C CA  . THR E 5 197 ? 37.89309  -7.79557  -19.11679 1.000 68.66344  ? 211 THR E CA  1 
ATOM   5937 C C   . THR E 5 197 ? 38.65609  -7.55633  -17.82079 1.000 63.96849  ? 211 THR E C   1 
ATOM   5938 O O   . THR E 5 197 ? 39.88641  -7.67431  -17.78602 1.000 77.67650  ? 211 THR E O   1 
ATOM   5939 C CB  . THR E 5 197 ? 37.57024  -6.47147  -19.81048 1.000 68.48753  ? 211 THR E CB  1 
ATOM   5940 O OG1 . THR E 5 197 ? 36.48447  -5.82862  -19.12975 1.000 73.72374  ? 211 THR E OG1 1 
ATOM   5941 C CG2 . THR E 5 197 ? 37.17553  -6.71591  -21.26016 1.000 77.10291  ? 211 THR E CG2 1 
ATOM   5942 N N   . PHE E 5 198 ? 37.94167  -7.23835  -16.73908 1.000 70.38983  ? 212 PHE E N   1 
ATOM   5943 C CA  . PHE E 5 198 ? 38.60712  -6.97064  -15.46833 1.000 62.17990  ? 212 PHE E CA  1 
ATOM   5944 C C   . PHE E 5 198 ? 39.28327  -8.22175  -14.91496 1.000 61.72238  ? 212 PHE E C   1 
ATOM   5945 O O   . PHE E 5 198 ? 40.35108  -8.13346  -14.29646 1.000 55.38316  ? 212 PHE E O   1 
ATOM   5946 C CB  . PHE E 5 198 ? 37.60445  -6.40977  -14.45977 1.000 58.18208  ? 212 PHE E CB  1 
ATOM   5947 C CG  . PHE E 5 198 ? 38.23166  -5.95876  -13.16942 1.000 58.12139  ? 212 PHE E CG  1 
ATOM   5948 C CD1 . PHE E 5 198 ? 38.86739  -4.73013  -13.08728 1.000 52.97777  ? 212 PHE E CD1 1 
ATOM   5949 C CD2 . PHE E 5 198 ? 38.18490  -6.76079  -12.04052 1.000 51.76433  ? 212 PHE E CD2 1 
ATOM   5950 C CE1 . PHE E 5 198 ? 39.44697  -4.31154  -11.90688 1.000 55.75551  ? 212 PHE E CE1 1 
ATOM   5951 C CE2 . PHE E 5 198 ? 38.76343  -6.34713  -10.85439 1.000 54.77030  ? 212 PHE E CE2 1 
ATOM   5952 C CZ  . PHE E 5 198 ? 39.39526  -5.12039  -10.78866 1.000 55.80690  ? 212 PHE E CZ  1 
ATOM   5953 N N   . TRP E 5 199 ? 38.67895  -9.39487  -15.12209 1.000 53.89633  ? 213 TRP E N   1 
ATOM   5954 C CA  . TRP E 5 199 ? 39.27721  -10.62854 -14.62049 1.000 61.77881  ? 213 TRP E CA  1 
ATOM   5955 C C   . TRP E 5 199 ? 40.49988  -11.02817 -15.43424 1.000 71.94145  ? 213 TRP E C   1 
ATOM   5956 O O   . TRP E 5 199 ? 41.46480  -11.57518 -14.88652 1.000 64.72602  ? 213 TRP E O   1 
ATOM   5957 C CB  . TRP E 5 199 ? 38.24972  -11.75721 -14.62921 1.000 52.35290  ? 213 TRP E CB  1 
ATOM   5958 C CG  . TRP E 5 199 ? 38.86616  -13.11411 -14.46396 1.000 60.10502  ? 213 TRP E CG  1 
ATOM   5959 C CD1 . TRP E 5 199 ? 38.95480  -14.09556 -15.40823 1.000 59.98811  ? 213 TRP E CD1 1 
ATOM   5960 C CD2 . TRP E 5 199 ? 39.49853  -13.63300 -13.28670 1.000 64.60142  ? 213 TRP E CD2 1 
ATOM   5961 N NE1 . TRP E 5 199 ? 39.59296  -15.19748 -14.88930 1.000 55.69702  ? 213 TRP E NE1 1 
ATOM   5962 C CE2 . TRP E 5 199 ? 39.93830  -14.93796 -13.58926 1.000 65.50734  ? 213 TRP E CE2 1 
ATOM   5963 C CE3 . TRP E 5 199 ? 39.73046  -13.12323 -12.00477 1.000 53.57690  ? 213 TRP E CE3 1 
ATOM   5964 C CZ2 . TRP E 5 199 ? 40.59538  -15.73956 -12.65730 1.000 66.38660  ? 213 TRP E CZ2 1 
ATOM   5965 C CZ3 . TRP E 5 199 ? 40.38285  -13.92038 -11.08084 1.000 59.36503  ? 213 TRP E CZ3 1 
ATOM   5966 C CH2 . TRP E 5 199 ? 40.80451  -15.21571 -11.41006 1.000 64.61885  ? 213 TRP E CH2 1 
ATOM   5967 N N   . GLN E 5 200 ? 40.47860  -10.76826 -16.74140 1.000 69.72881  ? 214 GLN E N   1 
ATOM   5968 C CA  . GLN E 5 200 ? 41.56115  -11.21092 -17.61213 1.000 66.01447  ? 214 GLN E CA  1 
ATOM   5969 C C   . GLN E 5 200 ? 42.82267  -10.37295 -17.47653 1.000 67.13863  ? 214 GLN E C   1 
ATOM   5970 O O   . GLN E 5 200 ? 43.81447  -10.67858 -18.14807 1.000 81.46217  ? 214 GLN E O   1 
ATOM   5971 C CB  . GLN E 5 200 ? 41.08392  -11.22444 -19.06391 1.000 70.32409  ? 214 GLN E CB  1 
ATOM   5972 C CG  . GLN E 5 200 ? 40.35075  -12.50482 -19.43483 1.000 62.14984  ? 214 GLN E CG  1 
ATOM   5973 C CD  . GLN E 5 200 ? 39.32787  -12.30232 -20.53148 1.000 67.04878  ? 214 GLN E CD  1 
ATOM   5974 O OE1 . GLN E 5 200 ? 39.06239  -11.17410 -20.95202 1.000 59.57232  ? 214 GLN E OE1 1 
ATOM   5975 N NE2 . GLN E 5 200 ? 38.74193  -13.39905 -21.00012 1.000 67.00791  ? 214 GLN E NE2 1 
ATOM   5976 N N   . ASN E 5 201 ? 42.81248  -9.33874  -16.63890 1.000 62.02470  ? 215 ASN E N   1 
ATOM   5977 C CA  . ASN E 5 201 ? 44.01677  -8.58963  -16.30745 1.000 59.20357  ? 215 ASN E CA  1 
ATOM   5978 C C   . ASN E 5 201 ? 44.72566  -9.31431  -15.17052 1.000 69.77448  ? 215 ASN E C   1 
ATOM   5979 O O   . ASN E 5 201 ? 44.24013  -9.30949  -14.03294 1.000 69.92704  ? 215 ASN E O   1 
ATOM   5980 C CB  . ASN E 5 201 ? 43.66677  -7.14487  -15.93100 1.000 47.61742  ? 215 ASN E CB  1 
ATOM   5981 C CG  . ASN E 5 201 ? 44.88480  -6.31452  -15.52737 1.000 58.67573  ? 215 ASN E CG  1 
ATOM   5982 O OD1 . ASN E 5 201 ? 46.01504  -6.80071  -15.48883 1.000 63.28292  ? 215 ASN E OD1 1 
ATOM   5983 N ND2 . ASN E 5 201 ? 44.64850  -5.04043  -15.23533 1.000 53.83481  ? 215 ASN E ND2 1 
ATOM   5984 N N   . PRO E 5 202 ? 45.87175  -9.94886  -15.44173 1.000 73.77760  ? 216 PRO E N   1 
ATOM   5985 C CA  . PRO E 5 202 ? 46.56893  -10.72379 -14.40239 1.000 54.34867  ? 216 PRO E CA  1 
ATOM   5986 C C   . PRO E 5 202 ? 47.20106  -9.88193  -13.30507 1.000 64.00643  ? 216 PRO E C   1 
ATOM   5987 O O   . PRO E 5 202 ? 47.80109  -10.45140 -12.38426 1.000 53.90902  ? 216 PRO E O   1 
ATOM   5988 C CB  . PRO E 5 202 ? 47.65145  -11.47687 -15.19406 1.000 61.47406  ? 216 PRO E CB  1 
ATOM   5989 C CG  . PRO E 5 202 ? 47.23731  -11.36788 -16.64571 1.000 84.00302  ? 216 PRO E CG  1 
ATOM   5990 C CD  . PRO E 5 202 ? 46.53370  -10.05871 -16.75034 1.000 64.82957  ? 216 PRO E CD  1 
ATOM   5991 N N   . ARG E 5 203 ? 47.11135  -8.55473  -13.37581 1.000 61.00919  ? 217 ARG E N   1 
ATOM   5992 C CA  . ARG E 5 203 ? 47.61333  -7.70677  -12.30506 1.000 63.98587  ? 217 ARG E CA  1 
ATOM   5993 C C   . ARG E 5 203 ? 46.57058  -7.43554  -11.22796 1.000 71.84513  ? 217 ARG E C   1 
ATOM   5994 O O   . ARG E 5 203 ? 46.93182  -6.97557  -10.13920 1.000 64.51898  ? 217 ARG E O   1 
ATOM   5995 C CB  . ARG E 5 203 ? 48.12083  -6.37723  -12.87496 1.000 57.27481  ? 217 ARG E CB  1 
ATOM   5996 N N   . ASN E 5 204 ? 45.29645  -7.71400  -11.49828 1.000 64.32149  ? 218 ASN E N   1 
ATOM   5997 C CA  . ASN E 5 204 ? 44.24207  -7.50335  -10.51537 1.000 56.33748  ? 218 ASN E CA  1 
ATOM   5998 C C   . ASN E 5 204 ? 44.28069  -8.59564  -9.45217  1.000 62.24197  ? 218 ASN E C   1 
ATOM   5999 O O   . ASN E 5 204 ? 44.39879  -9.78249  -9.76995  1.000 60.66755  ? 218 ASN E O   1 
ATOM   6000 C CB  . ASN E 5 204 ? 42.87834  -7.47054  -11.20158 1.000 54.53406  ? 218 ASN E CB  1 
ATOM   6001 C CG  . ASN E 5 204 ? 42.66127  -6.19830  -11.99103 1.000 49.72533  ? 218 ASN E CG  1 
ATOM   6002 O OD1 . ASN E 5 204 ? 43.23884  -5.15990  -11.67330 1.000 54.65948  ? 218 ASN E OD1 1 
ATOM   6003 N ND2 . ASN E 5 204 ? 41.82403  -6.26814  -13.02202 1.000 51.46471  ? 218 ASN E ND2 1 
ATOM   6004 N N   . HIS E 5 205 ? 44.17143  -8.19237  -8.18928  1.000 60.83345  ? 219 HIS E N   1 
ATOM   6005 C CA  . HIS E 5 205 ? 44.32316  -9.08953  -7.04934  1.000 55.20452  ? 219 HIS E CA  1 
ATOM   6006 C C   . HIS E 5 205 ? 42.97459  -9.27385  -6.36268  1.000 58.27944  ? 219 HIS E C   1 
ATOM   6007 O O   . HIS E 5 205 ? 42.37833  -8.29911  -5.89448  1.000 54.32754  ? 219 HIS E O   1 
ATOM   6008 C CB  . HIS E 5 205 ? 45.35338  -8.53260  -6.06827  1.000 54.08712  ? 219 HIS E CB  1 
ATOM   6009 C CG  . HIS E 5 205 ? 45.65837  -9.45021  -4.92828  1.000 60.85606  ? 219 HIS E CG  1 
ATOM   6010 N ND1 . HIS E 5 205 ? 45.54512  -10.82034 -5.02640  1.000 69.18484  ? 219 HIS E ND1 1 
ATOM   6011 C CD2 . HIS E 5 205 ? 46.07062  -9.19563  -3.66444  1.000 62.73548  ? 219 HIS E CD2 1 
ATOM   6012 C CE1 . HIS E 5 205 ? 45.87605  -11.37104 -3.87239  1.000 61.87697  ? 219 HIS E CE1 1 
ATOM   6013 N NE2 . HIS E 5 205 ? 46.19798  -10.40694 -3.02854  1.000 71.94353  ? 219 HIS E NE2 1 
ATOM   6014 N N   . PHE E 5 206 ? 42.50846  -10.52018 -6.28990  1.000 51.15448  ? 220 PHE E N   1 
ATOM   6015 C CA  . PHE E 5 206 ? 41.22775  -10.86851 -5.68012  1.000 47.43115  ? 220 PHE E CA  1 
ATOM   6016 C C   . PHE E 5 206 ? 41.46528  -11.68975 -4.41984  1.000 49.85384  ? 220 PHE E C   1 
ATOM   6017 O O   . PHE E 5 206 ? 42.14545  -12.71921 -4.47144  1.000 51.42863  ? 220 PHE E O   1 
ATOM   6018 C CB  . PHE E 5 206 ? 40.35383  -11.66849 -6.65146  1.000 47.31646  ? 220 PHE E CB  1 
ATOM   6019 C CG  . PHE E 5 206 ? 40.06553  -10.95739 -7.94039  1.000 53.92840  ? 220 PHE E CG  1 
ATOM   6020 C CD1 . PHE E 5 206 ? 40.98021  -10.97905 -8.98146  1.000 57.09688  ? 220 PHE E CD1 1 
ATOM   6021 C CD2 . PHE E 5 206 ? 38.87249  -10.27630 -8.11616  1.000 48.08082  ? 220 PHE E CD2 1 
ATOM   6022 C CE1 . PHE E 5 206 ? 40.71278  -10.32504 -10.16809 1.000 58.19484  ? 220 PHE E CE1 1 
ATOM   6023 C CE2 . PHE E 5 206 ? 38.60090  -9.62048  -9.29911  1.000 49.95052  ? 220 PHE E CE2 1 
ATOM   6024 C CZ  . PHE E 5 206 ? 39.52107  -9.64505  -10.32629 1.000 56.32311  ? 220 PHE E CZ  1 
ATOM   6025 N N   . ARG E 5 207 ? 40.89558  -11.24951 -3.29548  1.000 47.58754  ? 221 ARG E N   1 
ATOM   6026 C CA  . ARG E 5 207 ? 41.02844  -11.96807 -2.03201  1.000 51.92642  ? 221 ARG E CA  1 
ATOM   6027 C C   . ARG E 5 207 ? 39.67964  -12.07986 -1.33897  1.000 44.97758  ? 221 ARG E C   1 
ATOM   6028 O O   . ARG E 5 207 ? 38.97229  -11.07938 -1.17420  1.000 38.35952  ? 221 ARG E O   1 
ATOM   6029 C CB  . ARG E 5 207 ? 42.02838  -11.29129 -1.08272  1.000 36.79201  ? 221 ARG E CB  1 
ATOM   6030 C CG  . ARG E 5 207 ? 42.25135  -12.08862 0.20290   1.000 40.61989  ? 221 ARG E CG  1 
ATOM   6031 C CD  . ARG E 5 207 ? 43.43164  -11.58349 1.02352   1.000 54.69654  ? 221 ARG E CD  1 
ATOM   6032 N NE  . ARG E 5 207 ? 43.09148  -10.41279 1.82244   1.000 48.21008  ? 221 ARG E NE  1 
ATOM   6033 C CZ  . ARG E 5 207 ? 43.46568  -9.17354  1.53419   1.000 53.09077  ? 221 ARG E CZ  1 
ATOM   6034 N NH1 . ARG E 5 207 ? 44.20976  -8.90524  0.47322   1.000 65.06962  ? 221 ARG E NH1 1 
ATOM   6035 N NH2 . ARG E 5 207 ? 43.08748  -8.17889  2.33325   1.000 51.88900  ? 221 ARG E NH2 1 
ATOM   6036 N N   . CYS E 5 208 ? 39.33799  -13.29467 -0.92299  1.000 40.26529  ? 222 CYS E N   1 
ATOM   6037 C CA  . CYS E 5 208 ? 38.19339  -13.54115 -0.05888  1.000 37.19177  ? 222 CYS E CA  1 
ATOM   6038 C C   . CYS E 5 208 ? 38.67280  -13.64060 1.38496   1.000 33.78897  ? 222 CYS E C   1 
ATOM   6039 O O   . CYS E 5 208 ? 39.56984  -14.43065 1.69100   1.000 44.64158  ? 222 CYS E O   1 
ATOM   6040 C CB  . CYS E 5 208 ? 37.47248  -14.82199 -0.46742  1.000 40.68148  ? 222 CYS E CB  1 
ATOM   6041 S SG  . CYS E 5 208 ? 36.04956  -15.18691 0.55688   1.000 53.32855  ? 222 CYS E SG  1 
ATOM   6042 N N   . GLN E 5 209 ? 38.06939  -12.84964 2.26689   1.000 34.91293  ? 223 GLN E N   1 
ATOM   6043 C CA  . GLN E 5 209 ? 38.56222  -12.64906 3.62480   1.000 36.27975  ? 223 GLN E CA  1 
ATOM   6044 C C   . GLN E 5 209 ? 37.45586  -12.99486 4.60764   1.000 32.44094  ? 223 GLN E C   1 
ATOM   6045 O O   . GLN E 5 209 ? 36.38044  -12.38921 4.56910   1.000 32.37229  ? 223 GLN E O   1 
ATOM   6046 C CB  . GLN E 5 209 ? 39.01756  -11.19969 3.80854   1.000 42.40453  ? 223 GLN E CB  1 
ATOM   6047 C CG  . GLN E 5 209 ? 39.74559  -10.90064 5.09761   1.000 38.65884  ? 223 GLN E CG  1 
ATOM   6048 C CD  . GLN E 5 209 ? 40.43218  -9.54662  5.05938   1.000 38.07895  ? 223 GLN E CD  1 
ATOM   6049 O OE1 . GLN E 5 209 ? 41.33853  -9.31815  4.25778   1.000 57.12628  ? 223 GLN E OE1 1 
ATOM   6050 N NE2 . GLN E 5 209 ? 39.99304  -8.63925  5.91498   1.000 37.71470  ? 223 GLN E NE2 1 
ATOM   6051 N N   . VAL E 5 210 ? 37.71371  -13.95519 5.49018   1.000 35.10570  ? 224 VAL E N   1 
ATOM   6052 C CA  . VAL E 5 210 ? 36.71180  -14.41241 6.44817   1.000 29.52341  ? 224 VAL E CA  1 
ATOM   6053 C C   . VAL E 5 210 ? 37.24930  -14.19524 7.85288   1.000 32.76412  ? 224 VAL E C   1 
ATOM   6054 O O   . VAL E 5 210 ? 38.13631  -14.92883 8.30836   1.000 33.26278  ? 224 VAL E O   1 
ATOM   6055 C CB  . VAL E 5 210 ? 36.32996  -15.88093 6.23471   1.000 35.47043  ? 224 VAL E CB  1 
ATOM   6056 C CG1 . VAL E 5 210 ? 35.31643  -16.30650 7.28641   1.000 24.97122  ? 224 VAL E CG1 1 
ATOM   6057 C CG2 . VAL E 5 210 ? 35.77485  -16.08288 4.83022   1.000 29.93837  ? 224 VAL E CG2 1 
ATOM   6058 N N   . GLN E 5 211 ? 36.70326  -13.20080 8.54572   1.000 33.91393  ? 225 GLN E N   1 
ATOM   6059 C CA  . GLN E 5 211 ? 37.03828  -12.96671 9.94355   1.000 26.95818  ? 225 GLN E CA  1 
ATOM   6060 C C   . GLN E 5 211 ? 36.26055  -13.94531 10.81357  1.000 33.51603  ? 225 GLN E C   1 
ATOM   6061 O O   . GLN E 5 211 ? 35.02378  -13.96832 10.78037  1.000 29.31166  ? 225 GLN E O   1 
ATOM   6062 C CB  . GLN E 5 211 ? 36.72002  -11.52589 10.33545  1.000 29.85890  ? 225 GLN E CB  1 
ATOM   6063 C CG  . GLN E 5 211 ? 36.80672  -11.24518 11.82743  1.000 31.35520  ? 225 GLN E CG  1 
ATOM   6064 C CD  . GLN E 5 211 ? 38.23155  -11.16619 12.33635  1.000 37.37639  ? 225 GLN E CD  1 
ATOM   6065 O OE1 . GLN E 5 211 ? 38.99267  -10.28040 11.94926  1.000 33.42508  ? 225 GLN E OE1 1 
ATOM   6066 N NE2 . GLN E 5 211 ? 38.59805  -12.09213 13.21659  1.000 32.45211  ? 225 GLN E NE2 1 
ATOM   6067 N N   . PHE E 5 212 ? 36.98218  -14.75552 11.58307  1.000 32.16145  ? 226 PHE E N   1 
ATOM   6068 C CA  . PHE E 5 212 ? 36.38543  -15.70283 12.51295  1.000 25.98401  ? 226 PHE E CA  1 
ATOM   6069 C C   . PHE E 5 212 ? 36.59555  -15.21054 13.93872  1.000 30.59256  ? 226 PHE E C   1 
ATOM   6070 O O   . PHE E 5 212 ? 37.70477  -14.80322 14.30338  1.000 38.06277  ? 226 PHE E O   1 
ATOM   6071 C CB  . PHE E 5 212 ? 36.98903  -17.09600 12.33728  1.000 27.95507  ? 226 PHE E CB  1 
ATOM   6072 C CG  . PHE E 5 212 ? 36.49932  -18.10331 13.34443  1.000 28.84906  ? 226 PHE E CG  1 
ATOM   6073 C CD1 . PHE E 5 212 ? 35.21785  -18.63068 13.25402  1.000 29.29714  ? 226 PHE E CD1 1 
ATOM   6074 C CD2 . PHE E 5 212 ? 37.32408  -18.53102 14.37422  1.000 24.72973  ? 226 PHE E CD2 1 
ATOM   6075 C CE1 . PHE E 5 212 ? 34.76732  -19.56158 14.17389  1.000 20.84850  ? 226 PHE E CE1 1 
ATOM   6076 C CE2 . PHE E 5 212 ? 36.88124  -19.46387 15.29727  1.000 23.37833  ? 226 PHE E CE2 1 
ATOM   6077 C CZ  . PHE E 5 212 ? 35.60242  -19.98049 15.19798  1.000 23.36866  ? 226 PHE E CZ  1 
ATOM   6078 N N   . TYR E 5 213 ? 35.53123  -15.24434 14.73540  1.000 28.35278  ? 227 TYR E N   1 
ATOM   6079 C CA  . TYR E 5 213 ? 35.57764  -14.88559 16.14931  1.000 30.62387  ? 227 TYR E CA  1 
ATOM   6080 C C   . TYR E 5 213 ? 35.44940  -16.16536 16.96401  1.000 30.38359  ? 227 TYR E C   1 
ATOM   6081 O O   . TYR E 5 213 ? 34.37971  -16.78216 16.99629  1.000 31.88353  ? 227 TYR E O   1 
ATOM   6082 C CB  . TYR E 5 213 ? 34.47097  -13.89642 16.50256  1.000 19.47404  ? 227 TYR E CB  1 
ATOM   6083 C CG  . TYR E 5 213 ? 34.54726  -12.59787 15.73610  1.000 25.21217  ? 227 TYR E CG  1 
ATOM   6084 C CD1 . TYR E 5 213 ? 35.34953  -11.55428 16.17781  1.000 23.28248  ? 227 TYR E CD1 1 
ATOM   6085 C CD2 . TYR E 5 213 ? 33.81733  -12.41616 14.56747  1.000 24.94939  ? 227 TYR E CD2 1 
ATOM   6086 C CE1 . TYR E 5 213 ? 35.42242  -10.36469 15.47716  1.000 23.48264  ? 227 TYR E CE1 1 
ATOM   6087 C CE2 . TYR E 5 213 ? 33.88559  -11.23422 13.85944  1.000 29.08125  ? 227 TYR E CE2 1 
ATOM   6088 C CZ  . TYR E 5 213 ? 34.68359  -10.20889 14.31958  1.000 29.62851  ? 227 TYR E CZ  1 
ATOM   6089 O OH  . TYR E 5 213 ? 34.74742  -9.03077  13.61068  1.000 33.55482  ? 227 TYR E OH  1 
ATOM   6090 N N   . GLY E 5 214 ? 36.53414  -16.55862 17.62351  1.000 28.84302  ? 228 GLY E N   1 
ATOM   6091 C CA  . GLY E 5 214 ? 36.54641  -17.81576 18.33997  1.000 28.68385  ? 228 GLY E CA  1 
ATOM   6092 C C   . GLY E 5 214 ? 36.80928  -17.67936 19.82185  1.000 32.76007  ? 228 GLY E C   1 
ATOM   6093 O O   . GLY E 5 214 ? 36.09243  -16.96936 20.53447  1.000 31.27159  ? 228 GLY E O   1 
ATOM   6094 N N   . LEU E 5 215 ? 37.84024  -18.35834 20.29814  1.000 36.09006  ? 229 LEU E N   1 
ATOM   6095 C CA  . LEU E 5 215 ? 38.14918  -18.36215 21.71659  1.000 38.29747  ? 229 LEU E CA  1 
ATOM   6096 C C   . LEU E 5 215 ? 39.04221  -17.18173 22.07786  1.000 36.66759  ? 229 LEU E C   1 
ATOM   6097 O O   . LEU E 5 215 ? 39.78740  -16.65634 21.24362  1.000 40.98525  ? 229 LEU E O   1 
ATOM   6098 C CB  . LEU E 5 215 ? 38.82215  -19.67592 22.11237  1.000 29.19341  ? 229 LEU E CB  1 
ATOM   6099 C CG  . LEU E 5 215 ? 38.03364  -20.94080 21.77784  1.000 37.06869  ? 229 LEU E CG  1 
ATOM   6100 C CD1 . LEU E 5 215 ? 38.77066  -22.17489 22.27464  1.000 39.92458  ? 229 LEU E CD1 1 
ATOM   6101 C CD2 . LEU E 5 215 ? 36.63476  -20.86932 22.36927  1.000 26.68255  ? 229 LEU E CD2 1 
ATOM   6102 N N   . SER E 5 216 ? 38.94910  -16.76395 23.33550  1.000 28.85445  ? 230 SER E N   1 
ATOM   6103 C CA  . SER E 5 216 ? 39.80266  -15.71699 23.86705  1.000 45.58062  ? 230 SER E CA  1 
ATOM   6104 C C   . SER E 5 216 ? 41.08452  -16.31596 24.43708  1.000 45.44153  ? 230 SER E C   1 
ATOM   6105 O O   . SER E 5 216 ? 41.23915  -17.53344 24.54870  1.000 54.52689  ? 230 SER E O   1 
ATOM   6106 C CB  . SER E 5 216 ? 39.06823  -14.93401 24.94709  1.000 54.62818  ? 230 SER E CB  1 
ATOM   6107 O OG  . SER E 5 216 ? 38.80562  -15.77642 26.05592  1.000 54.96064  ? 230 SER E OG  1 
ATOM   6108 N N   . GLU E 5 217 ? 42.01053  -15.43107 24.81368  1.000 57.52899  ? 231 GLU E N   1 
ATOM   6109 C CA  . GLU E 5 217 ? 43.25629  -15.87377 25.43116  1.000 40.09928  ? 231 GLU E CA  1 
ATOM   6110 C C   . GLU E 5 217 ? 43.01071  -16.51328 26.79051  1.000 45.67236  ? 231 GLU E C   1 
ATOM   6111 O O   . GLU E 5 217 ? 43.74347  -17.42430 27.18988  1.000 61.19678  ? 231 GLU E O   1 
ATOM   6112 C CB  . GLU E 5 217 ? 44.21607  -14.69304 25.56650  1.000 45.68571  ? 231 GLU E CB  1 
ATOM   6113 N N   . ASN E 5 218 ? 41.98557  -16.05354 27.51095  1.000 64.62066  ? 232 ASN E N   1 
ATOM   6114 C CA  . ASN E 5 218 ? 41.66020  -16.59235 28.82578  1.000 63.26083  ? 232 ASN E CA  1 
ATOM   6115 C C   . ASN E 5 218 ? 41.03802  -17.98246 28.76239  1.000 68.53693  ? 232 ASN E C   1 
ATOM   6116 O O   . ASN E 5 218 ? 41.04164  -18.69226 29.77550  1.000 73.57142  ? 232 ASN E O   1 
ATOM   6117 C CB  . ASN E 5 218 ? 40.71352  -15.63929 29.56166  1.000 58.62450  ? 232 ASN E CB  1 
ATOM   6118 N N   . ASP E 5 219 ? 40.50418  -18.38499 27.61035  1.000 59.82425  ? 233 ASP E N   1 
ATOM   6119 C CA  . ASP E 5 219 ? 39.93319  -19.71892 27.47672  1.000 51.95474  ? 233 ASP E CA  1 
ATOM   6120 C C   . ASP E 5 219 ? 41.03142  -20.77528 27.50994  1.000 61.07936  ? 233 ASP E C   1 
ATOM   6121 O O   . ASP E 5 219 ? 42.07909  -20.62714 26.87522  1.000 61.92091  ? 233 ASP E O   1 
ATOM   6122 C CB  . ASP E 5 219 ? 39.13914  -19.83342 26.17594  1.000 48.72807  ? 233 ASP E CB  1 
ATOM   6123 C CG  . ASP E 5 219 ? 37.78159  -19.15700 26.25428  1.000 48.01751  ? 233 ASP E CG  1 
ATOM   6124 O OD1 . ASP E 5 219 ? 37.09381  -19.31420 27.28545  1.000 55.33744  ? 233 ASP E OD1 1 
ATOM   6125 O OD2 . ASP E 5 219 ? 37.39966  -18.47055 25.28244  1.000 42.75023  ? 233 ASP E OD2 1 
ATOM   6126 N N   . GLU E 5 220 ? 40.79099  -21.84510 28.26057  1.000 50.70572  ? 234 GLU E N   1 
ATOM   6127 C CA  . GLU E 5 220 ? 41.75320  -22.93144 28.34136  1.000 54.02533  ? 234 GLU E CA  1 
ATOM   6128 C C   . GLU E 5 220 ? 41.61494  -23.84453 27.12883  1.000 61.72159  ? 234 GLU E C   1 
ATOM   6129 O O   . GLU E 5 220 ? 40.52315  -24.02666 26.58044  1.000 57.32885  ? 234 GLU E O   1 
ATOM   6130 C CB  . GLU E 5 220 ? 41.56189  -23.73064 29.63309  1.000 51.99896  ? 234 GLU E CB  1 
ATOM   6131 N N   . TRP E 5 221 ? 42.74242  -24.41025 26.70239  1.000 47.21435  ? 235 TRP E N   1 
ATOM   6132 C CA  . TRP E 5 221 ? 42.77354  -25.29423 25.54551  1.000 47.52538  ? 235 TRP E CA  1 
ATOM   6133 C C   . TRP E 5 221 ? 43.80022  -26.38961 25.77942  1.000 47.39529  ? 235 TRP E C   1 
ATOM   6134 O O   . TRP E 5 221 ? 44.96383  -26.10036 26.07349  1.000 58.59195  ? 235 TRP E O   1 
ATOM   6135 C CB  . TRP E 5 221 ? 43.10428  -24.52204 24.26328  1.000 44.25096  ? 235 TRP E CB  1 
ATOM   6136 C CG  . TRP E 5 221 ? 42.85333  -25.31252 23.02659  1.000 42.55415  ? 235 TRP E CG  1 
ATOM   6137 C CD1 . TRP E 5 221 ? 43.78759  -25.85223 22.19316  1.000 49.91657  ? 235 TRP E CD1 1 
ATOM   6138 C CD2 . TRP E 5 221 ? 41.57649  -25.66853 22.48359  1.000 42.81028  ? 235 TRP E CD2 1 
ATOM   6139 N NE1 . TRP E 5 221 ? 43.17268  -26.51648 21.15768  1.000 48.49847  ? 235 TRP E NE1 1 
ATOM   6140 C CE2 . TRP E 5 221 ? 41.81504  -26.42137 21.31426  1.000 48.04412  ? 235 TRP E CE2 1 
ATOM   6141 C CE3 . TRP E 5 221 ? 40.25551  -25.41974 22.86895  1.000 34.23930  ? 235 TRP E CE3 1 
ATOM   6142 C CZ2 . TRP E 5 221 ? 40.78111  -26.92811 20.52674  1.000 46.63804  ? 235 TRP E CZ2 1 
ATOM   6143 C CZ3 . TRP E 5 221 ? 39.22855  -25.92309 22.08546  1.000 40.17302  ? 235 TRP E CZ3 1 
ATOM   6144 C CH2 . TRP E 5 221 ? 39.49807  -26.66892 20.92751  1.000 46.75175  ? 235 TRP E CH2 1 
ATOM   6145 N N   . THR E 5 222 ? 43.36491  -27.64514 25.64787  1.000 51.04180  ? 236 THR E N   1 
ATOM   6146 C CA  . THR E 5 222 ? 44.23149  -28.79738 25.86350  1.000 61.27509  ? 236 THR E CA  1 
ATOM   6147 C C   . THR E 5 222 ? 44.16481  -29.80678 24.72341  1.000 71.74739  ? 236 THR E C   1 
ATOM   6148 O O   . THR E 5 222 ? 44.74807  -30.88999 24.83930  1.000 77.93660  ? 236 THR E O   1 
ATOM   6149 C CB  . THR E 5 222 ? 43.88658  -29.49389 27.18527  1.000 68.48815  ? 236 THR E CB  1 
ATOM   6150 O OG1 . THR E 5 222 ? 42.46757  -29.67916 27.27465  1.000 54.07397  ? 236 THR E OG1 1 
ATOM   6151 C CG2 . THR E 5 222 ? 44.36837  -28.66468 28.36796  1.000 65.64756  ? 236 THR E CG2 1 
ATOM   6152 N N   . GLN E 5 223 ? 43.46950  -29.49068 23.63518  1.000 71.15909  ? 237 GLN E N   1 
ATOM   6153 C CA  . GLN E 5 223 ? 43.43027  -30.37856 22.48663  1.000 64.21885  ? 237 GLN E CA  1 
ATOM   6154 C C   . GLN E 5 223 ? 44.75735  -30.31803 21.73185  1.000 76.98870  ? 237 GLN E C   1 
ATOM   6155 O O   . GLN E 5 223 ? 45.59527  -29.44171 21.96302  1.000 72.49396  ? 237 GLN E O   1 
ATOM   6156 C CB  . GLN E 5 223 ? 42.26842  -30.00839 21.56713  1.000 61.11562  ? 237 GLN E CB  1 
ATOM   6157 C CG  . GLN E 5 223 ? 40.90405  -30.05338 22.23857  1.000 62.68008  ? 237 GLN E CG  1 
ATOM   6158 C CD  . GLN E 5 223 ? 40.17648  -31.36101 21.99660  1.000 78.31688  ? 237 GLN E CD  1 
ATOM   6159 O OE1 . GLN E 5 223 ? 39.79456  -31.67119 20.86579  1.000 71.87835  ? 237 GLN E OE1 1 
ATOM   6160 N NE2 . GLN E 5 223 ? 39.98226  -32.13790 23.05930  1.000 66.00852  ? 237 GLN E NE2 1 
ATOM   6161 N N   . ASP E 5 224 ? 44.94901  -31.27233 20.81560  1.000 70.82393  ? 238 ASP E N   1 
ATOM   6162 C CA  . ASP E 5 224 ? 46.18976  -31.30870 20.04628  1.000 71.42421  ? 238 ASP E CA  1 
ATOM   6163 C C   . ASP E 5 224 ? 46.20771  -30.24396 18.95677  1.000 69.46442  ? 238 ASP E C   1 
ATOM   6164 O O   . ASP E 5 224 ? 47.23420  -29.58623 18.74798  1.000 65.10064  ? 238 ASP E O   1 
ATOM   6165 C CB  . ASP E 5 224 ? 46.40139  -32.69521 19.43507  1.000 75.13860  ? 238 ASP E CB  1 
ATOM   6166 C CG  . ASP E 5 224 ? 46.96763  -33.68821 20.42739  1.000 79.47868  ? 238 ASP E CG  1 
ATOM   6167 O OD1 . ASP E 5 224 ? 47.54306  -33.24868 21.44401  1.000 86.66440  ? 238 ASP E OD1 1 
ATOM   6168 O OD2 . ASP E 5 224 ? 46.84415  -34.90765 20.18940  1.000 87.73215  ? 238 ASP E OD2 1 
ATOM   6169 N N   . ARG E 5 225 ? 45.08816  -30.05977 18.25916  1.000 61.99582  ? 239 ARG E N   1 
ATOM   6170 C CA  . ARG E 5 225 ? 45.01962  -29.07947 17.18859  1.000 47.35968  ? 239 ARG E CA  1 
ATOM   6171 C C   . ARG E 5 225 ? 45.13438  -27.66487 17.75009  1.000 50.32467  ? 239 ARG E C   1 
ATOM   6172 O O   . ARG E 5 225 ? 44.99553  -27.42640 18.95385  1.000 55.01638  ? 239 ARG E O   1 
ATOM   6173 C CB  . ARG E 5 225 ? 43.71973  -29.23011 16.40182  1.000 53.63997  ? 239 ARG E CB  1 
ATOM   6174 C CG  . ARG E 5 225 ? 42.46089  -29.02214 17.22748  1.000 54.52774  ? 239 ARG E CG  1 
ATOM   6175 C CD  . ARG E 5 225 ? 41.22250  -29.10242 16.34786  1.000 50.26252  ? 239 ARG E CD  1 
ATOM   6176 N NE  . ARG E 5 225 ? 39.99341  -29.02273 17.12592  1.000 59.40295  ? 239 ARG E NE  1 
ATOM   6177 C CZ  . ARG E 5 225 ? 39.32573  -27.90128 17.35868  1.000 52.08988  ? 239 ARG E CZ  1 
ATOM   6178 N NH1 . ARG E 5 225 ? 39.73094  -26.74046 16.86844  1.000 43.95376  ? 239 ARG E NH1 1 
ATOM   6179 N NH2 . ARG E 5 225 ? 38.22423  -27.94520 18.10272  1.000 45.05589  ? 239 ARG E NH2 1 
ATOM   6180 N N   . ALA E 5 226 ? 45.39345  -26.71860 16.84985  1.000 46.22114  ? 240 ALA E N   1 
ATOM   6181 C CA  . ALA E 5 226 ? 45.58322  -25.33110 17.24815  1.000 46.62262  ? 240 ALA E CA  1 
ATOM   6182 C C   . ALA E 5 226 ? 44.32670  -24.78129 17.91385  1.000 49.25023  ? 240 ALA E C   1 
ATOM   6183 O O   . ALA E 5 226 ? 43.19862  -25.14563 17.56897  1.000 51.84517  ? 240 ALA E O   1 
ATOM   6184 C CB  . ALA E 5 226 ? 45.95403  -24.47178 16.03845  1.000 39.41700  ? 240 ALA E CB  1 
ATOM   6185 N N   . LYS E 5 227 ? 44.53682  -23.90107 18.87979  1.000 44.22927  ? 241 LYS E N   1 
ATOM   6186 C CA  . LYS E 5 227 ? 43.43909  -23.31243 19.62988  1.000 37.87210  ? 241 LYS E CA  1 
ATOM   6187 C C   . LYS E 5 227 ? 42.60262  -22.42886 18.71339  1.000 38.02774  ? 241 LYS E C   1 
ATOM   6188 O O   . LYS E 5 227 ? 43.13448  -21.47056 18.13947  1.000 32.71791  ? 241 LYS E O   1 
ATOM   6189 C CB  . LYS E 5 227 ? 43.98735  -22.51079 20.80567  1.000 34.63199  ? 241 LYS E CB  1 
ATOM   6190 C CG  . LYS E 5 227 ? 42.93330  -21.84011 21.65994  1.000 39.17408  ? 241 LYS E CG  1 
ATOM   6191 C CD  . LYS E 5 227 ? 43.57969  -21.01571 22.75833  1.000 44.59820  ? 241 LYS E CD  1 
ATOM   6192 C CE  . LYS E 5 227 ? 42.53821  -20.36053 23.64366  1.000 40.26510  ? 241 LYS E CE  1 
ATOM   6193 N NZ  . LYS E 5 227 ? 43.13734  -19.26727 24.45476  1.000 53.60005  ? 241 LYS E NZ  1 
ATOM   6194 N N   . PRO E 5 228 ? 41.30177  -22.69895 18.55271  1.000 43.37491  ? 242 PRO E N   1 
ATOM   6195 C CA  . PRO E 5 228 ? 40.49823  -21.92979 17.59193  1.000 32.57897  ? 242 PRO E CA  1 
ATOM   6196 C C   . PRO E 5 228 ? 40.21434  -20.51234 18.06607  1.000 33.74149  ? 242 PRO E C   1 
ATOM   6197 O O   . PRO E 5 228 ? 39.08684  -20.18807 18.45555  1.000 36.12573  ? 242 PRO E O   1 
ATOM   6198 C CB  . PRO E 5 228 ? 39.21086  -22.75556 17.48205  1.000 36.42166  ? 242 PRO E CB  1 
ATOM   6199 C CG  . PRO E 5 228 ? 39.09218  -23.41881 18.82242  1.000 37.49241  ? 242 PRO E CG  1 
ATOM   6200 C CD  . PRO E 5 228 ? 40.49777  -23.69360 19.28801  1.000 32.59431  ? 242 PRO E CD  1 
ATOM   6201 N N   . VAL E 5 229 ? 41.23450  -19.65925 18.03559  1.000 31.48041  ? 243 VAL E N   1 
ATOM   6202 C CA  . VAL E 5 229 ? 41.10940  -18.28482 18.50949  1.000 38.04386  ? 243 VAL E CA  1 
ATOM   6203 C C   . VAL E 5 229 ? 40.54215  -17.41313 17.39814  1.000 37.44115  ? 243 VAL E C   1 
ATOM   6204 O O   . VAL E 5 229 ? 40.40017  -17.85870 16.25420  1.000 35.94435  ? 243 VAL E O   1 
ATOM   6205 C CB  . VAL E 5 229 ? 42.46615  -17.73456 18.98859  1.000 38.10371  ? 243 VAL E CB  1 
ATOM   6206 C CG1 . VAL E 5 229 ? 42.96032  -18.49808 20.20641  1.000 30.00051  ? 243 VAL E CG1 1 
ATOM   6207 C CG2 . VAL E 5 229 ? 43.48256  -17.82202 17.86238  1.000 28.55214  ? 243 VAL E CG2 1 
ATOM   6208 N N   . THR E 5 230 ? 40.21393  -16.16787 17.73404  1.000 44.05118  ? 244 THR E N   1 
ATOM   6209 C CA  . THR E 5 230 ? 39.80162  -15.19303 16.73521  1.000 32.93613  ? 244 THR E CA  1 
ATOM   6210 C C   . THR E 5 230 ? 40.90631  -15.00977 15.70178  1.000 40.90469  ? 244 THR E C   1 
ATOM   6211 O O   . THR E 5 230 ? 42.05366  -14.71493 16.04784  1.000 38.34867  ? 244 THR E O   1 
ATOM   6212 C CB  . THR E 5 230 ? 39.47555  -13.86279 17.41823  1.000 23.88316  ? 244 THR E CB  1 
ATOM   6213 O OG1 . THR E 5 230 ? 38.29874  -14.01724 18.21907  1.000 36.11453  ? 244 THR E OG1 1 
ATOM   6214 C CG2 . THR E 5 230 ? 39.24686  -12.76319 16.40114  1.000 23.46418  ? 244 THR E CG2 1 
ATOM   6215 N N   . GLN E 5 231 ? 40.56548  -15.20021 14.42993  1.000 33.43709  ? 245 GLN E N   1 
ATOM   6216 C CA  . GLN E 5 231 ? 41.57463  -15.16227 13.38101  1.000 30.54768  ? 245 GLN E CA  1 
ATOM   6217 C C   . GLN E 5 231 ? 40.91083  -14.83069 12.05517  1.000 35.80328  ? 245 GLN E C   1 
ATOM   6218 O O   . GLN E 5 231 ? 39.68968  -14.90925 11.90421  1.000 33.95715  ? 245 GLN E O   1 
ATOM   6219 C CB  . GLN E 5 231 ? 42.32226  -16.49038 13.28072  1.000 27.25086  ? 245 GLN E CB  1 
ATOM   6220 C CG  . GLN E 5 231 ? 41.46074  -17.62794 12.77376  1.000 30.36453  ? 245 GLN E CG  1 
ATOM   6221 C CD  . GLN E 5 231 ? 42.11393  -18.97598 12.97897  1.000 38.92123  ? 245 GLN E CD  1 
ATOM   6222 O OE1 . GLN E 5 231 ? 42.69311  -19.54712 12.05379  1.000 48.10285  ? 245 GLN E OE1 1 
ATOM   6223 N NE2 . GLN E 5 231 ? 42.02669  -19.49391 14.19931  1.000 33.01484  ? 245 GLN E NE2 1 
ATOM   6224 N N   . ILE E 5 232 ? 41.74385  -14.46561 11.08936  1.000 38.14007  ? 246 ILE E N   1 
ATOM   6225 C CA  . ILE E 5 232 ? 41.31359  -14.20775 9.72414   1.000 39.14218  ? 246 ILE E CA  1 
ATOM   6226 C C   . ILE E 5 232 ? 41.86697  -15.31833 8.84527   1.000 37.47625  ? 246 ILE E C   1 
ATOM   6227 O O   . ILE E 5 232 ? 43.07639  -15.57376 8.84246   1.000 45.86647  ? 246 ILE E O   1 
ATOM   6228 C CB  . ILE E 5 232 ? 41.78294  -12.83221 9.23503   1.000 37.54291  ? 246 ILE E CB  1 
ATOM   6229 C CG1 . ILE E 5 232 ? 41.16170  -11.73432 10.09579  1.000 22.49983  ? 246 ILE E CG1 1 
ATOM   6230 C CG2 . ILE E 5 232 ? 41.42780  -12.64808 7.76743   1.000 30.42682  ? 246 ILE E CG2 1 
ATOM   6231 C CD1 . ILE E 5 232 ? 41.58310  -10.34523 9.69762   1.000 32.47727  ? 246 ILE E CD1 1 
ATOM   6232 N N   . VAL E 5 233 ? 40.98259  -15.98999 8.11833   1.000 30.61862  ? 247 VAL E N   1 
ATOM   6233 C CA  . VAL E 5 233 ? 41.35903  -17.01137 7.15330   1.000 26.65840  ? 247 VAL E CA  1 
ATOM   6234 C C   . VAL E 5 233 ? 40.93942  -16.51402 5.78130   1.000 35.65894  ? 247 VAL E C   1 
ATOM   6235 O O   . VAL E 5 233 ? 39.81260  -16.03491 5.60927   1.000 38.02604  ? 247 VAL E O   1 
ATOM   6236 C CB  . VAL E 5 233 ? 40.70791  -18.36640 7.47425   1.000 31.82295  ? 247 VAL E CB  1 
ATOM   6237 C CG1 . VAL E 5 233 ? 41.28761  -19.45330 6.58759   1.000 30.97896  ? 247 VAL E CG1 1 
ATOM   6238 C CG2 . VAL E 5 233 ? 40.90358  -18.70433 8.94589   1.000 39.11587  ? 247 VAL E CG2 1 
ATOM   6239 N N   . SER E 5 234 ? 41.84183  -16.61776 4.81056   1.000 39.10346  ? 248 SER E N   1 
ATOM   6240 C CA  . SER E 5 234 ? 41.62049  -16.00505 3.51271   1.000 38.17181  ? 248 SER E CA  1 
ATOM   6241 C C   . SER E 5 234 ? 42.13967  -16.91087 2.40714   1.000 33.86156  ? 248 SER E C   1 
ATOM   6242 O O   . SER E 5 234 ? 42.90690  -17.84834 2.63950   1.000 40.61078  ? 248 SER E O   1 
ATOM   6243 C CB  . SER E 5 234 ? 42.28557  -14.62668 3.43091   1.000 29.89175  ? 248 SER E CB  1 
ATOM   6244 O OG  . SER E 5 234 ? 43.64565  -14.69808 3.81955   1.000 54.47227  ? 248 SER E OG  1 
ATOM   6245 N N   . ALA E 5 235 ? 41.68565  -16.61566 1.19249   1.000 39.10582  ? 249 ALA E N   1 
ATOM   6246 C CA  . ALA E 5 235 ? 42.16438  -17.24768 -0.02571  1.000 41.74855  ? 249 ALA E CA  1 
ATOM   6247 C C   . ALA E 5 235 ? 42.13287  -16.19474 -1.12323  1.000 46.84655  ? 249 ALA E C   1 
ATOM   6248 O O   . ALA E 5 235 ? 41.41905  -15.19342 -1.01944  1.000 42.13755  ? 249 ALA E O   1 
ATOM   6249 C CB  . ALA E 5 235 ? 41.32304  -18.47385 -0.39676  1.000 39.92906  ? 249 ALA E CB  1 
ATOM   6250 N N   . GLU E 5 236 ? 42.92001  -16.41492 -2.17472  1.000 51.02316  ? 250 GLU E N   1 
ATOM   6251 C CA  . GLU E 5 236 ? 43.13266  -15.37221 -3.16681  1.000 43.93995  ? 250 GLU E CA  1 
ATOM   6252 C C   . GLU E 5 236 ? 43.27231  -15.96236 -4.56403  1.000 52.31585  ? 250 GLU E C   1 
ATOM   6253 O O   . GLU E 5 236 ? 43.48637  -17.16426 -4.74283  1.000 53.20942  ? 250 GLU E O   1 
ATOM   6254 C CB  . GLU E 5 236 ? 44.36681  -14.52627 -2.82068  1.000 60.86006  ? 250 GLU E CB  1 
ATOM   6255 C CG  . GLU E 5 236 ? 45.61547  -15.33375 -2.49589  1.000 67.60496  ? 250 GLU E CG  1 
ATOM   6256 C CD  . GLU E 5 236 ? 46.62532  -14.54183 -1.67523  1.000 86.03591  ? 250 GLU E CD  1 
ATOM   6257 O OE1 . GLU E 5 236 ? 46.34020  -13.36398 -1.35735  1.000 76.66304  ? 250 GLU E OE1 1 
ATOM   6258 O OE2 . GLU E 5 236 ? 47.69846  -15.09932 -1.34384  1.000 74.33128  ? 250 GLU E OE2 1 
ATOM   6259 N N   . ALA E 5 237 ? 43.13342  -15.08244 -5.55631  1.000 44.91110  ? 251 ALA E N   1 
ATOM   6260 C CA  . ALA E 5 237 ? 43.32529  -15.41565 -6.96106  1.000 50.53277  ? 251 ALA E CA  1 
ATOM   6261 C C   . ALA E 5 237 ? 43.74931  -14.15163 -7.69611  1.000 51.73905  ? 251 ALA E C   1 
ATOM   6262 O O   . ALA E 5 237 ? 43.51379  -13.03489 -7.22707  1.000 57.17792  ? 251 ALA E O   1 
ATOM   6263 C CB  . ALA E 5 237 ? 42.05789  -16.01140 -7.58569  1.000 38.80059  ? 251 ALA E CB  1 
ATOM   6264 N N   . TRP E 5 238 ? 44.37542  -14.33427 -8.86181  1.000 64.87799  ? 252 TRP E N   1 
ATOM   6265 C CA  . TRP E 5 238 ? 44.94461  -13.21725 -9.60773  1.000 57.61447  ? 252 TRP E CA  1 
ATOM   6266 C C   . TRP E 5 238 ? 44.35391  -13.00925 -10.99301 1.000 52.53722  ? 252 TRP E C   1 
ATOM   6267 O O   . TRP E 5 238 ? 44.22903  -11.86209 -11.42352 1.000 68.06656  ? 252 TRP E O   1 
ATOM   6268 C CB  . TRP E 5 238 ? 46.46725  -13.38196 -9.73228  1.000 49.65241  ? 252 TRP E CB  1 
ATOM   6269 C CG  . TRP E 5 238 ? 47.16062  -13.05285 -8.45885  1.000 48.45046  ? 252 TRP E CG  1 
ATOM   6270 C CD1 . TRP E 5 238 ? 47.44657  -13.90763 -7.43334  1.000 57.29921  ? 252 TRP E CD1 1 
ATOM   6271 C CD2 . TRP E 5 238 ? 47.62093  -11.76285 -8.04692  1.000 50.21484  ? 252 TRP E CD2 1 
ATOM   6272 N NE1 . TRP E 5 238 ? 48.06960  -13.23103 -6.41127  1.000 49.99060  ? 252 TRP E NE1 1 
ATOM   6273 C CE2 . TRP E 5 238 ? 48.19031  -11.91210 -6.76424  1.000 52.02182  ? 252 TRP E CE2 1 
ATOM   6274 C CE3 . TRP E 5 238 ? 47.61535  -10.49682 -8.64076  1.000 52.09415  ? 252 TRP E CE3 1 
ATOM   6275 C CZ2 . TRP E 5 238 ? 48.75160  -10.84248 -6.06646  1.000 52.42626  ? 252 TRP E CZ2 1 
ATOM   6276 C CZ3 . TRP E 5 238 ? 48.17286  -9.43732  -7.94719  1.000 55.85353  ? 252 TRP E CZ3 1 
ATOM   6277 C CH2 . TRP E 5 238 ? 48.73276  -9.61659  -6.67261  1.000 55.11211  ? 252 TRP E CH2 1 
ATOM   6278 N N   . GLY E 5 239 ? 43.98608  -14.06385 -11.70462 1.000 55.52876  ? 253 GLY E N   1 
ATOM   6279 C CA  . GLY E 5 239 ? 43.44933  -13.85879 -13.03632 1.000 68.80430  ? 253 GLY E CA  1 
ATOM   6280 C C   . GLY E 5 239 ? 44.43121  -14.22970 -14.12303 1.000 66.80762  ? 253 GLY E C   1 
ATOM   6281 O O   . GLY E 5 239 ? 45.62791  -13.94636 -14.01027 1.000 56.55399  ? 253 GLY E O   1 
ATOM   6282 N N   . ARG E 5 240 ? 43.93793  -14.86766 -15.17765 1.000 68.08018  ? 254 ARG E N   1 
ATOM   6283 C CA  . ARG E 5 240 ? 44.77710  -15.40012 -16.23826 1.000 66.04960  ? 254 ARG E CA  1 
ATOM   6284 C C   . ARG E 5 240 ? 44.54104  -14.63624 -17.53322 1.000 75.82577  ? 254 ARG E C   1 
ATOM   6285 O O   . ARG E 5 240 ? 43.61623  -13.82877 -17.65199 1.000 73.78437  ? 254 ARG E O   1 
ATOM   6286 C CB  . ARG E 5 240 ? 44.50832  -16.89651 -16.44003 1.000 63.41274  ? 254 ARG E CB  1 
ATOM   6287 N N   . ALA E 5 241 ? 45.40136  -14.90798 -18.50971 1.000 92.48140  ? 255 ALA E N   1 
ATOM   6288 C CA  . ALA E 5 241 ? 45.29187  -14.30315 -19.82971 1.000 81.81429  ? 255 ALA E CA  1 
ATOM   6289 C C   . ALA E 5 241 ? 44.34215  -15.10699 -20.71251 1.000 78.28743  ? 255 ALA E C   1 
ATOM   6290 O O   . ALA E 5 241 ? 43.12845  -14.91143 -20.67419 1.000 64.18239  ? 255 ALA E O   1 
ATOM   6291 C CB  . ALA E 5 241 ? 46.66103  -14.19965 -20.47929 1.000 87.13495  ? 255 ALA E CB  1 
HETATM 6292 C C1  . NAG F 6 .   ? -22.52107 17.94074  57.12182  1.000 74.75911  ? 201 NAG A C1  1 
HETATM 6293 C C2  . NAG F 6 .   ? -23.16377 17.02488  56.08311  1.000 74.15911  ? 201 NAG A C2  1 
HETATM 6294 C C3  . NAG F 6 .   ? -24.17098 17.80671  55.24390  1.000 75.61911  ? 201 NAG A C3  1 
HETATM 6295 C C4  . NAG F 6 .   ? -25.17687 18.51551  56.14170  1.000 75.57911  ? 201 NAG A C4  1 
HETATM 6296 C C5  . NAG F 6 .   ? -24.45898 19.35310  57.19752  1.000 81.17911  ? 201 NAG A C5  1 
HETATM 6297 C C6  . NAG F 6 .   ? -25.40327 19.94936  58.21525  1.000 84.82911  ? 201 NAG A C6  1 
HETATM 6298 C C7  . NAG F 6 .   ? -21.88522 15.10176  55.25178  1.000 55.34911  ? 201 NAG A C7  1 
HETATM 6299 C C8  . NAG F 6 .   ? -20.81219 14.63998  54.31309  1.000 49.96911  ? 201 NAG A C8  1 
HETATM 6300 N N2  . NAG F 6 .   ? -22.15535 16.41089  55.23390  1.000 63.48911  ? 201 NAG A N2  1 
HETATM 6301 O O3  . NAG F 6 .   ? -24.85209 16.91332  54.37052  1.000 79.77911  ? 201 NAG A O3  1 
HETATM 6302 O O4  . NAG F 6 .   ? -26.01326 19.36361  55.36301  1.000 91.24911  ? 201 NAG A O4  1 
HETATM 6303 O O5  . NAG F 6 .   ? -23.53522 18.53455  57.92969  1.000 77.47911  ? 201 NAG A O5  1 
HETATM 6304 O O6  . NAG F 6 .   ? -26.15488 18.93926  58.87468  1.000 92.47911  ? 201 NAG A O6  1 
HETATM 6305 O O7  . NAG F 6 .   ? -22.48061 14.32513  55.99245  1.000 48.18911  ? 201 NAG A O7  1 
HETATM 6306 C C   . ACT G 7 .   ? 22.64135  4.54144   78.10491  1.000 59.22802  ? 201 ACT B C   1 
HETATM 6307 O O   . ACT G 7 .   ? 22.37679  5.74157   78.39867  1.000 57.86802  ? 201 ACT B O   1 
HETATM 6308 O OXT . ACT G 7 .   ? 22.40040  3.49295   78.77329  1.000 51.57802  ? 201 ACT B OXT 1 
HETATM 6309 C CH3 . ACT G 7 .   ? 23.36742  4.30193   76.73154  1.000 37.51802  ? 201 ACT B CH3 1 
HETATM 6310 C C1  . NAG H 6 .   ? 23.70629  9.85703   47.82605  1.000 64.24422  ? 202 NAG B C1  1 
HETATM 6311 C C2  . NAG H 6 .   ? 23.57232  8.68372   46.86028  1.000 74.40422  ? 202 NAG B C2  1 
HETATM 6312 C C3  . NAG H 6 .   ? 24.04121  7.40104   47.53717  1.000 80.66422  ? 202 NAG B C3  1 
HETATM 6313 C C4  . NAG H 6 .   ? 25.46188  7.57322   48.06292  1.000 86.51422  ? 202 NAG B C4  1 
HETATM 6314 C C5  . NAG H 6 .   ? 25.56962  8.81774   48.94668  1.000 86.66422  ? 202 NAG B C5  1 
HETATM 6315 C C6  . NAG H 6 .   ? 26.99432  9.13463   49.34482  1.000 85.12422  ? 202 NAG B C6  1 
HETATM 6316 C C7  . NAG H 6 .   ? 21.83111  8.93576   45.15167  1.000 74.88422  ? 202 NAG B C7  1 
HETATM 6317 C C8  . NAG H 6 .   ? 20.39100  8.70624   44.80168  1.000 62.75422  ? 202 NAG B C8  1 
HETATM 6318 N N2  . NAG H 6 .   ? 22.21007  8.53941   46.37190  1.000 61.18422  ? 202 NAG B N2  1 
HETATM 6319 O O3  . NAG H 6 .   ? 23.97829  6.32184   46.61050  1.000 75.81422  ? 202 NAG B O3  1 
HETATM 6320 O O4  . NAG H 6 .   ? 25.84355  6.43125   48.82215  1.000 95.79422  ? 202 NAG B O4  1 
HETATM 6321 O O5  . NAG H 6 .   ? 25.07064  9.97260   48.25252  1.000 76.06422  ? 202 NAG B O5  1 
HETATM 6322 O O6  . NAG H 6 .   ? 27.05277  10.13623  50.35186  1.000 69.15422  ? 202 NAG B O6  1 
HETATM 6323 O O7  . NAG H 6 .   ? 22.61496  9.46275   44.36687  1.000 80.24422  ? 202 NAG B O7  1 
HETATM 6324 C C   . ACT I 7 .   ? 19.14879  10.37108  63.84741  1.000 56.66570  ? 203 ACT B C   1 
HETATM 6325 O O   . ACT I 7 .   ? 19.41768  9.13471   63.90313  1.000 56.66570  ? 203 ACT B O   1 
HETATM 6326 O OXT . ACT I 7 .   ? 18.10894  10.92489  63.39326  1.000 56.66570  ? 203 ACT B OXT 1 
HETATM 6327 C CH3 . ACT I 7 .   ? 20.24057  11.35843  64.40989  1.000 56.66570  ? 203 ACT B CH3 1 
HETATM 6328 C C1  . GOL J 8 .   ? 15.62170  10.33270  42.93040  1.000 48.08524  ? 204 GOL B C1  1 
HETATM 6329 O O1  . GOL J 8 .   ? 15.79787  9.54833   44.08820  1.000 48.08524  ? 204 GOL B O1  1 
HETATM 6330 C C2  . GOL J 8 .   ? 14.41125  11.24077  43.22896  1.000 48.08524  ? 204 GOL B C2  1 
HETATM 6331 O O2  . GOL J 8 .   ? 14.72718  12.58893  43.12814  1.000 48.08524  ? 204 GOL B O2  1 
HETATM 6332 C C3  . GOL J 8 .   ? 13.36538  10.78855  42.20787  1.000 48.08524  ? 204 GOL B C3  1 
HETATM 6333 O O3  . GOL J 8 .   ? 13.50064  9.41154   42.09258  1.000 48.08524  ? 204 GOL B O3  1 
HETATM 6334 C C   . ACT K 7 .   ? 9.85027   0.90073   28.92985  1.000 55.09548  ? 301 ACT E C   1 
HETATM 6335 O O   . ACT K 7 .   ? 9.58052   -0.33009  29.04294  1.000 62.79548  ? 301 ACT E O   1 
HETATM 6336 O OXT . ACT K 7 .   ? 10.71426  1.46407   28.18831  1.000 45.53548  ? 301 ACT E OXT 1 
HETATM 6337 C CH3 . ACT K 7 .   ? 9.00695   1.86906   29.81719  1.000 47.28548  ? 301 ACT E CH3 1 
HETATM 6338 C C   . ACT L 7 .   ? 20.69214  -20.60405 37.01128  1.000 60.71591  ? 302 ACT E C   1 
HETATM 6339 O O   . ACT L 7 .   ? 21.43168  -20.90161 37.99869  1.000 60.12591  ? 302 ACT E O   1 
HETATM 6340 O OXT . ACT L 7 .   ? 20.79284  -20.96086 35.80071  1.000 47.41591  ? 302 ACT E OXT 1 
HETATM 6341 C CH3 . ACT L 7 .   ? 19.49092  -19.66581 37.30874  1.000 47.89591  ? 302 ACT E CH3 1 
HETATM 6342 O O   . HOH M 9 .   ? -3.14614  20.13717  51.02708  1.000 38.47154  ? 301 HOH A O   1 
HETATM 6343 O O   . HOH M 9 .   ? 6.98955   18.09518  56.76093  1.000 22.64752  ? 302 HOH A O   1 
HETATM 6344 O O   . HOH M 9 .   ? -9.28262  31.36959  55.51381  1.000 42.56573  ? 303 HOH A O   1 
HETATM 6345 O O   . HOH M 9 .   ? 16.17416  8.75175   49.20241  1.000 39.68497  ? 304 HOH A O   1 
HETATM 6346 O O   . HOH M 9 .   ? 11.21835  17.28599  56.54799  1.000 22.08035  ? 305 HOH A O   1 
HETATM 6347 O O   . HOH M 9 .   ? -5.89755  5.49222   51.76543  1.000 45.65261  ? 306 HOH A O   1 
HETATM 6348 O O   . HOH M 9 .   ? -16.52843 19.98902  78.52781  1.000 59.44061  ? 307 HOH A O   1 
HETATM 6349 O O   . HOH M 9 .   ? 2.65945   17.28616  61.01812  1.000 28.19739  ? 308 HOH A O   1 
HETATM 6350 O O   . HOH M 9 .   ? -18.89513 12.54071  52.39053  1.000 39.95070  ? 309 HOH A O   1 
HETATM 6351 O O   . HOH M 9 .   ? -5.25171  21.59095  47.92707  1.000 24.75741  ? 310 HOH A O   1 
HETATM 6352 O O   . HOH M 9 .   ? -7.23831  7.55927   61.31737  1.000 30.86090  ? 311 HOH A O   1 
HETATM 6353 O O   . HOH M 9 .   ? 0.22069   15.57794  46.27200  1.000 24.73198  ? 312 HOH A O   1 
HETATM 6354 O O   . HOH M 9 .   ? 18.71782  15.29697  50.74461  1.000 25.87928  ? 313 HOH A O   1 
HETATM 6355 O O   . HOH M 9 .   ? -13.64296 8.29674   52.60503  1.000 40.20294  ? 314 HOH A O   1 
HETATM 6356 O O   . HOH M 9 .   ? -16.25678 18.84913  53.38952  1.000 33.96089  ? 315 HOH A O   1 
HETATM 6357 O O   . HOH M 9 .   ? 0.30458   14.74715  52.71796  1.000 41.34343  ? 316 HOH A O   1 
HETATM 6358 O O   . HOH M 9 .   ? -1.63727  29.82191  37.85124  1.000 43.64168  ? 317 HOH A O   1 
HETATM 6359 O O   . HOH M 9 .   ? 4.76593   16.85563  50.59898  1.000 24.41178  ? 318 HOH A O   1 
HETATM 6360 O O   . HOH M 9 .   ? -13.56204 7.49345   42.99366  1.000 43.99363  ? 319 HOH A O   1 
HETATM 6361 O O   . HOH M 9 .   ? -15.21238 19.81106  51.13215  1.000 36.94742  ? 320 HOH A O   1 
HETATM 6362 O O   . HOH M 9 .   ? -0.06307  24.27483  41.49130  1.000 26.42605  ? 321 HOH A O   1 
HETATM 6363 O O   . HOH M 9 .   ? -8.90963  6.57912   68.29213  1.000 41.04802  ? 322 HOH A O   1 
HETATM 6364 O O   . HOH M 9 .   ? -5.08685  6.46219   59.63275  1.000 37.54357  ? 323 HOH A O   1 
HETATM 6365 O O   . HOH M 9 .   ? 5.72930   26.17282  48.63195  1.000 24.81194  ? 324 HOH A O   1 
HETATM 6366 O O   . HOH M 9 .   ? -20.00649 10.87698  46.25741  1.000 42.87523  ? 325 HOH A O   1 
HETATM 6367 O O   . HOH M 9 .   ? -13.22086 3.29847   60.02574  1.000 47.32432  ? 326 HOH A O   1 
HETATM 6368 O O   . HOH M 9 .   ? -27.98704 21.17460  56.24959  1.000 51.29697  ? 327 HOH A O   1 
HETATM 6369 O O   . HOH M 9 .   ? -7.90256  26.24770  49.38185  1.000 30.45542  ? 328 HOH A O   1 
HETATM 6370 O O   . HOH M 9 .   ? -4.80878  13.14383  47.11889  1.000 30.20616  ? 329 HOH A O   1 
HETATM 6371 O O   . HOH M 9 .   ? -9.63472  25.48165  61.23489  1.000 41.26098  ? 330 HOH A O   1 
HETATM 6372 O O   . HOH M 9 .   ? 0.90423   8.85109   43.20263  1.000 26.10648  ? 331 HOH A O   1 
HETATM 6373 O O   . HOH M 9 .   ? -2.30428  36.87430  50.43838  1.000 40.94792  ? 332 HOH A O   1 
HETATM 6374 O O   . HOH M 9 .   ? -1.96081  8.90986   56.45626  1.000 28.13464  ? 333 HOH A O   1 
HETATM 6375 O O   . HOH M 9 .   ? 7.77748   28.38731  62.11862  1.000 40.63225  ? 334 HOH A O   1 
HETATM 6376 O O   . HOH M 9 .   ? 7.59781   15.62932  57.53176  1.000 28.08289  ? 335 HOH A O   1 
HETATM 6377 O O   . HOH M 9 .   ? -11.05178 28.11140  49.66649  1.000 45.55376  ? 336 HOH A O   1 
HETATM 6378 O O   . HOH M 9 .   ? -21.75872 18.42789  52.89359  1.000 50.74900  ? 337 HOH A O   1 
HETATM 6379 O O   . HOH M 9 .   ? 1.01232   24.88882  62.72015  1.000 57.77182  ? 338 HOH A O   1 
HETATM 6380 O O   . HOH M 9 .   ? 0.90448   12.73487  48.95448  1.000 40.49150  ? 339 HOH A O   1 
HETATM 6381 O O   . HOH M 9 .   ? -12.38731 4.14659   62.12423  1.000 43.46633  ? 340 HOH A O   1 
HETATM 6382 O O   . HOH M 9 .   ? -16.50287 20.20228  59.62983  1.000 46.16775  ? 341 HOH A O   1 
HETATM 6383 O O   . HOH M 9 .   ? -8.78171  24.84365  55.44333  1.000 50.76566  ? 342 HOH A O   1 
HETATM 6384 O O   . HOH M 9 .   ? -20.00363 4.93557   45.88307  1.000 49.09365  ? 343 HOH A O   1 
HETATM 6385 O O   . HOH M 9 .   ? 9.42916   9.46171   49.33896  1.000 48.75469  ? 344 HOH A O   1 
HETATM 6386 O O   . HOH M 9 .   ? -14.38141 5.48526   33.38419  1.000 50.15542  ? 345 HOH A O   1 
HETATM 6387 O O   . HOH M 9 .   ? 0.90807   4.73546   45.12731  1.000 55.11011  ? 346 HOH A O   1 
HETATM 6388 O O   . HOH M 9 .   ? 18.66334  16.88164  53.35461  1.000 51.94848  ? 347 HOH A O   1 
HETATM 6389 O O   . HOH M 9 .   ? -9.87189  34.05651  38.06995  1.000 53.56910  ? 348 HOH A O   1 
HETATM 6390 O O   . HOH M 9 .   ? 3.63165   7.06860   43.11724  1.000 51.30821  ? 349 HOH A O   1 
HETATM 6391 O O   . HOH M 9 .   ? -10.26999 28.25934  32.19955  1.000 52.41188  ? 350 HOH A O   1 
HETATM 6392 O O   . HOH M 9 .   ? -2.31387  4.53734   51.51648  1.000 53.85019  ? 351 HOH A O   1 
HETATM 6393 O O   . HOH M 9 .   ? -18.56423 20.70588  54.75687  1.000 55.10885  ? 352 HOH A O   1 
HETATM 6394 O O   . HOH M 9 .   ? -3.56586  5.37960   63.04006  1.000 59.90801  ? 353 HOH A O   1 
HETATM 6395 O O   . HOH M 9 .   ? 7.29558   12.76888  53.14288  1.000 29.76703  ? 354 HOH A O   1 
HETATM 6396 O O   . HOH M 9 .   ? -3.31246  23.97093  66.56226  1.000 57.70379  ? 355 HOH A O   1 
HETATM 6397 O O   . HOH M 9 .   ? -24.01159 22.50217  48.63715  1.000 52.32211  ? 356 HOH A O   1 
HETATM 6398 O O   . HOH M 9 .   ? 13.80108  17.16814  56.88314  1.000 42.71046  ? 357 HOH A O   1 
HETATM 6399 O O   . HOH M 9 .   ? -24.76261 21.36526  46.62992  1.000 65.09053  ? 358 HOH A O   1 
HETATM 6400 O O   . HOH M 9 .   ? -12.62070 22.00654  50.47607  1.000 49.21480  ? 359 HOH A O   1 
HETATM 6401 O O   . HOH M 9 .   ? -1.15828  9.94085   58.42784  1.000 31.10760  ? 360 HOH A O   1 
HETATM 6402 O O   . HOH M 9 .   ? -21.49592 22.73273  29.97648  1.000 57.65401  ? 361 HOH A O   1 
HETATM 6403 O O   . HOH M 9 .   ? -21.94711 21.44123  31.94276  1.000 61.80314  ? 362 HOH A O   1 
HETATM 6404 O O   . HOH M 9 .   ? 2.96608   13.16357  49.91553  1.000 42.05464  ? 363 HOH A O   1 
HETATM 6405 O O   . HOH N 9 .   ? 20.75882  11.77965  50.89936  1.000 50.24850  ? 301 HOH B O   1 
HETATM 6406 O O   . HOH N 9 .   ? 0.11658   16.85350  34.12317  1.000 29.00935  ? 302 HOH B O   1 
HETATM 6407 O O   . HOH N 9 .   ? 6.99813   0.03809   93.83358  1.000 44.31830  ? 303 HOH B O   1 
HETATM 6408 O O   . HOH N 9 .   ? 17.66114  8.40124   88.11592  1.000 52.32299  ? 304 HOH B O   1 
HETATM 6409 O O   . HOH N 9 .   ? 23.98314  3.17284   71.09461  1.000 56.54290  ? 305 HOH B O   1 
HETATM 6410 O O   . HOH N 9 .   ? 14.47515  21.24996  25.83413  1.000 53.83889  ? 306 HOH B O   1 
HETATM 6411 O O   . HOH N 9 .   ? 3.30952   15.21652  69.86654  1.000 29.96658  ? 307 HOH B O   1 
HETATM 6412 O O   . HOH N 9 .   ? 6.39495   9.29791   22.47208  1.000 36.05339  ? 308 HOH B O   1 
HETATM 6413 O O   . HOH N 9 .   ? 5.14442   17.22212  74.05229  1.000 45.11332  ? 309 HOH B O   1 
HETATM 6414 O O   . HOH N 9 .   ? 12.28631  16.65968  30.90226  1.000 31.71846  ? 310 HOH B O   1 
HETATM 6415 O O   . HOH N 9 .   ? -4.31493  19.26328  34.71175  1.000 24.01615  ? 311 HOH B O   1 
HETATM 6416 O O   . HOH N 9 .   ? 15.39221  27.94501  39.53656  1.000 29.11237  ? 312 HOH B O   1 
HETATM 6417 O O   . HOH N 9 .   ? 10.82846  19.46309  34.06580  1.000 28.00238  ? 313 HOH B O   1 
HETATM 6418 O O   . HOH N 9 .   ? 8.90474   18.90408  72.05045  1.000 37.89300  ? 314 HOH B O   1 
HETATM 6419 O O   . HOH N 9 .   ? -19.98866 10.43258  43.76533  1.000 43.49064  ? 315 HOH B O   1 
HETATM 6420 O O   . HOH N 9 .   ? 14.51700  14.68605  35.69865  1.000 27.13122  ? 316 HOH B O   1 
HETATM 6421 O O   . HOH N 9 .   ? 9.06035   25.99030  33.59117  1.000 26.17133  ? 317 HOH B O   1 
HETATM 6422 O O   . HOH N 9 .   ? -13.53254 7.41408   38.77758  1.000 37.96073  ? 318 HOH B O   1 
HETATM 6423 O O   . HOH N 9 .   ? 15.84264  -0.72643  71.95461  1.000 35.97253  ? 319 HOH B O   1 
HETATM 6424 O O   . HOH N 9 .   ? 4.29580   10.25733  45.30876  1.000 37.77844  ? 320 HOH B O   1 
HETATM 6425 O O   . HOH N 9 .   ? 9.51720   26.82069  52.21147  1.000 39.85449  ? 321 HOH B O   1 
HETATM 6426 O O   . HOH N 9 .   ? -7.71199  13.64101  28.11685  1.000 38.92598  ? 322 HOH B O   1 
HETATM 6427 O O   . HOH N 9 .   ? 5.65733   11.59204  31.86261  1.000 18.42360  ? 323 HOH B O   1 
HETATM 6428 O O   . HOH N 9 .   ? 12.95910  23.55136  28.20998  1.000 31.97213  ? 324 HOH B O   1 
HETATM 6429 O O   . HOH N 9 .   ? 4.68615   7.70314   78.45333  1.000 32.65668  ? 325 HOH B O   1 
HETATM 6430 O O   . HOH N 9 .   ? 19.64226  19.24318  51.80317  1.000 31.79176  ? 326 HOH B O   1 
HETATM 6431 O O   . HOH N 9 .   ? 0.16886   12.84957  46.05905  1.000 31.05750  ? 327 HOH B O   1 
HETATM 6432 O O   . HOH N 9 .   ? 19.43161  1.54556   81.63980  1.000 29.16955  ? 328 HOH B O   1 
HETATM 6433 O O   . HOH N 9 .   ? 0.10256   19.65836  57.85228  1.000 31.37828  ? 329 HOH B O   1 
HETATM 6434 O O   . HOH N 9 .   ? 6.43951   12.81995  75.61799  1.000 33.92005  ? 330 HOH B O   1 
HETATM 6435 O O   . HOH N 9 .   ? 11.31423  4.48739   96.54735  1.000 40.05486  ? 331 HOH B O   1 
HETATM 6436 O O   . HOH N 9 .   ? 16.98125  16.62615  49.21332  1.000 27.98892  ? 332 HOH B O   1 
HETATM 6437 O O   . HOH N 9 .   ? -3.42513  10.33321  17.14262  1.000 44.19301  ? 333 HOH B O   1 
HETATM 6438 O O   . HOH N 9 .   ? 15.96743  23.79726  32.19090  1.000 35.56551  ? 334 HOH B O   1 
HETATM 6439 O O   . HOH N 9 .   ? 15.05990  13.41400  30.63756  1.000 41.60472  ? 335 HOH B O   1 
HETATM 6440 O O   . HOH N 9 .   ? 5.06103   9.80518   83.60236  1.000 58.26698  ? 336 HOH B O   1 
HETATM 6441 O O   . HOH N 9 .   ? 8.47414   26.49173  48.60937  1.000 27.69095  ? 337 HOH B O   1 
HETATM 6442 O O   . HOH N 9 .   ? 12.82422  -6.67870  82.11711  1.000 53.62200  ? 338 HOH B O   1 
HETATM 6443 O O   . HOH N 9 .   ? 5.33968   -7.52804  87.29562  1.000 63.15547  ? 339 HOH B O   1 
HETATM 6444 O O   . HOH N 9 .   ? -11.44570 7.06559   40.54056  1.000 41.72296  ? 340 HOH B O   1 
HETATM 6445 O O   . HOH N 9 .   ? 13.22604  22.70904  70.31249  1.000 45.66995  ? 341 HOH B O   1 
HETATM 6446 O O   . HOH N 9 .   ? 7.35424   12.69612  56.40047  1.000 23.73827  ? 342 HOH B O   1 
HETATM 6447 O O   . HOH N 9 .   ? 12.22313  6.40020   88.50708  1.000 36.65260  ? 343 HOH B O   1 
HETATM 6448 O O   . HOH N 9 .   ? 6.61687   8.08432   34.78474  1.000 31.31927  ? 344 HOH B O   1 
HETATM 6449 O O   . HOH N 9 .   ? 18.69815  15.58980  38.91048  1.000 36.09467  ? 345 HOH B O   1 
HETATM 6450 O O   . HOH N 9 .   ? 3.28935   4.67492   38.56939  1.000 51.55892  ? 346 HOH B O   1 
HETATM 6451 O O   . HOH N 9 .   ? 9.41559   10.57080  82.55929  1.000 32.77693  ? 347 HOH B O   1 
HETATM 6452 O O   . HOH N 9 .   ? 13.26486  4.17762   66.41280  1.000 41.40676  ? 348 HOH B O   1 
HETATM 6453 O O   . HOH N 9 .   ? 22.02634  4.22825   83.24136  1.000 50.61672  ? 349 HOH B O   1 
HETATM 6454 O O   . HOH N 9 .   ? 8.63966   1.21153   90.78749  1.000 36.90342  ? 350 HOH B O   1 
HETATM 6455 O O   . HOH N 9 .   ? 15.35152  9.16571   38.46110  1.000 44.43488  ? 351 HOH B O   1 
HETATM 6456 O O   . HOH N 9 .   ? 10.41892  15.42800  58.19899  1.000 23.84583  ? 352 HOH B O   1 
HETATM 6457 O O   . HOH N 9 .   ? 10.74208  5.48475   39.01878  1.000 47.83529  ? 353 HOH B O   1 
HETATM 6458 O O   . HOH N 9 .   ? -4.07293  6.28354   39.78049  1.000 37.75814  ? 354 HOH B O   1 
HETATM 6459 O O   . HOH N 9 .   ? -9.57604  5.42829   31.03042  1.000 47.08496  ? 355 HOH B O   1 
HETATM 6460 O O   . HOH N 9 .   ? 6.41354   6.07555   38.75468  1.000 51.38371  ? 356 HOH B O   1 
HETATM 6461 O O   . HOH N 9 .   ? 11.72829  17.14469  21.38895  1.000 51.48534  ? 357 HOH B O   1 
HETATM 6462 O O   . HOH N 9 .   ? 12.27613  26.78014  60.66980  1.000 37.17213  ? 358 HOH B O   1 
HETATM 6463 O O   . HOH N 9 .   ? 10.10780  26.43228  61.91047  1.000 32.07072  ? 359 HOH B O   1 
HETATM 6464 O O   . HOH N 9 .   ? -10.36548 9.80456   25.75582  1.000 45.56939  ? 360 HOH B O   1 
HETATM 6465 O O   . HOH N 9 .   ? 13.85429  25.80364  64.29709  1.000 43.28313  ? 361 HOH B O   1 
HETATM 6466 O O   . HOH N 9 .   ? 4.56321   7.34415   40.31003  1.000 30.16703  ? 362 HOH B O   1 
HETATM 6467 O O   . HOH N 9 .   ? -1.55561  22.59487  67.17043  1.000 44.50876  ? 363 HOH B O   1 
HETATM 6468 O O   . HOH N 9 .   ? 16.10987  11.75665  38.26403  1.000 39.64699  ? 364 HOH B O   1 
HETATM 6469 O O   . HOH N 9 .   ? 22.83771  20.64083  41.98238  1.000 48.20052  ? 365 HOH B O   1 
HETATM 6470 O O   . HOH N 9 .   ? 10.03420  5.39710   89.50267  1.000 44.67658  ? 366 HOH B O   1 
HETATM 6471 O O   . HOH N 9 .   ? 14.04322  -9.19962  95.11551  1.000 60.59420  ? 367 HOH B O   1 
HETATM 6472 O O   . HOH N 9 .   ? 12.59060  15.49532  78.20078  1.000 45.38833  ? 368 HOH B O   1 
HETATM 6473 O O   . HOH N 9 .   ? 8.86582   5.31396   37.40008  1.000 39.51802  ? 369 HOH B O   1 
HETATM 6474 O O   . HOH N 9 .   ? 3.53619   24.83608  18.57137  1.000 45.64356  ? 370 HOH B O   1 
HETATM 6475 O O   . HOH N 9 .   ? 1.75497   11.05840  44.56226  1.000 28.20621  ? 371 HOH B O   1 
HETATM 6476 O O   . HOH N 9 .   ? -0.52151  19.39405  33.35951  1.000 34.38794  ? 372 HOH B O   1 
HETATM 6477 O O   . HOH N 9 .   ? 6.35674   -2.77690  89.41804  1.000 54.91577  ? 373 HOH B O   1 
HETATM 6478 O O   . HOH N 9 .   ? 15.06120  22.51147  30.01844  1.000 42.36518  ? 374 HOH B O   1 
HETATM 6479 O O   . HOH N 9 .   ? 16.94628  28.44431  41.68932  1.000 39.73917  ? 375 HOH B O   1 
HETATM 6480 O O   . HOH N 9 .   ? 8.86549   21.47772  71.82442  1.000 46.88329  ? 376 HOH B O   1 
HETATM 6481 O O   . HOH N 9 .   ? 0.09925   4.41949   38.17342  1.000 51.98580  ? 377 HOH B O   1 
HETATM 6482 O O   . HOH N 9 .   ? 6.55718   27.08327  34.69606  1.000 39.13177  ? 378 HOH B O   1 
HETATM 6483 O O   . HOH N 9 .   ? 0.27175   6.17411   60.40532  1.000 60.35148  ? 379 HOH B O   1 
HETATM 6484 O O   . HOH N 9 .   ? 11.18229  26.72643  65.37469  1.000 56.93864  ? 380 HOH B O   1 
HETATM 6485 O O   . HOH N 9 .   ? -3.04491  16.22870  18.16836  1.000 50.56232  ? 381 HOH B O   1 
HETATM 6486 O O   . HOH N 9 .   ? 8.21514   10.62815  56.93458  1.000 35.21384  ? 382 HOH B O   1 
HETATM 6487 O O   . HOH N 9 .   ? -22.88740 17.16511  37.25537  1.000 63.32325  ? 383 HOH B O   1 
HETATM 6488 O O   . HOH O 9 .   ? -2.68138  20.37873  33.69831  1.000 34.31261  ? 101 HOH C O   1 
HETATM 6489 O O   . HOH O 9 .   ? 5.26808   30.27613  39.66579  1.000 43.21446  ? 102 HOH C O   1 
HETATM 6490 O O   . HOH O 9 .   ? 4.72710   24.96738  35.15586  1.000 31.61596  ? 103 HOH C O   1 
HETATM 6491 O O   . HOH P 9 .   ? -0.77144  4.80170   27.02655  1.000 35.45001  ? 301 HOH D O   1 
HETATM 6492 O O   . HOH P 9 .   ? 8.62935   -8.79646  20.53011  1.000 44.62665  ? 302 HOH D O   1 
HETATM 6493 O O   . HOH P 9 .   ? 24.41785  -14.05667 -7.42905  1.000 42.43414  ? 303 HOH D O   1 
HETATM 6494 O O   . HOH P 9 .   ? 7.51047   5.53168   34.89279  1.000 36.81176  ? 304 HOH D O   1 
HETATM 6495 O O   . HOH P 9 .   ? 24.78431  -17.38297 -17.94846 1.000 43.02022  ? 305 HOH D O   1 
HETATM 6496 O O   . HOH P 9 .   ? 0.79410   4.07065   5.45222   1.000 38.93455  ? 306 HOH D O   1 
HETATM 6497 O O   . HOH P 9 .   ? 19.65723  -13.74730 -12.93493 1.000 38.41806  ? 307 HOH D O   1 
HETATM 6498 O O   . HOH P 9 .   ? 16.61924  0.60194   0.75483   1.000 40.79877  ? 308 HOH D O   1 
HETATM 6499 O O   . HOH P 9 .   ? 3.60611   -5.88169  9.25993   1.000 35.41450  ? 309 HOH D O   1 
HETATM 6500 O O   . HOH P 9 .   ? 11.08583  -12.11774 -3.60760  1.000 38.58770  ? 310 HOH D O   1 
HETATM 6501 O O   . HOH P 9 .   ? 19.22002  1.66184   15.67750  1.000 26.16707  ? 311 HOH D O   1 
HETATM 6502 O O   . HOH P 9 .   ? 2.42594   -10.37604 14.77488  1.000 46.30374  ? 312 HOH D O   1 
HETATM 6503 O O   . HOH P 9 .   ? 20.32904  -20.27041 -20.91001 1.000 57.58351  ? 313 HOH D O   1 
HETATM 6504 O O   . HOH P 9 .   ? 33.23935  -27.35961 -22.32321 1.000 74.99169  ? 314 HOH D O   1 
HETATM 6505 O O   . HOH P 9 .   ? -6.43964  8.12314   14.26587  1.000 41.44341  ? 315 HOH D O   1 
HETATM 6506 O O   . HOH P 9 .   ? 10.52811  -2.79141  25.87192  1.000 33.75491  ? 316 HOH D O   1 
HETATM 6507 O O   . HOH P 9 .   ? 25.27214  -14.22830 -10.32791 1.000 41.19124  ? 317 HOH D O   1 
HETATM 6508 O O   . HOH P 9 .   ? 9.28316   9.77501   11.37224  1.000 42.30919  ? 318 HOH D O   1 
HETATM 6509 O O   . HOH P 9 .   ? 12.83350  -12.10983 -12.79702 1.000 47.53086  ? 319 HOH D O   1 
HETATM 6510 O O   . HOH P 9 .   ? 3.95232   -8.95238  16.58222  1.000 35.61585  ? 320 HOH D O   1 
HETATM 6511 O O   . HOH P 9 .   ? 2.94635   7.93418   17.21986  1.000 36.96750  ? 321 HOH D O   1 
HETATM 6512 O O   . HOH P 9 .   ? 2.94325   -5.78807  -2.50512  1.000 40.67433  ? 322 HOH D O   1 
HETATM 6513 O O   . HOH P 9 .   ? 20.24961  -1.02717  6.47652   1.000 53.76092  ? 323 HOH D O   1 
HETATM 6514 O O   . HOH P 9 .   ? -4.09451  -7.42609  18.36056  1.000 43.71157  ? 324 HOH D O   1 
HETATM 6515 O O   . HOH P 9 .   ? 12.40996  4.20258   -10.20672 1.000 51.40350  ? 325 HOH D O   1 
HETATM 6516 O O   . HOH P 9 .   ? 7.71591   -12.62060 7.89887   1.000 46.61872  ? 326 HOH D O   1 
HETATM 6517 O O   . HOH P 9 .   ? 38.34854  -22.27071 -12.65619 1.000 52.70487  ? 327 HOH D O   1 
HETATM 6518 O O   . HOH P 9 .   ? 42.02184  -21.10338 -2.93708  1.000 52.22115  ? 328 HOH D O   1 
HETATM 6519 O O   . HOH P 9 .   ? 2.31006   10.19518  19.86557  1.000 48.10985  ? 329 HOH D O   1 
HETATM 6520 O O   . HOH P 9 .   ? 19.87389  -3.26463  10.29546  1.000 40.26772  ? 330 HOH D O   1 
HETATM 6521 O O   . HOH P 9 .   ? 13.65726  7.14615   5.25774   1.000 54.35809  ? 331 HOH D O   1 
HETATM 6522 O O   . HOH P 9 .   ? 34.68882  -30.57594 -4.44300  1.000 52.39901  ? 332 HOH D O   1 
HETATM 6523 O O   . HOH P 9 .   ? 1.78869   6.33971   27.55732  1.000 40.70292  ? 333 HOH D O   1 
HETATM 6524 O O   . HOH P 9 .   ? -9.06987  3.83357   20.18012  1.000 48.49272  ? 334 HOH D O   1 
HETATM 6525 O O   . HOH P 9 .   ? 1.50556   -5.59904  0.19708   1.000 32.27307  ? 335 HOH D O   1 
HETATM 6526 O O   . HOH P 9 .   ? -1.51633  11.16494  15.39464  1.000 46.98649  ? 336 HOH D O   1 
HETATM 6527 O O   . HOH P 9 .   ? -1.30666  -2.74106  22.73813  1.000 39.16117  ? 337 HOH D O   1 
HETATM 6528 O O   . HOH P 9 .   ? 7.81392   7.96377   -3.87018  1.000 49.83690  ? 338 HOH D O   1 
HETATM 6529 O O   . HOH P 9 .   ? 0.41438   -2.41770  25.14752  1.000 58.64255  ? 339 HOH D O   1 
HETATM 6530 O O   . HOH P 9 .   ? 20.59628  -11.89350 -1.77422  1.000 50.35920  ? 340 HOH D O   1 
HETATM 6531 O O   . HOH P 9 .   ? 19.69240  -7.07007  -14.93603 1.000 46.04008  ? 341 HOH D O   1 
HETATM 6532 O O   . HOH P 9 .   ? 22.05003  -2.99882  -4.38631  1.000 45.19569  ? 342 HOH D O   1 
HETATM 6533 O O   . HOH P 9 .   ? 18.80308  -8.70644  -16.03448 1.000 53.83003  ? 343 HOH D O   1 
HETATM 6534 O O   . HOH P 9 .   ? 18.72896  -1.54343  -4.37866  1.000 45.66965  ? 344 HOH D O   1 
HETATM 6535 O O   . HOH P 9 .   ? 5.33629   8.74863   17.05555  1.000 49.65350  ? 345 HOH D O   1 
HETATM 6536 O O   . HOH P 9 .   ? 3.23564   -8.86491  20.97089  1.000 35.23911  ? 346 HOH D O   1 
HETATM 6537 O O   . HOH P 9 .   ? 15.67972  -13.98787 -6.22339  1.000 53.13803  ? 347 HOH D O   1 
HETATM 6538 O O   . HOH P 9 .   ? 18.43408  -1.69443  9.19674   1.000 52.82186  ? 348 HOH D O   1 
HETATM 6539 O O   . HOH P 9 .   ? 15.86793  -12.83975 -3.39611  1.000 50.49083  ? 349 HOH D O   1 
HETATM 6540 O O   . HOH P 9 .   ? 9.38144   -5.91713  23.91264  1.000 35.68747  ? 350 HOH D O   1 
HETATM 6541 O O   . HOH P 9 .   ? -3.57420  -7.08831  9.86671   1.000 46.57832  ? 351 HOH D O   1 
HETATM 6542 O O   . HOH P 9 .   ? -2.45436  -8.14484  11.60807  1.000 47.14131  ? 352 HOH D O   1 
HETATM 6543 O O   . HOH P 9 .   ? 9.57588   -15.18084 8.00863   1.000 56.99442  ? 353 HOH D O   1 
HETATM 6544 O O   . HOH P 9 .   ? 34.69209  -28.09585 -0.46178  1.000 45.71228  ? 354 HOH D O   1 
HETATM 6545 O O   . HOH P 9 .   ? 12.05945  9.18029   12.55434  1.000 43.10912  ? 355 HOH D O   1 
HETATM 6546 O O   . HOH P 9 .   ? 35.51084  -28.57261 -2.73335  1.000 48.21829  ? 356 HOH D O   1 
HETATM 6547 O O   . HOH P 9 .   ? 15.86466  -11.11394 12.29224  1.000 58.15137  ? 357 HOH D O   1 
HETATM 6548 O O   . HOH P 9 .   ? -5.30181  -13.40551 15.97276  1.000 57.91400  ? 358 HOH D O   1 
HETATM 6549 O O   . HOH P 9 .   ? 2.57217   -7.70292  -0.30806  1.000 45.81202  ? 359 HOH D O   1 
HETATM 6550 O O   . HOH Q 9 .   ? 14.35722  16.42938  28.91535  1.000 44.47466  ? 401 HOH E O   1 
HETATM 6551 O O   . HOH Q 9 .   ? 28.96864  6.78478   28.30716  1.000 44.69860  ? 402 HOH E O   1 
HETATM 6552 O O   . HOH Q 9 .   ? 13.53221  0.27904   25.87303  1.000 27.05082  ? 403 HOH E O   1 
HETATM 6553 O O   . HOH Q 9 .   ? 21.53409  -24.76065 29.77529  1.000 33.30730  ? 404 HOH E O   1 
HETATM 6554 O O   . HOH Q 9 .   ? 8.97352   -2.51907  27.97036  1.000 45.68007  ? 405 HOH E O   1 
HETATM 6555 O O   . HOH Q 9 .   ? 5.83424   6.73480   30.66202  1.000 26.25841  ? 406 HOH E O   1 
HETATM 6556 O O   . HOH Q 9 .   ? 32.38051  -31.15271 8.90805   1.000 51.59686  ? 407 HOH E O   1 
HETATM 6557 O O   . HOH Q 9 .   ? 23.88971  -11.17789 36.91783  1.000 30.89940  ? 408 HOH E O   1 
HETATM 6558 O O   . HOH Q 9 .   ? 11.05216  9.72056   26.72026  1.000 28.62492  ? 409 HOH E O   1 
HETATM 6559 O O   . HOH Q 9 .   ? 23.90870  9.80027   36.67855  1.000 50.51893  ? 410 HOH E O   1 
HETATM 6560 O O   . HOH Q 9 .   ? 37.85725  -8.38708  10.63493  1.000 34.21233  ? 411 HOH E O   1 
HETATM 6561 O O   . HOH Q 9 .   ? 23.18613  1.16385   38.10685  1.000 27.26506  ? 412 HOH E O   1 
HETATM 6562 O O   . HOH Q 9 .   ? 21.54569  8.36920   33.22008  1.000 35.64612  ? 413 HOH E O   1 
HETATM 6563 O O   . HOH Q 9 .   ? 35.48727  -16.71112 25.42388  1.000 42.65636  ? 414 HOH E O   1 
HETATM 6564 O O   . HOH Q 9 .   ? 10.94546  10.27560  21.79191  1.000 40.49673  ? 415 HOH E O   1 
HETATM 6565 O O   . HOH Q 9 .   ? 41.88821  -24.96841 15.33767  1.000 42.03457  ? 416 HOH E O   1 
HETATM 6566 O O   . HOH Q 9 .   ? 14.37487  4.98012   26.62219  1.000 23.01766  ? 417 HOH E O   1 
HETATM 6567 O O   . HOH Q 9 .   ? 17.01027  3.16990   26.33346  1.000 26.28473  ? 418 HOH E O   1 
HETATM 6568 O O   . HOH Q 9 .   ? 29.85199  -10.46305 2.55391   1.000 39.00439  ? 419 HOH E O   1 
HETATM 6569 O O   . HOH Q 9 .   ? 28.07941  -1.15350  18.77749  1.000 37.73199  ? 420 HOH E O   1 
HETATM 6570 O O   . HOH Q 9 .   ? 28.58152  7.58355   25.78974  1.000 38.30180  ? 421 HOH E O   1 
HETATM 6571 O O   . HOH Q 9 .   ? 27.31934  -5.34128  24.70181  1.000 24.11110  ? 422 HOH E O   1 
HETATM 6572 O O   . HOH Q 9 .   ? 29.50737  -18.44030 36.62482  1.000 29.89816  ? 423 HOH E O   1 
HETATM 6573 O O   . HOH Q 9 .   ? 26.273    -27.097   23.180    1.000 45.99309  ? 424 HOH E O   1 
HETATM 6574 O O   . HOH Q 9 .   ? 25.93793  10.27318  27.41833  1.000 38.22730  ? 425 HOH E O   1 
HETATM 6575 O O   . HOH Q 9 .   ? 35.74497  -9.92555  6.80458   1.000 23.01811  ? 426 HOH E O   1 
HETATM 6576 O O   . HOH Q 9 .   ? 14.69802  -13.19798 22.62650  1.000 38.26316  ? 427 HOH E O   1 
HETATM 6577 O O   . HOH Q 9 .   ? 12.55770  2.94789   26.03554  1.000 25.06401  ? 428 HOH E O   1 
HETATM 6578 O O   . HOH Q 9 .   ? 30.18936  -4.65811  -9.88846  1.000 45.74830  ? 429 HOH E O   1 
HETATM 6579 O O   . HOH Q 9 .   ? 15.84742  18.79678  24.00039  1.000 49.96742  ? 430 HOH E O   1 
HETATM 6580 O O   . HOH Q 9 .   ? 35.28064  -15.90091 22.90539  1.000 25.52019  ? 431 HOH E O   1 
HETATM 6581 O O   . HOH Q 9 .   ? 36.49809  -24.30015 2.12760   1.000 41.32124  ? 432 HOH E O   1 
HETATM 6582 O O   . HOH Q 9 .   ? 41.50374  -22.84329 8.51194   1.000 41.92273  ? 433 HOH E O   1 
HETATM 6583 O O   . HOH Q 9 .   ? 17.38464  3.58557   15.43333  1.000 23.53835  ? 434 HOH E O   1 
HETATM 6584 O O   . HOH Q 9 .   ? 12.88576  1.53615   39.53635  1.000 48.43024  ? 435 HOH E O   1 
HETATM 6585 O O   . HOH Q 9 .   ? 33.01594  -7.10243  1.08494   1.000 38.74440  ? 436 HOH E O   1 
HETATM 6586 O O   . HOH Q 9 .   ? 8.96445   8.32547   22.66383  1.000 27.57703  ? 437 HOH E O   1 
HETATM 6587 O O   . HOH Q 9 .   ? 17.33823  -16.88162 28.25919  1.000 32.55167  ? 438 HOH E O   1 
HETATM 6588 O O   . HOH Q 9 .   ? 8.61084   -7.68461  35.39688  1.000 47.32578  ? 439 HOH E O   1 
HETATM 6589 O O   . HOH Q 9 .   ? 32.36408  -6.10054  28.76727  1.000 42.06945  ? 440 HOH E O   1 
HETATM 6590 O O   . HOH Q 9 .   ? 43.36953  -7.56327  -2.60085  1.000 43.11376  ? 441 HOH E O   1 
HETATM 6591 O O   . HOH Q 9 .   ? 14.08784  -8.77629  32.99981  1.000 33.40623  ? 442 HOH E O   1 
HETATM 6592 O O   . HOH Q 9 .   ? 32.01601  -2.22657  19.13122  1.000 41.41391  ? 443 HOH E O   1 
HETATM 6593 O O   . HOH Q 9 .   ? 25.48014  -6.83897  -4.74883  1.000 42.42865  ? 444 HOH E O   1 
HETATM 6594 O O   . HOH Q 9 .   ? 16.96475  10.02358  21.80395  1.000 45.37907  ? 445 HOH E O   1 
HETATM 6595 O O   . HOH Q 9 .   ? 29.40338  5.57401   21.97544  1.000 41.25374  ? 446 HOH E O   1 
HETATM 6596 O O   . HOH Q 9 .   ? 24.63904  -6.03775  37.96715  1.000 40.18379  ? 447 HOH E O   1 
HETATM 6597 O O   . HOH Q 9 .   ? 32.49410  -1.95099  -4.47451  1.000 38.43766  ? 448 HOH E O   1 
HETATM 6598 O O   . HOH Q 9 .   ? 10.93949  -9.72916  29.19761  1.000 31.99543  ? 449 HOH E O   1 
HETATM 6599 O O   . HOH Q 9 .   ? 31.14430  -0.05710  26.08517  1.000 36.17163  ? 450 HOH E O   1 
HETATM 6600 O O   . HOH Q 9 .   ? 33.81556  -5.46223  27.08929  1.000 42.19854  ? 451 HOH E O   1 
HETATM 6601 O O   . HOH Q 9 .   ? 27.84444  -8.07872  16.72914  1.000 40.35889  ? 452 HOH E O   1 
HETATM 6602 O O   . HOH Q 9 .   ? 20.12119  -5.17398  38.30577  1.000 42.16294  ? 453 HOH E O   1 
HETATM 6603 O O   . HOH Q 9 .   ? 9.73810   -7.70721  25.56686  1.000 28.81046  ? 454 HOH E O   1 
HETATM 6604 O O   . HOH Q 9 .   ? 33.76441  -15.37007 19.65911  1.000 33.41041  ? 455 HOH E O   1 
HETATM 6605 O O   . HOH Q 9 .   ? 19.13878  -24.02600 28.24761  1.000 34.57954  ? 456 HOH E O   1 
HETATM 6606 O O   . HOH Q 9 .   ? 18.04206  -16.75831 37.99329  1.000 33.22939  ? 457 HOH E O   1 
HETATM 6607 O O   . HOH Q 9 .   ? 24.26795  -17.99032 18.96326  1.000 45.05590  ? 458 HOH E O   1 
HETATM 6608 O O   . HOH Q 9 .   ? 28.63373  -12.48724 38.67664  1.000 49.10370  ? 459 HOH E O   1 
HETATM 6609 O O   . HOH Q 9 .   ? 34.73593  -6.77723  19.96625  1.000 40.25562  ? 460 HOH E O   1 
HETATM 6610 O O   . HOH Q 9 .   ? 37.39146  -20.98610 29.93795  1.000 48.58973  ? 461 HOH E O   1 
HETATM 6611 O O   . HOH Q 9 .   ? 28.63732  8.70400   20.47552  1.000 39.88285  ? 462 HOH E O   1 
HETATM 6612 O O   . HOH Q 9 .   ? 33.07194  -0.22180  24.90749  1.000 48.09847  ? 463 HOH E O   1 
HETATM 6613 O O   . HOH Q 9 .   ? 29.16232  -12.44997 6.50138   1.000 33.68636  ? 464 HOH E O   1 
HETATM 6614 O O   . HOH Q 9 .   ? 25.78627  -9.60686  0.29796   1.000 39.15435  ? 465 HOH E O   1 
HETATM 6615 O O   . HOH Q 9 .   ? 26.62648  -9.42451  15.10184  1.000 45.84915  ? 466 HOH E O   1 
HETATM 6616 O O   . HOH Q 9 .   ? 14.17784  10.66797  24.02652  1.000 40.03525  ? 467 HOH E O   1 
HETATM 6617 O O   . HOH Q 9 .   ? 31.09802  -5.59152  5.40154   1.000 56.09236  ? 468 HOH E O   1 
HETATM 6618 O O   . HOH Q 9 .   ? 33.14785  -11.01590 30.06187  1.000 35.48506  ? 469 HOH E O   1 
HETATM 6619 O O   . HOH Q 9 .   ? 34.89631  -9.28785  19.79476  1.000 33.36968  ? 470 HOH E O   1 
HETATM 6620 O O   . HOH Q 9 .   ? 7.98031   -3.76619  31.51685  1.000 51.86291  ? 471 HOH E O   1 
HETATM 6621 O O   . HOH Q 9 .   ? 8.83859   -7.98146  28.46421  1.000 33.13309  ? 472 HOH E O   1 
HETATM 6622 O O   . HOH Q 9 .   ? 30.26008  -3.15333  5.67433   1.000 53.88317  ? 473 HOH E O   1 
HETATM 6623 O O   . HOH Q 9 .   ? 30.15400  7.67993   22.05530  1.000 53.77108  ? 474 HOH E O   1 
HETATM 6624 O O   . HOH Q 9 .   ? 19.69341  -13.08180 15.88429  1.000 52.40024  ? 475 HOH E O   1 
HETATM 6625 O O   . HOH Q 9 .   ? 11.50321  -13.26596 28.58797  1.000 44.14268  ? 476 HOH E O   1 
HETATM 6626 O O   . HOH Q 9 .   ? 17.368    -20.416   28.756    1.000 45.57709  ? 477 HOH E O   1 
HETATM 6627 O O   . HOH Q 9 .   ? 25.13581  -24.67877 35.94077  1.000 44.54307  ? 478 HOH E O   1 
HETATM 6628 O O   . HOH Q 9 .   ? 10.95167  11.02385  23.99422  1.000 35.52813  ? 479 HOH E O   1 
HETATM 6629 O O   . HOH Q 9 .   ? 22.73993  -1.41536  40.21006  1.000 57.62718  ? 480 HOH E O   1 
HETATM 6630 O O   . HOH Q 9 .   ? 13.06267  -15.28249 29.96784  1.000 43.03727  ? 481 HOH E O   1 
HETATM 6631 O O   . HOH Q 9 .   ? 15.56123  -16.83165 30.16659  1.000 40.03284  ? 482 HOH E O   1 
HETATM 6632 O O   . HOH Q 9 .   ? 30.23851  -8.15614  1.30730   1.000 34.54078  ? 483 HOH E O   1 
HETATM 6633 O O   . HOH Q 9 .   ? 28.03323  -10.62104 4.85802   1.000 41.03603  ? 484 HOH E O   1 
HETATM 6634 O O   . HOH Q 9 .   ? 27.25129  -14.03366 7.43316   1.000 51.70901  ? 485 HOH E O   1 
HETATM 6635 O O   . HOH Q 9 .   ? 19.84871  -17.30623 40.01713  1.000 50.60362  ? 486 HOH E O   1 
HETATM 6636 O O   . HOH Q 9 .   ? 7.11684   10.58885  19.09295  1.000 58.39049  ? 487 HOH E O   1 
HETATM 6637 O O   . HOH Q 9 .   ? 27.90767  -7.18724  0.36497   1.000 50.58309  ? 488 HOH E O   1 
HETATM 6638 O O   . HOH Q 9 .   ? 5.43090   8.96354   32.21633  1.000 21.36697  ? 489 HOH E O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLU A 1   ? 0.85843 0.85436 0.94808 -0.03811 -0.03069 0.02647  1   GLU A N   
2    C CA  . GLU A 1   ? 0.81989 0.80534 0.90067 -0.03502 -0.03474 0.02030  1   GLU A CA  
3    C C   . GLU A 1   ? 0.96894 0.94342 1.05486 -0.04172 -0.03518 0.01538  1   GLU A C   
4    O O   . GLU A 1   ? 1.08109 1.04710 1.16401 -0.03822 -0.03556 0.01475  1   GLU A O   
5    C CB  . GLU A 1   ? 0.65947 0.64256 0.73036 -0.02412 -0.03537 0.02305  1   GLU A CB  
6    N N   . ASP A 2   ? 0.87272 0.84766 0.96636 -0.05134 -0.03515 0.01180  2   ASP A N   
7    C CA  . ASP A 2   ? 0.87011 0.83570 0.97036 -0.05867 -0.03491 0.00776  2   ASP A CA  
8    C C   . ASP A 2   ? 0.79989 0.75353 0.89266 -0.05694 -0.03889 0.00082  2   ASP A C   
9    O O   . ASP A 2   ? 0.80723 0.75179 0.90162 -0.05788 -0.03871 -0.00087 2   ASP A O   
10   C CB  . ASP A 2   ? 0.91704 0.88668 1.02723 -0.06944 -0.03388 0.00555  2   ASP A CB  
11   C CG  . ASP A 2   ? 0.97120 0.94794 1.09209 -0.07374 -0.02898 0.01147  2   ASP A CG  
12   O OD1 . ASP A 2   ? 0.90957 0.88207 1.03328 -0.07237 -0.02642 0.01473  2   ASP A OD1 
13   O OD2 . ASP A 2   ? 1.07275 1.05939 1.19912 -0.07841 -0.02757 0.01286  2   ASP A OD2 
14   N N   . ILE A 3   ? 0.64379 0.59718 0.72825 -0.05432 -0.04238 -0.00329 3   ILE A N   
15   C CA  . ILE A 3   ? 0.61745 0.55953 0.69449 -0.05280 -0.04605 -0.01019 3   ILE A CA  
16   C C   . ILE A 3   ? 0.50581 0.44298 0.57543 -0.04372 -0.04631 -0.00827 3   ILE A C   
17   O O   . ILE A 3   ? 0.66045 0.60340 0.72414 -0.03569 -0.04574 -0.00355 3   ILE A O   
18   C CB  . ILE A 3   ? 0.56011 0.50326 0.62952 -0.05171 -0.04936 -0.01466 3   ILE A CB  
19   C CG1 . ILE A 3   ? 0.44928 0.39700 0.52613 -0.06100 -0.04931 -0.01706 3   ILE A CG1 
20   C CG2 . ILE A 3   ? 0.41383 0.34509 0.47493 -0.04959 -0.05291 -0.02169 3   ILE A CG2 
21   C CD1 . ILE A 3   ? 0.34828 0.29603 0.41796 -0.06062 -0.05260 -0.02198 3   ILE A CD1 
22   N N   . VAL A 4   ? 0.50268 0.42934 0.57253 -0.04493 -0.04719 -0.01201 4   VAL A N   
23   C CA  . VAL A 4   ? 0.53612 0.45760 0.59954 -0.03694 -0.04751 -0.01080 4   VAL A CA  
24   C C   . VAL A 4   ? 0.49053 0.40483 0.54294 -0.03282 -0.05154 -0.01732 4   VAL A C   
25   O O   . VAL A 4   ? 0.49754 0.40497 0.55006 -0.03830 -0.05390 -0.02430 4   VAL A O   
26   C CB  . VAL A 4   ? 0.46259 0.37731 0.53298 -0.04029 -0.04579 -0.01061 4   VAL A CB  
27   C CG1 . VAL A 4   ? 0.43756 0.34835 0.50146 -0.03151 -0.04589 -0.00861 4   VAL A CG1 
28   C CG2 . VAL A 4   ? 0.51765 0.43892 0.59937 -0.04548 -0.04154 -0.00474 4   VAL A CG2 
29   N N   . ALA A 5   ? 0.45688 0.37269 0.49975 -0.02327 -0.05221 -0.01515 5   ALA A N   
30   C CA  . ALA A 5   ? 0.40631 0.31564 0.43802 -0.01853 -0.05565 -0.02094 5   ALA A CA  
31   C C   . ALA A 5   ? 0.31811 0.22776 0.34192 -0.00832 -0.05538 -0.01757 5   ALA A C   
32   O O   . ALA A 5   ? 0.35464 0.27138 0.38044 -0.00428 -0.05272 -0.01029 5   ALA A O   
33   C CB  . ALA A 5   ? 0.32544 0.23857 0.35192 -0.01859 -0.05740 -0.02328 5   ALA A CB  
34   N N   . ASP A 6   ? 0.32927 0.23111 0.34405 -0.00429 -0.05811 -0.02311 6   ASP A N   
35   C CA  . ASP A 6   ? 0.29198 0.19424 0.29793 0.00566  -0.05821 -0.02076 6   ASP A CA  
36   C C   . ASP A 6   ? 0.39819 0.30895 0.39788 0.01164  -0.05780 -0.01678 6   ASP A C   
37   O O   . ASP A 6   ? 0.39332 0.30957 0.39039 0.01868  -0.05614 -0.01080 6   ASP A O   
38   C CB  . ASP A 6   ? 0.38089 0.27310 0.37841 0.00810  -0.06126 -0.02831 6   ASP A CB  
39   C CG  . ASP A 6   ? 0.41365 0.29752 0.41656 0.00344  -0.06168 -0.03202 6   ASP A CG  
40   O OD1 . ASP A 6   ? 0.35817 0.24376 0.37115 -0.00125 -0.05943 -0.02840 6   ASP A OD1 
41   O OD2 . ASP A 6   ? 0.33902 0.21455 0.33602 0.00448  -0.06416 -0.03865 6   ASP A OD2 
42   N N   . HIS A 7   ? 0.39850 0.31046 0.39562 0.00908  -0.05926 -0.01998 7   HIS A N   
43   C CA  . HIS A 7   ? 0.41547 0.33499 0.40612 0.01471  -0.05906 -0.01681 7   HIS A CA  
44   C C   . HIS A 7   ? 0.40792 0.33304 0.40352 0.00847  -0.05889 -0.01679 7   HIS A C   
45   O O   . HIS A 7   ? 0.37418 0.29441 0.37343 0.00099  -0.06029 -0.02222 7   HIS A O   
46   C CB  . HIS A 7   ? 0.30907 0.22297 0.28682 0.02102  -0.06154 -0.02179 7   HIS A CB  
47   C CG  . HIS A 7   ? 0.43655 0.34513 0.40917 0.02699  -0.06188 -0.02247 7   HIS A CG  
48   N ND1 . HIS A 7   ? 0.42744 0.34153 0.39808 0.03438  -0.06002 -0.01600 7   HIS A ND1 
49   C CD2 . HIS A 7   ? 0.35646 0.25505 0.32569 0.02661  -0.06383 -0.02887 7   HIS A CD2 
50   C CE1 . HIS A 7   ? 0.37318 0.28104 0.33928 0.03842  -0.06087 -0.01840 7   HIS A CE1 
51   N NE2 . HIS A 7   ? 0.37599 0.27453 0.34121 0.03382  -0.06318 -0.02623 7   HIS A NE2 
52   N N   . VAL A 8   ? 0.43173 0.36744 0.42764 0.01157  -0.05713 -0.01060 8   VAL A N   
53   C CA  . VAL A 8   ? 0.32203 0.26497 0.32219 0.00673  -0.05679 -0.00976 8   VAL A CA  
54   C C   . VAL A 8   ? 0.41202 0.36067 0.40286 0.01392  -0.05727 -0.00795 8   VAL A C   
55   O O   . VAL A 8   ? 0.38100 0.33391 0.36728 0.02172  -0.05605 -0.00299 8   VAL A O   
56   C CB  . VAL A 8   ? 0.34985 0.30162 0.36176 0.00225  -0.05362 -0.00338 8   VAL A CB  
57   C CG1 . VAL A 8   ? 0.25755 0.21720 0.27380 -0.00294 -0.05340 -0.00301 8   VAL A CG1 
58   C CG2 . VAL A 8   ? 0.47730 0.42293 0.49811 -0.00436 -0.05281 -0.00488 8   VAL A CG2 
59   N N   . ALA A 9   ? 0.35962 0.30823 0.34748 0.01145  -0.05899 -0.01192 9   ALA A N   
60   C CA  . ALA A 9   ? 0.35278 0.30647 0.33176 0.01788  -0.05944 -0.01056 9   ALA A CA  
61   C C   . ALA A 9   ? 0.34513 0.30695 0.32870 0.01302  -0.05922 -0.00970 9   ALA A C   
62   O O   . ALA A 9   ? 0.29095 0.25148 0.28207 0.00443  -0.05966 -0.01272 9   ALA A O   
63   C CB  . ALA A 9   ? 0.25489 0.19880 0.22204 0.02183  -0.06205 -0.01716 9   ALA A CB  
64   N N   . SER A 10  ? 0.30024 0.27085 0.27922 0.01869  -0.05847 -0.00545 10  SER A N   
65   C CA  . SER A 10  ? 0.29880 0.27753 0.27979 0.01577  -0.05854 -0.00483 10  SER A CA  
66   C C   . SER A 10  ? 0.29005 0.26690 0.25870 0.02207  -0.06021 -0.00736 10  SER A C   
67   O O   . SER A 10  ? 0.31626 0.29607 0.27750 0.03061  -0.05950 -0.00381 10  SER A O   
68   C CB  . SER A 10  ? 0.31241 0.30491 0.30020 0.01643  -0.05576 0.00312  10  SER A CB  
69   O OG  . SER A 10  ? 0.43073 0.42564 0.43100 0.00855  -0.05414 0.00465  10  SER A OG  
70   N N   . TYR A 11  ? 0.30820 0.28010 0.27465 0.01787  -0.06227 -0.01343 11  TYR A N   
71   C CA  . TYR A 11  ? 0.30635 0.27552 0.26124 0.02297  -0.06379 -0.01646 11  TYR A CA  
72   C C   . TYR A 11  ? 0.33853 0.31502 0.29618 0.01888  -0.06416 -0.01665 11  TYR A C   
73   O O   . TYR A 11  ? 0.34631 0.31668 0.30254 0.01429  -0.06602 -0.02267 11  TYR A O   
74   C CB  . TYR A 11  ? 0.36377 0.31854 0.31171 0.02233  -0.06605 -0.02442 11  TYR A CB  
75   C CG  . TYR A 11  ? 0.34219 0.28883 0.28768 0.02537  -0.06605 -0.02553 11  TYR A CG  
76   C CD1 . TYR A 11  ? 0.36035 0.30957 0.30017 0.03404  -0.06481 -0.02107 11  TYR A CD1 
77   C CD2 . TYR A 11  ? 0.31535 0.25171 0.26391 0.01965  -0.06738 -0.03130 11  TYR A CD2 
78   C CE1 . TYR A 11  ? 0.41179 0.35384 0.34914 0.03694  -0.06490 -0.02229 11  TYR A CE1 
79   C CE2 . TYR A 11  ? 0.33343 0.26263 0.27962 0.02252  -0.06749 -0.03255 11  TYR A CE2 
80   C CZ  . TYR A 11  ? 0.44100 0.37314 0.38153 0.03118  -0.06628 -0.02809 11  TYR A CZ  
81   O OH  . TYR A 11  ? 0.36373 0.28916 0.30193 0.03405  -0.06644 -0.02944 11  TYR A OH  
82   N N   . GLY A 12  A 0.26731 0.25697 0.22877 0.02055  -0.06239 -0.01019 11  GLY A N   
83   C CA  . GLY A 12  A 0.29756 0.29469 0.26098 0.02568  -0.06007 -0.00303 11  GLY A CA  
84   C C   . GLY A 12  A 0.24421 0.25343 0.21988 0.02037  -0.05805 0.00212  11  GLY A C   
85   O O   . GLY A 12  A 0.35066 0.36054 0.33470 0.01170  -0.05839 -0.00035 11  GLY A O   
86   N N   . VAL A 13  ? 0.27591 0.29471 0.25269 0.02543  -0.05582 0.00919  12  VAL A N   
87   C CA  . VAL A 13  ? 0.29863 0.33041 0.28597 0.02145  -0.05359 0.01459  12  VAL A CA  
88   C C   . VAL A 13  ? 0.36911 0.41121 0.35290 0.02454  -0.05369 0.01666  12  VAL A C   
89   O O   . VAL A 13  ? 0.31685 0.36168 0.29198 0.03325  -0.05343 0.01955  12  VAL A O   
90   C CB  . VAL A 13  ? 0.31517 0.35160 0.30623 0.02494  -0.05089 0.02123  12  VAL A CB  
91   C CG1 . VAL A 13  ? 0.31495 0.36401 0.31767 0.01975  -0.04839 0.02622  12  VAL A CG1 
92   C CG2 . VAL A 13  ? 0.28621 0.31167 0.27892 0.02337  -0.05094 0.01911  12  VAL A CG2 
93   N N   . ASN A 14  ? 0.34521 0.39293 0.33541 0.01751  -0.05410 0.01501  13  ASN A N   
94   C CA  . ASN A 14  ? 0.39778 0.45601 0.38571 0.01946  -0.05428 0.01666  13  ASN A CA  
95   C C   . ASN A 14  ? 0.38993 0.46280 0.38886 0.01569  -0.05182 0.02227  13  ASN A C   
96   O O   . ASN A 14  ? 0.37193 0.44630 0.38157 0.00682  -0.05117 0.02116  13  ASN A O   
97   C CB  . ASN A 14  ? 0.39907 0.45322 0.38543 0.01447  -0.05672 0.01026  13  ASN A CB  
98   C CG  . ASN A 14  ? 0.36445 0.40400 0.33987 0.01773  -0.05904 0.00428  13  ASN A CG  
99   O OD1 . ASN A 14  ? 0.44086 0.47933 0.40697 0.02229  -0.06032 0.00245  13  ASN A OD1 
100  N ND2 . ASN A 14  ? 0.29495 0.32316 0.27142 0.01534  -0.05950 0.00110  13  ASN A ND2 
101  N N   . LEU A 15  ? 0.36117 0.44480 0.35749 0.02227  -0.05036 0.02809  14  LEU A N   
102  C CA  . LEU A 15  ? 0.31986 0.41806 0.32589 0.01963  -0.04778 0.03380  14  LEU A CA  
103  C C   . LEU A 15  ? 0.48583 0.59617 0.48880 0.02306  -0.04795 0.03598  14  LEU A C   
104  O O   . LEU A 15  ? 0.47332 0.58253 0.46540 0.03139  -0.04888 0.03647  14  LEU A O   
105  C CB  . LEU A 15  ? 0.36097 0.46153 0.36822 0.02441  -0.04521 0.03989  14  LEU A CB  
106  C CG  . LEU A 15  ? 0.35407 0.47021 0.36877 0.02436  -0.04225 0.04674  14  LEU A CG  
107  C CD1 . LEU A 15  ? 0.37465 0.49625 0.40287 0.01372  -0.04084 0.04632  14  LEU A CD1 
108  C CD2 . LEU A 15  ? 0.32003 0.43617 0.33333 0.03050  -0.04005 0.05225  14  LEU A CD2 
109  N N   . TYR A 16  ? 0.41491 0.53687 0.42748 0.01656  -0.04699 0.03716  15  TYR A N   
110  C CA  . TYR A 16  ? 0.34387 0.47969 0.35525 0.01947  -0.04674 0.04007  15  TYR A CA  
111  C C   . TYR A 16  ? 0.33793 0.48790 0.36209 0.01332  -0.04418 0.04399  15  TYR A C   
112  O O   . TYR A 16  ? 0.40131 0.55045 0.43522 0.00394  -0.04377 0.04151  15  TYR A O   
113  C CB  . TYR A 16  ? 0.33186 0.46604 0.33869 0.01781  -0.04945 0.03479  15  TYR A CB  
114  C CG  . TYR A 16  ? 0.45400 0.60186 0.45792 0.02224  -0.04935 0.03784  15  TYR A CG  
115  C CD1 . TYR A 16  ? 0.49043 0.63757 0.48231 0.03252  -0.04992 0.03959  15  TYR A CD1 
116  C CD2 . TYR A 16  ? 0.52688 0.68864 0.54010 0.01623  -0.04857 0.03899  15  TYR A CD2 
117  C CE1 . TYR A 16  ? 0.52417 0.68385 0.51325 0.03688  -0.04976 0.04252  15  TYR A CE1 
118  C CE2 . TYR A 16  ? 0.50131 0.67617 0.51190 0.02050  -0.04850 0.04182  15  TYR A CE2 
119  C CZ  . TYR A 16  ? 0.51209 0.68575 0.51055 0.03093  -0.04912 0.04365  15  TYR A CZ  
120  O OH  . TYR A 16  ? 0.51106 0.69764 0.50670 0.03549  -0.04901 0.04655  15  TYR A OH  
121  N N   . GLN A 17  ? 0.38185 0.54469 0.40593 0.01850  -0.04235 0.04998  16  GLN A N   
122  C CA  . GLN A 17  ? 0.43085 0.60819 0.46650 0.01341  -0.03963 0.05407  16  GLN A CA  
123  C C   . GLN A 17  ? 0.46906 0.66158 0.50319 0.01675  -0.03962 0.05670  16  GLN A C   
124  O O   . GLN A 17  ? 0.43593 0.62837 0.45943 0.02529  -0.04091 0.05747  16  GLN A O   
125  C CB  . GLN A 17  ? 0.37123 0.54995 0.41045 0.01581  -0.03655 0.05975  16  GLN A CB  
126  C CG  . GLN A 17  ? 0.39982 0.57733 0.42843 0.02729  -0.03637 0.06377  16  GLN A CG  
127  C CD  . GLN A 17  ? 0.45707 0.63240 0.48828 0.02946  -0.03371 0.06838  16  GLN A CD  
128  O OE1 . GLN A 17  ? 0.46249 0.64304 0.50434 0.02346  -0.03111 0.07077  16  GLN A OE1 
129  N NE2 . GLN A 17  ? 0.51722 0.68470 0.53855 0.03806  -0.03425 0.06959  16  GLN A NE2 
130  N N   . SER A 18  ? 0.40357 0.60927 0.44851 0.00987  -0.03803 0.05798  17  SER A N   
131  C CA  . SER A 18  ? 0.35671 0.57825 0.40145 0.01228  -0.03793 0.06041  17  SER A CA  
132  C C   . SER A 18  ? 0.40639 0.63674 0.44795 0.02080  -0.03584 0.06728  17  SER A C   
133  O O   . SER A 18  ? 0.48598 0.72342 0.52047 0.02782  -0.03663 0.06912  17  SER A O   
134  C CB  . SER A 18  ? 0.23662 0.47014 0.29424 0.00217  -0.03668 0.05965  17  SER A CB  
135  O OG  . SER A 18  ? 0.40590 0.64361 0.47358 -0.00224 -0.03328 0.06321  17  SER A OG  
136  N N   . TYR A 19  ? 0.42521 0.65526 0.47180 0.02042  -0.03309 0.07120  18  TYR A N   
137  C CA  . TYR A 19  ? 0.47427 0.71230 0.51808 0.02832  -0.03097 0.07779  18  TYR A CA  
138  C C   . TYR A 19  ? 0.47954 0.70842 0.50931 0.03904  -0.03269 0.07813  18  TYR A C   
139  O O   . TYR A 19  ? 0.53725 0.75127 0.56218 0.04044  -0.03368 0.07575  18  TYR A O   
140  C CB  . TYR A 19  ? 0.55316 0.79112 0.60499 0.02546  -0.02763 0.08160  18  TYR A CB  
141  C CG  . TYR A 19  ? 0.69730 0.94578 0.74822 0.03228  -0.02505 0.08861  18  TYR A CG  
142  C CD1 . TYR A 19  ? 0.61564 0.85712 0.65793 0.04124  -0.02481 0.09163  18  TYR A CD1 
143  C CD2 . TYR A 19  ? 0.68360 0.94927 0.74227 0.02974  -0.02283 0.09209  18  TYR A CD2 
144  C CE1 . TYR A 19  ? 0.73272 0.98379 0.77412 0.04748  -0.02243 0.09804  18  TYR A CE1 
145  C CE2 . TYR A 19  ? 0.66832 0.94369 0.72620 0.03591  -0.02042 0.09844  18  TYR A CE2 
146  C CZ  . TYR A 19  ? 0.68071 0.94859 0.72992 0.04479  -0.02024 0.10144  18  TYR A CZ  
147  O OH  . TYR A 19  ? 0.87442 1.15185 0.92280 0.05091  -0.01784 0.10773  18  TYR A OH  
148  N N   . GLY A 20  ? 0.49803 0.73601 0.52132 0.04657  -0.03294 0.08103  19  GLY A N   
149  C CA  . GLY A 20  ? 0.66737 0.89785 0.67702 0.05667  -0.03454 0.08106  19  GLY A CA  
150  C C   . GLY A 20  ? 0.66850 0.90425 0.67180 0.05980  -0.03662 0.07916  19  GLY A C   
151  O O   . GLY A 20  ? 0.81923 1.06606 0.81903 0.06614  -0.03594 0.08316  19  GLY A O   
152  N N   . PRO A 21  ? 0.67387 0.90160 0.67537 0.05552  -0.03918 0.07299  20  PRO A N   
153  C CA  . PRO A 21  ? 0.64238 0.85575 0.64652 0.04880  -0.04028 0.06780  20  PRO A CA  
154  C C   . PRO A 21  ? 0.62432 0.82145 0.61791 0.05511  -0.04130 0.06625  20  PRO A C   
155  O O   . PRO A 21  ? 0.65550 0.85052 0.63790 0.06389  -0.04213 0.06695  20  PRO A O   
156  C CB  . PRO A 21  ? 0.38238 0.59530 0.38681 0.04353  -0.04272 0.06221  20  PRO A CB  
157  C CG  . PRO A 21  ? 0.56758 0.78747 0.56304 0.05142  -0.04364 0.06366  20  PRO A CG  
158  C CD  . PRO A 21  ? 0.54469 0.77805 0.54184 0.05677  -0.04110 0.07074  20  PRO A CD  
159  N N   . SER A 22  ? 0.60674 0.74904 0.72008 0.08716  0.09103  0.03255  21  SER A N   
160  C CA  . SER A 22  ? 0.46536 0.59660 0.56515 0.08807  0.08689  0.02845  21  SER A CA  
161  C C   . SER A 22  ? 0.53748 0.66175 0.63768 0.08251  0.07951  0.03025  21  SER A C   
162  O O   . SER A 22  ? 0.39831 0.52725 0.50635 0.07735  0.07862  0.03545  21  SER A O   
163  C CB  . SER A 22  ? 0.44436 0.57696 0.53111 0.08909  0.09131  0.02838  21  SER A CB  
164  O OG  . SER A 22  ? 0.56446 0.70566 0.65412 0.08485  0.09473  0.03446  21  SER A OG  
165  N N   . GLY A 23  ? 0.46737 0.58040 0.55900 0.08368  0.07417  0.02573  22  GLY A N   
166  C CA  . GLY A 23  ? 0.39157 0.49711 0.48169 0.07884  0.06704  0.02660  22  GLY A CA  
167  C C   . GLY A 23  ? 0.46174 0.55795 0.53617 0.07972  0.06458  0.02331  22  GLY A C   
168  O O   . GLY A 23  ? 0.48468 0.57930 0.54951 0.08444  0.06793  0.01977  22  GLY A O   
169  N N   . GLN A 24  ? 0.34075 0.43085 0.41271 0.07505  0.05862  0.02448  23  GLN A N   
170  C CA  . GLN A 24  ? 0.36768 0.44812 0.42524 0.07536  0.05536  0.02149  23  GLN A CA  
171  C C   . GLN A 24  ? 0.36014 0.43233 0.41904 0.07139  0.04718  0.02093  23  GLN A C   
172  O O   . GLN A 24  ? 0.31596 0.39153 0.38446 0.06643  0.04477  0.02486  23  GLN A O   
173  C CB  . GLN A 24  ? 0.28549 0.36902 0.33476 0.07326  0.05855  0.02466  23  GLN A CB  
174  C CG  . GLN A 24  ? 0.30690 0.38049 0.34046 0.07397  0.05568  0.02142  23  GLN A CG  
175  C CD  . GLN A 24  ? 0.39123 0.46722 0.41702 0.07098  0.05782  0.02497  23  GLN A CD  
176  O OE1 . GLN A 24  ? 0.38713 0.46659 0.40555 0.07360  0.06342  0.02470  23  GLN A OE1 
177  N NE2 . GLN A 24  ? 0.27436 0.34846 0.30169 0.06539  0.05320  0.02822  23  GLN A NE2 
178  N N   . TYR A 25  ? 0.37510 0.43664 0.42448 0.07362  0.04295  0.01594  24  TYR A N   
179  C CA  . TYR A 25  ? 0.34477 0.39757 0.39320 0.07008  0.03508  0.01484  24  TYR A CA  
180  C C   . TYR A 25  ? 0.39111 0.43499 0.42401 0.07065  0.03275  0.01219  24  TYR A C   
181  O O   . TYR A 25  ? 0.37233 0.41143 0.39566 0.07562  0.03420  0.00783  24  TYR A O   
182  C CB  . TYR A 25  ? 0.19731 0.24487 0.25093 0.07196  0.03093  0.01105  24  TYR A CB  
183  C CG  . TYR A 25  ? 0.33972 0.37995 0.39427 0.06741  0.02302  0.01068  24  TYR A CG  
184  C CD1 . TYR A 25  ? 0.26564 0.29504 0.30829 0.06785  0.01825  0.00696  24  TYR A CD1 
185  C CD2 . TYR A 25  ? 0.22822 0.27264 0.29547 0.06243  0.02037  0.01415  24  TYR A CD2 
186  C CE1 . TYR A 25  ? 0.31550 0.33861 0.35914 0.06351  0.01106  0.00663  24  TYR A CE1 
187  C CE2 . TYR A 25  ? 0.26250 0.30081 0.33079 0.05807  0.01328  0.01375  24  TYR A CE2 
188  C CZ  . TYR A 25  ? 0.31103 0.33879 0.36760 0.05861  0.00864  0.00997  24  TYR A CZ  
189  O OH  . TYR A 25  ? 0.28373 0.30582 0.34161 0.05416  0.00161  0.00953  24  TYR A OH  
190  N N   . THR A 26  ? 0.36662 0.40811 0.39717 0.06560  0.02896  0.01469  25  THR A N   
191  C CA  . THR A 26  ? 0.31501 0.34768 0.33140 0.06541  0.02600  0.01253  25  THR A CA  
192  C C   . THR A 26  ? 0.31226 0.33928 0.33033 0.06012  0.01852  0.01327  25  THR A C   
193  O O   . THR A 26  ? 0.32074 0.35219 0.35062 0.05604  0.01651  0.01634  25  THR A O   
194  C CB  . THR A 26  ? 0.38142 0.41820 0.39007 0.06484  0.03067  0.01537  25  THR A CB  
195  O OG1 . THR A 26  ? 0.31367 0.35804 0.33101 0.05962  0.03113  0.02113  25  THR A OG1 
196  C CG2 . THR A 26  ? 0.31503 0.35756 0.32095 0.06998  0.03827  0.01443  25  THR A CG2 
197  N N   . HIS A 27  ? 0.32981 0.34705 0.33588 0.06021  0.01444  0.01035  26  HIS A N   
198  C CA  . HIS A 27  ? 0.27232 0.28457 0.27742 0.05504  0.00803  0.01139  26  HIS A CA  
199  C C   . HIS A 27  ? 0.33380 0.34455 0.32783 0.05379  0.00906  0.01294  26  HIS A C   
200  O O   . HIS A 27  ? 0.34527 0.35408 0.32844 0.05760  0.01269  0.01108  26  HIS A O   
201  C CB  . HIS A 27  ? 0.28048 0.28181 0.28145 0.05556  0.00127  0.00663  26  HIS A CB  
202  C CG  . HIS A 27  ? 0.30950 0.31180 0.32243 0.05471  -0.00159 0.00590  26  HIS A CG  
203  N ND1 . HIS A 27  ? 0.27814 0.27233 0.29093 0.05307  -0.00859 0.00296  26  HIS A ND1 
204  C CD2 . HIS A 27  ? 0.31367 0.32408 0.33903 0.05508  0.00151  0.00779  26  HIS A CD2 
205  C CE1 . HIS A 27  ? 0.32505 0.32229 0.34951 0.05236  -0.00970 0.00310  26  HIS A CE1 
206  N NE2 . HIS A 27  ? 0.25837 0.26530 0.29066 0.05361  -0.00368 0.00600  26  HIS A NE2 
207  N N   . GLU A 28  ? 0.32491 0.33672 0.32188 0.04835  0.00582  0.01636  27  GLU A N   
208  C CA  . GLU A 28  ? 0.29629 0.30668 0.28378 0.04636  0.00601  0.01832  27  GLU A CA  
209  C C   . GLU A 28  ? 0.29789 0.30054 0.28274 0.04223  -0.00167 0.01759  27  GLU A C   
210  O O   . GLU A 28  ? 0.34450 0.34778 0.33931 0.03886  -0.00600 0.01824  27  GLU A O   
211  C CB  . GLU A 28  ? 0.32548 0.34663 0.31950 0.04360  0.01058  0.02414  27  GLU A CB  
212  C CG  . GLU A 28  ? 0.31841 0.34814 0.31516 0.04741  0.01857  0.02523  27  GLU A CG  
213  C CD  . GLU A 28  ? 0.34479 0.38517 0.34828 0.04435  0.02279  0.03118  27  GLU A CD  
214  O OE1 . GLU A 28  ? 0.35382 0.39504 0.36056 0.03929  0.01941  0.03450  27  GLU A OE1 
215  O OE2 . GLU A 28  ? 0.44319 0.49118 0.44882 0.04703  0.02946  0.03248  27  GLU A OE2 
216  N N   . PHE A 29  ? 0.35644 0.35175 0.32783 0.04251  -0.00341 0.01608  28  PHE A N   
217  C CA  . PHE A 29  ? 0.30406 0.29243 0.27207 0.03844  -0.01037 0.01575  28  PHE A CA  
218  C C   . PHE A 29  ? 0.28470 0.27324 0.24431 0.03642  -0.00931 0.01859  28  PHE A C   
219  O O   . PHE A 29  ? 0.33121 0.31697 0.27892 0.03948  -0.00609 0.01735  28  PHE A O   
220  C CB  . PHE A 29  ? 0.28349 0.26026 0.24271 0.04063  -0.01533 0.01024  28  PHE A CB  
221  C CG  . PHE A 29  ? 0.38013 0.35032 0.33794 0.03630  -0.02284 0.00971  28  PHE A CG  
222  C CD1 . PHE A 29  ? 0.30204 0.27302 0.27098 0.03293  -0.02760 0.00977  28  PHE A CD1 
223  C CD2 . PHE A 29  ? 0.39058 0.35416 0.33623 0.03541  -0.02512 0.00925  28  PHE A CD2 
224  C CE1 . PHE A 29  ? 0.42352 0.38897 0.39158 0.02887  -0.03446 0.00914  28  PHE A CE1 
225  C CE2 . PHE A 29  ? 0.32026 0.27800 0.26501 0.03142  -0.03213 0.00870  28  PHE A CE2 
226  C CZ  . PHE A 29  ? 0.34028 0.29911 0.29635 0.02820  -0.03675 0.00858  28  PHE A CZ  
227  N N   . ASP A 30  ? 0.24371 0.23546 0.20954 0.03119  -0.01213 0.02234  29  ASP A N   
228  C CA  . ASP A 30  ? 0.30814 0.30110 0.26797 0.02855  -0.01140 0.02579  29  ASP A CA  
229  C C   . ASP A 30  ? 0.36956 0.36917 0.32565 0.03117  -0.00353 0.02806  29  ASP A C   
230  O O   . ASP A 30  ? 0.36956 0.36640 0.31383 0.03173  -0.00194 0.02837  29  ASP A O   
231  C CB  . ASP A 30  ? 0.32138 0.30331 0.26771 0.02808  -0.01637 0.02310  29  ASP A CB  
232  C CG  . ASP A 30  ? 0.39709 0.37395 0.34776 0.02414  -0.02430 0.02206  29  ASP A CG  
233  O OD1 . ASP A 30  ? 0.46743 0.45040 0.43131 0.02076  -0.02580 0.02453  29  ASP A OD1 
234  O OD2 . ASP A 30  ? 0.40861 0.37556 0.34962 0.02437  -0.02902 0.01872  29  ASP A OD2 
235  N N   . GLY A 31  ? 0.26907 0.27754 0.23528 0.03270  0.00142  0.02961  30  GLY A N   
236  C CA  . GLY A 31  ? 0.30409 0.32060 0.26920 0.03459  0.00900  0.03231  30  GLY A CA  
237  C C   . GLY A 31  ? 0.37807 0.39227 0.33326 0.04035  0.01372  0.02869  30  GLY A C   
238  O O   . GLY A 31  ? 0.45122 0.47199 0.40429 0.04200  0.02020  0.03065  30  GLY A O   
239  N N   . ASP A 32  ? 0.32407 0.32936 0.27313 0.04343  0.01072  0.02346  31  ASP A N   
240  C CA  . ASP A 32  ? 0.38014 0.38277 0.31989 0.04913  0.01483  0.01955  31  ASP A CA  
241  C C   . ASP A 32  ? 0.32880 0.33222 0.27640 0.05274  0.01543  0.01641  31  ASP A C   
242  O O   . ASP A 32  ? 0.35218 0.35333 0.30791 0.05102  0.01049  0.01557  31  ASP A O   
243  C CB  . ASP A 32  ? 0.42424 0.41512 0.34873 0.05029  0.01106  0.01571  31  ASP A CB  
244  C CG  . ASP A 32  ? 0.40454 0.39442 0.31902 0.04769  0.01156  0.01838  31  ASP A CG  
245  O OD1 . ASP A 32  ? 0.46306 0.46006 0.37571 0.04828  0.01773  0.02105  31  ASP A OD1 
246  O OD2 . ASP A 32  ? 0.45572 0.43772 0.36424 0.04494  0.00567  0.01783  31  ASP A OD2 
247  N N   . GLU A 33  ? 0.32648 0.33301 0.27136 0.05772  0.02138  0.01453  32  GLU A N   
248  C CA  . GLU A 33  ? 0.39799 0.40597 0.35032 0.06155  0.02260  0.01164  32  GLU A CA  
249  C C   . GLU A 33  ? 0.37983 0.37636 0.32461 0.06446  0.01784  0.00585  32  GLU A C   
250  O O   . GLU A 33  ? 0.46119 0.45179 0.39288 0.06765  0.01882  0.00266  32  GLU A O   
251  C CB  . GLU A 33  ? 0.44435 0.46013 0.39657 0.06589  0.03074  0.01164  32  GLU A CB  
252  C CG  . GLU A 33  ? 0.44258 0.45990 0.40171 0.07042  0.03243  0.00840  32  GLU A CG  
253  C CD  . GLU A 33  ? 0.57096 0.59680 0.53044 0.07446  0.04063  0.00860  32  GLU A CD  
254  O OE1 . GLU A 33  ? 0.52301 0.55354 0.47713 0.07348  0.04495  0.01135  32  GLU A OE1 
255  O OE2 . GLU A 33  ? 0.50486 0.53276 0.46994 0.07851  0.04268  0.00599  32  GLU A OE2 
256  N N   . GLN A 34  ? 0.32558 0.31900 0.27846 0.06321  0.01261  0.00453  33  GLN A N   
257  C CA  . GLN A 34  ? 0.32041 0.30333 0.26723 0.06594  0.00797  -0.00091 33  GLN A CA  
258  C C   . GLN A 34  ? 0.38605 0.36983 0.33330 0.07198  0.01178  -0.00455 33  GLN A C   
259  O O   . GLN A 34  ? 0.42792 0.40401 0.36458 0.07605  0.01113  -0.00917 33  GLN A O   
260  C CB  . GLN A 34  ? 0.29589 0.27528 0.25106 0.06213  0.00090  -0.00100 33  GLN A CB  
261  C CG  . GLN A 34  ? 0.33318 0.30916 0.28610 0.05665  -0.00422 0.00119  33  GLN A CG  
262  C CD  . GLN A 34  ? 0.34108 0.31491 0.30349 0.05276  -0.01077 0.00112  33  GLN A CD  
263  O OE1 . GLN A 34  ? 0.36629 0.34728 0.34199 0.05098  -0.01005 0.00346  33  GLN A OE1 
264  N NE2 . GLN A 34  ? 0.39323 0.35726 0.34881 0.05137  -0.01718 -0.00162 33  GLN A NE2 
265  N N   . PHE A 35  ? 0.41758 0.41052 0.37703 0.07268  0.01561  -0.00262 34  PHE A N   
266  C CA  . PHE A 35  ? 0.37207 0.36703 0.33329 0.07839  0.01957  -0.00578 34  PHE A CA  
267  C C   . PHE A 35  ? 0.40901 0.41609 0.38387 0.07789  0.02456  -0.00201 34  PHE A C   
268  O O   . PHE A 35  ? 0.45694 0.46943 0.44124 0.07301  0.02354  0.00249  34  PHE A O   
269  C CB  . PHE A 35  ? 0.40959 0.39632 0.37197 0.08043  0.01418  -0.01041 34  PHE A CB  
270  C CG  . PHE A 35  ? 0.29217 0.28063 0.26807 0.07647  0.00977  -0.00852 34  PHE A CG  
271  C CD1 . PHE A 35  ? 0.36599 0.36164 0.35449 0.07758  0.01230  -0.00757 34  PHE A CD1 
272  C CD2 . PHE A 35  ? 0.32013 0.30298 0.29608 0.07160  0.00303  -0.00785 34  PHE A CD2 
273  C CE1 . PHE A 35  ? 0.39358 0.39076 0.39431 0.07373  0.00822  -0.00584 34  PHE A CE1 
274  C CE2 . PHE A 35  ? 0.35481 0.33941 0.34302 0.06779  -0.00101 -0.00630 34  PHE A CE2 
275  C CZ  . PHE A 35  ? 0.33456 0.32630 0.33509 0.06879  0.00161  -0.00524 34  PHE A CZ  
276  N N   . TYR A 36  ? 0.38960 0.40085 0.36549 0.08304  0.02990  -0.00401 35  TYR A N   
277  C CA  . TYR A 36  ? 0.31737 0.33882 0.30696 0.08350  0.03395  -0.00158 35  TYR A CA  
278  C C   . TYR A 36  ? 0.34122 0.35966 0.33435 0.08819  0.03303  -0.00614 35  TYR A C   
279  O O   . TYR A 36  ? 0.39982 0.41020 0.38320 0.09225  0.03160  -0.01115 35  TYR A O   
280  C CB  . TYR A 36  ? 0.30251 0.33403 0.29148 0.08510  0.04219  0.00099  35  TYR A CB  
281  C CG  . TYR A 36  ? 0.46426 0.49492 0.44416 0.09151  0.04694  -0.00339 35  TYR A CG  
282  C CD1 . TYR A 36  ? 0.38073 0.41546 0.36704 0.09628  0.05032  -0.00583 35  TYR A CD1 
283  C CD2 . TYR A 36  ? 0.40685 0.43286 0.37192 0.09274  0.04808  -0.00510 35  TYR A CD2 
284  C CE1 . TYR A 36  ? 0.47220 0.50646 0.45052 0.10222  0.05466  -0.01006 35  TYR A CE1 
285  C CE2 . TYR A 36  ? 0.32703 0.35256 0.28382 0.09852  0.05253  -0.00922 35  TYR A CE2 
286  C CZ  . TYR A 36  ? 0.57741 0.60716 0.54092 0.10330  0.05582  -0.01178 35  TYR A CZ  
287  O OH  . TYR A 36  ? 0.58146 0.61090 0.53687 0.10913  0.06020  -0.01613 35  TYR A OH  
288  N N   . VAL A 37  ? 0.39896 0.42362 0.40605 0.08754  0.03360  -0.00437 36  VAL A N   
289  C CA  . VAL A 37  ? 0.44539 0.46877 0.45731 0.09205  0.03346  -0.00819 36  VAL A CA  
290  C C   . VAL A 37  ? 0.51214 0.54521 0.52770 0.09617  0.04141  -0.00776 36  VAL A C   
291  O O   . VAL A 37  ? 0.40870 0.45189 0.43327 0.09384  0.04539  -0.00309 36  VAL A O   
292  C CB  . VAL A 37  ? 0.41949 0.44288 0.44439 0.08882  0.02862  -0.00693 36  VAL A CB  
293  C CG1 . VAL A 37  ? 0.44084 0.46523 0.47229 0.09351  0.02976  -0.01002 36  VAL A CG1 
294  C CG2 . VAL A 37  ? 0.35059 0.36331 0.37094 0.08574  0.02051  -0.00871 36  VAL A CG2 
295  N N   . ASP A 38  ? 0.51330 0.54338 0.52180 0.10227  0.04369  -0.01269 37  ASP A N   
296  C CA  . ASP A 38  ? 0.49801 0.53680 0.51055 0.10681  0.05082  -0.01323 37  ASP A CA  
297  C C   . ASP A 38  ? 0.44701 0.48970 0.47430 0.10718  0.04993  -0.01277 37  ASP A C   
298  O O   . ASP A 38  ? 0.44443 0.48072 0.47279 0.10998  0.04613  -0.01689 37  ASP A O   
299  C CB  . ASP A 38  ? 0.53261 0.56642 0.53370 0.11326  0.05281  -0.01914 37  ASP A CB  
300  C CG  . ASP A 38  ? 0.58628 0.62972 0.58947 0.11769  0.06088  -0.01960 37  ASP A CG  
301  O OD1 . ASP A 38  ? 0.58729 0.63809 0.60304 0.11848  0.06315  -0.01827 37  ASP A OD1 
302  O OD2 . ASP A 38  ? 0.69718 0.74103 0.68942 0.12020  0.06500  -0.02124 37  ASP A OD2 
303  N N   . LEU A 39  ? 0.42717 0.48020 0.46587 0.10421  0.05326  -0.00768 38  LEU A N   
304  C CA  . LEU A 39  ? 0.50374 0.56039 0.55693 0.10372  0.05197  -0.00666 38  LEU A CA  
305  C C   . LEU A 39  ? 0.45870 0.51779 0.51468 0.11028  0.05560  -0.01060 38  LEU A C   
306  O O   . LEU A 39  ? 0.61815 0.67429 0.68115 0.11167  0.05221  -0.01275 38  LEU A O   
307  C CB  . LEU A 39  ? 0.34276 0.40988 0.40707 0.09884  0.05471  -0.00010 38  LEU A CB  
308  C CG  . LEU A 39  ? 0.38355 0.44811 0.44669 0.09216  0.05033  0.00368  38  LEU A CG  
309  C CD1 . LEU A 39  ? 0.37638 0.45184 0.44848 0.08783  0.05404  0.01015  38  LEU A CD1 
310  C CD2 . LEU A 39  ? 0.27658 0.33318 0.34390 0.08930  0.04229  0.00248  38  LEU A CD2 
311  N N   . GLY A 40  ? 0.55843 0.62271 0.60877 0.11435  0.06231  -0.01177 39  GLY A N   
312  C CA  . GLY A 40  ? 0.51961 0.58614 0.57198 0.12090  0.06580  -0.01601 39  GLY A CA  
313  C C   . GLY A 40  ? 0.60034 0.65548 0.64472 0.12527  0.06126  -0.02255 39  GLY A C   
314  O O   . GLY A 40  ? 0.58613 0.63977 0.63653 0.12880  0.05983  -0.02570 39  GLY A O   
315  N N   . ARG A 41  ? 0.53269 0.57949 0.56341 0.12508  0.05876  -0.02466 40  ARG A N   
316  C CA  . ARG A 41  ? 0.55654 0.59213 0.57828 0.12924  0.05451  -0.03088 40  ARG A CA  
317  C C   . ARG A 41  ? 0.68528 0.71081 0.70807 0.12586  0.04573  -0.03140 40  ARG A C   
318  O O   . ARG A 41  ? 0.64842 0.66434 0.66517 0.12908  0.04147  -0.03645 40  ARG A O   
319  C CB  . ARG A 41  ? 0.63308 0.66461 0.63878 0.13118  0.05653  -0.03328 40  ARG A CB  
320  C CG  . ARG A 41  ? 0.62282 0.66388 0.62606 0.13462  0.06522  -0.03329 40  ARG A CG  
321  C CD  . ARG A 41  ? 0.66040 0.69838 0.64809 0.13495  0.06729  -0.03433 40  ARG A CD  
322  N NE  . ARG A 41  ? 0.90753 0.95576 0.89363 0.13726  0.07576  -0.03359 40  ARG A NE  
323  C CZ  . ARG A 41  ? 0.91670 0.97399 0.90558 0.13332  0.08009  -0.02811 40  ARG A CZ  
324  N NH1 . ARG A 41  ? 0.88775 0.94522 0.88094 0.12692  0.07685  -0.02285 40  ARG A NH1 
325  N NH2 . ARG A 41  ? 1.03274 1.09925 1.02005 0.13583  0.08781  -0.02797 40  ARG A NH2 
326  N N   . LYS A 42  ? 0.63642 0.66397 0.66664 0.11945  0.04290  -0.02640 41  LYS A N   
327  C CA  . LYS A 42  ? 0.40018 0.41910 0.43207 0.11558  0.03467  -0.02655 41  LYS A CA  
328  C C   . LYS A 42  ? 0.44879 0.45620 0.46607 0.11587  0.03021  -0.02995 41  LYS A C   
329  O O   . LYS A 42  ? 0.56521 0.56302 0.57965 0.11699  0.02429  -0.03372 41  LYS A O   
330  C CB  . LYS A 42  ? 0.55776 0.57437 0.59870 0.11772  0.03135  -0.02908 41  LYS A CB  
331  N N   . GLU A 43  ? 0.48116 0.48946 0.48898 0.11474  0.03299  -0.02850 42  GLU A N   
332  C CA  . GLU A 43  ? 0.50208 0.50008 0.49538 0.11501  0.02944  -0.03142 42  GLU A CA  
333  C C   . GLU A 43  ? 0.60621 0.60459 0.59624 0.10897  0.02820  -0.02703 42  GLU A C   
334  O O   . GLU A 43  ? 0.40269 0.41029 0.39669 0.10655  0.03292  -0.02250 42  GLU A O   
335  C CB  . GLU A 43  ? 0.52056 0.51770 0.50240 0.12108  0.03431  -0.03545 42  GLU A CB  
336  N N   . THR A 44  ? 0.52219 0.51045 0.50500 0.10654  0.02168  -0.02844 43  THR A N   
337  C CA  . THR A 44  ? 0.46307 0.45007 0.44139 0.10113  0.01968  -0.02503 43  THR A CA  
338  C C   . THR A 44  ? 0.50568 0.48908 0.46869 0.10342  0.02222  -0.02684 43  THR A C   
339  O O   . THR A 44  ? 0.48228 0.45671 0.43507 0.10708  0.01998  -0.03173 43  THR A O   
340  C CB  . THR A 44  ? 0.42136 0.39955 0.40013 0.09712  0.01121  -0.02564 43  THR A CB  
341  O OG1 . THR A 44  ? 0.44318 0.42561 0.43650 0.09423  0.00909  -0.02338 43  THR A OG1 
342  C CG2 . THR A 44  ? 0.42328 0.39937 0.39630 0.09200  0.00889  -0.02276 43  THR A CG2 
343  N N   . VAL A 45  ? 0.49344 0.48359 0.45469 0.10112  0.02671  -0.02287 44  VAL A N   
344  C CA  . VAL A 45  ? 0.46653 0.45468 0.41374 0.10295  0.02992  -0.02400 44  VAL A CA  
345  C C   . VAL A 45  ? 0.46424 0.44841 0.40581 0.09740  0.02611  -0.02112 44  VAL A C   
346  O O   . VAL A 45  ? 0.50794 0.49916 0.45443 0.09308  0.02796  -0.01601 44  VAL A O   
347  C CB  . VAL A 45  ? 0.53646 0.53564 0.48499 0.10507  0.03854  -0.02202 44  VAL A CB  
348  C CG1 . VAL A 45  ? 0.38299 0.37973 0.31638 0.10658  0.04159  -0.02324 44  VAL A CG1 
349  C CG2 . VAL A 45  ? 0.51181 0.51522 0.46674 0.11060  0.04217  -0.02500 44  VAL A CG2 
350  N N   . TRP A 46  ? 0.42586 0.39869 0.35686 0.09757  0.02077  -0.02441 45  TRP A N   
351  C CA  . TRP A 46  ? 0.48745 0.45550 0.41231 0.09263  0.01667  -0.02225 45  TRP A CA  
352  C C   . TRP A 46  ? 0.44327 0.41366 0.35770 0.09269  0.02140  -0.02071 45  TRP A C   
353  O O   . TRP A 46  ? 0.51412 0.48332 0.41933 0.09739  0.02532  -0.02383 45  TRP A O   
354  C CB  . TRP A 46  ? 0.48490 0.43994 0.40160 0.09299  0.00947  -0.02646 45  TRP A CB  
355  C CG  . TRP A 46  ? 0.51045 0.46287 0.43687 0.09240  0.00443  -0.02784 45  TRP A CG  
356  C CD1 . TRP A 46  ? 0.47318 0.42258 0.40128 0.09698  0.00381  -0.03203 45  TRP A CD1 
357  C CD2 . TRP A 46  ? 0.52012 0.47291 0.45613 0.08676  -0.00075 -0.02501 45  TRP A CD2 
358  N NE1 . TRP A 46  ? 0.53357 0.48121 0.47144 0.09437  -0.00154 -0.03186 45  TRP A NE1 
359  C CE2 . TRP A 46  ? 0.52486 0.47468 0.46774 0.08807  -0.00432 -0.02764 45  TRP A CE2 
360  C CE3 . TRP A 46  ? 0.36857 0.32389 0.30801 0.08070  -0.00284 -0.02062 45  TRP A CE3 
361  C CZ2 . TRP A 46  ? 0.45064 0.40013 0.40344 0.08337  -0.00970 -0.02599 45  TRP A CZ2 
362  C CZ3 . TRP A 46  ? 0.37693 0.33202 0.32642 0.07625  -0.00815 -0.01916 45  TRP A CZ3 
363  C CH2 . TRP A 46  ? 0.44766 0.40000 0.40371 0.07752  -0.01142 -0.02181 45  TRP A CH2 
364  N N   . SER A 47  ? 0.50858 0.48233 0.42450 0.08732  0.02090  -0.01589 46  SER A N   
365  C CA  . SER A 47  ? 0.47177 0.44846 0.37885 0.08643  0.02514  -0.01359 46  SER A CA  
366  C C   . SER A 47  ? 0.53830 0.50486 0.43181 0.08465  0.02067  -0.01480 46  SER A C   
367  O O   . SER A 47  ? 0.67844 0.64540 0.56183 0.08475  0.02392  -0.01400 46  SER A O   
368  C CB  . SER A 47  ? 0.48721 0.47424 0.40388 0.08167  0.02769  -0.00729 46  SER A CB  
369  O OG  . SER A 47  ? 0.77358 0.77090 0.70082 0.08379  0.03332  -0.00600 46  SER A OG  
370  N N   . LEU A 48  ? 0.56989 0.52750 0.46286 0.08291  0.01333  -0.01665 47  LEU A N   
371  C CA  . LEU A 48  ? 0.51446 0.46170 0.39470 0.08145  0.00856  -0.01823 47  LEU A CA  
372  C C   . LEU A 48  ? 0.56913 0.50607 0.44324 0.08541  0.00465  -0.02410 47  LEU A C   
373  O O   . LEU A 48  ? 0.64989 0.58511 0.53242 0.08539  0.00086  -0.02550 47  LEU A O   
374  C CB  . LEU A 48  ? 0.57204 0.51795 0.45718 0.07505  0.00280  -0.01478 47  LEU A CB  
375  C CG  . LEU A 48  ? 0.63028 0.56705 0.50354 0.07242  -0.00198 -0.01519 47  LEU A CG  
376  C CD1 . LEU A 48  ? 0.55208 0.49130 0.41552 0.07228  0.00272  -0.01312 47  LEU A CD1 
377  C CD2 . LEU A 48  ? 0.43885 0.37503 0.31971 0.06641  -0.00800 -0.01228 47  LEU A CD2 
378  N N   . PRO A 49  ? 0.55737 0.48724 0.41705 0.08875  0.00531  -0.02764 48  PRO A N   
379  C CA  . PRO A 49  ? 0.57707 0.49805 0.43121 0.09338  0.00254  -0.03344 48  PRO A CA  
380  C C   . PRO A 49  ? 0.56913 0.48152 0.42554 0.09097  -0.00581 -0.03498 48  PRO A C   
381  O O   . PRO A 49  ? 0.60399 0.51220 0.46257 0.09401  -0.00817 -0.03869 48  PRO A O   
382  C CB  . PRO A 49  ? 0.64205 0.55681 0.47931 0.09601  0.00424  -0.03603 48  PRO A CB  
383  C CG  . PRO A 49  ? 0.64358 0.56697 0.47949 0.09432  0.01029  -0.03194 48  PRO A CG  
384  C CD  . PRO A 49  ? 0.57584 0.50548 0.42343 0.08846  0.00862  -0.02653 48  PRO A CD  
385  N N   . VAL A 50  ? 0.63649 0.54614 0.49253 0.08555  -0.01046 -0.03233 49  VAL A N   
386  C CA  . VAL A 50  ? 0.56822 0.46988 0.42616 0.08304  -0.01844 -0.03391 49  VAL A CA  
387  C C   . VAL A 50  ? 0.50967 0.41642 0.38320 0.08165  -0.02002 -0.03291 49  VAL A C   
388  O O   . VAL A 50  ? 0.67355 0.57392 0.54922 0.08104  -0.02591 -0.03534 49  VAL A O   
389  C CB  . VAL A 50  ? 0.63687 0.53509 0.49106 0.07753  -0.02282 -0.03129 49  VAL A CB  
390  C CG1 . VAL A 50  ? 0.56182 0.47035 0.42726 0.07276  -0.02093 -0.02560 49  VAL A CG1 
391  C CG2 . VAL A 50  ? 0.45148 0.34016 0.30499 0.07541  -0.03113 -0.03373 49  VAL A CG2 
392  N N   . LEU A 51  ? 0.56015 0.47821 0.44451 0.08109  -0.01490 -0.02940 50  LEU A N   
393  C CA  . LEU A 51  ? 0.52514 0.44848 0.42448 0.07972  -0.01604 -0.02824 50  LEU A CA  
394  C C   . LEU A 51  ? 0.55388 0.47627 0.45543 0.08509  -0.01468 -0.03215 50  LEU A C   
395  O O   . LEU A 51  ? 0.58253 0.50752 0.49555 0.08421  -0.01652 -0.03190 50  LEU A O   
396  C CB  . LEU A 51  ? 0.52631 0.46213 0.43659 0.07695  -0.01119 -0.02283 50  LEU A CB  
397  C CG  . LEU A 51  ? 0.58426 0.52239 0.49330 0.07172  -0.01188 -0.01849 50  LEU A CG  
398  C CD1 . LEU A 51  ? 0.41514 0.36565 0.33657 0.06905  -0.00752 -0.01326 50  LEU A CD1 
399  C CD2 . LEU A 51  ? 0.49582 0.42671 0.40486 0.06721  -0.01991 -0.01882 50  LEU A CD2 
400  N N   . ARG A 52  ? 0.51297 0.43162 0.40388 0.09055  -0.01166 -0.03583 51  ARG A N   
401  C CA  . ARG A 52  ? 0.50402 0.42191 0.39705 0.09594  -0.01029 -0.03970 51  ARG A CA  
402  C C   . ARG A 52  ? 0.61284 0.52123 0.50612 0.09599  -0.01763 -0.04326 51  ARG A C   
403  O O   . ARG A 52  ? 0.61390 0.52205 0.51209 0.09936  -0.01773 -0.04588 51  ARG A O   
404  C CB  . ARG A 52  ? 0.55335 0.46944 0.43443 0.10173  -0.00539 -0.04299 51  ARG A CB  
405  C CG  . ARG A 52  ? 0.60234 0.52967 0.48587 0.10277  0.00286  -0.04002 51  ARG A CG  
406  C CD  . ARG A 52  ? 0.78347 0.70868 0.65270 0.10633  0.00713  -0.04214 51  ARG A CD  
407  N NE  . ARG A 52  ? 0.79245 0.72869 0.66398 0.10605  0.01458  -0.03857 51  ARG A NE  
408  C CZ  . ARG A 52  ? 0.84897 0.78612 0.70962 0.10792  0.01929  -0.03902 51  ARG A CZ  
409  N NH1 . ARG A 52  ? 0.74357 0.67125 0.59001 0.11036  0.01756  -0.04291 51  ARG A NH1 
410  N NH2 . ARG A 52  ? 0.91956 0.86739 0.78357 0.10718  0.02587  -0.03544 51  ARG A NH2 
411  N N   . GLN A 53  ? 0.59682 0.49747 0.48512 0.09222  -0.02390 -0.04340 52  GLN A N   
412  C CA  . GLN A 53  ? 0.53438 0.42671 0.42393 0.09143  -0.03114 -0.04630 52  GLN A CA  
413  C C   . GLN A 53  ? 0.61570 0.51381 0.52100 0.08829  -0.03297 -0.04409 52  GLN A C   
414  O O   . GLN A 53  ? 0.65599 0.54878 0.56413 0.08854  -0.03787 -0.04670 52  GLN A O   
415  C CB  . GLN A 53  ? 0.64637 0.53019 0.52796 0.08756  -0.03726 -0.04654 52  GLN A CB  
416  C CG  . GLN A 53  ? 0.64985 0.53921 0.53828 0.08111  -0.03834 -0.04159 52  GLN A CG  
417  C CD  . GLN A 53  ? 0.53391 0.41507 0.41335 0.07779  -0.04378 -0.04197 52  GLN A CD  
418  O OE1 . GLN A 53  ? 0.77037 0.64285 0.64684 0.07704  -0.05011 -0.04487 52  GLN A OE1 
419  N NE2 . GLN A 53  ? 0.64749 0.53122 0.52236 0.07575  -0.04144 -0.03909 52  GLN A NE2 
420  N N   . PHE A 54  ? 0.57898 0.48767 0.49436 0.08521  -0.02930 -0.03931 53  PHE A N   
421  C CA  . PHE A 54  ? 0.55496 0.46975 0.48553 0.08196  -0.03070 -0.03687 53  PHE A CA  
422  C C   . PHE A 54  ? 0.58977 0.51025 0.52758 0.08633  -0.02620 -0.03773 53  PHE A C   
423  O O   . PHE A 54  ? 0.55394 0.47651 0.48665 0.09131  -0.02066 -0.03912 53  PHE A O   
424  C CB  . PHE A 54  ? 0.44920 0.37274 0.38763 0.07655  -0.02901 -0.03128 53  PHE A CB  
425  C CG  . PHE A 54  ? 0.50928 0.42788 0.44206 0.07194  -0.03369 -0.03025 53  PHE A CG  
426  C CD1 . PHE A 54  ? 0.43430 0.34333 0.36341 0.07020  -0.04102 -0.03309 53  PHE A CD1 
427  C CD2 . PHE A 54  ? 0.43789 0.36126 0.36887 0.06935  -0.03089 -0.02651 53  PHE A CD2 
428  C CE1 . PHE A 54  ? 0.43595 0.34050 0.36010 0.06603  -0.04542 -0.03231 53  PHE A CE1 
429  C CE2 . PHE A 54  ? 0.43869 0.35733 0.36461 0.06518  -0.03543 -0.02568 53  PHE A CE2 
430  C CZ  . PHE A 54  ? 0.50459 0.41388 0.42721 0.06358  -0.04268 -0.02865 53  PHE A CZ  
431  N N   . ARG A 55  ? 0.57811 0.50111 0.52803 0.08430  -0.02877 -0.03699 54  ARG A N   
432  C CA  . ARG A 55  ? 0.51395 0.44303 0.47309 0.08753  -0.02513 -0.03721 54  ARG A CA  
433  C C   . ARG A 55  ? 0.51797 0.45727 0.49196 0.08283  -0.02376 -0.03214 54  ARG A C   
434  O O   . ARG A 55  ? 0.68364 0.62205 0.66314 0.07740  -0.02874 -0.03038 54  ARG A O   
435  C CB  . ARG A 55  ? 0.47953 0.40088 0.43893 0.08996  -0.03004 -0.04162 54  ARG A CB  
436  N N   . PHE A 56  ? 0.45650 0.40564 0.43685 0.08484  -0.01699 -0.02983 56  PHE A N   
437  C CA  . PHE A 56  ? 0.49641 0.45581 0.49104 0.08085  -0.01504 -0.02495 56  PHE A CA  
438  C C   . PHE A 56  ? 0.48325 0.44866 0.48660 0.08470  -0.01096 -0.02540 56  PHE A C   
439  O O   . PHE A 56  ? 0.49627 0.46663 0.49739 0.08900  -0.00455 -0.02559 56  PHE A O   
440  C CB  . PHE A 56  ? 0.45407 0.42087 0.44819 0.07827  -0.01056 -0.02044 56  PHE A CB  
441  C CG  . PHE A 56  ? 0.36477 0.34213 0.37321 0.07419  -0.00848 -0.01532 56  PHE A CG  
442  C CD1 . PHE A 56  ? 0.38911 0.36678 0.40424 0.06794  -0.01328 -0.01268 56  PHE A CD1 
443  C CD2 . PHE A 56  ? 0.29786 0.28492 0.31320 0.07661  -0.00175 -0.01324 56  PHE A CD2 
444  C CE1 . PHE A 56  ? 0.30481 0.29214 0.33313 0.06416  -0.01144 -0.00801 56  PHE A CE1 
445  C CE2 . PHE A 56  ? 0.29022 0.28688 0.31870 0.07286  0.00012  -0.00846 56  PHE A CE2 
446  C CZ  . PHE A 56  ? 0.36711 0.36385 0.40208 0.06662  -0.00474 -0.00581 56  PHE A CZ  
447  N N   . ASP A 57  ? 0.54318 0.50822 0.55642 0.08305  -0.01472 -0.02561 57  ASP A N   
448  C CA  . ASP A 57  ? 0.56980 0.53976 0.59235 0.08622  -0.01196 -0.02610 57  ASP A CA  
449  C C   . ASP A 57  ? 0.60883 0.59131 0.63943 0.08608  -0.00467 -0.02168 57  ASP A C   
450  O O   . ASP A 57  ? 0.50146 0.49035 0.54128 0.08090  -0.00469 -0.01711 57  ASP A O   
451  C CB  . ASP A 57  ? 0.62947 0.59740 0.66203 0.08270  -0.01785 -0.02599 57  ASP A CB  
452  C CG  . ASP A 57  ? 0.70581 0.67624 0.74650 0.08637  -0.01639 -0.02747 57  ASP A CG  
453  O OD1 . ASP A 57  ? 0.53786 0.51333 0.57838 0.09133  -0.01024 -0.02801 57  ASP A OD1 
454  O OD2 . ASP A 57  ? 0.60351 0.57076 0.65074 0.08417  -0.02158 -0.02817 57  ASP A OD2 
455  N N   . PRO A 58  ? 0.66783 0.47860 0.57293 0.08364  0.04171  0.05814  58  PRO A N   
456  C CA  . PRO A 58  ? 0.57341 0.39608 0.49200 0.09215  0.03688  0.05634  58  PRO A CA  
457  C C   . PRO A 58  ? 0.68381 0.51115 0.59312 0.10821  0.03146  0.06221  58  PRO A C   
458  O O   . PRO A 58  ? 0.62714 0.46960 0.54826 0.11648  0.02604  0.05984  58  PRO A O   
459  C CB  . PRO A 58  ? 0.47153 0.29816 0.40282 0.09363  0.03732  0.05510  58  PRO A CB  
460  C CG  . PRO A 58  ? 0.60822 0.42292 0.52728 0.09216  0.04163  0.05928  58  PRO A CG  
461  C CD  . PRO A 58  ? 0.58746 0.39448 0.49463 0.08202  0.04477  0.05873  58  PRO A CD  
462  N N   . GLN A 59  ? 0.66617 0.48473 0.55596 0.11282  0.03179  0.06918  59  GLN A N   
463  C CA  . GLN A 59  ? 0.71077 0.53769 0.59081 0.12733  0.02514  0.07509  59  GLN A CA  
464  C C   . GLN A 59  ? 0.61804 0.45148 0.49452 0.12734  0.02109  0.07253  59  GLN A C   
465  O O   . GLN A 59  ? 0.56446 0.41659 0.44284 0.13877  0.01286  0.07327  59  GLN A O   
466  C CB  . GLN A 59  ? 0.69433 0.51045 0.55492 0.13065  0.02654  0.08294  59  GLN A CB  
467  C CG  . GLN A 59  ? 0.67439 0.50253 0.52630 0.14570  0.01894  0.08998  59  GLN A CG  
468  C CD  . GLN A 59  ? 0.80860 0.65157 0.67417 0.15748  0.01474  0.09157  59  GLN A CD  
469  O OE1 . GLN A 59  ? 0.88650 0.72261 0.75895 0.15656  0.01908  0.09169  59  GLN A OE1 
470  N NE2 . GLN A 59  ? 0.89451 0.76033 0.76465 0.16809  0.00579  0.09219  59  GLN A NE2 
471  N N   . PHE A 60  ? 0.61334 0.43562 0.48606 0.11369  0.02600  0.06849  60  PHE A N   
472  C CA  . PHE A 60  ? 0.57985 0.41205 0.45300 0.10939  0.02245  0.06297  60  PHE A CA  
473  C C   . PHE A 60  ? 0.49692 0.35736 0.39775 0.10672  0.01706  0.05158  60  PHE A C   
474  O O   . PHE A 60  ? 0.49328 0.37818 0.40056 0.10435  0.01024  0.04457  60  PHE A O   
475  C CB  . PHE A 60  ? 0.63743 0.45121 0.50394 0.09456  0.02983  0.06068  60  PHE A CB  
476  C CG  . PHE A 60  ? 0.91295 0.71390 0.75967 0.09009  0.03330  0.06602  60  PHE A CG  
477  C CD1 . PHE A 60  ? 1.07376 0.87419 0.89998 0.09675  0.02934  0.07193  60  PHE A CD1 
478  C CD2 . PHE A 60  ? 0.97754 0.77241 0.82844 0.07868  0.03924  0.06367  60  PHE A CD2 
479  C CE1 . PHE A 60  ? 1.19198 0.98356 1.00417 0.09165  0.03232  0.07503  60  PHE A CE1 
480  C CE2 . PHE A 60  ? 1.01576 0.80287 0.85271 0.07509  0.04152  0.06653  60  PHE A CE2 
481  C CZ  . PHE A 60  ? 1.23372 1.01808 1.05217 0.08129  0.03849  0.07208  60  PHE A CZ  
482  N N   . ALA A 61  ? 0.43521 0.29267 0.35229 0.10660  0.02018  0.04941  61  ALA A N   
483  C CA  . ALA A 61  ? 0.50321 0.38702 0.44680 0.10442  0.01515  0.03908  61  ALA A CA  
484  C C   . ALA A 61  ? 0.48654 0.39448 0.43521 0.11781  0.00626  0.04027  61  ALA A C   
485  O O   . ALA A 61  ? 0.46729 0.40311 0.42986 0.11570  -0.00086 0.03175  61  ALA A O   
486  C CB  . ALA A 61  ? 0.38135 0.25489 0.33983 0.10078  0.02108  0.03720  61  ALA A CB  
487  N N   . LEU A 62  ? 0.55560 0.45329 0.49335 0.13155  0.00676  0.05092  62  LEU A N   
488  C CA  . LEU A 62  ? 0.53191 0.45212 0.47369 0.14528  -0.00151 0.05373  62  LEU A CA  
489  C C   . LEU A 62  ? 0.47890 0.41792 0.41133 0.14581  -0.00910 0.05293  62  LEU A C   
490  O O   . LEU A 62  ? 0.56314 0.53187 0.50722 0.14943  -0.01751 0.04822  62  LEU A O   
491  C CB  . LEU A 62  ? 0.58373 0.48577 0.51313 0.15959  0.00161  0.06655  62  LEU A CB  
492  C CG  . LEU A 62  ? 0.59007 0.48418 0.53371 0.15315  0.00762  0.06372  62  LEU A CG  
493  C CD1 . LEU A 62  ? 0.64913 0.52432 0.57920 0.15340  0.01293  0.07139  62  LEU A CD1 
494  C CD2 . LEU A 62  ? 0.55716 0.47713 0.52266 0.16031  0.00150  0.05946  62  LEU A CD2 
495  N N   . THR A 63  ? 0.46557 0.38804 0.37653 0.14193  -0.00619 0.05752  63  THR A N   
496  C CA  . THR A 63  ? 0.43854 0.37786 0.33944 0.14105  -0.01277 0.05639  63  THR A CA  
497  C C   . THR A 63  ? 0.46475 0.42835 0.38280 0.12911  -0.01676 0.04202  63  THR A C   
498  O O   . THR A 63  ? 0.54187 0.53317 0.46461 0.13125  -0.02503 0.03782  63  THR A O   
499  C CB  . THR A 63  ? 0.50933 0.42425 0.38467 0.13741  -0.00776 0.06329  63  THR A CB  
500  O OG1 . THR A 63  ? 0.61501 0.50736 0.47435 0.14898  -0.00411 0.07683  63  THR A OG1 
501  C CG2 . THR A 63  ? 0.43365 0.36596 0.29786 0.13602  -0.01430 0.06204  63  THR A CG2 
502  N N   . ASN A 64  ? 0.43980 0.39359 0.36780 0.11634  -0.01081 0.03444  64  ASN A N   
503  C CA  . ASN A 64  ? 0.45420 0.42874 0.39951 0.10464  -0.01359 0.02078  64  ASN A CA  
504  C C   . ASN A 64  ? 0.47356 0.47638 0.44140 0.10875  -0.02045 0.01412  64  ASN A C   
505  O O   . ASN A 64  ? 0.51435 0.54329 0.48956 0.10595  -0.02716 0.00617  64  ASN A O   
506  C CB  . ASN A 64  ? 0.47164 0.42902 0.42459 0.09125  -0.00543 0.01552  64  ASN A CB  
507  C CG  . ASN A 64  ? 0.42954 0.38030 0.37125 0.08026  -0.00262 0.01237  64  ASN A CG  
508  O OD1 . ASN A 64  ? 0.47206 0.42248 0.39471 0.08331  -0.00486 0.01689  64  ASN A OD1 
509  N ND2 . ASN A 64  ? 0.44936 0.39549 0.40318 0.06736  0.00232  0.00476  64  ASN A ND2 
510  N N   . ILE A 65  ? 0.45051 0.44880 0.42940 0.11503  -0.01869 0.01699  65  ILE A N   
511  C CA  . ILE A 65  ? 0.45962 0.48471 0.46073 0.11848  -0.02489 0.01057  65  ILE A CA  
512  C C   . ILE A 65  ? 0.48514 0.53421 0.48137 0.12946  -0.03413 0.01381  65  ILE A C   
513  O O   . ILE A 65  ? 0.43929 0.51743 0.45002 0.12794  -0.04117 0.00552  65  ILE A O   
514  C CB  . ILE A 65  ? 0.50386 0.51825 0.51620 0.12372  -0.02073 0.01387  65  ILE A CB  
515  C CG1 . ILE A 65  ? 0.56378 0.55866 0.58333 0.11102  -0.01228 0.00941  65  ILE A CG1 
516  C CG2 . ILE A 65  ? 0.41008 0.45316 0.44425 0.12847  -0.02755 0.00817  65  ILE A CG2 
517  C CD1 . ILE A 65  ? 0.30702 0.31750 0.34316 0.09690  -0.01374 -0.00370 65  ILE A CD1 
518  N N   . ALA A 66  ? 0.43536 0.47291 0.41081 0.14021  -0.03424 0.02608  66  ALA A N   
519  C CA  . ALA A 66  ? 0.43437 0.49443 0.40366 0.15073  -0.04303 0.03064  66  ALA A CA  
520  C C   . ALA A 66  ? 0.45626 0.53737 0.42305 0.14203  -0.04862 0.02231  66  ALA A C   
521  O O   . ALA A 66  ? 0.46437 0.57489 0.43720 0.14576  -0.05714 0.01950  66  ALA A O   
522  C CB  . ALA A 66  ? 0.41231 0.45294 0.35845 0.16273  -0.04119 0.04592  66  ALA A CB  
523  N N   . VAL A 67  ? 0.50182 0.56865 0.45971 0.13019  -0.04375 0.01821  67  VAL A N   
524  C CA  . VAL A 67  ? 0.38470 0.47032 0.34185 0.12043  -0.04786 0.00865  67  VAL A CA  
525  C C   . VAL A 67  ? 0.36294 0.47227 0.34549 0.11247  -0.05105 -0.00541 67  VAL A C   
526  O O   . VAL A 67  ? 0.49710 0.63378 0.48423 0.11014  -0.05806 -0.01248 67  VAL A O   
527  C CB  . VAL A 67  ? 0.44502 0.50827 0.38792 0.10968  -0.04091 0.00764  67  VAL A CB  
528  C CG1 . VAL A 67  ? 0.35246 0.43429 0.29817 0.09803  -0.04380 -0.00433 67  VAL A CG1 
529  C CG2 . VAL A 67  ? 0.34202 0.38567 0.25826 0.11741  -0.03907 0.02129  67  VAL A CG2 
530  N N   . LEU A 68  ? 0.38040 0.47978 0.37961 0.10781  -0.04590 -0.00965 68  LEU A N   
531  C CA  . LEU A 68  ? 0.44093 0.56171 0.46507 0.10045  -0.04867 -0.02246 68  LEU A CA  
532  C C   . LEU A 68  ? 0.49102 0.64064 0.52560 0.10991  -0.05748 -0.02266 68  LEU A C   
533  O O   . LEU A 68  ? 0.42529 0.60135 0.47262 0.10448  -0.06309 -0.03305 68  LEU A O   
534  C CB  . LEU A 68  ? 0.33320 0.43725 0.37246 0.09496  -0.04159 -0.02500 68  LEU A CB  
535  C CG  . LEU A 68  ? 0.34742 0.43729 0.38944 0.08000  -0.03481 -0.03218 68  LEU A CG  
536  C CD1 . LEU A 68  ? 0.33496 0.39571 0.35445 0.07914  -0.02807 -0.02354 68  LEU A CD1 
537  C CD2 . LEU A 68  ? 0.24795 0.33364 0.31186 0.07368  -0.03066 -0.03763 68  LEU A CD2 
538  N N   . LYS A 69  ? 0.39254 0.53767 0.42219 0.12397  -0.05858 -0.01130 69  LYS A N   
539  C CA  . LYS A 69  ? 0.50929 0.68240 0.54812 0.13397  -0.06702 -0.01013 69  LYS A CA  
540  C C   . LYS A 69  ? 0.40915 0.60695 0.43884 0.13410  -0.07507 -0.01188 69  LYS A C   
541  O O   . LYS A 69  ? 0.54499 0.77291 0.58792 0.13240  -0.08212 -0.01963 69  LYS A O   
542  C CB  . LYS A 69  ? 0.46123 0.62267 0.49353 0.14987  -0.06604 0.00384  69  LYS A CB  
543  N N   . HIS A 70  ? 0.36129 0.54698 0.36800 0.13542  -0.07404 -0.00490 70  HIS A N   
544  C CA  . HIS A 70  ? 0.41229 0.62039 0.40849 0.13461  -0.08125 -0.00632 70  HIS A CA  
545  C C   . HIS A 70  ? 0.49574 0.72048 0.50245 0.11932  -0.08257 -0.02238 70  HIS A C   
546  O O   . HIS A 70  ? 0.48806 0.74335 0.50167 0.11790  -0.09018 -0.02883 70  HIS A O   
547  C CB  . HIS A 70  ? 0.52204 0.71056 0.49138 0.13745  -0.07869 0.00391  70  HIS A CB  
548  C CG  . HIS A 70  ? 0.74472 0.95302 0.70166 0.13373  -0.08473 0.00134  70  HIS A CG  
549  N ND1 . HIS A 70  ? 0.77373 0.98011 0.72584 0.11990  -0.08217 -0.00838 70  HIS A ND1 
550  C CD2 . HIS A 70  ? 0.82445 1.05529 0.77280 0.14180  -0.09305 0.00731  70  HIS A CD2 
551  C CE1 . HIS A 70  ? 0.66237 0.88894 0.60301 0.11929  -0.08850 -0.00880 70  HIS A CE1 
552  N NE2 . HIS A 70  ? 0.79138 1.03343 0.72940 0.13226  -0.09537 0.00081  70  HIS A NE2 
553  N N   . ASN A 71  ? 0.45340 0.65849 0.46183 0.10759  -0.07500 -0.02900 71  ASN A N   
554  C CA  . ASN A 71  ? 0.40557 0.62392 0.42357 0.09305  -0.07523 -0.04404 71  ASN A CA  
555  C C   . ASN A 71  ? 0.34655 0.58776 0.39025 0.08977  -0.07899 -0.05449 71  ASN A C   
556  O O   . ASN A 71  ? 0.40969 0.67495 0.46056 0.08230  -0.08358 -0.06542 71  ASN A O   
557  C CB  . ASN A 71  ? 0.37169 0.56317 0.38747 0.08214  -0.06581 -0.04766 71  ASN A CB  
558  C CG  . ASN A 71  ? 0.50222 0.67418 0.49232 0.08304  -0.06243 -0.03936 71  ASN A CG  
559  O OD1 . ASN A 71  ? 0.43385 0.61225 0.40742 0.09161  -0.06720 -0.03095 71  ASN A OD1 
560  N ND2 . ASN A 71  ? 0.45123 0.59962 0.43788 0.07415  -0.05420 -0.04124 71  ASN A ND2 
561  N N   . LEU A 72  ? 0.43781 0.67188 0.49538 0.09481  -0.07691 -0.05157 72  LEU A N   
562  C CA  . LEU A 72  ? 0.52578 0.78102 0.60803 0.09163  -0.08033 -0.06115 72  LEU A CA  
563  C C   . LEU A 72  ? 0.60602 0.89521 0.69075 0.09777  -0.09047 -0.06196 72  LEU A C   
564  O O   . LEU A 72  ? 0.53179 0.84496 0.63141 0.09031  -0.09466 -0.07369 72  LEU A O   
565  C CB  . LEU A 72  ? 0.39659 0.63790 0.49139 0.09703  -0.07633 -0.05649 72  LEU A CB  
566  C CG  . LEU A 72  ? 0.38441 0.64742 0.50491 0.09454  -0.07991 -0.06542 72  LEU A CG  
567  C CD1 . LEU A 72  ? 0.33700 0.60512 0.47133 0.07844  -0.07782 -0.08017 72  LEU A CD1 
568  C CD2 . LEU A 72  ? 0.41686 0.66643 0.54796 0.10097  -0.07606 -0.05973 72  LEU A CD2 
569  N N   . ASN A 73  ? 0.46166 0.75353 0.53189 0.11115  -0.09447 -0.04936 73  ASN A N   
570  C CA  . ASN A 73  ? 0.47638 0.80140 0.54749 0.11737  -0.10438 -0.04865 73  ASN A CA  
571  C C   . ASN A 73  ? 0.55036 0.89486 0.61564 0.10686  -0.10844 -0.05843 73  ASN A C   
572  O O   . ASN A 73  ? 0.50442 0.86998 0.57828 0.10119  -0.11174 -0.06543 73  ASN A O   
573  C CB  . ASN A 73  ? 0.58303 0.90450 0.63771 0.13348  -0.10714 -0.03209 73  ASN A CB  
574  C CG  . ASN A 73  ? 0.75456 1.06598 0.81834 0.14546  -0.10507 -0.02336 73  ASN A CG  
575  O OD1 . ASN A 73  ? 0.77740 1.09181 0.85999 0.14104  -0.10315 -0.02934 73  ASN A OD1 
576  N ND2 . ASN A 73  ? 0.73635 1.02833 0.78432 0.15744  -0.10262 -0.00877 73  ASN A ND2 
577  N N   . SER A 74  ? 0.43114 0.75869 0.47887 0.10116  -0.10420 -0.05794 74  SER A N   
578  C CA  . SER A 74  ? 0.39137 0.73543 0.43238 0.09066  -0.10707 -0.06752 74  SER A CA  
579  C C   . SER A 74  ? 0.47831 0.83349 0.53931 0.07649  -0.10583 -0.08471 74  SER A C   
580  O O   . SER A 74  ? 0.50443 0.87920 0.56736 0.06898  -0.10856 -0.09282 74  SER A O   
581  C CB  . SER A 74  ? 0.38733 0.70779 0.40667 0.08705  -0.10147 -0.06367 74  SER A CB  
582  O OG  . SER A 74  ? 0.79131 1.12485 0.80570 0.07517  -0.10261 -0.07466 74  SER A OG  
583  N N   . LEU A 75  ? 0.46221 0.79735 0.53654 0.07129  -0.09859 -0.08873 75  LEU A N   
584  C CA  . LEU A 75  ? 0.41408 0.75330 0.50604 0.05707  -0.09529 -0.10375 75  LEU A CA  
585  C C   . LEU A 75  ? 0.43910 0.78528 0.54512 0.05544  -0.09459 -0.10558 75  LEU A C   
586  O O   . LEU A 75  ? 0.46269 0.81099 0.57543 0.04409  -0.09107 -0.11507 75  LEU A O   
587  C CB  . LEU A 75  ? 0.42998 0.74197 0.52961 0.05138  -0.08659 -0.10569 75  LEU A CB  
588  C CG  . LEU A 75  ? 0.36201 0.64884 0.44309 0.04729  -0.07982 -0.10240 75  LEU A CG  
589  C CD1 . LEU A 75  ? 0.35773 0.61748 0.44771 0.04143  -0.07065 -0.10323 75  LEU A CD1 
590  C CD2 . LEU A 75  ? 0.33191 0.63123 0.40650 0.03672  -0.08073 -0.11291 75  LEU A CD2 
591  N N   . ILE A 76  ? 0.42225 0.77013 0.53172 0.06672  -0.09730 -0.09617 76  ILE A N   
592  C CA  . ILE A 76  ? 0.41028 0.76621 0.53043 0.06530  -0.09755 -0.09731 76  ILE A CA  
593  C C   . ILE A 76  ? 0.48933 0.86786 0.60292 0.06274  -0.10246 -0.10033 76  ILE A C   
594  O O   . ILE A 76  ? 0.44246 0.82710 0.56383 0.05471  -0.10098 -0.10727 76  ILE A O   
595  C CB  . ILE A 76  ? 0.47260 0.82561 0.59623 0.07818  -0.09929 -0.08599 76  ILE A CB  
596  C CG1 . ILE A 76  ? 0.38561 0.71507 0.51730 0.07881  -0.09317 -0.08403 76  ILE A CG1 
597  C CG2 . ILE A 76  ? 0.47371 0.83758 0.60637 0.07694  -0.10062 -0.08669 76  ILE A CG2 
598  C CD1 . ILE A 76  ? 0.43761 0.76091 0.57014 0.09224  -0.09380 -0.07213 76  ILE A CD1 
599  N N   . LYS A 77  ? 0.46616 0.85634 0.56411 0.06946  -0.10811 -0.09455 77  LYS A N   
600  C CA  . LYS A 77  ? 0.52344 0.93488 0.61374 0.06603  -0.11247 -0.09732 77  LYS A CA  
601  C C   . LYS A 77  ? 0.50200 0.91284 0.59195 0.05126  -0.10832 -0.11033 77  LYS A C   
602  O O   . LYS A 77  ? 0.59837 1.01993 0.69309 0.04352  -0.10773 -0.11750 77  LYS A O   
603  C CB  . LYS A 77  ? 0.45344 0.87424 0.52519 0.07663  -0.11877 -0.08644 77  LYS A CB  
604  C CG  . LYS A 77  ? 0.55505 0.97413 0.62582 0.09247  -0.12189 -0.07203 77  LYS A CG  
605  C CD  . LYS A 77  ? 0.54593 0.97118 0.59661 0.10285  -0.12717 -0.05999 77  LYS A CD  
606  C CE  . LYS A 77  ? 0.73231 1.15306 0.78230 0.11891  -0.12895 -0.04497 77  LYS A CE  
607  N NZ  . LYS A 77  ? 0.92298 1.35827 0.98565 0.12034  -0.13101 -0.04454 77  LYS A NZ  
608  N N   . ARG A 78  ? 0.46688 0.86418 0.55099 0.04732  -0.10493 -0.11328 78  ARG A N   
609  C CA  . ARG A 78  ? 0.46491 0.86070 0.54655 0.03405  -0.10050 -0.12456 78  ARG A CA  
610  C C   . ARG A 78  ? 0.44773 0.83361 0.54572 0.02353  -0.09304 -0.13422 78  ARG A C   
611  O O   . ARG A 78  ? 0.56549 0.95466 0.66339 0.01359  -0.08965 -0.14304 78  ARG A O   
612  C CB  . ARG A 78  ? 0.35521 0.73706 0.42615 0.03253  -0.09826 -0.12465 78  ARG A CB  
613  N N   . SER A 79  ? 0.52984 0.65579 0.54073 -0.05303 -0.03350 -0.06587 79  SER A N   
614  C CA  . SER A 79  ? 0.55263 0.68318 0.57409 -0.06414 -0.02991 -0.06468 79  SER A CA  
615  C C   . SER A 79  ? 0.62871 0.78637 0.66154 -0.07110 -0.03552 -0.06511 79  SER A C   
616  O O   . SER A 79  ? 0.65450 0.82080 0.69848 -0.07951 -0.03282 -0.06338 79  SER A O   
617  C CB  . SER A 79  ? 0.52413 0.65522 0.55425 -0.06000 -0.02328 -0.06071 79  SER A CB  
618  O OG  . SER A 79  ? 0.50333 0.65885 0.54348 -0.05252 -0.02559 -0.05876 79  SER A OG  
619  N N   . ASN A 80  ? 0.62193 0.79322 0.65244 -0.06791 -0.04331 -0.06711 80  ASN A N   
620  C CA  . ASN A 80  ? 0.66354 0.86328 0.70594 -0.07330 -0.04942 -0.06728 80  ASN A CA  
621  C C   . ASN A 80  ? 0.58784 0.81010 0.64707 -0.07088 -0.04654 -0.06336 80  ASN A C   
622  O O   . ASN A 80  ? 0.59556 0.83453 0.66716 -0.08010 -0.04683 -0.06228 80  ASN A O   
623  C CB  . ASN A 80  ? 0.50117 0.69756 0.54351 -0.08869 -0.05121 -0.06977 80  ASN A CB  
624  N N   . SER A 81  ? 0.50803 0.73009 0.56730 -0.05843 -0.04355 -0.06122 81  SER A N   
625  C CA  . SER A 81  ? 0.52756 0.77085 0.60080 -0.05367 -0.04099 -0.05779 81  SER A CA  
626  C C   . SER A 81  ? 0.49871 0.73997 0.58031 -0.06268 -0.03424 -0.05522 81  SER A C   
627  O O   . SER A 81  ? 0.63623 0.89955 0.73158 -0.06743 -0.03393 -0.05310 81  SER A O   
628  C CB  . SER A 81  ? 0.51662 0.79176 0.60106 -0.05282 -0.04752 -0.05765 81  SER A CB  
629  O OG  . SER A 81  ? 0.77845 1.05625 0.85567 -0.04298 -0.05366 -0.05940 81  SER A OG  
630  N N   . THR A 82  ? 0.48010 0.69475 0.55351 -0.06496 -0.02867 -0.05513 82  THR A N   
631  C CA  . THR A 82  ? 0.51810 0.72818 0.59833 -0.07216 -0.02194 -0.05223 82  THR A CA  
632  C C   . THR A 82  ? 0.49819 0.71538 0.58400 -0.06251 -0.01770 -0.04887 82  THR A C   
633  O O   . THR A 82  ? 0.46176 0.66402 0.53961 -0.05304 -0.01561 -0.04886 82  THR A O   
634  C CB  . THR A 82  ? 0.56366 0.74300 0.63351 -0.07759 -0.01761 -0.05321 82  THR A CB  
635  O OG1 . THR A 82  ? 0.54848 0.72173 0.61311 -0.08737 -0.02137 -0.05661 82  THR A OG1 
636  C CG2 . THR A 82  ? 0.42300 0.59732 0.50001 -0.08367 -0.01058 -0.04963 82  THR A CG2 
637  N N   . ALA A 83  ? 0.45197 0.69180 0.55119 -0.06497 -0.01641 -0.04605 83  ALA A N   
638  C CA  . ALA A 83  ? 0.43220 0.68181 0.53664 -0.05556 -0.01295 -0.04321 83  ALA A CA  
639  C C   . ALA A 83  ? 0.39611 0.63252 0.50182 -0.05927 -0.00568 -0.04002 83  ALA A C   
640  O O   . ALA A 83  ? 0.38952 0.61316 0.49476 -0.06994 -0.00316 -0.03948 83  ALA A O   
641  C CB  . ALA A 83  ? 0.36469 0.64713 0.48265 -0.05485 -0.01513 -0.04169 83  ALA A CB  
642  N N   . ALA A 84  ? 0.33338 0.57267 0.44042 -0.05007 -0.00245 -0.03792 84  ALA A N   
643  C CA  . ALA A 84  ? 0.37170 0.59941 0.47965 -0.05227 0.00396  -0.03464 84  ALA A CA  
644  C C   . ALA A 84  ? 0.35909 0.60187 0.47869 -0.06271 0.00674  -0.03127 84  ALA A C   
645  O O   . ALA A 84  ? 0.37483 0.64227 0.50371 -0.06491 0.00441  -0.03084 84  ALA A O   
646  C CB  . ALA A 84  ? 0.36348 0.59216 0.46976 -0.03981 0.00604  -0.03350 84  ALA A CB  
647  N N   . THR A 85  ? 0.46352 0.69123 0.58291 -0.06917 0.01183  -0.02857 85  THR A N   
648  C CA  . THR A 85  ? 0.40044 0.63898 0.52997 -0.07902 0.01532  -0.02464 85  THR A CA  
649  C C   . THR A 85  ? 0.45430 0.69940 0.58724 -0.07304 0.01983  -0.02075 85  THR A C   
650  O O   . THR A 85  ? 0.60812 0.83603 0.73426 -0.06700 0.02232  -0.02019 85  THR A O   
651  C CB  . THR A 85  ? 0.31657 0.53397 0.44370 -0.09035 0.01808  -0.02384 85  THR A CB  
652  O OG1 . THR A 85  ? 0.44571 0.65779 0.56916 -0.09643 0.01377  -0.02780 85  THR A OG1 
653  C CG2 . THR A 85  ? 0.38877 0.61612 0.52618 -0.10023 0.02204  -0.01917 85  THR A CG2 
654  N N   . ASN A 86  ? 0.48265 0.75276 0.62599 -0.07474 0.02083  -0.01808 86  ASN A N   
655  C CA  . ASN A 86  ? 0.37029 0.64837 0.51646 -0.06929 0.02518  -0.01441 86  ASN A CA  
656  C C   . ASN A 86  ? 0.37820 0.64264 0.52513 -0.07738 0.03047  -0.01006 86  ASN A C   
657  O O   . ASN A 86  ? 0.49813 0.76651 0.65171 -0.08904 0.03188  -0.00771 86  ASN A O   
658  C CB  . ASN A 86  ? 0.44919 0.75878 0.60623 -0.06864 0.02509  -0.01274 86  ASN A CB  
659  C CG  . ASN A 86  ? 0.45467 0.77930 0.61186 -0.05960 0.01997  -0.01659 86  ASN A CG  
660  O OD1 . ASN A 86  ? 0.49057 0.80333 0.63875 -0.05002 0.01751  -0.01985 86  ASN A OD1 
661  N ND2 . ASN A 86  ? 0.57654 0.92776 0.74448 -0.06256 0.01838  -0.01591 86  ASN A ND2 
662  N N   . GLU A 87  ? 0.45702 0.70529 0.59737 -0.07132 0.03318  -0.00886 87  GLU A N   
663  C CA  . GLU A 87  ? 0.45742 0.69470 0.59885 -0.07737 0.03817  -0.00411 87  GLU A CA  
664  C C   . GLU A 87  ? 0.39124 0.64733 0.53831 -0.07494 0.04150  0.00008  87  GLU A C   
665  O O   . GLU A 87  ? 0.39435 0.66751 0.54230 -0.06617 0.04035  -0.00118 87  GLU A O   
666  C CB  . GLU A 87  ? 0.37070 0.58127 0.50282 -0.07259 0.03930  -0.00452 87  GLU A CB  
667  C CG  . GLU A 87  ? 0.51490 0.70692 0.63987 -0.07239 0.03626  -0.00899 87  GLU A CG  
668  C CD  . GLU A 87  ? 0.55437 0.73717 0.68126 -0.08489 0.03675  -0.00892 87  GLU A CD  
669  O OE1 . GLU A 87  ? 0.68274 0.86634 0.81538 -0.09353 0.04029  -0.00470 87  GLU A OE1 
670  O OE2 . GLU A 87  ? 0.58782 0.76197 0.70992 -0.08602 0.03359  -0.01310 87  GLU A OE2 
671  N N   . VAL A 88  ? 0.47837 0.73100 0.62900 -0.08271 0.04587  0.00523  88  VAL A N   
672  C CA  . VAL A 88  ? 0.33758 0.60511 0.49220 -0.08106 0.04969  0.00989  88  VAL A CA  
673  C C   . VAL A 88  ? 0.37409 0.62693 0.52045 -0.07228 0.05110  0.01066  88  VAL A C   
674  O O   . VAL A 88  ? 0.40711 0.63867 0.54995 -0.07573 0.05272  0.01264  88  VAL A O   
675  C CB  . VAL A 88  ? 0.50981 0.78052 0.67189 -0.09365 0.05365  0.01557  88  VAL A CB  
676  C CG1 . VAL A 88  ? 0.42895 0.71651 0.59455 -0.09150 0.05773  0.02054  88  VAL A CG1 
677  C CG2 . VAL A 88  ? 0.40431 0.68728 0.57451 -0.10336 0.05173  0.01447  88  VAL A CG2 
678  N N   . PRO A 89  ? 0.30612 0.56894 0.44929 -0.06104 0.05041  0.00906  89  PRO A N   
679  C CA  . PRO A 89  ? 0.36618 0.61528 0.50150 -0.05321 0.05138  0.00972  89  PRO A CA  
680  C C   . PRO A 89  ? 0.44230 0.69209 0.57945 -0.05774 0.05594  0.01600  89  PRO A C   
681  O O   . PRO A 89  ? 0.50532 0.77126 0.64968 -0.06443 0.05874  0.01981  89  PRO A O   
682  C CB  . PRO A 89  ? 0.40891 0.67184 0.54118 -0.04078 0.04950  0.00619  89  PRO A CB  
683  C CG  . PRO A 89  ? 0.32870 0.61818 0.46962 -0.04326 0.04968  0.00632  89  PRO A CG  
684  C CD  . PRO A 89  ? 0.40520 0.69209 0.55185 -0.05479 0.04857  0.00645  89  PRO A CD  
685  N N   . GLU A 90  ? 0.50792 0.73965 0.63855 -0.05418 0.05655  0.01732  90  GLU A N   
686  C CA  . GLU A 90  ? 0.41025 0.64083 0.54072 -0.05654 0.06023  0.02321  90  GLU A CA  
687  C C   . GLU A 90  ? 0.34407 0.57707 0.46746 -0.04518 0.05969  0.02212  90  GLU A C   
688  O O   . GLU A 90  ? 0.36728 0.58740 0.48411 -0.03742 0.05669  0.01811  90  GLU A O   
689  C CB  . GLU A 90  ? 0.57215 0.77898 0.70150 -0.06283 0.06130  0.02632  90  GLU A CB  
690  C CG  . GLU A 90  ? 0.68460 0.88458 0.81911 -0.07323 0.06147  0.02625  90  GLU A CG  
691  C CD  . GLU A 90  ? 1.01887 1.19466 1.15207 -0.07844 0.06292  0.02918  90  GLU A CD  
692  O OE1 . GLU A 90  ? 0.86833 1.03690 0.99905 -0.07637 0.06454  0.03321  90  GLU A OE1 
693  O OE2 . GLU A 90  ? 0.85519 1.01924 0.98968 -0.08438 0.06238  0.02741  90  GLU A OE2 
694  N N   . VAL A 91  ? 0.49332 0.74244 0.61772 -0.04434 0.06268  0.02564  91  VAL A N   
695  C CA  . VAL A 91  ? 0.45631 0.71095 0.57372 -0.03360 0.06243  0.02426  91  VAL A CA  
696  C C   . VAL A 91  ? 0.42721 0.67597 0.54131 -0.03547 0.06511  0.02999  91  VAL A C   
697  O O   . VAL A 91  ? 0.37603 0.63097 0.49524 -0.04401 0.06869  0.03578  91  VAL A O   
698  C CB  . VAL A 91  ? 0.36020 0.64144 0.48060 -0.02910 0.06363  0.02269  91  VAL A CB  
699  C CG1 . VAL A 91  ? 0.31776 0.60333 0.42984 -0.01762 0.06361  0.02083  91  VAL A CG1 
700  C CG2 . VAL A 91  ? 0.33776 0.62496 0.46189 -0.02740 0.06046  0.01740  91  VAL A CG2 
701  N N   . THR A 92  ? 0.33853 0.57522 0.44405 -0.02763 0.06316  0.02849  92  THR A N   
702  C CA  . THR A 92  ? 0.36106 0.59173 0.46205 -0.02798 0.06474  0.03343  92  THR A CA  
703  C C   . THR A 92  ? 0.49687 0.73043 0.58855 -0.01647 0.06309  0.03006  92  THR A C   
704  O O   . THR A 92  ? 0.39828 0.62367 0.48548 -0.00884 0.05943  0.02430  92  THR A O   
705  C CB  . THR A 92  ? 0.35355 0.55976 0.45392 -0.03227 0.06339  0.03579  92  THR A CB  
706  O OG1 . THR A 92  ? 0.49278 0.69346 0.60060 -0.04113 0.06408  0.03653  92  THR A OG1 
707  C CG2 . THR A 92  ? 0.47655 0.67938 0.57511 -0.03576 0.06564  0.04271  92  THR A CG2 
708  N N   . VAL A 93  ? 0.33941 0.58414 0.42773 -0.01525 0.06586  0.03362  93  VAL A N   
709  C CA  . VAL A 93  ? 0.39011 0.63785 0.46854 -0.00470 0.06468  0.03062  93  VAL A CA  
710  C C   . VAL A 93  ? 0.38247 0.61774 0.45454 -0.00561 0.06433  0.03506  93  VAL A C   
711  O O   . VAL A 93  ? 0.39610 0.63249 0.47142 -0.01361 0.06727  0.04190  93  VAL A O   
712  C CB  . VAL A 93  ? 0.46239 0.73546 0.54093 -0.00099 0.06827  0.03024  93  VAL A CB  
713  C CG1 . VAL A 93  ? 0.68863 0.97383 0.77175 -0.00962 0.07339  0.03787  93  VAL A CG1 
714  C CG2 . VAL A 93  ? 0.41159 0.68639 0.47883 0.01059  0.06706  0.02630  93  VAL A CG2 
715  N N   . PHE A 94  ? 0.36308 0.58602 0.42635 0.00236  0.06045  0.03132  94  PHE A N   
716  C CA  . PHE A 94  ? 0.33725 0.54751 0.39417 0.00221  0.05899  0.03493  94  PHE A CA  
717  C C   . PHE A 94  ? 0.34619 0.55010 0.39242 0.01296  0.05499  0.02918  94  PHE A C   
718  O O   . PHE A 94  ? 0.42963 0.63428 0.47437 0.01979  0.05301  0.02258  94  PHE A O   
719  C CB  . PHE A 94  ? 0.25586 0.44631 0.31797 -0.00495 0.05738  0.03842  94  PHE A CB  
720  C CG  . PHE A 94  ? 0.28746 0.46445 0.35218 -0.00301 0.05407  0.03316  94  PHE A CG  
721  C CD1 . PHE A 94  ? 0.37492 0.55494 0.44773 -0.00770 0.05542  0.03196  94  PHE A CD1 
722  C CD2 . PHE A 94  ? 0.26497 0.42607 0.32387 0.00321  0.04956  0.02957  94  PHE A CD2 
723  C CE1 . PHE A 94  ? 0.39769 0.56507 0.47194 -0.00586 0.05254  0.02732  94  PHE A CE1 
724  C CE2 . PHE A 94  ? 0.35516 0.50377 0.41627 0.00492  0.04691  0.02515  94  PHE A CE2 
725  C CZ  . PHE A 94  ? 0.34641 0.49813 0.41481 0.00054  0.04852  0.02408  94  PHE A CZ  
726  N N   . SER A 95  ? 0.38291 0.58020 0.42153 0.01433  0.05360  0.03181  95  SER A N   
727  C CA  . SER A 95  ? 0.43548 0.62658 0.46300 0.02393  0.04968  0.02663  95  SER A CA  
728  C C   . SER A 95  ? 0.44994 0.61820 0.47708 0.02432  0.04440  0.02521  95  SER A C   
729  O O   . SER A 95  ? 0.43895 0.59615 0.47211 0.01708  0.04408  0.03017  95  SER A O   
730  C CB  . SER A 95  ? 0.32652 0.52418 0.34458 0.02574  0.05077  0.02977  95  SER A CB  
731  O OG  . SER A 95  ? 0.46565 0.65485 0.48544 0.01833  0.05060  0.03716  95  SER A OG  
732  N N   . LYS A 96  ? 0.44146 0.60273 0.46176 0.03299  0.04045  0.01843  96  LYS A N   
733  C CA  . LYS A 96  ? 0.43694 0.57710 0.45680 0.03394  0.03539  0.01674  96  LYS A CA  
734  C C   . LYS A 96  ? 0.47721 0.60769 0.49289 0.03157  0.03289  0.02138  96  LYS A C   
735  O O   . LYS A 96  ? 0.53807 0.65281 0.55825 0.02777  0.03029  0.02386  96  LYS A O   
736  C CB  . LYS A 96  ? 0.41994 0.55557 0.43289 0.04387  0.03185  0.00852  96  LYS A CB  
737  C CG  . LYS A 96  ? 0.52269 0.63683 0.53471 0.04547  0.02650  0.00641  96  LYS A CG  
738  C CD  . LYS A 96  ? 0.39457 0.50473 0.39935 0.05537  0.02329  -0.00167 96  LYS A CD  
739  C CE  . LYS A 96  ? 0.50721 0.59616 0.51213 0.05651  0.01824  -0.00367 96  LYS A CE  
740  N NZ  . LYS A 96  ? 0.52151 0.60115 0.53719 0.05008  0.01904  -0.00087 96  LYS A NZ  
741  N N   . SER A 97  ? 0.54057 0.68053 0.54778 0.03381  0.03369  0.02281  97  SER A N   
742  C CA  . SER A 97  ? 0.51230 0.64457 0.51338 0.03275  0.03069  0.02668  97  SER A CA  
743  C C   . SER A 97  ? 0.48456 0.63017 0.48465 0.02789  0.03503  0.03359  97  SER A C   
744  O O   . SER A 97  ? 0.51079 0.67275 0.51347 0.02668  0.04028  0.03432  97  SER A O   
745  C CB  . SER A 97  ? 0.38466 0.51293 0.37272 0.04189  0.02621  0.02042  97  SER A CB  
746  O OG  . SER A 97  ? 0.72792 0.84481 0.71673 0.04677  0.02263  0.01382  97  SER A OG  
747  N N   . PRO A 98  ? 0.53084 0.67013 0.52769 0.02472  0.03297  0.03922  98  PRO A N   
748  C CA  . PRO A 98  ? 0.59784 0.74980 0.59123 0.02120  0.03686  0.04573  98  PRO A CA  
749  C C   . PRO A 98  ? 0.54933 0.71618 0.53100 0.02842  0.03885  0.04156  98  PRO A C   
750  O O   . PRO A 98  ? 0.54319 0.70582 0.51509 0.03641  0.03507  0.03489  98  PRO A O   
751  C CB  . PRO A 98  ? 0.51941 0.65908 0.50948 0.01859  0.03249  0.05110  98  PRO A CB  
752  C CG  . PRO A 98  ? 0.53682 0.65865 0.53519 0.01692  0.02836  0.05000  98  PRO A CG  
753  C CD  . PRO A 98  ? 0.47376 0.59423 0.47199 0.02312  0.02736  0.04099  98  PRO A CD  
754  N N   . VAL A 99  ? 0.49961 0.68380 0.48242 0.02550  0.04506  0.04558  99  VAL A N   
755  C CA  . VAL A 99  ? 0.64725 0.84824 0.62107 0.03210  0.04852  0.04185  99  VAL A CA  
756  C C   . VAL A 99  ? 0.58936 0.79017 0.54823 0.03564  0.04675  0.04320  99  VAL A C   
757  O O   . VAL A 99  ? 0.61137 0.81264 0.56906 0.02998  0.04773  0.05103  99  VAL A O   
758  C CB  . VAL A 99  ? 0.55067 0.77109 0.53217 0.02723  0.05606  0.04609  99  VAL A CB  
759  C CG1 . VAL A 99  ? 0.65141 0.88992 0.62371 0.03433  0.06009  0.04280  99  VAL A CG1 
760  C CG2 . VAL A 99  ? 0.58272 0.80356 0.57801 0.02401  0.05724  0.04401  99  VAL A CG2 
761  N N   . THR A 100 ? 0.63789 0.83785 0.58482 0.04510  0.04415  0.03554  100 THR A N   
762  C CA  . THR A 100 ? 0.60696 0.80893 0.53762 0.04971  0.04303  0.03533  100 THR A CA  
763  C C   . THR A 100 ? 0.58831 0.80541 0.51068 0.05835  0.04720  0.02905  100 THR A C   
764  O O   . THR A 100 ? 0.53443 0.74801 0.45513 0.06558  0.04512  0.02070  100 THR A O   
765  C CB  . THR A 100 ? 0.62966 0.81220 0.55203 0.05300  0.03454  0.03179  100 THR A CB  
766  O OG1 . THR A 100 ? 0.66438 0.83589 0.59241 0.04508  0.03136  0.03937  100 THR A OG1 
767  C CG2 . THR A 100 ? 0.70861 0.89364 0.61210 0.06018  0.03308  0.02834  100 THR A CG2 
768  N N   . LEU A 101 ? 0.64616 0.88006 0.56365 0.05772  0.05332  0.03329  101 LEU A N   
769  C CA  . LEU A 101 ? 0.46691 0.71705 0.37703 0.06590  0.05831  0.02810  101 LEU A CA  
770  C C   . LEU A 101 ? 0.50433 0.74492 0.39924 0.07640  0.05342  0.01893  101 LEU A C   
771  O O   . LEU A 101 ? 0.55084 0.77962 0.43389 0.07730  0.04837  0.01902  101 LEU A O   
772  C CB  . LEU A 101 ? 0.50972 0.77669 0.41401 0.06365  0.06499  0.03475  101 LEU A CB  
773  C CG  . LEU A 101 ? 0.61367 0.89282 0.53242 0.05356  0.07099  0.04380  101 LEU A CG  
774  C CD1 . LEU A 101 ? 0.58255 0.87870 0.49393 0.05252  0.07787  0.04983  101 LEU A CD1 
775  C CD2 . LEU A 101 ? 0.61216 0.90117 0.54572 0.05322  0.07427  0.04080  101 LEU A CD2 
776  N N   . GLY A 102 ? 0.47286 0.71802 0.36840 0.08424  0.05457  0.01098  102 GLY A N   
777  C CA  . GLY A 102 ? 0.52689 0.76286 0.40876 0.09462  0.05037  0.00165  102 GLY A CA  
778  C C   . GLY A 102 ? 0.68091 0.89510 0.56511 0.09548  0.04218  -0.00317 102 GLY A C   
779  O O   . GLY A 102 ? 0.63381 0.83983 0.50839 0.10422  0.03871  -0.01157 102 GLY A O   
780  N N   . GLN A 103 ? 0.69382 0.89804 0.59041 0.08679  0.03920  0.00189  103 GLN A N   
781  C CA  . GLN A 103 ? 0.61645 0.80049 0.51655 0.08712  0.03197  -0.00206 103 GLN A CA  
782  C C   . GLN A 103 ? 0.67902 0.86458 0.59311 0.08702  0.03349  -0.00453 103 GLN A C   
783  O O   . GLN A 103 ? 0.46039 0.65770 0.38646 0.08118  0.03848  0.00045  103 GLN A O   
784  C CB  . GLN A 103 ? 0.65060 0.82132 0.55534 0.07826  0.02746  0.00478  103 GLN A CB  
785  N N   . PRO A 104 ? 0.51224 0.68571 0.42476 0.09320  0.02908  -0.01203 104 PRO A N   
786  C CA  . PRO A 104 ? 0.59195 0.76663 0.51634 0.09395  0.03025  -0.01470 104 PRO A CA  
787  C C   . PRO A 104 ? 0.62609 0.79642 0.56574 0.08366  0.03029  -0.00824 104 PRO A C   
788  O O   . PRO A 104 ? 0.64690 0.80381 0.58820 0.07784  0.02643  -0.00427 104 PRO A O   
789  C CB  . PRO A 104 ? 0.58606 0.74366 0.50423 0.10141  0.02416  -0.02284 104 PRO A CB  
790  C CG  . PRO A 104 ? 0.71423 0.85760 0.62190 0.10060  0.01852  -0.02245 104 PRO A CG  
791  C CD  . PRO A 104 ? 0.63401 0.79097 0.53387 0.09922  0.02240  -0.01812 104 PRO A CD  
792  N N   . ASN A 105 ? 0.54204 0.72398 0.49290 0.08156  0.03468  -0.00729 105 ASN A N   
793  C CA  . ASN A 105 ? 0.46706 0.64582 0.43218 0.07210  0.03538  -0.00186 105 ASN A CA  
794  C C   . ASN A 105 ? 0.43142 0.61678 0.40550 0.07397  0.03733  -0.00530 105 ASN A C   
795  O O   . ASN A 105 ? 0.45890 0.65089 0.42855 0.08267  0.03791  -0.01147 105 ASN A O   
796  C CB  . ASN A 105 ? 0.51839 0.70851 0.48796 0.06347  0.03998  0.00673  105 ASN A CB  
797  C CG  . ASN A 105 ? 0.53459 0.71459 0.51558 0.05333  0.03909  0.01291  105 ASN A CG  
798  O OD1 . ASN A 105 ? 0.54824 0.72012 0.53764 0.05170  0.03761  0.01116  105 ASN A OD1 
799  N ND2 . ASN A 105 ? 0.34089 0.52104 0.32182 0.04669  0.04013  0.02027  105 ASN A ND2 
800  N N   . ILE A 106 ? 0.51048 0.69369 0.49700 0.06588  0.03824  -0.00129 106 ILE A N   
801  C CA  . ILE A 106 ? 0.47474 0.66310 0.47022 0.06634  0.03953  -0.00393 106 ILE A CA  
802  C C   . ILE A 106 ? 0.45743 0.65609 0.46471 0.05633  0.04384  0.00247  106 ILE A C   
803  O O   . ILE A 106 ? 0.39657 0.58590 0.40865 0.04799  0.04340  0.00795  106 ILE A O   
804  C CB  . ILE A 106 ? 0.38358 0.55240 0.38132 0.06765  0.03457  -0.00757 106 ILE A CB  
805  C CG1 . ILE A 106 ? 0.38518 0.54207 0.37150 0.07692  0.02993  -0.01380 106 ILE A CG1 
806  C CG2 . ILE A 106 ? 0.38572 0.56074 0.39163 0.06835  0.03585  -0.01017 106 ILE A CG2 
807  C CD1 . ILE A 106 ? 0.42440 0.56193 0.41284 0.07824  0.02524  -0.01707 106 ILE A CD1 
808  N N   . LEU A 107 ? 0.43905 0.65667 0.45137 0.05715  0.04791  0.00176  107 LEU A N   
809  C CA  . LEU A 107 ? 0.37262 0.60010 0.39689 0.04775  0.05158  0.00686  107 LEU A CA  
810  C C   . LEU A 107 ? 0.45025 0.66929 0.48248 0.04579  0.04928  0.00437  107 LEU A C   
811  O O   . LEU A 107 ? 0.42863 0.64638 0.45899 0.05330  0.04702  -0.00173 107 LEU A O   
812  C CB  . LEU A 107 ? 0.35695 0.60983 0.38380 0.04894  0.05692  0.00760  107 LEU A CB  
813  C CG  . LEU A 107 ? 0.64101 0.90563 0.66889 0.04207  0.06172  0.01494  107 LEU A CG  
814  C CD1 . LEU A 107 ? 0.41936 0.67489 0.43557 0.04421  0.06037  0.01664  107 LEU A CD1 
815  C CD2 . LEU A 107 ? 0.46318 0.75360 0.49387 0.04426  0.06716  0.01514  107 LEU A CD2 
816  N N   . ILE A 108 ? 0.44170 0.65429 0.48224 0.03582  0.04991  0.00918  108 ILE A N   
817  C CA  . ILE A 108 ? 0.41267 0.61483 0.45992 0.03283  0.04786  0.00745  108 ILE A CA  
818  C C   . ILE A 108 ? 0.41472 0.63011 0.47250 0.02442  0.05150  0.01082  108 ILE A C   
819  O O   . ILE A 108 ? 0.46596 0.68485 0.52778 0.01613  0.05452  0.01700  108 ILE A O   
820  C CB  . ILE A 108 ? 0.41848 0.59743 0.46562 0.02875  0.04492  0.00956  108 ILE A CB  
821  C CG1 . ILE A 108 ? 0.46025 0.62636 0.49748 0.03687  0.04078  0.00594  108 ILE A CG1 
822  C CG2 . ILE A 108 ? 0.31253 0.48121 0.36634 0.02521  0.04364  0.00813  108 ILE A CG2 
823  C CD1 . ILE A 108 ? 0.39761 0.54244 0.43512 0.03319  0.03786  0.00847  108 ILE A CD1 
824  N N   . CYS A 109 ? 0.31848 0.54120 0.38063 0.02647  0.05102  0.00689  109 CYS A N   
825  C CA  . CYS A 109 ? 0.33735 0.57256 0.40968 0.01862  0.05362  0.00921  109 CYS A CA  
826  C C   . CYS A 109 ? 0.34514 0.56601 0.42140 0.01538  0.05084  0.00715  109 CYS A C   
827  O O   . CYS A 109 ? 0.31094 0.52978 0.38539 0.02193  0.04799  0.00177  109 CYS A O   
828  C CB  . CYS A 109 ? 0.39463 0.65375 0.46937 0.02349  0.05552  0.00671  109 CYS A CB  
829  S SG  . CYS A 109 ? 0.47185 0.74823 0.55989 0.01364  0.05812  0.00934  109 CYS A SG  
830  N N   . LEU A 110 ? 0.35780 0.56825 0.43891 0.00557  0.05181  0.01151  110 LEU A N   
831  C CA  . LEU A 110 ? 0.30696 0.50330 0.39155 0.00149  0.04989  0.01003  110 LEU A CA  
832  C C   . LEU A 110 ? 0.35766 0.56784 0.45065 -0.00524 0.05153  0.01049  110 LEU A C   
833  O O   . LEU A 110 ? 0.35013 0.56976 0.44876 -0.01332 0.05488  0.01530  110 LEU A O   
834  C CB  . LEU A 110 ? 0.36216 0.53867 0.44736 -0.00511 0.05020  0.01427  110 LEU A CB  
835  C CG  . LEU A 110 ? 0.46782 0.63032 0.55762 -0.01177 0.04974  0.01418  110 LEU A CG  
836  C CD1 . LEU A 110 ? 0.26696 0.41721 0.35267 -0.00514 0.04608  0.00849  110 LEU A CD1 
837  C CD2 . LEU A 110 ? 0.34562 0.49230 0.43730 -0.01881 0.05125  0.01959  110 LEU A CD2 
838  N N   . VAL A 111 ? 0.35026 0.56171 0.44399 -0.00201 0.04898  0.00563  111 VAL A N   
839  C CA  . VAL A 111 ? 0.36113 0.58239 0.46247 -0.00874 0.04935  0.00542  111 VAL A CA  
840  C C   . VAL A 111 ? 0.37469 0.57521 0.47585 -0.01325 0.04748  0.00432  111 VAL A C   
841  O O   . VAL A 111 ? 0.36005 0.54924 0.45626 -0.00691 0.04433  0.00005  111 VAL A O   
842  C CB  . VAL A 111 ? 0.33635 0.57592 0.43883 -0.00184 0.04767  0.00096  111 VAL A CB  
843  C CG1 . VAL A 111 ? 0.26127 0.51418 0.37267 -0.00988 0.04805  0.00153  111 VAL A CG1 
844  C CG2 . VAL A 111 ? 0.41916 0.67622 0.51982 0.00500  0.04966  0.00135  111 VAL A CG2 
845  N N   . ASP A 112 ? 0.41759 0.61253 0.52381 -0.02403 0.04966  0.00823  112 ASP A N   
846  C CA  . ASP A 112 ? 0.32151 0.49573 0.42738 -0.02897 0.04881  0.00773  112 ASP A CA  
847  C C   . ASP A 112 ? 0.35633 0.53661 0.46764 -0.03640 0.04847  0.00645  112 ASP A C   
848  O O   . ASP A 112 ? 0.41180 0.61207 0.52890 -0.03995 0.04943  0.00738  112 ASP A O   
849  C CB  . ASP A 112 ? 0.37592 0.53560 0.48267 -0.03528 0.05152  0.01312  112 ASP A CB  
850  C CG  . ASP A 112 ? 0.34431 0.47915 0.44825 -0.03602 0.05056  0.01220  112 ASP A CG  
851  O OD1 . ASP A 112 ? 0.37045 0.49902 0.47158 -0.03263 0.04804  0.00751  112 ASP A OD1 
852  O OD2 . ASP A 112 ? 0.47973 0.60145 0.58437 -0.03986 0.05247  0.01642  112 ASP A OD2 
853  N N   . ASN A 113 ? 0.34116 0.50383 0.45045 -0.03881 0.04707  0.00430  113 ASN A N   
854  C CA  . ASN A 113 ? 0.33538 0.49979 0.44809 -0.04597 0.04618  0.00246  113 ASN A CA  
855  C C   . ASN A 113 ? 0.29293 0.47827 0.40750 -0.04205 0.04338  -0.00119 113 ASN A C   
856  O O   . ASN A 113 ? 0.40645 0.60760 0.52766 -0.04859 0.04368  -0.00044 113 ASN A O   
857  C CB  . ASN A 113 ? 0.32861 0.49447 0.44802 -0.05813 0.04951  0.00705  113 ASN A CB  
858  C CG  . ASN A 113 ? 0.51800 0.68114 0.63982 -0.06629 0.04840  0.00485  113 ASN A CG  
859  O OD1 . ASN A 113 ? 0.58289 0.76236 0.71105 -0.07269 0.04852  0.00550  113 ASN A OD1 
860  N ND2 . ASN A 113 ? 0.54600 0.68870 0.66258 -0.06605 0.04726  0.00212  113 ASN A ND2 
861  N N   . ILE A 114 ? 0.29081 0.47626 0.39985 -0.03119 0.04053  -0.00502 114 ILE A N   
862  C CA  . ILE A 114 ? 0.28004 0.48439 0.39041 -0.02567 0.03762  -0.00854 114 ILE A CA  
863  C C   . ILE A 114 ? 0.34962 0.54648 0.45779 -0.02707 0.03416  -0.01242 114 ILE A C   
864  O O   . ILE A 114 ? 0.38870 0.56615 0.48985 -0.02322 0.03274  -0.01462 114 ILE A O   
865  C CB  . ILE A 114 ? 0.24853 0.45643 0.35361 -0.01276 0.03629  -0.01077 114 ILE A CB  
866  C CG1 . ILE A 114 ? 0.21977 0.43374 0.32544 -0.01125 0.03960  -0.00716 114 ILE A CG1 
867  C CG2 . ILE A 114 ? 0.25703 0.48459 0.36401 -0.00659 0.03338  -0.01424 114 ILE A CG2 
868  C CD1 . ILE A 114 ? 0.24982 0.46289 0.34874 0.00112  0.03832  -0.00963 114 ILE A CD1 
869  N N   . PHE A 115 ? 0.41966 0.63195 0.53372 -0.03269 0.03277  -0.01314 115 PHE A N   
870  C CA  . PHE A 115 ? 0.44959 0.65913 0.56080 -0.03188 0.02852  -0.01738 115 PHE A CA  
871  C C   . PHE A 115 ? 0.44401 0.67855 0.56303 -0.03506 0.02632  -0.01812 115 PHE A C   
872  O O   . PHE A 115 ? 0.38048 0.62643 0.50750 -0.04431 0.02845  -0.01514 115 PHE A O   
873  C CB  . PHE A 115 ? 0.32395 0.51119 0.43151 -0.03980 0.02881  -0.01781 115 PHE A CB  
874  C CG  . PHE A 115 ? 0.33831 0.51620 0.43901 -0.03605 0.02473  -0.02231 115 PHE A CG  
875  C CD1 . PHE A 115 ? 0.30410 0.46661 0.39642 -0.02664 0.02379  -0.02421 115 PHE A CD1 
876  C CD2 . PHE A 115 ? 0.33946 0.52438 0.44191 -0.04190 0.02161  -0.02455 115 PHE A CD2 
877  C CE1 . PHE A 115 ? 0.29449 0.44830 0.37996 -0.02301 0.02021  -0.02797 115 PHE A CE1 
878  C CE2 . PHE A 115 ? 0.35738 0.53381 0.45259 -0.03825 0.01767  -0.02852 115 PHE A CE2 
879  C CZ  . PHE A 115 ? 0.44947 0.61025 0.53603 -0.02866 0.01716  -0.03009 115 PHE A CZ  
880  N N   . PRO A 116 ? 0.34095 0.58508 0.45842 -0.02754 0.02201  -0.02177 116 PRO A N   
881  C CA  . PRO A 116 ? 0.32899 0.56132 0.43735 -0.01607 0.01941  -0.02508 116 PRO A CA  
882  C C   . PRO A 116 ? 0.39315 0.62794 0.49931 -0.00572 0.02129  -0.02440 116 PRO A C   
883  O O   . PRO A 116 ? 0.34380 0.59367 0.45579 -0.00657 0.02423  -0.02168 116 PRO A O   
884  C CB  . PRO A 116 ? 0.40930 0.65702 0.51924 -0.01256 0.01435  -0.02827 116 PRO A CB  
885  C CG  . PRO A 116 ? 0.39011 0.66458 0.51155 -0.01786 0.01508  -0.02620 116 PRO A CG  
886  C CD  . PRO A 116 ? 0.40971 0.67820 0.53517 -0.03017 0.01919  -0.02260 116 PRO A CD  
887  N N   . PRO A 117 ? 0.29837 0.51807 0.39585 0.00373  0.01970  -0.02682 117 PRO A N   
888  C CA  . PRO A 117 ? 0.31372 0.53429 0.40818 0.01368  0.02102  -0.02675 117 PRO A CA  
889  C C   . PRO A 117 ? 0.37771 0.62218 0.47569 0.02204  0.01965  -0.02820 117 PRO A C   
890  O O   . PRO A 117 ? 0.31726 0.56029 0.41015 0.03273  0.01695  -0.03124 117 PRO A O   
891  C CB  . PRO A 117 ? 0.34705 0.54404 0.43165 0.02039  0.01915  -0.02917 117 PRO A CB  
892  C CG  . PRO A 117 ? 0.35326 0.54531 0.43589 0.01767  0.01581  -0.03144 117 PRO A CG  
893  C CD  . PRO A 117 ? 0.38573 0.58482 0.47527 0.00500  0.01707  -0.02945 117 PRO A CD  
894  N N   . VAL A 118 ? 0.27416 0.54065 0.38111 0.01731  0.02175  -0.02584 118 VAL A N   
895  C CA  . VAL A 118 ? 0.32317 0.61483 0.43513 0.02455  0.02152  -0.02653 118 VAL A CA  
896  C C   . VAL A 118 ? 0.33086 0.63576 0.44863 0.02039  0.02650  -0.02262 118 VAL A C   
897  O O   . VAL A 118 ? 0.41069 0.72410 0.53607 0.00944  0.02831  -0.01958 118 VAL A O   
898  C CB  . VAL A 118 ? 0.42706 0.73708 0.54609 0.02226  0.01805  -0.02776 118 VAL A CB  
899  C CG1 . VAL A 118 ? 0.45539 0.79340 0.58151 0.02902  0.01872  -0.02767 118 VAL A CG1 
900  C CG2 . VAL A 118 ? 0.29439 0.59186 0.40671 0.02705  0.01290  -0.03147 118 VAL A CG2 
901  N N   . VAL A 119 ? 0.26464 0.57091 0.37845 0.02886  0.02872  -0.02265 119 VAL A N   
902  C CA  . VAL A 119 ? 0.34840 0.66350 0.46547 0.02504  0.03368  -0.01868 119 VAL A CA  
903  C C   . VAL A 119 ? 0.33645 0.66583 0.45173 0.03649  0.03529  -0.01991 119 VAL A C   
904  O O   . VAL A 119 ? 0.34873 0.67269 0.45749 0.04768  0.03283  -0.02381 119 VAL A O   
905  C CB  . VAL A 119 ? 0.33646 0.62816 0.44787 0.01986  0.03562  -0.01628 119 VAL A CB  
906  C CG1 . VAL A 119 ? 0.39770 0.67445 0.49892 0.03030  0.03499  -0.01853 119 VAL A CG1 
907  C CG2 . VAL A 119 ? 0.26080 0.56129 0.37776 0.01106  0.04035  -0.01100 119 VAL A CG2 
908  N N   . ASN A 120 ? 0.37593 0.72371 0.49695 0.03363  0.03966  -0.01651 120 ASN A N   
909  C CA  . ASN A 120 ? 0.45573 0.81575 0.57407 0.04333  0.04251  -0.01701 120 ASN A CA  
910  C C   . ASN A 120 ? 0.40984 0.76202 0.52405 0.03948  0.04658  -0.01333 120 ASN A C   
911  O O   . ASN A 120 ? 0.36506 0.72236 0.48531 0.02868  0.04955  -0.00860 120 ASN A O   
912  C CB  . ASN A 120 ? 0.61300 1.00409 0.74168 0.04424  0.04468  -0.01592 120 ASN A CB  
913  C CG  . ASN A 120 ? 0.54909 0.95047 0.68075 0.05191  0.04064  -0.01990 120 ASN A CG  
914  O OD1 . ASN A 120 ? 0.46438 0.85093 0.58832 0.06003  0.03681  -0.02398 120 ASN A OD1 
915  N ND2 . ASN A 120 ? 0.75218 1.17955 0.89548 0.04933  0.04142  -0.01845 120 ASN A ND2 
916  N N   . ILE A 121 ? 0.36944 0.70916 0.47332 0.04814  0.04651  -0.01539 121 ILE A N   
917  C CA  . ILE A 121 ? 0.44008 0.77335 0.53884 0.04612  0.04987  -0.01220 121 ILE A CA  
918  C C   . ILE A 121 ? 0.51093 0.85594 0.60435 0.05730  0.05209  -0.01416 121 ILE A C   
919  O O   . ILE A 121 ? 0.50288 0.84049 0.58889 0.06824  0.04948  -0.01905 121 ILE A O   
920  C CB  . ILE A 121 ? 0.47574 0.78006 0.56629 0.04484  0.04742  -0.01258 121 ILE A CB  
921  C CG1 . ILE A 121 ? 0.41777 0.70973 0.51290 0.03528  0.04525  -0.01152 121 ILE A CG1 
922  C CG2 . ILE A 121 ? 0.39770 0.69684 0.48423 0.04136  0.05060  -0.00847 121 ILE A CG2 
923  C CD1 . ILE A 121 ? 0.27951 0.54374 0.36753 0.03486  0.04287  -0.01218 121 ILE A CD1 
924  N N   . THR A 122 ? 0.48937 0.85212 0.58618 0.05460  0.05709  -0.01035 122 THR A N   
925  C CA  . THR A 122 ? 0.51512 0.89134 0.60710 0.06465  0.06018  -0.01187 122 THR A CA  
926  C C   . THR A 122 ? 0.39849 0.77521 0.48652 0.06033  0.06460  -0.00719 122 THR A C   
927  O O   . THR A 122 ? 0.46462 0.84683 0.55954 0.04915  0.06732  -0.00157 122 THR A O   
928  C CB  . THR A 122 ? 0.57589 0.98089 0.67761 0.06775  0.06251  -0.01217 122 THR A CB  
929  O OG1 . THR A 122 ? 0.65679 1.07555 0.77042 0.05537  0.06499  -0.00683 122 THR A OG1 
930  C CG2 . THR A 122 ? 0.45787 0.86271 0.56158 0.07481  0.05777  -0.01728 122 THR A CG2 
931  N N   . TRP A 123 ? 0.31402 0.68445 0.39052 0.06917  0.06514  -0.00953 123 TRP A N   
932  C CA  . TRP A 123 ? 0.47134 0.84220 0.54204 0.06664  0.06901  -0.00550 123 TRP A CA  
933  C C   . TRP A 123 ? 0.48930 0.88661 0.56209 0.07069  0.07489  -0.00419 123 TRP A C   
934  O O   . TRP A 123 ? 0.55295 0.96212 0.62513 0.08104  0.07536  -0.00862 123 TRP A O   
935  C CB  . TRP A 123 ? 0.43451 0.78420 0.49083 0.07362  0.06621  -0.00874 123 TRP A CB  
936  C CG  . TRP A 123 ? 0.46884 0.79254 0.52305 0.06847  0.06142  -0.00860 123 TRP A CG  
937  C CD1 . TRP A 123 ? 0.47788 0.78555 0.53031 0.07244  0.05632  -0.01326 123 TRP A CD1 
938  C CD2 . TRP A 123 ? 0.54661 0.85746 0.60047 0.05864  0.06156  -0.00326 123 TRP A CD2 
939  N NE1 . TRP A 123 ? 0.54256 0.82861 0.59380 0.06563  0.05355  -0.01122 123 TRP A NE1 
940  C CE2 . TRP A 123 ? 0.45024 0.73786 0.50255 0.05727  0.05659  -0.00514 123 TRP A CE2 
941  C CE3 . TRP A 123 ? 0.47055 0.78732 0.52537 0.05103  0.06554  0.00320  123 TRP A CE3 
942  C CZ2 . TRP A 123 ? 0.31402 0.58475 0.36626 0.04889  0.05556  -0.00093 123 TRP A CZ2 
943  C CZ3 . TRP A 123 ? 0.45914 0.75862 0.51357 0.04271  0.06420  0.00747  123 TRP A CZ3 
944  C CH2 . TRP A 123 ? 0.44715 0.72409 0.50058 0.04183  0.05928  0.00531  123 TRP A CH2 
945  N N   . LEU A 124 ? 0.39282 0.79917 0.46808 0.06270  0.07962  0.00214  124 LEU A N   
946  C CA  . LEU A 124 ? 0.44350 0.87467 0.52053 0.06534  0.08606  0.00447  124 LEU A CA  
947  C C   . LEU A 124 ? 0.57862 1.00441 0.64385 0.06603  0.08906  0.00723  124 LEU A C   
948  O O   . LEU A 124 ? 0.47749 0.88649 0.53913 0.05864  0.08752  0.01081  124 LEU A O   
949  C CB  . LEU A 124 ? 0.32349 0.77453 0.41573 0.05438  0.08977  0.01036  124 LEU A CB  
950  C CG  . LEU A 124 ? 0.52993 0.98880 0.63450 0.05271  0.08673  0.00806  124 LEU A CG  
951  C CD1 . LEU A 124 ? 0.42213 0.89594 0.54101 0.03947  0.08956  0.01430  124 LEU A CD1 
952  C CD2 . LEU A 124 ? 0.38198 0.85808 0.48758 0.06529  0.08744  0.00300  124 LEU A CD2 
953  N N   . SER A 125 ? 0.57266 1.01278 0.63168 0.07519  0.09332  0.00557  125 SER A N   
954  C CA  . SER A 125 ? 0.62476 1.06493 0.67281 0.07587  0.09726  0.00867  125 SER A CA  
955  C C   . SER A 125 ? 0.66412 1.13330 0.71690 0.07785  0.10502  0.01143  125 SER A C   
956  O O   . SER A 125 ? 0.56321 1.04549 0.61529 0.08860  0.10680  0.00664  125 SER A O   
957  C CB  . SER A 125 ? 0.62316 1.04636 0.65418 0.08696  0.09409  0.00257  125 SER A CB  
958  O OG  . SER A 125 ? 0.63833 1.06149 0.65801 0.08721  0.09754  0.00565  125 SER A OG  
959  N N   . ASN A 126 ? 0.61773 1.09680 0.67559 0.06761  0.10980  0.01934  126 ASN A N   
960  C CA  . ASN A 126 ? 0.84566 1.35135 0.90945 0.06735  0.11721  0.02319  126 ASN A CA  
961  C C   . ASN A 126 ? 0.92734 1.44580 1.00404 0.06915  0.11570  0.02046  126 ASN A C   
962  O O   . ASN A 126 ? 1.03731 1.56752 1.11342 0.07629  0.11780  0.01858  126 ASN A O   
963  C CB  . ASN A 126 ? 0.77074 1.27764 0.81908 0.07737  0.12037  0.02123  126 ASN A CB  
964  N N   . GLY A 127 ? 0.71972 1.23580 0.80805 0.06263  0.11194  0.02032  127 GLY A N   
965  C CA  . GLY A 127 ? 0.63944 1.16668 0.73995 0.06364  0.10963  0.01784  127 GLY A CA  
966  C C   . GLY A 127 ? 0.71328 1.23644 0.80910 0.07706  0.10565  0.00955  127 GLY A C   
967  O O   . GLY A 127 ? 0.74591 1.27392 0.85151 0.07735  0.10215  0.00715  127 GLY A O   
968  N N   . HIS A 128 ? 0.81140 1.32495 0.89213 0.08810  0.10576  0.00509  128 HIS A N   
969  C CA  . HIS A 128 ? 0.77433 1.28112 0.84945 0.10105  0.10173  -0.00286 128 HIS A CA  
970  C C   . HIS A 128 ? 0.65539 1.14446 0.72980 0.10069  0.09611  -0.00638 128 HIS A C   
971  O O   . HIS A 128 ? 0.52659 0.99583 0.59555 0.09322  0.09365  -0.00403 128 HIS A O   
972  C CB  . HIS A 128 ? 0.67160 1.17211 0.73000 0.11257  0.10346  -0.00669 128 HIS A CB  
973  C CG  . HIS A 128 ? 0.93333 1.45004 0.99140 0.11517  0.10864  -0.00440 128 HIS A CG  
974  N ND1 . HIS A 128 ? 0.97660 1.50663 1.04128 0.10528  0.11363  0.00304  128 HIS A ND1 
975  C CD2 . HIS A 128 ? 0.91663 1.43788 0.96866 0.12655  0.10977  -0.00847 128 HIS A CD2 
976  C CE1 . HIS A 128 ? 1.13956 1.68225 1.20242 0.11062  0.11778  0.00341  128 HIS A CE1 
977  N NE2 . HIS A 128 ? 1.14387 1.68177 1.19916 0.12356  0.11564  -0.00352 128 HIS A NE2 
978  N N   . SER A 129 ? 0.54032 1.02846 0.61848 0.10733  0.09186  -0.01157 129 SER A N   
979  C CA  . SER A 129 ? 0.52787 0.99176 0.60334 0.10634  0.08450  -0.01491 129 SER A CA  
980  C C   . SER A 129 ? 0.68631 1.12782 0.74483 0.11584  0.08165  -0.02020 129 SER A C   
981  O O   . SER A 129 ? 0.67927 1.12599 0.73057 0.12821  0.08331  -0.02476 129 SER A O   
982  C CB  . SER A 129 ? 0.39769 0.86951 0.48305 0.11007  0.08107  -0.01816 129 SER A CB  
983  O OG  . SER A 129 ? 0.82928 1.28019 0.91518 0.10476  0.07466  -0.01926 129 SER A OG  
984  N N   . VAL A 130 ? 0.58016 0.99668 0.63258 0.11004  0.07738  -0.01964 130 VAL A N   
985  C CA  . VAL A 130 ? 0.53827 0.93186 0.57536 0.11718  0.07396  -0.02416 130 VAL A CA  
986  C C   . VAL A 130 ? 0.45001 0.82559 0.48661 0.12084  0.06734  -0.02903 130 VAL A C   
987  O O   . VAL A 130 ? 0.65642 1.02334 0.70016 0.11228  0.06416  -0.02694 130 VAL A O   
988  C CB  . VAL A 130 ? 0.59218 0.97030 0.62268 0.10867  0.07365  -0.01991 130 VAL A CB  
989  C CG1 . VAL A 130 ? 0.53241 0.88954 0.54684 0.11654  0.07029  -0.02467 130 VAL A CG1 
990  C CG2 . VAL A 130 ? 0.48948 0.88607 0.52212 0.10321  0.08031  -0.01384 130 VAL A CG2 
991  N N   . THR A 131 ? 0.64423 1.01338 0.67190 0.13352  0.06543  -0.03548 131 THR A N   
992  C CA  . THR A 131 ? 0.57587 0.92795 0.60202 0.13834  0.05941  -0.04024 131 THR A CA  
993  C C   . THR A 131 ? 0.50246 0.82811 0.51448 0.14295  0.05534  -0.04417 131 THR A C   
994  O O   . THR A 131 ? 0.59950 0.90518 0.61099 0.14035  0.05026  -0.04518 131 THR A O   
995  C CB  . THR A 131 ? 0.71366 1.08022 0.74306 0.14979  0.05987  -0.04465 131 THR A CB  
996  O OG1 . THR A 131 ? 0.73606 1.11225 0.75729 0.16012  0.06396  -0.04751 131 THR A OG1 
997  C CG2 . THR A 131 ? 0.62804 1.01852 0.67338 0.14425  0.06213  -0.04090 131 THR A CG2 
998  N N   . GLU A 132 ? 0.61665 0.94161 0.61712 0.14953  0.05743  -0.04639 132 GLU A N   
999  C CA  . GLU A 132 ? 0.62732 0.92750 0.61422 0.15345  0.05322  -0.05020 132 GLU A CA  
1000 C C   . GLU A 132 ? 0.60919 0.89365 0.59572 0.14173  0.05094  -0.04550 132 GLU A C   
1001 O O   . GLU A 132 ? 0.62607 0.92031 0.61716 0.13278  0.05435  -0.03956 132 GLU A O   
1002 C CB  . GLU A 132 ? 0.56409 0.86832 0.53816 0.16281  0.05614  -0.05370 132 GLU A CB  
1003 N N   . GLY A 133 ? 0.52058 0.78056 0.50208 0.14187  0.04525  -0.04796 133 GLY A N   
1004 C CA  . GLY A 133 ? 0.48178 0.72575 0.46331 0.13166  0.04276  -0.04374 133 GLY A CA  
1005 C C   . GLY A 133 ? 0.51952 0.76526 0.51418 0.12039  0.04292  -0.03839 133 GLY A C   
1006 O O   . GLY A 133 ? 0.53832 0.77775 0.53498 0.11079  0.04295  -0.03329 133 GLY A O   
1007 N N   . VAL A 134 ? 0.42587 0.67988 0.42929 0.12137  0.04292  -0.03941 134 VAL A N   
1008 C CA  . VAL A 134 ? 0.46932 0.72497 0.48464 0.11102  0.04287  -0.03507 134 VAL A CA  
1009 C C   . VAL A 134 ? 0.48731 0.72475 0.50317 0.11252  0.03786  -0.03809 134 VAL A C   
1010 O O   . VAL A 134 ? 0.55708 0.79286 0.56951 0.12228  0.03584  -0.04327 134 VAL A O   
1011 C CB  . VAL A 134 ? 0.49646 0.77814 0.52227 0.10952  0.04689  -0.03319 134 VAL A CB  
1012 C CG1 . VAL A 134 ? 0.38474 0.66598 0.42187 0.09863  0.04617  -0.02934 134 VAL A CG1 
1013 C CG2 . VAL A 134 ? 0.42479 0.72488 0.45032 0.10776  0.05244  -0.02969 134 VAL A CG2 
1014 N N   . SER A 135 ? 0.43264 0.65613 0.45257 0.10309  0.03609  -0.03471 135 SER A N   
1015 C CA  . SER A 135 ? 0.38342 0.59004 0.40465 0.10305  0.03201  -0.03667 135 SER A CA  
1016 C C   . SER A 135 ? 0.41949 0.62443 0.45016 0.09103  0.03273  -0.03178 135 SER A C   
1017 O O   . SER A 135 ? 0.39000 0.60393 0.42533 0.08289  0.03594  -0.02692 135 SER A O   
1018 C CB  . SER A 135 ? 0.35958 0.54216 0.37169 0.10659  0.02809  -0.03916 135 SER A CB  
1019 O OG  . SER A 135 ? 0.42519 0.59874 0.43642 0.09888  0.02836  -0.03493 135 SER A OG  
1020 N N   . GLU A 136 ? 0.38590 0.57881 0.41893 0.08999  0.02986  -0.03306 136 GLU A N   
1021 C CA  . GLU A 136 ? 0.46074 0.65039 0.50176 0.07896  0.03051  -0.02902 136 GLU A CA  
1022 C C   . GLU A 136 ? 0.38275 0.55090 0.42231 0.07876  0.02700  -0.03061 136 GLU A C   
1023 O O   . GLU A 136 ? 0.38279 0.54238 0.41680 0.08732  0.02407  -0.03492 136 GLU A O   
1024 C CB  . GLU A 136 ? 0.38979 0.60057 0.43957 0.07562  0.03259  -0.02795 136 GLU A CB  
1025 C CG  . GLU A 136 ? 0.48036 0.69400 0.53104 0.08187  0.02993  -0.03205 136 GLU A CG  
1026 C CD  . GLU A 136 ? 0.52460 0.75973 0.58471 0.07774  0.03147  -0.03072 136 GLU A CD  
1027 O OE1 . GLU A 136 ? 0.55754 0.80965 0.62275 0.07303  0.03511  -0.02750 136 GLU A OE1 
1028 O OE2 . GLU A 136 ? 0.49278 0.72789 0.55521 0.07904  0.02891  -0.03275 136 GLU A OE2 
1029 N N   . THR A 137 ? 0.32303 0.48217 0.36752 0.06888  0.02762  -0.02691 137 THR A N   
1030 C CA  . THR A 137 ? 0.40782 0.54822 0.45215 0.06722  0.02524  -0.02771 137 THR A CA  
1031 C C   . THR A 137 ? 0.43201 0.58029 0.48001 0.06761  0.02444  -0.02962 137 THR A C   
1032 O O   . THR A 137 ? 0.36434 0.53305 0.41682 0.06734  0.02583  -0.02958 137 THR A O   
1033 C CB  . THR A 137 ? 0.36449 0.49289 0.41282 0.05667  0.02671  -0.02300 137 THR A CB  
1034 O OG1 . THR A 137 ? 0.32406 0.46577 0.37995 0.04820  0.02951  -0.01992 137 THR A OG1 
1035 C CG2 . THR A 137 ? 0.34954 0.47270 0.39506 0.05570  0.02736  -0.02041 137 THR A CG2 
1036 N N   . SER A 138 ? 0.36017 0.49220 0.40630 0.06814  0.02212  -0.03111 138 SER A N   
1037 C CA  . SER A 138 ? 0.30084 0.43722 0.35032 0.06611  0.02124  -0.03206 138 SER A CA  
1038 C C   . SER A 138 ? 0.31753 0.45719 0.37408 0.05403  0.02375  -0.02816 138 SER A C   
1039 O O   . SER A 138 ? 0.31820 0.45728 0.37735 0.04770  0.02632  -0.02451 138 SER A O   
1040 C CB  . SER A 138 ? 0.28403 0.40059 0.32864 0.06954  0.01845  -0.03429 138 SER A CB  
1041 O OG  . SER A 138 ? 0.47092 0.58228 0.50885 0.08040  0.01604  -0.03780 138 SER A OG  
1042 N N   . PHE A 139 ? 0.30874 0.45109 0.36804 0.05075  0.02283  -0.02892 139 PHE A N   
1043 C CA  . PHE A 139 ? 0.34343 0.48365 0.40810 0.03921  0.02478  -0.02585 139 PHE A CA  
1044 C C   . PHE A 139 ? 0.27639 0.39168 0.33813 0.03577  0.02516  -0.02456 139 PHE A C   
1045 O O   . PHE A 139 ? 0.37790 0.47927 0.43486 0.03980  0.02307  -0.02688 139 PHE A O   
1046 C CB  . PHE A 139 ? 0.35804 0.50799 0.42564 0.03686  0.02317  -0.02751 139 PHE A CB  
1047 C CG  . PHE A 139 ? 0.34351 0.51995 0.41702 0.03717  0.02353  -0.02752 139 PHE A CG  
1048 C CD1 . PHE A 139 ? 0.28468 0.47332 0.36540 0.02809  0.02654  -0.02400 139 PHE A CD1 
1049 C CD2 . PHE A 139 ? 0.34496 0.53421 0.41728 0.04657  0.02103  -0.03078 139 PHE A CD2 
1050 C CE1 . PHE A 139 ? 0.36573 0.57939 0.45271 0.02804  0.02719  -0.02367 139 PHE A CE1 
1051 C CE2 . PHE A 139 ? 0.34179 0.55638 0.42056 0.04700  0.02163  -0.03055 139 PHE A CE2 
1052 C CZ  . PHE A 139 ? 0.27091 0.49801 0.35720 0.03757  0.02478  -0.02696 139 PHE A CZ  
1053 N N   . LEU A 140 ? 0.27091 0.38075 0.33563 0.02870  0.02796  -0.02061 140 LEU A N   
1054 C CA  . LEU A 140 ? 0.24753 0.33510 0.31096 0.02510  0.02885  -0.01870 140 LEU A CA  
1055 C C   . LEU A 140 ? 0.33349 0.41623 0.40100 0.01509  0.03082  -0.01686 140 LEU A C   
1056 O O   . LEU A 140 ? 0.29147 0.38690 0.36438 0.00820  0.03264  -0.01483 140 LEU A O   
1057 C CB  . LEU A 140 ? 0.30487 0.38835 0.36890 0.02412  0.03039  -0.01531 140 LEU A CB  
1058 C CG  . LEU A 140 ? 0.36468 0.45341 0.42403 0.03338  0.02857  -0.01719 140 LEU A CG  
1059 C CD1 . LEU A 140 ? 0.46853 0.55199 0.52785 0.03169  0.02965  -0.01370 140 LEU A CD1 
1060 C CD2 . LEU A 140 ? 0.41421 0.49143 0.46729 0.04220  0.02536  -0.02130 140 LEU A CD2 
1061 N N   . SER A 141 ? 0.31486 0.37885 0.37955 0.01429  0.03061  -0.01760 141 SER A N   
1062 C CA  . SER A 141 ? 0.27397 0.33166 0.34052 0.00615  0.03211  -0.01710 141 SER A CA  
1063 C C   . SER A 141 ? 0.31072 0.36164 0.38230 -0.00285 0.03582  -0.01255 141 SER A C   
1064 O O   . SER A 141 ? 0.33727 0.38206 0.40991 -0.00225 0.03702  -0.00964 141 SER A O   
1065 C CB  . SER A 141 ? 0.36072 0.39992 0.42170 0.00890  0.03114  -0.01933 141 SER A CB  
1066 O OG  . SER A 141 ? 0.33730 0.35804 0.39780 0.00887  0.03290  -0.01701 141 SER A OG  
1067 N N   . LYS A 142 ? 0.25891 0.31068 0.33344 -0.01128 0.03741  -0.01198 142 LYS A N   
1068 C CA  . LYS A 142 ? 0.36377 0.40640 0.44263 -0.02021 0.04109  -0.00799 142 LYS A CA  
1069 C C   . LYS A 142 ? 0.33184 0.35960 0.40852 -0.02490 0.04213  -0.00951 142 LYS A C   
1070 O O   . LYS A 142 ? 0.44831 0.47864 0.52126 -0.02353 0.03989  -0.01335 142 LYS A O   
1071 C CB  . LYS A 142 ? 0.27166 0.33122 0.35683 -0.02715 0.04265  -0.00526 142 LYS A CB  
1072 C CG  . LYS A 142 ? 0.26197 0.33912 0.34835 -0.02207 0.04169  -0.00440 142 LYS A CG  
1073 C CD  . LYS A 142 ? 0.41684 0.50038 0.50882 -0.02851 0.04475  0.00080  142 LYS A CD  
1074 C CE  . LYS A 142 ? 0.32202 0.41250 0.41938 -0.03866 0.04660  0.00214  142 LYS A CE  
1075 N NZ  . LYS A 142 ? 0.42964 0.52003 0.53199 -0.04560 0.05008  0.00794  142 LYS A NZ  
1076 N N   . SER A 143 ? 0.32608 0.33802 0.40482 -0.03024 0.04557  -0.00641 143 SER A N   
1077 C CA  . SER A 143 ? 0.29982 0.29492 0.37562 -0.03394 0.04724  -0.00783 143 SER A CA  
1078 C C   . SER A 143 ? 0.39027 0.39208 0.46661 -0.04157 0.04722  -0.00968 143 SER A C   
1079 O O   . SER A 143 ? 0.33901 0.32933 0.41086 -0.04368 0.04762  -0.01226 143 SER A O   
1080 C CB  . SER A 143 ? 0.32075 0.29810 0.39950 -0.03759 0.05133  -0.00379 143 SER A CB  
1081 O OG  . SER A 143 ? 0.46969 0.45147 0.55446 -0.04587 0.05390  -0.00025 143 SER A OG  
1082 N N   . ASP A 144 ? 0.30310 0.32296 0.38467 -0.04598 0.04682  -0.00841 144 ASP A N   
1083 C CA  . ASP A 144 ? 0.23489 0.26377 0.31747 -0.05297 0.04588  -0.01051 144 ASP A CA  
1084 C C   . ASP A 144 ? 0.27000 0.31557 0.35015 -0.04783 0.04127  -0.01457 144 ASP A C   
1085 O O   . ASP A 144 ? 0.36770 0.42529 0.44987 -0.05316 0.03966  -0.01618 144 ASP A O   
1086 C CB  . ASP A 144 ? 0.23457 0.27397 0.32495 -0.06153 0.04813  -0.00665 144 ASP A CB  
1087 C CG  . ASP A 144 ? 0.31466 0.37540 0.40941 -0.05805 0.04699  -0.00473 144 ASP A CG  
1088 O OD1 . ASP A 144 ? 0.43263 0.49930 0.52439 -0.04871 0.04455  -0.00644 144 ASP A OD1 
1089 O OD2 . ASP A 144 ? 0.38903 0.46038 0.49005 -0.06476 0.04879  -0.00144 144 ASP A OD2 
1090 N N   . HIS A 145 ? 0.27470 0.32138 0.35099 -0.03765 0.03902  -0.01608 145 HIS A N   
1091 C CA  . HIS A 145 ? 0.35996 0.41899 0.43284 -0.03073 0.03462  -0.01997 145 HIS A CA  
1092 C C   . HIS A 145 ? 0.35396 0.43866 0.43259 -0.02987 0.03297  -0.01956 145 HIS A C   
1093 O O   . HIS A 145 ? 0.40470 0.50217 0.48180 -0.02437 0.02934  -0.02255 145 HIS A O   
1094 C CB  . HIS A 145 ? 0.26253 0.31655 0.33048 -0.03355 0.03257  -0.02367 145 HIS A CB  
1095 C CG  . HIS A 145 ? 0.37113 0.40023 0.43341 -0.03530 0.03501  -0.02397 145 HIS A CG  
1096 N ND1 . HIS A 145 ? 0.30016 0.31358 0.35925 -0.02923 0.03665  -0.02285 145 HIS A ND1 
1097 C CD2 . HIS A 145 ? 0.33927 0.35639 0.39876 -0.04259 0.03642  -0.02514 145 HIS A CD2 
1098 C CE1 . HIS A 145 ? 0.37639 0.36991 0.43142 -0.03243 0.03923  -0.02312 145 HIS A CE1 
1099 N NE2 . HIS A 145 ? 0.44941 0.44434 0.50406 -0.04034 0.03924  -0.02466 145 HIS A NE2 
1100 N N   . SER A 146 ? 0.30439 0.39719 0.38962 -0.03481 0.03569  -0.01571 146 SER A N   
1101 C CA  . SER A 146 ? 0.34370 0.45931 0.43367 -0.03182 0.03500  -0.01472 146 SER A CA  
1102 C C   . SER A 146 ? 0.30839 0.42154 0.39499 -0.02174 0.03480  -0.01441 146 SER A C   
1103 O O   . SER A 146 ? 0.27461 0.36922 0.35601 -0.01768 0.03485  -0.01491 146 SER A O   
1104 C CB  . SER A 146 ? 0.29911 0.42404 0.39682 -0.04116 0.03822  -0.01043 146 SER A CB  
1105 O OG  . SER A 146 ? 0.41977 0.53101 0.51774 -0.04297 0.04163  -0.00645 146 SER A OG  
1106 N N   . PHE A 147 ? 0.23934 0.37118 0.32885 -0.01774 0.03465  -0.01362 147 PHE A N   
1107 C CA  . PHE A 147 ? 0.21388 0.34478 0.29953 -0.00797 0.03409  -0.01393 147 PHE A CA  
1108 C C   . PHE A 147 ? 0.32051 0.46155 0.41002 -0.00963 0.03687  -0.00993 147 PHE A C   
1109 O O   . PHE A 147 ? 0.24507 0.39813 0.34083 -0.01730 0.03904  -0.00708 147 PHE A O   
1110 C CB  . PHE A 147 ? 0.22940 0.37272 0.31221 0.00188  0.03061  -0.01806 147 PHE A CB  
1111 C CG  . PHE A 147 ? 0.31150 0.44392 0.38905 0.00521  0.02756  -0.02180 147 PHE A CG  
1112 C CD1 . PHE A 147 ? 0.30374 0.44169 0.38307 0.00015  0.02598  -0.02338 147 PHE A CD1 
1113 C CD2 . PHE A 147 ? 0.29408 0.41040 0.36463 0.01312  0.02615  -0.02362 147 PHE A CD2 
1114 C CE1 . PHE A 147 ? 0.33308 0.46055 0.40652 0.00322  0.02311  -0.02664 147 PHE A CE1 
1115 C CE2 . PHE A 147 ? 0.36116 0.46696 0.42637 0.01616  0.02362  -0.02663 147 PHE A CE2 
1116 C CZ  . PHE A 147 ? 0.27497 0.38634 0.34124 0.01135  0.02213  -0.02811 147 PHE A CZ  
1117 N N   . PHE A 148 ? 0.26196 0.39746 0.34730 -0.00252 0.03672  -0.00966 148 PHE A N   
1118 C CA  . PHE A 148 ? 0.31854 0.46626 0.40539 -0.00123 0.03856  -0.00688 148 PHE A CA  
1119 C C   . PHE A 148 ? 0.34058 0.49299 0.42175 0.01057  0.03633  -0.01019 148 PHE A C   
1120 O O   . PHE A 148 ? 0.26651 0.40900 0.34259 0.01732  0.03350  -0.01393 148 PHE A O   
1121 C CB  . PHE A 148 ? 0.31512 0.45027 0.40267 -0.00636 0.04114  -0.00202 148 PHE A CB  
1122 C CG  . PHE A 148 ? 0.24456 0.35909 0.32665 -0.00144 0.03973  -0.00262 148 PHE A CG  
1123 C CD1 . PHE A 148 ? 0.34040 0.43574 0.42157 -0.00373 0.03933  -0.00332 148 PHE A CD1 
1124 C CD2 . PHE A 148 ? 0.27373 0.38795 0.35179 0.00494  0.03899  -0.00222 148 PHE A CD2 
1125 C CE1 . PHE A 148 ? 0.31001 0.38708 0.38733 0.00035  0.03829  -0.00340 148 PHE A CE1 
1126 C CE2 . PHE A 148 ? 0.31151 0.40716 0.38540 0.00879  0.03741  -0.00256 148 PHE A CE2 
1127 C CZ  . PHE A 148 ? 0.35504 0.43244 0.42911 0.00644  0.03712  -0.00298 148 PHE A CZ  
1128 N N   . LYS A 149 ? 0.31330 0.48108 0.39513 0.01303  0.03781  -0.00878 149 LYS A N   
1129 C CA  . LYS A 149 ? 0.29311 0.46751 0.36950 0.02421  0.03617  -0.01207 149 LYS A CA  
1130 C C   . LYS A 149 ? 0.37124 0.55327 0.44664 0.02464  0.03863  -0.00900 149 LYS A C   
1131 O O   . LYS A 149 ? 0.36635 0.55987 0.44715 0.01744  0.04178  -0.00490 149 LYS A O   
1132 C CB  . LYS A 149 ? 0.31725 0.51080 0.39575 0.02903  0.03497  -0.01546 149 LYS A CB  
1133 C CG  . LYS A 149 ? 0.36323 0.56237 0.43577 0.04155  0.03331  -0.01937 149 LYS A CG  
1134 C CD  . LYS A 149 ? 0.35704 0.57820 0.43335 0.04592  0.03279  -0.02179 149 LYS A CD  
1135 C CE  . LYS A 149 ? 0.34210 0.55703 0.41596 0.05153  0.02883  -0.02604 149 LYS A CE  
1136 N NZ  . LYS A 149 ? 0.40735 0.61587 0.47321 0.06387  0.02667  -0.02996 149 LYS A NZ  
1137 N N   . ILE A 150 ? 0.32604 0.50118 0.39413 0.03292  0.03710  -0.01096 150 ILE A N   
1138 C CA  . ILE A 150 ? 0.34628 0.52495 0.41124 0.03392  0.03881  -0.00836 150 ILE A CA  
1139 C C   . ILE A 150 ? 0.36383 0.55427 0.42312 0.04480  0.03809  -0.01238 150 ILE A C   
1140 O O   . ILE A 150 ? 0.29091 0.47321 0.34482 0.05315  0.03497  -0.01709 150 ILE A O   
1141 C CB  . ILE A 150 ? 0.23978 0.39666 0.30070 0.03281  0.03744  -0.00661 150 ILE A CB  
1142 C CG1 . ILE A 150 ? 0.23195 0.37852 0.29909 0.02198  0.03900  -0.00207 150 ILE A CG1 
1143 C CG2 . ILE A 150 ? 0.31232 0.47261 0.36812 0.03553  0.03819  -0.00479 150 ILE A CG2 
1144 C CD1 . ILE A 150 ? 0.27477 0.39903 0.33955 0.02104  0.03744  -0.00056 150 ILE A CD1 
1145 N N   . SER A 151 ? 0.26297 0.47226 0.32339 0.04478  0.04124  -0.01045 151 SER A N   
1146 C CA  . SER A 151 ? 0.42374 0.64476 0.47834 0.05505  0.04144  -0.01389 151 SER A CA  
1147 C C   . SER A 151 ? 0.36991 0.58747 0.41758 0.05626  0.04249  -0.01185 151 SER A C   
1148 O O   . SER A 151 ? 0.37554 0.59195 0.42556 0.04813  0.04462  -0.00644 151 SER A O   
1149 C CB  . SER A 151 ? 0.34074 0.58794 0.40157 0.05535  0.04454  -0.01361 151 SER A CB  
1150 O OG  . SER A 151 ? 0.41878 0.67670 0.47393 0.06637  0.04490  -0.01745 151 SER A OG  
1151 N N   . TYR A 152 ? 0.32658 0.54195 0.36523 0.06656  0.04081  -0.01625 152 TYR A N   
1152 C CA  . TYR A 152 ? 0.35773 0.56842 0.38786 0.06893  0.04093  -0.01536 152 TYR A CA  
1153 C C   . TYR A 152 ? 0.47777 0.70674 0.50284 0.07694  0.04355  -0.01770 152 TYR A C   
1154 O O   . TYR A 152 ? 0.45820 0.69745 0.48391 0.08416  0.04368  -0.02193 152 TYR A O   
1155 C CB  . TYR A 152 ? 0.44023 0.62800 0.46253 0.07383  0.03608  -0.01878 152 TYR A CB  
1156 C CG  . TYR A 152 ? 0.49970 0.66892 0.52679 0.06738  0.03365  -0.01706 152 TYR A CG  
1157 C CD1 . TYR A 152 ? 0.38412 0.54689 0.41400 0.06945  0.03155  -0.02034 152 TYR A CD1 
1158 C CD2 . TYR A 152 ? 0.42675 0.58495 0.45542 0.05948  0.03362  -0.01198 152 TYR A CD2 
1159 C CE1 . TYR A 152 ? 0.30502 0.45090 0.33871 0.06379  0.02988  -0.01878 152 TYR A CE1 
1160 C CE2 . TYR A 152 ? 0.33580 0.47729 0.36909 0.05400  0.03195  -0.01038 152 TYR A CE2 
1161 C CZ  . TYR A 152 ? 0.36048 0.49583 0.39606 0.05616  0.03026  -0.01388 152 TYR A CZ  
1162 O OH  . TYR A 152 ? 0.32053 0.43925 0.36014 0.05092  0.02910  -0.01230 152 TYR A OH  
1163 N N   . LEU A 153 ? 0.50994 0.74280 0.52975 0.07584  0.04572  -0.01477 153 LEU A N   
1164 C CA  . LEU A 153 ? 0.40271 0.65111 0.41574 0.08362  0.04861  -0.01685 153 LEU A CA  
1165 C C   . LEU A 153 ? 0.46910 0.70638 0.47053 0.08548  0.04720  -0.01649 153 LEU A C   
1166 O O   . LEU A 153 ? 0.39428 0.63189 0.39598 0.07811  0.04891  -0.01067 153 LEU A O   
1167 C CB  . LEU A 153 ? 0.55876 0.83139 0.57928 0.07880  0.05450  -0.01231 153 LEU A CB  
1168 C CG  . LEU A 153 ? 0.50816 0.79686 0.52129 0.08548  0.05854  -0.01303 153 LEU A CG  
1169 C CD1 . LEU A 153 ? 0.46248 0.75993 0.47284 0.09749  0.05853  -0.01980 153 LEU A CD1 
1170 C CD2 . LEU A 153 ? 0.57131 0.88074 0.59189 0.07796  0.06455  -0.00657 153 LEU A CD2 
1171 N N   . THR A 154 ? 0.39187 0.61861 0.38303 0.09511  0.04377  -0.02262 154 THR A N   
1172 C CA  . THR A 154 ? 0.52715 0.74564 0.50603 0.09796  0.04230  -0.02316 154 THR A CA  
1173 C C   . THR A 154 ? 0.46150 0.69999 0.43562 0.10052  0.04767  -0.02176 154 THR A C   
1174 O O   . THR A 154 ? 0.45956 0.71626 0.43669 0.10516  0.05157  -0.02355 154 THR A O   
1175 C CB  . THR A 154 ? 0.46749 0.67056 0.43629 0.10787  0.03744  -0.03059 154 THR A CB  
1176 O OG1 . THR A 154 ? 0.69485 0.90951 0.66240 0.11755  0.03921  -0.03605 154 THR A OG1 
1177 C CG2 . THR A 154 ? 0.43702 0.61929 0.41011 0.10485  0.03232  -0.03131 154 THR A CG2 
1178 N N   . LEU A 155 ? 0.54639 0.78193 0.51333 0.09735  0.04797  -0.01817 155 LEU A N   
1179 C CA  . LEU A 155 ? 0.57985 0.83422 0.54232 0.09839  0.05362  -0.01561 155 LEU A CA  
1180 C C   . LEU A 155 ? 0.63729 0.88235 0.58701 0.09812  0.05183  -0.01402 155 LEU A C   
1181 O O   . LEU A 155 ? 0.59718 0.82293 0.54446 0.09486  0.04647  -0.01331 155 LEU A O   
1182 C CB  . LEU A 155 ? 0.54837 0.81934 0.52340 0.08868  0.05891  -0.00818 155 LEU A CB  
1183 C CG  . LEU A 155 ? 0.45419 0.71761 0.43138 0.07773  0.05858  -0.00037 155 LEU A CG  
1184 C CD1 . LEU A 155 ? 0.57616 0.85887 0.56235 0.06979  0.06495  0.00675  155 LEU A CD1 
1185 C CD2 . LEU A 155 ? 0.45362 0.69749 0.43778 0.07186  0.05357  0.00042  155 LEU A CD2 
1186 N N   . LEU A 156 ? 0.73129 0.99100 0.67291 0.10170  0.05645  -0.01336 156 LEU A N   
1187 C CA  . LEU A 156 ? 0.49906 0.75505 0.42906 0.10004  0.05616  -0.01013 156 LEU A CA  
1188 C C   . LEU A 156 ? 0.54647 0.81982 0.48279 0.09182  0.06253  -0.00151 156 LEU A C   
1189 O O   . LEU A 156 ? 0.57811 0.87177 0.51419 0.09503  0.06889  -0.00122 156 LEU A O   
1190 C CB  . LEU A 156 ? 0.52072 0.77862 0.43409 0.11137  0.05656  -0.01663 156 LEU A CB  
1191 C CG  . LEU A 156 ? 0.69248 0.93153 0.59082 0.11352  0.05054  -0.01893 156 LEU A CG  
1192 C CD1 . LEU A 156 ? 0.59813 0.81486 0.50065 0.11144  0.04293  -0.02121 156 LEU A CD1 
1193 C CD2 . LEU A 156 ? 0.71345 0.95427 0.59563 0.12555  0.05113  -0.02671 156 LEU A CD2 
1194 N N   . PRO A 157 ? 0.58888 0.85538 0.53168 0.08121  0.06139  0.00582  157 PRO A N   
1195 C CA  . PRO A 157 ? 0.69884 0.98121 0.64895 0.07276  0.06755  0.01433  157 PRO A CA  
1196 C C   . PRO A 157 ? 0.79607 1.08973 0.73365 0.07551  0.07177  0.01676  157 PRO A C   
1197 O O   . PRO A 157 ? 0.72650 1.00905 0.65097 0.07744  0.06836  0.01663  157 PRO A O   
1198 C CB  . PRO A 157 ? 0.56806 0.83553 0.52515 0.06221  0.06416  0.02076  157 PRO A CB  
1199 C CG  . PRO A 157 ? 0.58570 0.83115 0.53432 0.06599  0.05659  0.01649  157 PRO A CG  
1200 C CD  . PRO A 157 ? 0.61854 0.86249 0.56298 0.07645  0.05464  0.00687  157 PRO A CD  
1201 N N   . SER A 158 ? 0.68366 0.99992 0.62536 0.07568  0.07923  0.01901  158 SER A N   
1202 C CA  . SER A 158 ? 0.76842 1.09855 0.69929 0.07831  0.08474  0.02170  158 SER A CA  
1203 C C   . SER A 158 ? 0.76417 1.10935 0.70488 0.06803  0.09103  0.03159  158 SER A C   
1204 O O   . SER A 158 ? 0.70448 1.05528 0.66125 0.06105  0.09255  0.03454  158 SER A O   
1205 C CB  . SER A 158 ? 0.86936 1.21439 0.79471 0.08976  0.08883  0.01477  158 SER A CB  
1206 O OG  . SER A 158 ? 0.86629 1.19674 0.78428 0.09895  0.08299  0.00549  158 SER A OG  
1207 N N   . ALA A 159 ? 0.77131 1.12272 0.70159 0.06717  0.09466  0.03667  159 ALA A N   
1208 C CA  . ALA A 159 ? 0.62014 0.98228 0.55774 0.05674  0.10002  0.04708  159 ALA A CA  
1209 C C   . ALA A 159 ? 0.71632 1.10243 0.66739 0.05446  0.10764  0.04917  159 ALA A C   
1210 O O   . ALA A 159 ? 0.72746 1.12028 0.69017 0.04401  0.11098  0.05714  159 ALA A O   
1211 C CB  . ALA A 159 ? 0.78109 1.14543 0.70275 0.05767  0.10246  0.05164  159 ALA A CB  
1212 N N   . GLU A 160 ? 0.63842 1.03751 0.58868 0.06386  0.11036  0.04233  160 GLU A N   
1213 C CA  . GLU A 160 ? 0.68069 1.10457 0.64370 0.06271  0.11759  0.04403  160 GLU A CA  
1214 C C   . GLU A 160 ? 0.80763 1.23352 0.78127 0.06726  0.11506  0.03673  160 GLU A C   
1215 O O   . GLU A 160 ? 0.86458 1.30985 0.84277 0.07304  0.11979  0.03387  160 GLU A O   
1216 C CB  . GLU A 160 ? 0.67918 1.12212 0.63200 0.06997  0.12510  0.04409  160 GLU A CB  
1217 N N   . GLU A 161 ? 0.72581 1.13188 0.70354 0.06493  0.10764  0.03382  161 GLU A N   
1218 C CA  . GLU A 161 ? 0.65623 1.06188 0.64354 0.06864  0.10456  0.02734  161 GLU A CA  
1219 C C   . GLU A 161 ? 0.55579 0.94849 0.55552 0.05816  0.10020  0.03030  161 GLU A C   
1220 O O   . GLU A 161 ? 0.73801 1.10840 0.73291 0.05620  0.09429  0.02985  161 GLU A O   
1221 C CB  . GLU A 161 ? 0.66586 1.05777 0.64089 0.08085  0.09939  0.01781  161 GLU A CB  
1222 C CG  . GLU A 161 ? 0.86143 1.26065 0.82050 0.09118  0.10291  0.01461  161 GLU A CG  
1223 C CD  . GLU A 161 ? 0.98656 1.37718 0.93638 0.10415  0.09909  0.00439  161 GLU A CD  
1224 O OE1 . GLU A 161 ? 1.00263 1.38194 0.95872 0.10517  0.09371  0.00003  161 GLU A OE1 
1225 O OE2 . GLU A 161 ? 1.00504 1.39988 0.94088 0.11339  0.10167  0.00075  161 GLU A OE2 
1226 N N   . SER A 162 ? 0.55941 0.96603 0.57505 0.05152  0.10307  0.03319  162 SER A N   
1227 C CA  . SER A 162 ? 0.55043 0.94663 0.57837 0.04146  0.09965  0.03570  162 SER A CA  
1228 C C   . SER A 162 ? 0.48779 0.88641 0.52483 0.04499  0.09683  0.02943  162 SER A C   
1229 O O   . SER A 162 ? 0.48197 0.89428 0.51848 0.05411  0.09849  0.02439  162 SER A O   
1230 C CB  . SER A 162 ? 0.46078 0.86927 0.49972 0.02912  0.10480  0.04478  162 SER A CB  
1231 O OG  . SER A 162 ? 0.58150 1.01614 0.62917 0.02990  0.11058  0.04534  162 SER A OG  
1232 N N   . TYR A 163 ? 0.66007 1.04512 0.70539 0.03778  0.09262  0.02993  163 TYR A N   
1233 C CA  . TYR A 163 ? 0.46863 0.85106 0.52056 0.04103  0.08871  0.02387  163 TYR A CA  
1234 C C   . TYR A 163 ? 0.53773 0.92148 0.60436 0.02950  0.08846  0.02749  163 TYR A C   
1235 O O   . TYR A 163 ? 0.50595 0.88441 0.57628 0.01898  0.08970  0.03399  163 TYR A O   
1236 C CB  . TYR A 163 ? 0.38778 0.74546 0.43065 0.04710  0.08194  0.01809  163 TYR A CB  
1237 C CG  . TYR A 163 ? 0.49086 0.84566 0.51892 0.05885  0.08133  0.01333  163 TYR A CG  
1238 C CD1 . TYR A 163 ? 0.50434 0.85051 0.52110 0.05861  0.08149  0.01612  163 TYR A CD1 
1239 C CD2 . TYR A 163 ? 0.42954 0.78997 0.45455 0.07026  0.08046  0.00603  163 TYR A CD2 
1240 C CE1 . TYR A 163 ? 0.58309 0.92610 0.58540 0.06914  0.08068  0.01136  163 TYR A CE1 
1241 C CE2 . TYR A 163 ? 0.57857 0.93535 0.58941 0.08107  0.07997  0.00127  163 TYR A CE2 
1242 C CZ  . TYR A 163 ? 0.57575 0.92369 0.57503 0.08031  0.08002  0.00378  163 TYR A CZ  
1243 O OH  . TYR A 163 ? 0.89159 1.23528 0.87594 0.09081  0.07926  -0.00133 163 TYR A OH  
1244 N N   . ASP A 164 ? 0.47412 0.86437 0.54866 0.03180  0.08662  0.02306  164 ASP A N   
1245 C CA  . ASP A 164 ? 0.46513 0.85655 0.55289 0.02192  0.08559  0.02501  164 ASP A CA  
1246 C C   . ASP A 164 ? 0.53572 0.91467 0.62398 0.02648  0.07965  0.01841  164 ASP A C   
1247 O O   . ASP A 164 ? 0.49531 0.87994 0.58042 0.03716  0.07831  0.01259  164 ASP A O   
1248 C CB  . ASP A 164 ? 0.51012 0.92952 0.60982 0.01840  0.09038  0.02761  164 ASP A CB  
1249 C CG  . ASP A 164 ? 0.69898 1.13011 0.80077 0.01080  0.09653  0.03550  164 ASP A CG  
1250 O OD1 . ASP A 164 ? 0.61396 1.03706 0.72067 -0.00077 0.09687  0.04101  164 ASP A OD1 
1251 O OD2 . ASP A 164 ? 0.60666 1.05470 0.70487 0.01659  0.10125  0.03627  164 ASP A OD2 
1252 N N   . CYS A 165 ? 0.48642 0.84815 0.57833 0.01868  0.07635  0.01940  165 CYS A N   
1253 C CA  . CYS A 165 ? 0.45140 0.80319 0.54546 0.02110  0.07131  0.01403  165 CYS A CA  
1254 C C   . CYS A 165 ? 0.40699 0.77547 0.51413 0.01478  0.07215  0.01484  165 CYS A C   
1255 O O   . CYS A 165 ? 0.39385 0.76437 0.50867 0.00319  0.07410  0.01996  165 CYS A O   
1256 C CB  . CYS A 165 ? 0.42905 0.75362 0.52005 0.01638  0.06751  0.01439  165 CYS A CB  
1257 S SG  . CYS A 165 ? 0.62842 0.93890 0.71902 0.02145  0.06146  0.00739  165 CYS A SG  
1258 N N   . LYS A 166 ? 0.29108 0.67140 0.40076 0.02233  0.07051  0.00988  166 LYS A N   
1259 C CA  . LYS A 166 ? 0.52025 0.91828 0.64235 0.01755  0.07055  0.01005  166 LYS A CA  
1260 C C   . LYS A 166 ? 0.41694 0.80095 0.53992 0.01758  0.06476  0.00567  166 LYS A C   
1261 O O   . LYS A 166 ? 0.37205 0.74748 0.48817 0.02777  0.06130  0.00030  166 LYS A O   
1262 C CB  . LYS A 166 ? 0.37407 0.79830 0.49960 0.02609  0.07308  0.00820  166 LYS A CB  
1263 C CG  . LYS A 166 ? 0.33492 0.78059 0.47462 0.02078  0.07326  0.00907  166 LYS A CG  
1264 C CD  . LYS A 166 ? 0.54054 1.01299 0.68431 0.02988  0.07615  0.00760  166 LYS A CD  
1265 C CE  . LYS A 166 ? 0.65797 1.15311 0.81712 0.02413  0.07598  0.00883  166 LYS A CE  
1266 N NZ  . LYS A 166 ? 0.71835 1.23936 0.88225 0.03421  0.07830  0.00698  166 LYS A NZ  
1267 N N   . VAL A 167 ? 0.25891 0.64020 0.38980 0.00622  0.06380  0.00796  167 VAL A N   
1268 C CA  . VAL A 167 ? 0.44148 0.80869 0.57277 0.00480  0.05864  0.00430  167 VAL A CA  
1269 C C   . VAL A 167 ? 0.37970 0.76547 0.52273 -0.00092 0.05776  0.00430  167 VAL A C   
1270 O O   . VAL A 167 ? 0.38905 0.78804 0.54094 -0.01068 0.06090  0.00889  167 VAL A O   
1271 C CB  . VAL A 167 ? 0.42638 0.76800 0.55441 -0.00355 0.05769  0.00641  167 VAL A CB  
1272 C CG1 . VAL A 167 ? 0.37412 0.69731 0.49090 0.00282  0.05757  0.00598  167 VAL A CG1 
1273 C CG2 . VAL A 167 ? 0.40364 0.75065 0.53906 -0.01636 0.06149  0.01267  167 VAL A CG2 
1274 N N   . GLU A 168 ? 0.40781 0.79469 0.55096 0.00508  0.05330  -0.00067 168 GLU A N   
1275 C CA  . GLU A 168 ? 0.48563 0.88929 0.63927 0.00055  0.05121  -0.00134 168 GLU A CA  
1276 C C   . GLU A 168 ? 0.37109 0.75577 0.52205 -0.00256 0.04594  -0.00447 168 GLU A C   
1277 O O   . GLU A 168 ? 0.37110 0.73992 0.51318 0.00587  0.04276  -0.00850 168 GLU A O   
1278 C CB  . GLU A 168 ? 0.51225 0.93853 0.66920 0.01148  0.05062  -0.00421 168 GLU A CB  
1279 C CG  . GLU A 168 ? 0.60199 1.04543 0.75921 0.01723  0.05610  -0.00202 168 GLU A CG  
1280 C CD  . GLU A 168 ? 0.60927 1.06895 0.76661 0.03085  0.05536  -0.00590 168 GLU A CD  
1281 O OE1 . GLU A 168 ? 0.73712 1.21463 0.90392 0.03095  0.05320  -0.00691 168 GLU A OE1 
1282 O OE2 . GLU A 168 ? 0.62129 1.07549 0.76920 0.04155  0.05670  -0.00803 168 GLU A OE2 
1283 N N   . HIS A 169 ? 0.39259 0.77848 0.55083 -0.01472 0.04515  -0.00264 169 HIS A N   
1284 C CA  . HIS A 169 ? 0.46678 0.83408 0.62192 -0.01882 0.04063  -0.00542 169 HIS A CA  
1285 C C   . HIS A 169 ? 0.40442 0.78465 0.56995 -0.02973 0.03897  -0.00458 169 HIS A C   
1286 O O   . HIS A 169 ? 0.41136 0.80480 0.58549 -0.03874 0.04235  -0.00029 169 HIS A O   
1287 C CB  . HIS A 169 ? 0.41598 0.75541 0.56380 -0.02382 0.04194  -0.00385 169 HIS A CB  
1288 C CG  . HIS A 169 ? 0.36752 0.68514 0.50958 -0.02506 0.03782  -0.00727 169 HIS A CG  
1289 N ND1 . HIS A 169 ? 0.35852 0.67092 0.50430 -0.03609 0.03637  -0.00706 169 HIS A ND1 
1290 C CD2 . HIS A 169 ? 0.30798 0.60747 0.44049 -0.01667 0.03503  -0.01097 169 HIS A CD2 
1291 C CE1 . HIS A 169 ? 0.43712 0.72924 0.57543 -0.03417 0.03309  -0.01052 169 HIS A CE1 
1292 N NE2 . HIS A 169 ? 0.33786 0.62203 0.46838 -0.02255 0.03229  -0.01272 169 HIS A NE2 
1293 N N   . TRP A 170 ? 0.35575 0.73163 0.52009 -0.02908 0.03361  -0.00861 170 TRP A N   
1294 C CA  . TRP A 170 ? 0.39935 0.78697 0.57274 -0.03915 0.03094  -0.00854 170 TRP A CA  
1295 C C   . TRP A 170 ? 0.41632 0.79335 0.59252 -0.05384 0.03333  -0.00514 170 TRP A C   
1296 O O   . TRP A 170 ? 0.62157 1.01325 0.80778 -0.06390 0.03318  -0.00328 170 TRP A O   
1297 C CB  . TRP A 170 ? 0.31214 0.69177 0.48089 -0.03588 0.02453  -0.01356 170 TRP A CB  
1298 C CG  . TRP A 170 ? 0.34781 0.73863 0.51467 -0.02178 0.02186  -0.01668 170 TRP A CG  
1299 C CD1 . TRP A 170 ? 0.35950 0.77480 0.53283 -0.01460 0.02371  -0.01568 170 TRP A CD1 
1300 C CD2 . TRP A 170 ? 0.33276 0.71006 0.49035 -0.01272 0.01721  -0.02114 170 TRP A CD2 
1301 N NE1 . TRP A 170 ? 0.40115 0.81875 0.56998 -0.00149 0.02037  -0.01940 170 TRP A NE1 
1302 C CE2 . TRP A 170 ? 0.35812 0.75254 0.51726 -0.00022 0.01624  -0.02265 170 TRP A CE2 
1303 C CE3 . TRP A 170 ? 0.46778 0.82004 0.61580 -0.01383 0.01407  -0.02384 170 TRP A CE3 
1304 C CZ2 . TRP A 170 ? 0.44696 0.83377 0.59847 0.01098  0.01199  -0.02661 170 TRP A CZ2 
1305 C CZ3 . TRP A 170 ? 0.44943 0.79469 0.58980 -0.00291 0.01001  -0.02762 170 TRP A CZ3 
1306 C CH2 . TRP A 170 ? 0.44558 0.80784 0.58777 0.00927  0.00886  -0.02890 170 TRP A CH2 
1307 N N   . GLY A 171 ? 0.45140 0.80328 0.61940 -0.05535 0.03552  -0.00414 171 GLY A N   
1308 C CA  . GLY A 171 ? 0.37969 0.72073 0.55023 -0.06851 0.03828  -0.00056 171 GLY A CA  
1309 C C   . GLY A 171 ? 0.34320 0.69785 0.52087 -0.07346 0.04384  0.00532  171 GLY A C   
1310 O O   . GLY A 171 ? 0.57467 0.92199 0.75546 -0.08479 0.04640  0.00891  171 GLY A O   
1311 N N   . LEU A 172 ? 0.37760 0.75113 0.55741 -0.06514 0.04597  0.00643  172 LEU A N   
1312 C CA  . LEU A 172 ? 0.54714 0.93596 0.73335 -0.06898 0.05152  0.01212  172 LEU A CA  
1313 C C   . LEU A 172 ? 0.61010 1.02890 0.80930 -0.07315 0.05152  0.01332  172 LEU A C   
1314 O O   . LEU A 172 ? 0.54322 0.97638 0.74508 -0.06653 0.04795  0.00963  172 LEU A O   
1315 C CB  . LEU A 172 ? 0.45322 0.84385 0.63292 -0.05723 0.05445  0.01274  172 LEU A CB  
1316 C CG  . LEU A 172 ? 0.28379 0.64725 0.45174 -0.05328 0.05497  0.01254  172 LEU A CG  
1317 C CD1 . LEU A 172 ? 0.28066 0.64906 0.44249 -0.04146 0.05720  0.01256  172 LEU A CD1 
1318 C CD2 . LEU A 172 ? 0.35520 0.70537 0.52431 -0.06489 0.05824  0.01771  172 LEU A CD2 
1319 N N   . ASP A 173 ? 0.61364 1.04199 0.82134 -0.08415 0.05556  0.01880  173 ASP A N   
1320 C CA  . ASP A 173 ? 0.50978 0.96826 0.73107 -0.08859 0.05636  0.02084  173 ASP A CA  
1321 C C   . ASP A 173 ? 0.56538 1.04609 0.78840 -0.07737 0.05958  0.02173  173 ASP A C   
1322 O O   . ASP A 173 ? 0.59802 1.10206 0.82887 -0.07328 0.05785  0.02005  173 ASP A O   
1323 C CB  . ASP A 173 ? 0.53675 0.99818 0.76635 -0.10354 0.06025  0.02687  173 ASP A CB  
1324 C CG  . ASP A 173 ? 0.75889 1.19997 0.98771 -0.11517 0.05710  0.02566  173 ASP A CG  
1325 O OD1 . ASP A 173 ? 0.75976 1.19483 0.98632 -0.11395 0.05125  0.02020  173 ASP A OD1 
1326 O OD2 . ASP A 173 ? 0.67700 1.10783 0.90706 -0.12542 0.06058  0.03024  173 ASP A OD2 
1327 N N   . LYS A 174 ? 0.49102 0.96489 0.70670 -0.07215 0.06419  0.02432  174 LYS A N   
1328 C CA  . LYS A 174 ? 0.54521 1.03628 0.75976 -0.06082 0.06774  0.02486  174 LYS A CA  
1329 C C   . LYS A 174 ? 0.52916 0.99894 0.72880 -0.05015 0.06765  0.02245  174 LYS A C   
1330 O O   . LYS A 174 ? 0.41407 0.85793 0.60610 -0.05363 0.06646  0.02239  174 LYS A O   
1331 C CB  . LYS A 174 ? 0.44536 0.95373 0.66704 -0.06700 0.07464  0.03185  174 LYS A CB  
1332 N N   . PRO A 175 ? 0.46500 0.94474 0.66029 -0.03697 0.06880  0.02027  175 PRO A N   
1333 C CA  . PRO A 175 ? 0.33243 0.79265 0.51359 -0.02737 0.06898  0.01832  175 PRO A CA  
1334 C C   . PRO A 175 ? 0.51353 0.96126 0.69033 -0.03394 0.07323  0.02378  175 PRO A C   
1335 O O   . PRO A 175 ? 0.49574 0.95810 0.67875 -0.04029 0.07826  0.02936  175 PRO A O   
1336 C CB  . PRO A 175 ? 0.43340 0.91256 0.61313 -0.01416 0.07103  0.01632  175 PRO A CB  
1337 C CG  . PRO A 175 ? 0.40894 0.91157 0.60053 -0.01406 0.06914  0.01475  175 PRO A CG  
1338 C CD  . PRO A 175 ? 0.52057 1.02914 0.72356 -0.02977 0.06962  0.01905  175 PRO A CD  
1339 N N   . LEU A 176 ? 0.47975 0.90032 0.64622 -0.03263 0.07115  0.02247  176 LEU A N   
1340 C CA  . LEU A 176 ? 0.51165 0.91758 0.67322 -0.03807 0.07432  0.02747  176 LEU A CA  
1341 C C   . LEU A 176 ? 0.51728 0.92112 0.66827 -0.02722 0.07628  0.02711  176 LEU A C   
1342 O O   . LEU A 176 ? 0.40159 0.79795 0.54476 -0.01624 0.07314  0.02170  176 LEU A O   
1343 C CB  . LEU A 176 ? 0.39735 0.77496 0.55475 -0.04351 0.07098  0.02663  176 LEU A CB  
1344 C CG  . LEU A 176 ? 0.60315 0.96483 0.75788 -0.05131 0.07383  0.03239  176 LEU A CG  
1345 C CD1 . LEU A 176 ? 0.52671 0.89040 0.69128 -0.06575 0.07542  0.03669  176 LEU A CD1 
1346 C CD2 . LEU A 176 ? 0.57575 0.90905 0.72106 -0.04807 0.07064  0.03001  176 LEU A CD2 
1347 N N   . LEU A 177 ? 0.44722 0.85748 0.59760 -0.03039 0.08141  0.03288  177 LEU A N   
1348 C CA  . LEU A 177 ? 0.49232 0.90077 0.63196 -0.02125 0.08352  0.03308  177 LEU A CA  
1349 C C   . LEU A 177 ? 0.47253 0.86051 0.60586 -0.02668 0.08434  0.03767  177 LEU A C   
1350 O O   . LEU A 177 ? 0.44004 0.82840 0.57919 -0.03784 0.08715  0.04378  177 LEU A O   
1351 C CB  . LEU A 177 ? 0.41567 0.85119 0.55861 -0.01862 0.08918  0.03594  177 LEU A CB  
1352 C CG  . LEU A 177 ? 0.49802 0.95106 0.64095 -0.00648 0.08880  0.03046  177 LEU A CG  
1353 C CD1 . LEU A 177 ? 0.45104 0.91412 0.60499 -0.00855 0.08552  0.02730  177 LEU A CD1 
1354 C CD2 . LEU A 177 ? 0.39049 0.86760 0.53464 -0.00327 0.09530  0.03376  177 LEU A CD2 
1355 N N   . LYS A 178 ? 0.47082 0.84082 0.59262 -0.01888 0.08170  0.03483  178 LYS A N   
1356 C CA  . LYS A 178 ? 0.52209 0.87291 0.63723 -0.02235 0.08193  0.03896  178 LYS A CA  
1357 C C   . LYS A 178 ? 0.45431 0.80938 0.55901 -0.01381 0.08395  0.03943  178 LYS A C   
1358 O O   . LYS A 178 ? 0.41914 0.77070 0.51572 -0.00278 0.08133  0.03369  178 LYS A O   
1359 C CB  . LYS A 178 ? 0.55309 0.87759 0.66407 -0.02154 0.07670  0.03554  178 LYS A CB  
1360 C CG  . LYS A 178 ? 0.42273 0.73014 0.53627 -0.03225 0.07704  0.04086  178 LYS A CG  
1361 C CD  . LYS A 178 ? 0.42186 0.73808 0.54720 -0.04377 0.07916  0.04401  178 LYS A CD  
1362 C CE  . LYS A 178 ? 0.56426 0.86096 0.69188 -0.05387 0.07925  0.04850  178 LYS A CE  
1363 N NZ  . LYS A 178 ? 0.56429 0.86670 0.70275 -0.06510 0.08057  0.05043  178 LYS A NZ  
1364 N N   . HIS A 179 ? 0.44395 0.80614 0.54840 -0.01895 0.08859  0.04623  179 HIS A N   
1365 C CA  . HIS A 179 ? 0.46863 0.83735 0.56299 -0.01178 0.09124  0.04733  179 HIS A CA  
1366 C C   . HIS A 179 ? 0.38388 0.72971 0.46713 -0.00966 0.08821  0.04805  179 HIS A C   
1367 O O   . HIS A 179 ? 0.47890 0.80703 0.56424 -0.01677 0.08616  0.05094  179 HIS A O   
1368 C CB  . HIS A 179 ? 0.43393 0.82155 0.53279 -0.01838 0.09787  0.05480  179 HIS A CB  
1369 C CG  . HIS A 179 ? 0.53077 0.92878 0.61934 -0.01066 0.10140  0.05571  179 HIS A CG  
1370 N ND1 . HIS A 179 ? 0.67622 1.06572 0.75581 -0.01222 0.10278  0.06095  179 HIS A ND1 
1371 C CD2 . HIS A 179 ? 0.54367 0.95970 0.62903 -0.00111 0.10389  0.05201  179 HIS A CD2 
1372 C CE1 . HIS A 179 ? 0.72616 1.12769 0.79668 -0.00414 0.10591  0.06024  179 HIS A CE1 
1373 N NE2 . HIS A 179 ? 0.62807 1.04567 0.70195 0.00282  0.10687  0.05476  179 HIS A NE2 
1374 N N   . TRP A 180 ? 0.56412 0.91050 0.63558 0.00034  0.08789  0.04528  180 TRP A N   
1375 C CA  . TRP A 180 ? 0.49949 0.82691 0.55965 0.00288  0.08499  0.04611  180 TRP A CA  
1376 C C   . TRP A 180 ? 0.61634 0.95460 0.66589 0.00860  0.08834  0.04771  180 TRP A C   
1377 O O   . TRP A 180 ? 0.60679 0.95877 0.65240 0.01742  0.08991  0.04305  180 TRP A O   
1378 C CB  . TRP A 180 ? 0.48187 0.79142 0.53634 0.01071  0.07867  0.03862  180 TRP A CB  
1379 C CG  . TRP A 180 ? 0.51659 0.80699 0.56018 0.01337  0.07509  0.03913  180 TRP A CG  
1380 C CD1 . TRP A 180 ? 0.36569 0.63561 0.41048 0.00785  0.07177  0.04186  180 TRP A CD1 
1381 C CD2 . TRP A 180 ? 0.52090 0.81108 0.55094 0.02221  0.07430  0.03677  180 TRP A CD2 
1382 N NE1 . TRP A 180 ? 0.38667 0.64442 0.42032 0.01248  0.06868  0.04161  180 TRP A NE1 
1383 C CE2 . TRP A 180 ? 0.48884 0.75825 0.51280 0.02113  0.06997  0.03834  180 TRP A CE2 
1384 C CE3 . TRP A 180 ? 0.52634 0.83178 0.54870 0.03100  0.07688  0.03339  180 TRP A CE3 
1385 C CZ2 . TRP A 180 ? 0.42750 0.69092 0.43783 0.02807  0.06762  0.03653  180 TRP A CZ2 
1386 C CZ3 . TRP A 180 ? 0.52165 0.82029 0.52968 0.03815  0.07493  0.03133  180 TRP A CZ3 
1387 C CH2 . TRP A 180 ? 0.46863 0.74643 0.47065 0.03642  0.07010  0.03286  180 TRP A CH2 
1388 N N   . GLU A 181 ? 0.65659 0.98858 0.70122 0.00383  0.08951  0.05434  181 GLU A N   
1389 C CA  . GLU A 181 ? 0.61476 0.95432 0.64743 0.00883  0.09227  0.05628  181 GLU A CA  
1390 C C   . GLU A 181 ? 0.65562 0.97426 0.67723 0.01028  0.08759  0.05729  181 GLU A C   
1391 O O   . GLU A 181 ? 0.58189 0.88398 0.60788 0.00356  0.08453  0.06054  181 GLU A O   
1392 C CB  . GLU A 181 ? 0.51895 0.87570 0.55608 0.00115  0.09927  0.06484  181 GLU A CB  
1393 N N   . PRO A 182 ? 0.76527 1.08395 0.77250 0.01913  0.08674  0.05434  182 PRO A N   
1394 C CA  . PRO A 182 ? 0.72786 1.02826 0.72407 0.02029  0.08206  0.05567  182 PRO A CA  
1395 C C   . PRO A 182 ? 0.54512 0.84881 0.53769 0.01389  0.08538  0.06511  182 PRO A C   
1396 O O   . PRO A 182 ? 0.73803 1.03436 0.73868 0.00443  0.08537  0.07180  182 PRO A O   
1397 C CB  . PRO A 182 ? 0.65361 0.95435 0.63569 0.03262  0.07997  0.04786  182 PRO A CB  
1398 C CG  . PRO A 182 ? 0.71123 1.03582 0.69448 0.03669  0.08645  0.04623  182 PRO A CG  
1399 C CD  . PRO A 182 ? 0.65902 0.99327 0.65959 0.02936  0.08934  0.04842  182 PRO A CD  
1400 N N   . SER B 3   ? 0.62066 0.96769 0.75076 -0.03347 -0.02134 -0.09341 3   SER B N   
1401 C CA  . SER B 3   ? 0.72065 1.05882 0.85310 -0.02494 -0.02263 -0.09026 3   SER B CA  
1402 C C   . SER B 3   ? 0.64540 0.98681 0.77877 -0.01452 -0.02748 -0.08614 3   SER B C   
1403 O O   . SER B 3   ? 0.54462 0.89086 0.67516 -0.01672 -0.03036 -0.08578 3   SER B O   
1404 C CB  . SER B 3   ? 0.63086 0.94282 0.75291 -0.03084 -0.02068 -0.08844 3   SER B CB  
1405 O OG  . SER B 3   ? 0.67452 0.97927 0.79029 -0.03273 -0.02359 -0.08630 3   SER B OG  
1406 N N   . PRO B 4   ? 0.43101 0.76505 0.56529 -0.00315 -0.02771 -0.08233 4   PRO B N   
1407 C CA  . PRO B 4   ? 0.45258 0.78638 0.58583 0.00696  -0.03198 -0.07806 4   PRO B CA  
1408 C C   . PRO B 4   ? 0.57683 0.89324 0.70075 0.00337  -0.03362 -0.07519 4   PRO B C   
1409 O O   . PRO B 4   ? 0.59509 0.89369 0.71276 -0.00333 -0.03106 -0.07492 4   PRO B O   
1410 C CB  . PRO B 4   ? 0.42660 0.75020 0.56016 0.01791  -0.03049 -0.07476 4   PRO B CB  
1411 C CG  . PRO B 4   ? 0.46159 0.78866 0.59955 0.01468  -0.02602 -0.07817 4   PRO B CG  
1412 C CD  . PRO B 4   ? 0.45876 0.78326 0.59393 0.00075  -0.02392 -0.08177 4   PRO B CD  
1413 N N   . GLU B 5   ? 0.48909 0.81099 0.61191 0.00804  -0.03793 -0.07306 5   GLU B N   
1414 C CA  . GLU B 5   ? 0.50577 0.81156 0.61975 0.00581  -0.03944 -0.07009 5   GLU B CA  
1415 C C   . GLU B 5   ? 0.56937 0.85706 0.67891 0.01537  -0.03954 -0.06482 5   GLU B C   
1416 O O   . GLU B 5   ? 0.50244 0.79478 0.61516 0.02581  -0.04061 -0.06292 5   GLU B O   
1417 C CB  . GLU B 5   ? 0.47321 0.79259 0.58684 0.00495  -0.04387 -0.07054 5   GLU B CB  
1418 C CG  . GLU B 5   ? 0.59772 0.93013 0.71547 0.01673  -0.04788 -0.06839 5   GLU B CG  
1419 C CD  . GLU B 5   ? 0.65888 0.99929 0.77363 0.01598  -0.05253 -0.06786 5   GLU B CD  
1420 O OE1 . GLU B 5   ? 0.57060 0.90851 0.68083 0.00554  -0.05233 -0.06980 5   GLU B OE1 
1421 O OE2 . GLU B 5   ? 0.76186 1.11016 0.87794 0.02590  -0.05631 -0.06545 5   GLU B OE2 
1422 N N   . ASP B 6   ? 0.47555 0.74240 0.57742 0.01171  -0.03820 -0.06255 6   ASP B N   
1423 C CA  . ASP B 6   ? 0.57014 0.81853 0.66716 0.01899  -0.03780 -0.05782 6   ASP B CA  
1424 C C   . ASP B 6   ? 0.41148 0.64786 0.50091 0.01737  -0.03943 -0.05506 6   ASP B C   
1425 O O   . ASP B 6   ? 0.44046 0.67446 0.52675 0.00852  -0.03903 -0.05671 6   ASP B O   
1426 C CB  . ASP B 6   ? 0.38761 0.62074 0.48334 0.01664  -0.03373 -0.05761 6   ASP B CB  
1427 C CG  . ASP B 6   ? 0.36945 0.58711 0.46163 0.02507  -0.03317 -0.05324 6   ASP B CG  
1428 O OD1 . ASP B 6   ? 0.45177 0.67134 0.54279 0.03343  -0.03568 -0.05056 6   ASP B OD1 
1429 O OD2 . ASP B 6   ? 0.48059 0.68389 0.57052 0.02321  -0.03027 -0.05249 6   ASP B OD2 
1430 N N   . PHE B 7   ? 0.36305 0.59125 0.44888 0.02596  -0.04098 -0.05090 7   PHE B N   
1431 C CA  . PHE B 7   ? 0.38188 0.59736 0.46016 0.02545  -0.04213 -0.04791 7   PHE B CA  
1432 C C   . PHE B 7   ? 0.38469 0.57968 0.45849 0.02913  -0.03984 -0.04423 7   PHE B C   
1433 O O   . PHE B 7   ? 0.35307 0.54544 0.42713 0.03759  -0.03981 -0.04207 7   PHE B O   
1434 C CB  . PHE B 7   ? 0.48176 0.70648 0.55867 0.03180  -0.04632 -0.04634 7   PHE B CB  
1435 C CG  . PHE B 7   ? 0.46022 0.70612 0.54147 0.02784  -0.04900 -0.04997 7   PHE B CG  
1436 C CD1 . PHE B 7   ? 0.44539 0.69198 0.52311 0.01884  -0.04957 -0.05172 7   PHE B CD1 
1437 C CD2 . PHE B 7   ? 0.43372 0.69905 0.52242 0.03297  -0.05079 -0.05174 7   PHE B CD2 
1438 C CE1 . PHE B 7   ? 0.56600 0.83206 0.64712 0.01436  -0.05200 -0.05525 7   PHE B CE1 
1439 C CE2 . PHE B 7   ? 0.48312 0.76940 0.57632 0.02882  -0.05336 -0.05527 7   PHE B CE2 
1440 C CZ  . PHE B 7   ? 0.51393 0.80044 0.60313 0.01912  -0.05400 -0.05708 7   PHE B CZ  
1441 N N   . VAL B 8   ? 0.41759 0.59823 0.48705 0.02279  -0.03784 -0.04357 8   VAL B N   
1442 C CA  . VAL B 8   ? 0.43737 0.59986 0.50370 0.02405  -0.03525 -0.04088 8   VAL B CA  
1443 C C   . VAL B 8   ? 0.38875 0.53808 0.44829 0.02467  -0.03562 -0.03754 8   VAL B C   
1444 O O   . VAL B 8   ? 0.32659 0.47625 0.38342 0.01966  -0.03633 -0.03814 8   VAL B O   
1445 C CB  . VAL B 8   ? 0.45544 0.61240 0.52317 0.01623  -0.03227 -0.04304 8   VAL B CB  
1446 C CG1 . VAL B 8   ? 0.36728 0.50622 0.43185 0.01725  -0.03001 -0.04020 8   VAL B CG1 
1447 C CG2 . VAL B 8   ? 0.36444 0.53401 0.43846 0.01537  -0.03148 -0.04649 8   VAL B CG2 
1448 N N   . TYR B 9   ? 0.33030 0.46762 0.38661 0.03057  -0.03484 -0.03413 9   TYR B N   
1449 C CA  . TYR B 9   ? 0.31698 0.44003 0.36689 0.03101  -0.03436 -0.03087 9   TYR B CA  
1450 C C   . TYR B 9   ? 0.44953 0.55772 0.49833 0.03012  -0.03137 -0.02927 9   TYR B C   
1451 O O   . TYR B 9   ? 0.38005 0.48634 0.43026 0.03400  -0.03042 -0.02889 9   TYR B O   
1452 C CB  . TYR B 9   ? 0.29572 0.41831 0.34131 0.03927  -0.03648 -0.02808 9   TYR B CB  
1453 C CG  . TYR B 9   ? 0.40354 0.51335 0.44198 0.03925  -0.03614 -0.02508 9   TYR B CG  
1454 C CD1 . TYR B 9   ? 0.29534 0.38911 0.33022 0.03974  -0.03354 -0.02249 9   TYR B CD1 
1455 C CD2 . TYR B 9   ? 0.47104 0.58509 0.50607 0.03860  -0.03834 -0.02493 9   TYR B CD2 
1456 C CE1 . TYR B 9   ? 0.37271 0.45542 0.40132 0.03950  -0.03286 -0.01993 9   TYR B CE1 
1457 C CE2 . TYR B 9   ? 0.58875 0.69087 0.61690 0.03856  -0.03768 -0.02228 9   TYR B CE2 
1458 C CZ  . TYR B 9   ? 0.38353 0.47024 0.40874 0.03903  -0.03482 -0.01982 9   TYR B CZ  
1459 O OH  . TYR B 9   ? 0.43875 0.51423 0.45742 0.03872  -0.03381 -0.01738 9   TYR B OH  
1460 N N   . GLN B 10  ? 0.38472 0.48275 0.43096 0.02499  -0.02988 -0.02840 10  GLN B N   
1461 C CA  . GLN B 10  ? 0.39463 0.47898 0.43968 0.02384  -0.02739 -0.02666 10  GLN B CA  
1462 C C   . GLN B 10  ? 0.32758 0.40078 0.36719 0.02470  -0.02679 -0.02357 10  GLN B C   
1463 O O   . GLN B 10  ? 0.33812 0.41275 0.37540 0.02284  -0.02756 -0.02351 10  GLN B O   
1464 C CB  . GLN B 10  ? 0.24485 0.32768 0.29276 0.01644  -0.02581 -0.02872 10  GLN B CB  
1465 C CG  . GLN B 10  ? 0.38976 0.48379 0.44239 0.01402  -0.02610 -0.03225 10  GLN B CG  
1466 C CD  . GLN B 10  ? 0.32924 0.41951 0.38312 0.00694  -0.02440 -0.03403 10  GLN B CD  
1467 O OE1 . GLN B 10  ? 0.33708 0.41713 0.39039 0.00599  -0.02289 -0.03272 10  GLN B OE1 
1468 N NE2 . GLN B 10  ? 0.32801 0.42631 0.38303 0.00180  -0.02468 -0.03706 10  GLN B NE2 
1469 N N   . PHE B 11  ? 0.31583 0.37775 0.35296 0.02722  -0.02520 -0.02114 11  PHE B N   
1470 C CA  . PHE B 11  ? 0.34032 0.39073 0.37271 0.02692  -0.02387 -0.01839 11  PHE B CA  
1471 C C   . PHE B 11  ? 0.32549 0.36617 0.35896 0.02371  -0.02150 -0.01764 11  PHE B C   
1472 O O   . PHE B 11  ? 0.28719 0.32416 0.32070 0.02587  -0.02078 -0.01723 11  PHE B O   
1473 C CB  . PHE B 11  ? 0.31509 0.36084 0.34150 0.03372  -0.02442 -0.01580 11  PHE B CB  
1474 C CG  . PHE B 11  ? 0.31268 0.34594 0.33380 0.03307  -0.02254 -0.01309 11  PHE B CG  
1475 C CD1 . PHE B 11  ? 0.31162 0.34398 0.33147 0.02947  -0.02222 -0.01290 11  PHE B CD1 
1476 C CD2 . PHE B 11  ? 0.31590 0.33799 0.33293 0.03568  -0.02076 -0.01089 11  PHE B CD2 
1477 C CE1 . PHE B 11  ? 0.25273 0.27420 0.26811 0.02867  -0.02010 -0.01057 11  PHE B CE1 
1478 C CE2 . PHE B 11  ? 0.43218 0.44320 0.44440 0.03439  -0.01871 -0.00862 11  PHE B CE2 
1479 C CZ  . PHE B 11  ? 0.30804 0.31924 0.31985 0.03097  -0.01836 -0.00847 11  PHE B CZ  
1480 N N   . LYS B 12  ? 0.31000 0.34667 0.34412 0.01868  -0.02032 -0.01746 12  LYS B N   
1481 C CA  . LYS B 12  ? 0.35610 0.38545 0.39210 0.01506  -0.01849 -0.01696 12  LYS B CA  
1482 C C   . LYS B 12  ? 0.30755 0.32772 0.34043 0.01445  -0.01679 -0.01443 12  LYS B C   
1483 O O   . LYS B 12  ? 0.29557 0.31597 0.32768 0.01255  -0.01643 -0.01424 12  LYS B O   
1484 C CB  . LYS B 12  ? 0.34923 0.38270 0.38941 0.00960  -0.01851 -0.01922 12  LYS B CB  
1485 C CG  . LYS B 12  ? 0.30339 0.34573 0.34662 0.00911  -0.01971 -0.02203 12  LYS B CG  
1486 C CD  . LYS B 12  ? 0.36982 0.41460 0.41538 0.00337  -0.01946 -0.02419 12  LYS B CD  
1487 C CE  . LYS B 12  ? 0.25301 0.30516 0.30136 0.00197  -0.02004 -0.02709 12  LYS B CE  
1488 N NZ  . LYS B 12  ? 0.35965 0.41184 0.40882 -0.00385 -0.01949 -0.02906 12  LYS B NZ  
1489 N N   . GLY B 13  ? 0.36500 0.37691 0.39569 0.01582  -0.01547 -0.01263 13  GLY B N   
1490 C CA  . GLY B 13  ? 0.36595 0.36937 0.39437 0.01423  -0.01344 -0.01050 13  GLY B CA  
1491 C C   . GLY B 13  ? 0.32282 0.32367 0.35554 0.00943  -0.01233 -0.01067 13  GLY B C   
1492 O O   . GLY B 13  ? 0.28029 0.27661 0.31297 0.00895  -0.01177 -0.01027 13  GLY B O   
1493 N N   . MET B 14  ? 0.26934 0.27275 0.30529 0.00599  -0.01204 -0.01124 14  MET B N   
1494 C CA  . MET B 14  ? 0.32657 0.32971 0.36717 0.00190  -0.01171 -0.01178 14  MET B CA  
1495 C C   . MET B 14  ? 0.37916 0.37764 0.42056 -0.00025 -0.00975 -0.01004 14  MET B C   
1496 O O   . MET B 14  ? 0.24032 0.23775 0.27972 0.00037  -0.00855 -0.00911 14  MET B O   
1497 C CB  . MET B 14  ? 0.23375 0.24317 0.27725 -0.00025 -0.01279 -0.01390 14  MET B CB  
1498 C CG  . MET B 14  ? 0.30036 0.31598 0.34352 0.00127  -0.01451 -0.01595 14  MET B CG  
1499 S SD  . MET B 14  ? 0.38647 0.40810 0.43200 -0.00247 -0.01531 -0.01873 14  MET B SD  
1500 C CE  . MET B 14  ? 0.25762 0.27552 0.30642 -0.00569 -0.01513 -0.01890 14  MET B CE  
1501 N N   . CYS B 15  ? 0.31280 0.30895 0.35718 -0.00291 -0.00942 -0.00969 15  CYS B N   
1502 C CA  . CYS B 15  ? 0.33166 0.32526 0.37827 -0.00541 -0.00773 -0.00829 15  CYS B CA  
1503 C C   . CYS B 15  ? 0.26512 0.26209 0.31717 -0.00831 -0.00855 -0.00911 15  CYS B C   
1504 O O   . CYS B 15  ? 0.30497 0.30319 0.35839 -0.00928 -0.01018 -0.01030 15  CYS B O   
1505 C CB  . CYS B 15  ? 0.27482 0.26235 0.31948 -0.00625 -0.00660 -0.00692 15  CYS B CB  
1506 S SG  . CYS B 15  ? 0.42492 0.40590 0.46137 -0.00251 -0.00534 -0.00564 15  CYS B SG  
1507 N N   . TYR B 16  ? 0.31616 0.31424 0.37090 -0.00945 -0.00729 -0.00842 16  TYR B N   
1508 C CA  . TYR B 16  ? 0.29571 0.29648 0.35524 -0.01151 -0.00795 -0.00882 16  TYR B CA  
1509 C C   . TYR B 16  ? 0.33403 0.33430 0.39725 -0.01337 -0.00661 -0.00725 16  TYR B C   
1510 O O   . TYR B 16  ? 0.28011 0.27916 0.34266 -0.01301 -0.00434 -0.00608 16  TYR B O   
1511 C CB  . TYR B 16  ? 0.23975 0.24294 0.29913 -0.01077 -0.00760 -0.00962 16  TYR B CB  
1512 C CG  . TYR B 16  ? 0.30438 0.30905 0.36021 -0.00975 -0.00886 -0.01142 16  TYR B CG  
1513 C CD1 . TYR B 16  ? 0.27302 0.27765 0.32473 -0.00771 -0.00843 -0.01147 16  TYR B CD1 
1514 C CD2 . TYR B 16  ? 0.38955 0.39594 0.44593 -0.01101 -0.01052 -0.01314 16  TYR B CD2 
1515 C CE1 . TYR B 16  ? 0.31427 0.32190 0.36339 -0.00700 -0.00979 -0.01327 16  TYR B CE1 
1516 C CE2 . TYR B 16  ? 0.33880 0.34752 0.39227 -0.01069 -0.01147 -0.01505 16  TYR B CE2 
1517 C CZ  . TYR B 16  ? 0.28436 0.29438 0.33465 -0.00872 -0.01118 -0.01515 16  TYR B CZ  
1518 O OH  . TYR B 16  ? 0.29147 0.30538 0.33955 -0.00864 -0.01231 -0.01718 16  TYR B OH  
1519 N N   . PHE B 17  ? 0.27352 0.27496 0.34045 -0.01558 -0.00802 -0.00729 17  PHE B N   
1520 C CA  . PHE B 17  ? 0.27354 0.27610 0.34475 -0.01787 -0.00723 -0.00602 17  PHE B CA  
1521 C C   . PHE B 17  ? 0.33792 0.34483 0.41436 -0.01854 -0.00859 -0.00615 17  PHE B C   
1522 O O   . PHE B 17  ? 0.33275 0.33978 0.40883 -0.01872 -0.01087 -0.00720 17  PHE B O   
1523 C CB  . PHE B 17  ? 0.29704 0.29640 0.36702 -0.02032 -0.00783 -0.00573 17  PHE B CB  
1524 C CG  . PHE B 17  ? 0.29639 0.29014 0.35991 -0.01897 -0.00687 -0.00570 17  PHE B CG  
1525 C CD1 . PHE B 17  ? 0.30654 0.29662 0.36728 -0.01930 -0.00435 -0.00449 17  PHE B CD1 
1526 C CD2 . PHE B 17  ? 0.30154 0.29355 0.36148 -0.01727 -0.00838 -0.00687 17  PHE B CD2 
1527 C CE1 . PHE B 17  ? 0.28836 0.27228 0.34216 -0.01749 -0.00353 -0.00427 17  PHE B CE1 
1528 C CE2 . PHE B 17  ? 0.36324 0.35041 0.41728 -0.01522 -0.00759 -0.00671 17  PHE B CE2 
1529 C CZ  . PHE B 17  ? 0.40520 0.38787 0.45581 -0.01511 -0.00526 -0.00532 17  PHE B CZ  
1530 N N   . THR B 18  ? 0.26124 0.27159 0.34226 -0.01875 -0.00711 -0.00507 18  THR B N   
1531 C CA  . THR B 18  ? 0.37277 0.38765 0.45909 -0.01878 -0.00839 -0.00485 18  THR B CA  
1532 C C   . THR B 18  ? 0.34328 0.36264 0.43555 -0.02078 -0.00742 -0.00356 18  THR B C   
1533 O O   . THR B 18  ? 0.35169 0.37110 0.44420 -0.02116 -0.00454 -0.00285 18  THR B O   
1534 C CB  . THR B 18  ? 0.37719 0.39280 0.46303 -0.01575 -0.00732 -0.00512 18  THR B CB  
1535 O OG1 . THR B 18  ? 0.36289 0.37486 0.44298 -0.01475 -0.00816 -0.00657 18  THR B OG1 
1536 C CG2 . THR B 18  ? 0.31610 0.33542 0.40645 -0.01496 -0.00871 -0.00477 18  THR B CG2 
1537 N N   . ASN B 19  ? 0.31141 0.33463 0.40817 -0.02234 -0.00987 -0.00334 19  ASN B N   
1538 C CA  . ASN B 19  ? 0.41278 0.44220 0.51619 -0.02466 -0.00954 -0.00229 19  ASN B CA  
1539 C C   . ASN B 19  ? 0.42688 0.45377 0.52842 -0.02841 -0.00792 -0.00205 19  ASN B C   
1540 O O   . ASN B 19  ? 0.35859 0.38772 0.46237 -0.02952 -0.00498 -0.00138 19  ASN B O   
1541 C CB  . ASN B 19  ? 0.43752 0.47252 0.54604 -0.02209 -0.00710 -0.00150 19  ASN B CB  
1542 C CG  . ASN B 19  ? 0.50728 0.54633 0.61938 -0.01915 -0.00913 -0.00132 19  ASN B CG  
1543 O OD1 . ASN B 19  ? 0.42694 0.46360 0.53664 -0.01895 -0.01226 -0.00189 19  ASN B OD1 
1544 N ND2 . ASN B 19  ? 0.80878 0.85346 0.92610 -0.01666 -0.00714 -0.00051 19  ASN B ND2 
1545 N N   . GLY B 20  ? 0.28470 0.30621 0.38144 -0.03045 -0.00962 -0.00268 20  GLY B N   
1546 C CA  . GLY B 20  ? 0.23829 0.25458 0.33064 -0.03340 -0.00785 -0.00254 20  GLY B CA  
1547 C C   . GLY B 20  ? 0.40863 0.41969 0.49553 -0.03076 -0.00494 -0.00248 20  GLY B C   
1548 O O   . GLY B 20  ? 0.37492 0.38259 0.45763 -0.02763 -0.00564 -0.00316 20  GLY B O   
1549 N N   . THR B 21  ? 0.32696 0.33757 0.41369 -0.03216 -0.00168 -0.00172 21  THR B N   
1550 C CA  . THR B 21  ? 0.33336 0.33920 0.41482 -0.02960 0.00117  -0.00145 21  THR B CA  
1551 C C   . THR B 21  ? 0.37143 0.38237 0.45734 -0.02811 0.00368  -0.00093 21  THR B C   
1552 O O   . THR B 21  ? 0.40681 0.41417 0.48884 -0.02730 0.00676  -0.00050 21  THR B O   
1553 C CB  . THR B 21  ? 0.38628 0.38462 0.46118 -0.03209 0.00348  -0.00100 21  THR B CB  
1554 O OG1 . THR B 21  ? 0.48828 0.48970 0.56705 -0.03706 0.00477  -0.00060 21  THR B OG1 
1555 C CG2 . THR B 21  ? 0.32427 0.31557 0.39263 -0.03186 0.00157  -0.00154 21  THR B CG2 
1556 N N   . GLU B 22  ? 0.42017 0.43894 0.51362 -0.02749 0.00253  -0.00092 22  GLU B N   
1557 C CA  . GLU B 22  ? 0.43087 0.45431 0.52841 -0.02539 0.00512  -0.00046 22  GLU B CA  
1558 C C   . GLU B 22  ? 0.40531 0.42404 0.49719 -0.02145 0.00621  -0.00079 22  GLU B C   
1559 O O   . GLU B 22  ? 0.37962 0.39697 0.46974 -0.02054 0.00960  -0.00038 22  GLU B O   
1560 C CB  . GLU B 22  ? 0.43408 0.46599 0.53979 -0.02439 0.00323  -0.00036 22  GLU B CB  
1561 C CG  . GLU B 22  ? 0.58136 0.62130 0.69468 -0.02497 0.00589  0.00037  22  GLU B CG  
1562 C CD  . GLU B 22  ? 0.69954 0.74816 0.82085 -0.02350 0.00341  0.00062  22  GLU B CD  
1563 O OE1 . GLU B 22  ? 0.76365 0.81276 0.88529 -0.01908 0.00331  0.00063  22  GLU B OE1 
1564 O OE2 . GLU B 22  ? 0.80379 0.85823 0.93031 -0.02678 0.00148  0.00081  22  GLU B OE2 
1565 N N   . ARG B 23  ? 0.38864 0.40496 0.47735 -0.01943 0.00342  -0.00163 23  ARG B N   
1566 C CA  . ARG B 23  ? 0.35442 0.36644 0.43706 -0.01645 0.00387  -0.00222 23  ARG B CA  
1567 C C   . ARG B 23  ? 0.35775 0.36445 0.43416 -0.01661 0.00207  -0.00283 23  ARG B C   
1568 O O   . ARG B 23  ? 0.43160 0.43850 0.50839 -0.01725 -0.00082 -0.00353 23  ARG B O   
1569 C CB  . ARG B 23  ? 0.32564 0.33982 0.40956 -0.01402 0.00249  -0.00293 23  ARG B CB  
1570 C CG  . ARG B 23  ? 0.45255 0.47155 0.54206 -0.01274 0.00433  -0.00229 23  ARG B CG  
1571 C CD  . ARG B 23  ? 0.85778 0.87434 0.94341 -0.00969 0.00579  -0.00282 23  ARG B CD  
1572 N NE  . ARG B 23  ? 0.74819 0.76856 0.83847 -0.00760 0.00698  -0.00235 23  ARG B NE  
1573 C CZ  . ARG B 23  ? 0.84884 0.87296 0.94369 -0.00702 0.01015  -0.00140 23  ARG B CZ  
1574 N NH1 . ARG B 23  ? 0.79290 0.81713 0.88810 -0.00901 0.01260  -0.00084 23  ARG B NH1 
1575 N NH2 . ARG B 23  ? 0.78815 0.81578 0.88702 -0.00428 0.01109  -0.00100 23  ARG B NH2 
1576 N N   . VAL B 24  ? 0.39261 0.39445 0.46306 -0.01578 0.00384  -0.00253 24  VAL B N   
1577 C CA  . VAL B 24  ? 0.28861 0.28563 0.35272 -0.01477 0.00236  -0.00301 24  VAL B CA  
1578 C C   . VAL B 24  ? 0.36765 0.36289 0.42656 -0.01181 0.00294  -0.00337 24  VAL B C   
1579 O O   . VAL B 24  ? 0.49089 0.48468 0.54794 -0.01125 0.00562  -0.00266 24  VAL B O   
1580 C CB  . VAL B 24  ? 0.29449 0.28625 0.35489 -0.01646 0.00365  -0.00212 24  VAL B CB  
1581 C CG1 . VAL B 24  ? 0.21164 0.19865 0.26570 -0.01456 0.00196  -0.00257 24  VAL B CG1 
1582 C CG2 . VAL B 24  ? 0.33564 0.32954 0.40108 -0.02030 0.00342  -0.00180 24  VAL B CG2 
1583 N N   . ARG B 25  ? 0.32929 0.32487 0.38573 -0.01021 0.00050  -0.00458 25  ARG B N   
1584 C CA  . ARG B 25  ? 0.20536 0.20058 0.25716 -0.00786 0.00046  -0.00522 25  ARG B CA  
1585 C C   . ARG B 25  ? 0.24662 0.24052 0.29395 -0.00613 -0.00163 -0.00588 25  ARG B C   
1586 O O   . ARG B 25  ? 0.28743 0.28257 0.33641 -0.00662 -0.00367 -0.00669 25  ARG B O   
1587 C CB  . ARG B 25  ? 0.30494 0.30376 0.35892 -0.00786 -0.00025 -0.00645 25  ARG B CB  
1588 C CG  . ARG B 25  ? 0.27766 0.27633 0.32659 -0.00632 -0.00022 -0.00737 25  ARG B CG  
1589 C CD  . ARG B 25  ? 0.24081 0.24139 0.29106 -0.00690 -0.00018 -0.00848 25  ARG B CD  
1590 N NE  . ARG B 25  ? 0.41169 0.41194 0.45650 -0.00627 -0.00011 -0.00962 25  ARG B NE  
1591 C CZ  . ARG B 25  ? 0.45263 0.45339 0.49618 -0.00703 -0.00023 -0.01102 25  ARG B CZ  
1592 N NH1 . ARG B 25  ? 0.39405 0.39526 0.44114 -0.00786 -0.00044 -0.01129 25  ARG B NH1 
1593 N NH2 . ARG B 25  ? 0.34271 0.34312 0.38062 -0.00708 -0.00019 -0.01217 25  ARG B NH2 
1594 N N   . LEU B 26  ? 0.24531 0.23677 0.28685 -0.00389 -0.00107 -0.00548 26  LEU B N   
1595 C CA  . LEU B 26  ? 0.21778 0.20889 0.25495 -0.00130 -0.00304 -0.00599 26  LEU B CA  
1596 C C   . LEU B 26  ? 0.28814 0.28342 0.32341 -0.00004 -0.00435 -0.00736 26  LEU B C   
1597 O O   . LEU B 26  ? 0.29913 0.29366 0.33198 0.00007  -0.00296 -0.00706 26  LEU B O   
1598 C CB  . LEU B 26  ? 0.34888 0.33366 0.37989 0.00065  -0.00171 -0.00434 26  LEU B CB  
1599 C CG  . LEU B 26  ? 0.31604 0.29951 0.34151 0.00449  -0.00349 -0.00437 26  LEU B CG  
1600 C CD1 . LEU B 26  ? 0.32356 0.29878 0.34410 0.00533  -0.00196 -0.00268 26  LEU B CD1 
1601 C CD2 . LEU B 26  ? 0.39378 0.37876 0.41452 0.00711  -0.00414 -0.00448 26  LEU B CD2 
1602 N N   . VAL B 27  ? 0.19136 0.19099 0.22741 0.00057  -0.00683 -0.00900 27  VAL B N   
1603 C CA  . VAL B 27  ? 0.26338 0.26777 0.29727 0.00134  -0.00829 -0.01056 27  VAL B CA  
1604 C C   . VAL B 27  ? 0.28054 0.28766 0.31238 0.00432  -0.01050 -0.01113 27  VAL B C   
1605 O O   . VAL B 27  ? 0.34166 0.35093 0.37627 0.00419  -0.01170 -0.01207 27  VAL B O   
1606 C CB  . VAL B 27  ? 0.28858 0.29695 0.32575 -0.00150 -0.00887 -0.01251 27  VAL B CB  
1607 C CG1 . VAL B 27  ? 0.26451 0.27730 0.29846 -0.00153 -0.00998 -0.01423 27  VAL B CG1 
1608 C CG2 . VAL B 27  ? 0.23608 0.24157 0.27566 -0.00360 -0.00667 -0.01174 27  VAL B CG2 
1609 N N   . SER B 28  ? 0.31837 0.32540 0.34516 0.00724  -0.01100 -0.01052 28  SER B N   
1610 C CA  . SER B 28  ? 0.29571 0.30657 0.32038 0.01097  -0.01329 -0.01101 28  SER B CA  
1611 C C   . SER B 28  ? 0.32843 0.34805 0.35345 0.01029  -0.01530 -0.01327 28  SER B C   
1612 O O   . SER B 28  ? 0.34292 0.36290 0.36527 0.00900  -0.01493 -0.01344 28  SER B O   
1613 C CB  . SER B 28  ? 0.31583 0.32121 0.33394 0.01503  -0.01293 -0.00885 28  SER B CB  
1614 O OG  . SER B 28  ? 0.60054 0.61155 0.61552 0.01839  -0.01536 -0.00945 28  SER B OG  
1615 N N   . ARG B 29  ? 0.28874 0.31533 0.31670 0.01082  -0.01721 -0.01512 29  ARG B N   
1616 C CA  . ARG B 29  ? 0.27420 0.30998 0.30325 0.00898  -0.01891 -0.01775 29  ARG B CA  
1617 C C   . ARG B 29  ? 0.31745 0.36117 0.34605 0.01304  -0.02144 -0.01852 29  ARG B C   
1618 O O   . ARG B 29  ? 0.36428 0.40886 0.39488 0.01577  -0.02189 -0.01846 29  ARG B O   
1619 C CB  . ARG B 29  ? 0.28305 0.32123 0.31674 0.00470  -0.01857 -0.01987 29  ARG B CB  
1620 C CG  . ARG B 29  ? 0.30005 0.33077 0.33521 0.00172  -0.01639 -0.01890 29  ARG B CG  
1621 C CD  . ARG B 29  ? 0.34648 0.37930 0.38493 -0.00222 -0.01638 -0.02103 29  ARG B CD  
1622 N NE  . ARG B 29  ? 0.35710 0.38343 0.39720 -0.00442 -0.01470 -0.01997 29  ARG B NE  
1623 C CZ  . ARG B 29  ? 0.44636 0.47012 0.48532 -0.00680 -0.01338 -0.02004 29  ARG B CZ  
1624 N NH1 . ARG B 29  ? 0.30814 0.33419 0.34359 -0.00797 -0.01334 -0.02124 29  ARG B NH1 
1625 N NH2 . ARG B 29  ? 0.30686 0.32566 0.34801 -0.00797 -0.01206 -0.01889 29  ARG B NH2 
1626 N N   . SER B 30  ? 0.36056 0.41038 0.38648 0.01343  -0.02309 -0.01934 30  SER B N   
1627 C CA  . SER B 30  ? 0.29863 0.35868 0.32484 0.01701  -0.02592 -0.02043 30  SER B CA  
1628 C C   . SER B 30  ? 0.37250 0.44323 0.40189 0.01243  -0.02702 -0.02390 30  SER B C   
1629 O O   . SER B 30  ? 0.38382 0.45465 0.41095 0.00806  -0.02664 -0.02492 30  SER B O   
1630 C CB  . SER B 30  ? 0.35270 0.41237 0.37292 0.02093  -0.02738 -0.01874 30  SER B CB  
1631 O OG  . SER B 30  ? 0.32463 0.37319 0.34080 0.02462  -0.02594 -0.01562 30  SER B OG  
1632 N N   . ILE B 31  ? 0.32559 0.40475 0.35963 0.01321  -0.02807 -0.02580 31  ILE B N   
1633 C CA  . ILE B 31  ? 0.36184 0.45010 0.39918 0.00795  -0.02841 -0.02934 31  ILE B CA  
1634 C C   . ILE B 31  ? 0.41636 0.51915 0.45631 0.01066  -0.03109 -0.03121 31  ILE B C   
1635 O O   . ILE B 31  ? 0.42548 0.53108 0.46778 0.01621  -0.03182 -0.03049 31  ILE B O   
1636 C CB  . ILE B 31  ? 0.32635 0.41080 0.36745 0.00481  -0.02645 -0.03036 31  ILE B CB  
1637 C CG1 . ILE B 31  ? 0.28600 0.35769 0.32504 0.00212  -0.02413 -0.02860 31  ILE B CG1 
1638 C CG2 . ILE B 31  ? 0.33342 0.42692 0.37706 -0.00065 -0.02661 -0.03418 31  ILE B CG2 
1639 C CD1 . ILE B 31  ? 0.34105 0.40560 0.38259 0.00276  -0.02269 -0.02748 31  ILE B CD1 
1640 N N   . TYR B 32  ? 0.34155 0.45365 0.38089 0.00673  -0.03246 -0.03366 32  TYR B N   
1641 C CA  . TYR B 32  ? 0.30210 0.43046 0.34494 0.00789  -0.03502 -0.03610 32  TYR B CA  
1642 C C   . TYR B 32  ? 0.38882 0.52372 0.43581 0.00150  -0.03383 -0.03986 32  TYR B C   
1643 O O   . TYR B 32  ? 0.38001 0.51245 0.42447 -0.00559 -0.03259 -0.04163 32  TYR B O   
1644 C CB  . TYR B 32  ? 0.31119 0.44660 0.35023 0.00723  -0.03756 -0.03653 32  TYR B CB  
1645 C CG  . TYR B 32  ? 0.29488 0.44886 0.33812 0.00851  -0.04057 -0.03905 32  TYR B CG  
1646 C CD1 . TYR B 32  ? 0.32327 0.48413 0.36930 0.01690  -0.04271 -0.03773 32  TYR B CD1 
1647 C CD2 . TYR B 32  ? 0.36779 0.53252 0.41193 0.00133  -0.04116 -0.04282 32  TYR B CD2 
1648 C CE1 . TYR B 32  ? 0.47719 0.65650 0.52787 0.01858  -0.04554 -0.04004 32  TYR B CE1 
1649 C CE2 . TYR B 32  ? 0.42956 0.61287 0.47826 0.00210  -0.04393 -0.04533 32  TYR B CE2 
1650 C CZ  . TYR B 32  ? 0.39139 0.58261 0.44388 0.01097  -0.04621 -0.04390 32  TYR B CZ  
1651 O OH  . TYR B 32  ? 0.59682 0.80797 0.65463 0.01223  -0.04905 -0.04641 32  TYR B OH  
1652 N N   . ASN B 33  ? 0.33901 0.48149 0.39161 0.00409  -0.03395 -0.04108 33  ASN B N   
1653 C CA  . ASN B 33  ? 0.45316 0.59924 0.50941 -0.00148 -0.03216 -0.04431 33  ASN B CA  
1654 C C   . ASN B 33  ? 0.31318 0.44384 0.36679 -0.00559 -0.02930 -0.04342 33  ASN B C   
1655 O O   . ASN B 33  ? 0.40276 0.52390 0.45677 -0.00204 -0.02820 -0.04103 33  ASN B O   
1656 C CB  . ASN B 33  ? 0.40257 0.56149 0.45933 -0.00801 -0.03302 -0.04823 33  ASN B CB  
1657 C CG  . ASN B 33  ? 0.44802 0.62494 0.50904 -0.00399 -0.03602 -0.04953 33  ASN B CG  
1658 O OD1 . ASN B 33  ? 0.43406 0.61642 0.49975 0.00245  -0.03656 -0.04894 33  ASN B OD1 
1659 N ND2 . ASN B 33  ? 0.40222 0.58845 0.46134 -0.00755 -0.03801 -0.05125 33  ASN B ND2 
1660 N N   . ARG B 34  ? 0.40510 0.53295 0.45555 -0.01297 -0.02812 -0.04527 34  ARG B N   
1661 C CA  . ARG B 34  ? 0.37774 0.49110 0.42513 -0.01634 -0.02568 -0.04421 34  ARG B CA  
1662 C C   . ARG B 34  ? 0.39551 0.50088 0.43704 -0.01831 -0.02528 -0.04280 34  ARG B C   
1663 O O   . ARG B 34  ? 0.45794 0.55242 0.49660 -0.02149 -0.02324 -0.04225 34  ARG B O   
1664 C CB  . ARG B 34  ? 0.49343 0.60730 0.54115 -0.02304 -0.02388 -0.04748 34  ARG B CB  
1665 C CG  . ARG B 34  ? 0.44152 0.55676 0.49399 -0.02117 -0.02317 -0.04801 34  ARG B CG  
1666 C CD  . ARG B 34  ? 0.39323 0.51019 0.44546 -0.02800 -0.02144 -0.05158 34  ARG B CD  
1667 N NE  . ARG B 34  ? 0.42810 0.53109 0.47710 -0.03089 -0.01950 -0.05071 34  ARG B NE  
1668 C CZ  . ARG B 34  ? 0.61885 0.71634 0.66289 -0.03739 -0.01798 -0.05245 34  ARG B CZ  
1669 N NH1 . ARG B 34  ? 0.44878 0.55267 0.48993 -0.04247 -0.01788 -0.05528 34  ARG B NH1 
1670 N NH2 . ARG B 34  ? 0.64799 0.73308 0.68940 -0.03887 -0.01654 -0.05135 34  ARG B NH2 
1671 N N   . GLU B 35  ? 0.44944 0.55976 0.48885 -0.01621 -0.02716 -0.04215 35  GLU B N   
1672 C CA  . GLU B 35  ? 0.40134 0.50405 0.43464 -0.01773 -0.02664 -0.04078 35  GLU B CA  
1673 C C   . GLU B 35  ? 0.42874 0.52312 0.46118 -0.01147 -0.02668 -0.03673 35  GLU B C   
1674 O O   . GLU B 35  ? 0.41451 0.51388 0.44797 -0.00591 -0.02873 -0.03537 35  GLU B O   
1675 C CB  . GLU B 35  ? 0.47473 0.58731 0.50503 -0.02005 -0.02863 -0.04269 35  GLU B CB  
1676 C CG  . GLU B 35  ? 0.70574 0.80999 0.72863 -0.02216 -0.02783 -0.04156 35  GLU B CG  
1677 C CD  . GLU B 35  ? 0.89839 1.01209 0.91740 -0.02530 -0.02989 -0.04366 35  GLU B CD  
1678 O OE1 . GLU B 35  ? 0.76858 0.89019 0.78833 -0.02077 -0.03283 -0.04270 35  GLU B OE1 
1679 O OE2 . GLU B 35  ? 1.12809 1.24077 1.14259 -0.03241 -0.02857 -0.04626 35  GLU B OE2 
1680 N N   . GLU B 36  ? 0.39803 0.47980 0.42838 -0.01231 -0.02435 -0.03483 36  GLU B N   
1681 C CA  . GLU B 36  ? 0.43767 0.51105 0.46606 -0.00781 -0.02386 -0.03127 36  GLU B CA  
1682 C C   . GLU B 36  ? 0.32838 0.40211 0.35105 -0.00794 -0.02459 -0.03083 36  GLU B C   
1683 O O   . GLU B 36  ? 0.36144 0.43319 0.38010 -0.01280 -0.02351 -0.03224 36  GLU B O   
1684 C CB  . GLU B 36  ? 0.29483 0.35641 0.32316 -0.00923 -0.02112 -0.02972 36  GLU B CB  
1685 C CG  . GLU B 36  ? 0.34041 0.39360 0.36731 -0.00524 -0.02015 -0.02623 36  GLU B CG  
1686 C CD  . GLU B 36  ? 0.44188 0.48536 0.46970 -0.00680 -0.01756 -0.02487 36  GLU B CD  
1687 O OE1 . GLU B 36  ? 0.62274 0.66537 0.65195 -0.01044 -0.01673 -0.02644 36  GLU B OE1 
1688 O OE2 . GLU B 36  ? 0.43811 0.47494 0.46508 -0.00438 -0.01633 -0.02224 36  GLU B OE2 
1689 N N   . ILE B 37  ? 0.31982 0.39525 0.34118 -0.00265 -0.02633 -0.02888 37  ILE B N   
1690 C CA  . ILE B 37  ? 0.42738 0.50395 0.44285 -0.00240 -0.02754 -0.02848 37  ILE B CA  
1691 C C   . ILE B 37  ? 0.37297 0.43798 0.38403 0.00056  -0.02592 -0.02511 37  ILE B C   
1692 O O   . ILE B 37  ? 0.39916 0.46012 0.40438 -0.00135 -0.02518 -0.02480 37  ILE B O   
1693 C CB  . ILE B 37  ? 0.41786 0.50712 0.43416 0.00114  -0.03132 -0.02923 37  ILE B CB  
1694 C CG1 . ILE B 37  ? 0.33446 0.42263 0.35281 0.00871  -0.03229 -0.02667 37  ILE B CG1 
1695 C CG2 . ILE B 37  ? 0.36815 0.47002 0.38899 -0.00266 -0.03256 -0.03295 37  ILE B CG2 
1696 C CD1 . ILE B 37  ? 0.41378 0.51366 0.43238 0.01358  -0.03605 -0.02692 37  ILE B CD1 
1697 N N   . VAL B 38  ? 0.42974 0.48902 0.44293 0.00488  -0.02512 -0.02268 38  VAL B N   
1698 C CA  . VAL B 38  ? 0.40683 0.45506 0.41601 0.00722  -0.02317 -0.01962 38  VAL B CA  
1699 C C   . VAL B 38  ? 0.37826 0.41893 0.39146 0.00683  -0.02053 -0.01843 38  VAL B C   
1700 O O   . VAL B 38  ? 0.34133 0.38479 0.35959 0.00743  -0.02101 -0.01906 38  VAL B O   
1701 C CB  . VAL B 38  ? 0.37871 0.42658 0.38424 0.01345  -0.02502 -0.01742 38  VAL B CB  
1702 C CG1 . VAL B 38  ? 0.38454 0.42143 0.38359 0.01429  -0.02290 -0.01485 38  VAL B CG1 
1703 C CG2 . VAL B 38  ? 0.49401 0.55333 0.49807 0.01499  -0.02878 -0.01889 38  VAL B CG2 
1704 N N   . ARG B 39  ? 0.38341 0.41472 0.39425 0.00580  -0.01771 -0.01672 39  ARG B N   
1705 C CA  . ARG B 39  ? 0.29742 0.32210 0.31205 0.00488  -0.01518 -0.01558 39  ARG B CA  
1706 C C   . ARG B 39  ? 0.35484 0.37046 0.36590 0.00652  -0.01281 -0.01285 39  ARG B C   
1707 O O   . ARG B 39  ? 0.38757 0.40029 0.39338 0.00611  -0.01186 -0.01235 39  ARG B O   
1708 C CB  . ARG B 39  ? 0.25583 0.28006 0.27281 0.00012  -0.01360 -0.01720 39  ARG B CB  
1709 C CG  . ARG B 39  ? 0.40197 0.41927 0.42200 -0.00083 -0.01086 -0.01576 39  ARG B CG  
1710 C CD  . ARG B 39  ? 0.33235 0.34837 0.35302 -0.00464 -0.00927 -0.01711 39  ARG B CD  
1711 N NE  . ARG B 39  ? 0.33451 0.35583 0.35752 -0.00697 -0.01087 -0.01957 39  ARG B NE  
1712 C CZ  . ARG B 39  ? 0.32352 0.34325 0.34705 -0.01013 -0.00978 -0.02087 39  ARG B CZ  
1713 N NH1 . ARG B 39  ? 0.32906 0.34262 0.35158 -0.01087 -0.00719 -0.01990 39  ARG B NH1 
1714 N NH2 . ARG B 39  ? 0.36728 0.39147 0.39203 -0.01245 -0.01116 -0.02321 39  ARG B NH2 
1715 N N   . PHE B 40  ? 0.31004 0.32092 0.32335 0.00804  -0.01169 -0.01120 40  PHE B N   
1716 C CA  . PHE B 40  ? 0.39161 0.39384 0.40263 0.00822  -0.00872 -0.00892 40  PHE B CA  
1717 C C   . PHE B 40  ? 0.31130 0.31145 0.32832 0.00531  -0.00661 -0.00885 40  PHE B C   
1718 O O   . PHE B 40  ? 0.27762 0.27827 0.29870 0.00542  -0.00721 -0.00883 40  PHE B O   
1719 C CB  . PHE B 40  ? 0.23033 0.22758 0.23744 0.01207  -0.00883 -0.00688 40  PHE B CB  
1720 C CG  . PHE B 40  ? 0.34333 0.33156 0.34740 0.01151  -0.00541 -0.00477 40  PHE B CG  
1721 C CD1 . PHE B 40  ? 0.33520 0.31980 0.34357 0.00949  -0.00318 -0.00403 40  PHE B CD1 
1722 C CD2 . PHE B 40  ? 0.33119 0.31485 0.32801 0.01257  -0.00433 -0.00366 40  PHE B CD2 
1723 C CE1 . PHE B 40  ? 0.29784 0.27521 0.30390 0.00838  0.00022  -0.00234 40  PHE B CE1 
1724 C CE2 . PHE B 40  ? 0.27012 0.24550 0.26401 0.01162  -0.00073 -0.00190 40  PHE B CE2 
1725 C CZ  . PHE B 40  ? 0.33232 0.30496 0.33114 0.00943  0.00163  -0.00131 40  PHE B CZ  
1726 N N   . ASP B 41  ? 0.25704 0.25483 0.27432 0.00295  -0.00416 -0.00877 41  ASP B N   
1727 C CA  . ASP B 41  ? 0.21688 0.21335 0.23982 0.00062  -0.00217 -0.00856 41  ASP B CA  
1728 C C   . ASP B 41  ? 0.27319 0.26366 0.29503 0.00069  0.00107  -0.00649 41  ASP B C   
1729 O O   . ASP B 41  ? 0.35453 0.34198 0.37193 0.00078  0.00302  -0.00598 41  ASP B O   
1730 C CB  . ASP B 41  ? 0.25178 0.25037 0.27570 -0.00172 -0.00166 -0.01016 41  ASP B CB  
1731 C CG  . ASP B 41  ? 0.27037 0.26778 0.29978 -0.00338 0.00029  -0.00980 41  ASP B CG  
1732 O OD1 . ASP B 41  ? 0.31373 0.30948 0.34681 -0.00327 0.00137  -0.00835 41  ASP B OD1 
1733 O OD2 . ASP B 41  ? 0.34149 0.33963 0.37112 -0.00485 0.00073  -0.01103 41  ASP B OD2 
1734 N N   . SER B 42  ? 0.29555 0.28418 0.32098 0.00030  0.00179  -0.00542 42  SER B N   
1735 C CA  . SER B 42  ? 0.29673 0.27999 0.32095 -0.00017 0.00501  -0.00361 42  SER B CA  
1736 C C   . SER B 42  ? 0.27646 0.25965 0.30302 -0.00186 0.00811  -0.00349 42  SER B C   
1737 O O   . SER B 42  ? 0.30147 0.28046 0.32548 -0.00215 0.01123  -0.00228 42  SER B O   
1738 C CB  . SER B 42  ? 0.23502 0.21687 0.26282 -0.00119 0.00516  -0.00281 42  SER B CB  
1739 O OG  . SER B 42  ? 0.25898 0.24491 0.29444 -0.00343 0.00503  -0.00342 42  SER B OG  
1740 N N   . ASP B 43  ? 0.27912 0.26636 0.30986 -0.00283 0.00759  -0.00474 43  ASP B N   
1741 C CA  . ASP B 43  ? 0.29173 0.27836 0.32346 -0.00354 0.01067  -0.00466 43  ASP B CA  
1742 C C   . ASP B 43  ? 0.27672 0.25987 0.30070 -0.00275 0.01202  -0.00476 43  ASP B C   
1743 O O   . ASP B 43  ? 0.40819 0.38834 0.43074 -0.00299 0.01560  -0.00407 43  ASP B O   
1744 C CB  . ASP B 43  ? 0.34214 0.33239 0.37814 -0.00424 0.00972  -0.00596 43  ASP B CB  
1745 C CG  . ASP B 43  ? 0.37600 0.36948 0.41954 -0.00514 0.00853  -0.00575 43  ASP B CG  
1746 O OD1 . ASP B 43  ? 0.29746 0.29056 0.34362 -0.00570 0.00912  -0.00456 43  ASP B OD1 
1747 O OD2 . ASP B 43  ? 0.31544 0.31133 0.36154 -0.00554 0.00704  -0.00682 43  ASP B OD2 
1748 N N   . VAL B 44  ? 0.31079 0.29465 0.32967 -0.00188 0.00921  -0.00568 44  VAL B N   
1749 C CA  . VAL B 44  ? 0.27899 0.26007 0.28996 -0.00143 0.00985  -0.00594 44  VAL B CA  
1750 C C   . VAL B 44  ? 0.30193 0.27807 0.30715 0.00003  0.01076  -0.00430 44  VAL B C   
1751 O O   . VAL B 44  ? 0.31453 0.28603 0.31411 -0.00004 0.01336  -0.00372 44  VAL B O   
1752 C CB  . VAL B 44  ? 0.29438 0.27964 0.30265 -0.00151 0.00626  -0.00782 44  VAL B CB  
1753 C CG1 . VAL B 44  ? 0.25099 0.23386 0.25061 -0.00138 0.00643  -0.00813 44  VAL B CG1 
1754 C CG2 . VAL B 44  ? 0.20492 0.19323 0.21735 -0.00340 0.00600  -0.00947 44  VAL B CG2 
1755 N N   . GLY B 45  ? 0.26128 0.23736 0.26694 0.00140  0.00888  -0.00352 45  GLY B N   
1756 C CA  . GLY B 45  ? 0.33814 0.30806 0.33747 0.00294  0.00992  -0.00182 45  GLY B CA  
1757 C C   . GLY B 45  ? 0.28576 0.25458 0.27669 0.00550  0.00735  -0.00177 45  GLY B C   
1758 O O   . GLY B 45  ? 0.39409 0.35646 0.37804 0.00703  0.00840  -0.00024 45  GLY B O   
1759 N N   . GLU B 46  ? 0.29342 0.26840 0.28447 0.00590  0.00402  -0.00343 46  GLU B N   
1760 C CA  . GLU B 46  ? 0.36698 0.34317 0.35114 0.00851  0.00086  -0.00352 46  GLU B CA  
1761 C C   . GLU B 46  ? 0.35801 0.34352 0.34619 0.00848  -0.00301 -0.00562 46  GLU B C   
1762 O O   . GLU B 46  ? 0.37777 0.36720 0.37230 0.00596  -0.00277 -0.00706 46  GLU B O   
1763 C CB  . GLU B 46  ? 0.29336 0.26581 0.26954 0.00787  0.00216  -0.00341 46  GLU B CB  
1764 C CG  . GLU B 46  ? 0.39430 0.37006 0.37191 0.00466  0.00282  -0.00537 46  GLU B CG  
1765 C CD  . GLU B 46  ? 0.50784 0.47947 0.47639 0.00389  0.00392  -0.00540 46  GLU B CD  
1766 O OE1 . GLU B 46  ? 0.46312 0.42810 0.42499 0.00546  0.00524  -0.00366 46  GLU B OE1 
1767 O OE2 . GLU B 46  ? 0.45673 0.43103 0.42400 0.00147  0.00359  -0.00722 46  GLU B OE2 
1768 N N   . PHE B 47  ? 0.33831 0.32746 0.32257 0.01138  -0.00655 -0.00579 47  PHE B N   
1769 C CA  . PHE B 47  ? 0.29415 0.29329 0.28209 0.01118  -0.01013 -0.00800 47  PHE B CA  
1770 C C   . PHE B 47  ? 0.27843 0.28099 0.26495 0.00746  -0.01014 -0.01003 47  PHE B C   
1771 O O   . PHE B 47  ? 0.41421 0.41279 0.39403 0.00672  -0.00904 -0.00964 47  PHE B O   
1772 C CB  . PHE B 47  ? 0.30245 0.30571 0.28682 0.01568  -0.01390 -0.00763 47  PHE B CB  
1773 C CG  . PHE B 47  ? 0.26974 0.27029 0.25552 0.01952  -0.01421 -0.00610 47  PHE B CG  
1774 C CD1 . PHE B 47  ? 0.37238 0.37866 0.36512 0.01981  -0.01555 -0.00726 47  PHE B CD1 
1775 C CD2 . PHE B 47  ? 0.27385 0.26512 0.25302 0.02260  -0.01288 -0.00357 47  PHE B CD2 
1776 C CE1 . PHE B 47  ? 0.34931 0.35205 0.34238 0.02324  -0.01555 -0.00591 47  PHE B CE1 
1777 C CE2 . PHE B 47  ? 0.35240 0.33973 0.33148 0.02591  -0.01285 -0.00221 47  PHE B CE2 
1778 C CZ  . PHE B 47  ? 0.35408 0.34713 0.34013 0.02628  -0.01418 -0.00338 47  PHE B CZ  
1779 N N   . ARG B 48  ? 0.33915 0.34821 0.33109 0.00485  -0.01115 -0.01226 48  ARG B N   
1780 C CA  . ARG B 48  ? 0.35796 0.36957 0.34791 0.00080  -0.01098 -0.01447 48  ARG B CA  
1781 C C   . ARG B 48  ? 0.33636 0.35861 0.32847 -0.00012 -0.01463 -0.01696 48  ARG B C   
1782 O O   . ARG B 48  ? 0.33247 0.35935 0.33086 0.00050  -0.01582 -0.01762 48  ARG B O   
1783 C CB  . ARG B 48  ? 0.40163 0.40897 0.39508 -0.00240 -0.00761 -0.01493 48  ARG B CB  
1784 C CG  . ARG B 48  ? 0.33612 0.33429 0.32728 -0.00217 -0.00356 -0.01294 48  ARG B CG  
1785 C CD  . ARG B 48  ? 0.36327 0.35768 0.34579 -0.00340 -0.00238 -0.01313 48  ARG B CD  
1786 N NE  . ARG B 48  ? 0.38437 0.37020 0.36417 -0.00274 0.00162  -0.01115 48  ARG B NE  
1787 C CZ  . ARG B 48  ? 0.39303 0.37426 0.37428 -0.00437 0.00553  -0.01108 48  ARG B CZ  
1788 N NH1 . ARG B 48  ? 0.23863 0.22176 0.22327 -0.00655 0.00593  -0.01269 48  ARG B NH1 
1789 N NH2 . ARG B 48  ? 0.36058 0.33500 0.33950 -0.00364 0.00926  -0.00936 48  ARG B NH2 
1790 N N   . ALA B 49  ? 0.35382 0.38014 0.34059 -0.00186 -0.01633 -0.01842 49  ALA B N   
1791 C CA  . ALA B 49  ? 0.38664 0.42430 0.37543 -0.00355 -0.01962 -0.02113 49  ALA B CA  
1792 C C   . ALA B 49  ? 0.35021 0.38849 0.34175 -0.00876 -0.01802 -0.02357 49  ALA B C   
1793 O O   . ALA B 49  ? 0.37521 0.40787 0.36217 -0.01250 -0.01561 -0.02430 49  ALA B O   
1794 C CB  . ALA B 49  ? 0.30092 0.34307 0.28276 -0.00442 -0.02201 -0.02203 49  ALA B CB  
1795 N N   . VAL B 50  ? 0.35737 0.40158 0.35561 -0.00888 -0.01914 -0.02480 50  VAL B N   
1796 C CA  . VAL B 50  ? 0.35684 0.40145 0.35680 -0.01386 -0.01783 -0.02724 50  VAL B CA  
1797 C C   . VAL B 50  ? 0.40133 0.45404 0.39793 -0.01834 -0.01960 -0.03046 50  VAL B C   
1798 O O   . VAL B 50  ? 0.52542 0.57488 0.51830 -0.02351 -0.01776 -0.03238 50  VAL B O   
1799 C CB  . VAL B 50  ? 0.42122 0.46816 0.42885 -0.01271 -0.01811 -0.02738 50  VAL B CB  
1800 C CG1 . VAL B 50  ? 0.28958 0.33540 0.29791 -0.01775 -0.01663 -0.02972 50  VAL B CG1 
1801 C CG2 . VAL B 50  ? 0.30597 0.34519 0.31636 -0.00891 -0.01648 -0.02431 50  VAL B CG2 
1802 N N   . THR B 51  ? 0.40068 0.46401 0.39816 -0.01647 -0.02312 -0.03114 51  THR B N   
1803 C CA  . THR B 51  ? 0.33970 0.41232 0.33393 -0.02075 -0.02520 -0.03414 51  THR B CA  
1804 C C   . THR B 51  ? 0.39410 0.47163 0.38468 -0.01739 -0.02821 -0.03301 51  THR B C   
1805 O O   . THR B 51  ? 0.38513 0.46024 0.37660 -0.01123 -0.02901 -0.03012 51  THR B O   
1806 C CB  . THR B 51  ? 0.34631 0.43105 0.34674 -0.02262 -0.02703 -0.03700 51  THR B CB  
1807 O OG1 . THR B 51  ? 0.40886 0.50161 0.41501 -0.01638 -0.02979 -0.03577 51  THR B OG1 
1808 C CG2 . THR B 51  ? 0.38036 0.45951 0.38403 -0.02537 -0.02426 -0.03786 51  THR B CG2 
1809 N N   . LEU B 52  ? 0.41469 0.49889 0.40044 -0.02174 -0.02991 -0.03539 52  LEU B N   
1810 C CA  . LEU B 52  ? 0.44490 0.53485 0.42650 -0.01908 -0.03331 -0.03461 52  LEU B CA  
1811 C C   . LEU B 52  ? 0.39342 0.49298 0.38107 -0.01190 -0.03686 -0.03326 52  LEU B C   
1812 O O   . LEU B 52  ? 0.51479 0.61361 0.49902 -0.00672 -0.03888 -0.03090 52  LEU B O   
1813 C CB  . LEU B 52  ? 0.46391 0.56278 0.44102 -0.02569 -0.03513 -0.03806 52  LEU B CB  
1814 C CG  . LEU B 52  ? 0.49903 0.60712 0.47228 -0.02372 -0.03954 -0.03788 52  LEU B CG  
1815 C CD1 . LEU B 52  ? 0.34111 0.43681 0.30534 -0.02179 -0.03847 -0.03509 52  LEU B CD1 
1816 C CD2 . LEU B 52  ? 0.45195 0.57139 0.42279 -0.03122 -0.04142 -0.04193 52  LEU B CD2 
1817 N N   . LEU B 53  ? 0.51770 0.62550 0.51361 -0.01127 -0.03746 -0.03469 53  LEU B N   
1818 C CA  . LEU B 53  ? 0.39850 0.51511 0.39996 -0.00406 -0.04045 -0.03352 53  LEU B CA  
1819 C C   . LEU B 53  ? 0.50560 0.61064 0.50585 0.00290  -0.03933 -0.02942 53  LEU B C   
1820 O O   . LEU B 53  ? 0.37882 0.48765 0.37925 0.00973  -0.04195 -0.02761 53  LEU B O   
1821 C CB  . LEU B 53  ? 0.38702 0.51231 0.39715 -0.00510 -0.04029 -0.03582 53  LEU B CB  
1822 C CG  . LEU B 53  ? 0.57972 0.71843 0.59613 0.00113  -0.04357 -0.03589 53  LEU B CG  
1823 C CD1 . LEU B 53  ? 0.45130 0.60497 0.46637 0.00103  -0.04780 -0.03750 53  LEU B CD1 
1824 C CD2 . LEU B 53  ? 0.47114 0.61599 0.49546 -0.00085 -0.04235 -0.03829 53  LEU B CD2 
1825 N N   . GLY B 54  ? 0.42786 0.51878 0.42645 0.00131  -0.03540 -0.02795 54  GLY B N   
1826 C CA  . GLY B 54  ? 0.32371 0.40325 0.32094 0.00660  -0.03378 -0.02436 54  GLY B CA  
1827 C C   . GLY B 54  ? 0.34212 0.41154 0.33085 0.00731  -0.03273 -0.02209 54  GLY B C   
1828 O O   . GLY B 54  ? 0.38210 0.44132 0.36908 0.01100  -0.03089 -0.01920 54  GLY B O   
1829 N N   . LEU B 55  ? 0.44298 0.51457 0.42581 0.00352  -0.03363 -0.02342 55  LEU B N   
1830 C CA  . LEU B 55  ? 0.47062 0.53178 0.44461 0.00381  -0.03225 -0.02139 55  LEU B CA  
1831 C C   . LEU B 55  ? 0.41722 0.47702 0.38705 0.01081  -0.03463 -0.01857 55  LEU B C   
1832 O O   . LEU B 55  ? 0.41720 0.46467 0.38254 0.01305  -0.03208 -0.01586 55  LEU B O   
1833 C CB  . LEU B 55  ? 0.42735 0.49084 0.39515 -0.00220 -0.03268 -0.02366 55  LEU B CB  
1834 C CG  . LEU B 55  ? 0.45762 0.50964 0.41547 -0.00302 -0.03067 -0.02202 55  LEU B CG  
1835 C CD1 . LEU B 55  ? 0.32102 0.35901 0.27914 -0.00230 -0.02568 -0.01984 55  LEU B CD1 
1836 C CD2 . LEU B 55  ? 0.41817 0.47129 0.37007 -0.01007 -0.03030 -0.02472 55  LEU B CD2 
1837 N N   . PRO B 56  ? 0.48525 0.55682 0.45587 0.01459  -0.03928 -0.01899 56  PRO B N   
1838 C CA  . PRO B 56  ? 0.41676 0.48518 0.38222 0.02204  -0.04140 -0.01597 56  PRO B CA  
1839 C C   . PRO B 56  ? 0.37283 0.43136 0.34013 0.02694  -0.03893 -0.01328 56  PRO B C   
1840 O O   . PRO B 56  ? 0.43931 0.48653 0.39951 0.03035  -0.03772 -0.01041 56  PRO B O   
1841 C CB  . PRO B 56  ? 0.42762 0.51289 0.39626 0.02539  -0.04679 -0.01734 56  PRO B CB  
1842 C CG  . PRO B 56  ? 0.39189 0.48792 0.36361 0.01795  -0.04760 -0.02115 56  PRO B CG  
1843 C CD  . PRO B 56  ? 0.40964 0.49788 0.38503 0.01233  -0.04282 -0.02221 56  PRO B CD  
1844 N N   . ALA B 57  ? 0.37463 0.43657 0.35059 0.02699  -0.03798 -0.01421 57  ALA B N   
1845 C CA  . ALA B 57  ? 0.41545 0.46779 0.39268 0.03100  -0.03560 -0.01184 57  ALA B CA  
1846 C C   . ALA B 57  ? 0.39974 0.43758 0.37390 0.02773  -0.03089 -0.01035 57  ALA B C   
1847 O O   . ALA B 57  ? 0.39021 0.41712 0.35951 0.03109  -0.02914 -0.00761 57  ALA B O   
1848 C CB  . ALA B 57  ? 0.36821 0.42719 0.35501 0.03094  -0.03549 -0.01341 57  ALA B CB  
1849 N N   . ALA B 58  ? 0.37715 0.41465 0.35368 0.02122  -0.02864 -0.01217 58  ALA B N   
1850 C CA  . ALA B 58  ? 0.34393 0.36923 0.31849 0.01827  -0.02407 -0.01095 58  ALA B CA  
1851 C C   . ALA B 58  ? 0.39755 0.41388 0.36223 0.01978  -0.02317 -0.00881 58  ALA B C   
1852 O O   . ALA B 58  ? 0.42299 0.42844 0.38496 0.02103  -0.02007 -0.00656 58  ALA B O   
1853 C CB  . ALA B 58  ? 0.34685 0.37382 0.32432 0.01173  -0.02219 -0.01335 58  ALA B CB  
1854 N N   . GLU B 59  ? 0.43401 0.45478 0.39282 0.01936  -0.02583 -0.00957 59  GLU B N   
1855 C CA  . GLU B 59  ? 0.50087 0.51286 0.44921 0.02078  -0.02521 -0.00758 59  GLU B CA  
1856 C C   . GLU B 59  ? 0.40701 0.41416 0.35091 0.02765  -0.02653 -0.00477 59  GLU B C   
1857 O O   . GLU B 59  ? 0.50668 0.50160 0.44358 0.02884  -0.02379 -0.00246 59  GLU B O   
1858 C CB  . GLU B 59  ? 0.50009 0.51864 0.44281 0.01864  -0.02831 -0.00916 59  GLU B CB  
1859 C CG  . GLU B 59  ? 0.54752 0.56770 0.49162 0.01148  -0.02633 -0.01180 59  GLU B CG  
1860 C CD  . GLU B 59  ? 0.95470 0.96839 0.88832 0.00854  -0.02523 -0.01173 59  GLU B CD  
1861 O OE1 . GLU B 59  ? 0.81216 0.83042 0.73936 0.00980  -0.02912 -0.01179 59  GLU B OE1 
1862 O OE2 . GLU B 59  ? 0.81164 0.81568 0.74329 0.00515  -0.02045 -0.01157 59  GLU B OE2 
1863 N N   . TYR B 60  ? 0.34670 0.36284 0.29412 0.03227  -0.03041 -0.00497 60  TYR B N   
1864 C CA  . TYR B 60  ? 0.43753 0.44864 0.37960 0.03953  -0.03182 -0.00228 60  TYR B CA  
1865 C C   . TYR B 60  ? 0.50802 0.50677 0.45058 0.04033  -0.02750 -0.00035 60  TYR B C   
1866 O O   . TYR B 60  ? 0.49440 0.48090 0.42831 0.04281  -0.02566 0.00219  60  TYR B O   
1867 C CB  . TYR B 60  ? 0.41479 0.43922 0.36163 0.04448  -0.03659 -0.00316 60  TYR B CB  
1868 C CG  . TYR B 60  ? 0.52837 0.54781 0.47037 0.05282  -0.03795 -0.00048 60  TYR B CG  
1869 C CD1 . TYR B 60  ? 0.49179 0.50024 0.42183 0.05671  -0.03802 0.00230  60  TYR B CD1 
1870 C CD2 . TYR B 60  ? 0.54555 0.57057 0.49406 0.05694  -0.03902 -0.00076 60  TYR B CD2 
1871 C CE1 . TYR B 60  ? 0.58496 0.58740 0.50920 0.06464  -0.03909 0.00483  60  TYR B CE1 
1872 C CE2 . TYR B 60  ? 0.69363 0.71303 0.63675 0.06494  -0.03998 0.00170  60  TYR B CE2 
1873 C CZ  . TYR B 60  ? 0.79149 0.79937 0.72227 0.06886  -0.04004 0.00453  60  TYR B CZ  
1874 O OH  . TYR B 60  ? 0.81282 0.81369 0.73695 0.07708  -0.04082 0.00705  60  TYR B OH  
1875 N N   . TRP B 61  ? 0.44180 0.44339 0.39395 0.03783  -0.02577 -0.00160 61  TRP B N   
1876 C CA  . TRP B 61  ? 0.48421 0.47526 0.43745 0.03783  -0.02187 -0.00004 61  TRP B CA  
1877 C C   . TRP B 61  ? 0.44787 0.42786 0.39720 0.03361  -0.01726 0.00094  61  TRP B C   
1878 O O   . TRP B 61  ? 0.47163 0.44019 0.41615 0.03477  -0.01434 0.00306  61  TRP B O   
1879 C CB  . TRP B 61  ? 0.41590 0.41315 0.38017 0.03545  -0.02132 -0.00181 61  TRP B CB  
1880 C CG  . TRP B 61  ? 0.48594 0.49319 0.45443 0.03966  -0.02500 -0.00275 61  TRP B CG  
1881 C CD1 . TRP B 61  ? 0.44587 0.45373 0.40943 0.04664  -0.02777 -0.00137 61  TRP B CD1 
1882 C CD2 . TRP B 61  ? 0.43969 0.45775 0.41794 0.03742  -0.02612 -0.00531 61  TRP B CD2 
1883 N NE1 . TRP B 61  ? 0.40041 0.41957 0.37081 0.04903  -0.03041 -0.00297 61  TRP B NE1 
1884 C CE2 . TRP B 61  ? 0.48477 0.51023 0.46414 0.04314  -0.02937 -0.00547 61  TRP B CE2 
1885 C CE3 . TRP B 61  ? 0.40291 0.42468 0.38855 0.03132  -0.02457 -0.00746 61  TRP B CE3 
1886 C CZ2 . TRP B 61  ? 0.37198 0.40868 0.35994 0.04248  -0.03084 -0.00785 61  TRP B CZ2 
1887 C CZ3 . TRP B 61  ? 0.40760 0.43959 0.40093 0.03058  -0.02620 -0.00973 61  TRP B CZ3 
1888 C CH2 . TRP B 61  ? 0.37869 0.41820 0.37329 0.03589  -0.02918 -0.00999 61  TRP B CH2 
1889 N N   . ASN B 62  ? 0.40089 0.38385 0.35188 0.02859  -0.01626 -0.00066 62  ASN B N   
1890 C CA  . ASN B 62  ? 0.39274 0.36604 0.34062 0.02483  -0.01156 0.00011  62  ASN B CA  
1891 C C   . ASN B 62  ? 0.54200 0.50532 0.47781 0.02716  -0.01076 0.00228  62  ASN B C   
1892 O O   . ASN B 62  ? 0.49130 0.44431 0.42361 0.02534  -0.00632 0.00358  62  ASN B O   
1893 C CB  . ASN B 62  ? 0.30763 0.28567 0.25861 0.01961  -0.01067 -0.00210 62  ASN B CB  
1894 C CG  . ASN B 62  ? 0.35741 0.34013 0.31908 0.01633  -0.00930 -0.00370 62  ASN B CG  
1895 O OD1 . ASN B 62  ? 0.43187 0.41243 0.39850 0.01703  -0.00796 -0.00293 62  ASN B OD1 
1896 N ND2 . ASN B 62  ? 0.34401 0.33248 0.30842 0.01258  -0.00962 -0.00595 62  ASN B ND2 
1897 N N   . SER B 63  ? 0.37770 0.34409 0.30691 0.03113  -0.01497 0.00268  63  SER B N   
1898 C CA  . SER B 63  ? 0.55639 0.51267 0.47296 0.03365  -0.01457 0.00485  63  SER B CA  
1899 C C   . SER B 63  ? 0.53253 0.47821 0.44378 0.03799  -0.01317 0.00744  63  SER B C   
1900 O O   . SER B 63  ? 0.74408 0.67876 0.64392 0.03974  -0.01192 0.00945  63  SER B O   
1901 C CB  . SER B 63  ? 0.49376 0.45729 0.40469 0.03669  -0.01998 0.00450  63  SER B CB  
1902 O OG  . SER B 63  ? 0.47932 0.44968 0.39236 0.04257  -0.02424 0.00487  63  SER B OG  
1903 N N   . GLN B 64  ? 0.58976 0.53752 0.50794 0.03954  -0.01319 0.00741  64  GLN B N   
1904 C CA  . GLN B 64  ? 0.57838 0.51558 0.49094 0.04351  -0.01182 0.00968  64  GLN B CA  
1905 C C   . GLN B 64  ? 0.63171 0.56047 0.54725 0.03872  -0.00612 0.01002  64  GLN B C   
1906 O O   . GLN B 64  ? 0.60129 0.53514 0.52713 0.03617  -0.00523 0.00879  64  GLN B O   
1907 C CB  . GLN B 64  ? 0.60542 0.54972 0.52257 0.04851  -0.01540 0.00943  64  GLN B CB  
1908 C CG  . GLN B 64  ? 0.64033 0.58578 0.54918 0.05594  -0.01992 0.01073  64  GLN B CG  
1909 C CD  . GLN B 64  ? 0.88673 0.84632 0.80360 0.05973  -0.02436 0.00928  64  GLN B CD  
1910 O OE1 . GLN B 64  ? 0.70029 0.67355 0.62499 0.05712  -0.02683 0.00689  64  GLN B OE1 
1911 N NE2 . GLN B 64  ? 1.04627 1.00228 0.96087 0.06574  -0.02506 0.01061  64  GLN B NE2 
1912 N N   . LYS B 65  ? 0.66997 0.58600 0.57624 0.03742  -0.00230 0.01167  65  LYS B N   
1913 C CA  . LYS B 65  ? 0.63933 0.54806 0.54820 0.03247  0.00335  0.01191  65  LYS B CA  
1914 C C   . LYS B 65  ? 0.56442 0.47158 0.47778 0.03311  0.00401  0.01220  65  LYS B C   
1915 O O   . LYS B 65  ? 0.60306 0.51389 0.52626 0.02876  0.00622  0.01109  65  LYS B O   
1916 C CB  . LYS B 65  ? 0.60132 0.49559 0.49758 0.03178  0.00726  0.01380  65  LYS B CB  
1917 N N   . ASP B 66  ? 0.64660 0.54807 0.55235 0.03871  0.00205  0.01370  66  ASP B N   
1918 C CA  . ASP B 66  ? 0.53802 0.43548 0.44576 0.03925  0.00320  0.01410  66  ASP B CA  
1919 C C   . ASP B 66  ? 0.46786 0.37857 0.38935 0.03825  0.00085  0.01204  66  ASP B C   
1920 O O   . ASP B 66  ? 0.48923 0.39893 0.41651 0.03513  0.00301  0.01160  66  ASP B O   
1921 C CB  . ASP B 66  ? 0.70341 0.59164 0.59916 0.04633  0.00149  0.01614  66  ASP B CB  
1922 C CG  . ASP B 66  ? 0.72231 0.62035 0.61799 0.05293  -0.00442 0.01589  66  ASP B CG  
1923 O OD1 . ASP B 66  ? 0.79463 0.70513 0.69741 0.05135  -0.00694 0.01421  66  ASP B OD1 
1924 O OD2 . ASP B 66  ? 0.95679 0.85013 0.84507 0.05972  -0.00645 0.01734  66  ASP B OD2 
1925 N N   . ILE B 67  ? 0.53223 0.45536 0.45873 0.04049  -0.00353 0.01066  67  ILE B N   
1926 C CA  . ILE B 67  ? 0.52896 0.46423 0.46788 0.03912  -0.00549 0.00855  67  ILE B CA  
1927 C C   . ILE B 67  ? 0.46716 0.40633 0.41530 0.03216  -0.00276 0.00708  67  ILE B C   
1928 O O   . ILE B 67  ? 0.50367 0.44568 0.45996 0.02949  -0.00188 0.00617  67  ILE B O   
1929 C CB  . ILE B 67  ? 0.52041 0.46829 0.46198 0.04271  -0.01059 0.00723  67  ILE B CB  
1930 C CG1 . ILE B 67  ? 0.56698 0.51292 0.50157 0.05048  -0.01354 0.00860  67  ILE B CG1 
1931 C CG2 . ILE B 67  ? 0.43429 0.39459 0.38857 0.03975  -0.01194 0.00470  67  ILE B CG2 
1932 C CD1 . ILE B 67  ? 0.64782 0.60810 0.58622 0.05411  -0.01868 0.00715  67  ILE B CD1 
1933 N N   . LEU B 68  ? 0.44160 0.38064 0.38814 0.02938  -0.00137 0.00687  68  LEU B N   
1934 C CA  . LEU B 68  ? 0.44406 0.38662 0.39871 0.02357  0.00134  0.00558  68  LEU B CA  
1935 C C   . LEU B 68  ? 0.41654 0.35266 0.37385 0.02022  0.00548  0.00630  68  LEU B C   
1936 O O   . LEU B 68  ? 0.47761 0.41915 0.44458 0.01707  0.00605  0.00515  68  LEU B O   
1937 C CB  . LEU B 68  ? 0.42749 0.36817 0.37737 0.02184  0.00284  0.00560  68  LEU B CB  
1938 C CG  . LEU B 68  ? 0.51933 0.46723 0.47653 0.01769  0.00366  0.00371  68  LEU B CG  
1939 C CD1 . LEU B 68  ? 0.33478 0.29403 0.30050 0.01774  0.00005  0.00171  68  LEU B CD1 
1940 C CD2 . LEU B 68  ? 0.45909 0.40533 0.40880 0.01753  0.00371  0.00366  68  LEU B CD2 
1941 N N   . GLU B 69  ? 0.39823 0.32267 0.34657 0.02066  0.00834  0.00818  69  GLU B N   
1942 C CA  . GLU B 69  ? 0.46453 0.38294 0.41472 0.01673  0.01250  0.00873  69  GLU B CA  
1943 C C   . GLU B 69  ? 0.44133 0.36132 0.39636 0.01705  0.01119  0.00841  69  GLU B C   
1944 O O   . GLU B 69  ? 0.47217 0.39353 0.43424 0.01273  0.01331  0.00789  69  GLU B O   
1945 C CB  . GLU B 69  ? 0.52601 0.43061 0.46390 0.01697  0.01590  0.01068  69  GLU B CB  
1946 C CG  . GLU B 69  ? 0.59350 0.49546 0.52677 0.01549  0.01826  0.01094  69  GLU B CG  
1947 C CD  . GLU B 69  ? 0.63331 0.54314 0.57719 0.01069  0.02054  0.00947  69  GLU B CD  
1948 O OE1 . GLU B 69  ? 0.65508 0.56617 0.60611 0.00678  0.02326  0.00912  69  GLU B OE1 
1949 O OE2 . GLU B 69  ? 0.68621 0.60093 0.63096 0.01092  0.01957  0.00865  69  GLU B OE2 
1950 N N   . ARG B 70  ? 0.39978 0.31988 0.35113 0.02219  0.00773  0.00867  70  ARG B N   
1951 C CA  . ARG B 70  ? 0.43082 0.35260 0.38659 0.02272  0.00650  0.00818  70  ARG B CA  
1952 C C   . ARG B 70  ? 0.45961 0.39385 0.42836 0.01986  0.00482  0.00608  70  ARG B C   
1953 O O   . ARG B 70  ? 0.39541 0.33045 0.37015 0.01661  0.00584  0.00555  70  ARG B O   
1954 C CB  . ARG B 70  ? 0.54687 0.46701 0.49611 0.02958  0.00325  0.00884  70  ARG B CB  
1955 C CG  . ARG B 70  ? 0.65006 0.56095 0.59435 0.03108  0.00441  0.00980  70  ARG B CG  
1956 C CD  . ARG B 70  ? 0.86218 0.77339 0.80139 0.03874  0.00099  0.01027  70  ARG B CD  
1957 N NE  . ARG B 70  ? 0.96601 0.89104 0.91556 0.03982  -0.00250 0.00827  70  ARG B NE  
1958 C CZ  . ARG B 70  ? 0.93392 0.86571 0.88298 0.04589  -0.00623 0.00793  70  ARG B CZ  
1959 N NH1 . ARG B 70  ? 0.91442 0.84106 0.85336 0.05205  -0.00748 0.00959  70  ARG B NH1 
1960 N NH2 . ARG B 70  ? 0.84028 0.78460 0.79915 0.04575  -0.00878 0.00585  70  ARG B NH2 
1961 N N   . LYS B 71  ? 0.39591 0.33940 0.36840 0.02070  0.00230  0.00483  71  LYS B N   
1962 C CA  . LYS B 71  ? 0.43925 0.39331 0.42265 0.01794  0.00090  0.00281  71  LYS B CA  
1963 C C   . LYS B 71  ? 0.41093 0.36529 0.40029 0.01256  0.00409  0.00254  71  LYS B C   
1964 O O   . LYS B 71  ? 0.36089 0.32043 0.35857 0.00991  0.00377  0.00145  71  LYS B O   
1965 C CB  . LYS B 71  ? 0.33290 0.29581 0.31753 0.01953  -0.00218 0.00142  71  LYS B CB  
1966 C CG  . LYS B 71  ? 0.43977 0.40572 0.42069 0.02492  -0.00584 0.00134  71  LYS B CG  
1967 C CD  . LYS B 71  ? 0.35923 0.32913 0.34563 0.02581  -0.00737 0.00040  71  LYS B CD  
1968 C CE  . LYS B 71  ? 0.46749 0.44692 0.46371 0.02188  -0.00823 -0.00189 71  LYS B CE  
1969 N NZ  . LYS B 71  ? 0.56334 0.55201 0.56301 0.02425  -0.01162 -0.00362 71  LYS B NZ  
1970 N N   . ARG B 72  ? 0.35192 0.30092 0.33707 0.01106  0.00721  0.00353  72  ARG B N   
1971 C CA  . ARG B 72  ? 0.31704 0.26713 0.30827 0.00644  0.01051  0.00331  72  ARG B CA  
1972 C C   . ARG B 72  ? 0.33130 0.27828 0.32564 0.00358  0.01243  0.00382  72  ARG B C   
1973 O O   . ARG B 72  ? 0.40475 0.35666 0.40758 0.00015  0.01344  0.00315  72  ARG B O   
1974 C CB  . ARG B 72  ? 0.35789 0.30278 0.34341 0.00563  0.01380  0.00418  72  ARG B CB  
1975 C CG  . ARG B 72  ? 0.38453 0.33352 0.36852 0.00694  0.01235  0.00332  72  ARG B CG  
1976 C CD  . ARG B 72  ? 0.32362 0.26580 0.29959 0.00672  0.01538  0.00430  72  ARG B CD  
1977 N NE  . ARG B 72  ? 0.43678 0.38308 0.41212 0.00686  0.01448  0.00322  72  ARG B NE  
1978 C CZ  . ARG B 72  ? 0.50931 0.45068 0.47726 0.00680  0.01649  0.00371  72  ARG B CZ  
1979 N NH1 . ARG B 72  ? 0.36270 0.29477 0.32308 0.00674  0.01957  0.00529  72  ARG B NH1 
1980 N NH2 . ARG B 72  ? 0.39083 0.33598 0.35817 0.00647  0.01557  0.00250  72  ARG B NH2 
1981 N N   . ALA B 73  ? 0.30491 0.24365 0.29207 0.00495  0.01287  0.00499  73  ALA B N   
1982 C CA  . ALA B 73  ? 0.34917 0.28410 0.33795 0.00173  0.01470  0.00535  73  ALA B CA  
1983 C C   . ALA B 73  ? 0.42578 0.36495 0.41961 0.00223  0.01170  0.00441  73  ALA B C   
1984 O O   . ALA B 73  ? 0.36447 0.30138 0.36035 -0.00097 0.01284  0.00446  73  ALA B O   
1985 C CB  . ALA B 73  ? 0.34675 0.26878 0.32382 0.00245  0.01717  0.00700  73  ALA B CB  
1986 N N   . ALA B 74  ? 0.31006 0.25552 0.30590 0.00571  0.00804  0.00341  74  ALA B N   
1987 C CA  . ALA B 74  ? 0.33010 0.27828 0.32905 0.00667  0.00550  0.00254  74  ALA B CA  
1988 C C   . ALA B 74  ? 0.43730 0.39193 0.44631 0.00230  0.00527  0.00138  74  ALA B C   
1989 O O   . ALA B 74  ? 0.36318 0.31731 0.37394 0.00147  0.00432  0.00096  74  ALA B O   
1990 C CB  . ALA B 74  ? 0.34974 0.30382 0.34834 0.01130  0.00191  0.00160  74  ALA B CB  
1991 N N   . VAL B 75  ? 0.33175 0.29199 0.34687 -0.00027 0.00612  0.00090  75  VAL B N   
1992 C CA  . VAL B 75  ? 0.40271 0.36884 0.42694 -0.00393 0.00579  0.00002  75  VAL B CA  
1993 C C   . VAL B 75  ? 0.33355 0.29526 0.35822 -0.00767 0.00783  0.00079  75  VAL B C   
1994 O O   . VAL B 75  ? 0.40929 0.37350 0.43874 -0.00995 0.00660  0.00018  75  VAL B O   
1995 C CB  . VAL B 75  ? 0.35544 0.32746 0.38514 -0.00525 0.00671  -0.00043 75  VAL B CB  
1996 C CG1 . VAL B 75  ? 0.24741 0.21546 0.27463 -0.00668 0.01056  0.00078  75  VAL B CG1 
1997 C CG2 . VAL B 75  ? 0.17845 0.15660 0.21703 -0.00807 0.00583  -0.00124 75  VAL B CG2 
1998 N N   . ASP B 76  ? 0.36395 0.31875 0.38305 -0.00877 0.01104  0.00205  76  ASP B N   
1999 C CA  . ASP B 76  ? 0.37080 0.32088 0.38920 -0.01303 0.01327  0.00263  76  ASP B CA  
2000 C C   . ASP B 76  ? 0.37950 0.32075 0.38983 -0.01173 0.01277  0.00304  76  ASP B C   
2001 O O   . ASP B 76  ? 0.47087 0.41001 0.48203 -0.01515 0.01302  0.00287  76  ASP B O   
2002 C CB  . ASP B 76  ? 0.34722 0.29316 0.36255 -0.01543 0.01744  0.00361  76  ASP B CB  
2003 C CG  . ASP B 76  ? 0.56471 0.51875 0.58748 -0.01627 0.01852  0.00325  76  ASP B CG  
2004 O OD1 . ASP B 76  ? 0.56242 0.52529 0.59444 -0.01716 0.01670  0.00236  76  ASP B OD1 
2005 O OD2 . ASP B 76  ? 0.58014 0.53102 0.59880 -0.01582 0.02129  0.00390  76  ASP B OD2 
2006 N N   . ARG B 77  ? 0.37612 0.31207 0.37829 -0.00669 0.01203  0.00358  77  ARG B N   
2007 C CA  . ARG B 77  ? 0.32122 0.24741 0.31444 -0.00468 0.01209  0.00419  77  ARG B CA  
2008 C C   . ARG B 77  ? 0.38573 0.31578 0.38225 -0.00281 0.00890  0.00307  77  ARG B C   
2009 O O   . ARG B 77  ? 0.46204 0.38575 0.45485 -0.00390 0.00935  0.00314  77  ARG B O   
2010 C CB  . ARG B 77  ? 0.28158 0.20033 0.26418 0.00068  0.01248  0.00540  77  ARG B CB  
2011 C CG  . ARG B 77  ? 0.38485 0.29610 0.35933 0.00517  0.01136  0.00583  77  ARG B CG  
2012 C CD  . ARG B 77  ? 0.34855 0.24668 0.30965 0.00797  0.01363  0.00760  77  ARG B CD  
2013 N NE  . ARG B 77  ? 0.69035 0.58125 0.64313 0.01360  0.01250  0.00816  77  ARG B NE  
2014 C CZ  . ARG B 77  ? 0.73888 0.61750 0.68314 0.01271  0.01473  0.00885  77  ARG B CZ  
2015 N NH1 . ARG B 77  ? 0.78735 0.66021 0.73065 0.00570  0.01801  0.00890  77  ARG B NH1 
2016 N NH2 . ARG B 77  ? 0.68137 0.55329 0.61753 0.01898  0.01378  0.00945  77  ARG B NH2 
2017 N N   . VAL B 78  ? 0.27240 0.21214 0.27514 -0.00029 0.00594  0.00193  78  VAL B N   
2018 C CA  . VAL B 78  ? 0.33148 0.27496 0.33702 0.00142  0.00321  0.00070  78  VAL B CA  
2019 C C   . VAL B 78  ? 0.30658 0.25666 0.32142 -0.00342 0.00235  -0.00046 78  VAL B C   
2020 O O   . VAL B 78  ? 0.43474 0.38175 0.44950 -0.00582 0.00233  -0.00073 78  VAL B O   
2021 C CB  . VAL B 78  ? 0.42060 0.37087 0.42702 0.00652  0.00048  -0.00013 78  VAL B CB  
2022 C CG1 . VAL B 78  ? 0.28440 0.23910 0.29417 0.00777  -0.00190 -0.00163 78  VAL B CG1 
2023 C CG2 . VAL B 78  ? 0.36736 0.31132 0.36425 0.01179  0.00087  0.00116  78  VAL B CG2 
2024 N N   . CYS B 79  ? 0.33225 0.29077 0.35437 -0.00478 0.00166  -0.00108 79  CYS B N   
2025 C CA  . CYS B 79  ? 0.37178 0.33704 0.40244 -0.00833 0.00034  -0.00215 79  CYS B CA  
2026 C C   . CYS B 79  ? 0.30062 0.26301 0.33289 -0.01340 0.00190  -0.00157 79  CYS B C   
2027 O O   . CYS B 79  ? 0.38447 0.34766 0.41937 -0.01580 0.00058  -0.00224 79  CYS B O   
2028 C CB  . CYS B 79  ? 0.23626 0.20926 0.27281 -0.00846 -0.00006 -0.00265 79  CYS B CB  
2029 S SG  . CYS B 79  ? 0.32669 0.30388 0.36128 -0.00375 -0.00196 -0.00365 79  CYS B SG  
2030 N N   . ARG B 80  ? 0.26720 0.22634 0.29766 -0.01544 0.00478  -0.00043 80  ARG B N   
2031 C CA  . ARG B 80  ? 0.26035 0.21849 0.29319 -0.02096 0.00630  -0.00010 80  ARG B CA  
2032 C C   . ARG B 80  ? 0.33160 0.28041 0.35723 -0.02251 0.00691  0.00012  80  ARG B C   
2033 O O   . ARG B 80  ? 0.43691 0.38624 0.46518 -0.02695 0.00649  -0.00026 80  ARG B O   
2034 C CB  . ARG B 80  ? 0.31437 0.27212 0.34735 -0.02309 0.00962  0.00083  80  ARG B CB  
2035 C CG  . ARG B 80  ? 0.40666 0.37346 0.44717 -0.02209 0.00935  0.00055  80  ARG B CG  
2036 C CD  . ARG B 80  ? 0.37519 0.34299 0.41762 -0.02503 0.01285  0.00126  80  ARG B CD  
2037 N NE  . ARG B 80  ? 0.45699 0.43211 0.50529 -0.02333 0.01310  0.00107  80  ARG B NE  
2038 C CZ  . ARG B 80  ? 0.40706 0.39091 0.46467 -0.02502 0.01267  0.00071  80  ARG B CZ  
2039 N NH1 . ARG B 80  ? 0.38385 0.37134 0.44666 -0.02873 0.01167  0.00052  80  ARG B NH1 
2040 N NH2 . ARG B 80  ? 0.39798 0.38676 0.45926 -0.02279 0.01324  0.00058  80  ARG B NH2 
2041 N N   . HIS B 81  ? 0.36401 0.30388 0.37997 -0.01880 0.00787  0.00075  81  HIS B N   
2042 C CA  . HIS B 81  ? 0.44027 0.37002 0.44820 -0.01953 0.00862  0.00093  81  HIS B CA  
2043 C C   . HIS B 81  ? 0.35748 0.29030 0.36865 -0.01920 0.00576  -0.00031 81  HIS B C   
2044 O O   . HIS B 81  ? 0.39818 0.32692 0.40783 -0.02315 0.00600  -0.00061 81  HIS B O   
2045 C CB  . HIS B 81  ? 0.28707 0.20683 0.28375 -0.01421 0.00992  0.00194  81  HIS B CB  
2046 C CG  . HIS B 81  ? 0.40758 0.31636 0.39511 -0.01331 0.01057  0.00210  81  HIS B CG  
2047 N ND1 . HIS B 81  ? 0.40330 0.29925 0.38075 -0.01598 0.01390  0.00306  81  HIS B ND1 
2048 C CD2 . HIS B 81  ? 0.42011 0.32819 0.40640 -0.01001 0.00868  0.00134  81  HIS B CD2 
2049 C CE1 . HIS B 81  ? 0.48375 0.37092 0.45370 -0.01416 0.01401  0.00297  81  HIS B CE1 
2050 N NE2 . HIS B 81  ? 0.42172 0.31640 0.39722 -0.01038 0.01088  0.00194  81  HIS B NE2 
2051 N N   . ASN B 82  ? 0.36202 0.30176 0.37715 -0.01488 0.00317  -0.00117 82  ASN B N   
2052 C CA  . ASN B 82  ? 0.35026 0.29223 0.36752 -0.01439 0.00082  -0.00247 82  ASN B CA  
2053 C C   . ASN B 82  ? 0.39127 0.33993 0.41687 -0.01957 -0.00069 -0.00328 82  ASN B C   
2054 O O   . ASN B 82  ? 0.30507 0.25198 0.33038 -0.02159 -0.00175 -0.00404 82  ASN B O   
2055 C CB  . ASN B 82  ? 0.32238 0.27024 0.34128 -0.00881 -0.00126 -0.00335 82  ASN B CB  
2056 C CG  . ASN B 82  ? 0.36239 0.30373 0.37262 -0.00298 -0.00051 -0.00272 82  ASN B CG  
2057 O OD1 . ASN B 82  ? 0.32695 0.25797 0.32894 -0.00277 0.00178  -0.00147 82  ASN B OD1 
2058 N ND2 . ASN B 82  ? 0.23298 0.18037 0.24474 0.00177  -0.00242 -0.00361 82  ASN B ND2 
2059 N N   . TYR B 83  ? 0.33602 0.29197 0.36860 -0.02157 -0.00075 -0.00306 83  TYR B N   
2060 C CA  . TYR B 83  ? 0.30651 0.26900 0.34685 -0.02592 -0.00232 -0.00359 83  TYR B CA  
2061 C C   . TYR B 83  ? 0.38993 0.34754 0.42820 -0.03141 -0.00139 -0.00327 83  TYR B C   
2062 O O   . TYR B 83  ? 0.38055 0.34018 0.42170 -0.03445 -0.00335 -0.00397 83  TYR B O   
2063 C CB  . TYR B 83  ? 0.31389 0.28437 0.36134 -0.02638 -0.00201 -0.00321 83  TYR B CB  
2064 C CG  . TYR B 83  ? 0.33895 0.31742 0.39475 -0.02903 -0.00421 -0.00375 83  TYR B CG  
2065 C CD1 . TYR B 83  ? 0.40093 0.38417 0.45999 -0.02685 -0.00672 -0.00479 83  TYR B CD1 
2066 C CD2 . TYR B 83  ? 0.39697 0.37830 0.45707 -0.03374 -0.00378 -0.00324 83  TYR B CD2 
2067 C CE1 . TYR B 83  ? 0.34114 0.33054 0.40667 -0.02881 -0.00878 -0.00513 83  TYR B CE1 
2068 C CE2 . TYR B 83  ? 0.37540 0.36439 0.44300 -0.03551 -0.00614 -0.00356 83  TYR B CE2 
2069 C CZ  . TYR B 83  ? 0.30399 0.29635 0.37385 -0.03278 -0.00864 -0.00441 83  TYR B CZ  
2070 O OH  . TYR B 83  ? 0.30489 0.30369 0.38104 -0.03410 -0.01101 -0.00458 83  TYR B OH  
2071 N N   . GLN B 84  ? 0.33488 0.28555 0.36742 -0.03311 0.00163  -0.00228 84  GLN B N   
2072 C CA  . GLN B 84  ? 0.38969 0.33459 0.41873 -0.03896 0.00287  -0.00215 84  GLN B CA  
2073 C C   . GLN B 84  ? 0.40872 0.34612 0.43146 -0.03876 0.00191  -0.00284 84  GLN B C   
2074 O O   . GLN B 84  ? 0.37419 0.31032 0.39698 -0.04389 0.00122  -0.00331 84  GLN B O   
2075 C CB  . GLN B 84  ? 0.27173 0.20849 0.29356 -0.04058 0.00677  -0.00109 84  GLN B CB  
2076 C CG  . GLN B 84  ? 0.47383 0.41746 0.50153 -0.04175 0.00837  -0.00049 84  GLN B CG  
2077 C CD  . GLN B 84  ? 0.48394 0.43808 0.52191 -0.04713 0.00731  -0.00087 84  GLN B CD  
2078 O OE1 . GLN B 84  ? 0.57211 0.52451 0.60921 -0.05311 0.00784  -0.00108 84  GLN B OE1 
2079 N NE2 . GLN B 84  ? 0.57609 0.54111 0.62343 -0.04494 0.00579  -0.00097 84  GLN B NE2 
2080 N N   . LEU B 85  ? 0.39116 0.32382 0.40838 -0.03286 0.00190  -0.00296 85  LEU B N   
2081 C CA  . LEU B 85  ? 0.41805 0.34474 0.43014 -0.03182 0.00108  -0.00379 85  LEU B CA  
2082 C C   . LEU B 85  ? 0.36862 0.30370 0.38836 -0.03286 -0.00223 -0.00509 85  LEU B C   
2083 O O   . LEU B 85  ? 0.39299 0.32425 0.41030 -0.03552 -0.00297 -0.00583 85  LEU B O   
2084 C CB  . LEU B 85  ? 0.35754 0.27907 0.36301 -0.02457 0.00180  -0.00363 85  LEU B CB  
2085 C CG  . LEU B 85  ? 0.42066 0.33252 0.41685 -0.02217 0.00488  -0.00220 85  LEU B CG  
2086 C CD1 . LEU B 85  ? 0.32809 0.23504 0.31757 -0.01461 0.00498  -0.00213 85  LEU B CD1 
2087 C CD2 . LEU B 85  ? 0.40044 0.30115 0.38884 -0.02783 0.00765  -0.00163 85  LEU B CD2 
2088 N N   . GLU B 86  ? 0.35253 0.29810 0.38059 -0.03092 -0.00408 -0.00539 86  GLU B N   
2089 C CA  . GLU B 86  ? 0.33727 0.28990 0.37167 -0.03195 -0.00707 -0.00656 86  GLU B CA  
2090 C C   . GLU B 86  ? 0.39610 0.35115 0.43445 -0.03827 -0.00823 -0.00647 86  GLU B C   
2091 O O   . GLU B 86  ? 0.38132 0.33700 0.42064 -0.04038 -0.01035 -0.00736 86  GLU B O   
2092 C CB  . GLU B 86  ? 0.29685 0.25880 0.33791 -0.02865 -0.00838 -0.00686 86  GLU B CB  
2093 C CG  . GLU B 86  ? 0.36305 0.32453 0.40103 -0.02277 -0.00753 -0.00694 86  GLU B CG  
2094 C CD  . GLU B 86  ? 0.37813 0.33675 0.41195 -0.01954 -0.00811 -0.00812 86  GLU B CD  
2095 O OE1 . GLU B 86  ? 0.36789 0.32467 0.40119 -0.02179 -0.00909 -0.00903 86  GLU B OE1 
2096 O OE2 . GLU B 86  ? 0.41148 0.37009 0.44256 -0.01462 -0.00756 -0.00817 86  GLU B OE2 
2097 N N   . LEU B 87  ? 0.40349 0.36025 0.44405 -0.04145 -0.00686 -0.00545 87  LEU B N   
2098 C CA  . LEU B 87  ? 0.34298 0.30368 0.38799 -0.04758 -0.00804 -0.00535 87  LEU B CA  
2099 C C   . LEU B 87  ? 0.39215 0.34456 0.43048 -0.05202 -0.00805 -0.00582 87  LEU B C   
2100 O O   . LEU B 87  ? 0.50311 0.45897 0.54466 -0.05647 -0.01035 -0.00621 87  LEU B O   
2101 C CB  . LEU B 87  ? 0.34147 0.30535 0.38945 -0.05023 -0.00586 -0.00431 87  LEU B CB  
2102 C CG  . LEU B 87  ? 0.38756 0.36169 0.44418 -0.04767 -0.00613 -0.00385 87  LEU B CG  
2103 C CD1 . LEU B 87  ? 0.39421 0.36909 0.45154 -0.04997 -0.00292 -0.00294 87  LEU B CD1 
2104 C CD2 . LEU B 87  ? 0.32236 0.30631 0.38772 -0.04915 -0.00946 -0.00416 87  LEU B CD2 
2105 N N   . ARG B 88  ? 0.38307 0.32414 0.41152 -0.05076 -0.00553 -0.00576 88  ARG B N   
2106 C CA  . ARG B 88  ? 0.46232 0.39330 0.48248 -0.05460 -0.00490 -0.00625 88  ARG B CA  
2107 C C   . ARG B 88  ? 0.48216 0.41023 0.49967 -0.05198 -0.00654 -0.00741 88  ARG B C   
2108 O O   . ARG B 88  ? 0.52369 0.44402 0.53490 -0.05547 -0.00638 -0.00799 88  ARG B O   
2109 C CB  . ARG B 88  ? 0.48628 0.40467 0.49552 -0.05413 -0.00092 -0.00556 88  ARG B CB  
2110 C CG  . ARG B 88  ? 0.68457 0.60359 0.69433 -0.05747 0.00148  -0.00456 88  ARG B CG  
2111 C CD  . ARG B 88  ? 0.66877 0.57601 0.66794 -0.05401 0.00524  -0.00371 88  ARG B CD  
2112 N NE  . ARG B 88  ? 0.72950 0.62318 0.71706 -0.05291 0.00657  -0.00404 88  ARG B NE  
2113 C CZ  . ARG B 88  ? 0.72296 0.60406 0.69918 -0.04936 0.00973  -0.00330 88  ARG B CZ  
2114 N NH1 . ARG B 88  ? 0.80831 0.68817 0.78273 -0.04686 0.01179  -0.00218 88  ARG B NH1 
2115 N NH2 . ARG B 88  ? 0.79526 0.66416 0.76110 -0.04808 0.01094  -0.00365 88  ARG B NH2 
2116 N N   . THR B 89  ? 0.44396 0.53731 0.36821 -0.03087 0.00374  0.03021  89  THR B N   
2117 C CA  . THR B 89  ? 0.34606 0.42155 0.26533 -0.02781 0.00385  0.02633  89  THR B CA  
2118 C C   . THR B 89  ? 0.42212 0.50227 0.35378 -0.02073 0.00577  0.02278  89  THR B C   
2119 O O   . THR B 89  ? 0.36803 0.44911 0.30289 -0.02265 0.00434  0.02507  89  THR B O   
2120 C CB  . THR B 89  ? 0.40170 0.46578 0.31298 -0.02410 0.00544  0.02179  89  THR B CB  
2121 O OG1 . THR B 89  ? 0.35781 0.43352 0.27873 -0.01742 0.00863  0.01795  89  THR B OG1 
2122 C CG2 . THR B 89  ? 0.32723 0.38215 0.22294 -0.03127 0.00282  0.02513  89  THR B CG2 
2123 N N   . THR B 90  ? 0.35761 0.43995 0.29554 -0.01281 0.00861  0.01731  90  THR B N   
2124 C CA  . THR B 90  ? 0.30031 0.38439 0.24810 -0.00637 0.00976  0.01374  90  THR B CA  
2125 C C   . THR B 90  ? 0.31571 0.41349 0.27279 -0.00600 0.00905  0.01622  90  THR B C   
2126 O O   . THR B 90  ? 0.33517 0.43018 0.29591 -0.00505 0.00832  0.01601  90  THR B O   
2127 C CB  . THR B 90  ? 0.31988 0.40599 0.27250 0.00126  0.01212  0.00824  90  THR B CB  
2128 O OG1 . THR B 90  ? 0.32076 0.42031 0.27679 0.00284  0.01299  0.00885  90  THR B OG1 
2129 C CG2 . THR B 90  ? 0.26523 0.33805 0.20919 0.00180  0.01295  0.00544  90  THR B CG2 
2130 N N   . LEU B 91  ? 0.31427 0.42759 0.27496 -0.00629 0.00929  0.01873  91  LEU B N   
2131 C CA  . LEU B 91  ? 0.33201 0.46051 0.30126 -0.00443 0.00883  0.02101  91  LEU B CA  
2132 C C   . LEU B 91  ? 0.33949 0.46906 0.30644 -0.01231 0.00632  0.02680  91  LEU B C   
2133 O O   . LEU B 91  ? 0.36226 0.50347 0.33591 -0.01084 0.00578  0.02875  91  LEU B O   
2134 C CB  . LEU B 91  ? 0.25677 0.40366 0.23048 -0.00125 0.01005  0.02227  91  LEU B CB  
2135 C CG  . LEU B 91  ? 0.28127 0.42866 0.25865 0.00840  0.01215  0.01630  91  LEU B CG  
2136 C CD1 . LEU B 91  ? 0.34730 0.51264 0.32782 0.01198  0.01341  0.01785  91  LEU B CD1 
2137 C CD2 . LEU B 91  ? 0.28755 0.43194 0.27075 0.01576  0.01185  0.01225  91  LEU B CD2 
2138 N N   . GLN B 92  ? 0.31955 0.43663 0.27628 -0.02018 0.00447  0.02951  92  GLN B N   
2139 C CA  . GLN B 92  ? 0.32413 0.43851 0.27690 -0.02793 0.00142  0.03480  92  GLN B CA  
2140 C C   . GLN B 92  ? 0.48470 0.58178 0.43384 -0.02745 0.00063  0.03273  92  GLN B C   
2141 O O   . GLN B 92  ? 0.54173 0.63436 0.48711 -0.03309 -0.00203 0.03662  92  GLN B O   
2142 C CB  . GLN B 92  ? 0.36569 0.47630 0.30722 -0.03763 -0.00124 0.04004  92  GLN B CB  
2143 C CG  . GLN B 92  ? 0.65282 0.78402 0.59828 -0.04257 -0.00228 0.04611  92  GLN B CG  
2144 C CD  . GLN B 92  ? 0.90444 1.02960 0.83741 -0.05427 -0.00625 0.05239  92  GLN B CD  
2145 O OE1 . GLN B 92  ? 0.89359 0.99754 0.81382 -0.05815 -0.00857 0.05203  92  GLN B OE1 
2146 N NE2 . GLN B 92  ? 0.91571 1.05942 0.85134 -0.05984 -0.00739 0.05848  92  GLN B NE2 
2147 N N   . ARG B 93  ? 0.37299 0.46088 0.32308 -0.02099 0.00272  0.02709  93  ARG B N   
2148 C CA  . ARG B 93  ? 0.38256 0.45539 0.32917 -0.02020 0.00225  0.02549  93  ARG B CA  
2149 C C   . ARG B 93  ? 0.49773 0.57555 0.45285 -0.01828 0.00181  0.02579  93  ARG B C   
2150 O O   . ARG B 93  ? 0.33582 0.42295 0.30049 -0.01227 0.00323  0.02297  93  ARG B O   
2151 C CB  . ARG B 93  ? 0.37855 0.44339 0.32486 -0.01409 0.00458  0.02001  93  ARG B CB  
2152 C CG  . ARG B 93  ? 0.38911 0.44069 0.33236 -0.01264 0.00446  0.01864  93  ARG B CG  
2153 C CD  . ARG B 93  ? 0.32944 0.37529 0.27159 -0.00753 0.00660  0.01416  93  ARG B CD  
2154 N NE  . ARG B 93  ? 0.38790 0.42535 0.33008 -0.00515 0.00688  0.01296  93  ARG B NE  
2155 C CZ  . ARG B 93  ? 0.35926 0.38469 0.29126 -0.00674 0.00604  0.01463  93  ARG B CZ  
2156 N NH1 . ARG B 93  ? 0.34833 0.36644 0.26808 -0.01095 0.00430  0.01742  93  ARG B NH1 
2157 N NH2 . ARG B 93  ? 0.27013 0.29042 0.20333 -0.00390 0.00665  0.01373  93  ARG B NH2 
2158 N N   . ARG B 94  ? 0.48785 0.55829 0.43827 -0.02310 -0.00049 0.02913  94  ARG B N   
2159 C CA  . ARG B 94  ? 0.39126 0.46451 0.34815 -0.02193 -0.00119 0.02972  94  ARG B CA  
2160 C C   . ARG B 94  ? 0.43325 0.48965 0.38392 -0.02254 -0.00200 0.02937  94  ARG B C   
2161 O O   . ARG B 94  ? 0.54956 0.59609 0.49010 -0.02808 -0.00437 0.03284  94  ARG B O   
2162 C CB  . ARG B 94  ? 0.40005 0.48436 0.35821 -0.02759 -0.00350 0.03521  94  ARG B CB  
2163 C CG  . ARG B 94  ? 0.40909 0.51313 0.37386 -0.02654 -0.00263 0.03646  94  ARG B CG  
2164 C CD  . ARG B 94  ? 0.35525 0.46962 0.33067 -0.01763 -0.00062 0.03253  94  ARG B CD  
2165 N NE  . ARG B 94  ? 0.55977 0.69476 0.54092 -0.01593 -0.00013 0.03467  94  ARG B NE  
2166 C CZ  . ARG B 94  ? 0.62969 0.77232 0.61196 -0.01286 0.00158  0.03328  94  ARG B CZ  
2167 N NH1 . ARG B 94  ? 0.47112 0.60238 0.44949 -0.01125 0.00293  0.02944  94  ARG B NH1 
2168 N NH2 . ARG B 94  ? 0.56258 0.72551 0.54987 -0.01099 0.00200  0.03596  94  ARG B NH2 
2169 N N   . VAL B 95  ? 0.37584 0.42869 0.33169 -0.01687 -0.00038 0.02551  95  VAL B N   
2170 C CA  . VAL B 95  ? 0.36449 0.40374 0.31584 -0.01648 -0.00074 0.02532  95  VAL B CA  
2171 C C   . VAL B 95  ? 0.43015 0.47277 0.38967 -0.01442 -0.00107 0.02494  95  VAL B C   
2172 O O   . VAL B 95  ? 0.44116 0.48951 0.40893 -0.00952 0.00013  0.02163  95  VAL B O   
2173 C CB  . VAL B 95  ? 0.34876 0.38082 0.29812 -0.01220 0.00133  0.02172  95  VAL B CB  
2174 C CG1 . VAL B 95  ? 0.35883 0.37948 0.30426 -0.01125 0.00114  0.02215  95  VAL B CG1 
2175 C CG2 . VAL B 95  ? 0.33170 0.35975 0.27174 -0.01374 0.00156  0.02189  95  VAL B CG2 
2176 N N   . GLU B 96  ? 0.48624 0.52427 0.44244 -0.01809 -0.00310 0.02829  96  GLU B N   
2177 C CA  . GLU B 96  ? 0.39163 0.43284 0.35474 -0.01644 -0.00364 0.02820  96  GLU B CA  
2178 C C   . GLU B 96  ? 0.32736 0.36052 0.29269 -0.01216 -0.00244 0.02523  96  GLU B C   
2179 O O   . GLU B 96  ? 0.35997 0.38244 0.31886 -0.01225 -0.00198 0.02538  96  GLU B O   
2180 C CB  . GLU B 96  ? 0.56467 0.60213 0.52298 -0.02171 -0.00629 0.03267  96  GLU B CB  
2181 C CG  . GLU B 96  ? 0.62081 0.66617 0.57619 -0.02762 -0.00828 0.03682  96  GLU B CG  
2182 C CD  . GLU B 96  ? 0.65850 0.69820 0.60799 -0.03348 -0.01159 0.04151  96  GLU B CD  
2183 O OE1 . GLU B 96  ? 0.78266 0.82493 0.73742 -0.03227 -0.01208 0.04176  96  GLU B OE1 
2184 O OE2 . GLU B 96  ? 0.93201 0.96340 0.87060 -0.03922 -0.01407 0.04489  96  GLU B OE2 
2185 N N   . PRO B 97  ? 0.31649 0.35458 0.28996 -0.00826 -0.00218 0.02280  97  PRO B N   
2186 C CA  . PRO B 97  ? 0.41672 0.44742 0.39218 -0.00528 -0.00159 0.02061  97  PRO B CA  
2187 C C   . PRO B 97  ? 0.47098 0.49253 0.44292 -0.00719 -0.00250 0.02305  97  PRO B C   
2188 O O   . PRO B 97  ? 0.49123 0.51346 0.46211 -0.00968 -0.00402 0.02556  97  PRO B O   
2189 C CB  . PRO B 97  ? 0.32869 0.36620 0.31187 -0.00105 -0.00207 0.01769  97  PRO B CB  
2190 C CG  . PRO B 97  ? 0.40243 0.45079 0.38749 -0.00159 -0.00294 0.01923  97  PRO B CG  
2191 C CD  . PRO B 97  ? 0.33741 0.38841 0.31771 -0.00578 -0.00251 0.02181  97  PRO B CD  
2192 N N   . THR B 98  ? 0.47281 0.48647 0.44293 -0.00588 -0.00161 0.02255  98  THR B N   
2193 C CA  . THR B 98  ? 0.31766 0.32308 0.28547 -0.00631 -0.00215 0.02444  98  THR B CA  
2194 C C   . THR B 98  ? 0.35600 0.36267 0.33122 -0.00395 -0.00253 0.02242  98  THR B C   
2195 O O   . THR B 98  ? 0.41498 0.42298 0.39382 -0.00191 -0.00194 0.02011  98  THR B O   
2196 C CB  . THR B 98  ? 0.49968 0.49716 0.46054 -0.00569 -0.00095 0.02564  98  THR B CB  
2197 O OG1 . THR B 98  ? 0.57167 0.56571 0.52329 -0.00760 -0.00129 0.02737  98  THR B OG1 
2198 C CG2 . THR B 98  ? 0.29553 0.28528 0.25401 -0.00534 -0.00134 0.02781  98  THR B CG2 
2199 N N   . VAL B 99  ? 0.34819 0.35382 0.32487 -0.00442 -0.00393 0.02336  99  VAL B N   
2200 C CA  . VAL B 99  ? 0.48298 0.48864 0.46508 -0.00216 -0.00494 0.02141  99  VAL B CA  
2201 C C   . VAL B 99  ? 0.42270 0.41956 0.40294 -0.00279 -0.00510 0.02327  99  VAL B C   
2202 O O   . VAL B 99  ? 0.40338 0.39588 0.37937 -0.00449 -0.00541 0.02596  99  VAL B O   
2203 C CB  . VAL B 99  ? 0.43330 0.44569 0.41833 -0.00114 -0.00642 0.02076  99  VAL B CB  
2204 C CG1 . VAL B 99  ? 0.32151 0.33249 0.31015 0.00221  -0.00789 0.01814  99  VAL B CG1 
2205 C CG2 . VAL B 99  ? 0.29464 0.31723 0.28092 -0.00056 -0.00601 0.01989  99  VAL B CG2 
2206 N N   . THR B 100 ? 0.40003 0.39419 0.38306 -0.00161 -0.00522 0.02210  100 THR B N   
2207 C CA  . THR B 100 ? 0.36167 0.34889 0.34332 -0.00221 -0.00505 0.02423  100 THR B CA  
2208 C C   . THR B 100 ? 0.34260 0.32781 0.32836 -0.00149 -0.00684 0.02255  100 THR B C   
2209 O O   . THR B 100 ? 0.37992 0.36752 0.36839 -0.00073 -0.00772 0.02018  100 THR B O   
2210 C CB  . THR B 100 ? 0.40507 0.39142 0.38381 -0.00241 -0.00310 0.02600  100 THR B CB  
2211 O OG1 . THR B 100 ? 0.57358 0.55673 0.54520 -0.00276 -0.00216 0.02847  100 THR B OG1 
2212 C CG2 . THR B 100 ? 0.54426 0.52742 0.52426 -0.00260 -0.00303 0.02776  100 THR B CG2 
2213 N N   . ILE B 101 ? 0.38732 0.36703 0.37257 -0.00177 -0.00780 0.02377  101 ILE B N   
2214 C CA  . ILE B 101 ? 0.46019 0.43572 0.44755 -0.00158 -0.00996 0.02263  101 ILE B CA  
2215 C C   . ILE B 101 ? 0.44515 0.41651 0.43180 -0.00347 -0.00921 0.02591  101 ILE B C   
2216 O O   . ILE B 101 ? 0.55369 0.52291 0.53744 -0.00364 -0.00758 0.02883  101 ILE B O   
2217 C CB  . ILE B 101 ? 0.42582 0.39849 0.41286 -0.00004 -0.01189 0.02132  101 ILE B CB  
2218 C CG1 . ILE B 101 ? 0.37947 0.35903 0.36729 0.00238  -0.01243 0.01878  101 ILE B CG1 
2219 C CG2 . ILE B 101 ? 0.37648 0.34277 0.36374 0.00023  -0.01469 0.01996  101 ILE B CG2 
2220 C CD1 . ILE B 101 ? 0.35838 0.33719 0.34568 0.00470  -0.01425 0.01761  101 ILE B CD1 
2221 N N   . SER B 102 ? 0.48076 0.45109 0.46944 -0.00486 -0.01070 0.02576  102 SER B N   
2222 C CA  . SER B 102 ? 0.55047 0.51865 0.53915 -0.00706 -0.01034 0.02944  102 SER B CA  
2223 C C   . SER B 102 ? 0.50487 0.46840 0.49482 -0.00912 -0.01401 0.02854  102 SER B C   
2224 O O   . SER B 102 ? 0.58929 0.55332 0.58007 -0.00925 -0.01623 0.02582  102 SER B O   
2225 C CB  . SER B 102 ? 0.43808 0.41251 0.42701 -0.00778 -0.00789 0.03208  102 SER B CB  
2226 O OG  . SER B 102 ? 0.77275 0.75118 0.76415 -0.00863 -0.00898 0.03002  102 SER B OG  
2227 N N   . PRO B 103 ? 0.61791 0.57591 0.60703 -0.01069 -0.01511 0.03077  103 PRO B N   
2228 C CA  . PRO B 103 ? 0.59269 0.54437 0.58133 -0.01336 -0.01934 0.03028  103 PRO B CA  
2229 C C   . PRO B 103 ? 0.77623 0.73201 0.76696 -0.01767 -0.02010 0.03335  103 PRO B C   
2230 O O   . PRO B 103 ? 0.75619 0.72032 0.74893 -0.01811 -0.01685 0.03639  103 PRO B O   
2231 C CB  . PRO B 103 ? 0.60888 0.55404 0.59572 -0.01381 -0.01969 0.03231  103 PRO B CB  
2232 C CG  . PRO B 103 ? 0.60694 0.55711 0.59423 -0.01271 -0.01529 0.03586  103 PRO B CG  
2233 C CD  . PRO B 103 ? 0.67767 0.63379 0.66516 -0.01002 -0.01290 0.03391  103 PRO B CD  
2234 N N   . SER B 104 ? 0.79471 0.74419 0.78402 -0.02080 -0.02489 0.03266  104 SER B N   
2235 C CA  . SER B 104 ? 0.88890 0.84177 0.87990 -0.02603 -0.02686 0.03576  104 SER B CA  
2236 C C   . SER B 104 ? 1.01784 0.96057 1.00551 -0.03074 -0.03234 0.03712  104 SER B C   
2237 O O   . SER B 104 ? 1.04785 0.98179 1.03214 -0.02945 -0.03369 0.03600  104 SER B O   
2238 C CB  . SER B 104 ? 0.75756 0.71344 0.74917 -0.02510 -0.02794 0.03252  104 SER B CB  
2239 O OG  . SER B 104 ? 0.83934 0.79922 0.83275 -0.03049 -0.02999 0.03578  104 SER B OG  
2240 N N   . ARG B 105 ? 1.09653 1.04010 1.08453 -0.03653 -0.03587 0.03972  105 ARG B N   
2241 C CA  . ARG B 105 ? 1.08710 1.01991 1.07061 -0.04230 -0.04216 0.04149  105 ARG B CA  
2242 C C   . ARG B 105 ? 1.14000 1.07264 1.12271 -0.04766 -0.04696 0.04245  105 ARG B C   
2243 O O   . ARG B 105 ? 1.34071 1.28593 1.32876 -0.04910 -0.04428 0.04488  105 ARG B O   
2244 C CB  . ARG B 105 ? 0.89180 0.82797 0.87729 -0.04671 -0.04082 0.04793  105 ARG B CB  
2245 N N   . THR B 106 ? 1.18581 1.10342 1.16084 -0.05032 -0.05439 0.04050  106 THR B N   
2246 C CA  . THR B 106 ? 1.15272 1.06700 1.12505 -0.05596 -0.06039 0.04144  106 THR B CA  
2247 C C   . THR B 106 ? 1.25950 1.16229 1.22560 -0.06475 -0.06789 0.04557  106 THR B C   
2248 O O   . THR B 106 ? 1.28246 1.18845 1.25080 -0.06896 -0.06661 0.05072  106 THR B O   
2249 C CB  . THR B 106 ? 1.08607 0.99061 1.05218 -0.05009 -0.06375 0.03431  106 THR B CB  
2250 O OG1 . THR B 106 ? 1.02879 0.92039 0.98763 -0.04401 -0.06542 0.02948  106 THR B OG1 
2251 C CG2 . THR B 106 ? 1.04626 0.96430 1.01913 -0.04422 -0.05740 0.03171  106 THR B CG2 
2252 N N   . HIS B 112 ? 1.11389 1.01520 1.08555 -0.03230 -0.03980 0.03944  112 HIS B N   
2253 C CA  . HIS B 112 ? 1.07329 0.98005 1.04664 -0.02810 -0.03842 0.03528  112 HIS B CA  
2254 C C   . HIS B 112 ? 0.89444 0.79018 0.86093 -0.02579 -0.04401 0.02971  112 HIS B C   
2255 O O   . HIS B 112 ? 0.84064 0.72479 0.80068 -0.02359 -0.04724 0.02711  112 HIS B O   
2256 C CB  . HIS B 112 ? 0.92395 0.83697 0.90017 -0.02203 -0.03299 0.03355  112 HIS B CB  
2257 C CG  . HIS B 112 ? 0.97839 0.90257 0.95974 -0.02266 -0.02760 0.03818  112 HIS B CG  
2258 N ND1 . HIS B 112 ? 1.00696 0.93314 0.98885 -0.01895 -0.02362 0.03877  112 HIS B ND1 
2259 C CD2 . HIS B 112 ? 0.94892 0.88253 0.93394 -0.02597 -0.02582 0.04248  112 HIS B CD2 
2260 C CE1 . HIS B 112 ? 0.98410 0.91915 0.96868 -0.01943 -0.01980 0.04305  112 HIS B CE1 
2261 N NE2 . HIS B 112 ? 0.84665 0.78724 0.83348 -0.02340 -0.02079 0.04537  112 HIS B NE2 
2262 N N   . ASN B 113 ? 0.90238 0.80147 0.86941 -0.02562 -0.04524 0.02783  113 ASN B N   
2263 C CA  . ASN B 113 ? 0.79932 0.68828 0.75882 -0.02200 -0.05048 0.02244  113 ASN B CA  
2264 C C   . ASN B 113 ? 0.67444 0.57155 0.63659 -0.01800 -0.04872 0.01930  113 ASN B C   
2265 O O   . ASN B 113 ? 0.55148 0.44111 0.50724 -0.01513 -0.05333 0.01538  113 ASN B O   
2266 C CB  . ASN B 113 ? 0.69779 0.57400 0.65004 -0.02799 -0.05800 0.02375  113 ASN B CB  
2267 C CG  . ASN B 113 ? 0.88767 0.77068 0.84381 -0.03388 -0.05884 0.02687  113 ASN B CG  
2268 O OD1 . ASN B 113 ? 0.96901 0.86681 0.93410 -0.03553 -0.05331 0.03019  113 ASN B OD1 
2269 N ND2 . ASN B 113 ? 0.80187 0.67349 0.75030 -0.03678 -0.06613 0.02581  113 ASN B ND2 
2270 N N   . LEU B 114 ? 0.65071 0.56185 0.62084 -0.01729 -0.04257 0.02083  114 LEU B N   
2271 C CA  . LEU B 114 ? 0.70051 0.61958 0.67317 -0.01419 -0.04083 0.01828  114 LEU B CA  
2272 C C   . LEU B 114 ? 0.59145 0.52245 0.57001 -0.01128 -0.03422 0.01882  114 LEU B C   
2273 O O   . LEU B 114 ? 0.54488 0.48163 0.52746 -0.01407 -0.03055 0.02295  114 LEU B O   
2274 C CB  . LEU B 114 ? 0.79166 0.71409 0.76653 -0.01960 -0.04222 0.02082  114 LEU B CB  
2275 C CG  . LEU B 114 ? 0.81559 0.74548 0.79278 -0.01687 -0.04076 0.01830  114 LEU B CG  
2276 C CD1 . LEU B 114 ? 0.65863 0.58062 0.62921 -0.01104 -0.04480 0.01269  114 LEU B CD1 
2277 C CD2 . LEU B 114 ? 0.79603 0.72973 0.77573 -0.02286 -0.04209 0.02152  114 LEU B CD2 
2278 N N   . LEU B 115 ? 0.55522 0.48975 0.53337 -0.00559 -0.03306 0.01498  115 LEU B N   
2279 C CA  . LEU B 115 ? 0.56896 0.51401 0.55145 -0.00344 -0.02774 0.01546  115 LEU B CA  
2280 C C   . LEU B 115 ? 0.55776 0.51070 0.54260 -0.00248 -0.02628 0.01416  115 LEU B C   
2281 O O   . LEU B 115 ? 0.43814 0.38935 0.42051 0.00045  -0.02906 0.01070  115 LEU B O   
2282 C CB  . LEU B 115 ? 0.45030 0.39554 0.43102 0.00159  -0.02737 0.01295  115 LEU B CB  
2283 C CG  . LEU B 115 ? 0.55178 0.49098 0.53088 0.00112  -0.02759 0.01440  115 LEU B CG  
2284 C CD1 . LEU B 115 ? 0.40712 0.34881 0.38497 0.00617  -0.02715 0.01207  115 LEU B CD1 
2285 C CD2 . LEU B 115 ? 0.46001 0.40206 0.44240 -0.00275 -0.02393 0.01905  115 LEU B CD2 
2286 N N   . VAL B 116 ? 0.46981 0.43071 0.45838 -0.00430 -0.02208 0.01682  116 VAL B N   
2287 C CA  . VAL B 116 ? 0.45471 0.42315 0.44524 -0.00346 -0.02026 0.01577  116 VAL B CA  
2288 C C   . VAL B 116 ? 0.40576 0.38086 0.39703 -0.00098 -0.01658 0.01556  116 VAL B C   
2289 O O   . VAL B 116 ? 0.40947 0.38617 0.40089 -0.00232 -0.01374 0.01854  116 VAL B O   
2290 C CB  . VAL B 116 ? 0.47248 0.44469 0.46532 -0.00742 -0.01885 0.01903  116 VAL B CB  
2291 C CG1 . VAL B 116 ? 0.44039 0.42008 0.43469 -0.00600 -0.01677 0.01760  116 VAL B CG1 
2292 C CG2 . VAL B 116 ? 0.46792 0.43421 0.45999 -0.01116 -0.02318 0.01998  116 VAL B CG2 
2293 N N   . CYS B 117 ? 0.39812 0.37695 0.38907 0.00264  -0.01698 0.01237  117 CYS B N   
2294 C CA  . CYS B 117 ? 0.42551 0.41187 0.41710 0.00398  -0.01399 0.01260  117 CYS B CA  
2295 C C   . CYS B 117 ? 0.40106 0.39311 0.39375 0.00339  -0.01197 0.01249  117 CYS B C   
2296 O O   . CYS B 117 ? 0.36656 0.36059 0.35969 0.00542  -0.01323 0.00979  117 CYS B O   
2297 C CB  . CYS B 117 ? 0.50430 0.49398 0.49518 0.00824  -0.01530 0.00995  117 CYS B CB  
2298 S SG  . CYS B 117 ? 0.46036 0.46026 0.45205 0.00822  -0.01224 0.01146  117 CYS B SG  
2299 N N   . SER B 118 ? 0.39734 0.39116 0.38942 0.00118  -0.00905 0.01534  118 SER B N   
2300 C CA  . SER B 118 ? 0.34486 0.34350 0.33672 0.00090  -0.00692 0.01541  118 SER B CA  
2301 C C   . SER B 118 ? 0.41459 0.41836 0.40496 0.00193  -0.00546 0.01496  118 SER B C   
2302 O O   . SER B 118 ? 0.32250 0.32532 0.31034 0.00082  -0.00464 0.01713  118 SER B O   
2303 C CB  . SER B 118 ? 0.31939 0.31687 0.30948 -0.00111 -0.00482 0.01882  118 SER B CB  
2304 O OG  . SER B 118 ? 0.48553 0.48068 0.47761 -0.00276 -0.00617 0.01997  118 SER B OG  
2305 N N   . VAL B 119 ? 0.31375 0.32274 0.30526 0.00376  -0.00545 0.01245  119 VAL B N   
2306 C CA  . VAL B 119 ? 0.34426 0.35959 0.33462 0.00427  -0.00423 0.01235  119 VAL B CA  
2307 C C   . VAL B 119 ? 0.36620 0.38341 0.35481 0.00370  -0.00226 0.01226  119 VAL B C   
2308 O O   . VAL B 119 ? 0.38075 0.40049 0.37127 0.00551  -0.00249 0.00977  119 VAL B O   
2309 C CB  . VAL B 119 ? 0.31388 0.33497 0.30654 0.00782  -0.00576 0.00966  119 VAL B CB  
2310 C CG1 . VAL B 119 ? 0.33134 0.36087 0.32325 0.00754  -0.00453 0.01066  119 VAL B CG1 
2311 C CG2 . VAL B 119 ? 0.29176 0.30972 0.28514 0.00942  -0.00806 0.00921  119 VAL B CG2 
2312 N N   . THR B 120 ? 0.33911 0.35416 0.32300 0.00160  -0.00061 0.01489  120 THR B N   
2313 C CA  . THR B 120 ? 0.40773 0.42264 0.38827 0.00157  0.00120  0.01505  120 THR B CA  
2314 C C   . THR B 120 ? 0.37893 0.39572 0.35430 0.00060  0.00211  0.01572  120 THR B C   
2315 O O   . THR B 120 ? 0.30391 0.32039 0.27675 -0.00134 0.00135  0.01759  120 THR B O   
2316 C CB  . THR B 120 ? 0.39509 0.40447 0.37199 0.00093  0.00212  0.01774  120 THR B CB  
2317 O OG1 . THR B 120 ? 0.42802 0.43242 0.40017 -0.00042 0.00181  0.02049  120 THR B OG1 
2318 C CG2 . THR B 120 ? 0.31496 0.32354 0.29703 0.00100  0.00111  0.01761  120 THR B CG2 
2319 N N   . ASP B 121 ? 0.38629 0.40500 0.35983 0.00162  0.00343  0.01435  121 ASP B N   
2320 C CA  . ASP B 121 ? 0.41320 0.43155 0.37967 0.00051  0.00426  0.01516  121 ASP B CA  
2321 C C   . ASP B 121 ? 0.39562 0.41942 0.36298 -0.00126 0.00327  0.01558  121 ASP B C   
2322 O O   . ASP B 121 ? 0.47485 0.49602 0.43647 -0.00442 0.00237  0.01844  121 ASP B O   
2323 C CB  . ASP B 121 ? 0.38304 0.39273 0.33986 -0.00064 0.00442  0.01825  121 ASP B CB  
2324 C CG  . ASP B 121 ? 0.58361 0.59059 0.53840 0.00193  0.00588  0.01829  121 ASP B CG  
2325 O OD1 . ASP B 121 ? 0.43138 0.44321 0.39058 0.00373  0.00688  0.01596  121 ASP B OD1 
2326 O OD2 . ASP B 121 ? 0.66995 0.67054 0.61852 0.00236  0.00592  0.02090  121 ASP B OD2 
2327 N N   . PHE B 122 ? 0.35944 0.39120 0.33345 0.00089  0.00318  0.01301  122 PHE B N   
2328 C CA  . PHE B 122 ? 0.42196 0.46204 0.39735 0.00006  0.00260  0.01364  122 PHE B CA  
2329 C C   . PHE B 122 ? 0.35856 0.40487 0.33504 0.00224  0.00370  0.01126  122 PHE B C   
2330 O O   . PHE B 122 ? 0.32920 0.37410 0.30749 0.00518  0.00446  0.00835  122 PHE B O   
2331 C CB  . PHE B 122 ? 0.37244 0.41790 0.35413 0.00185  0.00120  0.01327  122 PHE B CB  
2332 C CG  . PHE B 122 ? 0.36775 0.41333 0.35471 0.00650  0.00069  0.00964  122 PHE B CG  
2333 C CD1 . PHE B 122 ? 0.25634 0.30901 0.24625 0.01054  0.00061  0.00694  122 PHE B CD1 
2334 C CD2 . PHE B 122 ? 0.28196 0.31999 0.27003 0.00676  -0.00015 0.00920  122 PHE B CD2 
2335 C CE1 . PHE B 122 ? 0.27641 0.32689 0.26919 0.01480  -0.00078 0.00366  122 PHE B CE1 
2336 C CE2 . PHE B 122 ? 0.29744 0.33398 0.28894 0.01013  -0.00154 0.00625  122 PHE B CE2 
2337 C CZ  . PHE B 122 ? 0.26842 0.31033 0.26172 0.01417  -0.00211 0.00337  122 PHE B CZ  
2338 N N   . TYR B 123 ? 0.32197 0.37561 0.29718 0.00040  0.00360  0.01292  123 TYR B N   
2339 C CA  . TYR B 123 ? 0.31674 0.37775 0.29298 0.00245  0.00464  0.01116  123 TYR B CA  
2340 C C   . TYR B 123 ? 0.36361 0.43640 0.34149 0.00082  0.00397  0.01387  123 TYR B C   
2341 O O   . TYR B 123 ? 0.44038 0.51257 0.41439 -0.00451 0.00282  0.01791  123 TYR B O   
2342 C CB  . TYR B 123 ? 0.33453 0.38960 0.30333 0.00060  0.00581  0.01110  123 TYR B CB  
2343 C CG  . TYR B 123 ? 0.38337 0.44481 0.35366 0.00354  0.00709  0.00853  123 TYR B CG  
2344 C CD1 . TYR B 123 ? 0.35901 0.42916 0.32818 0.00168  0.00713  0.01040  123 TYR B CD1 
2345 C CD2 . TYR B 123 ? 0.29553 0.35483 0.26843 0.00797  0.00805  0.00455  123 TYR B CD2 
2346 C CE1 . TYR B 123 ? 0.24551 0.32171 0.21598 0.00480  0.00842  0.00811  123 TYR B CE1 
2347 C CE2 . TYR B 123 ? 0.28259 0.34706 0.25656 0.01101  0.00907  0.00206  123 TYR B CE2 
2348 C CZ  . TYR B 123 ? 0.30717 0.37993 0.27989 0.00976  0.00941  0.00370  123 TYR B CZ  
2349 O OH  . TYR B 123 ? 0.34224 0.42025 0.31589 0.01319  0.01055  0.00127  123 TYR B OH  
2350 N N   . PRO B 124 ? 0.35179 0.43577 0.33476 0.00531  0.00440  0.01216  124 PRO B N   
2351 C CA  . PRO B 124 ? 0.32000 0.40384 0.30620 0.01164  0.00510  0.00749  124 PRO B CA  
2352 C C   . PRO B 124 ? 0.28869 0.36861 0.27891 0.01606  0.00371  0.00486  124 PRO B C   
2353 O O   . PRO B 124 ? 0.31803 0.39409 0.30860 0.01413  0.00265  0.00640  124 PRO B O   
2354 C CB  . PRO B 124 ? 0.23431 0.33216 0.22281 0.01475  0.00566  0.00766  124 PRO B CB  
2355 C CG  . PRO B 124 ? 0.26320 0.37096 0.25301 0.01203  0.00476  0.01198  124 PRO B CG  
2356 C CD  . PRO B 124 ? 0.35367 0.45218 0.33873 0.00440  0.00400  0.01531  124 PRO B CD  
2357 N N   . ALA B 125 ? 0.32458 0.40463 0.31691 0.02187  0.00335  0.00098  125 ALA B N   
2358 C CA  . ALA B 125 ? 0.32929 0.40240 0.32341 0.02551  0.00127  -0.00175 125 ALA B CA  
2359 C C   . ALA B 125 ? 0.26055 0.33844 0.25638 0.02918  -0.00058 -0.00146 125 ALA B C   
2360 O O   . ALA B 125 ? 0.46165 0.53194 0.45760 0.03003  -0.00260 -0.00243 125 ALA B O   
2361 C CB  . ALA B 125 ? 0.25886 0.32954 0.25313 0.03038  0.00063  -0.00578 125 ALA B CB  
2362 N N   . GLN B 126 ? 0.31958 0.41040 0.31633 0.03161  -0.00005 0.00001  126 GLN B N   
2363 C CA  . GLN B 126 ? 0.30640 0.40368 0.30417 0.03673  -0.00173 0.00011  126 GLN B CA  
2364 C C   . GLN B 126 ? 0.43632 0.52957 0.43444 0.03239  -0.00250 0.00255  126 GLN B C   
2365 O O   . GLN B 126 ? 0.37660 0.47211 0.37470 0.02578  -0.00131 0.00631  126 GLN B O   
2366 C CB  . GLN B 126 ? 0.51039 0.62539 0.50943 0.03932  -0.00054 0.00243  126 GLN B CB  
2367 C CG  . GLN B 126 ? 0.77520 0.89973 0.77469 0.04659  -0.00208 0.00248  126 GLN B CG  
2368 C CD  . GLN B 126 ? 1.00525 1.15043 1.00657 0.04864  -0.00062 0.00589  126 GLN B CD  
2369 O OE1 . GLN B 126 ? 1.14042 1.29289 1.14309 0.04139  0.00110  0.00995  126 GLN B OE1 
2370 N NE2 . GLN B 126 ? 0.80526 0.95989 0.80574 0.05869  -0.00159 0.00451  126 GLN B NE2 
2371 N N   . ILE B 127 ? 0.43849 0.52444 0.43590 0.03607  -0.00489 0.00042  127 ILE B N   
2372 C CA  . ILE B 127 ? 0.47067 0.55088 0.46818 0.03241  -0.00574 0.00222  127 ILE B CA  
2373 C C   . ILE B 127 ? 0.43404 0.51031 0.42985 0.03901  -0.00871 -0.00038 127 ILE B C   
2374 O O   . ILE B 127 ? 0.34647 0.41762 0.33982 0.04473  -0.01069 -0.00400 127 ILE B O   
2375 C CB  . ILE B 127 ? 0.39250 0.45972 0.38931 0.02606  -0.00517 0.00264  127 ILE B CB  
2376 C CG1 . ILE B 127 ? 0.43911 0.50272 0.43576 0.02130  -0.00528 0.00568  127 ILE B CG1 
2377 C CG2 . ILE B 127 ? 0.27536 0.33119 0.27110 0.02858  -0.00720 -0.00084 127 ILE B CG2 
2378 C CD1 . ILE B 127 ? 0.40045 0.45575 0.39543 0.01499  -0.00389 0.00759  127 ILE B CD1 
2379 N N   . LYS B 128 ? 0.36973 0.44750 0.36579 0.03836  -0.00942 0.00145  128 LYS B N   
2380 C CA  . LYS B 128 ? 0.47302 0.54526 0.46614 0.04426  -0.01245 -0.00088 128 LYS B CA  
2381 C C   . LYS B 128 ? 0.37790 0.44035 0.37116 0.03895  -0.01302 0.00060  128 LYS B C   
2382 O O   . LYS B 128 ? 0.34644 0.41427 0.34190 0.03419  -0.01150 0.00414  128 LYS B O   
2383 C CB  . LYS B 128 ? 0.42039 0.50740 0.41299 0.05135  -0.01283 -0.00031 128 LYS B CB  
2384 C CG  . LYS B 128 ? 0.43002 0.51065 0.41707 0.05997  -0.01642 -0.00365 128 LYS B CG  
2385 C CD  . LYS B 128 ? 0.79688 0.86214 0.77902 0.06315  -0.01926 -0.00795 128 LYS B CD  
2386 C CE  . LYS B 128 ? 0.85519 0.91003 0.82932 0.07105  -0.02384 -0.01128 128 LYS B CE  
2387 N NZ  . LYS B 128 ? 0.74512 0.78048 0.71429 0.07003  -0.02747 -0.01434 128 LYS B NZ  
2388 N N   . VAL B 129 ? 0.42167 0.46951 0.41211 0.03945  -0.01550 -0.00181 129 VAL B N   
2389 C CA  . VAL B 129 ? 0.37235 0.41003 0.36260 0.03480  -0.01617 -0.00051 129 VAL B CA  
2390 C C   . VAL B 129 ? 0.38471 0.41507 0.37029 0.04043  -0.01988 -0.00299 129 VAL B C   
2391 O O   . VAL B 129 ? 0.49430 0.51720 0.47535 0.04511  -0.02297 -0.00627 129 VAL B O   
2392 C CB  . VAL B 129 ? 0.38322 0.41018 0.37407 0.02904  -0.01580 -0.00022 129 VAL B CB  
2393 C CG1 . VAL B 129 ? 0.31395 0.33189 0.30462 0.02466  -0.01625 0.00166  129 VAL B CG1 
2394 C CG2 . VAL B 129 ? 0.25421 0.28735 0.24779 0.02477  -0.01241 0.00171  129 VAL B CG2 
2395 N N   . ARG B 130 ? 0.32851 0.35984 0.31414 0.04003  -0.01999 -0.00144 130 ARG B N   
2396 C CA  . ARG B 130 ? 0.45343 0.47745 0.43370 0.04547  -0.02348 -0.00368 130 ARG B CA  
2397 C C   . ARG B 130 ? 0.47384 0.48766 0.45427 0.04019  -0.02386 -0.00209 130 ARG B C   
2398 O O   . ARG B 130 ? 0.38317 0.40050 0.36790 0.03422  -0.02112 0.00128  130 ARG B O   
2399 C CB  . ARG B 130 ? 0.48927 0.52664 0.46848 0.05254  -0.02352 -0.00369 130 ARG B CB  
2400 C CG  . ARG B 130 ? 0.48634 0.53382 0.46377 0.06012  -0.02375 -0.00551 130 ARG B CG  
2401 C CD  . ARG B 130 ? 0.61092 0.67589 0.58881 0.06612  -0.02296 -0.00410 130 ARG B CD  
2402 N NE  . ARG B 130 ? 0.64362 0.72508 0.62429 0.06884  -0.02085 -0.00303 130 ARG B NE  
2403 C CZ  . ARG B 130 ? 0.73912 0.84075 0.72344 0.07020  -0.01884 0.00028  130 ARG B CZ  
2404 N NH1 . ARG B 130 ? 0.85943 0.96767 0.84503 0.06947  -0.01879 0.00270  130 ARG B NH1 
2405 N NH2 . ARG B 130 ? 0.81406 0.93009 0.80088 0.07195  -0.01695 0.00153  130 ARG B NH2 
2406 N N   . TRP B 131 ? 0.41267 0.41302 0.38728 0.04268  -0.02765 -0.00446 131 TRP B N   
2407 C CA  . TRP B 131 ? 0.43653 0.42691 0.41015 0.03907  -0.02855 -0.00328 131 TRP B CA  
2408 C C   . TRP B 131 ? 0.50950 0.50137 0.47898 0.04534  -0.03029 -0.00452 131 TRP B C   
2409 O O   . TRP B 131 ? 0.45234 0.44494 0.41588 0.05365  -0.03295 -0.00760 131 TRP B O   
2410 C CB  . TRP B 131 ? 0.34234 0.31616 0.31174 0.03650  -0.03197 -0.00448 131 TRP B CB  
2411 C CG  . TRP B 131 ? 0.46658 0.43822 0.44102 0.02819  -0.02972 -0.00157 131 TRP B CG  
2412 C CD1 . TRP B 131 ? 0.40378 0.37339 0.37908 0.02560  -0.03007 -0.00176 131 TRP B CD1 
2413 C CD2 . TRP B 131 ? 0.37712 0.34875 0.35567 0.02217  -0.02689 0.00206  131 TRP B CD2 
2414 N NE1 . TRP B 131 ? 0.42555 0.39507 0.40539 0.01860  -0.02743 0.00164  131 TRP B NE1 
2415 C CE2 . TRP B 131 ? 0.42137 0.39169 0.40283 0.01671  -0.02547 0.00400  131 TRP B CE2 
2416 C CE3 . TRP B 131 ? 0.39257 0.36514 0.37205 0.02131  -0.02555 0.00392  131 TRP B CE3 
2417 C CZ2 . TRP B 131 ? 0.40734 0.37742 0.39188 0.01129  -0.02271 0.00772  131 TRP B CZ2 
2418 C CZ3 . TRP B 131 ? 0.36444 0.33543 0.34692 0.01551  -0.02305 0.00750  131 TRP B CZ3 
2419 C CH2 . TRP B 131 ? 0.48630 0.45612 0.47093 0.01096  -0.02161 0.00937  131 TRP B CH2 
2420 N N   . PHE B 132 ? 0.43131 0.42350 0.40322 0.04193  -0.02888 -0.00213 132 PHE B N   
2421 C CA  . PHE B 132 ? 0.40950 0.40253 0.37781 0.04707  -0.03039 -0.00299 132 PHE B CA  
2422 C C   . PHE B 132 ? 0.42016 0.39903 0.38649 0.04319  -0.03164 -0.00237 132 PHE B C   
2423 O O   . PHE B 132 ? 0.35646 0.33219 0.32724 0.03569  -0.02950 0.00057  132 PHE B O   
2424 C CB  . PHE B 132 ? 0.42381 0.43436 0.39747 0.04694  -0.02740 -0.00011 132 PHE B CB  
2425 C CG  . PHE B 132 ? 0.47369 0.50042 0.44861 0.05203  -0.02648 -0.00041 132 PHE B CG  
2426 C CD1 . PHE B 132 ? 0.52077 0.55409 0.50023 0.04818  -0.02414 0.00100  132 PHE B CD1 
2427 C CD2 . PHE B 132 ? 0.55082 0.58690 0.52197 0.06114  -0.02791 -0.00194 132 PHE B CD2 
2428 C CE1 . PHE B 132 ? 0.51609 0.56486 0.49672 0.05285  -0.02322 0.00100  132 PHE B CE1 
2429 C CE2 . PHE B 132 ? 0.58252 0.63521 0.55485 0.06634  -0.02691 -0.00172 132 PHE B CE2 
2430 C CZ  . PHE B 132 ? 0.54231 0.60129 0.51964 0.06190  -0.02454 -0.00018 132 PHE B CZ  
2431 N N   . ARG B 133 ? 0.39028 0.36048 0.34903 0.04887  -0.03521 -0.00511 133 ARG B N   
2432 C CA  . ARG B 133 ? 0.40425 0.36177 0.36033 0.04620  -0.03658 -0.00465 133 ARG B CA  
2433 C C   . ARG B 133 ? 0.42564 0.38935 0.37977 0.05182  -0.03672 -0.00519 133 ARG B C   
2434 O O   . ARG B 133 ? 0.48415 0.44783 0.43090 0.06065  -0.03957 -0.00847 133 ARG B O   
2435 C CB  . ARG B 133 ? 0.43829 0.37710 0.38550 0.04707  -0.04147 -0.00731 133 ARG B CB  
2436 C CG  . ARG B 133 ? 0.47403 0.39922 0.41765 0.04434  -0.04323 -0.00676 133 ARG B CG  
2437 C CD  . ARG B 133 ? 0.56993 0.47711 0.50137 0.04780  -0.04941 -0.01011 133 ARG B CD  
2438 N NE  . ARG B 133 ? 0.72417 0.62245 0.64902 0.05099  -0.05159 -0.01137 133 ARG B NE  
2439 C CZ  . ARG B 133 ? 0.82387 0.70814 0.74603 0.04578  -0.05335 -0.01012 133 ARG B CZ  
2440 N NH1 . ARG B 133 ? 0.89179 0.77012 0.81732 0.03709  -0.05332 -0.00721 133 ARG B NH1 
2441 N NH2 . ARG B 133 ? 0.94075 0.81764 0.85661 0.04954  -0.05516 -0.01159 133 ARG B NH2 
2442 N N   . ASN B 134 ? 0.40785 0.37687 0.36780 0.04718  -0.03387 -0.00191 134 ASN B N   
2443 C CA  . ASN B 134 ? 0.48356 0.46005 0.44287 0.05133  -0.03379 -0.00170 134 ASN B CA  
2444 C C   . ASN B 134 ? 0.52933 0.52409 0.48912 0.05831  -0.03337 -0.00232 134 ASN B C   
2445 O O   . ASN B 134 ? 0.49115 0.48915 0.44525 0.06681  -0.03538 -0.00463 134 ASN B O   
2446 C CB  . ASN B 134 ? 0.45602 0.41775 0.40661 0.05582  -0.03736 -0.00466 134 ASN B CB  
2447 C CG  . ASN B 134 ? 0.47518 0.42079 0.42574 0.04872  -0.03760 -0.00328 134 ASN B CG  
2448 O OD1 . ASN B 134 ? 0.36768 0.31561 0.32503 0.04164  -0.03455 0.00042  134 ASN B OD1 
2449 N ND2 . ASN B 134 ? 0.44818 0.37704 0.39008 0.05078  -0.04154 -0.00601 134 ASN B ND2 
2450 N N   . ASP B 135 ? 0.48771 0.49481 0.45380 0.05503  -0.03078 -0.00010 135 ASP B N   
2451 C CA  . ASP B 135 ? 0.42896 0.45614 0.39735 0.05981  -0.02968 0.00062  135 ASP B CA  
2452 C C   . ASP B 135 ? 0.47211 0.49916 0.43323 0.06997  -0.03223 -0.00357 135 ASP B C   
2453 O O   . ASP B 135 ? 0.50903 0.55345 0.47073 0.07608  -0.03158 -0.00320 135 ASP B O   
2454 C CB  . ASP B 135 ? 0.42011 0.46203 0.39070 0.06174  -0.02903 0.00302  135 ASP B CB  
2455 C CG  . ASP B 135 ? 0.48896 0.53253 0.46604 0.05179  -0.02693 0.00767  135 ASP B CG  
2456 O OD1 . ASP B 135 ? 0.45276 0.49893 0.43467 0.04462  -0.02491 0.01043  135 ASP B OD1 
2457 O OD2 . ASP B 135 ? 0.52236 0.56354 0.49862 0.05154  -0.02760 0.00846  135 ASP B OD2 
2458 N N   . GLN B 136 ? 0.49830 0.50629 0.45186 0.07200  -0.03543 -0.00721 136 GLN B N   
2459 C CA  . GLN B 136 ? 0.43561 0.43938 0.38005 0.08146  -0.03877 -0.01133 136 GLN B CA  
2460 C C   . GLN B 136 ? 0.51371 0.50952 0.45932 0.07676  -0.03896 -0.01184 136 GLN B C   
2461 O O   . GLN B 136 ? 0.46471 0.44595 0.41109 0.06916  -0.03956 -0.01135 136 GLN B O   
2462 C CB  . GLN B 136 ? 0.47434 0.46032 0.40642 0.08789  -0.04362 -0.01521 136 GLN B CB  
2463 C CG  . GLN B 136 ? 0.53220 0.50993 0.45176 0.09823  -0.04821 -0.01969 136 GLN B CG  
2464 C CD  . GLN B 136 ? 0.66231 0.61990 0.56743 0.10433  -0.05376 -0.02349 136 GLN B CD  
2465 O OE1 . GLN B 136 ? 0.68792 0.63118 0.59250 0.09777  -0.05479 -0.02300 136 GLN B OE1 
2466 N NE2 . GLN B 136 ? 0.55391 0.51001 0.44625 0.11739  -0.05753 -0.02722 136 GLN B NE2 
2467 N N   . GLU B 137 ? 0.49159 0.49786 0.43742 0.08142  -0.03842 -0.01257 137 GLU B N   
2468 C CA  . GLU B 137 ? 0.46269 0.46379 0.41065 0.07685  -0.03817 -0.01279 137 GLU B CA  
2469 C C   . GLU B 137 ? 0.46606 0.44437 0.40420 0.07773  -0.04333 -0.01616 137 GLU B C   
2470 O O   . GLU B 137 ? 0.52738 0.49685 0.45384 0.08678  -0.04788 -0.01970 137 GLU B O   
2471 C CB  . GLU B 137 ? 0.53263 0.54911 0.48172 0.08276  -0.03686 -0.01316 137 GLU B CB  
2472 C CG  . GLU B 137 ? 0.60983 0.61942 0.55970 0.07921  -0.03717 -0.01407 137 GLU B CG  
2473 C CD  . GLU B 137 ? 0.65335 0.67838 0.60517 0.08431  -0.03539 -0.01414 137 GLU B CD  
2474 O OE1 . GLU B 137 ? 0.69396 0.73562 0.64579 0.09145  -0.03424 -0.01345 137 GLU B OE1 
2475 O OE2 . GLU B 137 ? 0.62737 0.64865 0.58079 0.08117  -0.03512 -0.01465 137 GLU B OE2 
2476 N N   . GLU B 138 ? 0.55904 0.52777 0.50111 0.06824  -0.04295 -0.01475 138 GLU B N   
2477 C CA  . GLU B 138 ? 0.58482 0.53344 0.51882 0.06680  -0.04797 -0.01687 138 GLU B CA  
2478 C C   . GLU B 138 ? 0.69634 0.64585 0.62864 0.06930  -0.04912 -0.01852 138 GLU B C   
2479 O O   . GLU B 138 ? 0.63431 0.59631 0.57574 0.06554  -0.04486 -0.01656 138 GLU B O   
2480 C CB  . GLU B 138 ? 0.56501 0.50512 0.50447 0.05535  -0.04695 -0.01383 138 GLU B CB  
2481 C CG  . GLU B 138 ? 0.67182 0.60601 0.61075 0.05285  -0.04699 -0.01254 138 GLU B CG  
2482 C CD  . GLU B 138 ? 0.82142 0.73520 0.74801 0.05497  -0.05338 -0.01503 138 GLU B CD  
2483 O OE1 . GLU B 138 ? 0.79219 0.70066 0.70788 0.06436  -0.05755 -0.01880 138 GLU B OE1 
2484 O OE2 . GLU B 138 ? 0.93424 0.83707 0.86118 0.04742  -0.05445 -0.01301 138 GLU B OE2 
2485 N N   . THR B 139 ? 0.81390 0.74919 0.73347 0.07586  -0.05520 -0.02216 139 THR B N   
2486 C CA  . THR B 139 ? 0.68158 0.61420 0.59758 0.07849  -0.05739 -0.02402 139 THR B CA  
2487 C C   . THR B 139 ? 0.71963 0.63065 0.62809 0.07329  -0.06335 -0.02482 139 THR B C   
2488 O O   . THR B 139 ? 0.93506 0.84549 0.84675 0.06885  -0.06337 -0.02425 139 THR B O   
2489 C CB  . THR B 139 ? 0.61913 0.55542 0.52508 0.09262  -0.05985 -0.02758 139 THR B CB  
2490 O OG1 . THR B 139 ? 0.75671 0.68001 0.64954 0.09962  -0.06486 -0.03011 139 THR B OG1 
2491 C CG2 . THR B 139 ? 0.71163 0.67357 0.62718 0.09637  -0.05356 -0.02577 139 THR B CG2 
2492 N N   . ALA B 140 ? 0.73744 0.63083 0.63575 0.07323  -0.06862 -0.02583 140 ALA B N   
2493 C CA  . ALA B 140 ? 0.69748 0.57062 0.58904 0.06611  -0.07461 -0.02545 140 ALA B CA  
2494 C C   . ALA B 140 ? 0.85194 0.72792 0.75547 0.05299  -0.07094 -0.02076 140 ALA B C   
2495 O O   . ALA B 140 ? 0.92529 0.80919 0.83592 0.05075  -0.06652 -0.01875 140 ALA B O   
2496 C CB  . ALA B 140 ? 0.84381 0.69551 0.71777 0.07133  -0.08244 -0.02828 140 ALA B CB  
2497 N N   . GLY B 141 ? 0.70461 0.57437 0.60982 0.04469  -0.07299 -0.01882 141 GLY B N   
2498 C CA  . GLY B 141 ? 0.55099 0.42536 0.46727 0.03312  -0.06940 -0.01402 141 GLY B CA  
2499 C C   . GLY B 141 ? 0.52452 0.41885 0.45534 0.03022  -0.06154 -0.01171 141 GLY B C   
2500 O O   . GLY B 141 ? 0.62717 0.52667 0.56674 0.02194  -0.05799 -0.00766 141 GLY B O   
2501 N N   . VAL B 142 ? 0.62418 0.52965 0.55696 0.03705  -0.05887 -0.01398 142 VAL B N   
2502 C CA  . VAL B 142 ? 0.57090 0.49369 0.51565 0.03437  -0.05211 -0.01199 142 VAL B CA  
2503 C C   . VAL B 142 ? 0.67750 0.59865 0.62267 0.03162  -0.05371 -0.01217 142 VAL B C   
2504 O O   . VAL B 142 ? 0.81038 0.72535 0.74771 0.03748  -0.05794 -0.01545 142 VAL B O   
2505 C CB  . VAL B 142 ? 0.51879 0.45602 0.46592 0.04237  -0.04823 -0.01365 142 VAL B CB  
2506 C CG1 . VAL B 142 ? 0.51493 0.46762 0.47230 0.03929  -0.04231 -0.01174 142 VAL B CG1 
2507 C CG2 . VAL B 142 ? 0.53760 0.47825 0.48559 0.04400  -0.04637 -0.01283 142 VAL B CG2 
2508 N N   . VAL B 143 ? 0.68199 0.60860 0.63558 0.02328  -0.05048 -0.00861 143 VAL B N   
2509 C CA  . VAL B 143 ? 0.66821 0.59549 0.62363 0.01994  -0.05129 -0.00824 143 VAL B CA  
2510 C C   . VAL B 143 ? 0.58725 0.53081 0.55326 0.01758  -0.04404 -0.00618 143 VAL B C   
2511 O O   . VAL B 143 ? 0.64246 0.59140 0.61449 0.01252  -0.04012 -0.00270 143 VAL B O   
2512 C CB  . VAL B 143 ? 0.71195 0.62850 0.66536 0.01143  -0.05581 -0.00539 143 VAL B CB  
2513 C CG1 . VAL B 143 ? 0.52951 0.44976 0.48626 0.00763  -0.05593 -0.00450 143 VAL B CG1 
2514 C CG2 . VAL B 143 ? 0.77562 0.67332 0.71616 0.01342  -0.06411 -0.00751 143 VAL B CG2 
2515 N N   . SER B 144 ? 0.52867 0.47906 0.49582 0.02153  -0.04255 -0.00829 144 SER B N   
2516 C CA  . SER B 144 ? 0.53764 0.50221 0.51284 0.02018  -0.03620 -0.00686 144 SER B CA  
2517 C C   . SER B 144 ? 0.51457 0.48012 0.49178 0.01686  -0.03646 -0.00652 144 SER B C   
2518 O O   . SER B 144 ? 0.54798 0.50592 0.52003 0.01878  -0.04122 -0.00882 144 SER B O   
2519 C CB  . SER B 144 ? 0.50929 0.48338 0.48466 0.02751  -0.03360 -0.00921 144 SER B CB  
2520 O OG  . SER B 144 ? 0.59920 0.58514 0.58072 0.02585  -0.02836 -0.00797 144 SER B OG  
2521 N N   . THR B 145 ? 0.49086 0.46517 0.47459 0.01224  -0.03166 -0.00363 145 THR B N   
2522 C CA  . THR B 145 ? 0.46772 0.44622 0.45383 0.01054  -0.03071 -0.00364 145 THR B CA  
2523 C C   . THR B 145 ? 0.38672 0.37063 0.37204 0.01699  -0.02933 -0.00714 145 THR B C   
2524 O O   . THR B 145 ? 0.47465 0.46231 0.45909 0.02189  -0.02793 -0.00851 145 THR B O   
2525 C CB  . THR B 145 ? 0.40354 0.39078 0.39529 0.00586  -0.02551 0.00000  145 THR B CB  
2526 O OG1 . THR B 145 ? 0.38366 0.37897 0.37718 0.00859  -0.02062 -0.00018 145 THR B OG1 
2527 C CG2 . THR B 145 ? 0.40736 0.39147 0.40014 0.00045  -0.02600 0.00397  145 THR B CG2 
2528 N N   . PRO B 146 ? 0.45975 0.44512 0.44546 0.01715  -0.02969 -0.00836 146 PRO B N   
2529 C CA  . PRO B 146 ? 0.51606 0.50885 0.50212 0.02270  -0.02712 -0.01100 146 PRO B CA  
2530 C C   . PRO B 146 ? 0.43410 0.43807 0.42482 0.02132  -0.02079 -0.00901 146 PRO B C   
2531 O O   . PRO B 146 ? 0.42970 0.43524 0.42298 0.01644  -0.01836 -0.00581 146 PRO B O   
2532 C CB  . PRO B 146 ? 0.38066 0.37150 0.36617 0.02210  -0.02902 -0.01234 146 PRO B CB  
2533 C CG  . PRO B 146 ? 0.53642 0.52042 0.52197 0.01539  -0.03241 -0.00981 146 PRO B CG  
2534 C CD  . PRO B 146 ? 0.59981 0.58078 0.58568 0.01206  -0.03264 -0.00708 146 PRO B CD  
2535 N N   . LEU B 147 ? 0.42596 0.43729 0.41675 0.02593  -0.01846 -0.01075 147 LEU B N   
2536 C CA  . LEU B 147 ? 0.37440 0.39500 0.36799 0.02416  -0.01325 -0.00897 147 LEU B CA  
2537 C C   . LEU B 147 ? 0.38851 0.40956 0.38359 0.02018  -0.01145 -0.00790 147 LEU B C   
2538 O O   . LEU B 147 ? 0.44848 0.46762 0.44318 0.02107  -0.01315 -0.00975 147 LEU B O   
2539 C CB  . LEU B 147 ? 0.36595 0.39454 0.35902 0.02938  -0.01174 -0.01085 147 LEU B CB  
2540 C CG  . LEU B 147 ? 0.42573 0.46326 0.42020 0.02733  -0.00718 -0.00879 147 LEU B CG  
2541 C CD1 . LEU B 147 ? 0.30454 0.34216 0.29949 0.02348  -0.00599 -0.00550 147 LEU B CD1 
2542 C CD2 . LEU B 147 ? 0.51311 0.55940 0.50718 0.03247  -0.00645 -0.01011 147 LEU B CD2 
2543 N N   . ILE B 148 ? 0.38643 0.40974 0.38243 0.01621  -0.00830 -0.00481 148 ILE B N   
2544 C CA  . ILE B 148 ? 0.36032 0.38461 0.35682 0.01307  -0.00650 -0.00323 148 ILE B CA  
2545 C C   . ILE B 148 ? 0.40994 0.43988 0.40471 0.01369  -0.00243 -0.00299 148 ILE B C   
2546 O O   . ILE B 148 ? 0.33026 0.36155 0.32326 0.01282  -0.00046 -0.00118 148 ILE B O   
2547 C CB  . ILE B 148 ? 0.36661 0.38818 0.36370 0.00891  -0.00646 0.00039  148 ILE B CB  
2548 C CG1 . ILE B 148 ? 0.41599 0.43107 0.41400 0.00747  -0.01105 0.00037  148 ILE B CG1 
2549 C CG2 . ILE B 148 ? 0.36599 0.39099 0.36290 0.00689  -0.00405 0.00244  148 ILE B CG2 
2550 C CD1 . ILE B 148 ? 0.42599 0.43869 0.42468 0.00350  -0.01118 0.00414  148 ILE B CD1 
2551 N N   . ARG B 149 ? 0.47111 0.50344 0.46554 0.01494  -0.00158 -0.00473 149 ARG B N   
2552 C CA  . ARG B 149 ? 0.36557 0.40194 0.35704 0.01560  0.00187  -0.00481 149 ARG B CA  
2553 C C   . ARG B 149 ? 0.32134 0.35735 0.31036 0.01333  0.00395  -0.00224 149 ARG B C   
2554 O O   . ARG B 149 ? 0.32822 0.36496 0.31865 0.01285  0.00346  -0.00220 149 ARG B O   
2555 C CB  . ARG B 149 ? 0.26630 0.30519 0.25802 0.01882  0.00176  -0.00819 149 ARG B CB  
2556 C CG  . ARG B 149 ? 0.33556 0.37790 0.32347 0.01951  0.00506  -0.00850 149 ARG B CG  
2557 C CD  . ARG B 149 ? 0.48167 0.52610 0.47003 0.02275  0.00495  -0.01189 149 ARG B CD  
2558 N NE  . ARG B 149 ? 0.32993 0.37581 0.32027 0.02631  0.00300  -0.01416 149 ARG B NE  
2559 C CZ  . ARG B 149 ? 0.33099 0.38180 0.32029 0.02817  0.00427  -0.01433 149 ARG B CZ  
2560 N NH1 . ARG B 149 ? 0.35975 0.41316 0.34574 0.02581  0.00700  -0.01232 149 ARG B NH1 
2561 N NH2 . ARG B 149 ? 0.23431 0.28749 0.22508 0.03257  0.00243  -0.01622 149 ARG B NH2 
2562 N N   . ASN B 150 ? 0.33871 0.37375 0.32338 0.01216  0.00596  0.00017  150 ASN B N   
2563 C CA  . ASN B 150 ? 0.40571 0.43993 0.38602 0.01148  0.00787  0.00265  150 ASN B CA  
2564 C C   . ASN B 150 ? 0.38835 0.42470 0.36434 0.01356  0.00991  0.00119  150 ASN B C   
2565 O O   . ASN B 150 ? 0.41710 0.45454 0.39027 0.01426  0.01119  0.00260  150 ASN B O   
2566 C CB  . ASN B 150 ? 0.31682 0.34712 0.29160 0.01022  0.00876  0.00557  150 ASN B CB  
2567 C CG  . ASN B 150 ? 0.42703 0.45501 0.40559 0.00833  0.00700  0.00729  150 ASN B CG  
2568 O OD1 . ASN B 150 ? 0.31797 0.34630 0.30157 0.00756  0.00547  0.00757  150 ASN B OD1 
2569 N ND2 . ASN B 150 ? 0.42522 0.45050 0.40081 0.00721  0.00688  0.00865  150 ASN B ND2 
2570 N N   . GLY B 151 ? 0.34265 0.38027 0.31778 0.01493  0.01027  -0.00145 151 GLY B N   
2571 C CA  . GLY B 151 ? 0.33109 0.36994 0.30153 0.01700  0.01211  -0.00313 151 GLY B CA  
2572 C C   . GLY B 151 ? 0.34931 0.38439 0.30980 0.01684  0.01375  -0.00183 151 GLY B C   
2573 O O   . GLY B 151 ? 0.39436 0.42932 0.34954 0.01857  0.01507  -0.00345 151 GLY B O   
2574 N N   . ASP B 152 ? 0.38439 0.41530 0.34121 0.01471  0.01330  0.00107  152 ASP B N   
2575 C CA  . ASP B 152 ? 0.34957 0.37448 0.29510 0.01387  0.01376  0.00281  152 ASP B CA  
2576 C C   . ASP B 152 ? 0.34187 0.36695 0.28761 0.01076  0.01252  0.00361  152 ASP B C   
2577 O O   . ASP B 152 ? 0.36306 0.38242 0.30130 0.00825  0.01162  0.00638  152 ASP B O   
2578 C CB  . ASP B 152 ? 0.35858 0.37767 0.29765 0.01397  0.01375  0.00604  152 ASP B CB  
2579 C CG  . ASP B 152 ? 0.44901 0.46817 0.39457 0.01166  0.01238  0.00805  152 ASP B CG  
2580 O OD1 . ASP B 152 ? 0.35804 0.38155 0.31258 0.01024  0.01132  0.00683  152 ASP B OD1 
2581 O OD2 . ASP B 152 ? 0.51181 0.52641 0.45272 0.01186  0.01230  0.01082  152 ASP B OD2 
2582 N N   . TRP B 153 ? 0.31866 0.35063 0.27258 0.01110  0.01218  0.00150  153 TRP B N   
2583 C CA  . TRP B 153 ? 0.32765 0.36347 0.28337 0.00881  0.01116  0.00251  153 TRP B CA  
2584 C C   . TRP B 153 ? 0.28527 0.32038 0.24397 0.00651  0.00965  0.00508  153 TRP B C   
2585 O O   . TRP B 153 ? 0.28654 0.32287 0.24322 0.00343  0.00864  0.00751  153 TRP B O   
2586 C CB  . TRP B 153 ? 0.27248 0.30565 0.21839 0.00627  0.01126  0.00404  153 TRP B CB  
2587 C CG  . TRP B 153 ? 0.39335 0.42826 0.33712 0.00870  0.01269  0.00122  153 TRP B CG  
2588 C CD1 . TRP B 153 ? 0.27085 0.30105 0.20899 0.01134  0.01399  -0.00050 153 TRP B CD1 
2589 C CD2 . TRP B 153 ? 0.31220 0.35480 0.25939 0.00930  0.01306  -0.00019 153 TRP B CD2 
2590 N NE1 . TRP B 153 ? 0.36499 0.39851 0.30278 0.01325  0.01506  -0.00316 153 TRP B NE1 
2591 C CE2 . TRP B 153 ? 0.40175 0.44269 0.34502 0.01204  0.01454  -0.00298 153 TRP B CE2 
2592 C CE3 . TRP B 153 ? 0.31060 0.36223 0.26352 0.00829  0.01236  0.00084  153 TRP B CE3 
2593 C CZ2 . TRP B 153 ? 0.24518 0.29217 0.19012 0.01357  0.01533  -0.00489 153 TRP B CZ2 
2594 C CZ3 . TRP B 153 ? 0.45237 0.51115 0.40695 0.01015  0.01323  -0.00076 153 TRP B CZ3 
2595 C CH2 . TRP B 153 ? 0.30105 0.35695 0.25165 0.01264  0.01468  -0.00366 153 TRP B CH2 
2596 N N   . THR B 154 ? 0.25906 0.29249 0.22239 0.00764  0.00929  0.00486  154 THR B N   
2597 C CA  . THR B 154 ? 0.33718 0.37048 0.30478 0.00628  0.00781  0.00650  154 THR B CA  
2598 C C   . THR B 154 ? 0.38852 0.42389 0.36435 0.00866  0.00692  0.00428  154 THR B C   
2599 O O   . THR B 154 ? 0.36213 0.39741 0.33947 0.01041  0.00733  0.00244  154 THR B O   
2600 C CB  . THR B 154 ? 0.37636 0.40205 0.33819 0.00429  0.00760  0.00966  154 THR B CB  
2601 O OG1 . THR B 154 ? 0.35296 0.37621 0.31522 0.00616  0.00841  0.00933  154 THR B OG1 
2602 C CG2 . THR B 154 ? 0.36896 0.38916 0.31953 0.00220  0.00770  0.01181  154 THR B CG2 
2603 N N   . PHE B 155 ? 0.30042 0.33719 0.28071 0.00856  0.00529  0.00462  155 PHE B N   
2604 C CA  . PHE B 155 ? 0.28834 0.32456 0.27437 0.01045  0.00348  0.00284  155 PHE B CA  
2605 C C   . PHE B 155 ? 0.42029 0.45170 0.40688 0.00850  0.00244  0.00512  155 PHE B C   
2606 O O   . PHE B 155 ? 0.33948 0.36880 0.32264 0.00623  0.00301  0.00785  155 PHE B O   
2607 C CB  . PHE B 155 ? 0.35656 0.39811 0.34615 0.01363  0.00201  0.00063  155 PHE B CB  
2608 C CG  . PHE B 155 ? 0.36767 0.41407 0.35729 0.01641  0.00279  -0.00186 155 PHE B CG  
2609 C CD1 . PHE B 155 ? 0.30512 0.34976 0.29653 0.01912  0.00168  -0.00482 155 PHE B CD1 
2610 C CD2 . PHE B 155 ? 0.32241 0.37491 0.30990 0.01601  0.00430  -0.00097 155 PHE B CD2 
2611 C CE1 . PHE B 155 ? 0.30255 0.35113 0.29372 0.02211  0.00234  -0.00724 155 PHE B CE1 
2612 C CE2 . PHE B 155 ? 0.38425 0.44139 0.37170 0.01876  0.00513  -0.00318 155 PHE B CE2 
2613 C CZ  . PHE B 155 ? 0.34829 0.40332 0.33763 0.02221  0.00428  -0.00651 155 PHE B CZ  
2614 N N   . GLN B 156 ? 0.36684 0.39568 0.35710 0.00924  0.00049  0.00406  156 GLN B N   
2615 C CA  . GLN B 156 ? 0.30114 0.32560 0.29243 0.00779  -0.00096 0.00579  156 GLN B CA  
2616 C C   . GLN B 156 ? 0.31678 0.33903 0.31115 0.00966  -0.00420 0.00350  156 GLN B C   
2617 O O   . GLN B 156 ? 0.31663 0.33958 0.31192 0.01173  -0.00544 0.00090  156 GLN B O   
2618 C CB  . GLN B 156 ? 0.29097 0.31169 0.28062 0.00534  0.00007  0.00861  156 GLN B CB  
2619 C CG  . GLN B 156 ? 0.37255 0.39374 0.36391 0.00509  -0.00020 0.00821  156 GLN B CG  
2620 C CD  . GLN B 156 ? 0.39347 0.41333 0.38334 0.00321  0.00095  0.01178  156 GLN B CD  
2621 O OE1 . GLN B 156 ? 0.50788 0.52443 0.49835 0.00176  0.00005  0.01385  156 GLN B OE1 
2622 N NE2 . GLN B 156 ? 0.31984 0.34270 0.30722 0.00380  0.00305  0.01263  156 GLN B NE2 
2623 N N   . ILE B 157 ? 0.35035 0.36871 0.34516 0.00913  -0.00594 0.00441  157 ILE B N   
2624 C CA  . ILE B 157 ? 0.33282 0.34650 0.32829 0.01095  -0.00972 0.00237  157 ILE B CA  
2625 C C   . ILE B 157 ? 0.33734 0.34521 0.33257 0.00872  -0.01098 0.00447  157 ILE B C   
2626 O O   . ILE B 157 ? 0.37397 0.38284 0.36875 0.00753  -0.00919 0.00664  157 ILE B O   
2627 C CB  . ILE B 157 ? 0.29935 0.31655 0.29415 0.01610  -0.01105 -0.00053 157 ILE B CB  
2628 C CG1 . ILE B 157 ? 0.38109 0.39119 0.37394 0.01908  -0.01566 -0.00320 157 ILE B CG1 
2629 C CG2 . ILE B 157 ? 0.27915 0.30037 0.27384 0.01671  -0.01005 0.00090  157 ILE B CG2 
2630 C CD1 . ILE B 157 ? 0.29623 0.30958 0.28693 0.02580  -0.01723 -0.00614 157 ILE B CD1 
2631 N N   . LEU B 158 ? 0.34052 0.34160 0.33543 0.00782  -0.01440 0.00403  158 LEU B N   
2632 C CA  . LEU B 158 ? 0.39648 0.39112 0.39078 0.00555  -0.01612 0.00593  158 LEU B CA  
2633 C C   . LEU B 158 ? 0.43880 0.42695 0.43011 0.00884  -0.02052 0.00311  158 LEU B C   
2634 O O   . LEU B 158 ? 0.44941 0.43434 0.43859 0.01098  -0.02367 0.00049  158 LEU B O   
2635 C CB  . LEU B 158 ? 0.33099 0.32286 0.32637 0.00082  -0.01682 0.00870  158 LEU B CB  
2636 C CG  . LEU B 158 ? 0.49911 0.49539 0.49584 -0.00207 -0.01296 0.01265  158 LEU B CG  
2637 C CD1 . LEU B 158 ? 0.45743 0.46061 0.45384 -0.00039 -0.00913 0.01228  158 LEU B CD1 
2638 C CD2 . LEU B 158 ? 0.45373 0.44986 0.45193 -0.00604 -0.01430 0.01527  158 LEU B CD2 
2639 N N   . VAL B 159 ? 0.33450 0.32002 0.32458 0.00977  -0.02100 0.00356  159 VAL B N   
2640 C CA  . VAL B 159 ? 0.41526 0.39432 0.40100 0.01395  -0.02512 0.00085  159 VAL B CA  
2641 C C   . VAL B 159 ? 0.45976 0.42980 0.44379 0.01083  -0.02724 0.00267  159 VAL B C   
2642 O O   . VAL B 159 ? 0.42760 0.39930 0.41309 0.00978  -0.02499 0.00466  159 VAL B O   
2643 C CB  . VAL B 159 ? 0.38477 0.37115 0.37015 0.01938  -0.02374 -0.00066 159 VAL B CB  
2644 C CG1 . VAL B 159 ? 0.42240 0.40244 0.40187 0.02529  -0.02816 -0.00374 159 VAL B CG1 
2645 C CG2 . VAL B 159 ? 0.30718 0.30365 0.29469 0.02154  -0.02121 -0.00163 159 VAL B CG2 
2646 N N   . MET B 160 ? 0.51546 0.47540 0.49582 0.00904  -0.03191 0.00220  160 MET B N   
2647 C CA  . MET B 160 ? 0.47321 0.42371 0.45118 0.00552  -0.03457 0.00412  160 MET B CA  
2648 C C   . MET B 160 ? 0.54521 0.48705 0.51624 0.01071  -0.03854 0.00106  160 MET B C   
2649 O O   . MET B 160 ? 0.56486 0.50402 0.53077 0.01643  -0.04150 -0.00262 160 MET B O   
2650 C CB  . MET B 160 ? 0.50458 0.44843 0.48137 -0.00023 -0.03825 0.00597  160 MET B CB  
2651 C CG  . MET B 160 ? 0.69851 0.65075 0.68178 -0.00603 -0.03444 0.01031  160 MET B CG  
2652 S SD  . MET B 160 ? 0.97632 0.94022 0.96387 -0.00442 -0.03056 0.00930  160 MET B SD  
2653 C CE  . MET B 160 ? 0.67650 0.63266 0.65948 -0.00425 -0.03684 0.00651  160 MET B CE  
2654 N N   . LEU B 161 ? 0.41512 0.35249 0.38527 0.00934  -0.03862 0.00258  161 LEU B N   
2655 C CA  . LEU B 161 ? 0.46658 0.39444 0.42922 0.01399  -0.04260 -0.00004 161 LEU B CA  
2656 C C   . LEU B 161 ? 0.55210 0.46707 0.51082 0.00870  -0.04643 0.00200  161 LEU B C   
2657 O O   . LEU B 161 ? 0.61920 0.53632 0.58257 0.00369  -0.04365 0.00574  161 LEU B O   
2658 C CB  . LEU B 161 ? 0.45260 0.38801 0.41746 0.01802  -0.03906 -0.00031 161 LEU B CB  
2659 C CG  . LEU B 161 ? 0.47756 0.40396 0.43503 0.02266  -0.04258 -0.00249 161 LEU B CG  
2660 C CD1 . LEU B 161 ? 0.42540 0.34671 0.37406 0.03054  -0.04717 -0.00699 161 LEU B CD1 
2661 C CD2 . LEU B 161 ? 0.45166 0.38664 0.41277 0.02482  -0.03877 -0.00162 161 LEU B CD2 
2662 N N   . GLU B 162 ? 0.48160 0.38270 0.43087 0.00983  -0.05311 -0.00022 162 GLU B N   
2663 C CA  . GLU B 162 ? 0.58250 0.46967 0.52604 0.00502  -0.05771 0.00156  162 GLU B CA  
2664 C C   . GLU B 162 ? 0.57748 0.46053 0.51733 0.00942  -0.05755 0.00016  162 GLU B C   
2665 O O   . GLU B 162 ? 0.62135 0.50348 0.55570 0.01785  -0.05867 -0.00392 162 GLU B O   
2666 C CB  . GLU B 162 ? 0.67524 0.54664 0.60762 0.00476  -0.06589 -0.00041 162 GLU B CB  
2667 N N   . MET B 163 ? 0.48630 0.36789 0.42913 0.00422  -0.05600 0.00369  163 MET B N   
2668 C CA  . MET B 163 ? 0.62477 0.50485 0.56603 0.00805  -0.05467 0.00277  163 MET B CA  
2669 C C   . MET B 163 ? 0.56463 0.43243 0.50181 0.00271  -0.05769 0.00534  163 MET B C   
2670 O O   . MET B 163 ? 0.63795 0.50536 0.57851 -0.00528 -0.05781 0.00970  163 MET B O   
2671 C CB  . MET B 163 ? 0.48596 0.38173 0.43753 0.00847  -0.04729 0.00469  163 MET B CB  
2672 C CG  . MET B 163 ? 0.45330 0.35505 0.41281 0.00090  -0.04349 0.00994  163 MET B CG  
2673 S SD  . MET B 163 ? 0.69047 0.59986 0.65587 0.00113  -0.03763 0.01256  163 MET B SD  
2674 C CE  . MET B 163 ? 0.67288 0.58569 0.64385 -0.00664 -0.03486 0.01872  163 MET B CE  
2675 N N   . THR B 164 ? 0.66673 0.52522 0.59633 0.00740  -0.06017 0.00277  164 THR B N   
2676 C CA  . THR B 164 ? 0.69103 0.53946 0.61754 0.00336  -0.06180 0.00508  164 THR B CA  
2677 C C   . THR B 164 ? 0.56394 0.41900 0.49422 0.00793  -0.05718 0.00447  164 THR B C   
2678 O O   . THR B 164 ? 0.55146 0.40201 0.47487 0.01536  -0.05905 0.00045  164 THR B O   
2679 C CB  . THR B 164 ? 0.74536 0.57329 0.65697 0.00443  -0.07014 0.00251  164 THR B CB  
2680 O OG1 . THR B 164 ? 0.80213 0.62679 0.70528 0.01438  -0.07282 -0.00320 164 THR B OG1 
2681 C CG2 . THR B 164 ? 0.76771 0.58754 0.67614 -0.00381 -0.07519 0.00528  164 THR B CG2 
2682 N N   . PRO B 165 ? 0.57553 0.44119 0.51580 0.00416  -0.05139 0.00844  165 PRO B N   
2683 C CA  . PRO B 165 ? 0.65556 0.52931 0.59997 0.00844  -0.04693 0.00796  165 PRO B CA  
2684 C C   . PRO B 165 ? 0.68855 0.55266 0.62858 0.00899  -0.04812 0.00815  165 PRO B C   
2685 O O   . PRO B 165 ? 0.60416 0.46095 0.54346 0.00337  -0.04912 0.01141  165 PRO B O   
2686 C CB  . PRO B 165 ? 0.65953 0.54606 0.61426 0.00409  -0.04112 0.01225  165 PRO B CB  
2687 C CG  . PRO B 165 ? 0.67110 0.55514 0.62712 -0.00302 -0.04232 0.01585  165 PRO B CG  
2688 C CD  . PRO B 165 ? 0.57188 0.44249 0.51907 -0.00387 -0.04904 0.01378  165 PRO B CD  
2689 N N   . GLN B 166 ? 0.54118 0.40633 0.47834 0.01593  -0.04799 0.00485  166 GLN B N   
2690 C CA  . GLN B 166 ? 0.57121 0.43051 0.50589 0.01741  -0.04784 0.00492  166 GLN B CA  
2691 C C   . GLN B 166 ? 0.47957 0.35045 0.42340 0.01603  -0.04207 0.00804  166 GLN B C   
2692 O O   . GLN B 166 ? 0.50889 0.39271 0.45858 0.01715  -0.03891 0.00829  166 GLN B O   
2693 C CB  . GLN B 166 ? 0.58817 0.44359 0.51452 0.02616  -0.05083 -0.00012 166 GLN B CB  
2694 C CG  . GLN B 166 ? 0.82817 0.67108 0.74284 0.02949  -0.05714 -0.00385 166 GLN B CG  
2695 C CD  . GLN B 166 ? 0.94376 0.76815 0.85041 0.02448  -0.06188 -0.00278 166 GLN B CD  
2696 O OE1 . GLN B 166 ? 0.87153 0.68621 0.77236 0.02604  -0.06347 -0.00356 166 GLN B OE1 
2697 N NE2 . GLN B 166 ? 0.86194 0.68155 0.76810 0.01799  -0.06433 -0.00067 166 GLN B NE2 
2698 N N   . ARG B 167 ? 0.52351 0.38879 0.46759 0.01357  -0.04107 0.01055  167 ARG B N   
2699 C CA  . ARG B 167 ? 0.43200 0.30551 0.38262 0.01270  -0.03638 0.01351  167 ARG B CA  
2700 C C   . ARG B 167 ? 0.43346 0.31533 0.38480 0.01834  -0.03544 0.01094  167 ARG B C   
2701 O O   . ARG B 167 ? 0.50566 0.38336 0.45142 0.02353  -0.03804 0.00748  167 ARG B O   
2702 C CB  . ARG B 167 ? 0.51629 0.38090 0.46539 0.01055  -0.03607 0.01609  167 ARG B CB  
2703 C CG  . ARG B 167 ? 0.53072 0.40156 0.48517 0.00933  -0.03169 0.01977  167 ARG B CG  
2704 C CD  . ARG B 167 ? 0.52502 0.38663 0.47733 0.00797  -0.03152 0.02225  167 ARG B CD  
2705 N NE  . ARG B 167 ? 0.50280 0.35627 0.44957 0.01207  -0.03408 0.01882  167 ARG B NE  
2706 C CZ  . ARG B 167 ? 0.57845 0.42085 0.52108 0.01155  -0.03538 0.01954  167 ARG B CZ  
2707 N NH1 . ARG B 167 ? 0.60489 0.44372 0.54858 0.00688  -0.03442 0.02395  167 ARG B NH1 
2708 N NH2 . ARG B 167 ? 0.59111 0.42658 0.52819 0.01608  -0.03768 0.01595  167 ARG B NH2 
2709 N N   . GLY B 168 ? 0.48884 0.38291 0.44642 0.01731  -0.03201 0.01284  168 GLY B N   
2710 C CA  . GLY B 168 ? 0.31203 0.21673 0.27125 0.02118  -0.03116 0.01152  168 GLY B CA  
2711 C C   . GLY B 168 ? 0.38860 0.30376 0.34938 0.02339  -0.03129 0.00961  168 GLY B C   
2712 O O   . GLY B 168 ? 0.45532 0.38266 0.41939 0.02469  -0.02975 0.01011  168 GLY B O   
2713 N N   . ASP B 169 ? 0.38980 0.30045 0.34796 0.02357  -0.03337 0.00775  169 ASP B N   
2714 C CA  . ASP B 169 ? 0.50918 0.42887 0.46831 0.02607  -0.03358 0.00587  169 ASP B CA  
2715 C C   . ASP B 169 ? 0.43787 0.36929 0.40423 0.02215  -0.02975 0.00893  169 ASP B C   
2716 O O   . ASP B 169 ? 0.42058 0.34968 0.38983 0.01682  -0.02773 0.01214  169 ASP B O   
2717 C CB  . ASP B 169 ? 0.45226 0.36290 0.40701 0.02559  -0.03675 0.00404  169 ASP B CB  
2718 C CG  . ASP B 169 ? 0.48740 0.38678 0.43224 0.03122  -0.04167 0.00002  169 ASP B CG  
2719 O OD1 . ASP B 169 ? 0.53722 0.43912 0.47900 0.03723  -0.04224 -0.00204 169 ASP B OD1 
2720 O OD2 . ASP B 169 ? 0.54652 0.43430 0.48584 0.02964  -0.04532 -0.00095 169 ASP B OD2 
2721 N N   . VAL B 170 ? 0.30060 0.24478 0.26906 0.02513  -0.02892 0.00807  170 VAL B N   
2722 C CA  . VAL B 170 ? 0.38228 0.33713 0.35618 0.02161  -0.02590 0.01066  170 VAL B CA  
2723 C C   . VAL B 170 ? 0.40219 0.36220 0.37625 0.02375  -0.02646 0.00846  170 VAL B C   
2724 O O   . VAL B 170 ? 0.38259 0.34817 0.35439 0.02968  -0.02806 0.00566  170 VAL B O   
2725 C CB  . VAL B 170 ? 0.38765 0.35390 0.36411 0.02177  -0.02452 0.01260  170 VAL B CB  
2726 C CG1 . VAL B 170 ? 0.52682 0.50052 0.50122 0.02855  -0.02635 0.00992  170 VAL B CG1 
2727 C CG2 . VAL B 170 ? 0.35971 0.33621 0.34014 0.01814  -0.02218 0.01507  170 VAL B CG2 
2728 N N   . TYR B 171 ? 0.43599 0.39412 0.41214 0.01956  -0.02524 0.00972  171 TYR B N   
2729 C CA  . TYR B 171 ? 0.41278 0.37527 0.38941 0.02089  -0.02558 0.00793  171 TYR B CA  
2730 C C   . TYR B 171 ? 0.33471 0.30950 0.31598 0.01866  -0.02238 0.01008  171 TYR B C   
2731 O O   . TYR B 171 ? 0.37034 0.34476 0.35369 0.01380  -0.02008 0.01332  171 TYR B O   
2732 C CB  . TYR B 171 ? 0.31445 0.26732 0.29008 0.01749  -0.02671 0.00804  171 TYR B CB  
2733 C CG  . TYR B 171 ? 0.48534 0.42500 0.45498 0.01901  -0.03085 0.00602  171 TYR B CG  
2734 C CD1 . TYR B 171 ? 0.47110 0.40186 0.43937 0.01638  -0.03130 0.00777  171 TYR B CD1 
2735 C CD2 . TYR B 171 ? 0.38218 0.31713 0.34631 0.02321  -0.03471 0.00242  171 TYR B CD2 
2736 C CE1 . TYR B 171 ? 0.44362 0.36127 0.40538 0.01723  -0.03551 0.00610  171 TYR B CE1 
2737 C CE2 . TYR B 171 ? 0.50738 0.42799 0.46390 0.02433  -0.03937 0.00062  171 TYR B CE2 
2738 C CZ  . TYR B 171 ? 0.54479 0.45687 0.50024 0.02100  -0.03976 0.00252  171 TYR B CZ  
2739 O OH  . TYR B 171 ? 0.58239 0.47936 0.52932 0.02164  -0.04478 0.00088  171 TYR B OH  
2740 N N   . THR B 172 ? 0.34829 0.33349 0.33014 0.02256  -0.02248 0.00842  172 THR B N   
2741 C CA  . THR B 172 ? 0.46160 0.45915 0.44717 0.02047  -0.01991 0.01053  172 THR B CA  
2742 C C   . THR B 172 ? 0.42824 0.42903 0.41449 0.02160  -0.01963 0.00880  172 THR B C   
2743 O O   . THR B 172 ? 0.36134 0.36148 0.34500 0.02699  -0.02181 0.00549  172 THR B O   
2744 C CB  . THR B 172 ? 0.44410 0.45457 0.43055 0.02359  -0.01995 0.01112  172 THR B CB  
2745 O OG1 . THR B 172 ? 0.47461 0.48166 0.46022 0.02273  -0.02051 0.01255  172 THR B OG1 
2746 C CG2 . THR B 172 ? 0.36379 0.38635 0.35356 0.01983  -0.01773 0.01417  172 THR B CG2 
2747 N N   . CYS B 173 ? 0.40626 0.40952 0.39488 0.01699  -0.01724 0.01093  173 CYS B N   
2748 C CA  . CYS B 173 ? 0.33608 0.34427 0.32579 0.01773  -0.01648 0.00967  173 CYS B CA  
2749 C C   . CYS B 173 ? 0.39720 0.41969 0.38886 0.01823  -0.01501 0.01102  173 CYS B C   
2750 O O   . CYS B 173 ? 0.41857 0.44439 0.41098 0.01373  -0.01354 0.01441  173 CYS B O   
2751 C CB  . CYS B 173 ? 0.49569 0.49842 0.48608 0.01284  -0.01481 0.01118  173 CYS B CB  
2752 S SG  . CYS B 173 ? 0.52036 0.52735 0.51175 0.01401  -0.01423 0.00911  173 CYS B SG  
2753 N N   . HIS B 174 ? 0.35639 0.38696 0.34802 0.02371  -0.01577 0.00866  174 HIS B N   
2754 C CA  . HIS B 174 ? 0.41691 0.46347 0.41053 0.02508  -0.01468 0.01017  174 HIS B CA  
2755 C C   . HIS B 174 ? 0.41522 0.46660 0.40992 0.02498  -0.01329 0.00949  174 HIS B C   
2756 O O   . HIS B 174 ? 0.37567 0.42370 0.36890 0.02953  -0.01440 0.00609  174 HIS B O   
2757 C CB  . HIS B 174 ? 0.47975 0.53380 0.47188 0.03297  -0.01652 0.00826  174 HIS B CB  
2758 C CG  . HIS B 174 ? 0.48215 0.55518 0.47686 0.03406  -0.01547 0.01098  174 HIS B CG  
2759 N ND1 . HIS B 174 ? 0.44155 0.52696 0.43731 0.03759  -0.01463 0.01065  174 HIS B ND1 
2760 C CD2 . HIS B 174 ? 0.42502 0.50763 0.42147 0.03190  -0.01532 0.01449  174 HIS B CD2 
2761 C CE1 . HIS B 174 ? 0.45378 0.55656 0.45210 0.03728  -0.01390 0.01418  174 HIS B CE1 
2762 N NE2 . HIS B 174 ? 0.61300 0.71449 0.61181 0.03358  -0.01445 0.01663  174 HIS B NE2 
2763 N N   . VAL B 175 ? 0.33233 0.39045 0.32863 0.01979  -0.01127 0.01270  175 VAL B N   
2764 C CA  . VAL B 175 ? 0.34782 0.40868 0.34459 0.01869  -0.00973 0.01228  175 VAL B CA  
2765 C C   . VAL B 175 ? 0.44497 0.52199 0.44331 0.01809  -0.00873 0.01490  175 VAL B C   
2766 O O   . VAL B 175 ? 0.38982 0.47150 0.38821 0.01295  -0.00856 0.01893  175 VAL B O   
2767 C CB  . VAL B 175 ? 0.37092 0.42170 0.36624 0.01248  -0.00838 0.01373  175 VAL B CB  
2768 C CG1 . VAL B 175 ? 0.29321 0.34742 0.28841 0.01171  -0.00678 0.01322  175 VAL B CG1 
2769 C CG2 . VAL B 175 ? 0.32748 0.36469 0.32186 0.01284  -0.00930 0.01187  175 VAL B CG2 
2770 N N   . GLU B 176 ? 0.37059 0.45598 0.36976 0.02306  -0.00837 0.01294  176 GLU B N   
2771 C CA  . GLU B 176 ? 0.40446 0.50651 0.40534 0.02267  -0.00725 0.01561  176 GLU B CA  
2772 C C   . GLU B 176 ? 0.39496 0.49597 0.39533 0.02084  -0.00564 0.01487  176 GLU B C   
2773 O O   . GLU B 176 ? 0.48740 0.58076 0.48700 0.02452  -0.00570 0.01097  176 GLU B O   
2774 C CB  . GLU B 176 ? 0.46333 0.57887 0.46515 0.03148  -0.00806 0.01434  176 GLU B CB  
2775 C CG  . GLU B 176 ? 0.54569 0.66552 0.54772 0.03350  -0.00950 0.01565  176 GLU B CG  
2776 C CD  . GLU B 176 ? 0.55554 0.68596 0.55649 0.04431  -0.01062 0.01352  176 GLU B CD  
2777 O OE1 . GLU B 176 ? 0.76039 0.89109 0.75952 0.05088  -0.01076 0.01029  176 GLU B OE1 
2778 O OE2 . GLU B 176 ? 0.81216 0.95038 0.81330 0.04676  -0.01155 0.01507  176 GLU B OE2 
2779 N N   . HIS B 177 ? 0.43243 0.54057 0.43259 0.01482  -0.00456 0.01877  177 HIS B N   
2780 C CA  . HIS B 177 ? 0.34412 0.44977 0.34263 0.01233  -0.00308 0.01833  177 HIS B CA  
2781 C C   . HIS B 177 ? 0.36001 0.47957 0.35844 0.00796  -0.00256 0.02281  177 HIS B C   
2782 O O   . HIS B 177 ? 0.39586 0.52082 0.39404 0.00294  -0.00363 0.02726  177 HIS B O   
2783 C CB  . HIS B 177 ? 0.26670 0.35591 0.26149 0.00697  -0.00279 0.01831  177 HIS B CB  
2784 C CG  . HIS B 177 ? 0.37670 0.46190 0.36907 0.00583  -0.00129 0.01701  177 HIS B CG  
2785 N ND1 . HIS B 177 ? 0.41045 0.49513 0.39834 -0.00018 -0.00080 0.02008  177 HIS B ND1 
2786 C CD2 . HIS B 177 ? 0.31889 0.40000 0.31194 0.00998  -0.00052 0.01299  177 HIS B CD2 
2787 C CE1 . HIS B 177 ? 0.29052 0.37130 0.27655 0.00084  0.00057  0.01775  177 HIS B CE1 
2788 N NE2 . HIS B 177 ? 0.30722 0.38639 0.29687 0.00685  0.00085  0.01352  177 HIS B NE2 
2789 N N   . PRO B 178 ? 0.41787 0.54341 0.41627 0.00931  -0.00123 0.02206  178 PRO B N   
2790 C CA  . PRO B 178 ? 0.33730 0.47717 0.33549 0.00470  -0.00095 0.02684  178 PRO B CA  
2791 C C   . PRO B 178 ? 0.34738 0.48084 0.34048 -0.00568 -0.00210 0.03153  178 PRO B C   
2792 O O   . PRO B 178 ? 0.53606 0.68140 0.52864 -0.01108 -0.00298 0.03672  178 PRO B O   
2793 C CB  . PRO B 178 ? 0.34583 0.48772 0.34366 0.00797  0.00078  0.02423  178 PRO B CB  
2794 C CG  . PRO B 178 ? 0.31733 0.45342 0.31712 0.01707  0.00094  0.01837  178 PRO B CG  
2795 C CD  . PRO B 178 ? 0.27750 0.39879 0.27634 0.01567  -0.00025 0.01701  178 PRO B CD  
2796 N N   . SER B 179 ? 0.41976 0.53494 0.40826 -0.00860 -0.00247 0.03023  179 SER B N   
2797 C CA  . SER B 179 ? 0.46089 0.56740 0.44228 -0.01742 -0.00419 0.03449  179 SER B CA  
2798 C C   . SER B 179 ? 0.45925 0.56663 0.44105 -0.02079 -0.00639 0.03798  179 SER B C   
2799 O O   . SER B 179 ? 0.43463 0.53393 0.40959 -0.02815 -0.00855 0.04185  179 SER B O   
2800 C CB  . SER B 179 ? 0.45618 0.54322 0.43127 -0.01793 -0.00368 0.03188  179 SER B CB  
2801 O OG  . SER B 179 ? 0.36858 0.44713 0.34591 -0.01452 -0.00364 0.02945  179 SER B OG  
2802 N N   . LEU B 180 ? 0.43019 0.54593 0.41866 -0.01533 -0.00622 0.03661  180 LEU B N   
2803 C CA  . LEU B 180 ? 0.52916 0.64458 0.51837 -0.01727 -0.00809 0.03902  180 LEU B CA  
2804 C C   . LEU B 180 ? 0.50279 0.63954 0.49647 -0.01811 -0.00904 0.04328  180 LEU B C   
2805 O O   . LEU B 180 ? 0.53075 0.68199 0.52986 -0.01109 -0.00773 0.04158  180 LEU B O   
2806 C CB  . LEU B 180 ? 0.44755 0.55533 0.43987 -0.01026 -0.00749 0.03430  180 LEU B CB  
2807 C CG  . LEU B 180 ? 0.36818 0.45733 0.35710 -0.00935 -0.00656 0.03068  180 LEU B CG  
2808 C CD1 . LEU B 180 ? 0.36420 0.44768 0.35640 -0.00300 -0.00643 0.02657  180 LEU B CD1 
2809 C CD2 . LEU B 180 ? 0.39081 0.46671 0.37253 -0.01632 -0.00786 0.03381  180 LEU B CD2 
2810 N N   . GLN B 181 ? 0.55628 0.69513 0.54704 -0.02642 -0.01161 0.04907  181 GLN B N   
2811 C CA  . GLN B 181 ? 0.52522 0.68577 0.52075 -0.02768 -0.01278 0.05385  181 GLN B CA  
2812 C C   . GLN B 181 ? 0.49603 0.66142 0.49669 -0.02051 -0.01260 0.05165  181 GLN B C   
2813 O O   . GLN B 181 ? 0.56527 0.75137 0.57104 -0.01720 -0.01259 0.05385  181 GLN B O   
2814 C CB  . GLN B 181 ? 0.56710 0.72747 0.55741 -0.03950 -0.01633 0.06104  181 GLN B CB  
2815 N N   . SER B 182 ? 0.48295 0.63019 0.48185 -0.01769 -0.01249 0.04750  182 SER B N   
2816 C CA  . SER B 182 ? 0.54020 0.68830 0.54251 -0.01047 -0.01246 0.04458  182 SER B CA  
2817 C C   . SER B 182 ? 0.50527 0.63288 0.50556 -0.00619 -0.01145 0.03868  182 SER B C   
2818 O O   . SER B 182 ? 0.51883 0.63120 0.51470 -0.01062 -0.01125 0.03833  182 SER B O   
2819 C CB  . SER B 182 ? 0.39885 0.54869 0.40072 -0.01548 -0.01493 0.04888  182 SER B CB  
2820 O OG  . SER B 182 ? 0.71553 0.84674 0.71119 -0.02318 -0.01649 0.05054  182 SER B OG  
2821 N N   . PRO B 183 ? 0.45020 0.57700 0.45278 0.00237  -0.01109 0.03430  183 PRO B N   
2822 C CA  . PRO B 183 ? 0.43248 0.54119 0.43327 0.00590  -0.01048 0.02913  183 PRO B CA  
2823 C C   . PRO B 183 ? 0.36567 0.45712 0.36298 0.00039  -0.01116 0.03006  183 PRO B C   
2824 O O   . PRO B 183 ? 0.41317 0.50485 0.40944 -0.00393 -0.01257 0.03356  183 PRO B O   
2825 C CB  . PRO B 183 ? 0.47800 0.58956 0.48030 0.01514  -0.01114 0.02543  183 PRO B CB  
2826 C CG  . PRO B 183 ? 0.47385 0.60737 0.47891 0.01866  -0.01121 0.02775  183 PRO B CG  
2827 C CD  . PRO B 183 ? 0.35222 0.49469 0.35810 0.00942  -0.01156 0.03407  183 PRO B CD  
2828 N N   . ILE B 184 ? 0.38045 0.45738 0.37569 0.00077  -0.01024 0.02714  184 ILE B N   
2829 C CA  . ILE B 184 ? 0.30198 0.36264 0.29377 -0.00247 -0.01058 0.02755  184 ILE B CA  
2830 C C   . ILE B 184 ? 0.36804 0.42202 0.36126 0.00257  -0.01121 0.02436  184 ILE B C   
2831 O O   . ILE B 184 ? 0.37354 0.42769 0.36837 0.00814  -0.01113 0.02054  184 ILE B O   
2832 C CB  . ILE B 184 ? 0.32130 0.37160 0.30977 -0.00457 -0.00921 0.02674  184 ILE B CB  
2833 C CG1 . ILE B 184 ? 0.46814 0.52047 0.45230 -0.01052 -0.00928 0.03039  184 ILE B CG1 
2834 C CG2 . ILE B 184 ? 0.31572 0.35072 0.30134 -0.00530 -0.00924 0.02643  184 ILE B CG2 
2835 C CD1 . ILE B 184 ? 0.38793 0.43208 0.36821 -0.01124 -0.00780 0.02918  184 ILE B CD1 
2836 N N   . THR B 185 ? 0.39539 0.44253 0.38707 0.00057  -0.01225 0.02600  185 THR B N   
2837 C CA  . THR B 185 ? 0.38465 0.42333 0.37659 0.00438  -0.01304 0.02340  185 THR B CA  
2838 C C   . THR B 185 ? 0.39985 0.42368 0.38855 0.00080  -0.01281 0.02470  185 THR B C   
2839 O O   . THR B 185 ? 0.40205 0.42305 0.38776 -0.00373 -0.01318 0.02821  185 THR B O   
2840 C CB  . THR B 185 ? 0.44646 0.49231 0.43964 0.00696  -0.01456 0.02390  185 THR B CB  
2841 O OG1 . THR B 185 ? 0.47216 0.52124 0.46430 0.00131  -0.01522 0.02847  185 THR B OG1 
2842 C CG2 . THR B 185 ? 0.32391 0.38485 0.31961 0.01278  -0.01477 0.02222  185 THR B CG2 
2843 N N   . VAL B 186 ? 0.42323 0.43775 0.41185 0.00287  -0.01249 0.02219  186 VAL B N   
2844 C CA  . VAL B 186 ? 0.27757 0.27946 0.26359 0.00078  -0.01219 0.02341  186 VAL B CA  
2845 C C   . VAL B 186 ? 0.36045 0.35648 0.34728 0.00394  -0.01357 0.02126  186 VAL B C   
2846 O O   . VAL B 186 ? 0.36593 0.36345 0.35411 0.00773  -0.01459 0.01802  186 VAL B O   
2847 C CB  . VAL B 186 ? 0.35530 0.35258 0.34024 -0.00041 -0.01059 0.02327  186 VAL B CB  
2848 C CG1 . VAL B 186 ? 0.34410 0.33048 0.32679 -0.00141 -0.01020 0.02467  186 VAL B CG1 
2849 C CG2 . VAL B 186 ? 0.33847 0.33931 0.32064 -0.00342 -0.00951 0.02542  186 VAL B CG2 
2850 N N   . GLU B 187 ? 0.36706 0.35544 0.35195 0.00262  -0.01399 0.02302  187 GLU B N   
2851 C CA  . GLU B 187 ? 0.36295 0.34515 0.34774 0.00529  -0.01553 0.02127  187 GLU B CA  
2852 C C   . GLU B 187 ? 0.40236 0.37336 0.38572 0.00375  -0.01510 0.02216  187 GLU B C   
2853 O O   . GLU B 187 ? 0.34731 0.31468 0.32880 0.00100  -0.01362 0.02512  187 GLU B O   
2854 C CB  . GLU B 187 ? 0.36636 0.34967 0.35032 0.00552  -0.01658 0.02255  187 GLU B CB  
2855 C CG  . GLU B 187 ? 0.44884 0.44568 0.43456 0.00668  -0.01710 0.02268  187 GLU B CG  
2856 C CD  . GLU B 187 ? 0.77194 0.77060 0.75701 0.00639  -0.01833 0.02445  187 GLU B CD  
2857 O OE1 . GLU B 187 ? 0.51254 0.50123 0.49518 0.00401  -0.01848 0.02632  187 GLU B OE1 
2858 O OE2 . GLU B 187 ? 0.80324 0.81385 0.79004 0.00889  -0.01918 0.02411  187 GLU B OE2 
2859 N N   . TRP B 188 ? 0.29005 0.25557 0.27339 0.00572  -0.01670 0.01987  188 TRP B N   
2860 C CA  . TRP B 188 ? 0.33488 0.29071 0.31706 0.00398  -0.01680 0.02123  188 TRP B CA  
2861 C C   . TRP B 188 ? 0.34080 0.28997 0.32109 0.00609  -0.01908 0.01979  188 TRP B C   
2862 O O   . TRP B 188 ? 0.37573 0.32425 0.35486 0.00925  -0.02148 0.01647  188 TRP B O   
2863 C CB  . TRP B 188 ? 0.30218 0.25675 0.28533 0.00295  -0.01717 0.02045  188 TRP B CB  
2864 C CG  . TRP B 188 ? 0.40282 0.35007 0.38531 0.00032  -0.01716 0.02293  188 TRP B CG  
2865 C CD1 . TRP B 188 ? 0.44704 0.39481 0.42974 -0.00205 -0.01474 0.02658  188 TRP B CD1 
2866 C CD2 . TRP B 188 ? 0.29481 0.23366 0.27562 0.00001  -0.01986 0.02232  188 TRP B CD2 
2867 N NE1 . TRP B 188 ? 0.44793 0.39003 0.43023 -0.00390 -0.01546 0.02865  188 TRP B NE1 
2868 C CE2 . TRP B 188 ? 0.43223 0.36826 0.41339 -0.00326 -0.01873 0.02615  188 TRP B CE2 
2869 C CE3 . TRP B 188 ? 0.39674 0.32992 0.37476 0.00248  -0.02336 0.01903  188 TRP B CE3 
2870 C CZ2 . TRP B 188 ? 0.41390 0.34219 0.39354 -0.00520 -0.02101 0.02717  188 TRP B CZ2 
2871 C CZ3 . TRP B 188 ? 0.43735 0.36073 0.41262 0.00079  -0.02595 0.01956  188 TRP B CZ3 
2872 C CH2 . TRP B 188 ? 0.53171 0.45297 0.50822 -0.00355 -0.02478 0.02379  188 TRP B CH2 
2873 N N   . ARG B 189 ? 0.35838 0.30187 0.33726 0.00493  -0.01854 0.02216  189 ARG B N   
2874 C CA  . ARG B 189 ? 0.33204 0.26921 0.30873 0.00703  -0.02047 0.02096  189 ARG B CA  
2875 C C   . ARG B 189 ? 0.38271 0.30959 0.35776 0.00535  -0.02124 0.02206  189 ARG B C   
2876 O O   . ARG B 189 ? 0.40989 0.33451 0.38520 0.00272  -0.01934 0.02559  189 ARG B O   
2877 C CB  . ARG B 189 ? 0.32695 0.26521 0.30298 0.00698  -0.01968 0.02289  189 ARG B CB  
2878 C CG  . ARG B 189 ? 0.34947 0.29886 0.32701 0.00785  -0.01957 0.02246  189 ARG B CG  
2879 C CD  . ARG B 189 ? 0.38291 0.33284 0.35924 0.00616  -0.01930 0.02537  189 ARG B CD  
2880 N NE  . ARG B 189 ? 0.51406 0.47610 0.49203 0.00617  -0.01970 0.02557  189 ARG B NE  
2881 C CZ  . ARG B 189 ? 0.65178 0.62101 0.63076 0.00952  -0.02113 0.02372  189 ARG B CZ  
2882 N NH1 . ARG B 189 ? 0.66851 0.63233 0.64602 0.01352  -0.02251 0.02102  189 ARG B NH1 
2883 N NH2 . ARG B 189 ? 0.47562 0.45815 0.45655 0.00901  -0.02131 0.02483  189 ARG B NH2 
2884 N N   . ALA B 190 ? 0.32496 0.24554 0.29739 0.00708  -0.02429 0.01930  190 ALA B N   
2885 C CA  . ALA B 190 ? 0.33190 0.24253 0.30219 0.00462  -0.02579 0.02059  190 ALA B CA  
2886 C C   . ALA B 190 ? 0.42585 0.33044 0.39471 0.00451  -0.02504 0.02268  190 ALA B C   
2887 O O   . ALA B 190 ? 0.42433 0.32665 0.39102 0.00773  -0.02611 0.02067  190 ALA B O   
2888 C CB  . ALA B 190 ? 0.30931 0.21261 0.27494 0.00647  -0.03018 0.01694  190 ALA B CB  
2889 N N   . GLN B 191 ? 0.43575 0.33824 0.40556 0.00127  -0.02325 0.02681  191 GLN B N   
2890 C CA  . GLN B 191 ? 0.44763 0.34398 0.41571 0.00137  -0.02242 0.02923  191 GLN B CA  
2891 C C   . GLN B 191 ? 0.51781 0.40419 0.48289 -0.00001 -0.02498 0.02943  191 GLN B C   
2892 O O   . GLN B 191 ? 0.48295 0.36309 0.44599 0.00069  -0.02477 0.03072  191 GLN B O   
2893 C CB  . GLN B 191 ? 0.39344 0.29330 0.36289 -0.00019 -0.01899 0.03397  191 GLN B CB  
2894 C CG  . GLN B 191 ? 0.29044 0.19809 0.26103 0.00069  -0.01704 0.03400  191 GLN B CG  
2895 C CD  . GLN B 191 ? 0.40709 0.31488 0.37649 0.00301  -0.01775 0.03202  191 GLN B CD  
2896 O OE1 . GLN B 191 ? 0.45564 0.35825 0.42261 0.00395  -0.01758 0.03347  191 GLN B OE1 
2897 N NE2 . GLN B 191 ? 0.36912 0.28351 0.34017 0.00401  -0.01866 0.02897  191 GLN B NE2 
2898 N N   . SER B 192 ? 0.50735 0.39122 0.47133 -0.00217 -0.02779 0.02831  192 SER B N   
2899 C CA  . SER B 192 ? 0.54951 0.42249 0.50911 -0.00432 -0.03126 0.02856  192 SER B CA  
2900 C C   . SER B 192 ? 0.53801 0.40623 0.49349 -0.00420 -0.03586 0.02473  192 SER B C   
2901 O O   . SER B 192 ? 0.57085 0.44571 0.52818 -0.00309 -0.03575 0.02279  192 SER B O   
2902 C CB  . SER B 192 ? 0.39752 0.27138 0.35917 -0.00959 -0.03006 0.03435  192 SER B CB  
2903 O OG  . SER B 192 ? 0.53844 0.42235 0.50455 -0.01200 -0.02822 0.03654  192 SER B OG  
2904 N N   . THR B 193 ? 0.52689 0.38243 0.47561 -0.00509 -0.04026 0.02366  193 THR B N   
2905 C CA  . THR B 193 ? 0.65484 0.50217 0.59660 -0.00447 -0.04576 0.01995  193 THR B CA  
2906 C C   . THR B 193 ? 0.68093 0.52676 0.62289 -0.01172 -0.04815 0.02346  193 THR B C   
2907 O O   . THR B 193 ? 0.65438 0.49746 0.59690 -0.01733 -0.04835 0.02815  193 THR B O   
2908 C CB  . THR B 193 ? 0.57483 0.40713 0.50671 -0.00143 -0.05023 0.01674  193 THR B CB  
2909 O OG1 . THR B 193 ? 0.59338 0.42890 0.52528 0.00565  -0.04819 0.01342  193 THR B OG1 
2910 C CG2 . THR B 193 ? 0.53568 0.35702 0.45776 -0.00035 -0.05675 0.01303  193 THR B CG2 
2911 N N   . GLY B 194 ? 0.78455 0.63305 0.72612 -0.01166 -0.05002 0.02153  194 GLY B N   
2912 C CA  . GLY B 194 ? 0.87173 0.71931 0.81329 -0.01868 -0.05287 0.02471  194 GLY B CA  
2913 C C   . GLY B 194 ? 0.97777 0.80788 0.90788 -0.02118 -0.06080 0.02328  194 GLY B C   
2914 O O   . GLY B 194 ? 1.09994 0.92123 1.02626 -0.02601 -0.06334 0.02634  194 GLY B O   
2915 N N   . ALA C 1   ? 1.02283 0.75265 0.83471 -0.03759 0.01147  -0.02351 -1  ALA C N   
2916 C CA  . ALA C 1   ? 0.70812 0.41779 0.50751 -0.03211 0.01792  -0.01219 -1  ALA C CA  
2917 C C   . ALA C 1   ? 0.72029 0.44448 0.52877 -0.02289 0.01805  -0.00350 -1  ALA C C   
2918 O O   . ALA C 1   ? 0.74702 0.45763 0.54545 -0.01692 0.02486  0.00744  -1  ALA C O   
2919 C CB  . ALA C 1   ? 0.78289 0.46943 0.55849 -0.03191 0.03224  -0.00447 -1  ALA C CB  
2920 N N   . THR C 2   ? 0.60288 0.35488 0.43059 -0.02180 0.01041  -0.00856 0   THR C N   
2921 C CA  . THR C 2   ? 0.64052 0.40906 0.47862 -0.01327 0.00983  -0.00127 0   THR C CA  
2922 C C   . THR C 2   ? 0.62172 0.41639 0.48434 -0.01419 -0.00429 -0.01021 0   THR C C   
2923 O O   . THR C 2   ? 0.53267 0.34424 0.40575 -0.01889 -0.00972 -0.01978 0   THR C O   
2924 C CB  . THR C 2   ? 0.65399 0.43095 0.48662 -0.00853 0.02000  0.00575  0   THR C CB  
2925 O OG1 . THR C 2   ? 0.86236 0.61603 0.67351 -0.00489 0.03320  0.01711  0   THR C OG1 
2926 C CG2 . THR C 2   ? 0.60412 0.40543 0.45285 -0.00116 0.01646  0.00958  0   THR C CG2 
2927 N N   . PRO C 3   ? 0.55699 0.35592 0.42939 -0.00980 -0.01050 -0.00742 1   PRO C N   
2928 C CA  . PRO C 3   ? 0.53967 0.36544 0.43583 -0.00943 -0.02316 -0.01456 1   PRO C CA  
2929 C C   . PRO C 3   ? 0.55127 0.40018 0.45614 -0.00350 -0.02044 -0.01048 1   PRO C C   
2930 O O   . PRO C 3   ? 0.55108 0.39573 0.44679 0.00349  -0.01055 0.00095  1   PRO C O   
2931 C CB  . PRO C 3   ? 0.47355 0.29367 0.37453 -0.00586 -0.02873 -0.01097 1   PRO C CB  
2932 C CG  . PRO C 3   ? 0.49223 0.28499 0.37218 -0.00259 -0.01750 0.00014  1   PRO C CG  
2933 C CD  . PRO C 3   ? 0.62043 0.40088 0.48251 -0.00432 -0.00547 0.00321  1   PRO C CD  
2934 N N   . LEU C 4   ? 0.45230 0.32579 0.37489 -0.00640 -0.02930 -0.02005 2   LEU C N   
2935 C CA  . LEU C 4   ? 0.44119 0.33926 0.37482 -0.00115 -0.02856 -0.01751 2   LEU C CA  
2936 C C   . LEU C 4   ? 0.42552 0.34001 0.37652 0.00456  -0.03692 -0.01571 2   LEU C C   
2937 O O   . LEU C 4   ? 0.42009 0.33145 0.37828 0.00284  -0.04580 -0.01961 2   LEU C O   
2938 C CB  . LEU C 4   ? 0.43206 0.34900 0.37594 -0.00706 -0.03345 -0.02857 2   LEU C CB  
2939 C CG  . LEU C 4   ? 0.52809 0.43114 0.45617 -0.01324 -0.02581 -0.03149 2   LEU C CG  
2940 C CD1 . LEU C 4   ? 0.43659 0.36129 0.37529 -0.01752 -0.02936 -0.04068 2   LEU C CD1 
2941 C CD2 . LEU C 4   ? 0.46401 0.34946 0.37125 -0.00833 -0.01065 -0.01889 2   LEU C CD2 
2942 N N   . LEU C 5   ? 0.41849 0.35034 0.37597 0.01147  -0.03386 -0.00959 3   LEU C N   
2943 C CA  . LEU C 5   ? 0.40392 0.35217 0.37736 0.01766  -0.04062 -0.00685 3   LEU C CA  
2944 C C   . LEU C 5   ? 0.38685 0.36590 0.37854 0.01893  -0.04594 -0.01159 3   LEU C C   
2945 O O   . LEU C 5   ? 0.41067 0.39726 0.40051 0.01642  -0.04223 -0.01459 3   LEU C O   
2946 C CB  . LEU C 5   ? 0.41239 0.35023 0.37547 0.02660  -0.03113 0.00750  3   LEU C CB  
2947 C CG  . LEU C 5   ? 0.41806 0.36059 0.37325 0.03225  -0.01961 0.01623  3   LEU C CG  
2948 C CD1 . LEU C 5   ? 0.41651 0.36153 0.37257 0.04205  -0.01569 0.02790  3   LEU C CD1 
2949 C CD2 . LEU C 5   ? 0.57601 0.49454 0.50806 0.02958  -0.00757 0.02014  3   LEU C CD2 
2950 N N   . MET C 6   ? 0.41776 0.41465 0.42720 0.02289  -0.05472 -0.01219 4   MET C N   
2951 C CA  . MET C 6   ? 0.35568 0.38225 0.38290 0.02569  -0.05938 -0.01483 4   MET C CA  
2952 C C   . MET C 6   ? 0.37193 0.40314 0.39651 0.03553  -0.05123 -0.00222 4   MET C C   
2953 O O   . MET C 6   ? 0.35810 0.37985 0.37947 0.04086  -0.04966 0.00567  4   MET C O   
2954 C CB  . MET C 6   ? 0.33509 0.37991 0.38445 0.02375  -0.07454 -0.02395 4   MET C CB  
2955 C CG  . MET C 6   ? 0.37042 0.41291 0.42322 0.01389  -0.08267 -0.03710 4   MET C CG  
2956 S SD  . MET C 6   ? 0.49997 0.56297 0.57830 0.01079  -0.10087 -0.04878 4   MET C SD  
2957 C CE  . MET C 6   ? 0.32164 0.35998 0.39067 0.00180  -0.10511 -0.05657 4   MET C CE  
2958 N N   . GLN C 7   ? 0.42351 0.46858 0.44887 0.03783  -0.04583 -0.00031 5   GLN C N   
2959 C CA  . GLN C 7   ? 0.42452 0.47356 0.44593 0.04696  -0.03705 0.01165  5   GLN C CA  
2960 C C   . GLN C 7   ? 0.33635 0.41130 0.37883 0.05247  -0.04519 0.01160  5   GLN C C   
2961 O O   . GLN C 7   ? 0.41715 0.51393 0.47754 0.04927  -0.05526 0.00199  5   GLN C O   
2962 C CB  . GLN C 7   ? 0.47150 0.52309 0.48353 0.04707  -0.02724 0.01404  5   GLN C CB  
2963 C CG  . GLN C 7   ? 0.65936 0.68302 0.64756 0.04392  -0.01634 0.01776  5   GLN C CG  
2964 C CD  . GLN C 7   ? 0.91004 0.93671 0.88965 0.04297  -0.00762 0.01868  5   GLN C CD  
2965 O OE1 . GLN C 7   ? 0.85918 0.90619 0.85062 0.03992  -0.01243 0.01096  5   GLN C OE1 
2966 N NE2 . GLN C 7   ? 0.98289 0.98932 0.94177 0.04558  0.00530  0.02815  5   GLN C NE2 
2967 N N   . ALA C 8   ? 0.39013 0.46234 0.43031 0.06079  -0.04077 0.02239  6   ALA C N   
2968 C CA  . ALA C 8   ? 0.35227 0.44788 0.41091 0.06703  -0.04705 0.02399  6   ALA C CA  
2969 C C   . ALA C 8   ? 0.36808 0.48327 0.43111 0.07110  -0.04234 0.02666  6   ALA C C   
2970 O O   . ALA C 8   ? 0.32870 0.43429 0.37632 0.07281  -0.03079 0.03306  6   ALA C O   
2971 C CB  . ALA C 8   ? 0.33407 0.41858 0.38793 0.07437  -0.04373 0.03463  6   ALA C CB  
2972 N N   . LEU C 9   ? 0.33068 0.47354 0.41492 0.07260  -0.05146 0.02162  7   LEU C N   
2973 C CA  . LEU C 9   ? 0.28956 0.45304 0.37990 0.07613  -0.04822 0.02317  7   LEU C CA  
2974 C C   . LEU C 9   ? 0.42375 0.59947 0.52155 0.08601  -0.04680 0.03234  7   LEU C C   
2975 O O   . LEU C 9   ? 0.36133 0.54446 0.47192 0.08841  -0.05506 0.03160  7   LEU C O   
2976 C CB  . LEU C 9   ? 0.29241 0.48014 0.40141 0.07057  -0.05894 0.01055  7   LEU C CB  
2977 C CG  . LEU C 9   ? 0.43402 0.61291 0.53762 0.06054  -0.06105 0.00038  7   LEU C CG  
2978 C CD1 . LEU C 9   ? 0.28682 0.49012 0.41152 0.05546  -0.07380 -0.01239 7   LEU C CD1 
2979 C CD2 . LEU C 9   ? 0.30432 0.47369 0.39084 0.05940  -0.04901 0.00388  7   LEU C CD2 
2980 N N   . PRO C 10  ? 0.52102 0.69920 0.61121 0.09185  -0.03657 0.04095  8   PRO C N   
2981 C CA  . PRO C 10  ? 0.35521 0.54566 0.45256 0.10144  -0.03497 0.04970  8   PRO C CA  
2982 C C   . PRO C 10  ? 0.34916 0.57099 0.47079 0.10240  -0.04571 0.04309  8   PRO C C   
2983 O O   . PRO C 10  ? 0.36464 0.60137 0.49492 0.09726  -0.05038 0.03412  8   PRO C O   
2984 C CB  . PRO C 10  ? 0.42319 0.60842 0.50561 0.10608  -0.02136 0.05900  8   PRO C CB  
2985 C CG  . PRO C 10  ? 0.36907 0.53394 0.43363 0.09920  -0.01496 0.05654  8   PRO C CG  
2986 C CD  . PRO C 10  ? 0.41946 0.58933 0.49410 0.08999  -0.02598 0.04307  8   PRO C CD  
2987 N N   . MET C 11  ? 0.43292 0.66478 0.56562 0.10908  -0.04963 0.04759  9   MET C N   
2988 C CA  . MET C 11  ? 0.57830 0.84046 0.73392 0.11152  -0.05889 0.04310  9   MET C CA  
2989 C C   . MET C 11  ? 0.69702 0.97228 0.85254 0.11909  -0.05108 0.05109  9   MET C C   
2990 O O   . MET C 11  ? 0.78117 1.06481 0.94267 0.12707  -0.05036 0.05833  9   MET C O   
2991 C CB  . MET C 11  ? 0.39203 0.65879 0.56046 0.11436  -0.06793 0.04304  9   MET C CB  
2992 C CG  . MET C 11  ? 0.35038 0.60853 0.52224 0.10657  -0.07744 0.03365  9   MET C CG  
2993 S SD  . MET C 11  ? 0.56084 0.82328 0.74666 0.11023  -0.08748 0.03434  9   MET C SD  
2994 C CE  . MET C 11  ? 0.44241 0.69805 0.63321 0.09951  -0.09920 0.02091  9   MET C CE  
2995 N N   . GLY C 12  ? 0.83025 1.10702 0.97861 0.11633  -0.04514 0.04954  10  GLY C N   
2996 C CA  . GLY C 12  ? 0.81942 1.10692 0.96567 0.12261  -0.03700 0.05664  10  GLY C CA  
2997 C C   . GLY C 12  ? 0.86191 1.12672 0.98405 0.12393  -0.02266 0.06526  10  GLY C C   
2998 O O   . GLY C 12  ? 0.89509 1.14980 1.00646 0.11757  -0.01898 0.06119  10  GLY C O   
2999 N N   . LYS D 4   ? 0.58332 0.51564 0.45774 -0.11137 -0.01709 0.01241  2   LYS D N   
3000 C CA  . LYS D 4   ? 0.62950 0.58448 0.51247 -0.11717 -0.01261 0.00949  2   LYS D CA  
3001 C C   . LYS D 4   ? 0.68012 0.65524 0.57611 -0.10841 -0.01051 0.00441  2   LYS D C   
3002 O O   . LYS D 4   ? 0.65261 0.64439 0.55922 -0.10820 -0.00870 -0.00000 2   LYS D O   
3003 C CB  . LYS D 4   ? 0.78177 0.74169 0.65584 -0.12971 -0.00946 0.01336  2   LYS D CB  
3004 C CG  . LYS D 4   ? 0.99632 0.94885 0.86509 -0.14205 -0.00966 0.01585  2   LYS D CG  
3005 C CD  . LYS D 4   ? 0.81770 0.78462 0.69934 -0.14224 -0.00853 0.00989  2   LYS D CD  
3006 C CE  . LYS D 4   ? 0.96573 0.96197 0.85765 -0.14305 -0.00363 0.00503  2   LYS D CE  
3007 N NZ  . LYS D 4   ? 0.63018 0.64051 0.53481 -0.14080 -0.00327 -0.00146 2   LYS D NZ  
3008 N N   . GLU D 5   ? 0.46807 0.44128 0.36342 -0.10089 -0.01132 0.00463  3   GLU D N   
3009 C CA  . GLU D 5   ? 0.49008 0.48027 0.39828 -0.09219 -0.01032 -0.00035 3   GLU D CA  
3010 C C   . GLU D 5   ? 0.54969 0.53993 0.46884 -0.08453 -0.01197 -0.00341 3   GLU D C   
3011 O O   . GLU D 5   ? 0.50268 0.50922 0.43288 -0.08219 -0.01079 -0.00754 3   GLU D O   
3012 C CB  . GLU D 5   ? 0.40869 0.39482 0.31433 -0.08535 -0.01155 0.00015  3   GLU D CB  
3013 C CG  . GLU D 5   ? 0.80186 0.79643 0.69995 -0.09085 -0.00923 0.00169  3   GLU D CG  
3014 C CD  . GLU D 5   ? 0.95089 0.93786 0.84398 -0.08397 -0.01121 0.00256  3   GLU D CD  
3015 O OE1 . GLU D 5   ? 0.96571 0.93152 0.84818 -0.08335 -0.01408 0.00656  3   GLU D OE1 
3016 O OE2 . GLU D 5   ? 1.01150 1.01383 0.91172 -0.07854 -0.01047 -0.00148 3   GLU D OE2 
3017 N N   . VAL D 6   ? 0.45079 0.42338 0.36665 -0.08034 -0.01496 -0.00154 4   VAL D N   
3018 C CA  . VAL D 6   ? 0.50777 0.47992 0.43232 -0.07364 -0.01633 -0.00357 4   VAL D CA  
3019 C C   . VAL D 6   ? 0.48948 0.44924 0.40784 -0.07766 -0.01815 -0.00206 4   VAL D C   
3020 O O   . VAL D 6   ? 0.50485 0.44733 0.41297 -0.07913 -0.02073 0.00062  4   VAL D O   
3021 C CB  . VAL D 6   ? 0.50685 0.47262 0.43535 -0.06369 -0.01826 -0.00395 4   VAL D CB  
3022 C CG1 . VAL D 6   ? 0.44331 0.40831 0.37915 -0.05808 -0.01932 -0.00499 4   VAL D CG1 
3023 C CG2 . VAL D 6   ? 0.43455 0.41321 0.37099 -0.05929 -0.01711 -0.00638 4   VAL D CG2 
3024 N N   . GLU D 7   ? 0.44876 0.41725 0.37339 -0.07878 -0.01745 -0.00432 5   GLU D N   
3025 C CA  . GLU D 7   ? 0.59317 0.55263 0.51374 -0.08205 -0.01945 -0.00415 5   GLU D CA  
3026 C C   . GLU D 7   ? 0.53449 0.49826 0.46338 -0.07428 -0.02035 -0.00647 5   GLU D C   
3027 O O   . GLU D 7   ? 0.54806 0.52694 0.48608 -0.07175 -0.01858 -0.00877 5   GLU D O   
3028 C CB  . GLU D 7   ? 0.51382 0.48081 0.43290 -0.09252 -0.01766 -0.00492 5   GLU D CB  
3029 C CG  . GLU D 7   ? 0.84254 0.79525 0.75404 -0.09858 -0.02047 -0.00386 5   GLU D CG  
3030 C CD  . GLU D 7   ? 0.96377 0.90013 0.86248 -0.10562 -0.02187 0.00072  5   GLU D CD  
3031 O OE1 . GLU D 7   ? 0.85129 0.79439 0.74695 -0.11293 -0.01882 0.00267  5   GLU D OE1 
3032 O OE2 . GLU D 7   ? 0.93626 0.85338 0.82760 -0.10357 -0.02629 0.00227  5   GLU D OE2 
3033 N N   . GLN D 8   ? 0.50144 0.45239 0.42678 -0.07025 -0.02340 -0.00597 6   GLN D N   
3034 C CA  . GLN D 8   ? 0.51237 0.46717 0.44386 -0.06335 -0.02424 -0.00765 6   GLN D CA  
3035 C C   . GLN D 8   ? 0.54377 0.49417 0.47179 -0.06627 -0.02661 -0.00941 6   GLN D C   
3036 O O   . GLN D 8   ? 0.58538 0.52608 0.50590 -0.07328 -0.02835 -0.00902 6   GLN D O   
3037 C CB  . GLN D 8   ? 0.38230 0.32928 0.31390 -0.05534 -0.02582 -0.00679 6   GLN D CB  
3038 C CG  . GLN D 8   ? 0.42098 0.37207 0.35760 -0.05134 -0.02407 -0.00579 6   GLN D CG  
3039 C CD  . GLN D 8   ? 0.49880 0.44411 0.43711 -0.04377 -0.02545 -0.00562 6   GLN D CD  
3040 O OE1 . GLN D 8   ? 0.37371 0.31141 0.30896 -0.04197 -0.02644 -0.00526 6   GLN D OE1 
3041 N NE2 . GLN D 8   ? 0.43462 0.38461 0.37778 -0.03928 -0.02545 -0.00607 6   GLN D NE2 
3042 N N   . ASP D 9   ? 0.47916 0.43667 0.41270 -0.06075 -0.02693 -0.01127 7   ASP D N   
3043 C CA  . ASP D 9   ? 0.56659 0.52028 0.49750 -0.06115 -0.02991 -0.01380 7   ASP D CA  
3044 C C   . ASP D 9   ? 0.59859 0.53425 0.52093 -0.06072 -0.03414 -0.01358 7   ASP D C   
3045 O O   . ASP D 9   ? 0.48658 0.41697 0.40804 -0.05473 -0.03488 -0.01254 7   ASP D O   
3046 C CB  . ASP D 9   ? 0.46855 0.43235 0.40559 -0.05335 -0.02974 -0.01527 7   ASP D CB  
3047 C CG  . ASP D 9   ? 0.49330 0.47350 0.43811 -0.05279 -0.02670 -0.01573 7   ASP D CG  
3048 O OD1 . ASP D 9   ? 0.80403 0.79018 0.74971 -0.05907 -0.02584 -0.01768 7   ASP D OD1 
3049 O OD2 . ASP D 9   ? 0.52037 0.50749 0.47041 -0.04616 -0.02543 -0.01424 7   ASP D OD2 
3050 N N   . PRO D 10  ? 0.67112 0.59680 0.58734 -0.06681 -0.03739 -0.01486 8   PRO D N   
3051 C CA  . PRO D 10  ? 0.66126 0.56746 0.56826 -0.06675 -0.04240 -0.01455 8   PRO D CA  
3052 C C   . PRO D 10  ? 0.69661 0.59926 0.60360 -0.05777 -0.04644 -0.01794 8   PRO D C   
3053 O O   . PRO D 10  ? 0.65886 0.55831 0.56515 -0.05116 -0.04703 -0.01755 8   PRO D O   
3054 C CB  . PRO D 10  ? 0.66497 0.56248 0.56670 -0.07663 -0.04497 -0.01501 8   PRO D CB  
3055 C CG  . PRO D 10  ? 0.60666 0.52058 0.51479 -0.08292 -0.04002 -0.01505 8   PRO D CG  
3056 C CD  . PRO D 10  ? 0.61049 0.54174 0.52801 -0.07477 -0.03687 -0.01666 8   PRO D CD  
3057 N N   . GLY D 11  ? 0.97025 0.87478 0.87840 -0.05750 -0.04935 -0.02193 9   GLY D N   
3058 C CA  . GLY D 11  ? 0.73415 0.63394 0.64066 -0.05012 -0.05457 -0.02628 9   GLY D CA  
3059 C C   . GLY D 11  ? 0.74520 0.65702 0.65709 -0.04041 -0.05227 -0.02682 9   GLY D C   
3060 O O   . GLY D 11  ? 0.76545 0.68987 0.68340 -0.03928 -0.04673 -0.02375 9   GLY D O   
3061 N N   . PRO D 12  ? 0.73585 0.64401 0.64564 -0.03332 -0.05686 -0.03090 10  PRO D N   
3062 C CA  . PRO D 12  ? 0.58871 0.50983 0.50355 -0.02466 -0.05454 -0.03152 10  PRO D CA  
3063 C C   . PRO D 12  ? 0.56192 0.50089 0.48310 -0.02266 -0.05142 -0.03200 10  PRO D C   
3064 O O   . PRO D 12  ? 0.58976 0.53053 0.51081 -0.02464 -0.05372 -0.03521 10  PRO D O   
3065 C CB  . PRO D 12  ? 0.65986 0.57319 0.57018 -0.01823 -0.06120 -0.03726 10  PRO D CB  
3066 C CG  . PRO D 12  ? 0.76367 0.65582 0.66569 -0.02335 -0.06701 -0.03813 10  PRO D CG  
3067 C CD  . PRO D 12  ? 0.73898 0.63031 0.64138 -0.03295 -0.06475 -0.03515 10  PRO D CD  
3068 N N   . PHE D 13  ? 0.59405 0.54585 0.52075 -0.01872 -0.04644 -0.02873 11  PHE D N   
3069 C CA  . PHE D 13  ? 0.48125 0.44968 0.41278 -0.01539 -0.04384 -0.02855 11  PHE D CA  
3070 C C   . PHE D 13  ? 0.61976 0.59539 0.55098 -0.00736 -0.04571 -0.03185 11  PHE D C   
3071 O O   . PHE D 13  ? 0.58160 0.55862 0.51384 -0.00370 -0.04429 -0.03046 11  PHE D O   
3072 C CB  . PHE D 13  ? 0.47014 0.44792 0.40751 -0.01598 -0.03784 -0.02257 11  PHE D CB  
3073 C CG  . PHE D 13  ? 0.54181 0.51772 0.48058 -0.02290 -0.03596 -0.02057 11  PHE D CG  
3074 C CD1 . PHE D 13  ? 0.44440 0.41268 0.37954 -0.02898 -0.03870 -0.02347 11  PHE D CD1 
3075 C CD2 . PHE D 13  ? 0.46803 0.45045 0.41210 -0.02346 -0.03169 -0.01609 11  PHE D CD2 
3076 C CE1 . PHE D 13  ? 0.49729 0.46643 0.43399 -0.03576 -0.03651 -0.02198 11  PHE D CE1 
3077 C CE2 . PHE D 13  ? 0.39888 0.38190 0.34463 -0.02917 -0.03022 -0.01533 11  PHE D CE2 
3078 C CZ  . PHE D 13  ? 0.46942 0.44682 0.41145 -0.03546 -0.03228 -0.01831 11  PHE D CZ  
3079 N N   . ASN D 14  ? 0.55234 0.53368 0.48254 -0.00458 -0.04899 -0.03683 12  ASN D N   
3080 C CA  . ASN D 14  ? 0.54132 0.53387 0.47154 0.00347  -0.05047 -0.04048 12  ASN D CA  
3081 C C   . ASN D 14  ? 0.43242 0.44280 0.36624 0.00600  -0.04622 -0.03752 12  ASN D C   
3082 O O   . ASN D 14  ? 0.46664 0.48128 0.40082 0.00496  -0.04730 -0.03958 12  ASN D O   
3083 C CB  . ASN D 14  ? 0.51099 0.49777 0.43731 0.00607  -0.05811 -0.04904 12  ASN D CB  
3084 C CG  . ASN D 14  ? 0.65178 0.62046 0.57349 0.00526  -0.06314 -0.05182 12  ASN D CG  
3085 O OD1 . ASN D 14  ? 0.74914 0.71879 0.67026 0.01021  -0.06366 -0.05304 12  ASN D OD1 
3086 N ND2 . ASN D 14  ? 0.64714 0.59936 0.56538 -0.00115 -0.06693 -0.05273 12  ASN D ND2 
3087 N N   . VAL D 15  ? 0.48629 0.50669 0.42267 0.00912  -0.04157 -0.03259 13  VAL D N   
3088 C CA  . VAL D 15  ? 0.43659 0.47100 0.37578 0.01051  -0.03703 -0.02731 13  VAL D CA  
3089 C C   . VAL D 15  ? 0.54483 0.59448 0.48356 0.01726  -0.03577 -0.02729 13  VAL D C   
3090 O O   . VAL D 15  ? 0.50270 0.55261 0.44164 0.01928  -0.03543 -0.02785 13  VAL D O   
3091 C CB  . VAL D 15  ? 0.44467 0.47556 0.38781 0.00622  -0.03222 -0.01958 13  VAL D CB  
3092 C CG1 . VAL D 15  ? 0.42880 0.47278 0.37450 0.00889  -0.02784 -0.01307 13  VAL D CG1 
3093 C CG2 . VAL D 15  ? 0.48702 0.50963 0.43076 0.00022  -0.03291 -0.01985 13  VAL D CG2 
3094 N N   . PRO D 16  ? 0.42786 0.49141 0.36572 0.02104  -0.03518 -0.02715 14  PRO D N   
3095 C CA  . PRO D 16  ? 0.40236 0.48249 0.33927 0.02693  -0.03304 -0.02580 14  PRO D CA  
3096 C C   . PRO D 16  ? 0.49708 0.58128 0.43685 0.02507  -0.02678 -0.01572 14  PRO D C   
3097 O O   . PRO D 16  ? 0.41464 0.49367 0.35669 0.02127  -0.02444 -0.00975 14  PRO D O   
3098 C CB  . PRO D 16  ? 0.28734 0.37988 0.22178 0.03119  -0.03459 -0.02834 14  PRO D CB  
3099 C CG  . PRO D 16  ? 0.35557 0.43737 0.29049 0.02741  -0.03811 -0.03243 14  PRO D CG  
3100 C CD  . PRO D 16  ? 0.46237 0.52835 0.39991 0.02026  -0.03644 -0.02849 14  PRO D CD  
3101 N N   . GLU D 17  ? 0.32625 0.42031 0.26633 0.02777  -0.02440 -0.01431 15  GLU D N   
3102 C CA  . GLU D 17  ? 0.37178 0.47032 0.31499 0.02555  -0.01855 -0.00455 15  GLU D CA  
3103 C C   . GLU D 17  ? 0.37818 0.48331 0.32007 0.02581  -0.01610 0.00280  15  GLU D C   
3104 O O   . GLU D 17  ? 0.53264 0.64884 0.47022 0.03026  -0.01742 0.00072  15  GLU D O   
3105 C CB  . GLU D 17  ? 0.37552 0.48808 0.31886 0.02854  -0.01623 -0.00483 15  GLU D CB  
3106 C CG  . GLU D 17  ? 0.58088 0.69110 0.52968 0.02432  -0.01152 0.00213  15  GLU D CG  
3107 C CD  . GLU D 17  ? 0.69267 0.81979 0.64221 0.02640  -0.00831 0.00259  15  GLU D CD  
3108 O OE1 . GLU D 17  ? 0.60770 0.75095 0.55283 0.03130  -0.00877 -0.00038 15  GLU D OE1 
3109 O OE2 . GLU D 17  ? 0.67180 0.79718 0.62670 0.02314  -0.00532 0.00547  15  GLU D OE2 
3110 N N   . GLY D 18  ? 0.44281 0.54078 0.38839 0.02160  -0.01318 0.01090  16  GLY D N   
3111 C CA  . GLY D 18  ? 0.48297 0.58440 0.42736 0.02195  -0.01168 0.01815  16  GLY D CA  
3112 C C   . GLY D 18  ? 0.45940 0.55148 0.40449 0.02044  -0.01450 0.01610  16  GLY D C   
3113 O O   . GLY D 18  ? 0.48652 0.57851 0.43188 0.02039  -0.01375 0.02207  16  GLY D O   
3114 N N   . ALA D 19  ? 0.39948 0.48390 0.34478 0.01910  -0.01793 0.00778  17  ALA D N   
3115 C CA  . ALA D 19  ? 0.43313 0.51057 0.37948 0.01680  -0.02027 0.00507  17  ALA D CA  
3116 C C   . ALA D 19  ? 0.42833 0.49444 0.37996 0.01182  -0.01890 0.00902  17  ALA D C   
3117 O O   . ALA D 19  ? 0.42281 0.48334 0.37744 0.00964  -0.01711 0.01143  17  ALA D O   
3118 C CB  . ALA D 19  ? 0.31953 0.39241 0.26421 0.01599  -0.02433 -0.00459 17  ALA D CB  
3119 N N   . THR D 20  ? 0.42707 0.49104 0.38022 0.01050  -0.02005 0.00883  18  THR D N   
3120 C CA  . THR D 20  ? 0.40687 0.46159 0.36515 0.00626  -0.01962 0.01057  18  THR D CA  
3121 C C   . THR D 20  ? 0.46199 0.50881 0.42040 0.00187  -0.02150 0.00368  18  THR D C   
3122 O O   . THR D 20  ? 0.45147 0.50035 0.40700 0.00169  -0.02383 -0.00225 18  THR D O   
3123 C CB  . THR D 20  ? 0.37646 0.43420 0.33649 0.00754  -0.02033 0.01324  18  THR D CB  
3124 O OG1 . THR D 20  ? 0.46889 0.53122 0.42819 0.01099  -0.01879 0.02117  18  THR D OG1 
3125 C CG2 . THR D 20  ? 0.49288 0.54287 0.45862 0.00370  -0.02062 0.01316  18  THR D CG2 
3126 N N   . VAL D 21  ? 0.46260 0.50028 0.42421 -0.00179 -0.02064 0.00460  19  VAL D N   
3127 C CA  . VAL D 21  ? 0.39051 0.41937 0.35114 -0.00640 -0.02216 -0.00049 19  VAL D CA  
3128 C C   . VAL D 21  ? 0.45473 0.48033 0.41962 -0.01012 -0.02171 0.00011  19  VAL D C   
3129 O O   . VAL D 21  ? 0.41096 0.43649 0.38060 -0.00921 -0.02031 0.00456  19  VAL D O   
3130 C CB  . VAL D 21  ? 0.43592 0.45721 0.39527 -0.00677 -0.02208 -0.00100 19  VAL D CB  
3131 C CG1 . VAL D 21  ? 0.50322 0.51405 0.45960 -0.01133 -0.02433 -0.00576 19  VAL D CG1 
3132 C CG2 . VAL D 21  ? 0.55148 0.57879 0.50750 -0.00222 -0.02254 -0.00206 19  VAL D CG2 
3133 N N   . ALA D 22  ? 0.40344 0.42687 0.36697 -0.01447 -0.02310 -0.00463 20  ALA D N   
3134 C CA  . ALA D 22  ? 0.40271 0.42535 0.36987 -0.01837 -0.02268 -0.00529 20  ALA D CA  
3135 C C   . ALA D 22  ? 0.35344 0.36646 0.31778 -0.02393 -0.02302 -0.00760 20  ALA D C   
3136 O O   . ALA D 22  ? 0.46297 0.47276 0.42275 -0.02725 -0.02460 -0.01128 20  ALA D O   
3137 C CB  . ALA D 22  ? 0.45860 0.49027 0.42688 -0.01912 -0.02368 -0.00882 20  ALA D CB  
3138 N N   . PHE D 23  ? 0.44824 0.45622 0.41510 -0.02485 -0.02192 -0.00539 21  PHE D N   
3139 C CA  . PHE D 23  ? 0.34580 0.34511 0.30953 -0.02990 -0.02218 -0.00689 21  PHE D CA  
3140 C C   . PHE D 23  ? 0.36409 0.36858 0.33094 -0.03394 -0.02137 -0.00834 21  PHE D C   
3141 O O   . PHE D 23  ? 0.38326 0.39443 0.35647 -0.03123 -0.02071 -0.00724 21  PHE D O   
3142 C CB  . PHE D 23  ? 0.28985 0.28161 0.25429 -0.02779 -0.02169 -0.00445 21  PHE D CB  
3143 C CG  . PHE D 23  ? 0.35174 0.33951 0.31326 -0.02404 -0.02251 -0.00402 21  PHE D CG  
3144 C CD1 . PHE D 23  ? 0.30580 0.29985 0.27115 -0.01908 -0.02132 -0.00120 21  PHE D CD1 
3145 C CD2 . PHE D 23  ? 0.38370 0.36165 0.33848 -0.02544 -0.02472 -0.00649 21  PHE D CD2 
3146 C CE1 . PHE D 23  ? 0.38157 0.37457 0.34451 -0.01573 -0.02180 -0.00143 21  PHE D CE1 
3147 C CE2 . PHE D 23  ? 0.29303 0.26881 0.24555 -0.02124 -0.02602 -0.00737 21  PHE D CE2 
3148 C CZ  . PHE D 23  ? 0.35393 0.33841 0.31079 -0.01643 -0.02429 -0.00511 21  PHE D CZ  
3149 N N   . ASN D 24  ? 0.40494 0.40651 0.36739 -0.04047 -0.02167 -0.01087 22  ASN D N   
3150 C CA  . ASN D 24  ? 0.40290 0.41133 0.36787 -0.04506 -0.02053 -0.01271 22  ASN D CA  
3151 C C   . ASN D 24  ? 0.41227 0.41232 0.37252 -0.05009 -0.02005 -0.01195 22  ASN D C   
3152 O O   . ASN D 24  ? 0.50732 0.49518 0.46055 -0.05200 -0.02128 -0.01097 22  ASN D O   
3153 C CB  . ASN D 24  ? 0.38088 0.39773 0.34561 -0.04948 -0.02074 -0.01664 22  ASN D CB  
3154 C CG  . ASN D 24  ? 0.36252 0.39052 0.33264 -0.04393 -0.02129 -0.01796 22  ASN D CG  
3155 O OD1 . ASN D 24  ? 0.47829 0.50590 0.44672 -0.04075 -0.02247 -0.01806 22  ASN D OD1 
3156 N ND2 . ASN D 24  ? 0.32959 0.36763 0.30592 -0.04204 -0.02093 -0.01917 22  ASN D ND2 
3157 N N   . CYS D 25  ? 0.48338 0.49046 0.44724 -0.05174 -0.01871 -0.01274 23  CYS D N   
3158 C CA  . CYS D 25  ? 0.46980 0.47136 0.42940 -0.05573 -0.01802 -0.01182 23  CYS D CA  
3159 C C   . CYS D 25  ? 0.42714 0.44233 0.39030 -0.05966 -0.01639 -0.01460 23  CYS D C   
3160 O O   . CYS D 25  ? 0.47068 0.49791 0.44213 -0.05558 -0.01643 -0.01691 23  CYS D O   
3161 C CB  . CYS D 25  ? 0.41420 0.40905 0.37577 -0.04969 -0.01849 -0.00957 23  CYS D CB  
3162 S SG  . CYS D 25  ? 0.51313 0.50511 0.47149 -0.05215 -0.01784 -0.00923 23  CYS D SG  
3163 N N   . THR D 26  ? 0.40826 0.42180 0.36490 -0.06752 -0.01524 -0.01444 24  THR D N   
3164 C CA  . THR D 26  ? 0.37873 0.40696 0.33781 -0.07225 -0.01325 -0.01728 24  THR D CA  
3165 C C   . THR D 26  ? 0.40006 0.42464 0.35442 -0.07409 -0.01237 -0.01537 24  THR D C   
3166 O O   . THR D 26  ? 0.42083 0.42984 0.36631 -0.07606 -0.01308 -0.01162 24  THR D O   
3167 C CB  . THR D 26  ? 0.40155 0.43538 0.35727 -0.08180 -0.01195 -0.01909 24  THR D CB  
3168 O OG1 . THR D 26  ? 0.60792 0.62500 0.55340 -0.08774 -0.01268 -0.01543 24  THR D OG1 
3169 C CG2 . THR D 26  ? 0.47399 0.51643 0.43605 -0.07910 -0.01284 -0.02266 24  THR D CG2 
3170 N N   . TYR D 27  ? 0.38955 0.42893 0.34968 -0.07282 -0.01134 -0.01846 25  TYR D N   
3171 C CA  . TYR D 27  ? 0.36382 0.40347 0.32018 -0.07387 -0.01048 -0.01756 25  TYR D CA  
3172 C C   . TYR D 27  ? 0.44836 0.50569 0.40429 -0.08131 -0.00782 -0.02057 25  TYR D C   
3173 O O   . TYR D 27  ? 0.43686 0.51075 0.40053 -0.08134 -0.00739 -0.02550 25  TYR D O   
3174 C CB  . TYR D 27  ? 0.35352 0.39532 0.31826 -0.06382 -0.01227 -0.01920 25  TYR D CB  
3175 C CG  . TYR D 27  ? 0.34033 0.39969 0.31737 -0.05877 -0.01318 -0.02469 25  TYR D CG  
3176 C CD1 . TYR D 27  ? 0.32154 0.38071 0.30580 -0.05331 -0.01503 -0.02539 25  TYR D CD1 
3177 C CD2 . TYR D 27  ? 0.35163 0.42789 0.33261 -0.05900 -0.01267 -0.02934 25  TYR D CD2 
3178 C CE1 . TYR D 27  ? 0.38775 0.46114 0.38252 -0.04812 -0.01686 -0.03033 25  TYR D CE1 
3179 C CE2 . TYR D 27  ? 0.34047 0.43237 0.33278 -0.05352 -0.01459 -0.03527 25  TYR D CE2 
3180 C CZ  . TYR D 27  ? 0.36639 0.45582 0.36541 -0.04803 -0.01695 -0.03564 25  TYR D CZ  
3181 O OH  . TYR D 27  ? 0.42337 0.52668 0.43294 -0.04210 -0.01981 -0.04149 25  TYR D OH  
3182 N N   . SER D 28  ? 0.46195 0.51644 0.40850 -0.08754 -0.00613 -0.01771 26  SER D N   
3183 C CA  . SER D 28  ? 0.48940 0.56094 0.43382 -0.09642 -0.00290 -0.01964 26  SER D CA  
3184 C C   . SER D 28  ? 0.51488 0.60593 0.46602 -0.09180 -0.00240 -0.02464 26  SER D C   
3185 O O   . SER D 28  ? 0.49176 0.60429 0.44718 -0.09584 -0.00038 -0.02955 26  SER D O   
3186 C CB  . SER D 28  ? 0.36672 0.42603 0.29640 -0.10662 -0.00121 -0.01328 26  SER D CB  
3187 O OG  . SER D 28  ? 0.73880 0.78429 0.66202 -0.10176 -0.00280 -0.00961 26  SER D OG  
3188 N N   . ASN D 29  ? 0.41649 0.50179 0.36925 -0.08325 -0.00448 -0.02436 27  ASN D N   
3189 C CA  . ASN D 29  ? 0.44203 0.54515 0.40071 -0.07851 -0.00464 -0.02952 27  ASN D CA  
3190 C C   . ASN D 29  ? 0.42102 0.53741 0.39502 -0.06974 -0.00740 -0.03667 27  ASN D C   
3191 O O   . ASN D 29  ? 0.47040 0.57637 0.45085 -0.06114 -0.01060 -0.03644 27  ASN D O   
3192 C CB  . ASN D 29  ? 0.40341 0.49502 0.35807 -0.07271 -0.00625 -0.02701 27  ASN D CB  
3193 C CG  . ASN D 29  ? 0.51245 0.62195 0.47557 -0.06546 -0.00757 -0.03352 27  ASN D CG  
3194 O OD1 . ASN D 29  ? 0.44450 0.57647 0.41158 -0.06774 -0.00619 -0.03887 27  ASN D OD1 
3195 N ND2 . ASN D 29  ? 0.50016 0.60064 0.46676 -0.05643 -0.01058 -0.03386 27  ASN D ND2 
3196 N N   . SER D 30  ? 0.45840 0.59804 0.43807 -0.07198 -0.00639 -0.04310 28  SER D N   
3197 C CA  . SER D 30  ? 0.37671 0.52959 0.37042 -0.06330 -0.00992 -0.05064 28  SER D CA  
3198 C C   . SER D 30  ? 0.36426 0.51678 0.36602 -0.05216 -0.01393 -0.05366 28  SER D C   
3199 O O   . SER D 30  ? 0.46961 0.62176 0.48209 -0.04355 -0.01813 -0.05698 28  SER D O   
3200 C CB  . SER D 30  ? 0.30105 0.48129 0.29886 -0.06746 -0.00839 -0.05826 28  SER D CB  
3201 O OG  . SER D 30  ? 0.52556 0.70676 0.51652 -0.07874 -0.00451 -0.05572 28  SER D OG  
3202 N N   . ALA D 31  ? 0.38629 0.53855 0.38308 -0.05212 -0.01306 -0.05255 29  ALA D N   
3203 C CA  . ALA D 31  ? 0.41927 0.57224 0.42446 -0.04157 -0.01714 -0.05635 29  ALA D CA  
3204 C C   . ALA D 31  ? 0.31317 0.44264 0.32001 -0.03578 -0.01958 -0.05136 29  ALA D C   
3205 O O   . ALA D 31  ? 0.37845 0.50661 0.39305 -0.02735 -0.02312 -0.05424 29  ALA D O   
3206 C CB  . ALA D 31  ? 0.30449 0.46620 0.30347 -0.04293 -0.01549 -0.05730 29  ALA D CB  
3207 N N   . SER D 32  ? 0.36917 0.48137 0.36957 -0.04002 -0.01795 -0.04462 36  SER D N   
3208 C CA  . SER D 32  ? 0.31986 0.41180 0.32154 -0.03506 -0.01983 -0.04014 36  SER D CA  
3209 C C   . SER D 32  ? 0.35235 0.44624 0.36856 -0.02588 -0.02423 -0.04386 36  SER D C   
3210 O O   . SER D 32  ? 0.33152 0.43452 0.35413 -0.02472 -0.02565 -0.04701 36  SER D O   
3211 C CB  . SER D 32  ? 0.27100 0.34798 0.26441 -0.04077 -0.01775 -0.03375 36  SER D CB  
3212 O OG  . SER D 32  ? 0.45147 0.52421 0.43138 -0.04940 -0.01455 -0.03001 36  SER D OG  
3213 N N   . GLN D 33  ? 0.30958 0.39453 0.33097 -0.01938 -0.02674 -0.04356 37  GLN D N   
3214 C CA  . GLN D 33  ? 0.33657 0.42351 0.37243 -0.01081 -0.03154 -0.04741 37  GLN D CA  
3215 C C   . GLN D 33  ? 0.27621 0.34722 0.31547 -0.00863 -0.03252 -0.04207 37  GLN D C   
3216 O O   . GLN D 33  ? 0.46131 0.53396 0.50891 -0.00509 -0.03540 -0.04301 37  GLN D O   
3217 C CB  . GLN D 33  ? 0.22958 0.31940 0.27120 -0.00485 -0.03417 -0.05174 37  GLN D CB  
3218 C CG  . GLN D 33  ? 0.29579 0.38893 0.35350 0.00391  -0.04007 -0.05695 37  GLN D CG  
3219 C CD  . GLN D 33  ? 0.37605 0.47504 0.44024 0.00998  -0.04313 -0.06294 37  GLN D CD  
3220 O OE1 . GLN D 33  ? 0.36242 0.47121 0.41989 0.00824  -0.04119 -0.06556 37  GLN D OE1 
3221 N NE2 . GLN D 33  ? 0.33964 0.43273 0.41688 0.01701  -0.04805 -0.06504 37  GLN D NE2 
3222 N N   . SER D 34  ? 0.35288 0.40898 0.38553 -0.01049 -0.03041 -0.03657 38  SER D N   
3223 C CA  . SER D 34  ? 0.32243 0.36524 0.35864 -0.00828 -0.03104 -0.03184 38  SER D CA  
3224 C C   . SER D 34  ? 0.30067 0.33308 0.32506 -0.01388 -0.02749 -0.02605 38  SER D C   
3225 O O   . SER D 34  ? 0.32061 0.35101 0.33411 -0.01866 -0.02515 -0.02516 38  SER D O   
3226 C CB  . SER D 34  ? 0.42175 0.45754 0.46504 -0.00305 -0.03311 -0.03249 38  SER D CB  
3227 O OG  . SER D 34  ? 0.44471 0.48900 0.50069 0.00279  -0.03740 -0.03815 38  SER D OG  
3228 N N   . PHE D 35  ? 0.29283 0.31857 0.31928 -0.01312 -0.02751 -0.02211 39  PHE D N   
3229 C CA  . PHE D 35  ? 0.34666 0.36479 0.36331 -0.01754 -0.02490 -0.01766 39  PHE D CA  
3230 C C   . PHE D 35  ? 0.31888 0.32726 0.33866 -0.01470 -0.02504 -0.01356 39  PHE D C   
3231 O O   . PHE D 35  ? 0.36504 0.37434 0.39469 -0.01072 -0.02689 -0.01289 39  PHE D O   
3232 C CB  . PHE D 35  ? 0.29813 0.32398 0.31265 -0.02064 -0.02428 -0.01804 39  PHE D CB  
3233 C CG  . PHE D 35  ? 0.28400 0.32302 0.29785 -0.02334 -0.02414 -0.02292 39  PHE D CG  
3234 C CD1 . PHE D 35  ? 0.32486 0.36474 0.32831 -0.03018 -0.02152 -0.02285 39  PHE D CD1 
3235 C CD2 . PHE D 35  ? 0.33791 0.38876 0.36161 -0.01915 -0.02690 -0.02775 39  PHE D CD2 
3236 C CE1 . PHE D 35  ? 0.40747 0.46139 0.41028 -0.03355 -0.02079 -0.02714 39  PHE D CE1 
3237 C CE2 . PHE D 35  ? 0.42727 0.49296 0.45075 -0.02145 -0.02669 -0.03314 39  PHE D CE2 
3238 C CZ  . PHE D 35  ? 0.36135 0.42937 0.37436 -0.02902 -0.02319 -0.03265 39  PHE D CZ  
3239 N N   . PHE D 36  ? 0.23467 0.23391 0.24600 -0.01685 -0.02336 -0.01092 40  PHE D N   
3240 C CA  . PHE D 36  ? 0.27385 0.26572 0.28750 -0.01444 -0.02310 -0.00775 40  PHE D CA  
3241 C C   . PHE D 36  ? 0.33116 0.31757 0.33466 -0.01739 -0.02158 -0.00535 40  PHE D C   
3242 O O   . PHE D 36  ? 0.27876 0.26306 0.27272 -0.02132 -0.02111 -0.00622 40  PHE D O   
3243 C CB  . PHE D 36  ? 0.31721 0.30366 0.33370 -0.01154 -0.02382 -0.00924 40  PHE D CB  
3244 C CG  . PHE D 36  ? 0.30111 0.29288 0.32645 -0.00852 -0.02583 -0.01300 40  PHE D CG  
3245 C CD1 . PHE D 36  ? 0.26738 0.26247 0.28800 -0.00951 -0.02617 -0.01649 40  PHE D CD1 
3246 C CD2 . PHE D 36  ? 0.34795 0.34158 0.38627 -0.00474 -0.02765 -0.01306 40  PHE D CD2 
3247 C CE1 . PHE D 36  ? 0.34669 0.34848 0.37567 -0.00597 -0.02835 -0.02085 40  PHE D CE1 
3248 C CE2 . PHE D 36  ? 0.37714 0.37573 0.42445 -0.00132 -0.03037 -0.01749 40  PHE D CE2 
3249 C CZ  . PHE D 36  ? 0.28051 0.28400 0.32329 -0.00152 -0.03075 -0.02184 40  PHE D CZ  
3250 N N   . TRP D 37  ? 0.26951 0.25387 0.27530 -0.01557 -0.02102 -0.00235 41  TRP D N   
3251 C CA  . TRP D 37  ? 0.33646 0.31570 0.33399 -0.01671 -0.02021 -0.00106 41  TRP D CA  
3252 C C   . TRP D 37  ? 0.32240 0.29616 0.32148 -0.01390 -0.02027 -0.00118 41  TRP D C   
3253 O O   . TRP D 37  ? 0.31783 0.29357 0.32636 -0.01128 -0.02003 -0.00007 41  TRP D O   
3254 C CB  . TRP D 37  ? 0.20103 0.18479 0.19878 -0.01659 -0.01941 0.00181  41  TRP D CB  
3255 C CG  . TRP D 37  ? 0.25730 0.24576 0.25082 -0.01961 -0.01955 0.00073  41  TRP D CG  
3256 C CD1 . TRP D 37  ? 0.26695 0.26317 0.26552 -0.01931 -0.02005 0.00047  41  TRP D CD1 
3257 C CD2 . TRP D 37  ? 0.23607 0.22196 0.21999 -0.02337 -0.01961 -0.00084 41  TRP D CD2 
3258 N NE1 . TRP D 37  ? 0.30848 0.30859 0.30149 -0.02276 -0.01996 -0.00152 41  TRP D NE1 
3259 C CE2 . TRP D 37  ? 0.29326 0.28679 0.27746 -0.02571 -0.01959 -0.00207 41  TRP D CE2 
3260 C CE3 . TRP D 37  ? 0.29291 0.27042 0.26830 -0.02483 -0.02024 -0.00172 41  TRP D CE3 
3261 C CZ2 . TRP D 37  ? 0.26440 0.25788 0.24133 -0.03024 -0.01968 -0.00391 41  TRP D CZ2 
3262 C CZ3 . TRP D 37  ? 0.33732 0.31315 0.30506 -0.02911 -0.02088 -0.00320 41  TRP D CZ3 
3263 C CH2 . TRP D 37  ? 0.34921 0.33320 0.31809 -0.03216 -0.02034 -0.00416 41  TRP D CH2 
3264 N N   . TYR D 38  ? 0.30117 0.26789 0.29120 -0.01451 -0.02098 -0.00290 42  TYR D N   
3265 C CA  . TYR D 38  ? 0.30689 0.26902 0.29702 -0.01142 -0.02153 -0.00426 42  TYR D CA  
3266 C C   . TYR D 38  ? 0.35108 0.31143 0.33437 -0.01123 -0.02177 -0.00420 42  TYR D C   
3267 O O   . TYR D 38  ? 0.34631 0.30507 0.32203 -0.01386 -0.02239 -0.00411 42  TYR D O   
3268 C CB  . TYR D 38  ? 0.29303 0.24757 0.27801 -0.01070 -0.02347 -0.00760 42  TYR D CB  
3269 C CG  . TYR D 38  ? 0.31155 0.26861 0.30509 -0.00860 -0.02368 -0.00911 42  TYR D CG  
3270 C CD1 . TYR D 38  ? 0.26349 0.22570 0.26044 -0.01020 -0.02346 -0.00898 42  TYR D CD1 
3271 C CD2 . TYR D 38  ? 0.30719 0.26250 0.30587 -0.00463 -0.02448 -0.01165 42  TYR D CD2 
3272 C CE1 . TYR D 38  ? 0.30985 0.27508 0.31505 -0.00755 -0.02432 -0.01131 42  TYR D CE1 
3273 C CE2 . TYR D 38  ? 0.29927 0.25713 0.30650 -0.00232 -0.02516 -0.01382 42  TYR D CE2 
3274 C CZ  . TYR D 38  ? 0.38403 0.34664 0.39442 -0.00362 -0.02525 -0.01366 42  TYR D CZ  
3275 O OH  . TYR D 38  ? 0.28901 0.25490 0.30840 -0.00059 -0.02657 -0.01674 42  TYR D OH  
3276 N N   . ARG D 39  ? 0.28911 0.25072 0.27567 -0.00806 -0.02147 -0.00490 43  ARG D N   
3277 C CA  . ARG D 39  ? 0.42562 0.38785 0.40694 -0.00666 -0.02200 -0.00595 43  ARG D CA  
3278 C C   . ARG D 39  ? 0.46406 0.41975 0.44137 -0.00345 -0.02458 -0.01074 43  ARG D C   
3279 O O   . ARG D 39  ? 0.41449 0.37059 0.39803 -0.00124 -0.02436 -0.01229 43  ARG D O   
3280 C CB  . ARG D 39  ? 0.46198 0.43459 0.45073 -0.00556 -0.01916 -0.00270 43  ARG D CB  
3281 C CG  . ARG D 39  ? 0.55701 0.53355 0.54071 -0.00373 -0.01948 -0.00407 43  ARG D CG  
3282 C CD  . ARG D 39  ? 0.47787 0.46511 0.46915 -0.00236 -0.01643 -0.00145 43  ARG D CD  
3283 N NE  . ARG D 39  ? 0.66442 0.65531 0.65221 0.00083  -0.01742 -0.00578 43  ARG D NE  
3284 C CZ  . ARG D 39  ? 0.55812 0.55929 0.54489 0.00203  -0.01597 -0.00482 43  ARG D CZ  
3285 N NH1 . ARG D 39  ? 0.62189 0.63014 0.61062 0.00026  -0.01322 0.00117  43  ARG D NH1 
3286 N NH2 . ARG D 39  ? 0.60956 0.61457 0.59300 0.00560  -0.01766 -0.01035 43  ARG D NH2 
3287 N N   . GLN D 40  ? 0.39665 0.34609 0.36390 -0.00283 -0.02762 -0.01364 44  GLN D N   
3288 C CA  . GLN D 40  ? 0.43424 0.37618 0.39637 0.00101  -0.03128 -0.01884 44  GLN D CA  
3289 C C   . GLN D 40  ? 0.44207 0.38561 0.39936 0.00377  -0.03356 -0.02212 44  GLN D C   
3290 O O   . GLN D 40  ? 0.48944 0.42911 0.43954 0.00194  -0.03549 -0.02208 44  GLN D O   
3291 C CB  . GLN D 40  ? 0.43715 0.36529 0.38966 -0.00056 -0.03469 -0.01993 44  GLN D CB  
3292 C CG  . GLN D 40  ? 0.50079 0.41960 0.44736 0.00416  -0.03923 -0.02523 44  GLN D CG  
3293 C CD  . GLN D 40  ? 0.47822 0.38274 0.41425 0.00227  -0.04250 -0.02500 44  GLN D CD  
3294 O OE1 . GLN D 40  ? 0.41837 0.31835 0.34844 -0.00314 -0.04238 -0.02168 44  GLN D OE1 
3295 N NE2 . GLN D 40  ? 0.50183 0.39989 0.43545 0.00655  -0.04536 -0.02849 44  GLN D NE2 
3296 N N   . ASP D 41  ? 0.54878 0.49918 0.51066 0.00819  -0.03346 -0.02556 45  ASP D N   
3297 C CA  . ASP D 41  ? 0.54413 0.49716 0.50144 0.01212  -0.03647 -0.03050 45  ASP D CA  
3298 C C   . ASP D 41  ? 0.61793 0.55584 0.56465 0.01512  -0.04327 -0.03626 45  ASP D C   
3299 O O   . ASP D 41  ? 0.60859 0.53560 0.55221 0.01477  -0.04504 -0.03642 45  ASP D O   
3300 C CB  . ASP D 41  ? 0.54381 0.51109 0.50973 0.01565  -0.03400 -0.03286 45  ASP D CB  
3301 C CG  . ASP D 41  ? 0.63796 0.61898 0.61325 0.01236  -0.02770 -0.02624 45  ASP D CG  
3302 O OD1 . ASP D 41  ? 0.61749 0.59914 0.59099 0.00907  -0.02615 -0.02136 45  ASP D OD1 
3303 O OD2 . ASP D 41  ? 0.75368 0.74466 0.73808 0.01298  -0.02453 -0.02597 45  ASP D OD2 
3304 N N   . CYS D 42  ? 0.70892 0.64621 0.64979 0.01850  -0.04756 -0.04115 46  CYS D N   
3305 C CA  . CYS D 42  ? 0.70068 0.62155 0.63041 0.02141  -0.05529 -0.04647 46  CYS D CA  
3306 C C   . CYS D 42  ? 0.56452 0.48066 0.49419 0.02650  -0.05810 -0.05139 46  CYS D C   
3307 O O   . CYS D 42  ? 0.55119 0.48024 0.48895 0.03050  -0.05614 -0.05496 46  CYS D O   
3308 C CB  . CYS D 42  ? 0.81169 0.73522 0.73727 0.02543  -0.05993 -0.05218 46  CYS D CB  
3309 S SG  . CYS D 42  ? 0.88386 0.78387 0.79471 0.02721  -0.07050 -0.05716 46  CYS D SG  
3310 N N   . ARG D 43  ? 0.55446 0.45261 0.47494 0.02605  -0.06255 -0.05141 47  ARG D N   
3311 C CA  . ARG D 43  ? 0.73151 0.62164 0.64920 0.03118  -0.06644 -0.05603 47  ARG D CA  
3312 C C   . ARG D 43  ? 0.70024 0.60238 0.62990 0.03182  -0.06085 -0.05533 47  ARG D C   
3313 O O   . ARG D 43  ? 0.75565 0.65515 0.68546 0.03715  -0.06371 -0.06059 47  ARG D O   
3314 C CB  . ARG D 43  ? 0.79491 0.68247 0.70792 0.03949  -0.07390 -0.06564 47  ARG D CB  
3315 C CG  . ARG D 43  ? 0.95574 0.86362 0.87990 0.04475  -0.07143 -0.07161 47  ARG D CG  
3316 C CD  . ARG D 43  ? 0.98217 0.88777 0.90113 0.05375  -0.07978 -0.08253 47  ARG D CD  
3317 N NE  . ARG D 43  ? 0.93265 0.81816 0.84100 0.05803  -0.08754 -0.08624 47  ARG D NE  
3318 C CZ  . ARG D 43  ? 0.98337 0.84939 0.87829 0.06013  -0.09635 -0.08855 47  ARG D CZ  
3319 N NH1 . ARG D 43  ? 0.98008 0.84438 0.87139 0.05860  -0.09883 -0.08853 47  ARG D NH1 
3320 N NH2 . ARG D 43  ? 0.87762 0.72502 0.76241 0.06401  -0.10324 -0.09101 47  ARG D NH2 
3321 N N   . LYS D 44  ? 0.67976 0.59407 0.61945 0.02668  -0.05354 -0.04920 48  LYS D N   
3322 C CA  . LYS D 44  ? 0.56702 0.49176 0.51906 0.02663  -0.04865 -0.04818 48  LYS D CA  
3323 C C   . LYS D 44  ? 0.43959 0.35946 0.39256 0.02163  -0.04589 -0.04204 48  LYS D C   
3324 O O   . LYS D 44  ? 0.53046 0.43837 0.47339 0.01860  -0.04802 -0.03929 48  LYS D O   
3325 C CB  . LYS D 44  ? 0.60809 0.55144 0.57191 0.02541  -0.04308 -0.04650 48  LYS D CB  
3326 C CG  . LYS D 44  ? 0.67238 0.62467 0.63652 0.03056  -0.04518 -0.05324 48  LYS D CG  
3327 C CD  . LYS D 44  ? 0.70478 0.67555 0.68286 0.03071  -0.03986 -0.05370 48  LYS D CD  
3328 C CE  . LYS D 44  ? 0.78151 0.76534 0.76031 0.03501  -0.04093 -0.05996 48  LYS D CE  
3329 N NZ  . LYS D 44  ? 0.87771 0.88077 0.87011 0.03374  -0.03501 -0.05951 48  LYS D NZ  
3330 N N   . GLU D 45  ? 0.51043 0.44039 0.47606 0.02057  -0.04125 -0.04010 49  GLU D N   
3331 C CA  . GLU D 45  ? 0.40494 0.33187 0.37272 0.01744  -0.03949 -0.03621 49  GLU D CA  
3332 C C   . GLU D 45  ? 0.39857 0.33241 0.37174 0.01163  -0.03486 -0.02942 49  GLU D C   
3333 O O   . GLU D 45  ? 0.48619 0.42950 0.46500 0.01041  -0.03199 -0.02730 49  GLU D O   
3334 C CB  . GLU D 45  ? 0.42256 0.35484 0.40128 0.02062  -0.03857 -0.03936 49  GLU D CB  
3335 C CG  . GLU D 45  ? 0.44404 0.39007 0.43853 0.01831  -0.03343 -0.03645 49  GLU D CG  
3336 C CD  . GLU D 45  ? 0.47375 0.42991 0.47486 0.02054  -0.03225 -0.03969 49  GLU D CD  
3337 O OE1 . GLU D 45  ? 0.51661 0.47083 0.50955 0.02345  -0.03507 -0.04357 49  GLU D OE1 
3338 O OE2 . GLU D 45  ? 0.55258 0.51896 0.56725 0.01929  -0.02873 -0.03856 49  GLU D OE2 
3339 N N   . PRO D 46  ? 0.43201 0.36215 0.40334 0.00825  -0.03420 -0.02612 50  PRO D N   
3340 C CA  . PRO D 46  ? 0.42954 0.36680 0.40651 0.00357  -0.03047 -0.02072 50  PRO D CA  
3341 C C   . PRO D 46  ? 0.37389 0.32143 0.36603 0.00421  -0.02738 -0.01951 50  PRO D C   
3342 O O   . PRO D 46  ? 0.30451 0.25287 0.30337 0.00717  -0.02796 -0.02262 50  PRO D O   
3343 C CB  . PRO D 46  ? 0.43713 0.36857 0.40790 0.00054  -0.03125 -0.01919 50  PRO D CB  
3344 C CG  . PRO D 46  ? 0.46912 0.38845 0.42830 0.00283  -0.03542 -0.02251 50  PRO D CG  
3345 C CD  . PRO D 46  ? 0.40643 0.32658 0.36983 0.00878  -0.03704 -0.02741 50  PRO D CD  
3346 N N   . LYS D 47  ? 0.37353 0.32843 0.37101 0.00139  -0.02444 -0.01495 51  LYS D N   
3347 C CA  . LYS D 47  ? 0.43202 0.39498 0.44332 0.00108  -0.02191 -0.01244 51  LYS D CA  
3348 C C   . LYS D 47  ? 0.38308 0.34869 0.39685 -0.00208 -0.02074 -0.00795 51  LYS D C   
3349 O O   . LYS D 47  ? 0.34860 0.31473 0.35579 -0.00434 -0.02022 -0.00547 51  LYS D O   
3350 C CB  . LYS D 47  ? 0.31900 0.28949 0.33519 0.00144  -0.01965 -0.01105 51  LYS D CB  
3351 C CG  . LYS D 47  ? 0.62019 0.59064 0.63516 0.00509  -0.02097 -0.01673 51  LYS D CG  
3352 C CD  . LYS D 47  ? 0.53274 0.51384 0.55354 0.00495  -0.01813 -0.01550 51  LYS D CD  
3353 C CE  . LYS D 47  ? 0.69524 0.67842 0.71524 0.00905  -0.01974 -0.02252 51  LYS D CE  
3354 N NZ  . LYS D 47  ? 0.72867 0.72505 0.75823 0.00818  -0.01616 -0.02158 51  LYS D NZ  
3355 N N   . LEU D 48  ? 0.29380 0.26148 0.31746 -0.00174 -0.02086 -0.00775 52  LEU D N   
3356 C CA  . LEU D 48  ? 0.32776 0.29866 0.35499 -0.00371 -0.02060 -0.00458 52  LEU D CA  
3357 C C   . LEU D 48  ? 0.34161 0.31728 0.37148 -0.00527 -0.01859 0.00077  52  LEU D C   
3358 O O   . LEU D 48  ? 0.38888 0.36742 0.42630 -0.00494 -0.01723 0.00295  52  LEU D O   
3359 C CB  . LEU D 48  ? 0.32837 0.30083 0.36722 -0.00198 -0.02202 -0.00633 52  LEU D CB  
3360 C CG  . LEU D 48  ? 0.43524 0.41157 0.48002 -0.00277 -0.02285 -0.00421 52  LEU D CG  
3361 C CD1 . LEU D 48  ? 0.40535 0.38257 0.44071 -0.00451 -0.02332 -0.00531 52  LEU D CD1 
3362 C CD2 . LEU D 48  ? 0.28679 0.26438 0.34453 -0.00015 -0.02517 -0.00697 52  LEU D CD2 
3363 N N   . LEU D 49  ? 0.39349 0.37050 0.41682 -0.00716 -0.01834 0.00288  53  LEU D N   
3364 C CA  . LEU D 49  ? 0.32223 0.30397 0.34639 -0.00808 -0.01683 0.00792  53  LEU D CA  
3365 C C   . LEU D 49  ? 0.43640 0.42060 0.46853 -0.00808 -0.01781 0.01068  53  LEU D C   
3366 O O   . LEU D 49  ? 0.41404 0.39985 0.45374 -0.00785 -0.01727 0.01495  53  LEU D O   
3367 C CB  . LEU D 49  ? 0.35354 0.33574 0.36634 -0.00942 -0.01661 0.00776  53  LEU D CB  
3368 C CG  . LEU D 49  ? 0.44168 0.42949 0.45286 -0.00951 -0.01508 0.01212  53  LEU D CG  
3369 C CD1 . LEU D 49  ? 0.47148 0.46209 0.48437 -0.00841 -0.01323 0.01358  53  LEU D CD1 
3370 C CD2 . LEU D 49  ? 0.38661 0.37489 0.38768 -0.01058 -0.01565 0.01052  53  LEU D CD2 
3371 N N   . MET D 50  ? 0.36453 0.34921 0.39514 -0.00837 -0.01955 0.00818  54  MET D N   
3372 C CA  . MET D 50  ? 0.35736 0.34468 0.39595 -0.00730 -0.02157 0.00920  54  MET D CA  
3373 C C   . MET D 50  ? 0.50957 0.49903 0.54719 -0.00725 -0.02348 0.00410  54  MET D C   
3374 O O   . MET D 50  ? 0.29004 0.27929 0.31872 -0.00927 -0.02269 0.00142  54  MET D O   
3375 C CB  . MET D 50  ? 0.57076 0.56134 0.60738 -0.00751 -0.02134 0.01379  54  MET D CB  
3376 C CG  . MET D 50  ? 0.44693 0.44034 0.47273 -0.00913 -0.02043 0.01260  54  MET D CG  
3377 S SD  . MET D 50  ? 0.73040 0.72715 0.75228 -0.00867 -0.01901 0.01854  54  MET D SD  
3378 C CE  . MET D 50  ? 0.38748 0.38477 0.41868 -0.00635 -0.02165 0.02272  54  MET D CE  
3379 N N   . SER D 51  ? 0.35554 0.34728 0.40260 -0.00503 -0.02627 0.00277  55  SER D N   
3380 C CA  . SER D 51  ? 0.46080 0.45810 0.50809 -0.00452 -0.02833 -0.00221 55  SER D CA  
3381 C C   . SER D 51  ? 0.42688 0.42963 0.47038 -0.00530 -0.02874 -0.00144 55  SER D C   
3382 O O   . SER D 51  ? 0.52866 0.53035 0.57226 -0.00481 -0.02863 0.00316  55  SER D O   
3383 C CB  . SER D 51  ? 0.53864 0.53725 0.59838 -0.00078 -0.03206 -0.00524 55  SER D CB  
3384 O OG  . SER D 51  ? 0.78805 0.78185 0.85264 0.00027  -0.03183 -0.00598 55  SER D OG  
3385 N N   . VAL D 52  ? 0.36434 0.37384 0.40429 -0.00660 -0.02917 -0.00613 56  VAL D N   
3386 C CA  . VAL D 52  ? 0.42558 0.44190 0.46141 -0.00785 -0.02932 -0.00695 56  VAL D CA  
3387 C C   . VAL D 52  ? 0.46284 0.48778 0.50644 -0.00466 -0.03315 -0.01183 56  VAL D C   
3388 O O   . VAL D 52  ? 0.59809 0.62761 0.64490 -0.00405 -0.03423 -0.01677 56  VAL D O   
3389 C CB  . VAL D 52  ? 0.39633 0.41467 0.42135 -0.01304 -0.02650 -0.00878 56  VAL D CB  
3390 C CG1 . VAL D 52  ? 0.30965 0.33594 0.33161 -0.01453 -0.02665 -0.01027 56  VAL D CG1 
3391 C CG2 . VAL D 52  ? 0.27497 0.28408 0.29267 -0.01515 -0.02394 -0.00508 56  VAL D CG2 
3392 N N   . TYR D 53  ? 0.53032 0.55806 0.57663 -0.00207 -0.03560 -0.01089 57  TYR D N   
3393 C CA  . TYR D 53  ? 0.57848 0.61448 0.63226 0.00201  -0.04030 -0.01625 57  TYR D CA  
3394 C C   . TYR D 53  ? 0.57943 0.62413 0.62879 0.00157  -0.04072 -0.01846 57  TYR D C   
3395 O O   . TYR D 53  ? 0.51601 0.55834 0.55815 -0.00074 -0.03816 -0.01455 57  TYR D O   
3396 C CB  . TYR D 53  ? 0.57031 0.59967 0.63406 0.00736  -0.04500 -0.01362 57  TYR D CB  
3397 C CG  . TYR D 53  ? 0.75370 0.77450 0.82329 0.00767  -0.04472 -0.01147 57  TYR D CG  
3398 C CD1 . TYR D 53  ? 0.68755 0.71203 0.76235 0.00889  -0.04599 -0.01745 57  TYR D CD1 
3399 C CD2 . TYR D 53  ? 0.68499 0.69541 0.75515 0.00685  -0.04320 -0.00387 57  TYR D CD2 
3400 C CE1 . TYR D 53  ? 0.84374 0.86107 0.92450 0.00964  -0.04606 -0.01636 57  TYR D CE1 
3401 C CE2 . TYR D 53  ? 0.66398 0.66786 0.74045 0.00691  -0.04292 -0.00267 57  TYR D CE2 
3402 C CZ  . TYR D 53  ? 0.88608 0.89308 0.96804 0.00850  -0.04453 -0.00915 57  TYR D CZ  
3403 O OH  . TYR D 53  ? 1.03951 1.04062 1.12830 0.00900  -0.04455 -0.00881 57  TYR D OH  
3404 N N   . SER D 54  ? 0.56327 0.61936 0.61754 0.00427  -0.04430 -0.02569 58  SER D N   
3405 C CA  . SER D 54  ? 0.43561 0.50177 0.48719 0.00460  -0.04538 -0.02924 58  SER D CA  
3406 C C   . SER D 54  ? 0.57308 0.63327 0.62553 0.00934  -0.04872 -0.02475 58  SER D C   
3407 O O   . SER D 54  ? 0.59624 0.65976 0.64284 0.00853  -0.04773 -0.02413 58  SER D O   
3408 C CB  . SER D 54  ? 0.40164 0.48318 0.45917 0.00704  -0.04885 -0.03902 58  SER D CB  
3409 O OG  . SER D 54  ? 0.75612 0.84562 0.81037 0.00147  -0.04490 -0.04275 58  SER D OG  
3410 N N   . SER D 55  ? 0.63901 0.69014 0.69850 0.01414  -0.05284 -0.02141 63  SER D N   
3411 C CA  . SER D 55  ? 0.50356 0.54773 0.56302 0.01838  -0.05631 -0.01595 63  SER D CA  
3412 C C   . SER D 55  ? 0.69402 0.73104 0.74475 0.01487  -0.05132 -0.00738 63  SER D C   
3413 O O   . SER D 55  ? 0.75683 0.79263 0.80355 0.01730  -0.05273 -0.00376 63  SER D O   
3414 C CB  . SER D 55  ? 0.51970 0.55385 0.58862 0.02296  -0.06165 -0.01326 63  SER D CB  
3415 O OG  . SER D 55  ? 0.76576 0.78957 0.83559 0.01953  -0.05797 -0.00683 63  SER D OG  
3416 N N   . GLY D 56  ? 0.64270 0.67558 0.69011 0.00978  -0.04592 -0.00453 64  GLY D N   
3417 C CA  . GLY D 56  ? 0.61404 0.64166 0.65365 0.00693  -0.04153 0.00235  64  GLY D CA  
3418 C C   . GLY D 56  ? 0.65030 0.66699 0.69288 0.00684  -0.04056 0.01002  64  GLY D C   
3419 O O   . GLY D 56  ? 0.83693 0.84845 0.88082 0.00949  -0.04272 0.01608  64  GLY D O   
3420 N N   . ASN D 57  ? 0.67104 0.68439 0.71452 0.00363  -0.03740 0.00982  65  ASN D N   
3421 C CA  . ASN D 57  ? 0.65720 0.66193 0.70436 0.00293  -0.03600 0.01591  65  ASN D CA  
3422 C C   . ASN D 57  ? 0.53408 0.53723 0.57369 0.00125  -0.03231 0.02261  65  ASN D C   
3423 O O   . ASN D 57  ? 0.53022 0.53651 0.56188 -0.00115 -0.02898 0.02108  65  ASN D O   
3424 C CB  . ASN D 57  ? 0.51324 0.51630 0.56269 0.00063  -0.03391 0.01245  65  ASN D CB  
3425 C CG  . ASN D 57  ? 0.76501 0.76080 0.81918 -0.00021 -0.03236 0.01740  65  ASN D CG  
3426 O OD1 . ASN D 57  ? 0.91571 0.90720 0.97448 0.00080  -0.03373 0.02323  65  ASN D OD1 
3427 N ND2 . ASN D 57  ? 0.67375 0.66816 0.72668 -0.00225 -0.02964 0.01510  65  ASN D ND2 
3428 N N   . GLU D 58  ? 0.51937 0.51783 0.56138 0.00246  -0.03316 0.02999  67  GLU D N   
3429 C CA  . GLU D 58  ? 0.66457 0.66340 0.69965 0.00122  -0.02968 0.03677  67  GLU D CA  
3430 C C   . GLU D 58  ? 0.65718 0.65060 0.69743 -0.00096 -0.02756 0.04279  67  GLU D C   
3431 O O   . GLU D 58  ? 0.86040 0.84787 0.90859 -0.00030 -0.03039 0.04659  67  GLU D O   
3432 C CB  . GLU D 58  ? 0.57756 0.57777 0.60853 0.00431  -0.03217 0.04112  67  GLU D CB  
3433 C CG  . GLU D 58  ? 0.69784 0.70051 0.72080 0.00346  -0.02848 0.04793  67  GLU D CG  
3434 C CD  . GLU D 58  ? 0.91558 0.91868 0.93413 0.00698  -0.03125 0.05336  67  GLU D CD  
3435 O OE1 . GLU D 58  ? 0.89256 0.89133 0.91564 0.01001  -0.03651 0.05328  67  GLU D OE1 
3436 O OE2 . GLU D 58  ? 1.01501 1.02298 1.02530 0.00728  -0.02862 0.05734  67  GLU D OE2 
3437 N N   . ASP D 59  ? 0.49359 0.48929 0.52971 -0.00353 -0.02296 0.04327  68  ASP D N   
3438 C CA  . ASP D 59  ? 0.53431 0.52767 0.57509 -0.00602 -0.02019 0.04793  68  ASP D CA  
3439 C C   . ASP D 59  ? 0.47644 0.47601 0.50862 -0.00712 -0.01593 0.05157  68  ASP D C   
3440 O O   . ASP D 59  ? 0.53601 0.53921 0.56308 -0.00762 -0.01365 0.04688  68  ASP D O   
3441 C CB  . ASP D 59  ? 0.62934 0.62043 0.67594 -0.00717 -0.01965 0.04193  68  ASP D CB  
3442 C CG  . ASP D 59  ? 0.87521 0.86509 0.92806 -0.00966 -0.01700 0.04544  68  ASP D CG  
3443 O OD1 . ASP D 59  ? 0.84817 0.83554 0.90640 -0.01094 -0.01734 0.05253  68  ASP D OD1 
3444 O OD2 . ASP D 59  ? 0.92751 0.91885 0.97994 -0.01045 -0.01484 0.04099  68  ASP D OD2 
3445 N N   . GLY D 60  ? 0.52587 0.52667 0.55608 -0.00720 -0.01532 0.05985  74  GLY D N   
3446 C CA  . GLY D 60  ? 0.43961 0.44837 0.46193 -0.00784 -0.01130 0.06352  74  GLY D CA  
3447 C C   . GLY D 60  ? 0.53400 0.54873 0.54625 -0.00512 -0.01161 0.05894  74  GLY D C   
3448 O O   . GLY D 60  ? 0.50861 0.52285 0.51802 -0.00257 -0.01467 0.05840  74  GLY D O   
3449 N N   . ARG D 61  ? 0.51978 0.54032 0.52705 -0.00543 -0.00895 0.05483  75  ARG D N   
3450 C CA  . ARG D 61  ? 0.46590 0.49161 0.46443 -0.00321 -0.00957 0.04968  75  ARG D CA  
3451 C C   . ARG D 61  ? 0.47800 0.49918 0.47685 -0.00342 -0.01207 0.04151  75  ARG D C   
3452 O O   . ARG D 61  ? 0.51352 0.53800 0.50597 -0.00247 -0.01287 0.03673  75  ARG D O   
3453 C CB  . ARG D 61  ? 0.43835 0.47164 0.43168 -0.00303 -0.00669 0.04788  75  ARG D CB  
3454 C CG  . ARG D 61  ? 0.49306 0.53451 0.48450 -0.00295 -0.00363 0.05575  75  ARG D CG  
3455 C CD  . ARG D 61  ? 0.41984 0.47153 0.40602 -0.00180 -0.00129 0.05239  75  ARG D CD  
3456 N NE  . ARG D 61  ? 0.42654 0.47574 0.41697 -0.00330 -0.00062 0.04685  75  ARG D NE  
3457 C CZ  . ARG D 61  ? 0.44703 0.49305 0.43474 -0.00213 -0.00272 0.03816  75  ARG D CZ  
3458 N NH1 . ARG D 61  ? 0.38986 0.43559 0.37122 -0.00015 -0.00526 0.03380  75  ARG D NH1 
3459 N NH2 . ARG D 61  ? 0.39376 0.43635 0.38518 -0.00306 -0.00257 0.03374  75  ARG D NH2 
3460 N N   . PHE D 62  ? 0.42875 0.44314 0.43491 -0.00481 -0.01337 0.03977  76  PHE D N   
3461 C CA  . PHE D 62  ? 0.47666 0.48778 0.48282 -0.00567 -0.01507 0.03244  76  PHE D CA  
3462 C C   . PHE D 62  ? 0.40404 0.41377 0.41441 -0.00472 -0.01825 0.03142  76  PHE D C   
3463 O O   . PHE D 62  ? 0.43902 0.44578 0.45623 -0.00378 -0.01975 0.03531  76  PHE D O   
3464 C CB  . PHE D 62  ? 0.40921 0.41532 0.41963 -0.00735 -0.01424 0.02963  76  PHE D CB  
3465 C CG  . PHE D 62  ? 0.43921 0.44710 0.44534 -0.00763 -0.01198 0.02851  76  PHE D CG  
3466 C CD1 . PHE D 62  ? 0.48164 0.49318 0.49021 -0.00755 -0.00955 0.03327  76  PHE D CD1 
3467 C CD2 . PHE D 62  ? 0.44595 0.45217 0.44553 -0.00803 -0.01261 0.02252  76  PHE D CD2 
3468 C CE1 . PHE D 62  ? 0.55875 0.57405 0.56375 -0.00717 -0.00780 0.03105  76  PHE D CE1 
3469 C CE2 . PHE D 62  ? 0.46961 0.47727 0.46531 -0.00732 -0.01161 0.02051  76  PHE D CE2 
3470 C CZ  . PHE D 62  ? 0.52606 0.53919 0.52467 -0.00653 -0.00921 0.02426  76  PHE D CZ  
3471 N N   . THR D 63  ? 0.41369 0.42591 0.42024 -0.00504 -0.01958 0.02578  77  THR D N   
3472 C CA  . THR D 63  ? 0.40821 0.42167 0.41866 -0.00408 -0.02266 0.02273  77  THR D CA  
3473 C C   . THR D 63  ? 0.46273 0.47666 0.47187 -0.00692 -0.02267 0.01572  77  THR D C   
3474 O O   . THR D 63  ? 0.49739 0.51302 0.49964 -0.00910 -0.02149 0.01277  77  THR D O   
3475 C CB  . THR D 63  ? 0.46004 0.47939 0.46689 -0.00145 -0.02447 0.02317  77  THR D CB  
3476 O OG1 . THR D 63  ? 0.55082 0.56883 0.55839 0.00122  -0.02488 0.03069  77  THR D OG1 
3477 C CG2 . THR D 63  ? 0.36098 0.38351 0.37196 -0.00024 -0.02794 0.01810  77  THR D CG2 
3478 N N   . ALA D 64  ? 0.44459 0.45705 0.46023 -0.00696 -0.02424 0.01314  78  ALA D N   
3479 C CA  . ALA D 64  ? 0.37872 0.39291 0.39307 -0.00978 -0.02423 0.00705  78  ALA D CA  
3480 C C   . ALA D 64  ? 0.42010 0.44104 0.43948 -0.00820 -0.02721 0.00302  78  ALA D C   
3481 O O   . ALA D 64  ? 0.44661 0.46704 0.47334 -0.00448 -0.03003 0.00438  78  ALA D O   
3482 C CB  . ALA D 64  ? 0.32662 0.33484 0.34347 -0.01087 -0.02336 0.00636  78  ALA D CB  
3483 N N   . GLN D 65  ? 0.40634 0.43389 0.42198 -0.01109 -0.02692 -0.00222 79  GLN D N   
3484 C CA  . GLN D 65  ? 0.38964 0.42659 0.40983 -0.00964 -0.02965 -0.00741 79  GLN D CA  
3485 C C   . GLN D 65  ? 0.39246 0.43521 0.41029 -0.01452 -0.02821 -0.01303 79  GLN D C   
3486 O O   . GLN D 65  ? 0.36022 0.39966 0.37081 -0.01953 -0.02538 -0.01265 79  GLN D O   
3487 C CB  . GLN D 65  ? 0.37927 0.42274 0.39762 -0.00750 -0.03121 -0.00813 79  GLN D CB  
3488 C CG  . GLN D 65  ? 0.55766 0.60948 0.58277 -0.00320 -0.03560 -0.01277 79  GLN D CG  
3489 C CD  . GLN D 65  ? 0.64155 0.69611 0.66559 0.00138  -0.03834 -0.01152 79  GLN D CD  
3490 O OE1 . GLN D 65  ? 0.73120 0.78148 0.74973 0.00159  -0.03675 -0.00637 79  GLN D OE1 
3491 N NE2 . GLN D 65  ? 0.55067 0.61308 0.57973 0.00564  -0.04285 -0.01669 79  GLN D NE2 
3492 N N   . LEU D 66  ? 0.39413 0.44560 0.41804 -0.01293 -0.03053 -0.01823 80  LEU D N   
3493 C CA  . LEU D 66  ? 0.40210 0.46191 0.42469 -0.01735 -0.02922 -0.02366 80  LEU D CA  
3494 C C   . LEU D 66  ? 0.42822 0.50318 0.45340 -0.01705 -0.03098 -0.03012 80  LEU D C   
3495 O O   . LEU D 66  ? 0.42839 0.50767 0.46017 -0.01093 -0.03504 -0.03216 80  LEU D O   
3496 C CB  . LEU D 66  ? 0.36608 0.42536 0.39446 -0.01514 -0.03047 -0.02535 80  LEU D CB  
3497 C CG  . LEU D 66  ? 0.45505 0.52694 0.48410 -0.01784 -0.03011 -0.03186 80  LEU D CG  
3498 C CD1 . LEU D 66  ? 0.39565 0.46482 0.41459 -0.02572 -0.02574 -0.03040 80  LEU D CD1 
3499 C CD2 . LEU D 66  ? 0.49096 0.56445 0.52848 -0.01270 -0.03307 -0.03469 80  LEU D CD2 
3500 N N   . ASN D 67  ? 0.39369 0.47658 0.41375 -0.02375 -0.02824 -0.03350 81  ASN D N   
3501 C CA  . ASN D 67  ? 0.47895 0.57912 0.50193 -0.02460 -0.02932 -0.04093 81  ASN D CA  
3502 C C   . ASN D 67  ? 0.41093 0.52093 0.43274 -0.03062 -0.02687 -0.04505 81  ASN D C   
3503 O O   . ASN D 67  ? 0.35752 0.46617 0.37182 -0.03889 -0.02303 -0.04363 81  ASN D O   
3504 C CB  . ASN D 67  ? 0.21965 0.32259 0.23801 -0.02773 -0.02816 -0.04142 81  ASN D CB  
3505 C CG  . ASN D 67  ? 0.46567 0.58709 0.48870 -0.02672 -0.03018 -0.04975 81  ASN D CG  
3506 O OD1 . ASN D 67  ? 0.47692 0.61150 0.50484 -0.02671 -0.03106 -0.05589 81  ASN D OD1 
3507 N ND2 . ASN D 67  ? 0.49082 0.61460 0.51251 -0.02537 -0.03117 -0.05072 81  ASN D ND2 
3508 N N   . ARG D 68  ? 0.39911 0.51920 0.42818 -0.02647 -0.02942 -0.05021 82  ARG D N   
3509 C CA  . ARG D 68  ? 0.39440 0.52548 0.42220 -0.03154 -0.02706 -0.05401 82  ARG D CA  
3510 C C   . ARG D 68  ? 0.52349 0.67240 0.54946 -0.03847 -0.02471 -0.05974 82  ARG D C   
3511 O O   . ARG D 68  ? 0.51110 0.66717 0.53258 -0.04590 -0.02111 -0.06062 82  ARG D O   
3512 C CB  . ARG D 68  ? 0.30682 0.44589 0.34373 -0.02426 -0.03101 -0.05917 82  ARG D CB  
3513 C CG  . ARG D 68  ? 0.43496 0.55780 0.47413 -0.01912 -0.03271 -0.05411 82  ARG D CG  
3514 C CD  . ARG D 68  ? 0.50619 0.63843 0.55391 -0.01330 -0.03630 -0.06024 82  ARG D CD  
3515 N NE  . ARG D 68  ? 0.38743 0.50535 0.43715 -0.00975 -0.03729 -0.05604 82  ARG D NE  
3516 C CZ  . ARG D 68  ? 0.43343 0.54603 0.47705 -0.01355 -0.03395 -0.05321 82  ARG D CZ  
3517 N NH1 . ARG D 68  ? 0.38253 0.50116 0.41672 -0.02159 -0.02935 -0.05294 82  ARG D NH1 
3518 N NH2 . ARG D 68  ? 0.32698 0.42773 0.37397 -0.00931 -0.03550 -0.05058 82  ARG D NH2 
3519 N N   . ALA D 69  ? 0.51525 0.67188 0.54444 -0.03637 -0.02666 -0.06362 83  ALA D N   
3520 C CA  . ALA D 69  ? 0.50423 0.67972 0.53319 -0.04289 -0.02460 -0.07020 83  ALA D CA  
3521 C C   . ALA D 69  ? 0.41829 0.58654 0.43775 -0.05393 -0.01953 -0.06534 83  ALA D C   
3522 O O   . ALA D 69  ? 0.57917 0.75846 0.59555 -0.06324 -0.01582 -0.06758 83  ALA D O   
3523 C CB  . ALA D 69  ? 0.55273 0.73788 0.58790 -0.03649 -0.02880 -0.07627 83  ALA D CB  
3524 N N   . SER D 70  ? 0.36169 0.51182 0.37653 -0.05316 -0.01960 -0.05882 84  SER D N   
3525 C CA  . SER D 70  ? 0.40608 0.54594 0.41204 -0.06239 -0.01604 -0.05408 84  SER D CA  
3526 C C   . SER D 70  ? 0.33783 0.46040 0.33651 -0.06514 -0.01419 -0.04670 84  SER D C   
3527 O O   . SER D 70  ? 0.33743 0.45008 0.32797 -0.07297 -0.01185 -0.04274 84  SER D O   
3528 C CB  . SER D 70  ? 0.29691 0.42794 0.30162 -0.05947 -0.01760 -0.05211 84  SER D CB  
3529 O OG  . SER D 70  ? 0.51184 0.62942 0.51757 -0.05054 -0.02015 -0.04721 84  SER D OG  
3530 N N   . GLN D 71  ? 0.35561 0.47418 0.35730 -0.05861 -0.01575 -0.04530 85  GLN D N   
3531 C CA  . GLN D 71  ? 0.44763 0.55028 0.44329 -0.05943 -0.01467 -0.03915 85  GLN D CA  
3532 C C   . GLN D 71  ? 0.34775 0.43096 0.33740 -0.05939 -0.01476 -0.03295 85  GLN D C   
3533 O O   . GLN D 71  ? 0.38378 0.45487 0.36466 -0.06505 -0.01314 -0.02877 85  GLN D O   
3534 C CB  . GLN D 71  ? 0.27263 0.37988 0.26167 -0.06846 -0.01135 -0.03898 85  GLN D CB  
3535 C CG  . GLN D 71  ? 0.39307 0.52129 0.38868 -0.06687 -0.01149 -0.04559 85  GLN D CG  
3536 C CD  . GLN D 71  ? 0.41884 0.55414 0.40763 -0.07545 -0.00792 -0.04517 85  GLN D CD  
3537 O OE1 . GLN D 71  ? 0.47214 0.62827 0.46528 -0.07627 -0.00725 -0.05126 85  GLN D OE1 
3538 N NE2 . GLN D 71  ? 0.42431 0.54275 0.40211 -0.08146 -0.00595 -0.03812 85  GLN D NE2 
3539 N N   . TYR D 72  ? 0.34550 0.42613 0.33978 -0.05241 -0.01711 -0.03255 86  TYR D N   
3540 C CA  . TYR D 72  ? 0.35164 0.41744 0.34176 -0.05063 -0.01755 -0.02764 86  TYR D CA  
3541 C C   . TYR D 72  ? 0.32561 0.38271 0.31975 -0.04246 -0.01933 -0.02408 86  TYR D C   
3542 O O   . TYR D 72  ? 0.30230 0.36589 0.30443 -0.03655 -0.02141 -0.02599 86  TYR D O   
3543 C CB  . TYR D 72  ? 0.36690 0.43822 0.35828 -0.04969 -0.01851 -0.02976 86  TYR D CB  
3544 C CG  . TYR D 72  ? 0.44165 0.51033 0.42623 -0.05759 -0.01703 -0.03009 86  TYR D CG  
3545 C CD1 . TYR D 72  ? 0.43215 0.48657 0.41076 -0.05769 -0.01739 -0.02616 86  TYR D CD1 
3546 C CD2 . TYR D 72  ? 0.44457 0.52560 0.42929 -0.06502 -0.01558 -0.03482 86  TYR D CD2 
3547 C CE1 . TYR D 72  ? 0.46014 0.51105 0.43319 -0.06457 -0.01701 -0.02699 86  TYR D CE1 
3548 C CE2 . TYR D 72  ? 0.43315 0.51085 0.41246 -0.07289 -0.01460 -0.03510 86  TYR D CE2 
3549 C CZ  . TYR D 72  ? 0.47577 0.53759 0.44931 -0.07244 -0.01565 -0.03120 86  TYR D CZ  
3550 O OH  . TYR D 72  ? 0.64736 0.70487 0.61610 -0.08002 -0.01560 -0.03200 86  TYR D OH  
3551 N N   . ILE D 73  ? 0.34509 0.38762 0.33401 -0.04225 -0.01884 -0.01929 87  ILE D N   
3552 C CA  . ILE D 73  ? 0.37007 0.40429 0.36240 -0.03557 -0.02001 -0.01553 87  ILE D CA  
3553 C C   . ILE D 73  ? 0.37692 0.40485 0.36532 -0.03449 -0.02002 -0.01264 87  ILE D C   
3554 O O   . ILE D 73  ? 0.40065 0.42407 0.38183 -0.03908 -0.01929 -0.01272 87  ILE D O   
3555 C CB  . ILE D 73  ? 0.43390 0.45849 0.42420 -0.03554 -0.01951 -0.01349 87  ILE D CB  
3556 C CG1 . ILE D 73  ? 0.48880 0.52098 0.48142 -0.03712 -0.01936 -0.01686 87  ILE D CG1 
3557 C CG2 . ILE D 73  ? 0.39242 0.41085 0.38829 -0.02909 -0.02060 -0.01040 87  ILE D CG2 
3558 C CD1 . ILE D 73  ? 0.55436 0.57754 0.54146 -0.03887 -0.01862 -0.01538 87  ILE D CD1 
3559 N N   . SER D 74  ? 0.29672 0.32446 0.28970 -0.02848 -0.02113 -0.01010 88  SER D N   
3560 C CA  . SER D 74  ? 0.29008 0.31436 0.27946 -0.02670 -0.02105 -0.00744 88  SER D CA  
3561 C C   . SER D 74  ? 0.33664 0.35416 0.32844 -0.02214 -0.02095 -0.00262 88  SER D C   
3562 O O   . SER D 74  ? 0.32251 0.33966 0.32096 -0.01929 -0.02161 -0.00127 88  SER D O   
3563 C CB  . SER D 74  ? 0.30994 0.34368 0.30112 -0.02433 -0.02228 -0.00894 88  SER D CB  
3564 O OG  . SER D 74  ? 0.50265 0.53889 0.50039 -0.01861 -0.02393 -0.00679 88  SER D OG  
3565 N N   . LEU D 75  ? 0.32615 0.33901 0.31292 -0.02164 -0.02030 -0.00057 89  LEU D N   
3566 C CA  . LEU D 75  ? 0.34762 0.35695 0.33623 -0.01777 -0.01972 0.00386  89  LEU D CA  
3567 C C   . LEU D 75  ? 0.36667 0.38006 0.35169 -0.01556 -0.01966 0.00540  89  LEU D C   
3568 O O   . LEU D 75  ? 0.41125 0.42475 0.39022 -0.01736 -0.01998 0.00260  89  LEU D O   
3569 C CB  . LEU D 75  ? 0.37285 0.37361 0.35860 -0.01873 -0.01904 0.00388  89  LEU D CB  
3570 C CG  . LEU D 75  ? 0.35817 0.35728 0.34576 -0.01534 -0.01808 0.00754  89  LEU D CG  
3571 C CD1 . LEU D 75  ? 0.35017 0.35055 0.34682 -0.01308 -0.01784 0.01101  89  LEU D CD1 
3572 C CD2 . LEU D 75  ? 0.27102 0.26270 0.25474 -0.01583 -0.01809 0.00576  89  LEU D CD2 
3573 N N   . LEU D 76  ? 0.41467 0.43123 0.40324 -0.01169 -0.01955 0.00986  90  LEU D N   
3574 C CA  . LEU D 76  ? 0.43582 0.45749 0.42066 -0.00887 -0.01937 0.01209  90  LEU D CA  
3575 C C   . LEU D 76  ? 0.42235 0.44251 0.40761 -0.00689 -0.01758 0.01712  90  LEU D C   
3576 O O   . LEU D 76  ? 0.38148 0.39886 0.37263 -0.00639 -0.01699 0.02108  90  LEU D O   
3577 C CB  . LEU D 76  ? 0.48594 0.51378 0.47303 -0.00595 -0.02095 0.01358  90  LEU D CB  
3578 C CG  . LEU D 76  ? 0.40628 0.43931 0.39292 -0.00742 -0.02271 0.00760  90  LEU D CG  
3579 C CD1 . LEU D 76  ? 0.51464 0.55338 0.50411 -0.00330 -0.02505 0.00867  90  LEU D CD1 
3580 C CD2 . LEU D 76  ? 0.50107 0.53704 0.48127 -0.00906 -0.02257 0.00353  90  LEU D CD2 
3581 N N   . ILE D 77  ? 0.41421 0.43710 0.39379 -0.00585 -0.01691 0.01644  91  ILE D N   
3582 C CA  . ILE D 77  ? 0.46773 0.49268 0.44706 -0.00395 -0.01493 0.02040  91  ILE D CA  
3583 C C   . ILE D 77  ? 0.54355 0.57767 0.51847 -0.00064 -0.01468 0.02285  91  ILE D C   
3584 O O   . ILE D 77  ? 0.43138 0.46944 0.40074 0.00048  -0.01579 0.01843  91  ILE D O   
3585 C CB  . ILE D 77  ? 0.45311 0.47450 0.42951 -0.00471 -0.01480 0.01629  91  ILE D CB  
3586 C CG1 . ILE D 77  ? 0.45955 0.47159 0.43851 -0.00766 -0.01556 0.01340  91  ILE D CG1 
3587 C CG2 . ILE D 77  ? 0.37349 0.39912 0.35119 -0.00288 -0.01253 0.01973  91  ILE D CG2 
3588 C CD1 . ILE D 77  ? 0.32120 0.32800 0.29660 -0.00779 -0.01630 0.00929  91  ILE D CD1 
3589 N N   . ARG D 78  ? 0.46006 0.49723 0.43727 0.00100  -0.01359 0.02990  92  ARG D N   
3590 C CA  . ARG D 78  ? 0.44794 0.49418 0.42014 0.00442  -0.01307 0.03355  92  ARG D CA  
3591 C C   . ARG D 78  ? 0.47052 0.52273 0.44048 0.00516  -0.01031 0.03566  92  ARG D C   
3592 O O   . ARG D 78  ? 0.47025 0.51948 0.44459 0.00303  -0.00836 0.03750  92  ARG D O   
3593 C CB  . ARG D 78  ? 0.29522 0.34109 0.26966 0.00577  -0.01355 0.04104  92  ARG D CB  
3594 C CG  . ARG D 78  ? 0.67364 0.71575 0.65066 0.00609  -0.01685 0.03805  92  ARG D CG  
3595 C CD  . ARG D 78  ? 0.65126 0.69098 0.63086 0.00810  -0.01856 0.04501  92  ARG D CD  
3596 N NE  . ARG D 78  ? 0.70946 0.74144 0.69641 0.00565  -0.01786 0.04999  92  ARG D NE  
3597 C CZ  . ARG D 78  ? 0.82173 0.84711 0.81586 0.00366  -0.01923 0.04643  92  ARG D CZ  
3598 N NH1 . ARG D 78  ? 0.58258 0.60836 0.57700 0.00307  -0.02077 0.03839  92  ARG D NH1 
3599 N NH2 . ARG D 78  ? 0.77493 0.79382 0.77627 0.00200  -0.01902 0.05096  92  ARG D NH2 
3600 N N   . ASP D 79  ? 0.44169 0.50381 0.40516 0.00852  -0.01031 0.03459  93  ASP D N   
3601 C CA  . ASP D 79  ? 0.39292 0.46469 0.35367 0.01010  -0.00771 0.03656  93  ASP D CA  
3602 C C   . ASP D 79  ? 0.47104 0.53975 0.43430 0.00839  -0.00720 0.03137  93  ASP D C   
3603 O O   . ASP D 79  ? 0.47515 0.54522 0.44222 0.00676  -0.00443 0.03482  93  ASP D O   
3604 C CB  . ASP D 79  ? 0.44177 0.51699 0.40405 0.00936  -0.00463 0.04725  93  ASP D CB  
3605 C CG  . ASP D 79  ? 0.77217 0.86216 0.72882 0.01199  -0.00206 0.05027  93  ASP D CG  
3606 O OD1 . ASP D 79  ? 0.79471 0.89305 0.74469 0.01629  -0.00361 0.04724  93  ASP D OD1 
3607 O OD2 . ASP D 79  ? 0.71352 0.80792 0.67267 0.00972  0.00154  0.05534  93  ASP D OD2 
3608 N N   . SER D 80  ? 0.48454 0.54864 0.44561 0.00869  -0.01026 0.02284  94  SER D N   
3609 C CA  . SER D 80  ? 0.38985 0.44791 0.35233 0.00748  -0.01109 0.01727  94  SER D CA  
3610 C C   . SER D 80  ? 0.49086 0.55934 0.45213 0.01010  -0.00954 0.01611  94  SER D C   
3611 O O   . SER D 80  ? 0.44259 0.52300 0.39924 0.01379  -0.00962 0.01498  94  SER D O   
3612 C CB  . SER D 80  ? 0.40145 0.45254 0.36018 0.00733  -0.01524 0.00904  94  SER D CB  
3613 O OG  . SER D 80  ? 0.48118 0.54093 0.43461 0.01097  -0.01715 0.00528  94  SER D OG  
3614 N N   . LYS D 81  ? 0.39534 0.46062 0.36106 0.00851  -0.00825 0.01571  95  LYS D N   
3615 C CA  . LYS D 81  ? 0.41251 0.48845 0.37849 0.01064  -0.00669 0.01364  95  LYS D CA  
3616 C C   . LYS D 81  ? 0.48258 0.55200 0.44723 0.01235  -0.01051 0.00405  95  LYS D C   
3617 O O   . LYS D 81  ? 0.43842 0.49339 0.40302 0.01051  -0.01331 0.00116  95  LYS D O   
3618 C CB  . LYS D 81  ? 0.40470 0.48377 0.37775 0.00745  -0.00212 0.02082  95  LYS D CB  
3619 C CG  . LYS D 81  ? 0.57984 0.65834 0.55479 0.00486  0.00032  0.03094  95  LYS D CG  
3620 C CD  . LYS D 81  ? 0.73630 0.82203 0.71666 0.00190  0.00500  0.03890  95  LYS D CD  
3621 C CE  . LYS D 81  ? 0.83613 0.92214 0.81584 0.00032  0.00657  0.04941  95  LYS D CE  
3622 N NZ  . LYS D 81  ? 0.60540 0.69977 0.57615 0.00430  0.00560  0.04978  95  LYS D NZ  
3623 N N   . LEU D 82  ? 0.46455 0.54524 0.42765 0.01612  -0.01090 -0.00099 96  LEU D N   
3624 C CA  . LEU D 82  ? 0.39766 0.47228 0.35894 0.01889  -0.01552 -0.01071 96  LEU D CA  
3625 C C   . LEU D 82  ? 0.37832 0.43991 0.34426 0.01595  -0.01554 -0.01073 96  LEU D C   
3626 O O   . LEU D 82  ? 0.44033 0.48831 0.40333 0.01646  -0.02011 -0.01642 96  LEU D O   
3627 C CB  . LEU D 82  ? 0.40646 0.49785 0.36720 0.02367  -0.01547 -0.01607 96  LEU D CB  
3628 C CG  . LEU D 82  ? 0.64112 0.74764 0.59675 0.02815  -0.01636 -0.01838 96  LEU D CG  
3629 C CD1 . LEU D 82  ? 0.61374 0.73642 0.56935 0.03334  -0.01724 -0.02586 96  LEU D CD1 
3630 C CD2 . LEU D 82  ? 0.53908 0.63492 0.48909 0.02996  -0.02231 -0.02379 96  LEU D CD2 
3631 N N   . SER D 83  ? 0.36151 0.42675 0.33457 0.01279  -0.01071 -0.00426 97  SER D N   
3632 C CA  . SER D 83  ? 0.32432 0.37894 0.30299 0.01039  -0.01058 -0.00439 97  SER D CA  
3633 C C   . SER D 83  ? 0.42794 0.46641 0.40601 0.00735  -0.01232 -0.00234 97  SER D C   
3634 O O   . SER D 83  ? 0.48603 0.51461 0.46714 0.00619  -0.01331 -0.00394 97  SER D O   
3635 C CB  . SER D 83  ? 0.39233 0.45557 0.37981 0.00735  -0.00515 0.00223  97  SER D CB  
3636 O OG  . SER D 83  ? 0.50443 0.56906 0.49330 0.00418  -0.00216 0.01155  97  SER D OG  
3637 N N   . ASP D 84  ? 0.30730 0.34419 0.28169 0.00624  -0.01273 0.00068  98  ASP D N   
3638 C CA  . ASP D 84  ? 0.39536 0.41912 0.36891 0.00335  -0.01453 0.00131  98  ASP D CA  
3639 C C   . ASP D 84  ? 0.37755 0.39000 0.34460 0.00406  -0.01941 -0.00586 98  ASP D C   
3640 O O   . ASP D 84  ? 0.45327 0.45471 0.41957 0.00114  -0.02069 -0.00575 98  ASP D O   
3641 C CB  . ASP D 84  ? 0.36051 0.38722 0.33244 0.00212  -0.01378 0.00569  98  ASP D CB  
3642 C CG  . ASP D 84  ? 0.40813 0.44117 0.38603 0.00075  -0.00988 0.01399  98  ASP D CG  
3643 O OD1 . ASP D 84  ? 0.48529 0.51521 0.47012 -0.00111 -0.00821 0.01681  98  ASP D OD1 
3644 O OD2 . ASP D 84  ? 0.47015 0.51074 0.44568 0.00171  -0.00896 0.01761  98  ASP D OD2 
3645 N N   . SER D 85  ? 0.35766 0.37263 0.31982 0.00784  -0.02244 -0.01205 99  SER D N   
3646 C CA  . SER D 85  ? 0.47547 0.47787 0.43079 0.00864  -0.02805 -0.01865 99  SER D CA  
3647 C C   . SER D 85  ? 0.42075 0.41073 0.37687 0.00731  -0.02919 -0.01966 99  SER D C   
3648 O O   . SER D 85  ? 0.48541 0.47804 0.44504 0.00981  -0.02867 -0.02162 99  SER D O   
3649 C CB  . SER D 85  ? 0.42146 0.42937 0.37278 0.01418  -0.03180 -0.02592 99  SER D CB  
3650 O OG  . SER D 85  ? 0.43713 0.45825 0.38761 0.01611  -0.03080 -0.02544 99  SER D OG  
3651 N N   . ALA D 86  ? 0.42970 0.40738 0.38265 0.00342  -0.03065 -0.01859 100 ALA D N   
3652 C CA  . ALA D 86  ? 0.39957 0.36556 0.35208 0.00210  -0.03182 -0.01916 100 ALA D CA  
3653 C C   . ALA D 86  ? 0.41053 0.36556 0.35755 -0.00279 -0.03348 -0.01798 100 ALA D C   
3654 O O   . ALA D 86  ? 0.43949 0.39631 0.38402 -0.00505 -0.03380 -0.01736 100 ALA D O   
3655 C CB  . ALA D 86  ? 0.31371 0.28496 0.27559 0.00137  -0.02739 -0.01504 100 ALA D CB  
3656 N N   . THR D 87  ? 0.34406 0.28877 0.28927 -0.00450 -0.03446 -0.01790 101 THR D N   
3657 C CA  . THR D 87  ? 0.40290 0.33939 0.34377 -0.01006 -0.03491 -0.01591 101 THR D CA  
3658 C C   . THR D 87  ? 0.40724 0.35015 0.35599 -0.01232 -0.03053 -0.01168 101 THR D C   
3659 O O   . THR D 87  ? 0.42093 0.36589 0.37560 -0.00990 -0.02910 -0.01132 101 THR D O   
3660 C CB  . THR D 87  ? 0.35696 0.27772 0.28904 -0.01052 -0.03928 -0.01834 101 THR D CB  
3661 O OG1 . THR D 87  ? 0.52414 0.43742 0.44874 -0.00820 -0.04455 -0.02270 101 THR D OG1 
3662 C CG2 . THR D 87  ? 0.33703 0.25131 0.26472 -0.01722 -0.03886 -0.01545 101 THR D CG2 
3663 N N   . TYR D 88  ? 0.39669 0.34329 0.34614 -0.01664 -0.02887 -0.00926 102 TYR D N   
3664 C CA  . TYR D 88  ? 0.36430 0.31817 0.32156 -0.01813 -0.02556 -0.00610 102 TYR D CA  
3665 C C   . TYR D 88  ? 0.42003 0.36862 0.37369 -0.02275 -0.02594 -0.00609 102 TYR D C   
3666 O O   . TYR D 88  ? 0.42561 0.37146 0.37322 -0.02730 -0.02688 -0.00652 102 TYR D O   
3667 C CB  . TYR D 88  ? 0.39710 0.36168 0.35858 -0.01847 -0.02357 -0.00394 102 TYR D CB  
3668 C CG  . TYR D 88  ? 0.43200 0.40369 0.39765 -0.01406 -0.02235 -0.00268 102 TYR D CG  
3669 C CD1 . TYR D 88  ? 0.33864 0.31082 0.29943 -0.01173 -0.02399 -0.00508 102 TYR D CD1 
3670 C CD2 . TYR D 88  ? 0.39046 0.36857 0.36497 -0.01234 -0.01979 0.00080  102 TYR D CD2 
3671 C CE1 . TYR D 88  ? 0.43356 0.41451 0.39783 -0.00795 -0.02244 -0.00393 102 TYR D CE1 
3672 C CE2 . TYR D 88  ? 0.33101 0.31611 0.30890 -0.00938 -0.01821 0.00281  102 TYR D CE2 
3673 C CZ  . TYR D 88  ? 0.33091 0.31839 0.30347 -0.00726 -0.01920 0.00050  102 TYR D CZ  
3674 O OH  . TYR D 88  ? 0.47985 0.47656 0.45550 -0.00456 -0.01719 0.00253  102 TYR D OH  
3675 N N   . LEU D 89  ? 0.41490 0.36298 0.37252 -0.02174 -0.02520 -0.00580 103 LEU D N   
3676 C CA  . LEU D 89  ? 0.39926 0.34307 0.35272 -0.02533 -0.02560 -0.00605 103 LEU D CA  
3677 C C   . LEU D 89  ? 0.38224 0.33666 0.34327 -0.02699 -0.02325 -0.00507 103 LEU D C   
3678 O O   . LEU D 89  ? 0.37287 0.33376 0.34372 -0.02344 -0.02217 -0.00456 103 LEU D O   
3679 C CB  . LEU D 89  ? 0.43890 0.37546 0.39088 -0.02211 -0.02711 -0.00752 103 LEU D CB  
3680 C CG  . LEU D 89  ? 0.48438 0.41107 0.43008 -0.01869 -0.03020 -0.00972 103 LEU D CG  
3681 C CD1 . LEU D 89  ? 0.45342 0.37636 0.40073 -0.01428 -0.03136 -0.01181 103 LEU D CD1 
3682 C CD2 . LEU D 89  ? 0.40727 0.32240 0.34020 -0.02259 -0.03328 -0.00997 103 LEU D CD2 
3683 N N   . CYS D 90  ? 0.34901 0.30531 0.30573 -0.03246 -0.02283 -0.00513 104 CYS D N   
3684 C CA  . CYS D 90  ? 0.42225 0.38940 0.38511 -0.03403 -0.02121 -0.00559 104 CYS D CA  
3685 C C   . CYS D 90  ? 0.38477 0.35020 0.34633 -0.03406 -0.02145 -0.00654 104 CYS D C   
3686 O O   . CYS D 90  ? 0.51611 0.47319 0.46766 -0.03744 -0.02227 -0.00617 104 CYS D O   
3687 C CB  . CYS D 90  ? 0.30558 0.27784 0.26475 -0.04014 -0.02044 -0.00603 104 CYS D CB  
3688 S SG  . CYS D 90  ? 0.46436 0.45232 0.43050 -0.04217 -0.01887 -0.00813 104 CYS D SG  
3689 N N   . VAL D 91  ? 0.31393 0.28670 0.28530 -0.03006 -0.02118 -0.00775 105 VAL D N   
3690 C CA  . VAL D 91  ? 0.35963 0.33191 0.33116 -0.02841 -0.02180 -0.00944 105 VAL D CA  
3691 C C   . VAL D 91  ? 0.39142 0.37725 0.37009 -0.02868 -0.02121 -0.01179 105 VAL D C   
3692 O O   . VAL D 91  ? 0.41145 0.40474 0.40093 -0.02530 -0.02159 -0.01270 105 VAL D O   
3693 C CB  . VAL D 91  ? 0.31432 0.28202 0.29199 -0.02201 -0.02303 -0.01019 105 VAL D CB  
3694 C CG1 . VAL D 91  ? 0.35175 0.31759 0.32748 -0.02003 -0.02416 -0.01248 105 VAL D CG1 
3695 C CG2 . VAL D 91  ? 0.40405 0.36157 0.37627 -0.02109 -0.02372 -0.00883 105 VAL D CG2 
3696 N N   . VAL D 92  ? 0.31473 0.30390 0.28711 -0.03256 -0.02061 -0.01284 106 VAL D N   
3697 C CA  . VAL D 92  ? 0.48628 0.49073 0.46392 -0.03360 -0.01999 -0.01598 106 VAL D CA  
3698 C C   . VAL D 92  ? 0.41992 0.42743 0.39812 -0.03067 -0.02083 -0.01853 106 VAL D C   
3699 O O   . VAL D 92  ? 0.35252 0.35170 0.32039 -0.03246 -0.02075 -0.01693 106 VAL D O   
3700 C CB  . VAL D 92  ? 0.39299 0.40296 0.36293 -0.04190 -0.01793 -0.01541 106 VAL D CB  
3701 C CG1 . VAL D 92  ? 0.40318 0.43133 0.37860 -0.04275 -0.01727 -0.01968 106 VAL D CG1 
3702 C CG2 . VAL D 92  ? 0.36637 0.37468 0.33697 -0.04379 -0.01758 -0.01395 106 VAL D CG2 
3703 N N   . MET D 93  ? 0.37592 0.39505 0.36598 -0.02568 -0.02220 -0.02275 107 MET D N   
3704 C CA  . MET D 93  ? 0.41500 0.43909 0.40809 -0.02134 -0.02365 -0.02645 107 MET D CA  
3705 C C   . MET D 93  ? 0.41059 0.45270 0.40527 -0.02319 -0.02312 -0.03067 107 MET D C   
3706 O O   . MET D 93  ? 0.41188 0.46520 0.41585 -0.02183 -0.02402 -0.03380 107 MET D O   
3707 C CB  . MET D 93  ? 0.33157 0.35462 0.33865 -0.01324 -0.02657 -0.02902 107 MET D CB  
3708 C CG  . MET D 93  ? 0.32636 0.35398 0.33786 -0.00779 -0.02871 -0.03372 107 MET D CG  
3709 S SD  . MET D 93  ? 0.45362 0.48395 0.48501 0.00084  -0.03286 -0.03811 107 MET D SD  
3710 C CE  . MET D 93  ? 0.37574 0.42478 0.41550 0.00186  -0.03470 -0.04349 107 MET D CE  
3711 N N   . GLY D 94  ? 0.48867 0.53407 0.47392 -0.02610 -0.02186 -0.03087 108 GLY D N   
3712 C CA  . GLY D 94  ? 0.35254 0.41737 0.33922 -0.02720 -0.02127 -0.03554 108 GLY D CA  
3713 C C   . GLY D 94  ? 0.40226 0.47120 0.39040 -0.02116 -0.02317 -0.03925 108 GLY D C   
3714 O O   . GLY D 94  ? 0.43986 0.49672 0.43007 -0.01567 -0.02525 -0.03875 108 GLY D O   
3715 N N   . PHE D 95  ? 0.40732 0.49442 0.39462 -0.02187 -0.02253 -0.04350 109 PHE D N   
3716 C CA  . PHE D 95  ? 0.37098 0.46414 0.35993 -0.01530 -0.02465 -0.04789 109 PHE D CA  
3717 C C   . PHE D 95  ? 0.37172 0.44924 0.34590 -0.01693 -0.02368 -0.04247 109 PHE D C   
3718 O O   . PHE D 95  ? 0.52339 0.59882 0.48225 -0.02502 -0.02049 -0.03735 109 PHE D O   
3719 C CB  . PHE D 95  ? 0.41448 0.53262 0.40432 -0.01608 -0.02387 -0.05369 109 PHE D CB  
3720 C CG  . PHE D 95  ? 0.48554 0.61284 0.47803 -0.00834 -0.02647 -0.05938 109 PHE D CG  
3721 C CD1 . PHE D 95  ? 0.38320 0.51215 0.39185 0.00231  -0.03166 -0.06625 109 PHE D CD1 
3722 C CD2 . PHE D 95  ? 0.31266 0.44697 0.29146 -0.01178 -0.02395 -0.05783 109 PHE D CD2 
3723 C CE1 . PHE D 95  ? 0.37383 0.51177 0.38580 0.01002  -0.03454 -0.07243 109 PHE D CE1 
3724 C CE2 . PHE D 95  ? 0.44303 0.58682 0.42398 -0.00389 -0.02655 -0.06350 109 PHE D CE2 
3725 C CZ  . PHE D 95  ? 0.36210 0.50808 0.36009 0.00732  -0.03197 -0.07131 109 PHE D CZ  
3726 N N   . GLN D 96  ? 0.40146 0.46732 0.38022 -0.00942 -0.02673 -0.04358 110 GLN D N   
3727 C CA  . GLN D 96  ? 0.72333 0.77422 0.68943 -0.00866 -0.02707 -0.03998 110 GLN D CA  
3728 C C   . GLN D 96  ? 0.56787 0.60066 0.51932 -0.01669 -0.02486 -0.03170 110 GLN D C   
3729 O O   . GLN D 96  ? 0.59278 0.61619 0.52837 -0.01983 -0.02435 -0.02741 110 GLN D O   
3730 C CB  . GLN D 96  ? 0.61207 0.67409 0.56936 -0.00785 -0.02677 -0.04188 110 GLN D CB  
3731 C CG  . GLN D 96  ? 0.54045 0.61495 0.51063 0.00278  -0.03047 -0.05066 110 GLN D CG  
3732 C CD  . GLN D 96  ? 0.74989 0.83855 0.71085 0.00351  -0.02989 -0.05278 110 GLN D CD  
3733 O OE1 . GLN D 96  ? 0.81178 0.90068 0.75618 -0.00480 -0.02634 -0.04683 110 GLN D OE1 
3734 N NE2 . GLN D 96  ? 0.75919 0.86007 0.73080 0.01327  -0.03349 -0.06122 110 GLN D NE2 
3735 N N   . LYS D 97  ? 0.54045 0.56770 0.49692 -0.01962 -0.02410 -0.02953 111 LYS D N   
3736 C CA  . LYS D 97  ? 0.47732 0.48715 0.42173 -0.02598 -0.02294 -0.02285 111 LYS D CA  
3737 C C   . LYS D 97  ? 0.49605 0.50039 0.45031 -0.02480 -0.02335 -0.02248 111 LYS D C   
3738 O O   . LYS D 97  ? 0.42651 0.44212 0.39032 -0.02584 -0.02243 -0.02431 111 LYS D O   
3739 C CB  . LYS D 97  ? 0.42365 0.43756 0.35603 -0.03658 -0.01967 -0.01868 111 LYS D CB  
3740 C CG  . LYS D 97  ? 0.49647 0.49032 0.41303 -0.04296 -0.01957 -0.01184 111 LYS D CG  
3741 C CD  . LYS D 97  ? 0.71462 0.71192 0.61744 -0.05364 -0.01669 -0.00738 111 LYS D CD  
3742 C CE  . LYS D 97  ? 0.81528 0.79322 0.70557 -0.06136 -0.01695 -0.00095 111 LYS D CE  
3743 N NZ  . LYS D 97  ? 0.92731 0.88358 0.81242 -0.05542 -0.02102 0.00040  111 LYS D NZ  
3744 N N   . LEU D 98  ? 0.48603 0.47393 0.43765 -0.02228 -0.02492 -0.02040 112 LEU D N   
3745 C CA  . LEU D 98  ? 0.38608 0.36813 0.34491 -0.02134 -0.02510 -0.01935 112 LEU D CA  
3746 C C   . LEU D 98  ? 0.42876 0.39609 0.37436 -0.02685 -0.02480 -0.01449 112 LEU D C   
3747 O O   . LEU D 98  ? 0.40698 0.36078 0.34336 -0.02522 -0.02676 -0.01332 112 LEU D O   
3748 C CB  . LEU D 98  ? 0.29517 0.27317 0.26436 -0.01310 -0.02741 -0.02224 112 LEU D CB  
3749 C CG  . LEU D 98  ? 0.38757 0.36098 0.36439 -0.01202 -0.02729 -0.02082 112 LEU D CG  
3750 C CD1 . LEU D 98  ? 0.29023 0.27523 0.27806 -0.01302 -0.02624 -0.02122 112 LEU D CD1 
3751 C CD2 . LEU D 98  ? 0.38871 0.35750 0.37375 -0.00515 -0.02924 -0.02336 112 LEU D CD2 
3752 N N   . VAL D 99  ? 0.34435 0.31419 0.28941 -0.03271 -0.02300 -0.01235 113 VAL D N   
3753 C CA  . VAL D 99  ? 0.46558 0.42309 0.39827 -0.03898 -0.02301 -0.00830 113 VAL D CA  
3754 C C   . VAL D 99  ? 0.45090 0.40242 0.38832 -0.03670 -0.02379 -0.00793 113 VAL D C   
3755 O O   . VAL D 99  ? 0.42020 0.38100 0.36720 -0.03644 -0.02246 -0.00871 113 VAL D O   
3756 C CB  . VAL D 99  ? 0.46445 0.42979 0.39219 -0.04813 -0.02044 -0.00657 113 VAL D CB  
3757 C CG1 . VAL D 99  ? 0.38727 0.33789 0.30223 -0.05489 -0.02120 -0.00249 113 VAL D CG1 
3758 C CG2 . VAL D 99  ? 0.44514 0.42007 0.36896 -0.05037 -0.01914 -0.00718 113 VAL D CG2 
3759 N N   . PHE D 100 ? 0.46163 0.39812 0.39170 -0.03477 -0.02626 -0.00695 114 PHE D N   
3760 C CA  . PHE D 100 ? 0.40420 0.33517 0.33646 -0.03293 -0.02721 -0.00680 114 PHE D CA  
3761 C C   . PHE D 100 ? 0.49346 0.41815 0.41645 -0.03990 -0.02751 -0.00443 114 PHE D C   
3762 O O   . PHE D 100 ? 0.42278 0.33585 0.33317 -0.04390 -0.02936 -0.00255 114 PHE D O   
3763 C CB  . PHE D 100 ? 0.42446 0.34425 0.35432 -0.02661 -0.03026 -0.00840 114 PHE D CB  
3764 C CG  . PHE D 100 ? 0.44690 0.37383 0.38954 -0.01960 -0.02987 -0.01127 114 PHE D CG  
3765 C CD1 . PHE D 100 ? 0.33446 0.26533 0.28008 -0.01665 -0.03008 -0.01327 114 PHE D CD1 
3766 C CD2 . PHE D 100 ? 0.34879 0.27900 0.30063 -0.01621 -0.02935 -0.01197 114 PHE D CD2 
3767 C CE1 . PHE D 100 ? 0.37306 0.31001 0.33151 -0.01055 -0.03017 -0.01632 114 PHE D CE1 
3768 C CE2 . PHE D 100 ? 0.41501 0.35127 0.37908 -0.01090 -0.02895 -0.01412 114 PHE D CE2 
3769 C CZ  . PHE D 100 ? 0.45939 0.39854 0.42724 -0.00812 -0.02955 -0.01650 114 PHE D CZ  
3770 N N   . GLY D 101 ? 0.50575 0.43760 0.43484 -0.04131 -0.02607 -0.00449 115 GLY D N   
3771 C CA  . GLY D 101 ? 0.27776 0.20388 0.19978 -0.04695 -0.02690 -0.00327 115 GLY D CA  
3772 C C   . GLY D 101 ? 0.40015 0.31075 0.31464 -0.04427 -0.03087 -0.00362 115 GLY D C   
3773 O O   . GLY D 101 ? 0.42856 0.33550 0.34522 -0.03741 -0.03246 -0.00525 115 GLY D O   
3774 N N   . THR D 102 ? 0.40291 0.30472 0.30890 -0.04975 -0.03288 -0.00272 116 THR D N   
3775 C CA  . THR D 102 ? 0.51118 0.39776 0.40973 -0.04692 -0.03780 -0.00395 116 THR D CA  
3776 C C   . THR D 102 ? 0.48342 0.37558 0.38941 -0.04097 -0.03827 -0.00681 116 THR D C   
3777 O O   . THR D 102 ? 0.56486 0.44820 0.46741 -0.03589 -0.04220 -0.00923 116 THR D O   
3778 C CB  . THR D 102 ? 0.66640 0.54063 0.55394 -0.05478 -0.04063 -0.00226 116 THR D CB  
3779 O OG1 . THR D 102 ? 0.78729 0.67266 0.67932 -0.06145 -0.03740 -0.00167 116 THR D OG1 
3780 C CG2 . THR D 102 ? 0.56559 0.42856 0.44191 -0.05919 -0.04181 0.00108  116 THR D CG2 
3781 N N   . GLY D 103 ? 0.41548 0.32247 0.33104 -0.04120 -0.03465 -0.00677 117 GLY D N   
3782 C CA  . GLY D 103 ? 0.49331 0.40779 0.41616 -0.03531 -0.03428 -0.00852 117 GLY D CA  
3783 C C   . GLY D 103 ? 0.51065 0.42609 0.43187 -0.03705 -0.03576 -0.00993 117 GLY D C   
3784 O O   . GLY D 103 ? 0.57706 0.48222 0.49017 -0.04145 -0.03896 -0.01060 117 GLY D O   
3785 N N   . THR D 104 ? 0.51164 0.43938 0.44061 -0.03357 -0.03369 -0.01033 118 THR D N   
3786 C CA  . THR D 104 ? 0.49599 0.42680 0.42434 -0.03300 -0.03530 -0.01248 118 THR D CA  
3787 C C   . THR D 104 ? 0.41076 0.34405 0.34104 -0.02544 -0.03655 -0.01446 118 THR D C   
3788 O O   . THR D 104 ? 0.43324 0.37569 0.37060 -0.02156 -0.03347 -0.01277 118 THR D O   
3789 C CB  . THR D 104 ? 0.40278 0.34749 0.33753 -0.03492 -0.03201 -0.01146 118 THR D CB  
3790 O OG1 . THR D 104 ? 0.43277 0.37782 0.36670 -0.04182 -0.03050 -0.01033 118 THR D OG1 
3791 C CG2 . THR D 104 ? 0.50693 0.45473 0.44035 -0.03431 -0.03411 -0.01432 118 THR D CG2 
3792 N N   . ARG D 105 ? 0.39036 0.31590 0.31463 -0.02348 -0.04128 -0.01823 119 ARG D N   
3793 C CA  . ARG D 105 ? 0.48946 0.41906 0.41525 -0.01610 -0.04276 -0.02121 119 ARG D CA  
3794 C C   . ARG D 105 ? 0.48442 0.42850 0.41473 -0.01352 -0.04110 -0.02177 119 ARG D C   
3795 O O   . ARG D 105 ? 0.50786 0.45333 0.43662 -0.01615 -0.04228 -0.02298 119 ARG D O   
3796 C CB  . ARG D 105 ? 0.48130 0.39722 0.39887 -0.01373 -0.04949 -0.02617 119 ARG D CB  
3797 C CG  . ARG D 105 ? 0.52604 0.44575 0.44518 -0.00575 -0.05110 -0.03000 119 ARG D CG  
3798 C CD  . ARG D 105 ? 0.77881 0.68282 0.68935 -0.00291 -0.05868 -0.03532 119 ARG D CD  
3799 N NE  . ARG D 105 ? 0.95352 0.85193 0.85916 -0.00378 -0.06395 -0.03897 119 ARG D NE  
3800 C CZ  . ARG D 105 ? 1.12038 1.02313 1.02570 0.00250  -0.06835 -0.04535 119 ARG D CZ  
3801 N NH1 . ARG D 105 ? 1.14699 1.06025 1.05597 0.00982  -0.06791 -0.04878 119 ARG D NH1 
3802 N NH2 . ARG D 105 ? 1.00281 0.90024 0.90454 0.00137  -0.07343 -0.04887 119 ARG D NH2 
3803 N N   . LEU D 106 ? 0.48213 0.43743 0.41803 -0.00853 -0.03829 -0.02080 120 LEU D N   
3804 C CA  . LEU D 106 ? 0.39625 0.36646 0.33591 -0.00556 -0.03616 -0.02019 120 LEU D CA  
3805 C C   . LEU D 106 ? 0.47355 0.44920 0.41229 0.00088  -0.03827 -0.02445 120 LEU D C   
3806 O O   . LEU D 106 ? 0.42887 0.40448 0.36947 0.00359  -0.03772 -0.02495 120 LEU D O   
3807 C CB  . LEU D 106 ? 0.40650 0.38685 0.35369 -0.00604 -0.03052 -0.01410 120 LEU D CB  
3808 C CG  . LEU D 106 ? 0.48230 0.47785 0.43259 -0.00245 -0.02807 -0.01213 120 LEU D CG  
3809 C CD1 . LEU D 106 ? 0.41389 0.41370 0.36164 -0.00324 -0.02937 -0.01357 120 LEU D CD1 
3810 C CD2 . LEU D 106 ? 0.30246 0.30493 0.25989 -0.00277 -0.02331 -0.00556 120 LEU D CD2 
3811 N N   . LEU D 107 ? 0.47981 0.46150 0.41616 0.00358  -0.04082 -0.02825 121 LEU D N   
3812 C CA  . LEU D 107 ? 0.50529 0.49586 0.44102 0.01030  -0.04291 -0.03316 121 LEU D CA  
3813 C C   . LEU D 107 ? 0.47680 0.48517 0.41510 0.01278  -0.03984 -0.03132 121 LEU D C   
3814 O O   . LEU D 107 ? 0.51405 0.52439 0.45027 0.01258  -0.04188 -0.03339 121 LEU D O   
3815 C CB  . LEU D 107 ? 0.50342 0.48360 0.43276 0.01266  -0.05071 -0.04126 121 LEU D CB  
3816 C CG  . LEU D 107 ? 0.83836 0.82892 0.76719 0.02062  -0.05388 -0.04812 121 LEU D CG  
3817 C CD1 . LEU D 107 ? 0.73515 0.73026 0.66711 0.02353  -0.05146 -0.04784 121 LEU D CD1 
3818 C CD2 . LEU D 107 ? 0.89024 0.86900 0.81296 0.02336  -0.06294 -0.05677 121 LEU D CD2 
3819 N N   . VAL D 108 ? 0.46584 0.48706 0.40856 0.01489  -0.03501 -0.02728 122 VAL D N   
3820 C CA  . VAL D 108 ? 0.41519 0.45367 0.35933 0.01740  -0.03176 -0.02431 122 VAL D CA  
3821 C C   . VAL D 108 ? 0.50586 0.55607 0.44767 0.02397  -0.03447 -0.03101 122 VAL D C   
3822 O O   . VAL D 108 ? 0.55028 0.60368 0.49339 0.02655  -0.03450 -0.03360 122 VAL D O   
3823 C CB  . VAL D 108 ? 0.45290 0.49867 0.40267 0.01551  -0.02527 -0.01559 122 VAL D CB  
3824 C CG1 . VAL D 108 ? 0.40472 0.46644 0.35438 0.01762  -0.02218 -0.01122 122 VAL D CG1 
3825 C CG2 . VAL D 108 ? 0.38063 0.41452 0.33342 0.00994  -0.02361 -0.01058 122 VAL D CG2 
3826 N N   . SER D 109 ? 0.57844 0.63631 0.51720 0.02713  -0.03705 -0.03471 123 SER D N   
3827 C CA  . SER D 109 ? 0.46499 0.53624 0.40167 0.03418  -0.04010 -0.04199 123 SER D CA  
3828 C C   . SER D 109 ? 0.50565 0.59877 0.44332 0.03698  -0.03484 -0.03720 123 SER D C   
3829 O O   . SER D 109 ? 0.52077 0.61710 0.45884 0.03456  -0.03120 -0.03014 123 SER D O   
3830 C CB  . SER D 109 ? 0.52067 0.58702 0.45344 0.03680  -0.04739 -0.05058 123 SER D CB  
3831 O OG  . SER D 109 ? 0.80898 0.85699 0.73958 0.03588  -0.05349 -0.05645 123 SER D OG  
3832 N N   . PRO D 110 ? 0.48834 0.59721 0.42602 0.04216  -0.03454 -0.04097 124 PRO D N   
3833 C CA  . PRO D 110 ? 0.59172 0.72252 0.52945 0.04428  -0.02908 -0.03560 124 PRO D CA  
3834 C C   . PRO D 110 ? 0.48212 0.62449 0.41565 0.04938  -0.03181 -0.03945 124 PRO D C   
3835 O O   . PRO D 110 ? 0.53696 0.67469 0.46833 0.05304  -0.03874 -0.04913 124 PRO D O   
3836 C CB  . PRO D 110 ? 0.52725 0.67153 0.46666 0.04789  -0.02837 -0.04011 124 PRO D CB  
3837 C CG  . PRO D 110 ? 0.58501 0.71911 0.52268 0.05205  -0.03679 -0.05244 124 PRO D CG  
3838 C CD  . PRO D 110 ? 0.45520 0.56350 0.39242 0.04667  -0.03956 -0.05080 124 PRO D CD  
3839 N N   . ASN D 111 ? 0.43215 0.58946 0.36444 0.04973  -0.02659 -0.03169 125 ASN D N   
3840 C CA  . ASN D 111 ? 0.60334 0.77447 0.53132 0.05525  -0.02850 -0.03454 125 ASN D CA  
3841 C C   . ASN D 111 ? 0.51131 0.70655 0.43740 0.06183  -0.02795 -0.03906 125 ASN D C   
3842 O O   . ASN D 111 ? 0.64827 0.85965 0.57344 0.06141  -0.02166 -0.03115 125 ASN D O   
3843 C CB  . ASN D 111 ? 0.75608 0.92905 0.68257 0.05256  -0.02389 -0.02367 125 ASN D CB  
3844 N N   . ILE D 112 ? 0.52527 0.72328 0.45076 0.06790  -0.03487 -0.05207 126 ILE D N   
3845 C CA  . ILE D 112 ? 0.60329 0.82566 0.52747 0.07515  -0.03544 -0.05882 126 ILE D CA  
3846 C C   . ILE D 112 ? 0.69901 0.94182 0.61856 0.08030  -0.03427 -0.05758 126 ILE D C   
3847 O O   . ILE D 112 ? 0.63364 0.87484 0.55134 0.08475  -0.04023 -0.06479 126 ILE D O   
3848 C CB  . ILE D 112 ? 0.67157 0.88980 0.59652 0.08112  -0.04461 -0.07415 126 ILE D CB  
3849 C CG1 . ILE D 112 ? 0.55000 0.74357 0.47806 0.07598  -0.04678 -0.07491 126 ILE D CG1 
3850 C CG2 . ILE D 112 ? 0.63053 0.87522 0.55526 0.08842  -0.04477 -0.08146 126 ILE D CG2 
3851 C CD1 . ILE D 112 ? 0.41102 0.60818 0.34252 0.07163  -0.03993 -0.06804 126 ILE D CD1 
3852 N N   . GLN D 113 ? 0.71988 0.98203 0.63746 0.07958  -0.02670 -0.04834 127 GLN D N   
3853 C CA  . GLN D 113 ? 0.78903 1.06992 0.70090 0.08402  -0.02484 -0.04493 127 GLN D CA  
3854 C C   . GLN D 113 ? 0.88893 1.18991 0.79847 0.09453  -0.03095 -0.05890 127 GLN D C   
3855 O O   . GLN D 113 ? 0.85333 1.15586 0.76031 0.09970  -0.03583 -0.06437 127 GLN D O   
3856 C CB  . GLN D 113 ? 0.58791 0.88435 0.49746 0.08022  -0.01543 -0.03113 127 GLN D CB  
3857 N N   . ASN D 114 ? 0.87245 1.18992 0.78342 0.09822  -0.03118 -0.06577 128 ASN D N   
3858 C CA  . ASN D 114 ? 0.78172 1.12078 0.69111 0.10905  -0.03739 -0.08022 128 ASN D CA  
3859 C C   . ASN D 114 ? 0.67242 1.00151 0.58659 0.11206  -0.04530 -0.09423 128 ASN D C   
3860 O O   . ASN D 114 ? 0.75469 1.09435 0.67132 0.11247  -0.04350 -0.09704 128 ASN D O   
3861 C CB  . ASN D 114 ? 0.81295 1.18630 0.71878 0.11233  -0.03096 -0.07688 128 ASN D CB  
3862 C CG  . ASN D 114 ? 0.96286 1.34522 0.86237 0.10990  -0.02388 -0.06253 128 ASN D CG  
3863 O OD1 . ASN D 114 ? 0.86413 1.25160 0.75929 0.11558  -0.02718 -0.06507 128 ASN D OD1 
3864 N ND2 . ASN D 114 ? 0.94581 1.32958 0.84481 0.10159  -0.01458 -0.04755 128 ASN D ND2 
3865 N N   . PRO D 115 ? 0.62319 0.93180 0.53872 0.11412  -0.05442 -0.10335 129 PRO D N   
3866 C CA  . PRO D 115 ? 0.65833 0.95524 0.57724 0.11748  -0.06318 -0.11663 129 PRO D CA  
3867 C C   . PRO D 115 ? 0.78983 1.10993 0.71296 0.12735  -0.06603 -0.12834 129 PRO D C   
3868 O O   . PRO D 115 ? 0.84652 1.18618 0.77104 0.13309  -0.06462 -0.12991 129 PRO D O   
3869 C CB  . PRO D 115 ? 0.60487 0.87694 0.52418 0.11721  -0.07169 -0.12221 129 PRO D CB  
3870 C CG  . PRO D 115 ? 0.72910 0.99532 0.64656 0.11093  -0.06555 -0.10959 129 PRO D CG  
3871 C CD  . PRO D 115 ? 0.65218 0.94696 0.56622 0.11307  -0.05732 -0.10185 129 PRO D CD  
3872 N N   . ASP D 116 ? 0.71084 1.02683 0.63872 0.12905  -0.06911 -0.13567 130 ASP D N   
3873 C CA  . ASP D 116 ? 0.57076 0.90469 0.50651 0.13819  -0.07158 -0.14687 130 ASP D CA  
3874 C C   . ASP D 116 ? 0.66181 0.97227 0.60290 0.14072  -0.08038 -0.15718 130 ASP D C   
3875 O O   . ASP D 116 ? 0.59027 0.90717 0.53549 0.14302  -0.08047 -0.16194 130 ASP D O   
3876 C CB  . ASP D 116 ? 0.60788 0.97269 0.54382 0.13792  -0.06319 -0.14294 130 ASP D CB  
3877 C CG  . ASP D 116 ? 0.75084 1.14111 0.69526 0.14779  -0.06471 -0.15381 130 ASP D CG  
3878 O OD1 . ASP D 116 ? 0.75477 1.13868 0.70456 0.15556  -0.07211 -0.16426 130 ASP D OD1 
3879 O OD2 . ASP D 116 ? 0.76988 1.18734 0.71590 0.14761  -0.05845 -0.15186 130 ASP D OD2 
3880 N N   . PRO D 117 ? 0.57612 0.85899 0.51728 0.14023  -0.08802 -0.16054 131 PRO D N   
3881 C CA  . PRO D 117 ? 0.67077 0.92661 0.61486 0.14075  -0.09621 -0.16729 131 PRO D CA  
3882 C C   . PRO D 117 ? 0.72792 0.99454 0.68029 0.15106  -0.10078 -0.17925 131 PRO D C   
3883 O O   . PRO D 117 ? 0.90853 1.19202 0.86549 0.15894  -0.10215 -0.18570 131 PRO D O   
3884 C CB  . PRO D 117 ? 0.72353 0.95305 0.66601 0.13810  -0.10281 -0.16780 131 PRO D CB  
3885 C CG  . PRO D 117 ? 0.64129 0.88950 0.58390 0.14111  -0.10006 -0.16705 131 PRO D CG  
3886 C CD  . PRO D 117 ? 0.63817 0.91390 0.57700 0.13922  -0.08973 -0.15844 131 PRO D CD  
3887 N N   . ALA D 118 ? 1.00018 0.77469 0.66806 0.10401  -0.09908 -0.07337 132 ALA D N   
3888 C CA  . ALA D 118 ? 0.89015 0.66032 0.54920 0.11211  -0.09988 -0.07888 132 ALA D CA  
3889 C C   . ALA D 118 ? 0.98138 0.74878 0.65320 0.10405  -0.09816 -0.07695 132 ALA D C   
3890 O O   . ALA D 118 ? 0.91834 0.69002 0.60384 0.09320  -0.09258 -0.06976 132 ALA D O   
3891 C CB  . ALA D 118 ? 0.94173 0.72008 0.58694 0.12236  -0.08921 -0.07648 132 ALA D CB  
3892 N N   . VAL D 119 ? 0.95085 0.71091 0.61765 0.10978  -0.10308 -0.08353 133 VAL D N   
3893 C CA  . VAL D 119 ? 0.83224 0.58879 0.50899 0.10424  -0.10230 -0.08250 133 VAL D CA  
3894 C C   . VAL D 119 ? 0.89683 0.65763 0.56415 0.11433  -0.09508 -0.08341 133 VAL D C   
3895 O O   . VAL D 119 ? 0.93549 0.69134 0.58979 0.12563  -0.10004 -0.09117 133 VAL D O   
3896 C CB  . VAL D 119 ? 0.93525 0.67740 0.61604 0.10104  -0.11617 -0.08979 133 VAL D CB  
3897 C CG1 . VAL D 119 ? 0.87364 0.61179 0.56288 0.09687  -0.11516 -0.08863 133 VAL D CG1 
3898 C CG2 . VAL D 119 ? 0.82174 0.56133 0.51296 0.09007  -0.12278 -0.08857 133 VAL D CG2 
3899 N N   . TYR D 120 ? 0.81829 0.58869 0.49211 0.11022  -0.08336 -0.07574 134 TYR D N   
3900 C CA  . TYR D 120 ? 0.82634 0.60336 0.49285 0.11865  -0.07521 -0.07561 134 TYR D CA  
3901 C C   . TYR D 120 ? 0.88389 0.65864 0.56067 0.11414  -0.07505 -0.07472 134 TYR D C   
3902 O O   . TYR D 120 ? 0.79819 0.57084 0.48932 0.10213  -0.07612 -0.07044 134 TYR D O   
3903 C CB  . TYR D 120 ? 0.75762 0.54899 0.42181 0.11831  -0.06087 -0.06739 134 TYR D CB  
3904 C CG  . TYR D 120 ? 0.84390 0.63803 0.49845 0.12207  -0.05991 -0.06669 134 TYR D CG  
3905 C CD1 . TYR D 120 ? 0.98992 0.78152 0.62815 0.13449  -0.06447 -0.07367 134 TYR D CD1 
3906 C CD2 . TYR D 120 ? 0.79044 0.58980 0.45177 0.11353  -0.05425 -0.05898 134 TYR D CD2 
3907 C CE1 . TYR D 120 ? 0.96440 0.75873 0.59335 0.13812  -0.06377 -0.07271 134 TYR D CE1 
3908 C CE2 . TYR D 120 ? 0.93554 0.73721 0.58782 0.11749  -0.05349 -0.05800 134 TYR D CE2 
3909 C CZ  . TYR D 120 ? 0.97821 0.77748 0.61428 0.12974  -0.05835 -0.06472 134 TYR D CZ  
3910 O OH  . TYR D 120 ? 0.85609 0.65777 0.48269 0.13389  -0.05785 -0.06350 134 TYR D OH  
3911 N N   . GLN D 121 ? 0.85202 0.62759 0.52119 0.12411  -0.07368 -0.07879 135 GLN D N   
3912 C CA  . GLN D 121 ? 0.76767 0.54270 0.44500 0.12196  -0.07261 -0.07784 135 GLN D CA  
3913 C C   . GLN D 121 ? 0.87576 0.66685 0.55353 0.12289  -0.05820 -0.07115 135 GLN D C   
3914 O O   . GLN D 121 ? 0.71459 0.51397 0.38043 0.13206  -0.05173 -0.07190 135 GLN D O   
3915 C CB  . GLN D 121 ? 0.89045 0.65458 0.55974 0.13268  -0.08190 -0.08752 135 GLN D CB  
3916 C CG  . GLN D 121 ? 0.92001 0.68076 0.59840 0.13023  -0.08318 -0.08697 135 GLN D CG  
3917 C CD  . GLN D 121 ? 1.17730 0.92071 0.85170 0.13585  -0.09655 -0.09627 135 GLN D CD  
3918 O OE1 . GLN D 121 ? 1.15210 0.88584 0.81724 0.14091  -0.10515 -0.10345 135 GLN D OE1 
3919 N NE2 . GLN D 121 ? 1.23932 0.97836 0.92047 0.13489  -0.09848 -0.09615 135 GLN D NE2 
3920 N N   . LEU D 122 ? 0.89579 0.69153 0.58708 0.11297  -0.05318 -0.06458 136 LEU D N   
3921 C CA  . LEU D 122 ? 0.81432 0.62580 0.50809 0.11126  -0.03936 -0.05744 136 LEU D CA  
3922 C C   . LEU D 122 ? 0.86817 0.68122 0.56779 0.11242  -0.03904 -0.05785 136 LEU D C   
3923 O O   . LEU D 122 ? 0.94958 0.75410 0.65962 0.10545  -0.04583 -0.05778 136 LEU D O   
3924 C CB  . LEU D 122 ? 0.86086 0.67865 0.56572 0.09729  -0.03200 -0.04814 136 LEU D CB  
3925 C CG  . LEU D 122 ? 0.89867 0.71884 0.59827 0.09594  -0.02862 -0.04546 136 LEU D CG  
3926 C CD1 . LEU D 122 ? 0.85547 0.66277 0.55431 0.09523  -0.04093 -0.05046 136 LEU D CD1 
3927 C CD2 . LEU D 122 ? 0.69595 0.52515 0.40563 0.08364  -0.01804 -0.03565 136 LEU D CD2 
3928 N N   . ARG D 123 ? 0.85356 0.67784 0.54646 0.12119  -0.03121 -0.05815 137 ARG D N   
3929 C CA  . ARG D 123 ? 1.00028 0.82745 0.69757 0.12437  -0.03084 -0.05907 137 ARG D CA  
3930 C C   . ARG D 123 ? 0.97111 0.81204 0.68009 0.11406  -0.01988 -0.04977 137 ARG D C   
3931 O O   . ARG D 123 ? 0.88896 0.74099 0.59788 0.10896  -0.00942 -0.04353 137 ARG D O   
3932 C CB  . ARG D 123 ? 0.78391 0.61660 0.46785 0.14020  -0.02881 -0.06524 137 ARG D CB  
3933 N N   . ASP D 124 ? 1.08426 0.92381 0.80294 0.11093  -0.02257 -0.04889 138 ASP D N   
3934 C CA  . ASP D 124 ? 0.81850 0.67110 0.54852 0.10130  -0.01305 -0.04060 138 ASP D CA  
3935 C C   . ASP D 124 ? 0.92203 0.79292 0.64594 0.10803  -0.00094 -0.03877 138 ASP D C   
3936 O O   . ASP D 124 ? 1.14562 1.01867 0.85992 0.12143  -0.00199 -0.04478 138 ASP D O   
3937 C CB  . ASP D 124 ? 0.86670 0.71341 0.60688 0.09836  -0.01962 -0.04082 138 ASP D CB  
3938 C CG  . ASP D 124 ? 1.09006 0.94827 0.84357 0.08582  -0.01145 -0.03190 138 ASP D CG  
3939 O OD1 . ASP D 124 ? 1.07617 0.94986 0.82983 0.08231  0.00076  -0.02633 138 ASP D OD1 
3940 O OD2 . ASP D 124 ? 1.11018 0.96162 0.87374 0.07921  -0.01735 -0.03045 138 ASP D OD2 
3941 N N   . SER D 125 ? 0.78957 0.67380 0.51899 0.09839  0.01076  -0.03053 139 SER D N   
3942 C CA  . SER D 125 ? 0.96399 0.86650 0.68828 0.10298  0.02298  -0.02810 139 SER D CA  
3943 C C   . SER D 125 ? 0.98183 0.89297 0.71101 0.10730  0.02386  -0.02889 139 SER D C   
3944 O O   . SER D 125 ? 1.14750 1.07141 0.86972 0.11652  0.03021  -0.03061 139 SER D O   
3945 C CB  . SER D 125 ? 0.82718 0.74053 0.55626 0.09061  0.03506  -0.01904 139 SER D CB  
3946 O OG  . SER D 125 ? 0.95263 0.86694 0.69658 0.07752  0.03575  -0.01331 139 SER D OG  
3947 N N   . LYS D 126 ? 1.01804 0.92277 0.75894 0.10098  0.01752  -0.02765 140 LYS D N   
3948 C CA  . LYS D 126 ? 1.10841 1.02082 0.85477 0.10482  0.01764  -0.02795 140 LYS D CA  
3949 C C   . LYS D 126 ? 1.21218 1.10832 0.95757 0.11327  0.00382  -0.03531 140 LYS D C   
3950 O O   . LYS D 126 ? 1.38318 1.27311 1.13872 0.10749  -0.00191 -0.03355 140 LYS D O   
3951 C CB  . LYS D 126 ? 0.86508 0.78553 0.62600 0.09021  0.02290  -0.01948 140 LYS D CB  
3952 N N   . SER D 127 ? 1.15880 1.04755 0.89157 0.12676  -0.00153 -0.04352 141 SER D N   
3953 C CA  . SER D 127 ? 1.33976 1.21176 1.06938 0.13609  -0.01466 -0.05152 141 SER D CA  
3954 C C   . SER D 127 ? 1.26484 1.11747 1.00155 0.12629  -0.02549 -0.05116 141 SER D C   
3955 O O   . SER D 127 ? 1.30971 1.14478 1.04152 0.13239  -0.03713 -0.05821 141 SER D O   
3956 C CB  . SER D 127 ? 1.35036 1.22936 1.08394 0.14319  -0.01476 -0.05257 141 SER D CB  
3957 N N   . ASP D 129 ? 1.21802 1.02339 0.93145 0.14923  -0.05605 -0.07446 143 ASP D N   
3958 C CA  . ASP D 129 ? 1.27373 1.05617 0.98532 0.14879  -0.07009 -0.08036 143 ASP D CA  
3959 C C   . ASP D 129 ? 1.26010 1.03614 0.97900 0.13350  -0.07245 -0.07570 143 ASP D C   
3960 O O   . ASP D 129 ? 1.13071 0.89214 0.84476 0.13319  -0.08142 -0.08070 143 ASP D O   
3961 C CB  . ASP D 129 ? 1.12789 0.89949 0.84498 0.15064  -0.07802 -0.08206 143 ASP D CB  
3962 N N   . LYS D 130 ? 1.16935 0.95694 0.89995 0.12085  -0.06429 -0.06632 144 LYS D N   
3963 C CA  . LYS D 130 ? 1.12058 0.90384 0.85933 0.10598  -0.06554 -0.06141 144 LYS D CA  
3964 C C   . LYS D 130 ? 1.08817 0.87549 0.81938 0.10656  -0.06169 -0.06192 144 LYS D C   
3965 O O   . LYS D 130 ? 1.08319 0.88375 0.80690 0.11352  -0.05260 -0.06146 144 LYS D O   
3966 C CB  . LYS D 130 ? 0.90896 0.70433 0.66153 0.09293  -0.05704 -0.05148 144 LYS D CB  
3967 N N   . SER D 131 ? 0.99722 0.77337 0.73037 0.09912  -0.06869 -0.06275 145 SER D N   
3968 C CA  . SER D 131 ? 0.99775 0.77694 0.72442 0.09921  -0.06604 -0.06296 145 SER D CA  
3969 C C   . SER D 131 ? 0.91612 0.68706 0.65130 0.08614  -0.07157 -0.06055 145 SER D C   
3970 O O   . SER D 131 ? 0.86644 0.62524 0.60884 0.07975  -0.08052 -0.06164 145 SER D O   
3971 C CB  . SER D 131 ? 0.90167 0.67417 0.61248 0.11376  -0.07181 -0.07235 145 SER D CB  
3972 O OG  . SER D 131 ? 0.96335 0.71716 0.67247 0.11570  -0.08565 -0.07959 145 SER D OG  
3973 N N   . VAL D 132 ? 0.93397 0.71190 0.66808 0.08229  -0.06596 -0.05714 146 VAL D N   
3974 C CA  . VAL D 132 ? 0.82073 0.59285 0.56162 0.07141  -0.07053 -0.05532 146 VAL D CA  
3975 C C   . VAL D 132 ? 0.85367 0.62291 0.58303 0.07852  -0.07403 -0.06031 146 VAL D C   
3976 O O   . VAL D 132 ? 0.84437 0.61928 0.56144 0.08986  -0.06976 -0.06289 146 VAL D O   
3977 C CB  . VAL D 132 ? 0.79206 0.57567 0.54453 0.05844  -0.06026 -0.04553 146 VAL D CB  
3978 C CG1 . VAL D 132 ? 0.70929 0.49629 0.47298 0.05106  -0.05699 -0.04060 146 VAL D CG1 
3979 C CG2 . VAL D 132 ? 0.68517 0.48285 0.43069 0.06283  -0.04801 -0.04179 146 VAL D CG2 
3980 N N   . CYS D 133 ? 0.76392 0.52478 0.49732 0.07159  -0.08199 -0.06164 147 CYS D N   
3981 C CA  . CYS D 133 ? 0.76225 0.52044 0.48624 0.07676  -0.08632 -0.06599 147 CYS D CA  
3982 C C   . CYS D 133 ? 0.77728 0.54393 0.50766 0.06781  -0.07994 -0.05908 147 CYS D C   
3983 O O   . CYS D 133 ? 0.83928 0.60592 0.58315 0.05507  -0.07980 -0.05423 147 CYS D O   
3984 C CB  . CYS D 133 ? 0.86072 0.60276 0.58337 0.07668  -0.10131 -0.07385 147 CYS D CB  
3985 S SG  . CYS D 133 ? 1.02365 0.75250 0.74057 0.08541  -0.10995 -0.08180 147 CYS D SG  
3986 N N   . LEU D 134 ? 0.77198 0.54564 0.49240 0.07463  -0.07463 -0.05863 148 LEU D N   
3987 C CA  . LEU D 134 ? 0.72665 0.50842 0.45123 0.06806  -0.06772 -0.05201 148 LEU D CA  
3988 C C   . LEU D 134 ? 0.73169 0.50865 0.44939 0.07182  -0.07564 -0.05660 148 LEU D C   
3989 O O   . LEU D 134 ? 0.88473 0.66341 0.58838 0.08289  -0.07500 -0.05986 148 LEU D O   
3990 C CB  . LEU D 134 ? 0.71335 0.50810 0.43225 0.07198  -0.05359 -0.04624 148 LEU D CB  
3991 C CG  . LEU D 134 ? 0.76142 0.56368 0.48201 0.06701  -0.04581 -0.03954 148 LEU D CG  
3992 C CD1 . LEU D 134 ? 0.59160 0.39649 0.32888 0.05220  -0.04191 -0.03263 148 LEU D CD1 
3993 C CD2 . LEU D 134 ? 0.68115 0.49382 0.39111 0.07401  -0.03364 -0.03582 148 LEU D CD2 
3994 N N   . PHE D 135 ? 0.72612 0.49760 0.45364 0.06255  -0.08320 -0.05692 149 PHE D N   
3995 C CA  . PHE D 135 ? 0.77710 0.54725 0.50104 0.06375  -0.08897 -0.05929 149 PHE D CA  
3996 C C   . PHE D 135 ? 0.85633 0.63752 0.58310 0.06008  -0.07823 -0.05116 149 PHE D C   
3997 O O   . PHE D 135 ? 0.75686 0.54236 0.49662 0.04906  -0.07252 -0.04460 149 PHE D O   
3998 C CB  . PHE D 135 ? 0.69237 0.45370 0.42651 0.05463  -0.10073 -0.06256 149 PHE D CB  
3999 C CG  . PHE D 135 ? 0.96038 0.72063 0.69133 0.05589  -0.10803 -0.06585 149 PHE D CG  
4000 C CD1 . PHE D 135 ? 0.93749 0.69957 0.65332 0.06788  -0.10845 -0.06928 149 PHE D CD1 
4001 C CD2 . PHE D 135 ? 0.97592 0.73411 0.71908 0.04496  -0.11446 -0.06544 149 PHE D CD2 
4002 C CE1 . PHE D 135 ? 0.88735 0.64913 0.60023 0.06920  -0.11548 -0.07222 149 PHE D CE1 
4003 C CE2 . PHE D 135 ? 0.90173 0.66022 0.64253 0.04617  -0.12136 -0.06852 149 PHE D CE2 
4004 C CZ  . PHE D 135 ? 0.83013 0.59039 0.55576 0.05842  -0.12200 -0.07187 149 PHE D CZ  
4005 N N   . THR D 136 ? 0.81571 0.60110 0.52993 0.06929  -0.07528 -0.05147 150 THR D N   
4006 C CA  . THR D 136 ? 0.73890 0.53394 0.45344 0.06739  -0.06407 -0.04355 150 THR D CA  
4007 C C   . THR D 136 ? 0.85370 0.64948 0.55842 0.07427  -0.06742 -0.04528 150 THR D C   
4008 O O   . THR D 136 ? 0.86922 0.65905 0.56576 0.08118  -0.07780 -0.05280 150 THR D O   
4009 C CB  . THR D 136 ? 0.81518 0.61770 0.52288 0.07202  -0.05132 -0.03916 150 THR D CB  
4010 O OG1 . THR D 136 ? 0.63290 0.44333 0.34015 0.06980  -0.04073 -0.03149 150 THR D OG1 
4011 C CG2 . THR D 136 ? 0.73493 0.53608 0.42536 0.08616  -0.05340 -0.04525 150 THR D CG2 
4012 N N   . ASP D 137 ? 0.79645 0.59947 0.50188 0.07221  -0.05839 -0.03808 151 ASP D N   
4013 C CA  . ASP D 137 ? 0.77414 0.57946 0.46967 0.07904  -0.05891 -0.03768 151 ASP D CA  
4014 C C   . ASP D 137 ? 0.82439 0.62507 0.52304 0.07813  -0.07208 -0.04304 151 ASP D C   
4015 O O   . ASP D 137 ? 0.87094 0.67217 0.55915 0.08597  -0.07586 -0.04520 151 ASP D O   
4016 C CB  . ASP D 137 ? 0.72861 0.53495 0.40509 0.09250  -0.05646 -0.04046 151 ASP D CB  
4017 C CG  . ASP D 137 ? 0.87855 0.69132 0.55128 0.09342  -0.04254 -0.03460 151 ASP D CG  
4018 O OD1 . ASP D 137 ? 0.90419 0.72170 0.58620 0.08488  -0.03329 -0.02686 151 ASP D OD1 
4019 O OD2 . ASP D 137 ? 0.87335 0.68681 0.53405 0.10239  -0.04072 -0.03783 151 ASP D OD2 
4020 N N   . PHE D 138 ? 0.82692 0.62347 0.53968 0.06840  -0.07923 -0.04509 152 PHE D N   
4021 C CA  . PHE D 138 ? 0.85366 0.64701 0.57074 0.06609  -0.09130 -0.04977 152 PHE D CA  
4022 C C   . PHE D 138 ? 0.89289 0.69297 0.61960 0.05954  -0.08737 -0.04340 152 PHE D C   
4023 O O   . PHE D 138 ? 0.89140 0.69738 0.61955 0.05784  -0.07550 -0.03574 152 PHE D O   
4024 C CB  . PHE D 138 ? 0.85483 0.64025 0.58154 0.05876  -0.10117 -0.05517 152 PHE D CB  
4025 C CG  . PHE D 138 ? 0.88321 0.66966 0.62512 0.04675  -0.09541 -0.04989 152 PHE D CG  
4026 C CD1 . PHE D 138 ? 0.80919 0.59344 0.55039 0.04695  -0.09070 -0.04929 152 PHE D CD1 
4027 C CD2 . PHE D 138 ? 0.88319 0.67335 0.64009 0.03540  -0.09488 -0.04567 152 PHE D CD2 
4028 C CE1 . PHE D 138 ? 0.78021 0.56581 0.53509 0.03584  -0.08568 -0.04435 152 PHE D CE1 
4029 C CE2 . PHE D 138 ? 0.79045 0.58179 0.56083 0.02418  -0.08960 -0.04089 152 PHE D CE2 
4030 C CZ  . PHE D 138 ? 0.85148 0.64045 0.62075 0.02427  -0.08508 -0.04013 152 PHE D CZ  
4031 N N   . ASP D 139 ? 0.87749 0.67672 0.61088 0.05578  -0.09740 -0.04673 153 ASP D N   
4032 C CA  . ASP D 139 ? 0.94318 0.74900 0.68403 0.05196  -0.09610 -0.04236 153 ASP D CA  
4033 C C   . ASP D 139 ? 0.97966 0.78725 0.74004 0.03762  -0.09525 -0.03911 153 ASP D C   
4034 O O   . ASP D 139 ? 0.91163 0.71403 0.67986 0.03054  -0.10130 -0.04271 153 ASP D O   
4035 C CB  . ASP D 139 ? 0.90670 0.71205 0.64228 0.05743  -0.10822 -0.04853 153 ASP D CB  
4036 C CG  . ASP D 139 ? 1.04027 0.85195 0.78778 0.05120  -0.11045 -0.04589 153 ASP D CG  
4037 O OD1 . ASP D 139 ? 1.09247 0.91043 0.83896 0.05358  -0.10234 -0.03946 153 ASP D OD1 
4038 O OD2 . ASP D 139 ? 1.12097 0.93139 0.87882 0.04395  -0.12038 -0.05028 153 ASP D OD2 
4039 N N   . SER D 140 ? 0.92288 0.73753 0.69073 0.03339  -0.08766 -0.03225 154 SER D N   
4040 C CA  . SER D 140 ? 0.86172 0.67901 0.64768 0.01976  -0.08478 -0.02843 154 SER D CA  
4041 C C   . SER D 140 ? 0.83785 0.65360 0.63511 0.01209  -0.09726 -0.03382 154 SER D C   
4042 O O   . SER D 140 ? 0.96726 0.78288 0.77850 0.00032  -0.09698 -0.03243 154 SER D O   
4043 C CB  . SER D 140 ? 0.75715 0.58202 0.54824 0.01753  -0.07473 -0.02068 154 SER D CB  
4044 O OG  . SER D 140 ? 0.68515 0.51103 0.46981 0.02004  -0.06161 -0.01462 154 SER D OG  
4045 N N   . GLN D 141 ? 0.97979 0.79456 0.77113 0.01806  -0.10819 -0.03993 155 GLN D N   
4046 C CA  . GLN D 141 ? 1.04570 0.85898 0.84676 0.01077  -0.12062 -0.04562 155 GLN D CA  
4047 C C   . GLN D 141 ? 0.94756 0.75060 0.74716 0.00821  -0.12842 -0.05182 155 GLN D C   
4048 O O   . GLN D 141 ? 1.06879 0.86895 0.87563 0.00152  -0.13906 -0.05685 155 GLN D O   
4049 C CB  . GLN D 141 ? 1.04715 0.86375 0.84232 0.01790  -0.12974 -0.05006 155 GLN D CB  
4050 N N   . THR D 142 ? 0.94328 0.74078 0.73378 0.01326  -0.12344 -0.05157 156 THR D N   
4051 C CA  . THR D 142 ? 0.97495 0.76206 0.76346 0.01183  -0.13016 -0.05713 156 THR D CA  
4052 C C   . THR D 142 ? 0.84656 0.63242 0.64881 -0.00050 -0.12566 -0.05296 156 THR D C   
4053 O O   . THR D 142 ? 0.86898 0.65979 0.67444 -0.00261 -0.11376 -0.04595 156 THR D O   
4054 C CB  . THR D 142 ? 0.96044 0.74291 0.73215 0.02425  -0.12731 -0.05935 156 THR D CB  
4055 O OG1 . THR D 142 ? 0.97151 0.75630 0.72999 0.03566  -0.13018 -0.06229 156 THR D OG1 
4056 C CG2 . THR D 142 ? 0.94862 0.71944 0.71714 0.02434  -0.13582 -0.06622 156 THR D CG2 
4057 N N   . ASN D 143 ? 0.94512 0.72423 0.75502 -0.00888 -0.13524 -0.05724 157 ASN D N   
4058 C CA  . ASN D 143 ? 0.96933 0.74591 0.79156 -0.02083 -0.13281 -0.05401 157 ASN D CA  
4059 C C   . ASN D 143 ? 0.98235 0.74813 0.79730 -0.01727 -0.13502 -0.05726 157 ASN D C   
4060 O O   . ASN D 143 ? 1.08517 0.84280 0.88889 -0.00914 -0.14339 -0.06440 157 ASN D O   
4061 C CB  . ASN D 143 ? 0.82221 0.59801 0.65785 -0.03326 -0.14180 -0.05616 157 ASN D CB  
4062 N N   . VAL D 144 ? 0.94420 0.71017 0.76554 -0.02320 -0.12744 -0.05207 158 VAL D N   
4063 C CA  . VAL D 144 ? 1.01280 0.76942 0.82946 -0.02092 -0.12887 -0.05419 158 VAL D CA  
4064 C C   . VAL D 144 ? 0.97904 0.72996 0.80860 -0.03454 -0.13367 -0.05351 158 VAL D C   
4065 O O   . VAL D 144 ? 1.12713 0.88484 0.96944 -0.04540 -0.12763 -0.04730 158 VAL D O   
4066 C CB  . VAL D 144 ? 1.02336 0.78543 0.83562 -0.01569 -0.11595 -0.04863 158 VAL D CB  
4067 C CG1 . VAL D 144 ? 0.87862 0.63168 0.68477 -0.01113 -0.11818 -0.05165 158 VAL D CG1 
4068 C CG2 . VAL D 144 ? 0.98241 0.75142 0.78299 -0.00399 -0.10997 -0.04798 158 VAL D CG2 
4069 N N   . SER D 145 ? 1.00610 0.74417 0.83194 -0.03407 -0.14445 -0.05988 159 SER D N   
4070 C CA  . SER D 145 ? 1.06566 0.79624 0.90210 -0.04669 -0.15047 -0.05982 159 SER D CA  
4071 C C   . SER D 145 ? 1.07044 0.79550 0.90602 -0.04629 -0.14651 -0.05736 159 SER D C   
4072 O O   . SER D 145 ? 1.07468 0.79264 0.89848 -0.03533 -0.14836 -0.06142 159 SER D O   
4073 C CB  . SER D 145 ? 1.12730 0.84587 0.96025 -0.04741 -0.16524 -0.06822 159 SER D CB  
4074 O OG  . SER D 145 ? 1.25788 0.96438 1.07781 -0.03705 -0.17027 -0.07406 159 SER D OG  
4075 N N   . GLN D 146 ? 1.19867 0.92745 1.04666 -0.05802 -0.14115 -0.05085 160 GLN D N   
4076 C CA  . GLN D 146 ? 1.21220 0.93586 1.06078 -0.05905 -0.13843 -0.04830 160 GLN D CA  
4077 C C   . GLN D 146 ? 1.21348 0.92014 1.05714 -0.05797 -0.15093 -0.05487 160 GLN D C   
4078 O O   . GLN D 146 ? 1.22069 0.92023 1.06870 -0.06582 -0.16066 -0.05820 160 GLN D O   
4079 C CB  . GLN D 146 ? 0.87454 0.60474 0.73788 -0.07342 -0.13198 -0.04055 160 GLN D CB  
4080 N N   . SER D 147 ? 1.20549 0.90566 1.03985 -0.04812 -0.15060 -0.05687 161 SER D N   
4081 C CA  . SER D 147 ? 1.24166 0.92447 1.06915 -0.04469 -0.16222 -0.06371 161 SER D CA  
4082 C C   . SER D 147 ? 1.36727 1.04113 1.20511 -0.05876 -0.16820 -0.06175 161 SER D C   
4083 O O   . SER D 147 ? 1.38006 1.06052 1.22859 -0.06842 -0.16155 -0.05443 161 SER D O   
4084 C CB  . SER D 147 ? 1.27071 0.94993 1.08782 -0.03179 -0.15920 -0.06520 161 SER D CB  
4085 O OG  . SER D 147 ? 1.34715 1.00856 1.15850 -0.02912 -0.17008 -0.07125 161 SER D OG  
4086 N N   . LYS D 148 ? 1.37539 1.03377 1.20948 -0.06014 -0.18096 -0.06843 162 LYS D N   
4087 C CA  . LYS D 148 ? 1.31990 0.96676 1.16146 -0.07269 -0.18818 -0.06749 162 LYS D CA  
4088 C C   . LYS D 148 ? 1.42239 1.05393 1.25703 -0.06701 -0.19256 -0.06957 162 LYS D C   
4089 O O   . LYS D 148 ? 1.40422 1.02335 1.24297 -0.07618 -0.19957 -0.06924 162 LYS D O   
4090 C CB  . LYS D 148 ? 1.13124 0.77026 0.97391 -0.07978 -0.19975 -0.07318 162 LYS D CB  
4091 N N   . ASP D 149 ? 1.39965 1.03178 1.22376 -0.05205 -0.18863 -0.07168 163 ASP D N   
4092 C CA  . ASP D 149 ? 1.27218 0.89238 1.09017 -0.04512 -0.19105 -0.07301 163 ASP D CA  
4093 C C   . ASP D 149 ? 1.34726 0.97905 1.17209 -0.04669 -0.17970 -0.06443 163 ASP D C   
4094 O O   . ASP D 149 ? 1.44856 1.09744 1.27553 -0.04425 -0.16866 -0.06015 163 ASP D O   
4095 C CB  . ASP D 149 ? 1.19663 0.81119 0.99897 -0.02743 -0.19356 -0.08087 163 ASP D CB  
4096 N N   . SER D 150 ? 1.40514 1.02728 1.23306 -0.05090 -0.18260 -0.06190 164 SER D N   
4097 C CA  . SER D 150 ? 1.24804 0.88086 1.08381 -0.05469 -0.17287 -0.05341 164 SER D CA  
4098 C C   . SER D 150 ? 1.31432 0.95530 1.14274 -0.03999 -0.16488 -0.05328 164 SER D C   
4099 O O   . SER D 150 ? 1.33944 0.99331 1.17413 -0.04241 -0.15499 -0.04620 164 SER D O   
4100 C CB  . SER D 150 ? 1.20520 0.82470 1.04587 -0.06340 -0.17916 -0.05075 164 SER D CB  
4101 N N   . ASP D 151 ? 1.10572 0.74025 0.92111 -0.02521 -0.16872 -0.06096 165 ASP D N   
4102 C CA  . ASP D 151 ? 1.16604 0.80744 0.97385 -0.01076 -0.16197 -0.06155 165 ASP D CA  
4103 C C   . ASP D 151 ? 1.25052 0.90712 1.05286 -0.00246 -0.15346 -0.06245 165 ASP D C   
4104 O O   . ASP D 151 ? 1.17442 0.84107 0.97243 0.00737  -0.14530 -0.06122 165 ASP D O   
4105 C CB  . ASP D 151 ? 1.25376 0.87742 1.04988 0.00146  -0.17146 -0.06953 165 ASP D CB  
4106 N N   . VAL D 152 ? 1.17796 0.83682 0.98024 -0.00607 -0.15511 -0.06443 166 VAL D N   
4107 C CA  . VAL D 152 ? 1.12674 0.79910 0.92341 0.00140  -0.14753 -0.06496 166 VAL D CA  
4108 C C   . VAL D 152 ? 1.06656 0.75261 0.87439 -0.01074 -0.14004 -0.05786 166 VAL D C   
4109 O O   . VAL D 152 ? 1.08507 0.76695 0.90051 -0.02226 -0.14550 -0.05736 166 VAL D O   
4110 C CB  . VAL D 152 ? 1.16448 0.82794 0.94915 0.01041  -0.15606 -0.07425 166 VAL D CB  
4111 C CG1 . VAL D 152 ? 1.16504 0.81612 0.95387 0.00013  -0.16753 -0.07746 166 VAL D CG1 
4112 C CG2 . VAL D 152 ? 1.10588 0.78364 0.88547 0.01651  -0.14827 -0.07382 166 VAL D CG2 
4113 N N   . TYR D 153 ? 0.90502 0.60734 0.71366 -0.00817 -0.12747 -0.05253 167 TYR D N   
4114 C CA  . TYR D 153 ? 0.89816 0.61395 0.71698 -0.01881 -0.11873 -0.04530 167 TYR D CA  
4115 C C   . TYR D 153 ? 0.86584 0.58973 0.67827 -0.01278 -0.11485 -0.04682 167 TYR D C   
4116 O O   . TYR D 153 ? 0.85050 0.57598 0.65092 0.00048  -0.11306 -0.05059 167 TYR D O   
4117 C CB  . TYR D 153 ? 0.74344 0.47150 0.56823 -0.02172 -0.10686 -0.03751 167 TYR D CB  
4118 C CG  . TYR D 153 ? 0.90463 0.62566 0.73446 -0.02584 -0.11026 -0.03579 167 TYR D CG  
4119 C CD1 . TYR D 153 ? 1.08009 0.79938 0.92244 -0.04090 -0.11177 -0.03090 167 TYR D CD1 
4120 C CD2 . TYR D 153 ? 0.87832 0.59447 0.70020 -0.01444 -0.11211 -0.03907 167 TYR D CD2 
4121 C CE1 . TYR D 153 ? 0.96681 0.67926 0.81323 -0.04465 -0.11517 -0.02897 167 TYR D CE1 
4122 C CE2 . TYR D 153 ? 1.00993 0.71932 0.83616 -0.01758 -0.11556 -0.03731 167 TYR D CE2 
4123 C CZ  . TYR D 153 ? 1.11513 0.82244 0.95345 -0.03278 -0.11717 -0.03209 167 TYR D CZ  
4124 O OH  . TYR D 153 ? 1.01377 0.71408 0.85593 -0.03591 -0.12077 -0.02996 167 TYR D OH  
4125 N N   . ILE D 154 ? 0.78341 0.51262 0.60379 -0.02243 -0.11353 -0.04381 168 ILE D N   
4126 C CA  . ILE D 154 ? 0.79132 0.52804 0.60687 -0.01794 -0.11032 -0.04457 168 ILE D CA  
4127 C C   . ILE D 154 ? 0.71380 0.46297 0.54059 -0.02870 -0.10078 -0.03666 168 ILE D C   
4128 O O   . ILE D 154 ? 0.78578 0.53371 0.62424 -0.04140 -0.10366 -0.03434 168 ILE D O   
4129 C CB  . ILE D 154 ? 0.95349 0.68088 0.76526 -0.01683 -0.12247 -0.05174 168 ILE D CB  
4130 C CG1 . ILE D 154 ? 0.98656 0.70277 0.78427 -0.00370 -0.13047 -0.06019 168 ILE D CG1 
4131 C CG2 . ILE D 154 ? 0.99143 0.72820 0.80233 -0.01595 -0.11893 -0.05069 168 ILE D CG2 
4132 C CD1 . ILE D 154 ? 1.14058 0.84532 0.93498 -0.00402 -0.14383 -0.06780 168 ILE D CD1 
4133 N N   . THR D 155 ? 0.72308 0.48393 0.54612 -0.02384 -0.08937 -0.03261 169 THR D N   
4134 C CA  . THR D 155 ? 0.60573 0.37783 0.43800 -0.03293 -0.07970 -0.02539 169 THR D CA  
4135 C C   . THR D 155 ? 0.67428 0.44793 0.50683 -0.03364 -0.08279 -0.02697 169 THR D C   
4136 O O   . THR D 155 ? 0.80968 0.57766 0.63346 -0.02552 -0.09082 -0.03331 169 THR D O   
4137 C CB  . THR D 155 ? 0.64236 0.42559 0.46994 -0.02780 -0.06616 -0.02035 169 THR D CB  
4138 O OG1 . THR D 155 ? 0.73771 0.52308 0.55262 -0.01581 -0.06477 -0.02321 169 THR D OG1 
4139 C CG2 . THR D 155 ? 0.60978 0.39233 0.43487 -0.02412 -0.06389 -0.02001 169 THR D CG2 
4140 N N   . ASP D 156 ? 0.74954 0.53140 0.59224 -0.04330 -0.07621 -0.02118 170 ASP D N   
4141 C CA  . ASP D 156 ? 0.66692 0.45208 0.51094 -0.04398 -0.07790 -0.02182 170 ASP D CA  
4142 C C   . ASP D 156 ? 0.73401 0.52491 0.56601 -0.03216 -0.07124 -0.02131 170 ASP D C   
4143 O O   . ASP D 156 ? 0.82600 0.61880 0.64908 -0.02423 -0.06499 -0.02042 170 ASP D O   
4144 C CB  . ASP D 156 ? 0.57483 0.36705 0.43352 -0.05762 -0.07248 -0.01583 170 ASP D CB  
4145 N N   . LYS D 157 ? 0.87174 0.66576 0.70343 -0.03098 -0.07270 -0.02183 171 LYS D N   
4146 C CA  . LYS D 157 ? 0.72142 0.52126 0.54263 -0.02120 -0.06568 -0.02012 171 LYS D CA  
4147 C C   . LYS D 157 ? 0.66166 0.47003 0.48568 -0.02476 -0.05099 -0.01207 171 LYS D C   
4148 O O   . LYS D 157 ? 0.69769 0.50937 0.53417 -0.03637 -0.04641 -0.00742 171 LYS D O   
4149 C CB  . LYS D 157 ? 0.71549 0.51763 0.53782 -0.02061 -0.06997 -0.02136 171 LYS D CB  
4150 C CG  . LYS D 157 ? 0.96023 0.75700 0.77115 -0.01010 -0.08044 -0.02879 171 LYS D CG  
4151 C CD  . LYS D 157 ? 0.94034 0.74175 0.75253 -0.00924 -0.08287 -0.02878 171 LYS D CD  
4152 C CE  . LYS D 157 ? 0.66646 0.47005 0.49539 -0.02249 -0.08638 -0.02751 171 LYS D CE  
4153 N NZ  . LYS D 157 ? 0.98954 0.79829 0.82022 -0.02113 -0.08984 -0.02816 171 LYS D NZ  
4154 N N   . CYS D 158 ? 0.68244 0.49440 0.49435 -0.01494 -0.04351 -0.01049 172 CYS D N   
4155 C CA  . CYS D 158 ? 0.61175 0.43146 0.42436 -0.01758 -0.02928 -0.00309 172 CYS D CA  
4156 C C   . CYS D 158 ? 0.65576 0.47888 0.45594 -0.00770 -0.02361 -0.00158 172 CYS D C   
4157 O O   . CYS D 158 ? 0.65973 0.48035 0.44658 0.00385  -0.02694 -0.00577 172 CYS D O   
4158 C CB  . CYS D 158 ? 0.74431 0.56493 0.55501 -0.01716 -0.02431 -0.00196 172 CYS D CB  
4159 S SG  . CYS D 158 ? 0.80113 0.63038 0.62164 -0.02864 -0.00980 0.00698  172 CYS D SG  
4160 N N   . VAL D 159 ? 0.61365 0.44205 0.41778 -0.01216 -0.01509 0.00436  173 VAL D N   
4161 C CA  . VAL D 159 ? 0.53810 0.36906 0.33107 -0.00378 -0.00948 0.00669  173 VAL D CA  
4162 C C   . VAL D 159 ? 0.56024 0.39627 0.34818 -0.00378 0.00469  0.01286  173 VAL D C   
4163 O O   . VAL D 159 ? 0.63443 0.47422 0.43180 -0.01372 0.01309  0.01838  173 VAL D O   
4164 C CB  . VAL D 159 ? 0.67928 0.51197 0.47917 -0.00779 -0.00988 0.00904  173 VAL D CB  
4165 C CG1 . VAL D 159 ? 0.65678 0.49087 0.44381 0.00211  -0.00539 0.01115  173 VAL D CG1 
4166 C CG2 . VAL D 159 ? 0.67772 0.50685 0.48518 -0.01026 -0.02362 0.00319  173 VAL D CG2 
4167 N N   . LEU D 160 ? 0.61416 0.45064 0.38709 0.00701  0.00757  0.01189  174 LEU D N   
4168 C CA  . LEU D 160 ? 0.66145 0.50320 0.42791 0.00770  0.02113  0.01766  174 LEU D CA  
4169 C C   . LEU D 160 ? 0.76210 0.60453 0.51713 0.01472  0.02643  0.02078  174 LEU D C   
4170 O O   . LEU D 160 ? 0.65611 0.49528 0.40455 0.02243  0.01882  0.01730  174 LEU D O   
4171 C CB  . LEU D 160 ? 0.58879 0.43192 0.34695 0.01393  0.02213  0.01497  174 LEU D CB  
4172 C CG  . LEU D 160 ? 0.77183 0.61236 0.51440 0.02793  0.01624  0.00920  174 LEU D CG  
4173 C CD1 . LEU D 160 ? 0.70620 0.55066 0.43436 0.03523  0.02608  0.01306  174 LEU D CD1 
4174 C CD2 . LEU D 160 ? 0.73488 0.57479 0.47618 0.03116  0.01222  0.00436  174 LEU D CD2 
4175 N N   . ASP D 161 ? 0.80598 0.65253 0.55833 0.01182  0.03961  0.02752  175 ASP D N   
4176 C CA  . ASP D 161 ? 0.72935 0.57580 0.47210 0.01644  0.04623  0.03198  175 ASP D CA  
4177 C C   . ASP D 161 ? 0.79859 0.64874 0.52871 0.02049  0.05752  0.03563  175 ASP D C   
4178 O O   . ASP D 161 ? 0.72163 0.57579 0.45620 0.01259  0.06783  0.04048  175 ASP D O   
4179 C CB  . ASP D 161 ? 0.80471 0.65138 0.55857 0.00669  0.05165  0.03742  175 ASP D CB  
4180 C CG  . ASP D 161 ? 0.85005 0.69458 0.59548 0.01240  0.05467  0.04082  175 ASP D CG  
4181 O OD1 . ASP D 161 ? 0.93142 0.77559 0.66117 0.02145  0.05869  0.04209  175 ASP D OD1 
4182 O OD2 . ASP D 161 ? 0.90180 0.74516 0.65629 0.00791  0.05301  0.04230  175 ASP D OD2 
4183 N N   . MET D 162 ? 0.72687 0.57616 0.44114 0.03244  0.05566  0.03324  176 MET D N   
4184 C CA  . MET D 162 ? 0.80735 0.66043 0.50801 0.03697  0.06648  0.03685  176 MET D CA  
4185 C C   . MET D 162 ? 0.77568 0.62696 0.47022 0.03687  0.07473  0.04355  176 MET D C   
4186 O O   . MET D 162 ? 0.90527 0.75332 0.58851 0.04582  0.07166  0.04310  176 MET D O   
4187 C CB  . MET D 162 ? 0.73994 0.59308 0.42615 0.04963  0.06095  0.03118  176 MET D CB  
4188 C CG  . MET D 162 ? 0.70877 0.56221 0.40068 0.05045  0.05213  0.02415  176 MET D CG  
4189 S SD  . MET D 162 ? 0.94160 0.79388 0.61690 0.06581  0.04415  0.01626  176 MET D SD  
4190 C CE  . MET D 162 ? 0.66676 0.52759 0.33076 0.06879  0.05793  0.01996  176 MET D CE  
4191 N N   . ARG D 163 ? 0.79655 0.64962 0.49843 0.02659  0.08527  0.04987  177 ARG D N   
4192 C CA  . ARG D 163 ? 0.91082 0.76054 0.61026 0.02462  0.09234  0.05619  177 ARG D CA  
4193 C C   . ARG D 163 ? 0.87854 0.72722 0.55865 0.03365  0.09886  0.05945  177 ARG D C   
4194 O O   . ARG D 163 ? 0.98108 0.82497 0.65391 0.03945  0.09731  0.06121  177 ARG D O   
4195 C CB  . ARG D 163 ? 0.81787 0.66962 0.52833 0.01145  0.10288  0.06183  177 ARG D CB  
4196 N N   . SER D 164 ? 0.81702 0.67057 0.48846 0.03505  0.10610  0.06034  178 SER D N   
4197 C CA  . SER D 164 ? 0.94212 0.79523 0.59479 0.04269  0.11322  0.06380  178 SER D CA  
4198 C C   . SER D 164 ? 1.06595 0.91595 0.70622 0.05595  0.10351  0.05932  178 SER D C   
4199 O O   . SER D 164 ? 1.15328 1.00118 0.77780 0.06276  0.10799  0.06263  178 SER D O   
4200 C CB  . SER D 164 ? 0.68771 0.54838 0.33451 0.04161  0.12186  0.06461  178 SER D CB  
4201 N N   . MET D 165 ? 0.90103 0.75036 0.54760 0.05946  0.09032  0.05195  179 MET D N   
4202 C CA  . MET D 165 ? 0.85895 0.70571 0.49433 0.07163  0.08017  0.04674  179 MET D CA  
4203 C C   . MET D 165 ? 0.88731 0.72899 0.52961 0.07265  0.06968  0.04467  179 MET D C   
4204 O O   . MET D 165 ? 1.01812 0.85773 0.65200 0.08228  0.06032  0.04011  179 MET D O   
4205 C CB  . MET D 165 ? 0.79449 0.64454 0.42879 0.07649  0.07276  0.03884  179 MET D CB  
4206 C CG  . MET D 165 ? 0.84492 0.70115 0.46915 0.07886  0.08181  0.03983  179 MET D CG  
4207 S SD  . MET D 165 ? 1.20351 1.06320 0.82734 0.08518  0.07277  0.03016  179 MET D SD  
4208 C CE  . MET D 165 ? 1.05773 0.91025 0.67754 0.09452  0.05659  0.02293  179 MET D CE  
4209 N N   . ASP D 166 ? 0.98520 0.82549 0.64259 0.06295  0.07100  0.04769  180 ASP D N   
4210 C CA  . ASP D 166 ? 1.00104 0.83800 0.66708 0.06288  0.06132  0.04570  180 ASP D CA  
4211 C C   . ASP D 166 ? 0.91688 0.75372 0.58567 0.06754  0.04664  0.03671  180 ASP D C   
4212 O O   . ASP D 166 ? 1.02685 0.86144 0.69249 0.07404  0.03720  0.03357  180 ASP D O   
4213 C CB  . ASP D 166 ? 0.86081 0.69406 0.51567 0.06998  0.06283  0.04992  180 ASP D CB  
4214 N N   . PHE D 167 ? 0.78778 0.62690 0.46223 0.06419  0.04463  0.03252  181 PHE D N   
4215 C CA  . PHE D 167 ? 0.81583 0.65375 0.49209 0.06822  0.03140  0.02382  181 PHE D CA  
4216 C C   . PHE D 167 ? 0.83341 0.67161 0.52830 0.05735  0.02758  0.02168  181 PHE D C   
4217 O O   . PHE D 167 ? 0.85012 0.69121 0.55070 0.05055  0.03478  0.02398  181 PHE D O   
4218 C CB  . PHE D 167 ? 0.80131 0.64084 0.46384 0.07675  0.03174  0.01998  181 PHE D CB  
4219 C CG  . PHE D 167 ? 0.75510 0.59220 0.41795 0.08159  0.01838  0.01070  181 PHE D CG  
4220 C CD1 . PHE D 167 ? 0.75876 0.59267 0.41314 0.09050  0.00809  0.00573  181 PHE D CD1 
4221 C CD2 . PHE D 167 ? 0.84180 0.67947 0.51294 0.07729  0.01606  0.00693  181 PHE D CD2 
4222 C CE1 . PHE D 167 ? 0.93403 0.76487 0.58813 0.09461  -0.00415 -0.00309 181 PHE D CE1 
4223 C CE2 . PHE D 167 ? 0.85148 0.68547 0.52225 0.08179  0.00382  -0.00164 181 PHE D CE2 
4224 C CZ  . PHE D 167 ? 0.81499 0.64533 0.47717 0.09025  -0.00622 -0.00680 181 PHE D CZ  
4225 N N   . LYS D 168 ? 0.73429 0.56990 0.43846 0.05549  0.01629  0.01743  182 LYS D N   
4226 C CA  . LYS D 168 ? 0.70335 0.53841 0.42402 0.04592  0.01056  0.01444  182 LYS D CA  
4227 C C   . LYS D 168 ? 0.79429 0.62591 0.51233 0.05135  -0.00233 0.00559  182 LYS D C   
4228 O O   . LYS D 168 ? 0.86166 0.69117 0.56864 0.06116  -0.00942 0.00136  182 LYS D O   
4229 C CB  . LYS D 168 ? 0.60397 0.43891 0.33866 0.03806  0.00770  0.01632  182 LYS D CB  
4230 C CG  . LYS D 168 ? 0.68932 0.52673 0.42826 0.03161  0.02031  0.02472  182 LYS D CG  
4231 C CD  . LYS D 168 ? 0.86456 0.70162 0.60735 0.03187  0.01778  0.02658  182 LYS D CD  
4232 C CE  . LYS D 168 ? 0.91602 0.75417 0.66028 0.02720  0.03083  0.03487  182 LYS D CE  
4233 N NZ  . LYS D 168 ? 0.92834 0.76575 0.67205 0.03095  0.02909  0.03699  182 LYS D NZ  
4234 N N   . SER D 169 ? 0.70402 0.53467 0.43172 0.04500  -0.00537 0.00279  183 SER D N   
4235 C CA  . SER D 169 ? 0.63129 0.45720 0.35720 0.04931  -0.01770 -0.00566 183 SER D CA  
4236 C C   . SER D 169 ? 0.66209 0.48577 0.40429 0.03841  -0.02281 -0.00740 183 SER D C   
4237 O O   . SER D 169 ? 0.65491 0.48161 0.40671 0.02933  -0.01507 -0.00255 183 SER D O   
4238 C CB  . SER D 169 ? 0.68061 0.50662 0.39282 0.05867  -0.01567 -0.00865 183 SER D CB  
4239 O OG  . SER D 169 ? 0.76143 0.59131 0.47787 0.05346  -0.00618 -0.00479 183 SER D OG  
4240 N N   . ASN D 170 ? 0.65384 0.47203 0.39858 0.03917  -0.03603 -0.01435 184 ASN D N   
4241 C CA  . ASN D 170 ? 0.57519 0.38948 0.33303 0.03012  -0.04290 -0.01720 184 ASN D CA  
4242 C C   . ASN D 170 ? 0.70936 0.51941 0.46137 0.03490  -0.04598 -0.02202 184 ASN D C   
4243 O O   . ASN D 170 ? 0.66204 0.47086 0.39962 0.04635  -0.04712 -0.02576 184 ASN D O   
4244 C CB  . ASN D 170 ? 0.63327 0.44347 0.39671 0.02792  -0.05582 -0.02231 184 ASN D CB  
4245 C CG  . ASN D 170 ? 0.65528 0.47039 0.42722 0.02214  -0.05331 -0.01771 184 ASN D CG  
4246 O OD1 . ASN D 170 ? 0.84298 0.66240 0.62465 0.01351  -0.04447 -0.01135 184 ASN D OD1 
4247 N ND2 . ASN D 170 ? 0.67193 0.48667 0.44020 0.02704  -0.06115 -0.02107 184 ASN D ND2 
4248 N N   . SER D 171 ? 0.68408 0.49199 0.44723 0.02626  -0.04724 -0.02187 185 SER D N   
4249 C CA  . SER D 171 ? 0.68871 0.49171 0.44759 0.03060  -0.05130 -0.02668 185 SER D CA  
4250 C C   . SER D 171 ? 0.67396 0.47224 0.44686 0.01973  -0.05677 -0.02732 185 SER D C   
4251 O O   . SER D 171 ? 0.71280 0.51420 0.49878 0.00816  -0.05343 -0.02232 185 SER D O   
4252 C CB  . SER D 171 ? 0.64477 0.45385 0.39648 0.03552  -0.03991 -0.02320 185 SER D CB  
4253 O OG  . SER D 171 ? 0.68924 0.50406 0.45214 0.02506  -0.03051 -0.01616 185 SER D OG  
4254 N N   . ALA D 172 ? 0.69350 0.48378 0.46295 0.02377  -0.06529 -0.03362 186 ALA D N   
4255 C CA  . ALA D 172 ? 0.69452 0.47883 0.47490 0.01499  -0.07076 -0.03451 186 ALA D CA  
4256 C C   . ALA D 172 ? 0.68577 0.46621 0.45911 0.02249  -0.07163 -0.03793 186 ALA D C   
4257 O O   . ALA D 172 ? 0.81036 0.58862 0.57014 0.03482  -0.07391 -0.04305 186 ALA D O   
4258 C CB  . ALA D 172 ? 0.62526 0.40051 0.41041 0.01058  -0.08432 -0.03999 186 ALA D CB  
4259 N N   . VAL D 173 ? 0.62037 0.40038 0.40276 0.01532  -0.06972 -0.03508 187 VAL D N   
4260 C CA  . VAL D 173 ? 0.69805 0.47577 0.47545 0.02188  -0.06955 -0.03737 187 VAL D CA  
4261 C C   . VAL D 173 ? 0.71828 0.48330 0.50075 0.01803  -0.08144 -0.04197 187 VAL D C   
4262 O O   . VAL D 173 ? 0.74950 0.51152 0.54395 0.00591  -0.08500 -0.03971 187 VAL D O   
4263 C CB  . VAL D 173 ? 0.73882 0.52741 0.52151 0.01768  -0.05681 -0.02989 187 VAL D CB  
4264 C CG1 . VAL D 173 ? 0.76134 0.54909 0.53876 0.02553  -0.05657 -0.03238 187 VAL D CG1 
4265 C CG2 . VAL D 173 ? 0.62478 0.42489 0.40263 0.02002  -0.04491 -0.02491 187 VAL D CG2 
4266 N N   . ALA D 174 ? 0.76302 0.52021 0.53596 0.02839  -0.08760 -0.04854 188 ALA D N   
4267 C CA  . ALA D 174 ? 0.73270 0.47645 0.50873 0.02605  -0.09855 -0.05300 188 ALA D CA  
4268 C C   . ALA D 174 ? 0.81537 0.55778 0.58554 0.03510  -0.09706 -0.05494 188 ALA D C   
4269 O O   . ALA D 174 ? 0.83150 0.57897 0.59036 0.04718  -0.09259 -0.05726 188 ALA D O   
4270 C CB  . ALA D 174 ? 0.77006 0.50125 0.53959 0.02973  -0.11161 -0.06138 188 ALA D CB  
4271 N N   . TRP D 175 ? 0.75911 0.49508 0.53695 0.02931  -0.10075 -0.05387 189 TRP D N   
4272 C CA  . TRP D 175 ? 0.88462 0.61792 0.65770 0.03797  -0.10096 -0.05614 189 TRP D CA  
4273 C C   . TRP D 175 ? 0.91545 0.63323 0.69358 0.03299  -0.11198 -0.05870 189 TRP D C   
4274 O O   . TRP D 175 ? 0.84637 0.55722 0.63251 0.02161  -0.11810 -0.05781 189 TRP D O   
4275 C CB  . TRP D 175 ? 0.82948 0.57801 0.60740 0.03650  -0.08802 -0.04868 189 TRP D CB  
4276 C CG  . TRP D 175 ? 0.77442 0.52530 0.56712 0.02164  -0.08568 -0.04148 189 TRP D CG  
4277 C CD1 . TRP D 175 ? 0.86032 0.60695 0.65952 0.01775  -0.08822 -0.03966 189 TRP D CD1 
4278 C CD2 . TRP D 175 ? 0.84011 0.59800 0.64281 0.00865  -0.08050 -0.03517 189 TRP D CD2 
4279 N NE1 . TRP D 175 ? 0.87484 0.62578 0.68729 0.00276  -0.08481 -0.03252 189 TRP D NE1 
4280 C CE2 . TRP D 175 ? 0.85833 0.61623 0.67328 -0.00305 -0.07993 -0.02983 189 TRP D CE2 
4281 C CE3 . TRP D 175 ? 0.79640 0.56054 0.59870 0.00609  -0.07626 -0.03349 189 TRP D CE3 
4282 C CZ2 . TRP D 175 ? 0.69956 0.46370 0.52624 -0.01729 -0.07509 -0.02327 189 TRP D CZ2 
4283 C CZ3 . TRP D 175 ? 0.73175 0.50176 0.54597 -0.00766 -0.07151 -0.02695 189 TRP D CZ3 
4284 C CH2 . TRP D 175 ? 0.80454 0.57462 0.63077 -0.01925 -0.07087 -0.02210 189 TRP D CH2 
4285 N N   . SER D 176 ? 0.95418 0.66661 0.72735 0.04175  -0.11436 -0.06185 190 SER D N   
4286 C CA  . SER D 176 ? 1.04941 0.74559 0.82531 0.03911  -0.12490 -0.06459 190 SER D CA  
4287 C C   . SER D 176 ? 1.03798 0.73450 0.81007 0.04911  -0.12302 -0.06546 190 SER D C   
4288 O O   . SER D 176 ? 0.97296 0.67812 0.73633 0.06140  -0.11710 -0.06762 190 SER D O   
4289 C CB  . SER D 176 ? 1.06830 0.74691 0.83620 0.04274  -0.13806 -0.07359 190 SER D CB  
4290 O OG  . SER D 176 ? 1.17726 0.83959 0.94273 0.04606  -0.14729 -0.07788 190 SER D OG  
4291 N N   . ASN D 177 ? 1.12464 0.81191 0.90327 0.04377  -0.12820 -0.06371 191 ASN D N   
4292 C CA  . ASN D 177 ? 1.05932 0.74433 0.83463 0.05348  -0.12857 -0.06511 191 ASN D CA  
4293 C C   . ASN D 177 ? 1.17933 0.84516 0.94333 0.06479  -0.14032 -0.07494 191 ASN D C   
4294 O O   . ASN D 177 ? 1.21224 0.87696 0.97030 0.07688  -0.14028 -0.07799 191 ASN D O   
4295 C CB  . ASN D 177 ? 0.96008 0.64439 0.74743 0.04282  -0.12839 -0.05806 191 ASN D CB  
4296 N N   . LYS D 178 ? 1.16465 0.81574 0.92554 0.06120  -0.15027 -0.08012 192 LYS D N   
4297 C CA  . LYS D 178 ? 1.23244 0.86371 0.98229 0.07081  -0.16199 -0.08982 192 LYS D CA  
4298 C C   . LYS D 178 ? 1.29230 0.92833 1.02825 0.08771  -0.15933 -0.09680 192 LYS D C   
4299 O O   . LYS D 178 ? 1.29963 0.94850 1.03255 0.08937  -0.15283 -0.09638 192 LYS D O   
4300 C CB  . LYS D 178 ? 1.00737 0.62364 0.75753 0.06163  -0.17265 -0.09349 192 LYS D CB  
4301 N N   . SER D 179 ? 1.32171 0.94701 1.04887 0.10050  -0.16443 -0.10325 193 SER D N   
4302 C CA  . SER D 179 ? 1.28082 0.91015 0.99428 0.11732  -0.16215 -0.11043 193 SER D CA  
4303 C C   . SER D 179 ? 1.31435 0.93335 1.01704 0.12074  -0.16982 -0.11895 193 SER D C   
4304 O O   . SER D 179 ? 1.25117 0.87821 0.94347 0.13164  -0.16583 -0.12331 193 SER D O   
4305 C CB  . SER D 179 ? 1.17565 0.79634 0.88337 0.13011  -0.16554 -0.11502 193 SER D CB  
4306 N N   . ASP D 180 ? 1.24193 0.84380 0.94663 0.11151  -0.18070 -0.12142 194 ASP D N   
4307 C CA  . ASP D 180 ? 1.37627 0.96896 1.07179 0.11308  -0.18845 -0.12922 194 ASP D CA  
4308 C C   . ASP D 180 ? 1.40154 1.00944 1.10068 0.10587  -0.18249 -0.12508 194 ASP D C   
4309 O O   . ASP D 180 ? 1.34805 0.95124 1.03995 0.10709  -0.18811 -0.13092 194 ASP D O   
4310 C CB  . ASP D 180 ? 1.25823 0.82773 0.95510 0.10473  -0.20218 -0.13314 194 ASP D CB  
4311 N N   . PHE D 181 ? 1.50220 1.12793 1.21204 0.09861  -0.17144 -0.11531 195 PHE D N   
4312 C CA  . PHE D 181 ? 1.38080 1.02049 1.09499 0.09123  -0.16537 -0.11058 195 PHE D CA  
4313 C C   . PHE D 181 ? 1.17836 0.83065 0.88112 0.10366  -0.15823 -0.11314 195 PHE D C   
4314 O O   . PHE D 181 ? 1.25932 0.92089 0.95793 0.11333  -0.15046 -0.11232 195 PHE D O   
4315 C CB  . PHE D 181 ? 1.32315 0.97625 1.05241 0.07899  -0.15598 -0.09939 195 PHE D CB  
4316 C CG  . PHE D 181 ? 1.14650 0.81603 0.87973 0.07335  -0.14726 -0.09380 195 PHE D CG  
4317 C CD1 . PHE D 181 ? 1.08607 0.75327 0.82493 0.06247  -0.15169 -0.09294 195 PHE D CD1 
4318 C CD2 . PHE D 181 ? 1.15494 0.84230 0.88642 0.07876  -0.13450 -0.08926 195 PHE D CD2 
4319 C CE1 . PHE D 181 ? 1.13087 0.81268 0.87334 0.05791  -0.14372 -0.08775 195 PHE D CE1 
4320 C CE2 . PHE D 181 ? 0.98924 0.69029 0.72379 0.07369  -0.12647 -0.08395 195 PHE D CE2 
4321 C CZ  . PHE D 181 ? 1.02176 0.71980 0.76179 0.06360  -0.13112 -0.08319 195 PHE D CZ  
4322 N N   . ALA D 182 ? 1.14287 0.79595 0.84050 0.10326  -0.16092 -0.11615 196 ALA D N   
4323 C CA  . ALA D 182 ? 1.18970 0.85446 0.87620 0.11381  -0.15456 -0.11808 196 ALA D CA  
4324 C C   . ALA D 182 ? 1.16095 0.83603 0.85228 0.10527  -0.15077 -0.11302 196 ALA D C   
4325 O O   . ALA D 182 ? 1.17450 0.84335 0.87342 0.09418  -0.15739 -0.11236 196 ALA D O   
4326 C CB  . ALA D 182 ? 1.14303 0.79597 0.81347 0.12646  -0.16347 -0.12952 196 ALA D CB  
4327 N N   . CYS D 183 ? 1.12821 0.81917 0.81485 0.11067  -0.14003 -0.10948 197 CYS D N   
4328 C CA  . CYS D 183 ? 1.09893 0.80024 0.78981 0.10349  -0.13533 -0.10400 197 CYS D CA  
4329 C C   . CYS D 183 ? 1.25528 0.94872 0.94003 0.10389  -0.14552 -0.11037 197 CYS D C   
4330 O O   . CYS D 183 ? 1.20742 0.90522 0.89903 0.09498  -0.14554 -0.10655 197 CYS D O   
4331 C CB  . CYS D 183 ? 0.97494 0.69314 0.65983 0.11031  -0.12218 -0.09946 197 CYS D CB  
4332 S SG  . CYS D 183 ? 1.19999 0.93144 0.89443 0.10670  -0.10847 -0.09013 197 CYS D SG  
4333 N N   . ALA D 184 ? 1.28680 0.96898 0.95876 0.11414  -0.15428 -0.12023 198 ALA D N   
4334 C CA  . ALA D 184 ? 1.23417 0.90856 0.90005 0.11424  -0.16475 -0.12687 198 ALA D CA  
4335 C C   . ALA D 184 ? 1.27685 0.94141 0.95496 0.10016  -0.17389 -0.12647 198 ALA D C   
4336 O O   . ALA D 184 ? 1.21303 0.87879 0.89344 0.09434  -0.17839 -0.12682 198 ALA D O   
4337 C CB  . ALA D 184 ? 1.24007 0.90316 0.88984 0.12757  -0.17248 -0.13794 198 ALA D CB  
4338 N N   . ASN D 185 ? 1.39504 1.05037 1.08114 0.09447  -0.17667 -0.12553 199 ASN D N   
4339 C CA  . ASN D 185 ? 1.39291 1.03861 1.09079 0.08042  -0.18487 -0.12465 199 ASN D CA  
4340 C C   . ASN D 185 ? 1.32702 0.98349 1.04147 0.06717  -0.17683 -0.11393 199 ASN D C   
4341 O O   . ASN D 185 ? 1.34640 0.99675 1.07178 0.05444  -0.18244 -0.11220 199 ASN D O   
4342 C CB  . ASN D 185 ? 1.20113 0.82839 0.89733 0.08141  -0.19362 -0.13004 199 ASN D CB  
4343 N N   . ALA D 186 ? 1.35316 1.02546 1.06945 0.06951  -0.16379 -0.10682 200 ALA D N   
4344 C CA  . ALA D 186 ? 1.31369 0.99578 1.04512 0.05740  -0.15549 -0.09682 200 ALA D CA  
4345 C C   . ALA D 186 ? 1.21244 0.89867 0.95318 0.04576  -0.15742 -0.09379 200 ALA D C   
4346 O O   . ALA D 186 ? 1.18013 0.86224 0.93311 0.03292  -0.16110 -0.09104 200 ALA D O   
4347 C CB  . ALA D 186 ? 1.18870 0.88673 0.91851 0.06290  -0.14113 -0.09054 200 ALA D CB  
4348 N N   . PHE D 187 ? 1.19725 0.89201 0.93225 0.05023  -0.15495 -0.09418 201 PHE D N   
4349 C CA  . PHE D 187 ? 1.20147 0.90203 0.94481 0.04077  -0.15611 -0.09128 201 PHE D CA  
4350 C C   . PHE D 187 ? 1.44706 1.13722 1.18503 0.04157  -0.16977 -0.09992 201 PHE D C   
4351 O O   . PHE D 187 ? 1.47845 1.17206 1.20745 0.04855  -0.17172 -0.10345 201 PHE D O   
4352 C CB  . PHE D 187 ? 1.09606 0.81200 0.83664 0.04493  -0.14528 -0.08600 201 PHE D CB  
4353 C CG  . PHE D 187 ? 1.05559 0.78176 0.80050 0.04404  -0.13169 -0.07784 201 PHE D CG  
4354 C CD1 . PHE D 187 ? 1.01490 0.74821 0.77443 0.03155  -0.12527 -0.06975 201 PHE D CD1 
4355 C CD2 . PHE D 187 ? 1.09763 0.82673 0.83197 0.05545  -0.12530 -0.07848 201 PHE D CD2 
4356 C CE1 . PHE D 187 ? 0.84152 0.58427 0.60484 0.03018  -0.11286 -0.06245 201 PHE D CE1 
4357 C CE2 . PHE D 187 ? 1.06347 0.80272 0.80193 0.05408  -0.11285 -0.07108 201 PHE D CE2 
4358 C CZ  . PHE D 187 ? 0.97342 0.71926 0.72628 0.04130  -0.10670 -0.06307 201 PHE D CZ  
4359 N N   . ASN D 188 ? 1.51337 1.19043 1.25668 0.03397  -0.17946 -0.10329 202 ASN D N   
4360 C CA  . ASN D 188 ? 1.47275 1.13886 1.21215 0.03264  -0.19300 -0.11152 202 ASN D CA  
4361 C C   . ASN D 188 ? 1.51417 1.18140 1.26761 0.01735  -0.19787 -0.10913 202 ASN D C   
4362 O O   . ASN D 188 ? 1.56899 1.23447 1.32038 0.01598  -0.20637 -0.11422 202 ASN D O   
4363 C CB  . ASN D 188 ? 1.50825 1.15604 1.24048 0.03657  -0.20202 -0.11886 202 ASN D CB  
4364 C CG  . ASN D 188 ? 1.53415 1.17895 1.24920 0.05338  -0.20153 -0.12511 202 ASN D CG  
4365 O OD1 . ASN D 188 ? 1.44421 1.10094 1.15246 0.06189  -0.19417 -0.12364 202 ASN D OD1 
4366 N ND2 . ASN D 188 ? 1.55069 1.17926 1.25829 0.05831  -0.20929 -0.13212 202 ASN D ND2 
4367 N N   . ASN D 189 ? 1.49607 1.16679 1.26366 0.00574  -0.19273 -0.10167 203 ASN D N   
4368 C CA  . ASN D 189 ? 1.45906 1.13350 1.24067 -0.00892 -0.19575 -0.09869 203 ASN D CA  
4369 C C   . ASN D 189 ? 1.43038 1.12228 1.21688 -0.00978 -0.18760 -0.09325 203 ASN D C   
4370 O O   . ASN D 189 ? 1.32756 1.02379 1.12030 -0.01653 -0.19229 -0.09399 203 ASN D O   
4371 C CB  . ASN D 189 ? 1.31753 0.98872 1.11193 -0.02122 -0.19360 -0.09298 203 ASN D CB  
4372 N N   . SER D 190 ? 1.32432 1.02630 1.10793 -0.00296 -0.17551 -0.08783 204 SER D N   
4373 C CA  . SER D 190 ? 1.26013 0.97736 1.04640 -0.00226 -0.16720 -0.08261 204 SER D CA  
4374 C C   . SER D 190 ? 1.48343 1.20235 1.25707 0.00872  -0.17163 -0.08828 204 SER D C   
4375 O O   . SER D 190 ? 1.51395 1.22402 1.27445 0.01855  -0.17761 -0.09539 204 SER D O   
4376 C CB  . SER D 190 ? 1.09567 0.82202 0.88183 0.00125  -0.15285 -0.07512 204 SER D CB  
4377 N N   . ILE D 192 ? 1.41241 1.13692 1.15768 0.03278  -0.17998 -0.09930 206 ILE D N   
4378 C CA  . ILE D 192 ? 1.31660 1.04387 1.04689 0.04685  -0.17326 -0.09948 206 ILE D CA  
4379 C C   . ILE D 192 ? 1.29955 1.03093 1.01874 0.05554  -0.17772 -0.10358 206 ILE D C   
4380 O O   . ILE D 192 ? 1.39370 1.12048 1.11225 0.05357  -0.18936 -0.11003 206 ILE D O   
4381 C CB  . ILE D 192 ? 1.14362 0.85906 0.86428 0.05377  -0.17586 -0.10501 206 ILE D CB  
4382 N N   . PRO D 193 ? 1.29479 1.03492 1.00499 0.06486  -0.16863 -0.09980 207 PRO D N   
4383 C CA  . PRO D 193 ? 1.31602 1.06041 1.01460 0.07380  -0.17246 -0.10315 207 PRO D CA  
4384 C C   . PRO D 193 ? 1.32135 1.05746 1.00218 0.08587  -0.17841 -0.11196 207 PRO D C   
4385 O O   . PRO D 193 ? 1.29582 1.02679 0.97037 0.09114  -0.17459 -0.11323 207 PRO D O   
4386 C CB  . PRO D 193 ? 1.21911 0.97562 0.91573 0.07789  -0.15915 -0.09438 207 PRO D CB  
4387 N N   . GLU D 194 ? 1.36633 1.10169 1.03908 0.09034  -0.18800 -0.11828 208 GLU D N   
4388 C CA  . GLU D 194 ? 1.23384 0.96146 0.88900 0.10178  -0.19455 -0.12743 208 GLU D CA  
4389 C C   . GLU D 194 ? 1.10694 0.84051 0.74707 0.11481  -0.18502 -0.12526 208 GLU D C   
4390 O O   . GLU D 194 ? 1.21312 0.94072 0.83816 0.12503  -0.18840 -0.13239 208 GLU D O   
4391 C CB  . GLU D 194 ? 1.34103 1.06743 0.99186 0.10232  -0.20731 -0.13454 208 GLU D CB  
4392 N N   . ASP D 195 ? 1.17696 0.92184 0.82046 0.11455  -0.17321 -0.11578 209 ASP D N   
4393 C CA  . ASP D 195 ? 1.24801 0.99897 0.87795 0.12561  -0.16302 -0.11263 209 ASP D CA  
4394 C C   . ASP D 195 ? 1.22150 0.97278 0.85421 0.12521  -0.15200 -0.10798 209 ASP D C   
4395 O O   . ASP D 195 ? 1.27947 1.03709 0.90277 0.13279  -0.14189 -0.10412 209 ASP D O   
4396 C CB  . ASP D 195 ? 1.19506 0.95774 0.82508 0.12632  -0.15657 -0.10500 209 ASP D CB  
4397 N N   . THR D 196 ? 1.20547 0.95037 0.85056 0.11646  -0.15382 -0.10819 210 THR D N   
4398 C CA  . THR D 196 ? 1.21988 0.96611 0.86926 0.11510  -0.14360 -0.10330 210 THR D CA  
4399 C C   . THR D 196 ? 1.10857 0.85139 0.74264 0.12744  -0.14207 -0.10868 210 THR D C   
4400 O O   . THR D 196 ? 1.19829 0.93096 0.82500 0.13230  -0.15200 -0.11793 210 THR D O   
4401 C CB  . THR D 196 ? 1.07843 0.81783 0.74382 0.10315  -0.14727 -0.10283 210 THR D CB  
4402 O OG1 . THR D 196 ? 1.07554 0.81948 0.75543 0.09154  -0.14779 -0.09760 210 THR D OG1 
4403 C CG2 . THR D 196 ? 1.01211 0.75380 0.68198 0.10186  -0.13683 -0.09760 210 THR D CG2 
4404 N N   . PHE D 197 ? 1.04597 0.79738 0.67534 0.13228  -0.12944 -0.10296 211 PHE D N   
4405 C CA  . PHE D 197 ? 1.05781 0.80902 0.67267 0.14435  -0.12593 -0.10705 211 PHE D CA  
4406 C C   . PHE D 197 ? 1.20280 0.94890 0.82397 0.14245  -0.12464 -0.10818 211 PHE D C   
4407 O O   . PHE D 197 ? 1.18089 0.93122 0.81496 0.13389  -0.11739 -0.10089 211 PHE D O   
4408 C CB  . PHE D 197 ? 1.03085 0.79453 0.63787 0.14974  -0.11265 -0.10000 211 PHE D CB  
4409 C CG  . PHE D 197 ? 1.11789 0.88377 0.71087 0.16145  -0.10732 -0.10320 211 PHE D CG  
4410 C CD1 . PHE D 197 ? 1.17700 0.93586 0.75615 0.17184  -0.11577 -0.11339 211 PHE D CD1 
4411 C CD2 . PHE D 197 ? 1.04625 0.82178 0.63961 0.16202  -0.09372 -0.09620 211 PHE D CD2 
4412 C CE1 . PHE D 197 ? 1.17750 0.93917 0.74375 0.18294  -0.11064 -0.11662 211 PHE D CE1 
4413 C CE2 . PHE D 197 ? 1.16799 0.94696 0.74875 0.17272  -0.08856 -0.09920 211 PHE D CE2 
4414 C CZ  . PHE D 197 ? 1.29819 1.07040 0.86542 0.18344  -0.09698 -0.10946 211 PHE D CZ  
4415 N N   . PHE D 198 ? 1.23310 0.96999 0.84485 0.15068  -0.13180 -0.11742 212 PHE D N   
4416 C CA  . PHE D 198 ? 1.18423 0.91483 0.80003 0.15094  -0.13204 -0.11975 212 PHE D CA  
4417 C C   . PHE D 198 ? 1.27775 1.01164 0.87865 0.16484  -0.12685 -0.12363 212 PHE D C   
4418 O O   . PHE D 198 ? 1.29761 1.02230 0.88770 0.17366  -0.13483 -0.13326 212 PHE D O   
4419 C CB  . PHE D 198 ? 1.16882 0.88337 0.78789 0.14758  -0.14626 -0.12776 212 PHE D CB  
4420 C CG  . PHE D 198 ? 1.23721 0.94851 0.87334 0.13258  -0.15047 -0.12355 212 PHE D CG  
4421 C CD1 . PHE D 198 ? 1.22409 0.93609 0.86295 0.12702  -0.15619 -0.12347 212 PHE D CD1 
4422 C CD2 . PHE D 198 ? 1.19641 0.90445 0.84581 0.12413  -0.14885 -0.11977 212 PHE D CD2 
4423 C CE1 . PHE D 198 ? 1.18057 0.89052 0.83531 0.11319  -0.15988 -0.11982 212 PHE D CE1 
4424 C CE2 . PHE D 198 ? 1.14173 0.84712 0.80650 0.11009  -0.15256 -0.11595 212 PHE D CE2 
4425 C CZ  . PHE D 198 ? 1.13447 0.84101 0.80202 0.10456  -0.15793 -0.11607 212 PHE D CZ  
4426 N N   . PRO D 199 ? 1.23648 0.98352 0.83626 0.16703  -0.11338 -0.11654 213 PRO D N   
4427 C CA  . PRO D 199 ? 1.23216 0.98456 0.81838 0.17981  -0.10722 -0.11961 213 PRO D CA  
4428 C C   . PRO D 199 ? 1.30525 1.05036 0.89254 0.18407  -0.11039 -0.12524 213 PRO D C   
4429 O O   . PRO D 199 ? 1.37631 1.12237 0.95079 0.19624  -0.10923 -0.13108 213 PRO D O   
4430 C CB  . PRO D 199 ? 1.22896 0.99688 0.81846 0.17700  -0.09197 -0.10913 213 PRO D CB  
4431 C CG  . PRO D 199 ? 1.14380 0.91216 0.75151 0.16231  -0.09046 -0.10131 213 PRO D CG  
4432 C CD  . PRO D 199 ? 1.10412 0.86190 0.71537 0.15719  -0.10300 -0.10529 213 PRO D CD  
4433 N N   . GLY E 2   ? 0.86597 0.68119 0.86811 -0.02506 0.07600  0.07299  3   GLY E N   
4434 C CA  . GLY E 2   ? 0.59694 0.41193 0.60319 -0.02501 0.06144  0.07066  3   GLY E CA  
4435 C C   . GLY E 2   ? 0.64428 0.47733 0.67227 -0.02609 0.05546  0.06295  3   GLY E C   
4436 O O   . GLY E 2   ? 0.64324 0.49096 0.69421 -0.03088 0.06133  0.06033  3   GLY E O   
4437 N N   . VAL E 3   ? 0.57819 0.41020 0.59890 -0.02154 0.04376  0.05925  4   VAL E N   
4438 C CA  . VAL E 3   ? 0.47575 0.32371 0.51509 -0.02179 0.03683  0.05193  4   VAL E CA  
4439 C C   . VAL E 3   ? 0.37378 0.23114 0.41319 -0.01854 0.04328  0.04784  4   VAL E C   
4440 O O   . VAL E 3   ? 0.53552 0.38380 0.55372 -0.01330 0.04540  0.04921  4   VAL E O   
4441 C CB  . VAL E 3   ? 0.44544 0.28764 0.47707 -0.01844 0.02120  0.04983  4   VAL E CB  
4442 C CG1 . VAL E 3   ? 0.35502 0.21339 0.40524 -0.01835 0.01425  0.04229  4   VAL E CG1 
4443 C CG2 . VAL E 3   ? 0.35962 0.19288 0.39178 -0.02182 0.01508  0.05392  4   VAL E CG2 
4444 N N   . THR E 4   ? 0.38288 0.25852 0.44608 -0.02159 0.04650  0.04280  5   THR E N   
4445 C CA  . THR E 4   ? 0.49600 0.38259 0.56258 -0.01920 0.05348  0.03871  5   THR E CA  
4446 C C   . THR E 4   ? 0.42158 0.32015 0.49874 -0.01685 0.04384  0.03150  5   THR E C   
4447 O O   . THR E 4   ? 0.34579 0.25600 0.44457 -0.02059 0.03902  0.02809  5   THR E O   
4448 C CB  . THR E 4   ? 0.48365 0.38253 0.56939 -0.02450 0.06644  0.03865  5   THR E CB  
4449 O OG1 . THR E 4   ? 0.63781 0.52506 0.71393 -0.02681 0.07537  0.04551  5   THR E OG1 
4450 C CG2 . THR E 4   ? 0.57790 0.48743 0.66580 -0.02181 0.07408  0.03471  5   THR E CG2 
4451 N N   . GLN E 5   ? 0.34904 0.24488 0.41119 -0.01066 0.04128  0.02915  6   GLN E N   
4452 C CA  . GLN E 5   ? 0.37176 0.27849 0.44203 -0.00772 0.03313  0.02229  6   GLN E CA  
4453 C C   . GLN E 5   ? 0.34117 0.25891 0.41458 -0.00534 0.04169  0.01864  6   GLN E C   
4454 O O   . GLN E 5   ? 0.39704 0.30752 0.45397 -0.00254 0.04968  0.02136  6   GLN E O   
4455 C CB  . GLN E 5   ? 0.31609 0.21045 0.36639 -0.00214 0.02115  0.02196  6   GLN E CB  
4456 C CG  . GLN E 5   ? 0.31277 0.19812 0.36177 -0.00409 0.01072  0.02437  6   GLN E CG  
4457 C CD  . GLN E 5   ? 0.31393 0.18995 0.34675 0.00129  -0.00191 0.02273  6   GLN E CD  
4458 O OE1 . GLN E 5   ? 0.36400 0.22360 0.37631 0.00346  -0.00544 0.02709  6   GLN E OE1 
4459 N NE2 . GLN E 5   ? 0.29712 0.18365 0.33909 0.00356  -0.00875 0.01634  6   GLN E NE2 
4460 N N   . THR E 6   ? 0.33245 0.26773 0.42696 -0.00635 0.03998  0.01249  7   THR E N   
4461 C CA  . THR E 6   ? 0.41422 0.36147 0.51338 -0.00382 0.04667  0.00821  7   THR E CA  
4462 C C   . THR E 6   ? 0.35391 0.31258 0.46399 -0.00133 0.03704  0.00133  7   THR E C   
4463 O O   . THR E 6   ? 0.36970 0.33242 0.49270 -0.00369 0.02798  -0.00056 7   THR E O   
4464 C CB  . THR E 6   ? 0.44542 0.40619 0.56403 -0.00883 0.05921  0.00788  7   THR E CB  
4465 O OG1 . THR E 6   ? 0.35523 0.32775 0.49856 -0.01417 0.05560  0.00553  7   THR E OG1 
4466 C CG2 . THR E 6   ? 0.40122 0.35101 0.50888 -0.01108 0.06999  0.01458  7   THR E CG2 
4467 N N   . PRO E 7   ? 0.44171 0.40521 0.54621 0.00364  0.03857  -0.00243 8   PRO E N   
4468 C CA  . PRO E 7   ? 0.31066 0.26671 0.39586 0.00742  0.04733  -0.00007 8   PRO E CA  
4469 C C   . PRO E 7   ? 0.44176 0.37769 0.49933 0.01164  0.04146  0.00387  8   PRO E C   
4470 O O   . PRO E 7   ? 0.34808 0.27843 0.40217 0.01285  0.02950  0.00302  8   PRO E O   
4471 C CB  . PRO E 7   ? 0.27689 0.24569 0.36743 0.01140  0.04796  -0.00627 8   PRO E CB  
4472 C CG  . PRO E 7   ? 0.39374 0.36956 0.49621 0.01194  0.03544  -0.01119 8   PRO E CG  
4473 C CD  . PRO E 7   ? 0.30634 0.28397 0.42441 0.00581  0.03221  -0.00945 8   PRO E CD  
4474 N N   . ARG E 8   ? 0.36822 0.29348 0.40664 0.01380  0.04970  0.00811  9   ARG E N   
4475 C CA  . ARG E 8   ? 0.42628 0.33230 0.43788 0.01789  0.04464  0.01203  9   ARG E CA  
4476 C C   . ARG E 8   ? 0.39380 0.29792 0.39247 0.02452  0.03778  0.00800  9   ARG E C   
4477 O O   . ARG E 8   ? 0.42725 0.31910 0.41016 0.02767  0.02816  0.00889  9   ARG E O   
4478 C CB  . ARG E 8   ? 0.39487 0.29003 0.39054 0.01789  0.05601  0.01811  9   ARG E CB  
4479 C CG  . ARG E 8   ? 0.58207 0.47736 0.58896 0.01138  0.06276  0.02254  9   ARG E CG  
4480 C CD  . ARG E 8   ? 0.65000 0.53799 0.64503 0.01109  0.07603  0.02779  9   ARG E CD  
4481 N NE  . ARG E 8   ? 0.72395 0.59318 0.69033 0.01578  0.07438  0.03219  9   ARG E NE  
4482 C CZ  . ARG E 8   ? 0.86357 0.72805 0.81267 0.02077  0.07916  0.03239  9   ARG E CZ  
4483 N NH1 . ARG E 8   ? 0.66935 0.54600 0.62624 0.02177  0.08627  0.02864  9   ARG E NH1 
4484 N NH2 . ARG E 8   ? 0.66901 0.51615 0.59235 0.02488  0.07681  0.03644  9   ARG E NH2 
4485 N N   . TYR E 9   ? 0.34002 0.25621 0.34531 0.02665  0.04259  0.00352  10  TYR E N   
4486 C CA  . TYR E 9   ? 0.37031 0.28675 0.36584 0.03276  0.03690  -0.00086 10  TYR E CA  
4487 C C   . TYR E 9   ? 0.31607 0.25206 0.33400 0.03230  0.03662  -0.00750 10  TYR E C   
4488 O O   . TYR E 9   ? 0.38104 0.32993 0.41705 0.02846  0.04510  -0.00834 10  TYR E O   
4489 C CB  . TYR E 9   ? 0.35916 0.26788 0.33371 0.03734  0.04477  0.00102  10  TYR E CB  
4490 C CG  . TYR E 9   ? 0.40845 0.29752 0.35853 0.03880  0.04527  0.00737  10  TYR E CG  
4491 C CD1 . TYR E 9   ? 0.41624 0.29976 0.36515 0.03484  0.05376  0.01319  10  TYR E CD1 
4492 C CD2 . TYR E 9   ? 0.40008 0.27619 0.32800 0.04429  0.03754  0.00749  10  TYR E CD2 
4493 C CE1 . TYR E 9   ? 0.51706 0.38260 0.44333 0.03641  0.05435  0.01909  10  TYR E CE1 
4494 C CE2 . TYR E 9   ? 0.48350 0.34186 0.38876 0.04587  0.03800  0.01322  10  TYR E CE2 
4495 C CZ  . TYR E 9   ? 0.47363 0.32676 0.37806 0.04200  0.04643  0.01907  10  TYR E CZ  
4496 O OH  . TYR E 9   ? 0.69025 0.52577 0.57202 0.04376  0.04704  0.02486  10  TYR E OH  
4497 N N   . LEU E 10  ? 0.39194 0.33009 0.40842 0.03636  0.02701  -0.01227 11  LEU E N   
4498 C CA  . LEU E 10  ? 0.36025 0.31663 0.39788 0.03625  0.02549  -0.01871 11  LEU E CA  
4499 C C   . LEU E 10  ? 0.35426 0.30935 0.38199 0.04249  0.01757  -0.02318 11  LEU E C   
4500 O O   . LEU E 10  ? 0.38773 0.33079 0.40168 0.04499  0.00769  -0.02254 11  LEU E O   
4501 C CB  . LEU E 10  ? 0.26602 0.23075 0.32580 0.03115  0.01913  -0.02012 11  LEU E CB  
4502 C CG  . LEU E 10  ? 0.52519 0.51071 0.61136 0.02935  0.01977  -0.02598 11  LEU E CG  
4503 C CD1 . LEU E 10  ? 0.37914 0.37598 0.47316 0.02854  0.03323  -0.02672 11  LEU E CD1 
4504 C CD2 . LEU E 10  ? 0.46844 0.45970 0.57442 0.02344  0.01552  -0.02570 11  LEU E CD2 
4505 N N   . ILE E 11  ? 0.36823 0.33558 0.40281 0.04502  0.02205  -0.02769 12  ILE E N   
4506 C CA  . ILE E 11  ? 0.39285 0.36218 0.42244 0.05061  0.01500  -0.03278 12  ILE E CA  
4507 C C   . ILE E 11  ? 0.31351 0.30100 0.36863 0.04906  0.01133  -0.03857 12  ILE E C   
4508 O O   . ILE E 11  ? 0.31682 0.31888 0.38918 0.04657  0.01950  -0.04024 12  ILE E O   
4509 C CB  . ILE E 11  ? 0.37985 0.34818 0.39535 0.05544  0.02283  -0.03347 12  ILE E CB  
4510 C CG1 . ILE E 11  ? 0.47462 0.42504 0.46494 0.05689  0.02694  -0.02752 12  ILE E CG1 
4511 C CG2 . ILE E 11  ? 0.30125 0.27174 0.31218 0.06115  0.01544  -0.03887 12  ILE E CG2 
4512 C CD1 . ILE E 11  ? 0.45098 0.40097 0.42897 0.06060  0.03689  -0.02733 12  ILE E CD1 
4513 N N   . LYS E 12  ? 0.32516 0.31194 0.38293 0.05050  -0.00086 -0.04163 13  LYS E N   
4514 C CA  . LYS E 12  ? 0.23254 0.23567 0.31253 0.05003  -0.00546 -0.04747 13  LYS E CA  
4515 C C   . LYS E 12  ? 0.29672 0.29866 0.36815 0.05623  -0.01311 -0.05208 13  LYS E C   
4516 O O   . LYS E 12  ? 0.31452 0.30211 0.36370 0.06023  -0.01656 -0.05061 13  LYS E O   
4517 C CB  . LYS E 12  ? 0.31340 0.31864 0.40880 0.04519  -0.01333 -0.04714 13  LYS E CB  
4518 C CG  . LYS E 12  ? 0.35102 0.35571 0.45412 0.03884  -0.00689 -0.04229 13  LYS E CG  
4519 C CD  . LYS E 12  ? 0.31494 0.33543 0.43531 0.03602  0.00494  -0.04349 13  LYS E CD  
4520 C CE  . LYS E 12  ? 0.33763 0.37668 0.48471 0.03394  0.00176  -0.04883 13  LYS E CE  
4521 N NZ  . LYS E 12  ? 0.41357 0.46800 0.57802 0.03077  0.01332  -0.04984 13  LYS E NZ  
4522 N N   . THR E 13  ? 0.35596 0.37316 0.44517 0.05713  -0.01573 -0.05779 14  THR E N   
4523 C CA  . THR E 13  ? 0.31226 0.32898 0.39573 0.06267  -0.02394 -0.06245 14  THR E CA  
4524 C C   . THR E 13  ? 0.31662 0.33524 0.41162 0.06136  -0.03628 -0.06492 14  THR E C   
4525 O O   . THR E 13  ? 0.38159 0.40646 0.49372 0.05621  -0.03756 -0.06417 14  THR E O   
4526 C CB  . THR E 13  ? 0.38436 0.41589 0.47671 0.06591  -0.01827 -0.06744 14  THR E CB  
4527 O OG1 . THR E 13  ? 0.40212 0.45164 0.52096 0.06211  -0.01565 -0.07008 14  THR E OG1 
4528 C CG2 . THR E 13  ? 0.42455 0.45320 0.50364 0.06775  -0.00656 -0.06513 14  THR E CG2 
4529 N N   . ARG E 14  ? 0.43669 0.32162 0.37317 0.08792  -0.02394 0.02849  15  ARG E N   
4530 C CA  . ARG E 14  ? 0.46901 0.34137 0.38715 0.09090  -0.02173 0.03234  15  ARG E CA  
4531 C C   . ARG E 14  ? 0.40722 0.27259 0.31385 0.09509  -0.02988 0.02951  15  ARG E C   
4532 O O   . ARG E 14  ? 0.47977 0.34773 0.38906 0.09811  -0.03713 0.02701  15  ARG E O   
4533 C CB  . ARG E 14  ? 0.45976 0.32888 0.37305 0.09353  -0.01743 0.03803  15  ARG E CB  
4534 C CG  . ARG E 14  ? 0.49837 0.35769 0.39502 0.09457  -0.01453 0.04111  15  ARG E CG  
4535 C CD  . ARG E 14  ? 0.75720 0.62117 0.65547 0.09249  -0.01055 0.04373  15  ARG E CD  
4536 N NE  . ARG E 14  ? 0.78661 0.65381 0.68894 0.09580  -0.01686 0.04265  15  ARG E NE  
4537 C CZ  . ARG E 14  ? 0.99418 0.85638 0.88688 0.09915  -0.02213 0.04200  15  ARG E CZ  
4538 N NH1 . ARG E 14  ? 0.90326 0.75673 0.78115 0.09982  -0.02170 0.04237  15  ARG E NH1 
4539 N NH2 . ARG E 14  ? 0.96759 0.83366 0.86578 0.10181  -0.02788 0.04083  15  ARG E NH2 
4540 N N   . GLY E 15  ? 0.41384 0.27034 0.30780 0.09523  -0.02879 0.02974  16  GLY E N   
4541 C CA  . GLY E 15  ? 0.40789 0.25720 0.29001 0.09878  -0.03609 0.02693  16  GLY E CA  
4542 C C   . GLY E 15  ? 0.43608 0.28970 0.32469 0.09646  -0.04119 0.02066  16  GLY E C   
4543 O O   . GLY E 15  ? 0.51026 0.35721 0.38816 0.09888  -0.04651 0.01820  16  GLY E O   
4544 N N   . GLN E 16  ? 0.41377 0.27811 0.31934 0.09180  -0.03966 0.01794  17  GLN E N   
4545 C CA  . GLN E 16  ? 0.46625 0.33515 0.37913 0.08926  -0.04414 0.01183  17  GLN E CA  
4546 C C   . GLN E 16  ? 0.41657 0.28095 0.32458 0.08590  -0.03912 0.01205  17  GLN E C   
4547 O O   . GLN E 16  ? 0.42976 0.28929 0.33170 0.08481  -0.03158 0.01677  17  GLN E O   
4548 C CB  . GLN E 16  ? 0.38294 0.26521 0.31626 0.08554  -0.04471 0.00853  17  GLN E CB  
4549 C CG  . GLN E 16  ? 0.41375 0.30154 0.35387 0.08871  -0.05123 0.00660  17  GLN E CG  
4550 C CD  . GLN E 16  ? 0.44087 0.34196 0.40147 0.08471  -0.05207 0.00233  17  GLN E CD  
4551 O OE1 . GLN E 16  ? 0.40137 0.30792 0.37129 0.07967  -0.04546 0.00321  17  GLN E OE1 
4552 N NE2 . GLN E 16  ? 0.47919 0.38538 0.44685 0.08687  -0.06024 -0.00245 17  GLN E NE2 
4553 N N   . GLN E 17  ? 0.39596 0.26201 0.30706 0.08429  -0.04351 0.00667  18  GLN E N   
4554 C CA  . GLN E 17  ? 0.48960 0.35215 0.39763 0.08096  -0.03974 0.00593  18  GLN E CA  
4555 C C   . GLN E 17  ? 0.48279 0.35555 0.40828 0.07509  -0.03731 0.00306  18  GLN E C   
4556 O O   . GLN E 17  ? 0.41934 0.30160 0.35854 0.07395  -0.04084 -0.00027 18  GLN E O   
4557 C CB  . GLN E 17  ? 0.41686 0.27290 0.31450 0.08336  -0.04628 0.00187  18  GLN E CB  
4558 C CG  . GLN E 17  ? 0.61294 0.47609 0.52043 0.08377  -0.05504 -0.00463 18  GLN E CG  
4559 C CD  . GLN E 17  ? 0.77043 0.62743 0.66819 0.08589  -0.06149 -0.00891 18  GLN E CD  
4560 O OE1 . GLN E 17  ? 0.87497 0.72324 0.76021 0.08603  -0.05869 -0.00748 18  GLN E OE1 
4561 N NE2 . GLN E 17  ? 0.70899 0.57055 0.61263 0.08759  -0.07026 -0.01441 18  GLN E NE2 
4562 N N   . VAL E 18  ? 0.35917 0.22962 0.28393 0.07132  -0.03127 0.00425  19  VAL E N   
4563 C CA  . VAL E 18  ? 0.35797 0.23672 0.29775 0.06545  -0.02807 0.00220  19  VAL E CA  
4564 C C   . VAL E 18  ? 0.36499 0.23869 0.30022 0.06286  -0.02600 0.00082  19  VAL E C   
4565 O O   . VAL E 18  ? 0.40513 0.26925 0.32657 0.06467  -0.02343 0.00357  19  VAL E O   
4566 C CB  . VAL E 18  ? 0.40240 0.28551 0.34946 0.06273  -0.02039 0.00704  19  VAL E CB  
4567 C CG1 . VAL E 18  ? 0.35115 0.22537 0.28646 0.06313  -0.01325 0.01272  19  VAL E CG1 
4568 C CG2 . VAL E 18  ? 0.34466 0.23690 0.30768 0.05677  -0.01787 0.00466  19  VAL E CG2 
4569 N N   . THR E 19  ? 0.35651 0.23671 0.30368 0.05853  -0.02703 -0.00362 20  THR E N   
4570 C CA  . THR E 19  ? 0.29559 0.17227 0.24105 0.05538  -0.02491 -0.00527 20  THR E CA  
4571 C C   . THR E 19  ? 0.30566 0.18995 0.26585 0.04916  -0.01998 -0.00554 20  THR E C   
4572 O O   . THR E 19  ? 0.35593 0.24942 0.32971 0.04682  -0.02255 -0.00912 20  THR E O   
4573 C CB  . THR E 19  ? 0.44152 0.31702 0.38490 0.05672  -0.03260 -0.01150 20  THR E CB  
4574 O OG1 . THR E 19  ? 0.52775 0.39546 0.45625 0.06256  -0.03715 -0.01095 20  THR E OG1 
4575 C CG2 . THR E 19  ? 0.30850 0.18027 0.25030 0.05340  -0.03027 -0.01328 20  THR E CG2 
4576 N N   . LEU E 20  ? 0.40681 0.28710 0.36425 0.04650  -0.01292 -0.00180 21  LEU E N   
4577 C CA  . LEU E 20  ? 0.42152 0.30743 0.39103 0.04058  -0.00775 -0.00138 21  LEU E CA  
4578 C C   . LEU E 20  ? 0.42091 0.30371 0.39017 0.03751  -0.00748 -0.00433 21  LEU E C   
4579 O O   . LEU E 20  ? 0.39076 0.26504 0.34812 0.03972  -0.00800 -0.00421 21  LEU E O   
4580 C CB  . LEU E 20  ? 0.32116 0.20505 0.28870 0.03963  0.00010  0.00514  21  LEU E CB  
4581 C CG  . LEU E 20  ? 0.35549 0.24086 0.32125 0.04305  0.00065  0.00879  21  LEU E CG  
4582 C CD1 . LEU E 20  ? 0.25161 0.13436 0.21514 0.04191  0.00860  0.01496  21  LEU E CD1 
4583 C CD2 . LEU E 20  ? 0.33397 0.23005 0.31330 0.04189  -0.00243 0.00614  21  LEU E CD2 
4584 N N   . SER E 21  ? 0.39660 0.28620 0.37902 0.03230  -0.00651 -0.00701 22  SER E N   
4585 C CA  . SER E 21  ? 0.42838 0.31592 0.41231 0.02906  -0.00665 -0.01030 22  SER E CA  
4586 C C   . SER E 21  ? 0.44148 0.32993 0.43173 0.02364  0.00052  -0.00738 22  SER E C   
4587 O O   . SER E 21  ? 0.36907 0.26328 0.36762 0.02113  0.00415  -0.00489 22  SER E O   
4588 C CB  . SER E 21  ? 0.44759 0.34182 0.44142 0.02767  -0.01300 -0.01727 22  SER E CB  
4589 O OG  . SER E 21  ? 0.54431 0.43556 0.53803 0.02523  -0.01371 -0.02068 22  SER E OG  
4590 N N   . CYS E 22  ? 0.42653 0.30904 0.41261 0.02188  0.00240  -0.00777 23  CYS E N   
4591 C CA  . CYS E 22  ? 0.41352 0.29521 0.40394 0.01705  0.00889  -0.00492 23  CYS E CA  
4592 C C   . CYS E 22  ? 0.51505 0.39512 0.50825 0.01386  0.00756  -0.00916 23  CYS E C   
4593 O O   . CYS E 22  ? 0.48906 0.36252 0.47315 0.01628  0.00516  -0.01098 23  CYS E O   
4594 C CB  . CYS E 22  ? 0.47629 0.34995 0.45589 0.01901  0.01427  0.00099  23  CYS E CB  
4595 S SG  . CYS E 22  ? 0.45998 0.33038 0.44249 0.01384  0.02184  0.00462  23  CYS E SG  
4596 N N   . SER E 23  ? 0.43015 0.31613 0.43579 0.00837  0.00917  -0.01081 24  SER E N   
4597 C CA  . SER E 23  ? 0.45234 0.33651 0.46132 0.00469  0.00903  -0.01413 24  SER E CA  
4598 C C   . SER E 23  ? 0.44776 0.32803 0.45689 0.00103  0.01592  -0.00961 24  SER E C   
4599 O O   . SER E 23  ? 0.36466 0.24962 0.38198 -0.00268 0.01983  -0.00713 24  SER E O   
4600 C CB  . SER E 23  ? 0.39554 0.28832 0.41822 0.00085  0.00599  -0.01950 24  SER E CB  
4601 O OG  . SER E 23  ? 0.51249 0.40796 0.53474 0.00437  -0.00109 -0.02446 24  SER E OG  
4602 N N   . PRO E 24  ? 0.34891 0.22071 0.34937 0.00189  0.01756  -0.00848 25  PRO E N   
4603 C CA  . PRO E 24  ? 0.35937 0.22698 0.35962 -0.00114 0.02391  -0.00400 25  PRO E CA  
4604 C C   . PRO E 24  ? 0.34080 0.21163 0.35212 -0.00738 0.02538  -0.00593 25  PRO E C   
4605 O O   . PRO E 24  ? 0.38245 0.25822 0.40130 -0.00941 0.02164  -0.01105 25  PRO E O   
4606 C CB  . PRO E 24  ? 0.28272 0.14064 0.27096 0.00184  0.02414  -0.00361 25  PRO E CB  
4607 C CG  . PRO E 24  ? 0.37475 0.23268 0.36087 0.00385  0.01777  -0.00958 25  PRO E CG  
4608 C CD  . PRO E 24  ? 0.34864 0.21428 0.33942 0.00551  0.01349  -0.01165 25  PRO E CD  
4609 N N   . ILE E 25  ? 0.35990 0.22767 0.37222 -0.01047 0.03098  -0.00168 26  ILE E N   
4610 C CA  . ILE E 25  ? 0.36331 0.23215 0.38436 -0.01638 0.03283  -0.00293 26  ILE E CA  
4611 C C   . ILE E 25  ? 0.39695 0.26203 0.41648 -0.01659 0.02945  -0.00787 26  ILE E C   
4612 O O   . ILE E 25  ? 0.51822 0.37647 0.52791 -0.01299 0.02845  -0.00804 26  ILE E O   
4613 C CB  . ILE E 25  ? 0.45237 0.31684 0.47257 -0.01886 0.03904  0.00276  26  ILE E CB  
4614 C CG1 . ILE E 25  ? 0.49999 0.37015 0.52518 -0.02025 0.04218  0.00666  26  ILE E CG1 
4615 C CG2 . ILE E 25  ? 0.34675 0.20895 0.37255 -0.02413 0.04060  0.00149  26  ILE E CG2 
4616 C CD1 . ILE E 25  ? 0.38803 0.25392 0.41128 -0.02176 0.04793  0.01259  26  ILE E CD1 
4617 N N   . SER E 26  ? 0.37822 0.24794 0.40761 -0.02080 0.02764  -0.01219 27  SER E N   
4618 C CA  . SER E 26  ? 0.43992 0.30727 0.46949 -0.02128 0.02398  -0.01760 27  SER E CA  
4619 C C   . SER E 26  ? 0.39553 0.25370 0.41835 -0.02139 0.02662  -0.01577 27  SER E C   
4620 O O   . SER E 26  ? 0.49405 0.34977 0.51952 -0.02499 0.03131  -0.01225 27  SER E O   
4621 C CB  . SER E 26  ? 0.43372 0.30726 0.47627 -0.02689 0.02320  -0.02160 27  SER E CB  
4622 O OG  . SER E 26  ? 0.53637 0.40850 0.57989 -0.02716 0.01915  -0.02739 27  SER E OG  
4623 N N   . GLY E 27  ? 0.42154 0.27451 0.43551 -0.01740 0.02353  -0.01823 28  GLY E N   
4624 C CA  . GLY E 27  ? 0.38756 0.23172 0.39440 -0.01684 0.02569  -0.01700 28  GLY E CA  
4625 C C   . GLY E 27  ? 0.41072 0.24900 0.40624 -0.01246 0.02838  -0.01227 28  GLY E C   
4626 O O   . GLY E 27  ? 0.51862 0.34941 0.50647 -0.01076 0.02922  -0.01221 28  GLY E O   
4627 N N   . HIS E 28  ? 0.41613 0.25761 0.41068 -0.01069 0.02990  -0.00846 29  HIS E N   
4628 C CA  . HIS E 28  ? 0.34875 0.18490 0.33267 -0.00637 0.03239  -0.00417 29  HIS E CA  
4629 C C   . HIS E 28  ? 0.41025 0.24349 0.38399 -0.00104 0.02807  -0.00703 29  HIS E C   
4630 O O   . HIS E 28  ? 0.44286 0.28071 0.41840 0.00017  0.02293  -0.01112 29  HIS E O   
4631 C CB  . HIS E 28  ? 0.35924 0.19994 0.34546 -0.00602 0.03508  0.00048  29  HIS E CB  
4632 C CG  . HIS E 28  ? 0.44735 0.28803 0.43942 -0.01017 0.04047  0.00484  29  HIS E CG  
4633 N ND1 . HIS E 28  ? 0.41352 0.25553 0.40527 -0.00956 0.04421  0.01006  29  HIS E ND1 
4634 C CD2 . HIS E 28  ? 0.44376 0.28297 0.44190 -0.01495 0.04261  0.00478  29  HIS E CD2 
4635 C CE1 . HIS E 28  ? 0.45762 0.29898 0.45479 -0.01374 0.04829  0.01298  29  HIS E CE1 
4636 N NE2 . HIS E 28  ? 0.36103 0.20053 0.36203 -0.01709 0.04741  0.00997  29  HIS E NE2 
4637 N N   . ARG E 29  ? 0.42851 0.25386 0.39139 0.00215  0.03016  -0.00497 37  ARG E N   
4638 C CA  . ARG E 29  ? 0.43334 0.25462 0.38503 0.00712  0.02657  -0.00739 37  ARG E CA  
4639 C C   . ARG E 29  ? 0.38113 0.19996 0.32344 0.01167  0.02829  -0.00327 37  ARG E C   
4640 O O   . ARG E 29  ? 0.44912 0.26593 0.38260 0.01592  0.02474  -0.00503 37  ARG E O   
4641 C CB  . ARG E 29  ? 0.40803 0.22146 0.35359 0.00730  0.02693  -0.00968 37  ARG E CB  
4642 C CG  . ARG E 29  ? 0.49673 0.31210 0.45036 0.00346  0.02420  -0.01472 37  ARG E CG  
4643 C CD  . ARG E 29  ? 0.76789 0.57766 0.71373 0.00559  0.02087  -0.01946 37  ARG E CD  
4644 N NE  . ARG E 29  ? 0.96373 0.77574 0.90490 0.00918  0.01480  -0.02325 37  ARG E NE  
4645 C CZ  . ARG E 29  ? 1.05514 0.87229 1.00274 0.00796  0.00951  -0.02853 37  ARG E CZ  
4646 N NH1 . ARG E 29  ? 1.05459 0.87537 1.01374 0.00308  0.00966  -0.03079 37  ARG E NH1 
4647 N NH2 . ARG E 29  ? 1.08287 0.90137 1.02521 0.01175  0.00387  -0.03169 37  ARG E NH2 
4648 N N   . SER E 30  ? 0.36597 0.32785 0.37309 -0.01089 0.00104  -0.03867 38  SER E N   
4649 C CA  . SER E 30  ? 0.37961 0.33897 0.38703 -0.01158 0.00034  -0.03581 38  SER E CA  
4650 C C   . SER E 30  ? 0.37223 0.33007 0.38190 -0.01200 -0.00199 -0.03782 38  SER E C   
4651 O O   . SER E 30  ? 0.36951 0.32904 0.38165 -0.01323 -0.00211 -0.03993 38  SER E O   
4652 C CB  . SER E 30  ? 0.33666 0.29750 0.34589 -0.01353 0.00241  -0.03248 38  SER E CB  
4653 O OG  . SER E 30  ? 0.34587 0.30442 0.35605 -0.01463 0.00141  -0.02989 38  SER E OG  
4654 N N   . VAL E 31  ? 0.35437 0.30890 0.36311 -0.01095 -0.00361 -0.03706 39  VAL E N   
4655 C CA  . VAL E 31  ? 0.28836 0.24035 0.29912 -0.01118 -0.00534 -0.03850 39  VAL E CA  
4656 C C   . VAL E 31  ? 0.41786 0.36674 0.42888 -0.01222 -0.00558 -0.03526 39  VAL E C   
4657 O O   . VAL E 31  ? 0.32986 0.27748 0.33907 -0.01116 -0.00548 -0.03233 39  VAL E O   
4658 C CB  . VAL E 31  ? 0.41588 0.36671 0.42634 -0.00878 -0.00700 -0.04038 39  VAL E CB  
4659 C CG1 . VAL E 31  ? 0.39772 0.34522 0.41046 -0.00879 -0.00815 -0.04146 39  VAL E CG1 
4660 C CG2 . VAL E 31  ? 0.32383 0.27785 0.33457 -0.00797 -0.00695 -0.04347 39  VAL E CG2 
4661 N N   . SER E 32  ? 0.39028 0.33784 0.40335 -0.01443 -0.00592 -0.03577 40  SER E N   
4662 C CA  . SER E 32  ? 0.33326 0.27750 0.34703 -0.01584 -0.00640 -0.03306 40  SER E CA  
4663 C C   . SER E 32  ? 0.33175 0.27176 0.34665 -0.01572 -0.00772 -0.03536 40  SER E C   
4664 O O   . SER E 32  ? 0.28594 0.22603 0.30144 -0.01562 -0.00793 -0.03905 40  SER E O   
4665 C CB  . SER E 32  ? 0.30802 0.25390 0.32312 -0.01920 -0.00570 -0.03124 40  SER E CB  
4666 O OG  . SER E 32  ? 0.40019 0.34986 0.41488 -0.01918 -0.00396 -0.02866 40  SER E OG  
4667 N N   . TRP E 33  ? 0.36297 0.29911 0.37830 -0.01561 -0.00832 -0.03305 41  TRP E N   
4668 C CA  . TRP E 33  ? 0.27740 0.20865 0.29404 -0.01566 -0.00911 -0.03481 41  TRP E CA  
4669 C C   . TRP E 33  ? 0.32269 0.25086 0.34014 -0.01894 -0.00933 -0.03324 41  TRP E C   
4670 O O   . TRP E 33  ? 0.32536 0.25396 0.34299 -0.01981 -0.00923 -0.02924 41  TRP E O   
4671 C CB  . TRP E 33  ? 0.28554 0.21446 0.30257 -0.01257 -0.00969 -0.03345 41  TRP E CB  
4672 C CG  . TRP E 33  ? 0.34772 0.27903 0.36438 -0.00964 -0.00998 -0.03531 41  TRP E CG  
4673 C CD1 . TRP E 33  ? 0.25863 0.19350 0.27339 -0.00794 -0.01010 -0.03402 41  TRP E CD1 
4674 C CD2 . TRP E 33  ? 0.26000 0.19015 0.27824 -0.00823 -0.01020 -0.03863 41  TRP E CD2 
4675 N NE1 . TRP E 33  ? 0.36017 0.29646 0.37538 -0.00582 -0.01074 -0.03625 41  TRP E NE1 
4676 C CE2 . TRP E 33  ? 0.34053 0.27417 0.35822 -0.00579 -0.01074 -0.03889 41  TRP E CE2 
4677 C CE3 . TRP E 33  ? 0.30772 0.23397 0.32762 -0.00883 -0.00982 -0.04136 41  TRP E CE3 
4678 C CZ2 . TRP E 33  ? 0.30017 0.23413 0.31970 -0.00387 -0.01107 -0.04136 41  TRP E CZ2 
4679 C CZ3 . TRP E 33  ? 0.32519 0.25140 0.34666 -0.00664 -0.00971 -0.04395 41  TRP E CZ3 
4680 C CH2 . TRP E 33  ? 0.28872 0.21905 0.31037 -0.00416 -0.01040 -0.04371 41  TRP E CH2 
4681 N N   . TYR E 34  ? 0.25620 0.18114 0.27400 -0.02084 -0.00957 -0.03635 42  TYR E N   
4682 C CA  . TYR E 34  ? 0.31336 0.23459 0.33154 -0.02440 -0.01006 -0.03551 42  TYR E CA  
4683 C C   . TYR E 34  ? 0.31513 0.22962 0.33374 -0.02405 -0.01011 -0.03802 42  TYR E C   
4684 O O   . TYR E 34  ? 0.30672 0.22010 0.32528 -0.02191 -0.00957 -0.04138 42  TYR E O   
4685 C CB  . TYR E 34  ? 0.29274 0.21655 0.31012 -0.02825 -0.01020 -0.03688 42  TYR E CB  
4686 C CG  . TYR E 34  ? 0.32573 0.25559 0.34356 -0.02922 -0.00987 -0.03340 42  TYR E CG  
4687 C CD1 . TYR E 34  ? 0.30831 0.24335 0.32578 -0.02714 -0.00892 -0.03393 42  TYR E CD1 
4688 C CD2 . TYR E 34  ? 0.29861 0.22886 0.31751 -0.03221 -0.01031 -0.02938 42  TYR E CD2 
4689 C CE1 . TYR E 34  ? 0.23057 0.17064 0.24862 -0.02784 -0.00807 -0.03066 42  TYR E CE1 
4690 C CE2 . TYR E 34  ? 0.23427 0.17000 0.25411 -0.03284 -0.00956 -0.02575 42  TYR E CE2 
4691 C CZ  . TYR E 34  ? 0.25844 0.19889 0.27779 -0.03056 -0.00826 -0.02646 42  TYR E CZ  
4692 O OH  . TYR E 34  ? 0.24441 0.18985 0.26487 -0.03105 -0.00699 -0.02278 42  TYR E OH  
4693 N N   . GLN E 35  ? 0.30398 0.21387 0.32332 -0.02613 -0.01056 -0.03618 43  GLN E N   
4694 C CA  . GLN E 35  ? 0.28782 0.19035 0.30751 -0.02648 -0.01027 -0.03850 43  GLN E CA  
4695 C C   . GLN E 35  ? 0.37188 0.27143 0.38979 -0.03146 -0.01073 -0.04072 43  GLN E C   
4696 O O   . GLN E 35  ? 0.36729 0.26854 0.38518 -0.03491 -0.01176 -0.03801 43  GLN E O   
4697 C CB  . GLN E 35  ? 0.35200 0.25076 0.37393 -0.02520 -0.01039 -0.03485 43  GLN E CB  
4698 C CG  . GLN E 35  ? 0.34379 0.23462 0.36668 -0.02491 -0.00961 -0.03703 43  GLN E CG  
4699 C CD  . GLN E 35  ? 0.36091 0.24761 0.38611 -0.02530 -0.00987 -0.03321 43  GLN E CD  
4700 O OE1 . GLN E 35  ? 0.46989 0.35554 0.49492 -0.02904 -0.01075 -0.03139 43  GLN E OE1 
4701 N NE2 . GLN E 35  ? 0.36539 0.25007 0.39313 -0.02149 -0.00917 -0.03158 43  GLN E NE2 
4702 N N   . GLN E 36  ? 0.32752 0.22271 0.34384 -0.03190 -0.00992 -0.04546 44  GLN E N   
4703 C CA  . GLN E 36  ? 0.37662 0.26834 0.39014 -0.03673 -0.01029 -0.04838 44  GLN E CA  
4704 C C   . GLN E 36  ? 0.45389 0.33603 0.46705 -0.03734 -0.00942 -0.05045 44  GLN E C   
4705 O O   . GLN E 36  ? 0.48438 0.36268 0.49766 -0.03435 -0.00767 -0.05345 44  GLN E O   
4706 C CB  . GLN E 36  ? 0.40968 0.30428 0.42078 -0.03700 -0.00970 -0.05254 44  GLN E CB  
4707 C CG  . GLN E 36  ? 0.58996 0.47984 0.59729 -0.04157 -0.00976 -0.05640 44  GLN E CG  
4708 C CD  . GLN E 36  ? 0.51491 0.40965 0.52080 -0.04649 -0.01158 -0.05484 44  GLN E CD  
4709 O OE1 . GLN E 36  ? 0.60054 0.50139 0.60566 -0.04678 -0.01163 -0.05566 44  GLN E OE1 
4710 N NE2 . GLN E 36  ? 0.56352 0.45588 0.56952 -0.05041 -0.01309 -0.05220 44  GLN E NE2 
4711 N N   . THR E 37  ? 0.50056 0.37881 0.51357 -0.04121 -0.01050 -0.04869 45  THR E N   
4712 C CA  . THR E 37  ? 0.60810 0.47665 0.62050 -0.04282 -0.00974 -0.05057 45  THR E CA  
4713 C C   . THR E 37  ? 0.58074 0.44593 0.58920 -0.04932 -0.01096 -0.05281 45  THR E C   
4714 O O   . THR E 37  ? 0.60464 0.47552 0.61247 -0.05280 -0.01296 -0.05064 45  THR E O   
4715 C CB  . THR E 37  ? 0.53415 0.40034 0.55039 -0.04170 -0.01007 -0.04591 45  THR E CB  
4716 O OG1 . THR E 37  ? 0.64244 0.51321 0.65950 -0.04492 -0.01219 -0.04154 45  THR E OG1 
4717 C CG2 . THR E 37  ? 0.46042 0.32987 0.48012 -0.03560 -0.00909 -0.04347 45  THR E CG2 
4718 N N   . PRO E 38  ? 0.75899 0.61489 0.76468 -0.05122 -0.00975 -0.05697 46  PRO E N   
4719 C CA  . PRO E 38  ? 0.66410 0.51601 0.66543 -0.05801 -0.01120 -0.05904 46  PRO E CA  
4720 C C   . PRO E 38  ? 0.81941 0.67078 0.82308 -0.06154 -0.01343 -0.05433 46  PRO E C   
4721 O O   . PRO E 38  ? 0.83838 0.68558 0.84554 -0.05954 -0.01277 -0.05195 46  PRO E O   
4722 C CB  . PRO E 38  ? 0.70385 0.54469 0.70183 -0.05822 -0.00868 -0.06460 46  PRO E CB  
4723 C CG  . PRO E 38  ? 0.78105 0.62250 0.78147 -0.05137 -0.00586 -0.06584 46  PRO E CG  
4724 C CD  . PRO E 38  ? 0.59166 0.44033 0.59777 -0.04735 -0.00679 -0.06017 46  PRO E CD  
4725 N N   . GLY E 39  ? 0.82208 0.67815 0.82428 -0.06676 -0.01607 -0.05257 47  GLY E N   
4726 C CA  . GLY E 39  ? 0.90744 0.76335 0.91178 -0.07093 -0.01841 -0.04802 47  GLY E CA  
4727 C C   . GLY E 39  ? 0.86801 0.73305 0.87754 -0.06888 -0.01950 -0.04126 47  GLY E C   
4728 O O   . GLY E 39  ? 0.73308 0.60015 0.74450 -0.07282 -0.02167 -0.03691 47  GLY E O   
4729 N N   . GLN E 40  ? 0.88148 0.75186 0.89326 -0.06292 -0.01797 -0.04018 48  GLN E N   
4730 C CA  . GLN E 40  ? 0.97140 0.85004 0.98725 -0.06072 -0.01852 -0.03417 48  GLN E CA  
4731 C C   . GLN E 40  ? 0.94064 0.82837 0.95582 -0.05996 -0.01858 -0.03392 48  GLN E C   
4732 O O   . GLN E 40  ? 0.94560 0.84023 0.96352 -0.05991 -0.01920 -0.02888 48  GLN E O   
4733 C CB  . GLN E 40  ? 0.77861 0.65643 0.79773 -0.05456 -0.01681 -0.03216 48  GLN E CB  
4734 C CG  . GLN E 40  ? 0.86185 0.73607 0.88449 -0.05500 -0.01729 -0.02769 48  GLN E CG  
4735 C CD  . GLN E 40  ? 0.95985 0.84134 0.98573 -0.05512 -0.01827 -0.02107 48  GLN E CD  
4736 O OE1 . GLN E 40  ? 0.96635 0.85318 0.99183 -0.05852 -0.01957 -0.01944 48  GLN E OE1 
4737 N NE2 . GLN E 40  ? 0.94158 0.82344 0.97076 -0.05127 -0.01744 -0.01698 48  GLN E NE2 
4738 N N   . GLY E 41  ? 0.61458 0.50237 0.62642 -0.05935 -0.01773 -0.03903 49  GLY E N   
4739 C CA  . GLY E 41  ? 0.68664 0.58290 0.69830 -0.05817 -0.01752 -0.03886 49  GLY E CA  
4740 C C   . GLY E 41  ? 0.67657 0.57677 0.69059 -0.05185 -0.01587 -0.03752 49  GLY E C   
4741 O O   . GLY E 41  ? 0.62029 0.51638 0.63534 -0.04799 -0.01474 -0.03807 49  GLY E O   
4742 N N   . LEU E 42  ? 0.41767 0.32604 0.43259 -0.05098 -0.01574 -0.03558 50  LEU E N   
4743 C CA  . LEU E 42  ? 0.43754 0.35002 0.45389 -0.04557 -0.01428 -0.03470 50  LEU E CA  
4744 C C   . LEU E 42  ? 0.45811 0.37213 0.47734 -0.04375 -0.01419 -0.02909 50  LEU E C   
4745 O O   . LEU E 42  ? 0.44721 0.36466 0.46810 -0.04630 -0.01486 -0.02470 50  LEU E O   
4746 C CB  . LEU E 42  ? 0.31962 0.23960 0.33560 -0.04540 -0.01384 -0.03519 50  LEU E CB  
4747 C CG  . LEU E 42  ? 0.39579 0.31594 0.40975 -0.04338 -0.01288 -0.04051 50  LEU E CG  
4748 C CD1 . LEU E 42  ? 0.40649 0.33440 0.42137 -0.04136 -0.01200 -0.03974 50  LEU E CD1 
4749 C CD2 . LEU E 42  ? 0.50400 0.41886 0.51785 -0.03926 -0.01192 -0.04302 50  LEU E CD2 
4750 N N   . GLN E 43  ? 0.30924 0.22097 0.32915 -0.03930 -0.01328 -0.02896 51  GLN E N   
4751 C CA  . GLN E 43  ? 0.35102 0.26385 0.37307 -0.03702 -0.01298 -0.02392 51  GLN E CA  
4752 C C   . GLN E 43  ? 0.33200 0.24939 0.35362 -0.03247 -0.01178 -0.02359 51  GLN E C   
4753 O O   . GLN E 43  ? 0.30652 0.22297 0.32711 -0.02967 -0.01132 -0.02714 51  GLN E O   
4754 C CB  . GLN E 43  ? 0.39727 0.30329 0.42051 -0.03601 -0.01312 -0.02339 51  GLN E CB  
4755 C CG  . GLN E 43  ? 0.47357 0.37435 0.49725 -0.04071 -0.01429 -0.02329 51  GLN E CG  
4756 C CD  . GLN E 43  ? 0.63233 0.53671 0.65774 -0.04419 -0.01531 -0.01827 51  GLN E CD  
4757 O OE1 . GLN E 43  ? 0.69113 0.59592 0.71586 -0.04896 -0.01654 -0.01884 51  GLN E OE1 
4758 N NE2 . GLN E 43  ? 0.61621 0.52337 0.64386 -0.04188 -0.01475 -0.01307 51  GLN E NE2 
4759 N N   . PHE E 44  ? 0.35465 0.27672 0.37702 -0.03183 -0.01118 -0.01924 52  PHE E N   
4760 C CA  . PHE E 44  ? 0.31533 0.24158 0.33662 -0.02807 -0.00995 -0.01880 52  PHE E CA  
4761 C C   . PHE E 44  ? 0.33497 0.25874 0.35607 -0.02430 -0.00977 -0.01748 52  PHE E C   
4762 O O   . PHE E 44  ? 0.33451 0.25617 0.35696 -0.02432 -0.00991 -0.01364 52  PHE E O   
4763 C CB  . PHE E 44  ? 0.38271 0.31415 0.40464 -0.02889 -0.00889 -0.01449 52  PHE E CB  
4764 C CG  . PHE E 44  ? 0.32104 0.25627 0.34124 -0.02544 -0.00729 -0.01412 52  PHE E CG  
4765 C CD1 . PHE E 44  ? 0.28972 0.22727 0.30843 -0.02425 -0.00693 -0.01822 52  PHE E CD1 
4766 C CD2 . PHE E 44  ? 0.25299 0.18932 0.27287 -0.02360 -0.00603 -0.00964 52  PHE E CD2 
4767 C CE1 . PHE E 44  ? 0.24512 0.18573 0.26201 -0.02150 -0.00553 -0.01805 52  PHE E CE1 
4768 C CE2 . PHE E 44  ? 0.25376 0.19291 0.27124 -0.02079 -0.00443 -0.00960 52  PHE E CE2 
4769 C CZ  . PHE E 44  ? 0.33374 0.27493 0.34970 -0.01986 -0.00426 -0.01390 52  PHE E CZ  
4770 N N   . LEU E 45  ? 0.27605 0.20043 0.29574 -0.02114 -0.00956 -0.02035 53  LEU E N   
4771 C CA  . LEU E 45  ? 0.34347 0.26666 0.36282 -0.01751 -0.00957 -0.01881 53  LEU E CA  
4772 C C   . LEU E 45  ? 0.29689 0.22445 0.31410 -0.01555 -0.00860 -0.01620 53  LEU E C   
4773 O O   . LEU E 45  ? 0.31977 0.24725 0.33684 -0.01481 -0.00814 -0.01188 53  LEU E O   
4774 C CB  . LEU E 45  ? 0.32133 0.24283 0.34065 -0.01529 -0.01002 -0.02282 53  LEU E CB  
4775 C CG  . LEU E 45  ? 0.45555 0.37112 0.47692 -0.01591 -0.01045 -0.02457 53  LEU E CG  
4776 C CD1 . LEU E 45  ? 0.30645 0.22120 0.32780 -0.01487 -0.01032 -0.02941 53  LEU E CD1 
4777 C CD2 . LEU E 45  ? 0.35711 0.26982 0.38010 -0.01361 -0.01065 -0.02133 53  LEU E CD2 
4778 N N   . PHE E 46  ? 0.29667 0.22779 0.31206 -0.01474 -0.00809 -0.01883 54  PHE E N   
4779 C CA  . PHE E 46  ? 0.29646 0.23113 0.30917 -0.01306 -0.00689 -0.01714 54  PHE E CA  
4780 C C   . PHE E 46  ? 0.36510 0.30330 0.37677 -0.01325 -0.00629 -0.02066 54  PHE E C   
4781 O O   . PHE E 46  ? 0.28932 0.22728 0.30212 -0.01389 -0.00704 -0.02450 54  PHE E O   
4782 C CB  . PHE E 46  ? 0.35635 0.29025 0.36704 -0.00987 -0.00741 -0.01602 54  PHE E CB  
4783 C CG  . PHE E 46  ? 0.38426 0.31529 0.39666 -0.00857 -0.00902 -0.01800 54  PHE E CG  
4784 C CD1 . PHE E 46  ? 0.24862 0.18009 0.26167 -0.00824 -0.00963 -0.02243 54  PHE E CD1 
4785 C CD2 . PHE E 46  ? 0.27677 0.20477 0.29048 -0.00748 -0.00966 -0.01509 54  PHE E CD2 
4786 C CE1 . PHE E 46  ? 0.31191 0.24073 0.32698 -0.00679 -0.01066 -0.02387 54  PHE E CE1 
4787 C CE2 . PHE E 46  ? 0.28544 0.21080 0.30131 -0.00607 -0.01074 -0.01649 54  PHE E CE2 
4788 C CZ  . PHE E 46  ? 0.32290 0.24861 0.33949 -0.00569 -0.01115 -0.02086 54  PHE E CZ  
4789 N N   . GLU E 47  ? 0.33962 0.28085 0.34912 -0.01264 -0.00465 -0.01921 55  GLU E N   
4790 C CA  . GLU E 47  ? 0.30987 0.25450 0.31830 -0.01250 -0.00372 -0.02205 55  GLU E CA  
4791 C C   . GLU E 47  ? 0.31772 0.26310 0.32229 -0.00992 -0.00328 -0.02223 55  GLU E C   
4792 O O   . GLU E 47  ? 0.45744 0.40208 0.45961 -0.00893 -0.00236 -0.01891 55  GLU E O   
4793 C CB  . GLU E 47  ? 0.33189 0.27946 0.34150 -0.01455 -0.00171 -0.02017 55  GLU E CB  
4794 C CG  . GLU E 47  ? 0.32851 0.27961 0.33709 -0.01412 -0.00019 -0.02243 55  GLU E CG  
4795 C CD  . GLU E 47  ? 0.39702 0.35126 0.40732 -0.01584 0.00222  -0.01977 55  GLU E CD  
4796 O OE1 . GLU E 47  ? 0.47923 0.43322 0.49148 -0.01741 0.00262  -0.01585 55  GLU E OE1 
4797 O OE2 . GLU E 47  ? 0.35939 0.31652 0.36952 -0.01562 0.00376  -0.02134 55  GLU E OE2 
4798 N N   . TYR E 48  ? 0.40208 0.34887 0.40588 -0.00899 -0.00396 -0.02602 56  TYR E N   
4799 C CA  . TYR E 48  ? 0.33263 0.28025 0.33252 -0.00708 -0.00391 -0.02671 56  TYR E CA  
4800 C C   . TYR E 48  ? 0.35969 0.31021 0.35857 -0.00754 -0.00212 -0.02870 56  TYR E C   
4801 O O   . TYR E 48  ? 0.32698 0.27935 0.32875 -0.00868 -0.00199 -0.03108 56  TYR E O   
4802 C CB  . TYR E 48  ? 0.28268 0.22958 0.28284 -0.00553 -0.00644 -0.02896 56  TYR E CB  
4803 C CG  . TYR E 48  ? 0.31323 0.25734 0.31368 -0.00457 -0.00772 -0.02614 56  TYR E CG  
4804 C CD1 . TYR E 48  ? 0.32054 0.26222 0.32473 -0.00540 -0.00830 -0.02557 56  TYR E CD1 
4805 C CD2 . TYR E 48  ? 0.43513 0.37888 0.43189 -0.00303 -0.00817 -0.02383 56  TYR E CD2 
4806 C CE1 . TYR E 48  ? 0.39772 0.33668 0.40265 -0.00450 -0.00921 -0.02273 56  TYR E CE1 
4807 C CE2 . TYR E 48  ? 0.38535 0.32688 0.38275 -0.00210 -0.00921 -0.02077 56  TYR E CE2 
4808 C CZ  . TYR E 48  ? 0.34813 0.28729 0.34995 -0.00275 -0.00965 -0.02017 56  TYR E CZ  
4809 O OH  . TYR E 48  ? 0.48333 0.42017 0.48624 -0.00177 -0.01047 -0.01699 56  TYR E OH  
4810 N N   . PHE E 49  ? 0.35283 0.30354 0.34749 -0.00669 -0.00052 -0.02759 57  PHE E N   
4811 C CA  . PHE E 49  ? 0.33536 0.28815 0.32867 -0.00698 0.00169  -0.02917 57  PHE E CA  
4812 C C   . PHE E 49  ? 0.36419 0.31592 0.35155 -0.00564 0.00205  -0.02947 57  PHE E C   
4813 O O   . PHE E 49  ? 0.35727 0.30695 0.34113 -0.00488 0.00247  -0.02660 57  PHE E O   
4814 C CB  . PHE E 49  ? 0.28198 0.23577 0.27691 -0.00821 0.00486  -0.02629 57  PHE E CB  
4815 C CG  . PHE E 49  ? 0.34570 0.30149 0.33986 -0.00838 0.00769  -0.02747 57  PHE E CG  
4816 C CD1 . PHE E 49  ? 0.38925 0.34798 0.38715 -0.00940 0.00775  -0.03001 57  PHE E CD1 
4817 C CD2 . PHE E 49  ? 0.30250 0.25700 0.29212 -0.00748 0.01056  -0.02599 57  PHE E CD2 
4818 C CE1 . PHE E 49  ? 0.34970 0.31029 0.34746 -0.00948 0.01055  -0.03088 57  PHE E CE1 
4819 C CE2 . PHE E 49  ? 0.30985 0.26561 0.29891 -0.00759 0.01357  -0.02710 57  PHE E CE2 
4820 C CZ  . PHE E 49  ? 0.37553 0.33447 0.36899 -0.00857 0.01353  -0.02946 57  PHE E CZ  
4821 N N   . SER E 50  ? 0.39661 0.34970 0.38268 -0.00549 0.00176  -0.03291 58  SER E N   
4822 C CA  . SER E 50  ? 0.51089 0.46286 0.49075 -0.00475 0.00188  -0.03377 58  SER E CA  
4823 C C   . SER E 50  ? 0.39292 0.34329 0.36987 -0.00373 -0.00099 -0.03247 58  SER E C   
4824 O O   . SER E 50  ? 0.54333 0.49189 0.51432 -0.00324 -0.00038 -0.03098 58  SER E O   
4825 C CB  . SER E 50  ? 0.46508 0.41567 0.44094 -0.00484 0.00597  -0.03188 58  SER E CB  
4826 O OG  . SER E 50  ? 0.77746 0.72668 0.74691 -0.00456 0.00642  -0.03367 58  SER E OG  
4827 N N   . GLU E 51  ? 0.36726 0.31823 0.34843 -0.00339 -0.00391 -0.03285 63  GLU E N   
4828 C CA  . GLU E 51  ? 0.48102 0.43119 0.46128 -0.00231 -0.00693 -0.03162 63  GLU E CA  
4829 C C   . GLU E 51  ? 0.45211 0.40007 0.43096 -0.00176 -0.00647 -0.02738 63  GLU E C   
4830 O O   . GLU E 51  ? 0.44273 0.39011 0.42022 -0.00078 -0.00866 -0.02572 63  GLU E O   
4831 C CB  . GLU E 51  ? 0.38960 0.34035 0.36473 -0.00201 -0.00860 -0.03299 63  GLU E CB  
4832 C CG  . GLU E 51  ? 0.53231 0.48536 0.50915 -0.00252 -0.00945 -0.03696 63  GLU E CG  
4833 C CD  . GLU E 51  ? 0.87288 0.82634 0.84416 -0.00276 -0.01109 -0.03822 63  GLU E CD  
4834 O OE1 . GLU E 51  ? 0.82574 0.77923 0.79507 -0.00219 -0.01385 -0.03655 63  GLU E OE1 
4835 O OE2 . GLU E 51  ? 0.90610 0.85986 0.87497 -0.00366 -0.00963 -0.04073 63  GLU E OE2 
4836 N N   . THR E 52  ? 0.38536 0.33238 0.36492 -0.00236 -0.00371 -0.02520 64  THR E N   
4837 C CA  . THR E 52  ? 0.43194 0.37701 0.41095 -0.00188 -0.00316 -0.02089 64  THR E CA  
4838 C C   . THR E 52  ? 0.46695 0.41174 0.45185 -0.00291 -0.00248 -0.01956 64  THR E C   
4839 O O   . THR E 52  ? 0.40243 0.34862 0.39035 -0.00417 -0.00144 -0.02140 64  THR E O   
4840 C CB  . THR E 52  ? 0.43511 0.37899 0.40822 -0.00160 -0.00015 -0.01850 64  THR E CB  
4841 O OG1 . THR E 52  ? 0.54555 0.49000 0.52033 -0.00258 0.00317  -0.01832 64  THR E OG1 
4842 C CG2 . THR E 52  ? 0.51675 0.46059 0.48314 -0.00121 -0.00053 -0.02063 64  THR E CG2 
4843 N N   . GLN E 53  ? 0.31147 0.25450 0.29797 -0.00256 -0.00318 -0.01624 65  GLN E N   
4844 C CA  . GLN E 53  ? 0.43889 0.38118 0.43051 -0.00391 -0.00276 -0.01466 65  GLN E CA  
4845 C C   . GLN E 53  ? 0.33304 0.27590 0.32424 -0.00487 0.00043  -0.01196 65  GLN E C   
4846 O O   . GLN E 53  ? 0.47009 0.41210 0.45796 -0.00398 0.00214  -0.00860 65  GLN E O   
4847 C CB  . GLN E 53  ? 0.29420 0.23416 0.28775 -0.00326 -0.00431 -0.01172 65  GLN E CB  
4848 C CG  . GLN E 53  ? 0.30506 0.24368 0.30370 -0.00502 -0.00421 -0.01030 65  GLN E CG  
4849 C CD  . GLN E 53  ? 0.37113 0.30701 0.37188 -0.00436 -0.00556 -0.00744 65  GLN E CD  
4850 O OE1 . GLN E 53  ? 0.54031 0.47523 0.54113 -0.00439 -0.00455 -0.00318 65  GLN E OE1 
4851 N NE2 . GLN E 53  ? 0.33899 0.27362 0.34184 -0.00363 -0.00765 -0.00952 65  GLN E NE2 
4852 N N   . ARG E 54  ? 0.39066 0.33512 0.38535 -0.00666 0.00135  -0.01313 66  ARG E N   
4853 C CA  . ARG E 54  ? 0.43869 0.38435 0.43394 -0.00761 0.00448  -0.01020 66  ARG E CA  
4854 C C   . ARG E 54  ? 0.35798 0.30281 0.35714 -0.00895 0.00452  -0.00598 66  ARG E C   
4855 O O   . ARG E 54  ? 0.51609 0.46060 0.51447 -0.00855 0.00672  -0.00161 66  ARG E O   
4856 C CB  . ARG E 54  ? 0.32283 0.27133 0.32017 -0.00897 0.00556  -0.01290 66  ARG E CB  
4857 C CG  . ARG E 54  ? 0.39358 0.34374 0.39158 -0.00960 0.00919  -0.00969 66  ARG E CG  
4858 C CD  . ARG E 54  ? 0.47400 0.42714 0.47358 -0.01048 0.01048  -0.01233 66  ARG E CD  
4859 N NE  . ARG E 54  ? 0.42468 0.37960 0.42557 -0.01092 0.01433  -0.00878 66  ARG E NE  
4860 C CZ  . ARG E 54  ? 0.36440 0.31896 0.36173 -0.00950 0.01774  -0.00838 66  ARG E CZ  
4861 N NH1 . ARG E 54  ? 0.34812 0.30061 0.33977 -0.00785 0.01749  -0.01143 66  ARG E NH1 
4862 N NH2 . ARG E 54  ? 0.42538 0.38162 0.42493 -0.00986 0.02156  -0.00474 66  ARG E NH2 
4863 N N   . ASN E 55  ? 0.38692 0.33118 0.39020 -0.01060 0.00223  -0.00721 67  ASN E N   
4864 C CA  . ASN E 55  ? 0.36689 0.30993 0.37394 -0.01233 0.00173  -0.00367 67  ASN E CA  
4865 C C   . ASN E 55  ? 0.41345 0.35334 0.42195 -0.01230 -0.00115 -0.00517 67  ASN E C   
4866 O O   . ASN E 55  ? 0.31894 0.25825 0.32670 -0.01143 -0.00271 -0.00926 67  ASN E O   
4867 C CB  . ASN E 55  ? 0.41727 0.36266 0.42831 -0.01538 0.00219  -0.00328 67  ASN E CB  
4868 C CG  . ASN E 55  ? 0.54132 0.48990 0.55223 -0.01544 0.00547  -0.00059 67  ASN E CG  
4869 O OD1 . ASN E 55  ? 0.65838 0.60935 0.66851 -0.01531 0.00663  -0.00319 67  ASN E OD1 
4870 N ND2 . ASN E 55  ? 0.57562 0.52422 0.58769 -0.01556 0.00723  0.00487  67  ASN E ND2 
4871 N N   . LYS E 56  ? 0.38070 0.31851 0.39172 -0.01326 -0.00164 -0.00158 68  LYS E N   
4872 C CA  . LYS E 56  ? 0.34893 0.28311 0.36167 -0.01313 -0.00384 -0.00219 68  LYS E CA  
4873 C C   . LYS E 56  ? 0.39099 0.32355 0.40786 -0.01624 -0.00450 -0.00016 68  LYS E C   
4874 O O   . LYS E 56  ? 0.43363 0.36779 0.45191 -0.01766 -0.00324 0.00384  68  LYS E O   
4875 C CB  . LYS E 56  ? 0.41107 0.34375 0.42180 -0.01035 -0.00382 0.00077  68  LYS E CB  
4876 C CG  . LYS E 56  ? 0.62633 0.55533 0.63942 -0.00984 -0.00572 0.00095  68  LYS E CG  
4877 C CD  . LYS E 56  ? 0.60482 0.53337 0.61558 -0.00687 -0.00573 0.00384  68  LYS E CD  
4878 C CE  . LYS E 56  ? 0.61296 0.54261 0.62219 -0.00649 -0.00372 0.00900  68  LYS E CE  
4879 N NZ  . LYS E 56  ? 0.75048 0.67841 0.76416 -0.00847 -0.00359 0.01274  68  LYS E NZ  
4880 N N   . GLY E 57  ? 0.36269 0.29199 0.38148 -0.01742 -0.00635 -0.00287 69  GLY E N   
4881 C CA  . GLY E 57  ? 0.37025 0.29697 0.39240 -0.02065 -0.00730 -0.00140 69  GLY E CA  
4882 C C   . GLY E 57  ? 0.42053 0.34401 0.44434 -0.01976 -0.00760 0.00260  69  GLY E C   
4883 O O   . GLY E 57  ? 0.46068 0.38516 0.48314 -0.01710 -0.00660 0.00591  69  GLY E O   
4884 N N   . ASN E 58  ? 0.42547 0.34477 0.45203 -0.02208 -0.00892 0.00226  70  ASN E N   
4885 C CA  . ASN E 58  ? 0.45213 0.36793 0.48108 -0.02159 -0.00925 0.00605  70  ASN E CA  
4886 C C   . ASN E 58  ? 0.42683 0.33791 0.45642 -0.01990 -0.01008 0.00336  70  ASN E C   
4887 O O   . ASN E 58  ? 0.52515 0.43199 0.55757 -0.02061 -0.01057 0.00525  70  ASN E O   
4888 C CB  . ASN E 58  ? 0.35560 0.26989 0.38784 -0.02577 -0.00994 0.00874  70  ASN E CB  
4889 C CG  . ASN E 58  ? 0.74742 0.66667 0.77982 -0.02805 -0.00925 0.01088  70  ASN E CG  
4890 O OD1 . ASN E 58  ? 0.85437 0.77754 0.88568 -0.02599 -0.00753 0.01398  70  ASN E OD1 
4891 N ND2 . ASN E 58  ? 0.61120 0.53026 0.64486 -0.03237 -0.01046 0.00929  70  ASN E ND2 
4892 N N   . PHE E 59  ? 0.36006 0.27180 0.38751 -0.01764 -0.01012 -0.00075 71  PHE E N   
4893 C CA  . PHE E 59  ? 0.38087 0.28839 0.40959 -0.01593 -0.01062 -0.00305 71  PHE E CA  
4894 C C   . PHE E 59  ? 0.40866 0.31630 0.43789 -0.01234 -0.01046 0.00076  71  PHE E C   
4895 O O   . PHE E 59  ? 0.42367 0.33524 0.45067 -0.01064 -0.00995 0.00370  71  PHE E O   
4896 C CB  . PHE E 59  ? 0.33430 0.24278 0.36119 -0.01491 -0.01072 -0.00846 71  PHE E CB  
4897 C CG  . PHE E 59  ? 0.40506 0.31095 0.43218 -0.01816 -0.01098 -0.01282 71  PHE E CG  
4898 C CD1 . PHE E 59  ? 0.24730 0.15640 0.27298 -0.02103 -0.01100 -0.01390 71  PHE E CD1 
4899 C CD2 . PHE E 59  ? 0.41574 0.31588 0.44445 -0.01841 -0.01101 -0.01565 71  PHE E CD2 
4900 C CE1 . PHE E 59  ? 0.37138 0.27829 0.39677 -0.02427 -0.01139 -0.01776 71  PHE E CE1 
4901 C CE2 . PHE E 59  ? 0.36301 0.26025 0.39102 -0.02159 -0.01109 -0.01986 71  PHE E CE2 
4902 C CZ  . PHE E 59  ? 0.39345 0.29425 0.41960 -0.02463 -0.01145 -0.02092 71  PHE E CZ  
4903 N N   . PRO E 60  ? 0.38855 0.29181 0.42062 -0.01117 -0.01071 0.00092  72  PRO E N   
4904 C CA  . PRO E 60  ? 0.38748 0.29120 0.42049 -0.00781 -0.01067 0.00502  72  PRO E CA  
4905 C C   . PRO E 60  ? 0.33514 0.24322 0.36504 -0.00468 -0.01093 0.00413  72  PRO E C   
4906 O O   . PRO E 60  ? 0.33760 0.24741 0.36554 -0.00474 -0.01112 -0.00014 72  PRO E O   
4907 C CB  . PRO E 60  ? 0.35597 0.25385 0.39323 -0.00741 -0.01067 0.00447  72  PRO E CB  
4908 C CG  . PRO E 60  ? 0.41237 0.30592 0.45055 -0.01133 -0.01062 0.00103  72  PRO E CG  
4909 C CD  . PRO E 60  ? 0.26333 0.16078 0.29784 -0.01288 -0.01082 -0.00248 72  PRO E CD  
4910 N N   . GLY E 61  ? 0.39238 0.30223 0.42181 -0.00205 -0.01103 0.00840  74  GLY E N   
4911 C CA  . GLY E 61  ? 0.25958 0.17372 0.28542 0.00055  -0.01156 0.00827  74  GLY E CA  
4912 C C   . GLY E 61  ? 0.38784 0.30182 0.41494 0.00213  -0.01241 0.00487  74  GLY E C   
4913 O O   . GLY E 61  ? 0.37330 0.29106 0.39721 0.00341  -0.01308 0.00337  74  GLY E O   
4914 N N   . ARG E 62  ? 0.40575 0.31525 0.43750 0.00206  -0.01225 0.00369  75  ARG E N   
4915 C CA  . ARG E 62  ? 0.33420 0.24344 0.36778 0.00383  -0.01264 0.00087  75  ARG E CA  
4916 C C   . ARG E 62  ? 0.38938 0.29992 0.42076 0.00256  -0.01261 -0.00464 75  ARG E C   
4917 O O   . ARG E 62  ? 0.34147 0.25318 0.37367 0.00420  -0.01301 -0.00688 75  ARG E O   
4918 C CB  . ARG E 62  ? 0.30318 0.20659 0.34229 0.00415  -0.01182 0.00097  75  ARG E CB  
4919 C CG  . ARG E 62  ? 0.37695 0.27518 0.41694 0.00087  -0.01085 -0.00199 75  ARG E CG  
4920 C CD  . ARG E 62  ? 0.53370 0.42550 0.57874 0.00127  -0.00978 -0.00142 75  ARG E CD  
4921 N NE  . ARG E 62  ? 0.39225 0.27867 0.43774 -0.00236 -0.00910 -0.00305 75  ARG E NE  
4922 C CZ  . ARG E 62  ? 0.41642 0.29860 0.46160 -0.00437 -0.00832 -0.00806 75  ARG E CZ  
4923 N NH1 . ARG E 62  ? 0.44606 0.32855 0.49104 -0.00278 -0.00781 -0.01174 75  ARG E NH1 
4924 N NH2 . ARG E 62  ? 0.39061 0.26819 0.43555 -0.00818 -0.00809 -0.00928 75  ARG E NH2 
4925 N N   . PHE E 63  ? 0.30783 0.25362 0.29350 0.01948  0.00884  0.01407  76  PHE E N   
4926 C CA  . PHE E 63  ? 0.30866 0.25796 0.29945 0.01643  0.00661  0.01282  76  PHE E CA  
4927 C C   . PHE E 63  ? 0.32345 0.27824 0.31882 0.01918  0.00370  0.01166  76  PHE E C   
4928 O O   . PHE E 63  ? 0.38544 0.34159 0.38095 0.01991  0.00304  0.01278  76  PHE E O   
4929 C CB  . PHE E 63  ? 0.26461 0.21239 0.25518 0.01059  0.00687  0.01448  76  PHE E CB  
4930 C CG  . PHE E 63  ? 0.25136 0.19431 0.23803 0.00722  0.00966  0.01513  76  PHE E CG  
4931 C CD1 . PHE E 63  ? 0.27847 0.21719 0.26047 0.00719  0.01251  0.01654  76  PHE E CD1 
4932 C CD2 . PHE E 63  ? 0.29132 0.23372 0.27888 0.00385  0.00973  0.01419  76  PHE E CD2 
4933 C CE1 . PHE E 63  ? 0.30368 0.23786 0.28235 0.00397  0.01526  0.01682  76  PHE E CE1 
4934 C CE2 . PHE E 63  ? 0.30190 0.24015 0.28602 0.00067  0.01237  0.01448  76  PHE E CE2 
4935 C CZ  . PHE E 63  ? 0.27489 0.20910 0.25476 0.00077  0.01508  0.01571  76  PHE E CZ  
4936 N N   . SER E 64  ? 0.26617 0.22432 0.26552 0.02060  0.00216  0.00907  77  SER E N   
4937 C CA  . SER E 64  ? 0.34630 0.30973 0.35048 0.02299  -0.00044 0.00745  77  SER E CA  
4938 C C   . SER E 64  ? 0.34284 0.30819 0.35170 0.02037  -0.00166 0.00542  77  SER E C   
4939 O O   . SER E 64  ? 0.29251 0.25585 0.30070 0.01793  -0.00040 0.00468  77  SER E O   
4940 C CB  . SER E 64  ? 0.26530 0.23167 0.26923 0.02927  -0.00086 0.00562  77  SER E CB  
4941 O OG  . SER E 64  ? 0.31185 0.27926 0.31670 0.03111  -0.00057 0.00290  77  SER E OG  
4942 N N   . GLY E 65  ? 0.30601 0.27502 0.31951 0.02079  -0.00390 0.00439  78  GLY E N   
4943 C CA  . GLY E 65  ? 0.34507 0.31513 0.36280 0.01806  -0.00485 0.00266  78  GLY E CA  
4944 C C   . GLY E 65  ? 0.29669 0.27199 0.31984 0.02117  -0.00671 -0.00035 78  GLY E C   
4945 O O   . GLY E 65  ? 0.35084 0.32938 0.37440 0.02554  -0.00750 -0.00105 78  GLY E O   
4946 N N   . ARG E 66  ? 0.38776 0.36359 0.41483 0.01860  -0.00723 -0.00214 79  ARG E N   
4947 C CA  . ARG E 66  ? 0.31855 0.29923 0.35136 0.02079  -0.00848 -0.00587 79  ARG E CA  
4948 C C   . ARG E 66  ? 0.30935 0.28794 0.34504 0.01633  -0.00859 -0.00640 79  ARG E C   
4949 O O   . ARG E 66  ? 0.34369 0.31804 0.37688 0.01214  -0.00722 -0.00514 79  ARG E O   
4950 C CB  . ARG E 66  ? 0.36397 0.34863 0.39811 0.02411  -0.00768 -0.00982 79  ARG E CB  
4951 C CG  . ARG E 66  ? 0.64824 0.63945 0.68793 0.02783  -0.00913 -0.01405 79  ARG E CG  
4952 C CD  . ARG E 66  ? 0.78200 0.77759 0.82281 0.03126  -0.00853 -0.01817 79  ARG E CD  
4953 N NE  . ARG E 66  ? 0.93607 0.92836 0.97119 0.03208  -0.00708 -0.01617 79  ARG E NE  
4954 C CZ  . ARG E 66  ? 1.10335 1.09838 1.13796 0.03576  -0.00662 -0.01890 79  ARG E CZ  
4955 N NH1 . ARG E 66  ? 0.86124 0.86321 0.90074 0.03916  -0.00765 -0.02398 79  ARG E NH1 
4956 N NH2 . ARG E 66  ? 1.14571 1.13656 1.17491 0.03615  -0.00513 -0.01673 79  ARG E NH2 
4957 N N   . GLN E 67  ? 0.33754 0.31873 0.37813 0.01720  -0.01008 -0.00826 80  GLN E N   
4958 C CA  . GLN E 67  ? 0.37386 0.35271 0.41733 0.01338  -0.00990 -0.00926 80  GLN E CA  
4959 C C   . GLN E 67  ? 0.35817 0.34232 0.40804 0.01546  -0.01018 -0.01433 80  GLN E C   
4960 O O   . GLN E 67  ? 0.42343 0.41224 0.47608 0.01949  -0.01175 -0.01575 80  GLN E O   
4961 C CB  . GLN E 67  ? 0.29324 0.26803 0.33592 0.01135  -0.01150 -0.00571 80  GLN E CB  
4962 C CG  . GLN E 67  ? 0.26933 0.23978 0.31334 0.00721  -0.01105 -0.00595 80  GLN E CG  
4963 C CD  . GLN E 67  ? 0.34952 0.31593 0.39276 0.00606  -0.01305 -0.00255 80  GLN E CD  
4964 O OE1 . GLN E 67  ? 0.31310 0.28207 0.35830 0.00908  -0.01510 -0.00203 80  GLN E OE1 
4965 N NE2 . GLN E 67  ? 0.30667 0.26674 0.34683 0.00181  -0.01251 -0.00030 80  GLN E NE2 
4966 N N   . PHE E 68  ? 0.29941 0.28308 0.35163 0.01250  -0.00848 -0.01734 81  PHE E N   
4967 C CA  . PHE E 68  ? 0.30094 0.28989 0.35968 0.01372  -0.00825 -0.02293 81  PHE E CA  
4968 C C   . PHE E 68  ? 0.39615 0.38214 0.45821 0.01112  -0.00865 -0.02312 81  PHE E C   
4969 O O   . PHE E 68  ? 0.44278 0.42248 0.50178 0.00861  -0.00926 -0.01879 81  PHE E O   
4970 C CB  . PHE E 68  ? 0.31396 0.30458 0.37392 0.01184  -0.00582 -0.02682 81  PHE E CB  
4971 C CG  . PHE E 68  ? 0.35878 0.35168 0.41548 0.01458  -0.00541 -0.02676 81  PHE E CG  
4972 C CD1 . PHE E 68  ? 0.30775 0.30787 0.36671 0.02021  -0.00643 -0.03016 81  PHE E CD1 
4973 C CD2 . PHE E 68  ? 0.39450 0.38210 0.44558 0.01169  -0.00402 -0.02334 81  PHE E CD2 
4974 C CE1 . PHE E 68  ? 0.33763 0.33893 0.39305 0.02312  -0.00607 -0.02989 81  PHE E CE1 
4975 C CE2 . PHE E 68  ? 0.41709 0.40612 0.46515 0.01428  -0.00347 -0.02335 81  PHE E CE2 
4976 C CZ  . PHE E 68  ? 0.47622 0.47175 0.52632 0.02010  -0.00450 -0.02650 81  PHE E CZ  
4977 N N   . SER E 69  ? 0.37912 0.36968 0.44756 0.01182  -0.00828 -0.02842 83  SER E N   
4978 C CA  . SER E 69  ? 0.43569 0.42355 0.50779 0.00992  -0.00856 -0.02910 83  SER E CA  
4979 C C   . SER E 69  ? 0.40734 0.38693 0.47723 0.00386  -0.00640 -0.02749 83  SER E C   
4980 O O   . SER E 69  ? 0.43546 0.40971 0.50569 0.00209  -0.00689 -0.02571 83  SER E O   
4981 C CB  . SER E 69  ? 0.45975 0.45506 0.53952 0.01209  -0.00843 -0.03579 83  SER E CB  
4982 O OG  . SER E 69  ? 0.62349 0.62196 0.70581 0.01028  -0.00598 -0.04065 83  SER E OG  
4983 N N   . ASN E 70  ? 0.40199 0.38010 0.46934 0.00075  -0.00398 -0.02806 84  ASN E N   
4984 C CA  . ASN E 70  ? 0.32980 0.29952 0.39358 -0.00516 -0.00176 -0.02592 84  ASN E CA  
4985 C C   . ASN E 70  ? 0.39270 0.35589 0.44871 -0.00660 -0.00270 -0.01926 84  ASN E C   
4986 O O   . ASN E 70  ? 0.40389 0.36085 0.45545 -0.01127 -0.00075 -0.01730 84  ASN E O   
4987 C CB  . ASN E 70  ? 0.37328 0.34486 0.43846 -0.00835 0.00166  -0.03037 84  ASN E CB  
4988 C CG  . ASN E 70  ? 0.43678 0.41220 0.49931 -0.00661 0.00185  -0.03032 84  ASN E CG  
4989 O OD1 . ASN E 70  ? 0.55834 0.53424 0.61740 -0.00338 -0.00028 -0.02667 84  ASN E OD1 
4990 N ND2 . ASN E 70  ? 0.48212 0.46012 0.54634 -0.00885 0.00461  -0.03460 84  ASN E ND2 
4991 N N   . SER E 71  ? 0.36064 0.32554 0.41493 -0.00279 -0.00547 -0.01609 85  SER E N   
4992 C CA  . SER E 71  ? 0.45131 0.41169 0.49912 -0.00342 -0.00675 -0.01033 85  SER E CA  
4993 C C   . SER E 71  ? 0.37593 0.33606 0.41918 -0.00497 -0.00508 -0.00941 85  SER E C   
4994 O O   . SER E 71  ? 0.36847 0.32550 0.40648 -0.00561 -0.00592 -0.00510 85  SER E O   
4995 C CB  . SER E 71  ? 0.32184 0.27374 0.36614 -0.00695 -0.00719 -0.00644 85  SER E CB  
4996 O OG  . SER E 71  ? 0.54549 0.49712 0.59336 -0.00480 -0.00931 -0.00638 85  SER E OG  
4997 N N   . ARG E 72  ? 0.38633 0.34987 0.43165 -0.00558 -0.00275 -0.01360 86  ARG E N   
4998 C CA  . ARG E 72  ? 0.35000 0.31411 0.39161 -0.00609 -0.00137 -0.01314 86  ARG E CA  
4999 C C   . ARG E 72  ? 0.39127 0.35887 0.43156 -0.00129 -0.00323 -0.01147 86  ARG E C   
5000 O O   . ARG E 72  ? 0.36506 0.33755 0.40898 0.00312  -0.00488 -0.01309 86  ARG E O   
5001 C CB  . ARG E 72  ? 0.42241 0.39084 0.46760 -0.00669 0.00116  -0.01874 86  ARG E CB  
5002 C CG  . ARG E 72  ? 0.67521 0.64371 0.71671 -0.00747 0.00282  -0.01858 86  ARG E CG  
5003 C CD  . ARG E 72  ? 0.55502 0.52821 0.60053 -0.00807 0.00527  -0.02456 86  ARG E CD  
5004 N NE  . ARG E 72  ? 0.63932 0.62069 0.69018 -0.00239 0.00400  -0.02889 86  ARG E NE  
5005 C CZ  . ARG E 72  ? 0.59949 0.58471 0.64942 0.00220  0.00325  -0.02943 86  ARG E CZ  
5006 N NH1 . ARG E 72  ? 0.61472 0.59644 0.65910 0.00165  0.00389  -0.02620 86  ARG E NH1 
5007 N NH2 . ARG E 72  ? 0.51973 0.51228 0.57413 0.00758  0.00185  -0.03334 86  ARG E NH2 
5008 N N   . SER E 73  ? 0.30217 0.26701 0.33699 -0.00235 -0.00276 -0.00825 87  SER E N   
5009 C CA  . SER E 73  ? 0.28603 0.25269 0.31863 0.00141  -0.00400 -0.00616 87  SER E CA  
5010 C C   . SER E 73  ? 0.33116 0.29846 0.36100 0.00189  -0.00212 -0.00694 87  SER E C   
5011 O O   . SER E 73  ? 0.36161 0.32624 0.38937 -0.00188 -0.00008 -0.00726 87  SER E O   
5012 C CB  . SER E 73  ? 0.23941 0.20184 0.26797 -0.00001 -0.00547 -0.00117 87  SER E CB  
5013 O OG  . SER E 73  ? 0.29448 0.25842 0.32076 0.00297  -0.00602 0.00054  87  SER E OG  
5014 N N   . GLU E 74  ? 0.28388 0.25446 0.31343 0.00665  -0.00272 -0.00724 88  GLU E N   
5015 C CA  . GLU E 74  ? 0.29330 0.26389 0.31983 0.00802  -0.00113 -0.00765 88  GLU E CA  
5016 C C   . GLU E 74  ? 0.33834 0.30652 0.36014 0.00950  -0.00149 -0.00373 88  GLU E C   
5017 O O   . GLU E 74  ? 0.39480 0.36417 0.41705 0.01186  -0.00319 -0.00222 88  GLU E O   
5018 C CB  . GLU E 74  ? 0.23321 0.20964 0.26317 0.01289  -0.00112 -0.01215 88  GLU E CB  
5019 C CG  . GLU E 74  ? 0.41096 0.38976 0.44477 0.01086  0.00036  -0.01674 88  GLU E CG  
5020 C CD  . GLU E 74  ? 0.38433 0.36985 0.42184 0.01605  0.00007  -0.02167 88  GLU E CD  
5021 O OE1 . GLU E 74  ? 0.51189 0.50017 0.54894 0.02148  -0.00158 -0.02138 88  GLU E OE1 
5022 O OE2 . GLU E 74  ? 0.49981 0.48804 0.54057 0.01471  0.00151  -0.02602 88  GLU E OE2 
5023 N N   . MET E 75  ? 0.30266 0.26755 0.32014 0.00787  0.00036  -0.00240 89  MET E N   
5024 C CA  . MET E 75  ? 0.31788 0.28000 0.33064 0.00874  0.00078  0.00085  89  MET E CA  
5025 C C   . MET E 75  ? 0.32454 0.28664 0.33513 0.01198  0.00246  -0.00053 89  MET E C   
5026 O O   . MET E 75  ? 0.39961 0.36188 0.41083 0.01102  0.00387  -0.00299 89  MET E O   
5027 C CB  . MET E 75  ? 0.37603 0.33349 0.38518 0.00336  0.00156  0.00388  89  MET E CB  
5028 C CG  . MET E 75  ? 0.53361 0.48848 0.53846 0.00347  0.00219  0.00686  89  MET E CG  
5029 S SD  . MET E 75  ? 0.50826 0.45840 0.50875 -0.00260 0.00409  0.00861  89  MET E SD  
5030 C CE  . MET E 75  ? 0.49862 0.44651 0.49543 -0.00043 0.00698  0.00812  89  MET E CE  
5031 N N   . ASN E 76  ? 0.29175 0.25346 0.29966 0.01590  0.00239  0.00095  90  ASN E N   
5032 C CA  . ASN E 76  ? 0.29200 0.25314 0.29732 0.02005  0.00372  -0.00013 90  ASN E CA  
5033 C C   . ASN E 76  ? 0.32463 0.28063 0.32401 0.02011  0.00536  0.00332  90  ASN E C   
5034 O O   . ASN E 76  ? 0.33971 0.29495 0.33786 0.01960  0.00481  0.00585  90  ASN E O   
5035 C CB  . ASN E 76  ? 0.34910 0.31538 0.35697 0.02633  0.00203  -0.00265 90  ASN E CB  
5036 C CG  . ASN E 76  ? 0.55332 0.51856 0.55757 0.03156  0.00303  -0.00332 90  ASN E CG  
5037 O OD1 . ASN E 76  ? 0.47914 0.44187 0.47891 0.03464  0.00338  -0.00090 90  ASN E OD1 
5038 N ND2 . ASN E 76  ? 0.44258 0.40956 0.44859 0.03264  0.00359  -0.00671 90  ASN E ND2 
5039 N N   . VAL E 77  ? 0.32993 0.28241 0.32586 0.02055  0.00758  0.00314  91  VAL E N   
5040 C CA  . VAL E 77  ? 0.33495 0.28201 0.32494 0.02150  0.00967  0.00582  91  VAL E CA  
5041 C C   . VAL E 77  ? 0.41738 0.36399 0.40522 0.02783  0.01018  0.00437  91  VAL E C   
5042 O O   . VAL E 77  ? 0.39005 0.33726 0.37900 0.02876  0.01072  0.00173  91  VAL E O   
5043 C CB  . VAL E 77  ? 0.38733 0.32949 0.37451 0.01606  0.01212  0.00711  91  VAL E CB  
5044 C CG1 . VAL E 77  ? 0.31651 0.25316 0.29809 0.01605  0.01437  0.00998  91  VAL E CG1 
5045 C CG2 . VAL E 77  ? 0.28825 0.23177 0.27797 0.01019  0.01109  0.00775  91  VAL E CG2 
5046 N N   . SER E 78  ? 0.42051 0.36618 0.40512 0.03232  0.00996  0.00596  92  SER E N   
5047 C CA  . SER E 78  ? 0.38783 0.33362 0.37013 0.03931  0.00975  0.00464  92  SER E CA  
5048 C C   . SER E 78  ? 0.38739 0.32603 0.36385 0.04039  0.01264  0.00575  92  SER E C   
5049 O O   . SER E 78  ? 0.41741 0.35627 0.39304 0.04539  0.01245  0.00371  92  SER E O   
5050 C CB  . SER E 78  ? 0.32543 0.27231 0.30546 0.04379  0.00862  0.00612  92  SER E CB  
5051 O OG  . SER E 78  ? 0.38923 0.33039 0.36421 0.04148  0.01078  0.00989  92  SER E OG  
5052 N N   . THR E 79  ? 0.38021 0.31269 0.35284 0.03593  0.01529  0.00866  93  THR E N   
5053 C CA  . THR E 79  ? 0.42744 0.35219 0.39429 0.03644  0.01849  0.00987  93  THR E CA  
5054 C C   . THR E 79  ? 0.35653 0.27817 0.32339 0.02886  0.02068  0.01091  93  THR E C   
5055 O O   . THR E 79  ? 0.57328 0.49333 0.53879 0.02522  0.02151  0.01328  93  THR E O   
5056 C CB  . THR E 79  ? 0.48283 0.40186 0.44268 0.04049  0.02005  0.01285  93  THR E CB  
5057 O OG1 . THR E 79  ? 0.50831 0.43051 0.46766 0.04795  0.01777  0.01173  93  THR E OG1 
5058 C CG2 . THR E 79  ? 0.52976 0.43963 0.48337 0.04050  0.02378  0.01426  93  THR E CG2 
5059 N N   . LEU E 80  ? 0.40622 0.32750 0.37471 0.02650  0.02156  0.00886  94  LEU E N   
5060 C CA  . LEU E 80  ? 0.36964 0.28931 0.33868 0.01918  0.02316  0.00931  94  LEU E CA  
5061 C C   . LEU E 80  ? 0.43467 0.34627 0.39792 0.01737  0.02696  0.01126  94  LEU E C   
5062 O O   . LEU E 80  ? 0.42679 0.33326 0.38610 0.02141  0.02881  0.01124  94  LEU E O   
5063 C CB  . LEU E 80  ? 0.36899 0.29175 0.34201 0.01697  0.02282  0.00608  94  LEU E CB  
5064 C CG  . LEU E 80  ? 0.38239 0.31254 0.36144 0.01584  0.01977  0.00425  94  LEU E CG  
5065 C CD1 . LEU E 80  ? 0.29708 0.23050 0.27976 0.01628  0.01962  0.00026  94  LEU E CD1 
5066 C CD2 . LEU E 80  ? 0.37398 0.30476 0.35404 0.00917  0.01941  0.00593  94  LEU E CD2 
5067 N N   . GLU E 81  ? 0.38544 0.29590 0.34820 0.01136  0.02810  0.01280  95  GLU E N   
5068 C CA  . GLU E 81  ? 0.40532 0.30900 0.36368 0.00796  0.03191  0.01394  95  GLU E CA  
5069 C C   . GLU E 81  ? 0.42766 0.33218 0.38796 0.00198  0.03270  0.01232  95  GLU E C   
5070 O O   . GLU E 81  ? 0.36400 0.27417 0.32853 -0.00063 0.03027  0.01121  95  GLU E O   
5071 C CB  . GLU E 81  ? 0.38610 0.28831 0.34238 0.00540  0.03293  0.01641  95  GLU E CB  
5072 C CG  . GLU E 81  ? 0.43079 0.33199 0.38456 0.01074  0.03253  0.01813  95  GLU E CG  
5073 C CD  . GLU E 81  ? 0.51370 0.40741 0.46161 0.01584  0.03517  0.01881  95  GLU E CD  
5074 O OE1 . GLU E 81  ? 0.55309 0.44053 0.49788 0.01385  0.03851  0.01868  95  GLU E OE1 
5075 O OE2 . GLU E 81  ? 0.76992 0.66383 0.71611 0.02201  0.03387  0.01944  95  GLU E OE2 
5076 N N   . LEU E 82  ? 0.37952 0.27793 0.33630 -0.00020 0.03634  0.01219  96  LEU E N   
5077 C CA  . LEU E 82  ? 0.33717 0.23596 0.29505 -0.00616 0.03754  0.01060  96  LEU E CA  
5078 C C   . LEU E 82  ? 0.36391 0.26733 0.32403 -0.01185 0.03584  0.01134  96  LEU E C   
5079 O O   . LEU E 82  ? 0.38744 0.29439 0.34995 -0.01558 0.03468  0.01000  96  LEU E O   
5080 C CB  . LEU E 82  ? 0.38211 0.27330 0.33560 -0.00798 0.04199  0.01057  96  LEU E CB  
5081 C CG  . LEU E 82  ? 0.54868 0.43394 0.49916 -0.00217 0.04393  0.01001  96  LEU E CG  
5082 C CD1 . LEU E 82  ? 0.43415 0.31128 0.38036 -0.00474 0.04862  0.00995  96  LEU E CD1 
5083 C CD2 . LEU E 82  ? 0.42928 0.31853 0.38334 0.00032  0.04210  0.00710  96  LEU E CD2 
5084 N N   . GLY E 83  ? 0.38420 0.28765 0.34338 -0.01245 0.03565  0.01338  97  GLY E N   
5085 C CA  . GLY E 83  ? 0.25327 0.16131 0.21461 -0.01712 0.03372  0.01401  97  GLY E CA  
5086 C C   . GLY E 83  ? 0.36802 0.28241 0.33355 -0.01599 0.02943  0.01406  97  GLY E C   
5087 O O   . GLY E 83  ? 0.34233 0.26038 0.30956 -0.01939 0.02744  0.01468  97  GLY E O   
5088 N N   . ASP E 84  ? 0.33045 0.24627 0.29773 -0.01122 0.02793  0.01325  98  ASP E N   
5089 C CA  . ASP E 84  ? 0.32317 0.24466 0.29466 -0.01053 0.02427  0.01284  98  ASP E CA  
5090 C C   . ASP E 84  ? 0.43219 0.35544 0.40533 -0.01417 0.02380  0.01116  98  ASP E C   
5091 O O   . ASP E 84  ? 0.42532 0.35251 0.40162 -0.01440 0.02116  0.01079  98  ASP E O   
5092 C CB  . ASP E 84  ? 0.27261 0.19572 0.24572 -0.00409 0.02287  0.01216  98  ASP E CB  
5093 C CG  . ASP E 84  ? 0.36725 0.28925 0.33859 -0.00040 0.02292  0.01398  98  ASP E CG  
5094 O OD1 . ASP E 84  ? 0.41723 0.33925 0.38787 -0.00299 0.02301  0.01565  98  ASP E OD1 
5095 O OD2 . ASP E 84  ? 0.35116 0.27255 0.32174 0.00521  0.02285  0.01356  98  ASP E OD2 
5096 N N   . SER E 85  ? 0.31151 0.23165 0.28244 -0.01707 0.02652  0.01002  99  SER E N   
5097 C CA  . SER E 85  ? 0.34143 0.26302 0.31326 -0.02115 0.02651  0.00839  99  SER E CA  
5098 C C   . SER E 85  ? 0.32860 0.25264 0.30064 -0.02574 0.02444  0.00987  99  SER E C   
5099 O O   . SER E 85  ? 0.42004 0.34321 0.39011 -0.02844 0.02488  0.01124  99  SER E O   
5100 C CB  . SER E 85  ? 0.27153 0.18924 0.24064 -0.02367 0.03003  0.00692  99  SER E CB  
5101 O OG  . SER E 85  ? 0.36187 0.27710 0.33076 -0.01899 0.03171  0.00540  99  SER E OG  
5102 N N   . ALA E 86  ? 0.30923 0.23628 0.28357 -0.02656 0.02225  0.00944  100 ALA E N   
5103 C CA  . ALA E 86  ? 0.36524 0.29423 0.33956 -0.02982 0.01974  0.01119  100 ALA E CA  
5104 C C   . ALA E 86  ? 0.40988 0.34074 0.38625 -0.03050 0.01818  0.01034  100 ALA E C   
5105 O O   . ALA E 86  ? 0.34391 0.27556 0.32260 -0.02809 0.01882  0.00818  100 ALA E O   
5106 C CB  . ALA E 86  ? 0.27778 0.20839 0.25333 -0.02736 0.01748  0.01325  100 ALA E CB  
5107 N N   . LEU E 87  ? 0.28258 0.21408 0.25797 -0.03376 0.01619  0.01191  101 LEU E N   
5108 C CA  . LEU E 87  ? 0.33688 0.26943 0.31395 -0.03425 0.01447  0.01178  101 LEU E CA  
5109 C C   . LEU E 87  ? 0.36413 0.29876 0.34442 -0.03045 0.01152  0.01307  101 LEU E C   
5110 O O   . LEU E 87  ? 0.31914 0.25432 0.29880 -0.03051 0.00956  0.01524  101 LEU E O   
5111 C CB  . LEU E 87  ? 0.34433 0.27557 0.31780 -0.03942 0.01382  0.01310  101 LEU E CB  
5112 C CG  . LEU E 87  ? 0.40912 0.33997 0.38311 -0.04070 0.01257  0.01325  101 LEU E CG  
5113 C CD1 . LEU E 87  ? 0.31656 0.24735 0.29205 -0.04137 0.01522  0.01003  101 LEU E CD1 
5114 C CD2 . LEU E 87  ? 0.30176 0.23071 0.27105 -0.04504 0.01129  0.01553  101 LEU E CD2 
5115 N N   . TYR E 88  ? 0.27167 0.20796 0.25571 -0.02711 0.01121  0.01137  102 TYR E N   
5116 C CA  . TYR E 88  ? 0.33771 0.27629 0.32516 -0.02337 0.00859  0.01210  102 TYR E CA  
5117 C C   . TYR E 88  ? 0.30381 0.24233 0.29249 -0.02511 0.00681  0.01245  102 TYR E C   
5118 O O   . TYR E 88  ? 0.31095 0.24954 0.30114 -0.02592 0.00787  0.01028  102 TYR E O   
5119 C CB  . TYR E 88  ? 0.21890 0.15968 0.20963 -0.01824 0.00915  0.00990  102 TYR E CB  
5120 C CG  . TYR E 88  ? 0.29230 0.23219 0.28114 -0.01584 0.01044  0.01051  102 TYR E CG  
5121 C CD1 . TYR E 88  ? 0.34303 0.28381 0.33213 -0.01339 0.00906  0.01230  102 TYR E CD1 
5122 C CD2 . TYR E 88  ? 0.21115 0.14888 0.19770 -0.01630 0.01329  0.00928  102 TYR E CD2 
5123 C CE1 . TYR E 88  ? 0.32131 0.26048 0.30806 -0.01166 0.01074  0.01296  102 TYR E CE1 
5124 C CE2 . TYR E 88  ? 0.29961 0.23535 0.28382 -0.01428 0.01483  0.01004  102 TYR E CE2 
5125 C CZ  . TYR E 88  ? 0.27156 0.20782 0.25567 -0.01212 0.01367  0.01196  102 TYR E CZ  
5126 O OH  . TYR E 88  ? 0.30348 0.23706 0.28475 -0.01048 0.01568  0.01274  102 TYR E OH  
5127 N N   . LEU E 89  ? 0.26594 0.20420 0.25397 -0.02565 0.00421  0.01502  103 LEU E N   
5128 C CA  . LEU E 89  ? 0.35167 0.28845 0.33956 -0.02754 0.00243  0.01610  103 LEU E CA  
5129 C C   . LEU E 89  ? 0.37929 0.31815 0.37170 -0.02374 0.00003  0.01607  103 LEU E C   
5130 O O   . LEU E 89  ? 0.36584 0.30702 0.35993 -0.02067 -0.00143 0.01680  103 LEU E O   
5131 C CB  . LEU E 89  ? 0.29240 0.22717 0.27587 -0.03068 0.00086  0.01903  103 LEU E CB  
5132 C CG  . LEU E 89  ? 0.34532 0.27785 0.32374 -0.03523 0.00291  0.01918  103 LEU E CG  
5133 C CD1 . LEU E 89  ? 0.37626 0.30865 0.35113 -0.03700 0.00105  0.02161  103 LEU E CD1 
5134 C CD2 . LEU E 89  ? 0.31304 0.24255 0.28939 -0.03857 0.00406  0.01871  103 LEU E CD2 
5135 N N   . CYS E 90  ? 0.35462 0.29263 0.34902 -0.02419 -0.00015 0.01500  104 CYS E N   
5136 C CA  . CYS E 90  ? 0.47422 0.41350 0.47259 -0.02131 -0.00256 0.01511  104 CYS E CA  
5137 C C   . CYS E 90  ? 0.33218 0.26744 0.32818 -0.02388 -0.00428 0.01749  104 CYS E C   
5138 O O   . CYS E 90  ? 0.31356 0.24500 0.30564 -0.02789 -0.00293 0.01806  104 CYS E O   
5139 C CB  . CYS E 90  ? 0.39768 0.33952 0.40109 -0.01904 -0.00151 0.01153  104 CYS E CB  
5140 S SG  . CYS E 90  ? 0.61084 0.54958 0.61422 -0.02305 0.00047  0.00967  104 CYS E SG  
5141 N N   . ALA E 91  ? 0.31580 0.25172 0.31385 -0.02139 -0.00725 0.01893  105 ALA E N   
5142 C CA  . ALA E 91  ? 0.38098 0.31283 0.37681 -0.02276 -0.00944 0.02147  105 ALA E CA  
5143 C C   . ALA E 91  ? 0.35195 0.28441 0.35288 -0.01980 -0.01101 0.02049  105 ALA E C   
5144 O O   . ALA E 91  ? 0.41008 0.34720 0.41577 -0.01602 -0.01184 0.01899  105 ALA E O   
5145 C CB  . ALA E 91  ? 0.28940 0.22149 0.28222 -0.02263 -0.01207 0.02441  105 ALA E CB  
5146 N N   . SER E 92  ? 0.32711 0.25460 0.32681 -0.02160 -0.01120 0.02125  106 SER E N   
5147 C CA  . SER E 92  ? 0.35114 0.27842 0.35563 -0.01921 -0.01242 0.02015  106 SER E CA  
5148 C C   . SER E 92  ? 0.36818 0.29066 0.37011 -0.01900 -0.01544 0.02351  106 SER E C   
5149 O O   . SER E 92  ? 0.35056 0.26812 0.34614 -0.02177 -0.01582 0.02642  106 SER E O   
5150 C CB  . SER E 92  ? 0.26438 0.18987 0.27088 -0.02123 -0.00941 0.01713  106 SER E CB  
5151 O OG  . SER E 92  ? 0.45020 0.36821 0.45194 -0.02503 -0.00859 0.01901  106 SER E OG  
5152 N N   . SER E 93  ? 0.38306 0.30714 0.38984 -0.01542 -0.01772 0.02300  107 SER E N   
5153 C CA  . SER E 93  ? 0.33462 0.25399 0.34001 -0.01444 -0.02068 0.02566  107 SER E CA  
5154 C C   . SER E 93  ? 0.42671 0.34597 0.43816 -0.01217 -0.02087 0.02336  107 SER E C   
5155 O O   . SER E 93  ? 0.34725 0.27231 0.36461 -0.01019 -0.01983 0.01987  107 SER E O   
5156 C CB  . SER E 93  ? 0.30868 0.23127 0.31376 -0.01174 -0.02435 0.02775  107 SER E CB  
5157 O OG  . SER E 93  ? 0.30383 0.23382 0.31507 -0.00828 -0.02491 0.02538  107 SER E OG  
5158 N N   . LEU E 94  ? 0.42689 0.33926 0.43652 -0.01238 -0.02217 0.02529  108 LEU E N   
5159 C CA  . LEU E 94  ? 0.40225 0.31356 0.41748 -0.01052 -0.02220 0.02307  108 LEU E CA  
5160 C C   . LEU E 94  ? 0.30692 0.22612 0.32924 -0.00578 -0.02447 0.02100  108 LEU E C   
5161 O O   . LEU E 94  ? 0.34754 0.27113 0.37601 -0.00440 -0.02316 0.01716  108 LEU E O   
5162 C CB  . LEU E 94  ? 0.39046 0.29244 0.40190 -0.01084 -0.02379 0.02618  108 LEU E CB  
5163 C CG  . LEU E 94  ? 0.40093 0.30037 0.41780 -0.00916 -0.02372 0.02405  108 LEU E CG  
5164 C CD1 . LEU E 94  ? 0.27324 0.17278 0.29342 -0.01204 -0.01928 0.01989  108 LEU E CD1 
5165 C CD2 . LEU E 94  ? 0.38247 0.27158 0.39444 -0.00909 -0.02551 0.02779  108 LEU E CD2 
5166 N N   . ARG E 95  ? 0.41891 0.34052 0.44042 -0.00335 -0.02779 0.02321  109 ARG E N   
5167 C CA  . ARG E 95  ? 0.39620 0.32480 0.42389 0.00097  -0.03004 0.02152  109 ARG E CA  
5168 C C   . ARG E 95  ? 0.34410 0.27958 0.37134 0.00155  -0.03011 0.02146  109 ARG E C   
5169 O O   . ARG E 95  ? 0.32365 0.25811 0.34575 -0.00119 -0.02892 0.02304  109 ARG E O   
5170 C CB  . ARG E 95  ? 0.38196 0.30775 0.41007 0.00364  -0.03391 0.02358  109 ARG E CB  
5171 C CG  . ARG E 95  ? 0.48161 0.39900 0.50924 0.00307  -0.03375 0.02411  109 ARG E CG  
5172 C CD  . ARG E 95  ? 0.61916 0.53271 0.64587 0.00591  -0.03782 0.02674  109 ARG E CD  
5173 N NE  . ARG E 95  ? 0.55264 0.45736 0.57898 0.00571  -0.03747 0.02720  109 ARG E NE  
5174 C CZ  . ARG E 95  ? 0.55290 0.44751 0.57189 0.00331  -0.03713 0.03061  109 ARG E CZ  
5175 N NH1 . ARG E 95  ? 0.49508 0.38753 0.50649 0.00102  -0.03737 0.03382  109 ARG E NH1 
5176 N NH2 . ARG E 95  ? 0.61073 0.49691 0.62967 0.00313  -0.03635 0.03075  109 ARG E NH2 
5177 N N   . ALA E 96  ? 0.34859 0.29091 0.38119 0.00502  -0.03128 0.01950  110 ALA E N   
5178 C CA  . ALA E 96  ? 0.45579 0.40437 0.48825 0.00568  -0.03087 0.01913  110 ALA E CA  
5179 C C   . ALA E 96  ? 0.40879 0.35754 0.43799 0.00544  -0.03329 0.02185  110 ALA E C   
5180 O O   . ALA E 96  ? 0.26020 0.20669 0.28949 0.00668  -0.03632 0.02334  110 ALA E O   
5181 C CB  . ALA E 96  ? 0.25918 0.21471 0.29786 0.00937  -0.03116 0.01617  110 ALA E CB  
5182 N N   . GLU E 97  ? 0.34885 0.30039 0.37524 0.00393  -0.03190 0.02225  111 GLU E N   
5183 C CA  . GLU E 97  ? 0.32365 0.27739 0.34794 0.00368  -0.03378 0.02382  111 GLU E CA  
5184 C C   . GLU E 97  ? 0.32127 0.26952 0.34072 0.00203  -0.03600 0.02677  111 GLU E C   
5185 O O   . GLU E 97  ? 0.28961 0.23936 0.30905 0.00334  -0.03918 0.02781  111 GLU E O   
5186 C CB  . GLU E 97  ? 0.27462 0.23438 0.30433 0.00723  -0.03600 0.02237  111 GLU E CB  
5187 C CG  . GLU E 97  ? 0.37230 0.33736 0.40585 0.00897  -0.03377 0.01965  111 GLU E CG  
5188 C CD  . GLU E 97  ? 0.36985 0.34109 0.40844 0.01210  -0.03556 0.01803  111 GLU E CD  
5189 O OE1 . GLU E 97  ? 0.53608 0.50893 0.57500 0.01247  -0.03814 0.01879  111 GLU E OE1 
5190 O OE2 . GLU E 97  ? 0.47815 0.45301 0.52041 0.01425  -0.03439 0.01576  111 GLU E OE2 
5191 N N   . SER E 98  ? 0.33264 0.27465 0.34778 -0.00080 -0.03431 0.02799  112 SER E N   
5192 C CA  . SER E 98  ? 0.30752 0.24339 0.31676 -0.00258 -0.03604 0.03105  112 SER E CA  
5193 C C   . SER E 98  ? 0.33729 0.27405 0.34112 -0.00555 -0.03540 0.03234  112 SER E C   
5194 O O   . SER E 98  ? 0.32401 0.26305 0.32733 -0.00754 -0.03229 0.03109  112 SER E O   
5195 C CB  . SER E 98  ? 0.31963 0.24797 0.32625 -0.00472 -0.03409 0.03167  112 SER E CB  
5196 O OG  . SER E 98  ? 0.38715 0.30929 0.38623 -0.00747 -0.03461 0.03475  112 SER E OG  
5197 N N   . GLY E 99  ? 0.38298 0.31800 0.38278 -0.00562 -0.03847 0.03471  113 GLY E N   
5198 C CA  . GLY E 99  ? 0.34142 0.27666 0.33545 -0.00873 -0.03808 0.03594  113 GLY E CA  
5199 C C   . GLY E 99  ? 0.34333 0.27130 0.33030 -0.01249 -0.03617 0.03789  113 GLY E C   
5200 O O   . GLY E 99  ? 0.41029 0.33850 0.39250 -0.01559 -0.03504 0.03846  113 GLY E O   
5201 N N   . GLU E 100 ? 0.35451 0.27607 0.34080 -0.01253 -0.03552 0.03865  114 GLU E N   
5202 C CA  . GLU E 100 ? 0.43163 0.34572 0.41132 -0.01637 -0.03319 0.04026  114 GLU E CA  
5203 C C   . GLU E 100 ? 0.40465 0.31927 0.38721 -0.01842 -0.02860 0.03753  114 GLU E C   
5204 O O   . GLU E 100 ? 0.36238 0.27540 0.34900 -0.01732 -0.02756 0.03610  114 GLU E O   
5205 C CB  . GLU E 100 ? 0.34267 0.24868 0.31931 -0.01535 -0.03515 0.04279  114 GLU E CB  
5206 C CG  . GLU E 100 ? 0.62690 0.53220 0.60012 -0.01278 -0.04011 0.04556  114 GLU E CG  
5207 C CD  . GLU E 100 ? 0.66040 0.55746 0.63126 -0.01062 -0.04242 0.04806  114 GLU E CD  
5208 O OE1 . GLU E 100 ? 0.62707 0.52405 0.60409 -0.00788 -0.04274 0.04664  114 GLU E OE1 
5209 O OE2 . GLU E 100 ? 0.73168 0.62207 0.69419 -0.01160 -0.04388 0.05145  114 GLU E OE2 
5210 N N   . LEU E 101 ? 0.33578 0.25287 0.31640 -0.02129 -0.02592 0.03655  115 LEU E N   
5211 C CA  . LEU E 101 ? 0.30270 0.22154 0.28620 -0.02271 -0.02186 0.03364  115 LEU E CA  
5212 C C   . LEU E 101 ? 0.36331 0.27682 0.34124 -0.02734 -0.01868 0.03397  115 LEU E C   
5213 O O   . LEU E 101 ? 0.42693 0.33722 0.39807 -0.03001 -0.01909 0.03627  115 LEU E O   
5214 C CB  . LEU E 101 ? 0.29786 0.22344 0.28374 -0.02216 -0.02084 0.03189  115 LEU E CB  
5215 C CG  . LEU E 101 ? 0.35194 0.28331 0.34323 -0.01805 -0.02329 0.03117  115 LEU E CG  
5216 C CD1 . LEU E 101 ? 0.38541 0.32201 0.37766 -0.01823 -0.02161 0.02972  115 LEU E CD1 
5217 C CD2 . LEU E 101 ? 0.31824 0.25063 0.31570 -0.01494 -0.02332 0.02931  115 LEU E CD2 
5218 N N   . PHE E 102 ? 0.28725 0.20037 0.26821 -0.02829 -0.01545 0.03133  116 PHE E N   
5219 C CA  . PHE E 102 ? 0.38894 0.29808 0.36592 -0.03279 -0.01179 0.03063  116 PHE E CA  
5220 C C   . PHE E 102 ? 0.27597 0.19040 0.25612 -0.03327 -0.00876 0.02727  116 PHE E C   
5221 O O   . PHE E 102 ? 0.29051 0.20869 0.27691 -0.03090 -0.00781 0.02430  116 PHE E O   
5222 C CB  . PHE E 102 ? 0.40129 0.30516 0.37916 -0.03376 -0.01038 0.02996  116 PHE E CB  
5223 C CG  . PHE E 102 ? 0.67647 0.57356 0.65017 -0.03331 -0.01310 0.03358  116 PHE E CG  
5224 C CD1 . PHE E 102 ? 0.60278 0.50117 0.58025 -0.02886 -0.01681 0.03450  116 PHE E CD1 
5225 C CD2 . PHE E 102 ? 0.76941 0.65859 0.73506 -0.03718 -0.01194 0.03609  116 PHE E CD2 
5226 C CE1 . PHE E 102 ? 0.67265 0.56448 0.64619 -0.02794 -0.01952 0.03784  116 PHE E CE1 
5227 C CE2 . PHE E 102 ? 0.81504 0.69713 0.77600 -0.03633 -0.01456 0.03975  116 PHE E CE2 
5228 C CZ  . PHE E 102 ? 0.68491 0.56828 0.64995 -0.03152 -0.01846 0.04062  116 PHE E CZ  
5229 N N   . PHE E 103 ? 0.28925 0.20400 0.26499 -0.03608 -0.00736 0.02767  117 PHE E N   
5230 C CA  . PHE E 103 ? 0.33911 0.25845 0.31721 -0.03615 -0.00480 0.02487  117 PHE E CA  
5231 C C   . PHE E 103 ? 0.38599 0.30379 0.36381 -0.03934 -0.00084 0.02218  117 PHE E C   
5232 O O   . PHE E 103 ? 0.45854 0.37131 0.43152 -0.04324 0.00048  0.02315  117 PHE E O   
5233 C CB  . PHE E 103 ? 0.29730 0.21801 0.27129 -0.03759 -0.00509 0.02620  117 PHE E CB  
5234 C CG  . PHE E 103 ? 0.31715 0.24173 0.29326 -0.03426 -0.00804 0.02730  117 PHE E CG  
5235 C CD1 . PHE E 103 ? 0.35901 0.28241 0.33270 -0.03363 -0.01161 0.03014  117 PHE E CD1 
5236 C CD2 . PHE E 103 ? 0.25487 0.18418 0.23509 -0.03176 -0.00716 0.02539  117 PHE E CD2 
5237 C CE1 . PHE E 103 ? 0.26873 0.19642 0.24489 -0.03081 -0.01415 0.03060  117 PHE E CE1 
5238 C CE2 . PHE E 103 ? 0.26187 0.19467 0.24391 -0.02918 -0.00939 0.02617  117 PHE E CE2 
5239 C CZ  . PHE E 103 ? 0.29894 0.23132 0.27934 -0.02883 -0.01285 0.02856  117 PHE E CZ  
5240 N N   . GLY E 104 ? 0.41031 0.33256 0.39320 -0.03755 0.00109  0.01866  118 GLY E N   
5241 C CA  . GLY E 104 ? 0.36302 0.28544 0.34608 -0.04029 0.00486  0.01548  118 GLY E CA  
5242 C C   . GLY E 104 ? 0.39710 0.31933 0.37552 -0.04311 0.00648  0.01586  118 GLY E C   
5243 O O   . GLY E 104 ? 0.33606 0.25833 0.31139 -0.04297 0.00477  0.01838  118 GLY E O   
5244 N N   . GLU E 105 ? 0.40602 0.32839 0.38432 -0.04584 0.00998  0.01289  119 GLU E N   
5245 C CA  . GLU E 105 ? 0.44292 0.36504 0.41705 -0.04880 0.01191  0.01274  119 GLU E CA  
5246 C C   . GLU E 105 ? 0.43251 0.35877 0.40937 -0.04564 0.01223  0.01128  119 GLU E C   
5247 O O   . GLU E 105 ? 0.44825 0.37430 0.42199 -0.04774 0.01378  0.01110  119 GLU E O   
5248 C CB  . GLU E 105 ? 0.39581 0.31653 0.36872 -0.05311 0.01571  0.00987  119 GLU E CB  
5249 C CG  . GLU E 105 ? 0.58215 0.49715 0.54938 -0.05762 0.01611  0.01207  119 GLU E CG  
5250 C CD  . GLU E 105 ? 0.80494 0.71869 0.77112 -0.06223 0.02035  0.00886  119 GLU E CD  
5251 O OE1 . GLU E 105 ? 0.86316 0.78062 0.83540 -0.06109 0.02240  0.00443  119 GLU E OE1 
5252 O OE2 . GLU E 105 ? 0.78375 0.69312 0.74300 -0.06697 0.02163  0.01057  119 GLU E OE2 
5253 N N   . GLY E 106 ? 0.35424 0.28387 0.33647 -0.04074 0.01098  0.01020  120 GLY E N   
5254 C CA  . GLY E 106 ? 0.35409 0.28661 0.33801 -0.03734 0.01110  0.00952  120 GLY E CA  
5255 C C   . GLY E 106 ? 0.46046 0.39541 0.44740 -0.03592 0.01380  0.00545  120 GLY E C   
5256 O O   . GLY E 106 ? 0.43792 0.37261 0.42505 -0.03868 0.01612  0.00287  120 GLY E O   
5257 N N   . SER E 107 ? 0.36004 0.32624 0.29817 0.06020  0.03158  0.01133  121 SER E N   
5258 C CA  . SER E 107 ? 0.35359 0.32204 0.29724 0.06134  0.03061  0.01190  121 SER E CA  
5259 C C   . SER E 107 ? 0.36779 0.33374 0.31268 0.06184  0.03042  0.01401  121 SER E C   
5260 O O   . SER E 107 ? 0.44786 0.41399 0.39094 0.06226  0.02918  0.01678  121 SER E O   
5261 C CB  . SER E 107 ? 0.32812 0.30218 0.27304 0.06270  0.02817  0.01322  121 SER E CB  
5262 O OG  . SER E 107 ? 0.40192 0.37830 0.34691 0.06215  0.02804  0.01056  121 SER E OG  
5263 N N   . ARG E 108 ? 0.36436 0.32800 0.31266 0.06188  0.03167  0.01271  122 ARG E N   
5264 C CA  . ARG E 108 ? 0.44279 0.40344 0.39305 0.06228  0.03150  0.01398  122 ARG E CA  
5265 C C   . ARG E 108 ? 0.40585 0.36954 0.36186 0.06395  0.03009  0.01643  122 ARG E C   
5266 O O   . ARG E 108 ? 0.37853 0.34328 0.33883 0.06470  0.03070  0.01543  122 ARG E O   
5267 C CB  . ARG E 108 ? 0.32151 0.27803 0.27207 0.06182  0.03361  0.01103  122 ARG E CB  
5268 C CG  . ARG E 108 ? 0.49820 0.45069 0.44945 0.06180  0.03332  0.01136  122 ARG E CG  
5269 C CD  . ARG E 108 ? 0.59935 0.54802 0.54799 0.06123  0.03529  0.00793  122 ARG E CD  
5270 N NE  . ARG E 108 ? 0.68951 0.63755 0.63203 0.05998  0.03598  0.00735  122 ARG E NE  
5271 C CZ  . ARG E 108 ? 0.85170 0.79836 0.79126 0.05913  0.03490  0.00868  122 ARG E CZ  
5272 N NH1 . ARG E 108 ? 0.66475 0.61048 0.60720 0.05927  0.03298  0.01083  122 ARG E NH1 
5273 N NH2 . ARG E 108 ? 0.80914 0.75556 0.74322 0.05817  0.03587  0.00818  122 ARG E NH2 
5274 N N   . LEU E 109 ? 0.31913 0.28465 0.27546 0.06474  0.02835  0.02007  123 LEU E N   
5275 C CA  . LEU E 109 ? 0.39078 0.36014 0.35253 0.06667  0.02705  0.02336  123 LEU E CA  
5276 C C   . LEU E 109 ? 0.38571 0.35147 0.35171 0.06699  0.02708  0.02529  123 LEU E C   
5277 O O   . LEU E 109 ? 0.36800 0.33150 0.33243 0.06634  0.02653  0.02697  123 LEU E O   
5278 C CB  . LEU E 109 ? 0.34537 0.32015 0.30516 0.06784  0.02519  0.02661  123 LEU E CB  
5279 C CG  . LEU E 109 ? 0.27338 0.25291 0.23850 0.07026  0.02387  0.03117  123 LEU E CG  
5280 C CD1 . LEU E 109 ? 0.25935 0.24249 0.22909 0.07143  0.02395  0.03032  123 LEU E CD1 
5281 C CD2 . LEU E 109 ? 0.31198 0.29695 0.27400 0.07171  0.02220  0.03442  123 LEU E CD2 
5282 N N   . THR E 110 ? 0.39197 0.35718 0.36376 0.06798  0.02772  0.02503  124 THR E N   
5283 C CA  . THR E 110 ? 0.37423 0.33627 0.35157 0.06858  0.02769  0.02694  124 THR E CA  
5284 C C   . THR E 110 ? 0.35385 0.32115 0.33722 0.07091  0.02677  0.03158  124 THR E C   
5285 O O   . THR E 110 ? 0.36377 0.33495 0.34951 0.07214  0.02705  0.03135  124 THR E O   
5286 C CB  . THR E 110 ? 0.42430 0.38128 0.40384 0.06829  0.02938  0.02309  124 THR E CB  
5287 O OG1 . THR E 110 ? 0.44645 0.39920 0.42024 0.06646  0.03022  0.01923  124 THR E OG1 
5288 C CG2 . THR E 110 ? 0.40224 0.35587 0.38853 0.06909  0.02925  0.02481  124 THR E CG2 
5289 N N   . VAL E 111 ? 0.34213 0.31014 0.32817 0.07160  0.02571  0.03608  125 VAL E N   
5290 C CA  . VAL E 111 ? 0.37798 0.35135 0.37027 0.07416  0.02504  0.04141  125 VAL E CA  
5291 C C   . VAL E 111 ? 0.43177 0.40071 0.43210 0.07462  0.02579  0.04280  125 VAL E C   
5292 O O   . VAL E 111 ? 0.35089 0.31439 0.35218 0.07325  0.02566  0.04263  125 VAL E O   
5293 C CB  . VAL E 111 ? 0.40414 0.38223 0.39459 0.07511  0.02356  0.04627  125 VAL E CB  
5294 C CG1 . VAL E 111 ? 0.25493 0.23980 0.25173 0.07826  0.02306  0.05213  125 VAL E CG1 
5295 C CG2 . VAL E 111 ? 0.36654 0.34778 0.34857 0.07449  0.02288  0.04403  125 VAL E CG2 
5296 N N   . LEU E 112 ? 0.41153 0.38278 0.41795 0.07656  0.02652  0.04408  126 LEU E N   
5297 C CA  . LEU E 112 ? 0.40165 0.36858 0.41635 0.07728  0.02750  0.04512  126 LEU E CA  
5298 C C   . LEU E 112 ? 0.34069 0.31332 0.36316 0.08013  0.02727  0.05204  126 LEU E C   
5299 O O   . LEU E 112 ? 0.37890 0.35964 0.40028 0.08195  0.02658  0.05512  126 LEU E O   
5300 C CB  . LEU E 112 ? 0.37531 0.33930 0.39115 0.07737  0.02915  0.04056  126 LEU E CB  
5301 C CG  . LEU E 112 ? 0.41682 0.37560 0.42570 0.07508  0.02981  0.03400  126 LEU E CG  
5302 C CD1 . LEU E 112 ? 0.37743 0.33413 0.38831 0.07581  0.03166  0.03039  126 LEU E CD1 
5303 C CD2 . LEU E 112 ? 0.39450 0.34647 0.40227 0.07319  0.02939  0.03231  126 LEU E CD2 
5304 N N   . GLU E 113 ? 0.40677 0.37532 0.43749 0.08064  0.02786  0.05448  127 GLU E N   
5305 C CA  . GLU E 113 ? 0.36866 0.34245 0.40815 0.08367  0.02824  0.06119  127 GLU E CA  
5306 C C   . GLU E 113 ? 0.41251 0.38905 0.45538 0.08560  0.02957  0.06055  127 GLU E C   
5307 O O   . GLU E 113 ? 0.42972 0.41391 0.47699 0.08845  0.02967  0.06586  127 GLU E O   
5308 C CB  . GLU E 113 ? 0.34020 0.30849 0.38878 0.08360  0.02863  0.06420  127 GLU E CB  
5309 C CG  . GLU E 113 ? 0.30744 0.28142 0.36591 0.08688  0.02923  0.07228  127 GLU E CG  
5310 C CD  . GLU E 113 ? 0.55600 0.53942 0.61191 0.08866  0.02804  0.07829  127 GLU E CD  
5311 O OE1 . GLU E 113 ? 0.59082 0.57335 0.64278 0.08717  0.02683  0.07892  127 GLU E OE1 
5312 O OE2 . GLU E 113 ? 0.67375 0.66584 0.73133 0.09172  0.02829  0.08230  127 GLU E OE2 
5313 N N   . ASP E 114 ? 0.48030 0.45149 0.52092 0.08432  0.03063  0.05437  128 ASP E N   
5314 C CA  . ASP E 114 ? 0.48719 0.45928 0.53262 0.08613  0.03227  0.05384  128 ASP E CA  
5315 C C   . ASP E 114 ? 0.44889 0.41726 0.48821 0.08451  0.03307  0.04672  128 ASP E C   
5316 O O   . ASP E 114 ? 0.57823 0.53976 0.61317 0.08225  0.03308  0.04200  128 ASP E O   
5317 C CB  . ASP E 114 ? 0.54128 0.50801 0.59681 0.08729  0.03365  0.05596  128 ASP E CB  
5318 C CG  . ASP E 114 ? 0.67343 0.64009 0.73402 0.08927  0.03565  0.05518  128 ASP E CG  
5319 O OD1 . ASP E 114 ? 0.63827 0.61144 0.69643 0.09034  0.03581  0.05516  128 ASP E OD1 
5320 O OD2 . ASP E 114 ? 0.92407 0.88411 0.99138 0.08976  0.03703  0.05448  128 ASP E OD2 
5321 N N   . LEU E 115 ? 0.53066 0.50400 0.57010 0.08582  0.03377  0.04625  129 LEU E N   
5322 C CA  . LEU E 115 ? 0.40043 0.37148 0.43491 0.08461  0.03474  0.04035  129 LEU E CA  
5323 C C   . LEU E 115 ? 0.52989 0.49501 0.56889 0.08552  0.03700  0.03774  129 LEU E C   
5324 O O   . LEU E 115 ? 0.53638 0.49904 0.57149 0.08476  0.03811  0.03290  129 LEU E O   
5325 C CB  . LEU E 115 ? 0.38322 0.36282 0.41575 0.08533  0.03422  0.04088  129 LEU E CB  
5326 C CG  . LEU E 115 ? 0.40169 0.38719 0.42855 0.08448  0.03193  0.04213  129 LEU E CG  
5327 C CD1 . LEU E 115 ? 0.36324 0.35693 0.38893 0.08512  0.03120  0.04186  129 LEU E CD1 
5328 C CD2 . LEU E 115 ? 0.39314 0.37327 0.41219 0.08160  0.03143  0.03798  129 LEU E CD2 
5329 N N   . ASN E 116 ? 0.53871 0.50160 0.58605 0.08732  0.03785  0.04091  130 ASN E N   
5330 C CA  . ASN E 116 ? 0.62119 0.57751 0.67281 0.08832  0.03999  0.03802  130 ASN E CA  
5331 C C   . ASN E 116 ? 0.59635 0.54369 0.64350 0.08624  0.04007  0.03201  130 ASN E C   
5332 O O   . ASN E 116 ? 0.67716 0.61878 0.72623 0.08708  0.04176  0.02835  130 ASN E O   
5333 C CB  . ASN E 116 ? 0.77239 0.72784 0.83459 0.09063  0.04084  0.04292  130 ASN E CB  
5334 C CG  . ASN E 116 ? 0.85160 0.81681 0.91843 0.09297  0.04066  0.04966  130 ASN E CG  
5335 O OD1 . ASN E 116 ? 0.85981 0.82730 0.93267 0.09417  0.04021  0.05539  130 ASN E OD1 
5336 N ND2 . ASN E 116 ? 0.82386 0.79541 0.88821 0.09375  0.04097  0.04919  130 ASN E ND2 
5337 N N   . LYS E 117 ? 0.58771 0.53401 0.62891 0.08381  0.03828  0.03091  131 LYS E N   
5338 C CA  . LYS E 117 ? 0.55620 0.49501 0.59279 0.08181  0.03806  0.02546  131 LYS E CA  
5339 C C   . LYS E 117 ? 0.56227 0.50140 0.58975 0.08055  0.03856  0.02047  131 LYS E C   
5340 O O   . LYS E 117 ? 0.57826 0.51208 0.60106 0.07914  0.03853  0.01578  131 LYS E O   
5341 C CB  . LYS E 117 ? 0.74089 0.67843 0.77681 0.07993  0.03594  0.02753  131 LYS E CB  
5342 C CG  . LYS E 117 ? 0.67790 0.61455 0.72377 0.08108  0.03558  0.03272  131 LYS E CG  
5343 C CD  . LYS E 117 ? 0.75173 0.69457 0.79795 0.08090  0.03391  0.03895  131 LYS E CD  
5344 C CE  . LYS E 117 ? 0.86156 0.80231 0.90145 0.07814  0.03211  0.03743  131 LYS E CE  
5345 N NZ  . LYS E 117 ? 0.48524 0.43252 0.52486 0.07835  0.03064  0.04361  131 LYS E NZ  
5346 N N   . VAL E 118 ? 0.47271 0.41819 0.49803 0.08108  0.03902  0.02144  132 VAL E N   
5347 C CA  . VAL E 118 ? 0.55810 0.50461 0.57573 0.07981  0.03953  0.01756  132 VAL E CA  
5348 C C   . VAL E 118 ? 0.43669 0.38062 0.45491 0.08129  0.04201  0.01382  132 VAL E C   
5349 O O   . VAL E 118 ? 0.51497 0.46112 0.53877 0.08343  0.04327  0.01558  132 VAL E O   
5350 C CB  . VAL E 118 ? 0.40848 0.36306 0.42415 0.07949  0.03860  0.02021  132 VAL E CB  
5351 C CG1 . VAL E 118 ? 0.37718 0.33248 0.38587 0.07799  0.03920  0.01644  132 VAL E CG1 
5352 C CG2 . VAL E 118 ? 0.33190 0.28942 0.34696 0.07866  0.03628  0.02408  132 VAL E CG2 
5353 N N   . PHE E 119 ? 0.38288 0.32260 0.39524 0.08039  0.04282  0.00889  133 PHE E N   
5354 C CA  . PHE E 119 ? 0.59839 0.53562 0.61028 0.08209  0.04532  0.00502  133 PHE E CA  
5355 C C   . PHE E 119 ? 0.44896 0.38728 0.45324 0.08099  0.04621  0.00182  133 PHE E C   
5356 O O   . PHE E 119 ? 0.41242 0.34918 0.41109 0.07897  0.04508  0.00032  133 PHE E O   
5357 C CB  . PHE E 119 ? 0.46894 0.39867 0.48261 0.08307  0.04579  0.00165  133 PHE E CB  
5358 C CG  . PHE E 119 ? 0.51441 0.44233 0.53689 0.08463  0.04566  0.00450  133 PHE E CG  
5359 C CD1 . PHE E 119 ? 0.51136 0.43918 0.53911 0.08745  0.04782  0.00469  133 PHE E CD1 
5360 C CD2 . PHE E 119 ? 0.49063 0.41706 0.51661 0.08345  0.04359  0.00733  133 PHE E CD2 
5361 C CE1 . PHE E 119 ? 0.57788 0.50397 0.61431 0.08906  0.04797  0.00763  133 PHE E CE1 
5362 C CE2 . PHE E 119 ? 0.66537 0.59024 0.70036 0.08502  0.04373  0.01046  133 PHE E CE2 
5363 C CZ  . PHE E 119 ? 0.54938 0.47398 0.58964 0.08783  0.04596  0.01058  133 PHE E CZ  
5364 N N   . PRO E 120 ? 0.47211 0.41322 0.47644 0.08235  0.04835  0.00103  134 PRO E N   
5365 C CA  . PRO E 120 ? 0.44512 0.38683 0.44316 0.08177  0.04976  -0.00193 134 PRO E CA  
5366 C C   . PRO E 120 ? 0.49148 0.42752 0.48602 0.08289  0.05101  -0.00660 134 PRO E C   
5367 O O   . PRO E 120 ? 0.41381 0.34546 0.41168 0.08444  0.05110  -0.00794 134 PRO E O   
5368 C CB  . PRO E 120 ? 0.34858 0.29520 0.34975 0.08328  0.05175  -0.00065 134 PRO E CB  
5369 C CG  . PRO E 120 ? 0.44355 0.38946 0.45167 0.08561  0.05227  0.00095  134 PRO E CG  
5370 C CD  . PRO E 120 ? 0.42148 0.36571 0.43218 0.08463  0.04975  0.00324  134 PRO E CD  
5371 N N   . PRO E 121 ? 0.48920 0.42531 0.47722 0.08229  0.05195  -0.00923 135 PRO E N   
5372 C CA  . PRO E 121 ? 0.54000 0.47167 0.52409 0.08372  0.05307  -0.01394 135 PRO E CA  
5373 C C   . PRO E 121 ? 0.51615 0.44824 0.50152 0.08710  0.05616  -0.01572 135 PRO E C   
5374 O O   . PRO E 121 ? 0.53078 0.46742 0.51843 0.08793  0.05787  -0.01345 135 PRO E O   
5375 C CB  . PRO E 121 ? 0.46571 0.39875 0.44244 0.08196  0.05307  -0.01514 135 PRO E CB  
5376 C CG  . PRO E 121 ? 0.40723 0.34592 0.38486 0.08090  0.05367  -0.01172 135 PRO E CG  
5377 C CD  . PRO E 121 ? 0.43751 0.37772 0.42139 0.08026  0.05186  -0.00806 135 PRO E CD  
5378 N N   . GLU E 122 ? 0.47624 0.40362 0.46031 0.08913  0.05678  -0.01994 136 GLU E N   
5379 C CA  . GLU E 122 ? 0.50450 0.43215 0.48728 0.09268  0.05989  -0.02266 136 GLU E CA  
5380 C C   . GLU E 122 ? 0.49797 0.42625 0.47263 0.09284  0.06077  -0.02591 136 GLU E C   
5381 O O   . GLU E 122 ? 0.57098 0.49630 0.54165 0.09128  0.05878  -0.02842 136 GLU E O   
5382 C CB  . GLU E 122 ? 0.50672 0.42899 0.49294 0.09534  0.06015  -0.02573 136 GLU E CB  
5383 C CG  . GLU E 122 ? 0.77482 0.69645 0.76960 0.09545  0.05949  -0.02215 136 GLU E CG  
5384 C CD  . GLU E 122 ? 0.94518 0.86398 0.94408 0.09934  0.06163  -0.02404 136 GLU E CD  
5385 O OE1 . GLU E 122 ? 1.14436 1.06676 1.14371 0.10188  0.06448  -0.02317 136 GLU E OE1 
5386 O OE2 . GLU E 122 ? 1.01291 0.92585 1.01496 0.09991  0.06053  -0.02634 136 GLU E OE2 
5387 N N   . VAL E 123 ? 0.48469 0.41731 0.45729 0.09475  0.06377  -0.02545 137 VAL E N   
5388 C CA  . VAL E 123 ? 0.56617 0.50087 0.53153 0.09507  0.06505  -0.02733 137 VAL E CA  
5389 C C   . VAL E 123 ? 0.54770 0.48272 0.51057 0.09964  0.06813  -0.03068 137 VAL E C   
5390 O O   . VAL E 123 ? 0.57489 0.51197 0.54165 0.10224  0.07056  -0.02920 137 VAL E O   
5391 C CB  . VAL E 123 ? 0.40054 0.34088 0.36567 0.09315  0.06604  -0.02320 137 VAL E CB  
5392 C CG1 . VAL E 123 ? 0.41142 0.35390 0.36948 0.09351  0.06749  -0.02467 137 VAL E CG1 
5393 C CG2 . VAL E 123 ? 0.55435 0.49451 0.52184 0.08910  0.06295  -0.02019 137 VAL E CG2 
5394 N N   . ALA E 124 ? 0.58414 0.51754 0.54044 0.10079  0.06798  -0.03515 138 ALA E N   
5395 C CA  . ALA E 124 ? 0.60696 0.54118 0.55953 0.10550  0.07076  -0.03886 138 ALA E CA  
5396 C C   . ALA E 124 ? 0.56066 0.49847 0.50541 0.10599  0.07179  -0.04015 138 ALA E C   
5397 O O   . ALA E 124 ? 0.59145 0.52834 0.53281 0.10295  0.06940  -0.04070 138 ALA E O   
5398 C CB  . ALA E 124 ? 0.45319 0.38120 0.40590 0.10746  0.06931  -0.04445 138 ALA E CB  
5399 N N   . VAL E 125 ? 0.60048 0.54284 0.54264 0.11004  0.07554  -0.04021 139 VAL E N   
5400 C CA  . VAL E 125 ? 0.69341 0.64007 0.62820 0.11163  0.07720  -0.04132 139 VAL E CA  
5401 C C   . VAL E 125 ? 0.63927 0.58501 0.56892 0.11650  0.07811  -0.04736 139 VAL E C   
5402 O O   . VAL E 125 ? 0.68173 0.62734 0.61354 0.12039  0.08026  -0.04839 139 VAL E O   
5403 C CB  . VAL E 125 ? 0.66860 0.62227 0.60465 0.11267  0.08106  -0.03600 139 VAL E CB  
5404 C CG1 . VAL E 125 ? 0.62929 0.58798 0.55803 0.11566  0.08355  -0.03707 139 VAL E CG1 
5405 C CG2 . VAL E 125 ? 0.60953 0.56406 0.54958 0.10765  0.07969  -0.03102 139 VAL E CG2 
5406 N N   . PHE E 126 ? 0.63994 0.58527 0.56277 0.11641  0.07643  -0.05147 140 PHE E N   
5407 C CA  . PHE E 126 ? 0.57233 0.51723 0.48934 0.12094  0.07675  -0.05802 140 PHE E CA  
5408 C C   . PHE E 126 ? 0.70386 0.65650 0.61384 0.12429  0.07992  -0.05739 140 PHE E C   
5409 O O   . PHE E 126 ? 0.69317 0.64881 0.59994 0.12181  0.07940  -0.05526 140 PHE E O   
5410 C CB  . PHE E 126 ? 0.53899 0.47793 0.45400 0.11853  0.07212  -0.06369 140 PHE E CB  
5411 C CG  . PHE E 126 ? 0.72702 0.65860 0.64959 0.11554  0.06925  -0.06388 140 PHE E CG  
5412 C CD1 . PHE E 126 ? 0.75172 0.68162 0.67891 0.11027  0.06707  -0.05926 140 PHE E CD1 
5413 C CD2 . PHE E 126 ? 0.71459 0.64122 0.63988 0.11831  0.06894  -0.06844 140 PHE E CD2 
5414 C CE1 . PHE E 126 ? 0.69797 0.62195 0.63234 0.10792  0.06469  -0.05882 140 PHE E CE1 
5415 C CE2 . PHE E 126 ? 0.71606 0.63624 0.64902 0.11578  0.06663  -0.06801 140 PHE E CE2 
5416 C CZ  . PHE E 126 ? 0.66622 0.58537 0.60375 0.11063  0.06454  -0.06298 140 PHE E CZ  
5417 N N   . GLU E 127 ? 0.75992 0.71606 0.66767 0.13016  0.08338  -0.05891 141 GLU E N   
5418 C CA  . GLU E 127 ? 0.76919 0.73374 0.67130 0.13409  0.08716  -0.05713 141 GLU E CA  
5419 C C   . GLU E 127 ? 0.68889 0.65502 0.58203 0.13551  0.08543  -0.06269 141 GLU E C   
5420 O O   . GLU E 127 ? 0.76631 0.72694 0.65748 0.13505  0.08181  -0.06932 141 GLU E O   
5421 C CB  . GLU E 127 ? 0.78646 0.75465 0.68925 0.14031  0.09150  -0.05672 141 GLU E CB  
5422 C CG  . GLU E 127 ? 0.74554 0.71371 0.65736 0.13913  0.09356  -0.05055 141 GLU E CG  
5423 C CD  . GLU E 127 ? 0.86041 0.83343 0.77303 0.14544  0.09832  -0.04908 141 GLU E CD  
5424 O OE1 . GLU E 127 ? 0.94916 0.92376 0.85553 0.15099  0.09954  -0.05407 141 GLU E OE1 
5425 O OE2 . GLU E 127 ? 0.80629 0.78184 0.72583 0.14494  0.10080  -0.04296 141 GLU E OE2 
5426 N N   . PRO E 128 ? 0.63149 0.60533 0.51957 0.13717  0.08792  -0.05996 142 PRO E N   
5427 C CA  . PRO E 128 ? 0.72317 0.69959 0.60262 0.13839  0.08620  -0.06472 142 PRO E CA  
5428 C C   . PRO E 128 ? 0.82433 0.80068 0.69818 0.14407  0.08591  -0.07265 142 PRO E C   
5429 O O   . PRO E 128 ? 0.73229 0.70961 0.60724 0.14882  0.08878  -0.07323 142 PRO E O   
5430 C CB  . PRO E 128 ? 0.69586 0.68178 0.57223 0.14028  0.09029  -0.05887 142 PRO E CB  
5431 C CG  . PRO E 128 ? 0.74884 0.73462 0.63345 0.13689  0.09227  -0.05101 142 PRO E CG  
5432 C CD  . PRO E 128 ? 0.68358 0.66382 0.57464 0.13705  0.09199  -0.05185 142 PRO E CD  
5433 N N   . SER E 129 ? 0.72950 0.70489 0.59730 0.14363  0.08231  -0.07890 143 SER E N   
5434 C CA  . SER E 129 ? 0.80920 0.78511 0.67156 0.14815  0.08112  -0.08702 143 SER E CA  
5435 C C   . SER E 129 ? 0.87498 0.86207 0.73327 0.15120  0.08375  -0.08442 143 SER E C   
5436 O O   . SER E 129 ? 0.80496 0.79876 0.66064 0.15002  0.08473  -0.07985 143 SER E O   
5437 C CB  . SER E 129 ? 0.84301 0.81447 0.70133 0.14586  0.07581  -0.09446 143 SER E CB  
5438 O OG  . SER E 129 ? 0.86896 0.84474 0.72164 0.14864  0.07429  -0.10060 143 SER E OG  
5439 N N   . GLU E 130 ? 0.83629 0.82533 0.69423 0.15530  0.08496  -0.08706 144 GLU E N   
5440 C CA  . GLU E 130 ? 0.77630 0.77575 0.62980 0.15878  0.08705  -0.08526 144 GLU E CA  
5441 C C   . GLU E 130 ? 0.77320 0.77634 0.61936 0.15827  0.08373  -0.08993 144 GLU E C   
5442 O O   . GLU E 130 ? 0.85090 0.86337 0.69353 0.15949  0.08528  -0.08597 144 GLU E O   
5443 C CB  . GLU E 130 ? 0.88766 0.88770 0.74156 0.16347  0.08852  -0.08818 144 GLU E CB  
5444 N N   . ALA E 131 ? 0.71158 0.70755 0.55590 0.15644  0.07908  -0.09809 145 ALA E N   
5445 C CA  . ALA E 131 ? 0.66612 0.66529 0.50397 0.15549  0.07548  -0.10271 145 ALA E CA  
5446 C C   . ALA E 131 ? 0.86028 0.86367 0.69709 0.15219  0.07592  -0.09645 145 ALA E C   
5447 O O   . ALA E 131 ? 0.96643 0.97815 0.79824 0.15288  0.07577  -0.09524 145 ALA E O   
5448 C CB  . ALA E 131 ? 0.69325 0.68291 0.53095 0.15362  0.07025  -0.11231 145 ALA E CB  
5449 N N   . GLU E 132 ? 0.82586 0.82366 0.66741 0.14872  0.07651  -0.09227 146 GLU E N   
5450 C CA  . GLU E 132 ? 0.79950 0.80093 0.64041 0.14557  0.07725  -0.08601 146 GLU E CA  
5451 C C   . GLU E 132 ? 0.69235 0.70381 0.53373 0.14741  0.08191  -0.07755 146 GLU E C   
5452 O O   . GLU E 132 ? 0.76169 0.77987 0.60008 0.14650  0.08220  -0.07402 146 GLU E O   
5453 C CB  . GLU E 132 ? 0.73571 0.72898 0.58176 0.14190  0.07721  -0.08309 146 GLU E CB  
5454 C CG  . GLU E 132 ? 0.73154 0.72792 0.57684 0.13853  0.07790  -0.07691 146 GLU E CG  
5455 C CD  . GLU E 132 ? 0.88178 0.87296 0.73478 0.13417  0.07898  -0.07042 146 GLU E CD  
5456 O OE1 . GLU E 132 ? 0.81046 0.79615 0.66955 0.13383  0.07933  -0.07024 146 GLU E OE1 
5457 O OE2 . GLU E 132 ? 0.74495 0.73786 0.59871 0.13042  0.07909  -0.06512 146 GLU E OE2 
5458 N N   . ILE E 133 ? 0.72661 0.73919 0.57225 0.15003  0.08556  -0.07396 147 ILE E N   
5459 C CA  . ILE E 133 ? 0.78233 0.80398 0.62963 0.15183  0.09001  -0.06558 147 ILE E CA  
5460 C C   . ILE E 133 ? 0.88738 0.91833 0.72867 0.15525  0.08990  -0.06672 147 ILE E C   
5461 O O   . ILE E 133 ? 1.03385 1.07296 0.87498 0.15582  0.09237  -0.06008 147 ILE E O   
5462 C CB  . ILE E 133 ? 0.77498 0.79567 0.62843 0.15406  0.09367  -0.06191 147 ILE E CB  
5463 N N   . SER E 134 ? 0.93424 0.96408 0.77078 0.15763  0.08699  -0.07508 148 SER E N   
5464 C CA  . SER E 134 ? 0.88776 0.92641 0.71808 0.16117  0.08647  -0.07692 148 SER E CA  
5465 C C   . SER E 134 ? 0.90830 0.94941 0.73343 0.15880  0.08301  -0.07940 148 SER E C   
5466 O O   . SER E 134 ? 0.97009 1.02051 0.79202 0.16036  0.08396  -0.07577 148 SER E O   
5467 C CB  . SER E 134 ? 0.92412 0.96080 0.75159 0.16502  0.08486  -0.08507 148 SER E CB  
5468 O OG  . SER E 134 ? 1.03867 1.07649 0.86983 0.16846  0.08868  -0.08164 148 SER E OG  
5469 N N   . HIS E 135 ? 0.86678 0.89985 0.69132 0.15516  0.07898  -0.08527 149 HIS E N   
5470 C CA  . HIS E 135 ? 0.86783 0.90301 0.68735 0.15302  0.07522  -0.08854 149 HIS E CA  
5471 C C   . HIS E 135 ? 0.83440 0.87309 0.65516 0.14973  0.07676  -0.08051 149 HIS E C   
5472 O O   . HIS E 135 ? 0.74593 0.79066 0.56244 0.14920  0.07521  -0.08025 149 HIS E O   
5473 C CB  . HIS E 135 ? 0.91404 0.93914 0.73317 0.15032  0.07023  -0.09753 149 HIS E CB  
5474 C CG  . HIS E 135 ? 0.91581 0.94255 0.73011 0.14803  0.06586  -0.10170 149 HIS E CG  
5475 N ND1 . HIS E 135 ? 1.09684 1.13390 0.90659 0.14902  0.06612  -0.09878 149 HIS E ND1 
5476 C CD2 . HIS E 135 ? 1.00208 1.02157 0.81586 0.14486  0.06101  -0.10843 149 HIS E CD2 
5477 C CE1 . HIS E 135 ? 1.17670 1.21306 0.98309 0.14649  0.06166  -0.10354 149 HIS E CE1 
5478 N NE2 . HIS E 135 ? 0.95318 0.97892 0.76197 0.14389  0.05844  -0.10951 149 HIS E NE2 
5479 N N   . THR E 136 ? 0.76162 0.79680 0.58832 0.14756  0.07978  -0.07393 150 THR E N   
5480 C CA  . THR E 136 ? 0.68809 0.72496 0.51655 0.14399  0.08103  -0.06685 150 THR E CA  
5481 C C   . THR E 136 ? 0.66456 0.70622 0.49823 0.14466  0.08623  -0.05698 150 THR E C   
5482 O O   . THR E 136 ? 0.72946 0.77334 0.56487 0.14198  0.08754  -0.05075 150 THR E O   
5483 C CB  . THR E 136 ? 0.74808 0.77490 0.57901 0.13957  0.07894  -0.06845 150 THR E CB  
5484 O OG1 . THR E 136 ? 0.75027 0.77089 0.58706 0.13973  0.08113  -0.06688 150 THR E OG1 
5485 C CG2 . THR E 136 ? 0.69752 0.71881 0.52434 0.13866  0.07352  -0.07820 150 THR E CG2 
5486 N N   . GLN E 137 ? 0.80921 0.85234 0.64581 0.14808  0.08917  -0.05534 151 GLN E N   
5487 C CA  . GLN E 137 ? 0.80318 0.84981 0.64596 0.14859  0.09400  -0.04621 151 GLN E CA  
5488 C C   . GLN E 137 ? 0.88851 0.92841 0.73708 0.14421  0.09493  -0.04232 151 GLN E C   
5489 O O   . GLN E 137 ? 0.88824 0.93104 0.74168 0.14306  0.09819  -0.03443 151 GLN E O   
5490 C CB  . GLN E 137 ? 0.70770 0.76464 0.54947 0.14997  0.09611  -0.03978 151 GLN E CB  
5491 N N   . LYS E 138 ? 0.75678 0.78750 0.60512 0.14189  0.09200  -0.04789 152 LYS E N   
5492 C CA  . LYS E 138 ? 0.82942 0.85304 0.68285 0.13820  0.09254  -0.04507 152 LYS E CA  
5493 C C   . LYS E 138 ? 0.75972 0.77501 0.61570 0.13886  0.09156  -0.04982 152 LYS E C   
5494 O O   . LYS E 138 ? 0.71784 0.73105 0.57056 0.14105  0.08917  -0.05692 152 LYS E O   
5495 C CB  . LYS E 138 ? 0.83873 0.85916 0.68926 0.13411  0.08962  -0.04611 152 LYS E CB  
5496 C CG  . LYS E 138 ? 0.59666 0.62429 0.44670 0.13270  0.09123  -0.03964 152 LYS E CG  
5497 C CD  . LYS E 138 ? 0.76666 0.79323 0.61161 0.12984  0.08765  -0.04236 152 LYS E CD  
5498 C CE  . LYS E 138 ? 0.81437 0.84889 0.65878 0.12899  0.08925  -0.03604 152 LYS E CE  
5499 N NZ  . LYS E 138 ? 1.13201 1.17577 0.97565 0.13305  0.09137  -0.03391 152 LYS E NZ  
5500 N N   . ALA E 139 ? 0.69886 0.70941 0.56108 0.13699  0.09342  -0.04585 153 ALA E N   
5501 C CA  . ALA E 139 ? 0.67691 0.68001 0.54294 0.13771  0.09311  -0.04881 153 ALA E CA  
5502 C C   . ALA E 139 ? 0.73903 0.73402 0.61085 0.13081  0.08979  -0.04731 153 ALA E C   
5503 O O   . ALA E 139 ? 0.60034 0.59619 0.47687 0.12765  0.09132  -0.04084 153 ALA E O   
5504 C CB  . ALA E 139 ? 0.52746 0.53412 0.39947 0.14025  0.09735  -0.04374 153 ALA E CB  
5505 N N   . THR E 140 ? 0.71823 0.70554 0.59040 0.12829  0.08506  -0.05311 154 THR E N   
5506 C CA  . THR E 140 ? 0.59055 0.57042 0.46829 0.12177  0.08138  -0.05186 154 THR E CA  
5507 C C   . THR E 140 ? 0.72669 0.70069 0.61161 0.12119  0.08102  -0.05208 154 THR E C   
5508 O O   . THR E 140 ? 0.55203 0.52274 0.43638 0.12374  0.07987  -0.05759 154 THR E O   
5509 C CB  . THR E 140 ? 0.47971 0.45532 0.35384 0.11891  0.07624  -0.05733 154 THR E CB  
5510 O OG1 . THR E 140 ? 0.67435 0.65632 0.54126 0.12016  0.07666  -0.05755 154 THR E OG1 
5511 C CG2 . THR E 140 ? 0.65394 0.62327 0.53365 0.11237  0.07296  -0.05467 154 THR E CG2 
5512 N N   . LEU E 141 ? 0.55796 0.53082 0.44972 0.11798  0.08198  -0.04621 155 LEU E N   
5513 C CA  . LEU E 141 ? 0.57092 0.53807 0.46996 0.11638  0.08086  -0.04595 155 LEU E CA  
5514 C C   . LEU E 141 ? 0.57506 0.53545 0.47667 0.11079  0.07604  -0.04690 155 LEU E C   
5515 O O   . LEU E 141 ? 0.58198 0.54293 0.48233 0.10721  0.07468  -0.04452 155 LEU E O   
5516 C CB  . LEU E 141 ? 0.61462 0.58473 0.52014 0.11607  0.08425  -0.03930 155 LEU E CB  
5517 C CG  . LEU E 141 ? 0.66719 0.64474 0.57186 0.12130  0.08953  -0.03660 155 LEU E CG  
5518 C CD1 . LEU E 141 ? 0.69124 0.67521 0.59319 0.12114  0.09200  -0.03229 155 LEU E CD1 
5519 C CD2 . LEU E 141 ? 0.61434 0.59217 0.52714 0.12168  0.09180  -0.03256 155 LEU E CD2 
5520 N N   . VAL E 142 ? 0.57770 0.53188 0.48303 0.11031  0.07362  -0.05019 156 VAL E N   
5521 C CA  . VAL E 142 ? 0.51308 0.46090 0.42198 0.10547  0.06926  -0.05072 156 VAL E CA  
5522 C C   . VAL E 142 ? 0.56367 0.50863 0.48084 0.10397  0.06940  -0.04726 156 VAL E C   
5523 O O   . VAL E 142 ? 0.70553 0.65028 0.62555 0.10716  0.07138  -0.04794 156 VAL E O   
5524 C CB  . VAL E 142 ? 0.52083 0.46357 0.42766 0.10594  0.06582  -0.05771 156 VAL E CB  
5525 C CG1 . VAL E 142 ? 0.49464 0.43084 0.40702 0.10122  0.06175  -0.05731 156 VAL E CG1 
5526 C CG2 . VAL E 142 ? 0.46692 0.41294 0.36569 0.10682  0.06502  -0.06104 156 VAL E CG2 
5527 N N   . CYS E 143 ? 0.59394 0.53715 0.51479 0.09936  0.06734  -0.04353 157 CYS E N   
5528 C CA  . CYS E 143 ? 0.48119 0.42226 0.40974 0.09760  0.06692  -0.04013 157 CYS E CA  
5529 C C   . CYS E 143 ? 0.58967 0.52472 0.52146 0.09441  0.06274  -0.04137 157 CYS E C   
5530 O O   . CYS E 143 ? 0.51690 0.45086 0.44627 0.09140  0.06020  -0.04139 157 CYS E O   
5531 C CB  . CYS E 143 ? 0.45788 0.40295 0.38863 0.09526  0.06827  -0.03424 157 CYS E CB  
5532 S SG  . CYS E 143 ? 0.69828 0.64201 0.63812 0.09333  0.06758  -0.03026 157 CYS E SG  
5533 N N   . LEU E 144 ? 0.55163 0.48306 0.48926 0.09520  0.06221  -0.04197 158 LEU E N   
5534 C CA  . LEU E 144 ? 0.54133 0.46722 0.48352 0.09259  0.05866  -0.04247 158 LEU E CA  
5535 C C   . LEU E 144 ? 0.51547 0.44173 0.46486 0.09098  0.05860  -0.03735 158 LEU E C   
5536 O O   . LEU E 144 ? 0.54218 0.46951 0.49542 0.09333  0.06077  -0.03627 158 LEU E O   
5537 C CB  . LEU E 144 ? 0.57220 0.49303 0.51569 0.09508  0.05784  -0.04799 158 LEU E CB  
5538 C CG  . LEU E 144 ? 0.63199 0.54955 0.57140 0.09441  0.05505  -0.05334 158 LEU E CG  
5539 C CD1 . LEU E 144 ? 0.69984 0.61125 0.64328 0.09614  0.05375  -0.05825 158 LEU E CD1 
5540 C CD2 . LEU E 144 ? 0.65524 0.57189 0.59520 0.08974  0.05189  -0.05068 158 LEU E CD2 
5541 N N   . ALA E 145 ? 0.54495 0.47078 0.49603 0.08722  0.05612  -0.03417 159 ALA E N   
5542 C CA  . ALA E 145 ? 0.40807 0.33395 0.36598 0.08562  0.05518  -0.02981 159 ALA E CA  
5543 C C   . ALA E 145 ? 0.54523 0.46586 0.50717 0.08423  0.05208  -0.03063 159 ALA E C   
5544 O O   . ALA E 145 ? 0.46432 0.38309 0.42377 0.08201  0.04970  -0.03154 159 ALA E O   
5545 C CB  . ALA E 145 ? 0.42270 0.35262 0.37968 0.08277  0.05480  -0.02537 159 ALA E CB  
5546 N N   . THR E 146 ? 0.46984 0.38825 0.43844 0.08563  0.05222  -0.03006 160 THR E N   
5547 C CA  . THR E 146 ? 0.58966 0.50268 0.56316 0.08492  0.04977  -0.03109 160 THR E CA  
5548 C C   . THR E 146 ? 0.48330 0.39688 0.46487 0.08450  0.04932  -0.02617 160 THR E C   
5549 O O   . THR E 146 ? 0.45672 0.37408 0.44058 0.08572  0.05120  -0.02335 160 THR E O   
5550 C CB  . THR E 146 ? 0.60153 0.50981 0.57540 0.08785  0.05042  -0.03689 160 THR E CB  
5551 O OG1 . THR E 146 ? 0.51435 0.42413 0.49028 0.09125  0.05348  -0.03682 160 THR E OG1 
5552 C CG2 . THR E 146 ? 0.49763 0.40570 0.46336 0.08833  0.05031  -0.04208 160 THR E CG2 
5553 N N   . GLY E 147 ? 0.51102 0.42125 0.49716 0.08280  0.04676  -0.02493 161 GLY E N   
5554 C CA  . GLY E 147 ? 0.48883 0.39929 0.48327 0.08284  0.04625  -0.02033 161 GLY E CA  
5555 C C   . GLY E 147 ? 0.51428 0.43076 0.50948 0.08143  0.04596  -0.01455 161 GLY E C   
5556 O O   . GLY E 147 ? 0.58468 0.50354 0.58566 0.08261  0.04668  -0.01104 161 GLY E O   
5557 N N   . PHE E 148 ? 0.48741 0.40663 0.47701 0.07906  0.04489  -0.01356 162 PHE E N   
5558 C CA  . PHE E 148 ? 0.51875 0.44360 0.50868 0.07777  0.04440  -0.00872 162 PHE E CA  
5559 C C   . PHE E 148 ? 0.49420 0.41901 0.48547 0.07555  0.04165  -0.00541 162 PHE E C   
5560 O O   . PHE E 148 ? 0.48096 0.40209 0.47058 0.07422  0.04014  -0.00708 162 PHE E O   
5561 C CB  . PHE E 148 ? 0.55156 0.48027 0.53474 0.07703  0.04561  -0.00946 162 PHE E CB  
5562 C CG  . PHE E 148 ? 0.46496 0.39201 0.44117 0.07537  0.04488  -0.01200 162 PHE E CG  
5563 C CD1 . PHE E 148 ? 0.49147 0.41604 0.46345 0.07659  0.04622  -0.01672 162 PHE E CD1 
5564 C CD2 . PHE E 148 ? 0.37602 0.30460 0.34964 0.07287  0.04298  -0.00957 162 PHE E CD2 
5565 C CE1 . PHE E 148 ? 0.44377 0.36761 0.40931 0.07524  0.04558  -0.01886 162 PHE E CE1 
5566 C CE2 . PHE E 148 ? 0.42700 0.35446 0.39434 0.07144  0.04246  -0.01158 162 PHE E CE2 
5567 C CZ  . PHE E 148 ? 0.49317 0.41840 0.45654 0.07257  0.04373  -0.01618 162 PHE E CZ  
5568 N N   . PHE E 149 ? 0.43253 0.36194 0.42704 0.07534  0.04098  -0.00062 163 PHE E N   
5569 C CA  . PHE E 149 ? 0.43860 0.36940 0.43426 0.07373  0.03863  0.00333  163 PHE E CA  
5570 C C   . PHE E 149 ? 0.43832 0.37594 0.43426 0.07368  0.03829  0.00739  163 PHE E C   
5571 O O   . PHE E 149 ? 0.44069 0.38139 0.44077 0.07535  0.03929  0.00885  163 PHE E O   
5572 C CB  . PHE E 149 ? 0.41462 0.34217 0.41804 0.07442  0.03763  0.00538  163 PHE E CB  
5573 C CG  . PHE E 149 ? 0.41868 0.34786 0.42369 0.07304  0.03540  0.00988  163 PHE E CG  
5574 C CD1 . PHE E 149 ? 0.43899 0.36524 0.44070 0.07100  0.03386  0.00875  163 PHE E CD1 
5575 C CD2 . PHE E 149 ? 0.37225 0.30659 0.38192 0.07400  0.03487  0.01545  163 PHE E CD2 
5576 C CE1 . PHE E 149 ? 0.45928 0.38736 0.46260 0.06993  0.03197  0.01331  163 PHE E CE1 
5577 C CE2 . PHE E 149 ? 0.44791 0.38438 0.45885 0.07318  0.03301  0.01992  163 PHE E CE2 
5578 C CZ  . PHE E 149 ? 0.59410 0.52731 0.60198 0.07114  0.03163  0.01897  163 PHE E CZ  
5579 N N   . PRO E 150 ? 0.42018 0.36053 0.41186 0.07193  0.03681  0.00918  164 PRO E N   
5580 C CA  . PRO E 150 ? 0.39724 0.33474 0.38407 0.06998  0.03562  0.00810  164 PRO E CA  
5581 C C   . PRO E 150 ? 0.45248 0.38862 0.43216 0.06910  0.03691  0.00380  164 PRO E C   
5582 O O   . PRO E 150 ? 0.43562 0.37198 0.41472 0.07021  0.03891  0.00129  164 PRO E O   
5583 C CB  . PRO E 150 ? 0.44473 0.38697 0.43020 0.06911  0.03394  0.01232  164 PRO E CB  
5584 C CG  . PRO E 150 ? 0.46733 0.41488 0.45282 0.06992  0.03469  0.01300  164 PRO E CG  
5585 C CD  . PRO E 150 ? 0.43651 0.38344 0.42796 0.07191  0.03611  0.01246  164 PRO E CD  
5586 N N   . ASP E 151 ? 0.48665 0.42186 0.46112 0.06729  0.03592  0.00341  165 ASP E N   
5587 C CA  . ASP E 151 ? 0.57032 0.50462 0.53794 0.06655  0.03718  -0.00015 165 ASP E CA  
5588 C C   . ASP E 151 ? 0.51548 0.45437 0.47964 0.06609  0.03812  0.00087  165 ASP E C   
5589 O O   . ASP E 151 ? 0.60418 0.54441 0.56373 0.06463  0.03758  0.00176  165 ASP E O   
5590 C CB  . ASP E 151 ? 0.53526 0.46694 0.49926 0.06488  0.03573  -0.00078 165 ASP E CB  
5591 C CG  . ASP E 151 ? 0.67377 0.60477 0.63092 0.06446  0.03711  -0.00439 165 ASP E CG  
5592 O OD1 . ASP E 151 ? 0.71489 0.64664 0.67078 0.06576  0.03934  -0.00676 165 ASP E OD1 
5593 O OD2 . ASP E 151 ? 0.81942 0.74960 0.77264 0.06297  0.03606  -0.00450 165 ASP E OD2 
5594 N N   . HIS E 152 ? 0.41929 0.36060 0.38632 0.06738  0.03954  0.00076  166 HIS E N   
5595 C CA  . HIS E 152 ? 0.38883 0.33449 0.35425 0.06695  0.04036  0.00146  166 HIS E CA  
5596 C C   . HIS E 152 ? 0.42137 0.36721 0.38604 0.06793  0.04313  -0.00126 166 HIS E C   
5597 O O   . HIS E 152 ? 0.51208 0.46071 0.48060 0.06891  0.04409  -0.00075 166 HIS E O   
5598 C CB  . HIS E 152 ? 0.34447 0.29440 0.31488 0.06752  0.03919  0.00454  166 HIS E CB  
5599 C CG  . HIS E 152 ? 0.42896 0.38052 0.39936 0.06683  0.03671  0.00782  166 HIS E CG  
5600 N ND1 . HIS E 152 ? 0.30210 0.25874 0.27518 0.06729  0.03539  0.01061  166 HIS E ND1 
5601 C CD2 . HIS E 152 ? 0.39217 0.34146 0.36034 0.06593  0.03532  0.00892  166 HIS E CD2 
5602 C CE1 . HIS E 152 ? 0.38868 0.34621 0.36085 0.06696  0.03346  0.01340  166 HIS E CE1 
5603 N NE2 . HIS E 152 ? 0.45343 0.40644 0.42289 0.06605  0.03343  0.01262  166 HIS E NE2 
5604 N N   . VAL E 153 ? 0.37275 0.31618 0.33266 0.06784  0.04446  -0.00391 167 VAL E N   
5605 C CA  . VAL E 153 ? 0.44200 0.38576 0.40108 0.06931  0.04734  -0.00627 167 VAL E CA  
5606 C C   . VAL E 153 ? 0.45059 0.39557 0.40412 0.06838  0.04878  -0.00689 167 VAL E C   
5607 O O   . VAL E 153 ? 0.43699 0.38100 0.38631 0.06688  0.04764  -0.00659 167 VAL E O   
5608 C CB  . VAL E 153 ? 0.43969 0.37962 0.39888 0.07115  0.04803  -0.00931 167 VAL E CB  
5609 C CG1 . VAL E 153 ? 0.41984 0.35868 0.38554 0.07245  0.04729  -0.00853 167 VAL E CG1 
5610 C CG2 . VAL E 153 ? 0.44354 0.38010 0.39860 0.07008  0.04646  -0.01083 167 VAL E CG2 
5611 N N   . GLU E 154 ? 0.44055 0.38795 0.39459 0.06938  0.05147  -0.00734 168 GLU E N   
5612 C CA  . GLU E 154 ? 0.41108 0.35989 0.36079 0.06908  0.05361  -0.00772 168 GLU E CA  
5613 C C   . GLU E 154 ? 0.44744 0.39692 0.39716 0.07166  0.05673  -0.00951 168 GLU E C   
5614 O O   . GLU E 154 ? 0.39895 0.35062 0.35328 0.07284  0.05821  -0.00882 168 GLU E O   
5615 C CB  . GLU E 154 ? 0.37587 0.32796 0.32719 0.06749  0.05386  -0.00550 168 GLU E CB  
5616 C CG  . GLU E 154 ? 0.47388 0.42568 0.42350 0.06527  0.05113  -0.00396 168 GLU E CG  
5617 C CD  . GLU E 154 ? 0.59050 0.54549 0.54275 0.06395  0.05087  -0.00238 168 GLU E CD  
5618 O OE1 . GLU E 154 ? 0.53875 0.49615 0.49492 0.06447  0.05266  -0.00235 168 GLU E OE1 
5619 O OE2 . GLU E 154 ? 0.58267 0.53786 0.53327 0.06247  0.04881  -0.00125 168 GLU E OE2 
5620 N N   . LEU E 155 ? 0.41644 0.36448 0.36103 0.07272  0.05766  -0.01174 169 LEU E N   
5621 C CA  . LEU E 155 ? 0.35948 0.30842 0.30302 0.07573  0.06058  -0.01373 169 LEU E CA  
5622 C C   . LEU E 155 ? 0.44378 0.39632 0.38460 0.07617  0.06362  -0.01258 169 LEU E C   
5623 O O   . LEU E 155 ? 0.45950 0.41230 0.39627 0.07461  0.06330  -0.01188 169 LEU E O   
5624 C CB  . LEU E 155 ? 0.42926 0.37488 0.36892 0.07705  0.05962  -0.01737 169 LEU E CB  
5625 C CG  . LEU E 155 ? 0.43510 0.38102 0.37353 0.08073  0.06202  -0.02035 169 LEU E CG  
5626 C CD1 . LEU E 155 ? 0.37291 0.31428 0.31049 0.08149  0.05981  -0.02417 169 LEU E CD1 
5627 C CD2 . LEU E 155 ? 0.41263 0.36196 0.34556 0.08230  0.06483  -0.02081 169 LEU E CD2 
5628 N N   . SER E 156 ? 0.40857 0.36407 0.35202 0.07845  0.06677  -0.01201 170 SER E N   
5629 C CA  . SER E 156 ? 0.45233 0.41173 0.39451 0.07933  0.07019  -0.01033 170 SER E CA  
5630 C C   . SER E 156 ? 0.48464 0.44642 0.42681 0.08334  0.07356  -0.01128 170 SER E C   
5631 O O   . SER E 156 ? 0.41258 0.37352 0.35783 0.08509  0.07354  -0.01243 170 SER E O   
5632 C CB  . SER E 156 ? 0.41443 0.37627 0.36209 0.07724  0.07074  -0.00700 170 SER E CB  
5633 O OG  . SER E 156 ? 0.42178 0.38435 0.37603 0.07756  0.07045  -0.00633 170 SER E OG  
5634 N N   . TRP E 157 ? 0.42978 0.39488 0.36848 0.08506  0.07663  -0.01055 171 TRP E N   
5635 C CA  . TRP E 157 ? 0.46716 0.43564 0.40507 0.08938  0.08028  -0.01099 171 TRP E CA  
5636 C C   . TRP E 157 ? 0.47557 0.44890 0.41881 0.08997  0.08395  -0.00676 171 TRP E C   
5637 O O   . TRP E 157 ? 0.49032 0.46519 0.43427 0.08790  0.08469  -0.00409 171 TRP E O   
5638 C CB  . TRP E 157 ? 0.37525 0.34491 0.30512 0.09157  0.08122  -0.01320 171 TRP E CB  
5639 C CG  . TRP E 157 ? 0.45735 0.42310 0.38271 0.09252  0.07847  -0.01817 171 TRP E CG  
5640 C CD1 . TRP E 157 ? 0.42628 0.38839 0.34777 0.09010  0.07492  -0.02042 171 TRP E CD1 
5641 C CD2 . TRP E 157 ? 0.51904 0.48412 0.44380 0.09622  0.07910  -0.02155 171 TRP E CD2 
5642 N NE1 . TRP E 157 ? 0.42614 0.38518 0.34520 0.09181  0.07315  -0.02511 171 TRP E NE1 
5643 C CE2 . TRP E 157 ? 0.59017 0.55078 0.51096 0.09564  0.07567  -0.02610 171 TRP E CE2 
5644 C CE3 . TRP E 157 ? 0.57459 0.54243 0.50205 0.10005  0.08228  -0.02113 171 TRP E CE3 
5645 C CZ2 . TRP E 157 ? 0.61720 0.57563 0.53672 0.09870  0.07524  -0.03064 171 TRP E CZ2 
5646 C CZ3 . TRP E 157 ? 0.47865 0.44453 0.40425 0.10335  0.08200  -0.02546 171 TRP E CZ3 
5647 C CH2 . TRP E 157 ? 0.49700 0.45801 0.41867 0.10263  0.07847  -0.03037 171 TRP E CH2 
5648 N N   . TRP E 158 ? 0.50589 0.48165 0.45329 0.09286  0.08637  -0.00603 172 TRP E N   
5649 C CA  . TRP E 158 ? 0.47630 0.45685 0.43021 0.09349  0.08986  -0.00175 172 TRP E CA  
5650 C C   . TRP E 158 ? 0.58730 0.57241 0.53978 0.09869  0.09421  -0.00118 172 TRP E C   
5651 O O   . TRP E 158 ? 0.55228 0.53688 0.50426 0.10168  0.09448  -0.00333 172 TRP E O   
5652 C CB  . TRP E 158 ? 0.54248 0.52250 0.50477 0.09164  0.08850  -0.00040 172 TRP E CB  
5653 C CG  . TRP E 158 ? 0.58589 0.56283 0.54998 0.08688  0.08464  -0.00036 172 TRP E CG  
5654 C CD1 . TRP E 158 ? 0.45087 0.42320 0.41185 0.08490  0.08057  -0.00302 172 TRP E CD1 
5655 C CD2 . TRP E 158 ? 0.58587 0.56438 0.55548 0.08374  0.08452  0.00248  172 TRP E CD2 
5656 N NE1 . TRP E 158 ? 0.56029 0.53165 0.52393 0.08102  0.07802  -0.00186 172 TRP E NE1 
5657 C CE2 . TRP E 158 ? 0.53815 0.51306 0.50692 0.08020  0.08025  0.00115  172 TRP E CE2 
5658 C CE3 . TRP E 158 ? 0.51776 0.50042 0.49338 0.08365  0.08761  0.00601  172 TRP E CE3 
5659 C CZ2 . TRP E 158 ? 0.49656 0.47188 0.46954 0.07678  0.07886  0.00272  172 TRP E CZ2 
5660 C CZ3 . TRP E 158 ? 0.49504 0.47763 0.47556 0.07991  0.08614  0.00746  172 TRP E CZ3 
5661 C CH2 . TRP E 158 ? 0.51015 0.48909 0.48896 0.07660  0.08174  0.00556  172 TRP E CH2 
5662 N N   . VAL E 159 ? 0.54686 0.53661 0.49881 0.10002  0.09776  0.00189  173 VAL E N   
5663 C CA  . VAL E 159 ? 0.57597 0.57132 0.52658 0.10534  0.10238  0.00331  173 VAL E CA  
5664 C C   . VAL E 159 ? 0.61876 0.61903 0.57859 0.10562  0.10608  0.00894  173 VAL E C   
5665 O O   . VAL E 159 ? 0.70136 0.70297 0.66457 0.10310  0.10700  0.01225  173 VAL E O   
5666 C CB  . VAL E 159 ? 0.58811 0.58596 0.53039 0.10744  0.10385  0.00264  173 VAL E CB  
5667 C CG1 . VAL E 159 ? 0.60920 0.61428 0.55106 0.11317  0.10917  0.00527  173 VAL E CG1 
5668 C CG2 . VAL E 159 ? 0.52614 0.51958 0.45990 0.10762  0.10022  -0.00330 173 VAL E CG2 
5669 N N   . ASN E 160 ? 0.61516 0.50148 0.60010 -0.01205 0.18631  -0.09417 174 ASN E N   
5670 C CA  . ASN E 160 ? 0.76215 0.63719 0.75023 -0.01028 0.20205  -0.10418 174 ASN E CA  
5671 C C   . ASN E 160 ? 0.72533 0.60020 0.72736 -0.00605 0.20869  -0.10436 174 ASN E C   
5672 O O   . ASN E 160 ? 0.75719 0.62926 0.76047 -0.00366 0.21533  -0.09956 174 ASN E O   
5673 C CB  . ASN E 160 ? 0.62161 0.49125 0.59545 -0.00798 0.21407  -0.09788 174 ASN E CB  
5674 C CG  . ASN E 160 ? 0.63752 0.50560 0.59774 -0.01222 0.20891  -0.09994 174 ASN E CG  
5675 O OD1 . ASN E 160 ? 0.68497 0.55167 0.64753 -0.01726 0.20107  -0.11160 174 ASN E OD1 
5676 N ND2 . ASN E 160 ? 0.68394 0.55205 0.62948 -0.00996 0.21301  -0.08870 174 ASN E ND2 
5677 N N   . GLY E 161 ? 0.62998 0.51126 0.64282 -0.00673 0.19786  -0.10476 175 GLY E N   
5678 C CA  . GLY E 161 ? 0.60353 0.48623 0.63014 -0.00350 0.19981  -0.10403 175 GLY E CA  
5679 C C   . GLY E 161 ? 0.60235 0.49140 0.62944 0.00224  0.20499  -0.08909 175 GLY E C   
5680 O O   . GLY E 161 ? 0.56811 0.45909 0.60600 0.00467  0.20454  -0.08648 175 GLY E O   
5681 N N   . LYS E 162 ? 0.51936 0.41481 0.53465 0.00314  0.20215  -0.07518 176 LYS E N   
5682 C CA  . LYS E 162 ? 0.61979 0.52358 0.63479 0.00831  0.20355  -0.05903 176 LYS E CA  
5683 C C   . LYS E 162 ? 0.63088 0.54754 0.64378 0.00607  0.18768  -0.04928 176 LYS E C   
5684 O O   . LYS E 162 ? 0.62768 0.54650 0.63114 0.00203  0.17942  -0.04906 176 LYS E O   
5685 C CB  . LYS E 162 ? 0.59200 0.49215 0.59437 0.01246  0.21540  -0.05031 176 LYS E CB  
5686 N N   . GLU E 163 ? 0.65611 0.58132 0.67790 0.00849  0.18355  -0.04155 177 GLU E N   
5687 C CA  . GLU E 163 ? 0.60324 0.54133 0.62373 0.00627  0.16922  -0.03191 177 GLU E CA  
5688 C C   . GLU E 163 ? 0.60836 0.55376 0.61637 0.00899  0.16963  -0.01757 177 GLU E C   
5689 O O   . GLU E 163 ? 0.64218 0.58725 0.64778 0.01502  0.18000  -0.00954 177 GLU E O   
5690 C CB  . GLU E 163 ? 0.55484 0.49994 0.58812 0.00819  0.16561  -0.02757 177 GLU E CB  
5691 C CG  . GLU E 163 ? 0.70441 0.66335 0.73641 0.00565  0.15151  -0.01724 177 GLU E CG  
5692 C CD  . GLU E 163 ? 0.54574 0.51178 0.58979 0.00722  0.14796  -0.01262 177 GLU E CD  
5693 O OE1 . GLU E 163 ? 0.69821 0.65874 0.75175 0.01089  0.15651  -0.01672 177 GLU E OE1 
5694 O OE2 . GLU E 163 ? 0.53976 0.51704 0.58368 0.00462  0.13663  -0.00497 177 GLU E OE2 
5695 N N   . VAL E 164 ? 0.46468 0.41650 0.46449 0.00475  0.15817  -0.01451 178 VAL E N   
5696 C CA  . VAL E 164 ? 0.47881 0.43812 0.46626 0.00707  0.15694  -0.00176 178 VAL E CA  
5697 C C   . VAL E 164 ? 0.57061 0.54575 0.56102 0.00602  0.14434  0.00886  178 VAL E C   
5698 O O   . VAL E 164 ? 0.56776 0.54688 0.56654 0.00149  0.13437  0.00503  178 VAL E O   
5699 C CB  . VAL E 164 ? 0.49381 0.44824 0.46793 0.00338  0.15464  -0.00619 178 VAL E CB  
5700 C CG1 . VAL E 164 ? 0.51113 0.45002 0.48253 0.00400  0.16763  -0.01720 178 VAL E CG1 
5701 C CG2 . VAL E 164 ? 0.41453 0.37253 0.39019 -0.00412 0.13981  -0.01260 178 VAL E CG2 
5702 N N   . HIS E 165 ? 0.51256 0.49658 0.49560 0.01038  0.14500  0.02224  179 HIS E N   
5703 C CA  . HIS E 165 ? 0.58065 0.58099 0.56539 0.00954  0.13354  0.03286  179 HIS E CA  
5704 C C   . HIS E 165 ? 0.55632 0.56357 0.52714 0.00949  0.12831  0.04050  179 HIS E C   
5705 O O   . HIS E 165 ? 0.62195 0.64170 0.59230 0.00602  0.11604  0.04564  179 HIS E O   
5706 C CB  . HIS E 165 ? 0.55555 0.56323 0.54790 0.01585  0.13855  0.04273  179 HIS E CB  
5707 C CG  . HIS E 165 ? 0.61043 0.61450 0.61751 0.01541  0.14072  0.03654  179 HIS E CG  
5708 N ND1 . HIS E 165 ? 0.63737 0.62913 0.64916 0.01893  0.15346  0.02990  179 HIS E ND1 
5709 C CD2 . HIS E 165 ? 0.66941 0.68015 0.68718 0.01181  0.13175  0.03564  179 HIS E CD2 
5710 C CE1 . HIS E 165 ? 0.59061 0.58203 0.61566 0.01788  0.15201  0.02522  179 HIS E CE1 
5711 N NE2 . HIS E 165 ? 0.64908 0.65150 0.67762 0.01362  0.13895  0.02868  179 HIS E NE2 
5712 N N   . SER E 166 ? 0.56332 0.56225 0.52250 0.01324  0.13762  0.04108  180 SER E N   
5713 C CA  . SER E 166 ? 0.58119 0.58568 0.52609 0.01417  0.13356  0.04847  180 SER E CA  
5714 C C   . SER E 166 ? 0.56862 0.57260 0.50866 0.00639  0.12285  0.04107  180 SER E C   
5715 O O   . SER E 166 ? 0.54695 0.53911 0.48776 0.00233  0.12498  0.02881  180 SER E O   
5716 C CB  . SER E 166 ? 0.52149 0.51513 0.45430 0.02029  0.14703  0.05048  180 SER E CB  
5717 O OG  . SER E 166 ? 0.76216 0.76045 0.68034 0.02153  0.14288  0.05733  180 SER E OG  
5718 N N   . GLY E 167 ? 0.62274 0.63991 0.55800 0.00436  0.11123  0.04826  181 GLY E N   
5719 C CA  . GLY E 167 ? 0.59539 0.61315 0.52591 -0.00306 0.10023  0.04210  181 GLY E CA  
5720 C C   . GLY E 167 ? 0.57968 0.59884 0.52156 -0.01032 0.09066  0.03428  181 GLY E C   
5721 O O   . GLY E 167 ? 0.51697 0.53253 0.45568 -0.01671 0.08314  0.02620  181 GLY E O   
5722 N N   . VAL E 168 ? 0.52745 0.55135 0.48194 -0.00938 0.09061  0.03652  182 VAL E N   
5723 C CA  . VAL E 168 ? 0.46890 0.49322 0.43406 -0.01565 0.08207  0.02958  182 VAL E CA  
5724 C C   . VAL E 168 ? 0.47395 0.51515 0.44292 -0.01795 0.07083  0.03898  182 VAL E C   
5725 O O   . VAL E 168 ? 0.48754 0.53924 0.45783 -0.01278 0.07338  0.05014  182 VAL E O   
5726 C CB  . VAL E 168 ? 0.57047 0.58599 0.54745 -0.01315 0.09081  0.02364  182 VAL E CB  
5727 C CG1 . VAL E 168 ? 0.38491 0.40159 0.37239 -0.01890 0.08140  0.01788  182 VAL E CG1 
5728 C CG2 . VAL E 168 ? 0.44079 0.43979 0.41479 -0.01190 0.10148  0.01273  182 VAL E CG2 
5729 N N   . CYS E 169 ? 0.44487 0.48861 0.41542 -0.02576 0.05846  0.03426  183 CYS E N   
5730 C CA  . CYS E 169 ? 0.45561 0.51389 0.43164 -0.02920 0.04800  0.04126  183 CYS E CA  
5731 C C   . CYS E 169 ? 0.38334 0.43623 0.36676 -0.03619 0.04029  0.03212  183 CYS E C   
5732 O O   . CYS E 169 ? 0.52638 0.57174 0.50523 -0.04184 0.03419  0.02307  183 CYS E O   
5733 C CB  . CYS E 169 ? 0.39991 0.47067 0.36688 -0.03197 0.03847  0.04805  183 CYS E CB  
5734 S SG  . CYS E 169 ? 0.88105 0.97271 0.85503 -0.03314 0.03013  0.06003  183 CYS E SG  
5735 N N   . THR E 170 ? 0.42390 0.48034 0.41815 -0.03560 0.04045  0.03452  184 THR E N   
5736 C CA  . THR E 170 ? 0.39494 0.44661 0.39617 -0.04158 0.03314  0.02711  184 THR E CA  
5737 C C   . THR E 170 ? 0.38256 0.44906 0.38670 -0.04602 0.02279  0.03529  184 THR E C   
5738 O O   . THR E 170 ? 0.44742 0.52685 0.45455 -0.04215 0.02515  0.04625  184 THR E O   
5739 C CB  . THR E 170 ? 0.35550 0.39776 0.36704 -0.03748 0.04201  0.02216  184 THR E CB  
5740 O OG1 . THR E 170 ? 0.39483 0.42423 0.40383 -0.03332 0.05255  0.01475  184 THR E OG1 
5741 C CG2 . THR E 170 ? 0.39327 0.42864 0.41071 -0.04325 0.03434  0.01347  184 THR E CG2 
5742 N N   . ASP E 171 ? 0.36117 0.42576 0.36400 -0.05419 0.01137  0.02980  185 ASP E N   
5743 C CA  . ASP E 171 ? 0.40812 0.48553 0.41329 -0.05967 0.00123  0.03631  185 ASP E CA  
5744 C C   . ASP E 171 ? 0.44931 0.53201 0.46543 -0.05647 0.00539  0.04190  185 ASP E C   
5745 O O   . ASP E 171 ? 0.49161 0.56312 0.51428 -0.05516 0.00942  0.03529  185 ASP E O   
5746 C CB  . ASP E 171 ? 0.45643 0.52654 0.45910 -0.06872 -0.01026 0.02763  185 ASP E CB  
5747 C CG  . ASP E 171 ? 0.56637 0.62953 0.55870 -0.07184 -0.01422 0.02067  185 ASP E CG  
5748 O OD1 . ASP E 171 ? 0.51502 0.58516 0.50065 -0.06939 -0.01237 0.02590  185 ASP E OD1 
5749 O OD2 . ASP E 171 ? 0.63009 0.68055 0.62065 -0.07649 -0.01928 0.00984  185 ASP E OD2 
5750 N N   . PRO E 172 ? 0.52835 0.62798 0.54691 -0.05482 0.00472  0.05363  186 PRO E N   
5751 C CA  . PRO E 172 ? 0.50690 0.61223 0.53603 -0.05203 0.00831  0.05902  186 PRO E CA  
5752 C C   . PRO E 172 ? 0.49522 0.59621 0.52948 -0.05890 0.00086  0.05426  186 PRO E C   
5753 O O   . PRO E 172 ? 0.46140 0.56032 0.50441 -0.05622 0.00530  0.05475  186 PRO E O   
5754 C CB  . PRO E 172 ? 0.42602 0.55182 0.45504 -0.05024 0.00671  0.07187  186 PRO E CB  
5755 C CG  . PRO E 172 ? 0.42409 0.55517 0.44294 -0.05502 -0.00154 0.07212  186 PRO E CG  
5756 C CD  . PRO E 172 ? 0.37534 0.48982 0.38718 -0.05465 0.00122  0.06228  186 PRO E CD  
5757 N N   . GLN E 173 ? 0.46417 0.56298 0.49278 -0.06755 -0.01026 0.04958  187 GLN E N   
5758 C CA  . GLN E 173 ? 0.58165 0.67438 0.61330 -0.07433 -0.01770 0.04463  187 GLN E CA  
5759 C C   . GLN E 173 ? 0.62566 0.70408 0.64968 -0.08044 -0.02506 0.03325  187 GLN E C   
5760 O O   . GLN E 173 ? 0.54031 0.62039 0.55599 -0.08265 -0.02880 0.03232  187 GLN E O   
5761 C CB  . GLN E 173 ? 0.62340 0.73216 0.65664 -0.08020 -0.02570 0.05322  187 GLN E CB  
5762 N N   . PRO E 174 ? 0.58079 0.64506 0.60714 -0.08297 -0.02747 0.02439  188 PRO E N   
5763 C CA  . PRO E 174 ? 0.53279 0.58241 0.55191 -0.08811 -0.03441 0.01276  188 PRO E CA  
5764 C C   . PRO E 174 ? 0.56910 0.62320 0.58134 -0.09790 -0.04747 0.01384  188 PRO E C   
5765 O O   . PRO E 174 ? 0.65596 0.72264 0.67022 -0.10162 -0.05164 0.02223  188 PRO E O   
5766 C CB  . PRO E 174 ? 0.62553 0.65973 0.65017 -0.08679 -0.03262 0.00389  188 PRO E CB  
5767 C CG  . PRO E 174 ? 0.61347 0.65406 0.64837 -0.08011 -0.02319 0.01088  188 PRO E CG  
5768 C CD  . PRO E 174 ? 0.53977 0.60019 0.57528 -0.08064 -0.02379 0.02425  188 PRO E CD  
5769 N N   . LEU E 175 ? 0.54888 0.59236 0.55288 -0.10217 -0.05381 0.00478  189 LEU E N   
5770 C CA  . LEU E 175 ? 0.64235 0.68576 0.63904 -0.11189 -0.06661 0.00328  189 LEU E CA  
5771 C C   . LEU E 175 ? 0.66085 0.68880 0.65770 -0.11583 -0.07204 -0.00521 189 LEU E C   
5772 O O   . LEU E 175 ? 0.61926 0.63284 0.61872 -0.11150 -0.06764 -0.01414 189 LEU E O   
5773 C CB  . LEU E 175 ? 0.48233 0.52235 0.46921 -0.11451 -0.07123 -0.00195 189 LEU E CB  
5774 C CG  . LEU E 175 ? 0.70370 0.75965 0.68750 -0.11282 -0.06940 0.00682  189 LEU E CG  
5775 C CD1 . LEU E 175 ? 0.68032 0.73102 0.65397 -0.11573 -0.07445 0.00055  189 LEU E CD1 
5776 C CD2 . LEU E 175 ? 0.57473 0.64825 0.55979 -0.11766 -0.07503 0.01760  189 LEU E CD2 
5777 N N   . LYS E 176 ? 0.72235 0.75306 0.71606 -0.12406 -0.08162 -0.00265 190 LYS E N   
5778 C CA  . LYS E 176 ? 0.68716 0.70255 0.67892 -0.12852 -0.08797 -0.01027 190 LYS E CA  
5779 C C   . LYS E 176 ? 0.68215 0.68526 0.66300 -0.13445 -0.09761 -0.01994 190 LYS E C   
5780 O O   . LYS E 176 ? 0.84425 0.85472 0.81826 -0.14104 -0.10508 -0.01679 190 LYS E O   
5781 C CB  . LYS E 176 ? 0.64672 0.67030 0.64040 -0.13441 -0.09258 -0.00246 190 LYS E CB  
5782 C CG  . LYS E 176 ? 0.78176 0.81300 0.78661 -0.12832 -0.08343 0.00467  190 LYS E CG  
5783 C CD  . LYS E 176 ? 0.71690 0.76066 0.72403 -0.13418 -0.08721 0.01407  190 LYS E CD  
5784 C CE  . LYS E 176 ? 0.79870 0.82904 0.80543 -0.13790 -0.09119 0.00974  190 LYS E CE  
5785 N NZ  . LYS E 176 ? 0.93407 0.97703 0.94730 -0.13968 -0.08953 0.01952  190 LYS E NZ  
5786 N N   . GLU E 177 ? 0.70538 0.69005 0.68477 -0.13190 -0.09747 -0.03201 191 GLU E N   
5787 C CA  . GLU E 177 ? 0.82233 0.79409 0.79146 -0.13682 -0.10654 -0.04221 191 GLU E CA  
5788 C C   . GLU E 177 ? 0.94139 0.90843 0.90304 -0.14646 -0.11854 -0.04241 191 GLU E C   
5789 O O   . GLU E 177 ? 0.94189 0.90229 0.89375 -0.15223 -0.12749 -0.04798 191 GLU E O   
5790 C CB  . GLU E 177 ? 0.78298 0.73662 0.75322 -0.13126 -0.10330 -0.05550 191 GLU E CB  
5791 C CG  . GLU E 177 ? 0.73272 0.68993 0.70996 -0.12218 -0.09087 -0.05608 191 GLU E CG  
5792 C CD  . GLU E 177 ? 0.87488 0.81529 0.85192 -0.11777 -0.08852 -0.07057 191 GLU E CD  
5793 O OE1 . GLU E 177 ? 0.79076 0.71647 0.76628 -0.11894 -0.09377 -0.07955 191 GLU E OE1 
5794 O OE2 . GLU E 177 ? 0.92334 0.86521 0.90149 -0.11307 -0.08136 -0.07321 191 GLU E OE2 
5795 N N   . GLN E 178 ? 0.94915 0.91921 0.91481 -0.14846 -0.11874 -0.03644 192 GLN E N   
5796 C CA  . GLN E 178 ? 0.85274 0.82081 0.81144 -0.15824 -0.12910 -0.03446 192 GLN E CA  
5797 C C   . GLN E 178 ? 0.84382 0.83053 0.80909 -0.16008 -0.12608 -0.02120 192 GLN E C   
5798 O O   . GLN E 178 ? 0.84594 0.83153 0.81719 -0.15832 -0.12254 -0.01845 192 GLN E O   
5799 C CB  . GLN E 178 ? 0.76480 0.71225 0.72017 -0.15846 -0.13293 -0.04356 192 GLN E CB  
5800 N N   . PRO E 179 ? 0.88126 0.88571 0.84557 -0.16362 -0.12764 -0.01298 193 PRO E N   
5801 C CA  . PRO E 179 ? 0.84725 0.87225 0.81963 -0.16321 -0.12292 -0.00036 193 PRO E CA  
5802 C C   . PRO E 179 ? 1.10962 1.13528 1.08289 -0.16953 -0.12655 0.00379  193 PRO E C   
5803 O O   . PRO E 179 ? 1.03455 1.07616 1.01587 -0.16824 -0.12165 0.01346  193 PRO E O   
5804 C CB  . PRO E 179 ? 0.74671 0.78784 0.71519 -0.16718 -0.12669 0.00523  193 PRO E CB  
5805 C CG  . PRO E 179 ? 0.72489 0.75518 0.68624 -0.16562 -0.12888 -0.00373 193 PRO E CG  
5806 C CD  . PRO E 179 ? 0.86675 0.87383 0.82296 -0.16727 -0.13335 -0.01514 193 PRO E CD  
5807 N N   . ALA E 180 ? 1.11014 1.11896 1.07510 -0.17617 -0.13480 -0.00313 194 ALA E N   
5808 C CA  . ALA E 180 ? 1.08849 1.09661 1.05297 -0.18273 -0.13821 0.00066  194 ALA E CA  
5809 C C   . ALA E 180 ? 1.02311 1.01986 0.99337 -0.17684 -0.13251 -0.00187 194 ALA E C   
5810 O O   . ALA E 180 ? 1.05548 1.06104 1.03242 -0.17696 -0.12869 0.00551  194 ALA E O   
5811 C CB  . ALA E 180 ? 1.08407 1.07922 1.03666 -0.18702 -0.14517 -0.00451 194 ALA E CB  
5812 N N   . LEU E 181 ? 1.03346 1.01110 1.00142 -0.17160 -0.13193 -0.01251 195 LEU E N   
5813 C CA  . LEU E 181 ? 1.06748 1.03299 1.04041 -0.16576 -0.12710 -0.01618 195 LEU E CA  
5814 C C   . LEU E 181 ? 1.03540 1.01461 1.02205 -0.15645 -0.11496 -0.00947 195 LEU E C   
5815 O O   . LEU E 181 ? 1.13994 1.12999 1.13104 -0.15131 -0.10935 -0.00708 195 LEU E O   
5816 C CB  . LEU E 181 ? 0.91681 0.86024 0.88469 -0.16120 -0.12888 -0.02988 195 LEU E CB  
5817 C CG  . LEU E 181 ? 0.96525 0.89880 0.92294 -0.15837 -0.13193 -0.03671 195 LEU E CG  
5818 C CD1 . LEU E 181 ? 0.81482 0.73394 0.77231 -0.14854 -0.12850 -0.04921 195 LEU E CD1 
5819 C CD2 . LEU E 181 ? 0.97945 0.90769 0.93211 -0.15995 -0.13376 -0.03470 195 LEU E CD2 
5820 N N   . ASN E 182 ? 1.13110 1.10927 1.12388 -0.15426 -0.11089 -0.00635 196 ASN E N   
5821 C CA  . ASN E 182 ? 1.12414 1.11196 1.12971 -0.14471 -0.09929 -0.00141 196 ASN E CA  
5822 C C   . ASN E 182 ? 0.99756 0.97027 1.00644 -0.13557 -0.09378 -0.01132 196 ASN E C   
5823 O O   . ASN E 182 ? 0.97609 0.95605 0.99467 -0.12704 -0.08372 -0.00872 196 ASN E O   
5824 C CB  . ASN E 182 ? 1.03292 1.02692 1.04433 -0.14587 -0.09679 0.00620  196 ASN E CB  
5825 C CG  . ASN E 182 ? 1.18744 1.20661 1.20635 -0.14607 -0.09222 0.01906  196 ASN E CG  
5826 O OD1 . ASN E 182 ? 1.16783 1.19956 1.18389 -0.14981 -0.09514 0.02305  196 ASN E OD1 
5827 N ND2 . ASN E 182 ? 1.12482 1.15167 1.15339 -0.14168 -0.08512 0.02538  196 ASN E ND2 
5828 N N   . ASP E 183 ? 0.98040 0.93232 0.98134 -0.13714 -0.10015 -0.02281 197 ASP E N   
5829 C CA  . ASP E 183 ? 0.90564 0.84301 0.90878 -0.12915 -0.09617 -0.03399 197 ASP E CA  
5830 C C   . ASP E 183 ? 0.89155 0.82817 0.89091 -0.12798 -0.09677 -0.03983 197 ASP E C   
5831 O O   . ASP E 183 ? 0.92528 0.84816 0.92427 -0.12303 -0.09552 -0.05106 197 ASP E O   
5832 C CB  . ASP E 183 ? 0.91853 0.83347 0.91486 -0.13070 -0.10297 -0.04424 197 ASP E CB  
5833 N N   . SER E 184 ? 0.84849 0.79979 0.84515 -0.13233 -0.09862 -0.03274 198 SER E N   
5834 C CA  . SER E 184 ? 0.59143 0.54186 0.58307 -0.13216 -0.10016 -0.03798 198 SER E CA  
5835 C C   . SER E 184 ? 0.62272 0.57391 0.62227 -0.12224 -0.08919 -0.04126 198 SER E C   
5836 O O   . SER E 184 ? 0.48916 0.45164 0.49829 -0.11648 -0.07960 -0.03383 198 SER E O   
5837 C CB  . SER E 184 ? 0.66166 0.62959 0.64988 -0.13801 -0.10338 -0.02851 198 SER E CB  
5838 O OG  . SER E 184 ? 0.78379 0.75374 0.76937 -0.13573 -0.10193 -0.03183 198 SER E OG  
5839 N N   . ARG E 185 ? 0.55251 0.49150 0.54775 -0.12040 -0.09056 -0.05266 199 ARG E N   
5840 C CA  . ARG E 185 ? 0.49357 0.43354 0.49488 -0.11216 -0.08041 -0.05625 199 ARG E CA  
5841 C C   . ARG E 185 ? 0.62209 0.57962 0.62365 -0.11198 -0.07632 -0.04674 199 ARG E C   
5842 O O   . ARG E 185 ? 0.56442 0.53105 0.55981 -0.11868 -0.08315 -0.04048 199 ARG E O   
5843 C CB  . ARG E 185 ? 0.59304 0.51602 0.58921 -0.11100 -0.08353 -0.07133 199 ARG E CB  
5844 C CG  . ARG E 185 ? 0.59455 0.49969 0.58997 -0.11044 -0.08797 -0.08127 199 ARG E CG  
5845 C CD  . ARG E 185 ? 0.60692 0.49548 0.59464 -0.11134 -0.09464 -0.09603 199 ARG E CD  
5846 N NE  . ARG E 185 ? 0.68157 0.56652 0.67493 -0.10389 -0.08605 -0.10476 199 ARG E NE  
5847 C CZ  . ARG E 185 ? 0.55066 0.42993 0.54010 -0.09881 -0.08042 -0.11407 199 ARG E CZ  
5848 N NH1 . ARG E 185 ? 0.69923 0.57820 0.68163 -0.09878 -0.08076 -0.11559 199 ARG E NH1 
5849 N NH2 . ARG E 185 ? 0.69748 0.57238 0.68913 -0.09330 -0.07297 -0.11958 199 ARG E NH2 
5850 N N   . TYR E 186 ? 0.65623 0.57410 0.62515 0.03665  0.00887  -0.02849 200 TYR E N   
5851 C CA  . TYR E 186 ? 0.53350 0.45893 0.49844 0.03059  0.01242  -0.02738 200 TYR E CA  
5852 C C   . TYR E 186 ? 0.57884 0.51942 0.54646 0.03421  0.01816  -0.03069 200 TYR E C   
5853 O O   . TYR E 186 ? 0.66538 0.61463 0.64137 0.04030  0.01988  -0.03258 200 TYR E O   
5854 C CB  . TYR E 186 ? 0.44102 0.37327 0.41047 0.02329  0.01181  -0.02004 200 TYR E CB  
5855 C CG  . TYR E 186 ? 0.62377 0.54213 0.58969 0.01819  0.00704  -0.01647 200 TYR E CG  
5856 C CD1 . TYR E 186 ? 0.62465 0.53349 0.58172 0.01231  0.00622  -0.01679 200 TYR E CD1 
5857 C CD2 . TYR E 186 ? 0.41058 0.32568 0.38218 0.01915  0.00342  -0.01293 200 TYR E CD2 
5858 C CE1 . TYR E 186 ? 0.46492 0.36140 0.41930 0.00730  0.00256  -0.01376 200 TYR E CE1 
5859 C CE2 . TYR E 186 ? 0.48988 0.39199 0.45745 0.01431  -0.00037 -0.00964 200 TYR E CE2 
5860 C CZ  . TYR E 186 ? 0.44506 0.33800 0.40426 0.00824  -0.00045 -0.01006 200 TYR E CZ  
5861 O OH  . TYR E 186 ? 0.42569 0.30590 0.38136 0.00315  -0.00355 -0.00710 200 TYR E OH  
5862 N N   . ALA E 187 ? 0.50558 0.44928 0.46589 0.03031  0.02114  -0.03145 201 ALA E N   
5863 C CA  . ALA E 187 ? 0.54543 0.50366 0.50631 0.03199  0.02723  -0.03329 201 ALA E CA  
5864 C C   . ALA E 187 ? 0.51539 0.48059 0.47315 0.02449  0.02908  -0.02826 201 ALA E C   
5865 O O   . ALA E 187 ? 0.52247 0.47888 0.47374 0.01890  0.02583  -0.02635 201 ALA E O   
5866 C CB  . ALA E 187 ? 0.60676 0.56030 0.55896 0.03672  0.02927  -0.04107 201 ALA E CB  
5867 N N   . LEU E 188 ? 0.44335 0.42425 0.40606 0.02443  0.03444  -0.02622 202 LEU E N   
5868 C CA  . LEU E 188 ? 0.40609 0.39439 0.36611 0.01789  0.03671  -0.02105 202 LEU E CA  
5869 C C   . LEU E 188 ? 0.52925 0.52970 0.48676 0.02012  0.04394  -0.02304 202 LEU E C   
5870 O O   . LEU E 188 ? 0.55299 0.56224 0.51803 0.02532  0.04800  -0.02555 202 LEU E O   
5871 C CB  . LEU E 188 ? 0.41224 0.40730 0.38321 0.01362  0.03562  -0.01381 202 LEU E CB  
5872 C CG  . LEU E 188 ? 0.51337 0.51433 0.48266 0.00628  0.03688  -0.00754 202 LEU E CG  
5873 C CD1 . LEU E 188 ? 0.46931 0.45784 0.43094 0.00081  0.03141  -0.00594 202 LEU E CD1 
5874 C CD2 . LEU E 188 ? 0.37358 0.38551 0.35620 0.00405  0.03802  -0.00175 202 LEU E CD2 
5875 N N   . SER E 189 ? 0.48133 0.48209 0.42813 0.01634  0.04557  -0.02211 203 SER E N   
5876 C CA  . SER E 189 ? 0.64836 0.65931 0.59019 0.01795  0.05265  -0.02352 203 SER E CA  
5877 C C   . SER E 189 ? 0.50012 0.51882 0.44070 0.01168  0.05514  -0.01643 203 SER E C   
5878 O O   . SER E 189 ? 0.43996 0.45399 0.37976 0.00598  0.05064  -0.01165 203 SER E O   
5879 C CB  . SER E 189 ? 0.62032 0.62396 0.54754 0.02063  0.05287  -0.03015 203 SER E CB  
5880 O OG  . SER E 189 ? 0.54855 0.54637 0.46482 0.01535  0.04986  -0.02809 203 SER E OG  
5881 N N   . SER E 190 ? 0.45622 0.48656 0.39648 0.01283  0.06269  -0.01592 204 SER E N   
5882 C CA  . SER E 190 ? 0.42568 0.46330 0.36360 0.00742  0.06617  -0.00931 204 SER E CA  
5883 C C   . SER E 190 ? 0.50328 0.54720 0.43128 0.00976  0.07390  -0.01167 204 SER E C   
5884 O O   . SER E 190 ? 0.51848 0.56586 0.44747 0.01554  0.07819  -0.01753 204 SER E O   
5885 C CB  . SER E 190 ? 0.33465 0.38247 0.28862 0.00488  0.06813  -0.00351 204 SER E CB  
5886 O OG  . SER E 190 ? 0.43377 0.48650 0.38549 -0.00106 0.07047  0.00341  204 SER E OG  
5887 N N   . ARG E 191 ? 0.41794 0.46287 0.33588 0.00539  0.07566  -0.00714 205 ARG E N   
5888 C CA  . ARG E 191 ? 0.48943 0.53975 0.39610 0.00693  0.08332  -0.00821 205 ARG E CA  
5889 C C   . ARG E 191 ? 0.59406 0.65415 0.50419 0.00227  0.08922  -0.00043 205 ARG E C   
5890 O O   . ARG E 191 ? 0.51987 0.57864 0.43311 -0.00325 0.08547  0.00606  205 ARG E O   
5891 C CB  . ARG E 191 ? 0.47589 0.51647 0.36299 0.00684  0.08001  -0.01083 205 ARG E CB  
5892 C CG  . ARG E 191 ? 0.48496 0.51348 0.36868 0.00928  0.07221  -0.01725 205 ARG E CG  
5893 C CD  . ARG E 191 ? 0.63685 0.65689 0.52058 0.00384  0.06370  -0.01344 205 ARG E CD  
5894 N NE  . ARG E 191 ? 0.56890 0.57672 0.44802 0.00532  0.05669  -0.01950 205 ARG E NE  
5895 C CZ  . ARG E 191 ? 0.62119 0.62284 0.50998 0.00532  0.05167  -0.02079 205 ARG E CZ  
5896 N NH1 . ARG E 191 ? 0.66742 0.67401 0.57079 0.00457  0.05234  -0.01692 205 ARG E NH1 
5897 N NH2 . ARG E 191 ? 0.55461 0.54447 0.43805 0.00600  0.04583  -0.02613 205 ARG E NH2 
5898 N N   . LEU E 192 ? 0.44416 0.51391 0.35412 0.00443  0.09879  -0.00126 206 LEU E N   
5899 C CA  . LEU E 192 ? 0.52514 0.60314 0.43487 0.00016  0.10592  0.00562  206 LEU E CA  
5900 C C   . LEU E 192 ? 0.64062 0.71871 0.53218 0.00212  0.11283  0.00366  206 LEU E C   
5901 O O   . LEU E 192 ? 0.57421 0.65656 0.46500 0.00720  0.11881  -0.00243 206 LEU E O   
5902 C CB  . LEU E 192 ? 0.45867 0.54966 0.38816 0.00016  0.11216  0.00707  206 LEU E CB  
5903 C CG  . LEU E 192 ? 0.51623 0.61708 0.44615 -0.00337 0.12218  0.01263  206 LEU E CG  
5904 C CD1 . LEU E 192 ? 0.50659 0.60368 0.43110 -0.01019 0.11934  0.02130  206 LEU E CD1 
5905 C CD2 . LEU E 192 ? 0.53449 0.64851 0.48612 -0.00287 0.12783  0.01244  206 LEU E CD2 
5906 N N   . ARG E 193 ? 0.61768 0.69073 0.49425 -0.00163 0.11181  0.00858  207 ARG E N   
5907 C CA  . ARG E 193 ? 0.57641 0.64774 0.43288 0.00006  0.11739  0.00734  207 ARG E CA  
5908 C C   . ARG E 193 ? 0.67979 0.75845 0.53471 -0.00392 0.12647  0.01476  207 ARG E C   
5909 O O   . ARG E 193 ? 0.59697 0.67531 0.45548 -0.00941 0.12415  0.02240  207 ARG E O   
5910 C CB  . ARG E 193 ? 0.42986 0.48877 0.26806 -0.00044 0.10904  0.00667  207 ARG E CB  
5911 C CG  . ARG E 193 ? 0.67175 0.72716 0.48891 0.00361  0.11282  0.00187  207 ARG E CG  
5912 C CD  . ARG E 193 ? 0.58788 0.63107 0.38940 0.00411  0.10315  -0.00091 207 ARG E CD  
5913 N NE  . ARG E 193 ? 0.78182 0.82158 0.56621 0.00941  0.10558  -0.00819 207 ARG E NE  
5914 C CZ  . ARG E 193 ? 0.73916 0.76901 0.50873 0.01113  0.09823  -0.01270 207 ARG E CZ  
5915 N NH1 . ARG E 193 ? 0.54886 0.57128 0.31846 0.00789  0.08815  -0.01074 207 ARG E NH1 
5916 N NH2 . ARG E 193 ? 0.65274 0.68032 0.40768 0.01624  0.10108  -0.01978 207 ARG E NH2 
5917 N N   . VAL E 194 ? 0.68346 0.76850 0.53328 -0.00123 0.13712  0.01236  208 VAL E N   
5918 C CA  . VAL E 194 ? 0.58794 0.67934 0.43432 -0.00470 0.14742  0.01874  208 VAL E CA  
5919 C C   . VAL E 194 ? 0.70945 0.79664 0.53153 -0.00199 0.15315  0.01657  208 VAL E C   
5920 O O   . VAL E 194 ? 0.75532 0.83662 0.56616 0.00291  0.14979  0.00935  208 VAL E O   
5921 C CB  . VAL E 194 ? 0.52505 0.63040 0.39217 -0.00471 0.15684  0.01828  208 VAL E CB  
5922 C CG1 . VAL E 194 ? 0.54115 0.65025 0.43133 -0.00728 0.15053  0.02057  208 VAL E CG1 
5923 C CG2 . VAL E 194 ? 0.61361 0.72332 0.48247 0.00196  0.16172  0.00877  208 VAL E CG2 
5924 N N   . SER E 195 ? 0.85546 0.94514 0.66888 -0.00530 0.16190  0.02296  209 SER E N   
5925 C CA  . SER E 195 ? 0.82460 0.91074 0.61441 -0.00274 0.16882  0.02130  209 SER E CA  
5926 C C   . SER E 195 ? 0.83305 0.92676 0.62688 0.00259  0.17754  0.01285  209 SER E C   
5927 O O   . SER E 195 ? 0.77305 0.87734 0.58877 0.00299  0.18192  0.01070  209 SER E O   
5928 C CB  . SER E 195 ? 0.72107 0.80817 0.50163 -0.00763 0.17742  0.03042  209 SER E CB  
5929 O OG  . SER E 195 ? 0.82390 0.92352 0.62355 -0.01037 0.18753  0.03231  209 SER E OG  
5930 N N   . ALA E 196 ? 0.86046 0.94866 0.63307 0.00700  0.17968  0.00761  210 ALA E N   
5931 C CA  . ALA E 196 ? 0.86866 0.96359 0.64330 0.01229  0.18840  -0.00080 210 ALA E CA  
5932 C C   . ALA E 196 ? 0.85754 0.96453 0.64170 0.00994  0.20313  0.00220  210 ALA E C   
5933 O O   . ALA E 196 ? 0.73165 0.84886 0.53228 0.01278  0.20939  -0.00361 210 ALA E O   
5934 C CB  . ALA E 196 ? 0.79210 0.87859 0.53985 0.01685  0.18891  -0.00613 210 ALA E CB  
5935 N N   . THR E 197 ? 0.90121 1.00777 0.67888 0.00364  0.20585  0.01041  211 THR E N   
5936 C CA  . THR E 197 ? 0.89958 1.01865 0.69067 -0.00062 0.21546  0.01269  211 THR E CA  
5937 C C   . THR E 197 ? 0.82674 0.95656 0.64721 -0.00244 0.21718  0.01391  211 THR E C   
5938 O O   . THR E 197 ? 0.99058 1.13314 0.82763 -0.00178 0.22534  0.01036  211 THR E O   
5939 C CB  . THR E 197 ? 0.90229 1.01813 0.68179 -0.00719 0.21486  0.02150  211 THR E CB  
5940 O OG1 . THR E 197 ? 0.97212 1.07926 0.74978 -0.01066 0.20499  0.02827  211 THR E OG1 
5941 C CG2 . THR E 197 ? 1.02276 1.13138 0.77541 -0.00499 0.21577  0.01939  211 THR E CG2 
5942 N N   . PHE E 198 ? 0.90711 1.03247 0.73491 -0.00441 0.20914  0.01866  212 PHE E N   
5943 C CA  . PHE E 198 ? 0.79052 0.92578 0.64625 -0.00627 0.20968  0.02009  212 PHE E CA  
5944 C C   . PHE E 198 ? 0.77693 0.91907 0.64916 -0.00006 0.20911  0.01049  212 PHE E C   
5945 O O   . PHE E 198 ? 0.68483 0.83920 0.58028 -0.00038 0.21412  0.00890  212 PHE E O   
5946 C CB  . PHE E 198 ? 0.74064 0.86933 0.60068 -0.01002 0.19809  0.02651  212 PHE E CB  
5947 C CG  . PHE E 198 ? 0.72722 0.86561 0.61552 -0.01310 0.19689  0.02865  212 PHE E CG  
5948 C CD1 . PHE E 198 ? 0.65610 0.80153 0.55529 -0.01975 0.20195  0.03434  212 PHE E CD1 
5949 C CD2 . PHE E 198 ? 0.64078 0.78043 0.54560 -0.01018 0.18755  0.02373  212 PHE E CD2 
5950 C CE1 . PHE E 198 ? 0.67976 0.83406 0.60464 -0.02243 0.20060  0.03577  212 PHE E CE1 
5951 C CE2 . PHE E 198 ? 0.66765 0.81589 0.59748 -0.01267 0.18601  0.02550  212 PHE E CE2 
5952 C CZ  . PHE E 198 ? 0.67481 0.83104 0.61456 -0.01835 0.19389  0.03194  212 PHE E CZ  
5953 N N   . TRP E 199 ? 0.68399 0.81835 0.54548 0.00551  0.20198  0.00357  213 TRP E N   
5954 C CA  . TRP E 199 ? 0.77714 0.91661 0.65357 0.01157  0.20005  -0.00585 213 TRP E CA  
5955 C C   . TRP E 199 ? 0.90179 1.05125 0.78041 0.01517  0.21347  -0.01200 213 TRP E C   
5956 O O   . TRP E 199 ? 0.80012 0.95958 0.69959 0.01841  0.21583  -0.01776 213 TRP E O   
5957 C CB  . TRP E 199 ? 0.66590 0.79335 0.52992 0.01618  0.18883  -0.01146 213 TRP E CB  
5958 C CG  . TRP E 199 ? 0.75975 0.89067 0.63330 0.02326  0.18864  -0.02184 213 TRP E CG  
5959 C CD1 . TRP E 199 ? 0.76358 0.89188 0.62381 0.02895  0.19199  -0.02981 213 TRP E CD1 
5960 C CD2 . TRP E 199 ? 0.80630 0.94367 0.70459 0.02568  0.18481  -0.02548 213 TRP E CD2 
5961 N NE1 . TRP E 199 ? 0.70268 0.83528 0.57828 0.03473  0.19048  -0.03817 213 TRP E NE1 
5962 C CE2 . TRP E 199 ? 0.81740 0.95541 0.71617 0.03297  0.18595  -0.03558 213 TRP E CE2 
5963 C CE3 . TRP E 199 ? 0.65795 0.80021 0.57752 0.02261  0.18022  -0.02130 213 TRP E CE3 
5964 C CZ2 . TRP E 199 ? 0.81996 0.96292 0.73952 0.03742  0.18247  -0.04132 213 TRP E CZ2 
5965 C CZ3 . TRP E 199 ? 0.72291 0.87016 0.66253 0.02704  0.17670  -0.02707 213 TRP E CZ3 
5966 C CH2 . TRP E 199 ? 0.78950 0.93683 0.72889 0.03446  0.17771  -0.03685 213 TRP E CH2 
5967 N N   . GLN E 200 ? 0.88181 1.02858 0.73898 0.01484  0.22233  -0.01108 214 GLN E N   
5968 C CA  . GLN E 200 ? 0.83212 0.98734 0.68878 0.01842  0.23543  -0.01752 214 GLN E CA  
5969 C C   . GLN E 200 ? 0.83396 1.00488 0.71212 0.01408  0.24285  -0.01493 214 GLN E C   
5970 O O   . GLN E 200 ? 1.01087 1.19126 0.89306 0.01663  0.25093  -0.02004 214 GLN E O   
5971 C CB  . GLN E 200 ? 0.89858 1.04623 0.72719 0.01840  0.23672  -0.01794 214 GLN E CB  
5972 C CG  . GLN E 200 ? 0.80444 0.94139 0.61557 0.02570  0.23210  -0.02563 214 GLN E CG  
5973 C CD  . GLN E 200 ? 0.88039 1.00509 0.66207 0.02432  0.22800  -0.02332 214 GLN E CD  
5974 O OE1 . GLN E 200 ? 0.78897 0.91192 0.56259 0.01799  0.22792  -0.01519 214 GLN E OE1 
5975 N NE2 . GLN E 200 ? 0.88798 1.00415 0.65387 0.03052  0.22388  -0.03068 214 GLN E NE2 
5976 N N   . ASN E 201 ? 0.76355 0.93755 0.65556 0.00812  0.23996  -0.00720 215 ASN E N   
5977 C CA  . ASN E 201 ? 0.71496 0.90407 0.63043 0.00476  0.24546  -0.00507 215 ASN E CA  
5978 C C   . ASN E 201 ? 0.83711 1.03497 0.77904 0.00903  0.24494  -0.01151 215 ASN E C   
5979 O O   . ASN E 201 ? 0.83691 1.03136 0.78864 0.00823  0.23800  -0.00973 215 ASN E O   
5980 C CB  . ASN E 201 ? 0.56775 0.75566 0.48584 -0.00355 0.24168  0.00559  215 ASN E CB  
5981 C CG  . ASN E 201 ? 0.69463 0.89754 0.63724 -0.00712 0.24636  0.00795  215 ASN E CG  
5982 O OD1 . ASN E 201 ? 0.74364 0.95831 0.70251 -0.00331 0.25237  0.00188  215 ASN E OD1 
5983 N ND2 . ASN E 201 ? 0.63273 0.83481 0.57794 -0.01435 0.24317  0.01662  215 ASN E ND2 
5984 N N   . PRO E 202 ? 0.88002 1.08901 0.83419 0.01382  0.25184  -0.01911 216 PRO E N   
5985 C CA  . PRO E 202 ? 0.62273 0.83997 0.60230 0.01853  0.25057  -0.02648 216 PRO E CA  
5986 C C   . PRO E 202 ? 0.73270 0.96031 0.73894 0.01443  0.24851  -0.02226 216 PRO E C   
5987 O O   . PRO E 202 ? 0.59486 0.82994 0.62349 0.01813  0.24638  -0.02825 216 PRO E O   
5988 C CB  . PRO E 202 ? 0.70866 0.93494 0.69213 0.02445  0.25882  -0.03486 216 PRO E CB  
5989 C CG  . PRO E 202 ? 1.00571 1.22507 0.96094 0.02383  0.26339  -0.03298 216 PRO E CG  
5990 C CD  . PRO E 202 ? 0.76845 0.98215 0.71263 0.01567  0.26070  -0.02182 216 PRO E CD  
5991 N N   . ARG E 203 ? 0.69491 0.92338 0.69979 0.00707  0.24845  -0.01275 217 ARG E N   
5992 C CA  . ARG E 203 ? 0.72178 0.95884 0.75056 0.00284  0.24525  -0.00862 217 ARG E CA  
5993 C C   . ARG E 203 ? 0.82399 1.05229 0.85350 -0.00023 0.23543  -0.00385 217 ARG E C   
5994 O O   . ARG E 203 ? 0.72189 0.95676 0.77278 -0.00241 0.23117  -0.00212 217 ARG E O   
5995 C CB  . ARG E 203 ? 0.63491 0.87767 0.66360 -0.00374 0.24995  -0.00135 217 ARG E CB  
5996 N N   . ASN E 204 ? 0.74124 0.95472 0.74796 -0.00016 0.23148  -0.00174 218 ASN E N   
5997 C CA  . ASN E 204 ? 0.64354 0.84751 0.64952 -0.00243 0.22009  0.00323  218 ASN E CA  
5998 C C   . ASN E 204 ? 0.71370 0.91754 0.73368 0.00352  0.20904  -0.00344 218 ASN E C   
5999 O O   . ASN E 204 ? 0.69581 0.89785 0.71143 0.01021  0.20816  -0.01136 218 ASN E O   
6000 C CB  . ASN E 204 ? 0.63574 0.82377 0.61254 -0.00361 0.21512  0.00753  218 ASN E CB  
6001 C CG  . ASN E 204 ? 0.57989 0.76586 0.54358 -0.01057 0.22014  0.01580  218 ASN E CG  
6002 O OD1 . ASN E 204 ? 0.63496 0.82902 0.61284 -0.01613 0.22067  0.02011  218 ASN E OD1 
6003 N ND2 . ASN E 204 ? 0.61463 0.78941 0.55138 -0.01039 0.21993  0.01738  218 ASN E ND2 
6004 N N   . HIS E 205 ? 0.69008 0.89515 0.72617 0.00113  0.20059  -0.00017 219 HIS E N   
6005 C CA  . HIS E 205 ? 0.61356 0.81905 0.66491 0.00631  0.19044  -0.00565 219 HIS E CA  
6006 C C   . HIS E 205 ? 0.66104 0.85172 0.70160 0.00543  0.17666  -0.00207 219 HIS E C   
6007 O O   . HIS E 205 ? 0.61224 0.79959 0.65236 -0.00066 0.17284  0.00566  219 HIS E O   
6008 C CB  . HIS E 205 ? 0.58539 0.80458 0.66510 0.00479  0.19152  -0.00559 219 HIS E CB  
6009 C CG  . HIS E 205 ? 0.66540 0.88573 0.76112 0.01076  0.18179  -0.01155 219 HIS E CG  
6010 N ND1 . HIS E 205 ? 0.77487 0.98929 0.86455 0.01830  0.17730  -0.01898 219 HIS E ND1 
6011 C CD2 . HIS E 205 ? 0.68026 0.90628 0.79713 0.01047  0.17548  -0.01115 219 HIS E CD2 
6012 C CE1 . HIS E 205 ? 0.67638 0.89230 0.78237 0.02246  0.16873  -0.02259 219 HIS E CE1 
6013 N NE2 . HIS E 205 ? 0.79605 1.01904 0.91843 0.01794  0.16732  -0.01800 219 HIS E NE2 
6014 N N   . PHE E 206 ? 0.57636 0.75826 0.60902 0.01139  0.16948  -0.00790 220 PHE E N   
6015 C CA  . PHE E 206 ? 0.53751 0.70486 0.55979 0.01105  0.15686  -0.00580 220 PHE E CA  
6016 C C   . PHE E 206 ? 0.56324 0.72990 0.60108 0.01565  0.14766  -0.01022 220 PHE E C   
6017 O O   . PHE E 206 ? 0.58012 0.74993 0.62400 0.02241  0.14866  -0.01807 220 PHE E O   
6018 C CB  . PHE E 206 ? 0.54799 0.70357 0.54626 0.01388  0.15556  -0.00887 220 PHE E CB  
6019 C CG  . PHE E 206 ? 0.63815 0.79270 0.61818 0.01022  0.16384  -0.00489 220 PHE E CG  
6020 C CD1 . PHE E 206 ? 0.67602 0.83924 0.65416 0.01201  0.17620  -0.00815 220 PHE E CD1 
6021 C CD2 . PHE E 206 ? 0.57268 0.71719 0.53698 0.00516  0.15925  0.00198  220 PHE E CD2 
6022 C CE1 . PHE E 206 ? 0.69678 0.85792 0.65644 0.00876  0.18393  -0.00418 220 PHE E CE1 
6023 C CE2 . PHE E 206 ? 0.60297 0.74557 0.54935 0.00223  0.16630  0.00585  220 PHE E CE2 
6024 C CZ  . PHE E 206 ? 0.68206 0.83256 0.62541 0.00401  0.17869  0.00296  220 PHE E CZ  
6025 N N   . ARG E 207 ? 0.53419 0.69613 0.57779 0.01222  0.13864  -0.00528 221 ARG E N   
6026 C CA  . ARG E 207 ? 0.58574 0.74517 0.64205 0.01623  0.12925  -0.00856 221 ARG E CA  
6027 C C   . ARG E 207 ? 0.50621 0.65061 0.55212 0.01384  0.11812  -0.00488 221 ARG E C   
6028 O O   . ARG E 207 ? 0.42475 0.56629 0.46645 0.00725  0.11636  0.00236  221 ARG E O   
6029 C CB  . ARG E 207 ? 0.38186 0.55384 0.46223 0.01497  0.12984  -0.00717 221 ARG E CB  
6030 C CG  . ARG E 207 ? 0.42715 0.59635 0.51987 0.02003  0.12007  -0.01099 221 ARG E CG  
6031 C CD  . ARG E 207 ? 0.59250 0.77573 0.70999 0.02044  0.12110  -0.01166 221 ARG E CD  
6032 N NE  . ARG E 207 ? 0.50806 0.69203 0.63167 0.01359  0.11757  -0.00418 221 ARG E NE  
6033 C CZ  . ARG E 207 ? 0.56414 0.75823 0.69483 0.00755  0.12482  0.00051  221 ARG E CZ  
6034 N NH1 . ARG E 207 ? 0.71179 0.91625 0.84431 0.00717  0.13650  -0.00119 221 ARG E NH1 
6035 N NH2 . ARG E 207 ? 0.54738 0.74083 0.68333 0.00165  0.12054  0.00698  221 ARG E NH2 
6036 N N   . CYS E 208 ? 0.45092 0.58570 0.49327 0.01915  0.11085  -0.01000 222 CYS E N   
6037 C CA  . CYS E 208 ? 0.41876 0.53963 0.45472 0.01748  0.10010  -0.00756 222 CYS E CA  
6038 C C   . CYS E 208 ? 0.36938 0.49185 0.42260 0.01916  0.09354  -0.00764 222 CYS E C   
6039 O O   . CYS E 208 ? 0.50199 0.62851 0.56567 0.02559  0.09329  -0.01352 222 CYS E O   
6040 C CB  . CYS E 208 ? 0.47232 0.58030 0.49310 0.02192  0.09620  -0.01305 222 CYS E CB  
6041 S SG  . CYS E 208 ? 0.64090 0.73137 0.65397 0.01960  0.08394  -0.01065 222 CYS E SG  
6042 N N   . GLN E 209 ? 0.38393 0.50291 0.43970 0.01366  0.08800  -0.00133 223 GLN E N   
6043 C CA  . GLN E 209 ? 0.39471 0.51675 0.46701 0.01410  0.08250  -0.00021 223 GLN E CA  
6044 C C   . GLN E 209 ? 0.35348 0.46035 0.41877 0.01275  0.07225  0.00187  223 GLN E C   
6045 O O   . GLN E 209 ? 0.35811 0.45824 0.41364 0.00675  0.07016  0.00703  223 GLN E O   
6046 C CB  . GLN E 209 ? 0.46429 0.59834 0.54855 0.00812  0.08660  0.00562  223 GLN E CB  
6047 C CG  . GLN E 209 ? 0.40837 0.54870 0.51179 0.00887  0.08216  0.00603  223 GLN E CG  
6048 C CD  . GLN E 209 ? 0.39169 0.54635 0.50878 0.00372  0.08824  0.01019  223 GLN E CD  
6049 O OE1 . GLN E 209 ? 0.62670 0.79344 0.75041 0.00452  0.09733  0.00807  223 GLN E OE1 
6050 N NE2 . GLN E 209 ? 0.38616 0.53932 0.50751 -0.00177 0.08364  0.01600  223 GLN E NE2 
6051 N N   . VAL E 210 ? 0.38748 0.48870 0.45768 0.01830  0.06599  -0.00215 224 VAL E N   
6052 C CA  . VAL E 210 ? 0.32432 0.41005 0.38739 0.01746  0.05679  -0.00072 224 VAL E CA  
6053 C C   . VAL E 210 ? 0.35996 0.44766 0.43727 0.01843  0.05107  0.00070  224 VAL E C   
6054 O O   . VAL E 210 ? 0.36261 0.45239 0.44884 0.02519  0.04911  -0.00402 224 VAL E O   
6055 C CB  . VAL E 210 ? 0.40753 0.48062 0.45957 0.02318  0.05378  -0.00666 224 VAL E CB  
6056 C CG1 . VAL E 210 ? 0.28217 0.33904 0.32758 0.02174  0.04492  -0.00490 224 VAL E CG1 
6057 C CG2 . VAL E 210 ? 0.34296 0.41412 0.38044 0.02228  0.05904  -0.00845 224 VAL E CG2 
6058 N N   . GLN E 211 ? 0.37424 0.46093 0.45340 0.01198  0.04804  0.00695  225 GLN E N   
6059 C CA  . GLN E 211 ? 0.28244 0.36903 0.37282 0.01235  0.04171  0.00863  225 GLN E CA  
6060 C C   . GLN E 211 ? 0.37453 0.44347 0.45546 0.01459  0.03347  0.00756  225 GLN E C   
6061 O O   . GLN E 211 ? 0.32948 0.38677 0.39746 0.01023  0.03124  0.01009  225 GLN E O   
6062 C CB  . GLN E 211 ? 0.31573 0.40755 0.41122 0.00445  0.04185  0.01550  225 GLN E CB  
6063 C CG  . GLN E 211 ? 0.33269 0.42192 0.43675 0.00391  0.03446  0.01771  225 GLN E CG  
6064 C CD  . GLN E 211 ? 0.39862 0.50048 0.52103 0.00865  0.03445  0.01478  225 GLN E CD  
6065 O OE1 . GLN E 211 ? 0.33952 0.45643 0.47405 0.00656  0.04014  0.01568  225 GLN E OE1 
6066 N NE2 . GLN E 211 ? 0.33761 0.43311 0.46231 0.01511  0.02797  0.01115  225 GLN E NE2 
6067 N N   . PHE E 212 ? 0.35596 0.42266 0.44337 0.02142  0.02903  0.00370  226 PHE E N   
6068 C CA  . PHE E 212 ? 0.28625 0.33571 0.36532 0.02407  0.02131  0.00280  226 PHE E CA  
6069 C C   . PHE E 212 ? 0.34213 0.39073 0.42952 0.02320  0.01497  0.00604  226 PHE E C   
6070 O O   . PHE E 212 ? 0.42760 0.48854 0.53008 0.02590  0.01498  0.00514  226 PHE E O   
6071 C CB  . PHE E 212 ? 0.31311 0.35803 0.39102 0.03313  0.02034  -0.00407 226 PHE E CB  
6072 C CG  . PHE E 212 ? 0.33325 0.35985 0.40303 0.03642  0.01255  -0.00496 226 PHE E CG  
6073 C CD1 . PHE E 212 ? 0.34963 0.36002 0.40351 0.03335  0.01085  -0.00416 226 PHE E CD1 
6074 C CD2 . PHE E 212 ? 0.27882 0.30407 0.35673 0.04267  0.00695  -0.00676 226 PHE E CD2 
6075 C CE1 . PHE E 212 ? 0.25108 0.24389 0.29717 0.03602  0.00444  -0.00487 226 PHE E CE1 
6076 C CE2 . PHE E 212 ? 0.27070 0.27784 0.33973 0.04579  0.00004  -0.00722 226 PHE E CE2 
6077 C CZ  . PHE E 212 ? 0.28140 0.27209 0.33441 0.04227  -0.00085 -0.00614 226 PHE E CZ  
6078 N N   . TYR E 213 ? 0.32177 0.35599 0.39952 0.01940  0.00970  0.00947  227 TYR E N   
6079 C CA  . TYR E 213 ? 0.35026 0.38060 0.43271 0.01860  0.00317  0.01248  227 TYR E CA  
6080 C C   . TYR E 213 ? 0.35546 0.36904 0.42993 0.02453  -0.00323 0.00977  227 TYR E C   
6081 O O   . TYR E 213 ? 0.38438 0.38231 0.44474 0.02264  -0.00473 0.01016  227 TYR E O   
6082 C CB  . TYR E 213 ? 0.21197 0.23840 0.28956 0.00953  0.00236  0.01857  227 TYR E CB  
6083 C CG  . TYR E 213 ? 0.27732 0.31875 0.36188 0.00354  0.00835  0.02180  227 TYR E CG  
6084 C CD1 . TYR E 213 ? 0.24340 0.29834 0.34289 0.00200  0.00870  0.02397  227 TYR E CD1 
6085 C CD2 . TYR E 213 ? 0.27681 0.31841 0.35274 -0.00050 0.01354  0.02261  227 TYR E CD2 
6086 C CE1 . TYR E 213 ? 0.23964 0.30736 0.34524 -0.00365 0.01452  0.02714  227 TYR E CE1 
6087 C CE2 . TYR E 213 ? 0.32331 0.37733 0.40432 -0.00577 0.01901  0.02592  227 TYR E CE2 
6088 C CZ  . TYR E 213 ? 0.32107 0.38784 0.41685 -0.00748 0.01971  0.02835  227 TYR E CZ  
6089 O OH  . TYR E 213 ? 0.36542 0.44360 0.46591 -0.01291 0.02550  0.03187  227 TYR E OH  
6090 N N   . GLY E 214 ? 0.33190 0.34849 0.41552 0.03169  -0.00704 0.00693  228 GLY E N   
6091 C CA  . GLY E 214 ? 0.33770 0.33839 0.41377 0.03836  -0.01301 0.00417  228 GLY E CA  
6092 C C   . GLY E 214 ? 0.39027 0.38530 0.46916 0.04016  -0.02065 0.00631  228 GLY E C   
6093 O O   . GLY E 214 ? 0.37417 0.36448 0.44953 0.03384  -0.02283 0.01126  228 GLY E O   
6094 N N   . LEU E 215 ? 0.43028 0.42562 0.51535 0.04903  -0.02496 0.00240  229 LEU E N   
6095 C CA  . LEU E 215 ? 0.46007 0.44866 0.54640 0.05209  -0.03305 0.00387  229 LEU E CA  
6096 C C   . LEU E 215 ? 0.42734 0.43445 0.53141 0.05104  -0.03372 0.00484  229 LEU E C   
6097 O O   . LEU E 215 ? 0.47126 0.49693 0.58906 0.05101  -0.02836 0.00265  229 LEU E O   
6098 C CB  . LEU E 215 ? 0.34880 0.32766 0.43275 0.06271  -0.03835 -0.00085 229 LEU E CB  
6099 C CG  . LEU E 215 ? 0.46049 0.42033 0.52763 0.06451  -0.03786 -0.00243 229 LEU E CG  
6100 C CD1 . LEU E 215 ? 0.50052 0.45042 0.56600 0.07538  -0.04375 -0.00678 229 LEU E CD1 
6101 C CD2 . LEU E 215 ? 0.34009 0.28235 0.39137 0.05719  -0.03916 0.00275  229 LEU E CD2 
6102 N N   . SER E 216 ? 0.33042 0.33202 0.43391 0.04996  -0.04013 0.00803  230 SER E N   
6103 C CA  . SER E 216 ? 0.53148 0.54880 0.65157 0.04956  -0.04224 0.00854  230 SER E CA  
6104 C C   . SER E 216 ? 0.52531 0.54604 0.65522 0.06009  -0.04850 0.00353  230 SER E C   
6105 O O   . SER E 216 ? 0.64690 0.65574 0.76914 0.06761  -0.05189 0.00036  230 SER E O   
6106 C CB  . SER E 216 ? 0.65031 0.66033 0.76498 0.04325  -0.04629 0.01409  230 SER E CB  
6107 O OG  . SER E 216 ? 0.66527 0.65585 0.76713 0.04773  -0.05389 0.01453  230 SER E OG  
6108 N N   . GLU E 217 ? 0.66704 0.70419 0.81460 0.06064  -0.05028 0.00264  231 GLU E N   
6109 C CA  . GLU E 217 ? 0.44093 0.48286 0.59980 0.07056  -0.05708 -0.00239 231 GLU E CA  
6110 C C   . GLU E 217 ? 0.52242 0.54463 0.66829 0.07528  -0.06720 -0.00101 231 GLU E C   
6111 O O   . GLU E 217 ? 0.72038 0.73773 0.86710 0.08516  -0.07330 -0.00523 231 GLU E O   
6112 C CB  . GLU E 217 ? 0.49692 0.56089 0.67804 0.06907  -0.05672 -0.00362 231 GLU E CB  
6113 N N   . ASN E 218 ? 0.77054 0.78081 0.90395 0.06847  -0.06903 0.00482  232 ASN E N   
6114 C CA  . ASN E 218 ? 0.76474 0.75505 0.88384 0.07197  -0.07787 0.00680  232 ASN E CA  
6115 C C   . ASN E 218 ? 0.84533 0.81363 0.94513 0.07585  -0.07868 0.00654  232 ASN E C   
6116 O O   . ASN E 218 ? 0.91848 0.86983 1.00707 0.08150  -0.08631 0.00691  232 ASN E O   
6117 C CB  . ASN E 218 ? 0.71028 0.69503 0.82216 0.06283  -0.07846 0.01292  232 ASN E CB  
6118 N N   . ASP E 219 ? 0.73675 0.70432 0.83197 0.07300  -0.07112 0.00590  233 ASP E N   
6119 C CA  . ASP E 219 ? 0.64954 0.59685 0.72766 0.07655  -0.07147 0.00507  233 ASP E CA  
6120 C C   . ASP E 219 ? 0.76393 0.71022 0.84658 0.08868  -0.07621 -0.00075 233 ASP E C   
6121 O O   . ASP E 219 ? 0.76264 0.72751 0.86256 0.09295  -0.07440 -0.00549 233 ASP E O   
6122 C CB  . ASP E 219 ? 0.60975 0.55835 0.68334 0.07061  -0.06236 0.00512  233 ASP E CB  
6123 C CG  . ASP E 219 ? 0.60645 0.54825 0.66975 0.05957  -0.05893 0.01085  233 ASP E CG  
6124 O OD1 . ASP E 219 ? 0.70921 0.63383 0.75953 0.05778  -0.06329 0.01436  233 ASP E OD1 
6125 O OD2 . ASP E 219 ? 0.53432 0.48770 0.60230 0.05279  -0.05182 0.01175  233 ASP E OD2 
6126 N N   . GLU E 220 ? 0.64510 0.56926 0.71223 0.09425  -0.08217 -0.00045 234 GLU E N   
6127 C CA  . GLU E 220 ? 0.68760 0.60799 0.75713 0.10622  -0.08734 -0.00579 234 GLU E CA  
6128 C C   . GLU E 220 ? 0.78650 0.70519 0.85344 0.10816  -0.08119 -0.00962 234 GLU E C   
6129 O O   . GLU E 220 ? 0.73782 0.64752 0.79290 0.10144  -0.07540 -0.00732 234 GLU E O   
6130 C CB  . GLU E 220 ? 0.67568 0.57162 0.72842 0.11176  -0.09629 -0.00370 234 GLU E CB  
6131 N N   . TRP E 221 ? 0.59572 0.52366 0.67455 0.11753  -0.08255 -0.01595 235 TRP E N   
6132 C CA  . TRP E 221 ? 0.59995 0.52780 0.67799 0.12054  -0.07703 -0.02057 235 TRP E CA  
6133 C C   . TRP E 221 ? 0.59858 0.52198 0.68024 0.13358  -0.08340 -0.02639 235 TRP E C   
6134 O O   . TRP E 221 ? 0.73016 0.66782 0.82824 0.13991  -0.08776 -0.02991 235 TRP E O   
6135 C CB  . TRP E 221 ? 0.54498 0.49741 0.63894 0.11600  -0.06789 -0.02307 235 TRP E CB  
6136 C CG  . TRP E 221 ? 0.52544 0.47628 0.61514 0.11678  -0.06110 -0.02682 235 TRP E CG  
6137 C CD1 . TRP E 221 ? 0.61122 0.57320 0.71218 0.12399  -0.05853 -0.03375 235 TRP E CD1 
6138 C CD2 . TRP E 221 ? 0.53874 0.47601 0.61184 0.11023  -0.05611 -0.02432 235 TRP E CD2 
6139 N NE1 . TRP E 221 ? 0.59836 0.55433 0.69003 0.12234  -0.05223 -0.03561 235 TRP E NE1 
6140 C CE2 . TRP E 221 ? 0.60330 0.54415 0.67801 0.11399  -0.05087 -0.02999 235 TRP E CE2 
6141 C CE3 . TRP E 221 ? 0.44014 0.36298 0.49781 0.10156  -0.05554 -0.01826 235 TRP E CE3 
6142 C CZ2 . TRP E 221 ? 0.59348 0.52387 0.65468 0.10946  -0.04556 -0.02981 235 TRP E CZ2 
6143 C CZ3 . TRP E 221 ? 0.52279 0.43565 0.56796 0.09700  -0.05016 -0.01820 235 TRP E CZ3 
6144 C CH2 . TRP E 221 ? 0.60427 0.52091 0.65117 0.10101  -0.04545 -0.02396 235 TRP E CH2 
6145 N N   . THR E 222 ? 0.65630 0.55989 0.72316 0.13761  -0.08405 -0.02765 236 THR E N   
6146 C CA  . THR E 222 ? 0.78799 0.68418 0.85601 0.15024  -0.09027 -0.03300 236 THR E CA  
6147 C C   . THR E 222 ? 0.92242 0.81564 0.98801 0.15335  -0.08474 -0.03808 236 THR E C   
6148 O O   . THR E 222 ? 1.00418 0.88843 1.06863 0.16368  -0.08945 -0.04256 236 THR E O   
6149 C CB  . THR E 222 ? 0.89421 0.76380 0.94422 0.15451  -0.09940 -0.02935 236 THR E CB  
6150 O OG1 . THR E 222 ? 0.72482 0.57505 0.75469 0.14600  -0.09581 -0.02387 236 THR E OG1 
6151 C CG2 . THR E 222 ? 0.85486 0.72915 0.91030 0.15551  -0.10705 -0.02654 236 THR E CG2 
6152 N N   . GLN E 223 ? 0.91309 0.81312 0.97751 0.14499  -0.07521 -0.03766 237 GLN E N   
6153 C CA  . GLN E 223 ? 0.82609 0.72505 0.88888 0.14771  -0.06964 -0.04296 237 GLN E CA  
6154 C C   . GLN E 223 ? 0.97317 0.89503 1.05702 0.15459  -0.06741 -0.05027 237 GLN E C   
6155 O O   . GLN E 223 ? 0.90444 0.84503 1.00497 0.15528  -0.06865 -0.05087 237 GLN E O   
6156 C CB  . GLN E 223 ? 0.78934 0.68876 0.84401 0.13670  -0.06064 -0.04036 237 GLN E CB  
6157 C CG  . GLN E 223 ? 0.82284 0.70070 0.85802 0.12923  -0.06194 -0.03374 237 GLN E CG  
6158 C CD  . GLN E 223 ? 1.03378 0.88929 1.05262 0.13109  -0.06141 -0.03543 237 GLN E CD  
6159 O OE1 . GLN E 223 ? 0.95187 0.81009 0.96909 0.12872  -0.05481 -0.03860 237 GLN E OE1 
6160 N NE2 . GLN E 223 ? 0.88967 0.72245 0.89590 0.13537  -0.06833 -0.03339 237 GLN E NE2 
6161 N N   . ASP E 224 ? 0.89574 0.81606 0.97918 0.15967  -0.06385 -0.05625 238 ASP E N   
6162 C CA  . ASP E 224 ? 0.88979 0.83115 0.99285 0.16640  -0.06098 -0.06385 238 ASP E CA  
6163 C C   . ASP E 224 ? 0.85361 0.81815 0.96757 0.15827  -0.05074 -0.06406 238 ASP E C   
6164 O O   . ASP E 224 ? 0.78449 0.77101 0.91803 0.16023  -0.04899 -0.06724 238 ASP E O   
6165 C CB  . ASP E 224 ? 0.94144 0.87317 1.04031 0.17480  -0.06051 -0.07050 238 ASP E CB  
6166 C CG  . ASP E 224 ? 1.00248 0.91858 1.09877 0.18629  -0.07106 -0.07261 238 ASP E CG  
6167 O OD1 . ASP E 224 ? 1.09022 1.00925 1.19338 0.18953  -0.07849 -0.07082 238 ASP E OD1 
6168 O OD2 . ASP E 224 ? 1.11519 1.01580 1.20243 0.19227  -0.07215 -0.07618 238 ASP E OD2 
6169 N N   . ARG E 225 ? 0.76474 0.72449 0.86634 0.14918  -0.04395 -0.06082 239 ARG E N   
6170 C CA  . ARG E 225 ? 0.57024 0.54974 0.67947 0.14142  -0.03423 -0.06054 239 ARG E CA  
6171 C C   . ARG E 225 ? 0.60026 0.59295 0.71890 0.13484  -0.03469 -0.05517 239 ARG E C   
6172 O O   . ARG E 225 ? 0.66348 0.64765 0.77924 0.13463  -0.04219 -0.05083 239 ARG E O   
6173 C CB  . ARG E 225 ? 0.65878 0.62811 0.75118 0.13355  -0.02824 -0.05813 239 ARG E CB  
6174 C CG  . ARG E 225 ? 0.68148 0.63265 0.75768 0.12622  -0.03193 -0.05058 239 ARG E CG  
6175 C CD  . ARG E 225 ? 0.63455 0.57850 0.69669 0.11838  -0.02569 -0.04909 239 ARG E CD  
6176 N NE  . ARG E 225 ? 0.76147 0.68713 0.80845 0.11171  -0.02902 -0.04272 239 ARG E NE  
6177 C CZ  . ARG E 225 ? 0.66787 0.59771 0.71360 0.10231  -0.02755 -0.03655 239 ARG E CZ  
6178 N NH1 . ARG E 225 ? 0.55372 0.50467 0.61166 0.09811  -0.02284 -0.03541 239 ARG E NH1 
6179 N NH2 . ARG E 225 ? 0.58924 0.50139 0.62128 0.09693  -0.03064 -0.03149 239 ARG E NH2 
6180 N N   . ALA E 226 ? 0.53775 0.55110 0.66734 0.12941  -0.02632 -0.05556 240 ALA E N   
6181 C CA  . ALA E 226 ? 0.53439 0.56221 0.67484 0.12305  -0.02570 -0.05107 240 ALA E CA  
6182 C C   . ALA E 226 ? 0.57701 0.59146 0.70281 0.11410  -0.02811 -0.04280 240 ALA E C   
6183 O O   . ALA E 226 ? 0.62016 0.62055 0.72917 0.10950  -0.02593 -0.04038 240 ALA E O   
6184 C CB  . ALA E 226 ? 0.43187 0.48186 0.58394 0.11811  -0.01509 -0.05258 240 ALA E CB  
6185 N N   . LYS E 227 ? 0.50945 0.52868 0.64238 0.11174  -0.03269 -0.03890 241 LYS E N   
6186 C CA  . LYS E 227 ? 0.43684 0.44448 0.55765 0.10361  -0.03538 -0.03133 241 LYS E CA  
6187 C C   . LYS E 227 ? 0.43771 0.45228 0.55489 0.09290  -0.02673 -0.02753 241 LYS E C   
6188 O O   . LYS E 227 ? 0.35927 0.39368 0.49018 0.08957  -0.02108 -0.02777 241 LYS E O   
6189 C CB  . LYS E 227 ? 0.39032 0.40400 0.52154 0.10395  -0.04192 -0.02884 241 LYS E CB  
6190 C CG  . LYS E 227 ? 0.45526 0.45797 0.57521 0.09578  -0.04483 -0.02131 241 LYS E CG  
6191 C CD  . LYS E 227 ? 0.51747 0.52801 0.64904 0.09652  -0.05109 -0.01965 241 LYS E CD  
6192 C CE  . LYS E 227 ? 0.47015 0.46945 0.59028 0.08860  -0.05395 -0.01245 241 LYS E CE  
6193 N NZ  . LYS E 227 ? 0.63038 0.64205 0.76413 0.08720  -0.05784 -0.01084 241 LYS E NZ  
6194 N N   . PRO E 228 ? 0.51667 0.51544 0.61594 0.08728  -0.02549 -0.02409 242 PRO E N   
6195 C CA  . PRO E 228 ? 0.37918 0.38419 0.47448 0.07789  -0.01764 -0.02107 242 PRO E CA  
6196 C C   . PRO E 228 ? 0.38948 0.40262 0.48992 0.06955  -0.01742 -0.01491 242 PRO E C   
6197 O O   . PRO E 228 ? 0.42716 0.42927 0.51619 0.06264  -0.01866 -0.00974 242 PRO E O   
6198 C CB  . PRO E 228 ? 0.44156 0.42546 0.51684 0.07543  -0.01819 -0.01988 242 PRO E CB  
6199 C CG  . PRO E 228 ? 0.46343 0.42942 0.53170 0.07958  -0.02700 -0.01861 242 PRO E CG  
6200 C CD  . PRO E 228 ? 0.39410 0.36822 0.47612 0.08916  -0.03139 -0.02275 242 PRO E CD  
6201 N N   . VAL E 229 ? 0.34842 0.38100 0.46669 0.07006  -0.01570 -0.01572 243 VAL E N   
6202 C CA  . VAL E 229 ? 0.42621 0.46776 0.55153 0.06269  -0.01563 -0.01039 243 VAL E CA  
6203 C C   . VAL E 229 ? 0.41602 0.46661 0.53996 0.05412  -0.00686 -0.00756 243 VAL E C   
6204 O O   . VAL E 229 ? 0.39834 0.45010 0.51729 0.05461  -0.00088 -0.01025 243 VAL E O   
6205 C CB  . VAL E 229 ? 0.41443 0.47289 0.56045 0.06684  -0.01777 -0.01281 243 VAL E CB  
6206 C CG1 . VAL E 229 ? 0.31503 0.36351 0.46135 0.07519  -0.02774 -0.01498 243 VAL E CG1 
6207 C CG2 . VAL E 229 ? 0.28324 0.35911 0.44250 0.07059  -0.01062 -0.01852 243 VAL E CG2 
6208 N N   . THR E 230 ? 0.49647 0.55298 0.62430 0.04646  -0.00629 -0.00218 244 THR E N   
6209 C CA  . THR E 230 ? 0.35226 0.41866 0.48050 0.03855  0.00170  0.00088  244 THR E CA  
6210 C C   . THR E 230 ? 0.44251 0.52750 0.58418 0.04126  0.00912  -0.00332 244 THR E C   
6211 O O   . THR E 230 ? 0.40016 0.49813 0.55878 0.04486  0.00840  -0.00585 244 THR E O   
6212 C CB  . THR E 230 ? 0.23451 0.30524 0.36771 0.03095  0.00026  0.00688  244 THR E CB  
6213 O OG1 . THR E 230 ? 0.40001 0.45312 0.51906 0.02746  -0.00517 0.01079  244 THR E OG1 
6214 C CG2 . THR E 230 ? 0.22432 0.30694 0.36028 0.02343  0.00851  0.01000  244 THR E CG2 
6215 N N   . GLN E 231 ? 0.35003 0.43627 0.48416 0.03962  0.01631  -0.00440 245 GLN E N   
6216 C CA  . GLN E 231 ? 0.30455 0.40684 0.44928 0.04251  0.02412  -0.00884 245 GLN E CA  
6217 C C   . GLN E 231 ? 0.37403 0.47786 0.50847 0.03699  0.03240  -0.00703 245 GLN E C   
6218 O O   . GLN E 231 ? 0.36016 0.45134 0.47873 0.03262  0.03124  -0.00376 245 GLN E O   
6219 C CB  . GLN E 231 ? 0.26285 0.36293 0.40963 0.05260  0.02243  -0.01626 245 GLN E CB  
6220 C CG  . GLN E 231 ? 0.31383 0.39772 0.44217 0.05465  0.02198  -0.01817 245 GLN E CG  
6221 C CD  . GLN E 231 ? 0.42358 0.50190 0.55335 0.06487  0.01813  -0.02493 245 GLN E CD  
6222 O OE1 . GLN E 231 ? 0.53693 0.62150 0.66926 0.06955  0.02332  -0.03056 245 GLN E OE1 
6223 N NE2 . GLN E 231 ? 0.35355 0.41961 0.48125 0.06855  0.00901  -0.02444 245 GLN E NE2 
6224 N N   . ILE E 232 ? 0.39530 0.51481 0.53903 0.03737  0.04083  -0.00946 246 ILE E N   
6225 C CA  . ILE E 232 ? 0.41031 0.53245 0.54447 0.03337  0.04939  -0.00855 246 ILE E CA  
6226 C C   . ILE E 232 ? 0.38943 0.51291 0.52158 0.04061  0.05344  -0.01586 246 ILE E C   
6227 O O   . ILE E 232 ? 0.48702 0.62179 0.63390 0.04632  0.05545  -0.02101 246 ILE E O   
6228 C CB  . ILE E 232 ? 0.38115 0.51948 0.52584 0.02730  0.05705  -0.00503 246 ILE E CB  
6229 C CG1 . ILE E 232 ? 0.19092 0.32702 0.33695 0.02003  0.05281  0.00213  246 ILE E CG1 
6230 C CG2 . ILE E 232 ? 0.29402 0.43450 0.42756 0.02417  0.06614  -0.00446 246 ILE E CG2 
6231 C CD1 . ILE E 232 ? 0.30892 0.45966 0.46541 0.01373  0.05989  0.00600  246 ILE E CD1 
6232 N N   . VAL E 233 ? 0.31226 0.42432 0.42678 0.04052  0.05439  -0.01674 247 VAL E N   
6233 C CA  . VAL E 233 ? 0.26345 0.37582 0.37363 0.04666  0.05880  -0.02356 247 VAL E CA  
6234 C C   . VAL E 233 ? 0.37954 0.49589 0.47945 0.04182  0.06757  -0.02201 247 VAL E C   
6235 O O   . VAL E 233 ? 0.41642 0.52490 0.50350 0.03548  0.06665  -0.01682 247 VAL E O   
6236 C CB  . VAL E 233 ? 0.33904 0.43335 0.43674 0.05158  0.05194  -0.02688 247 VAL E CB  
6237 C CG1 . VAL E 233 ? 0.32833 0.42416 0.42457 0.05896  0.05606  -0.03480 247 VAL E CG1 
6238 C CG2 . VAL E 233 ? 0.43139 0.51885 0.53598 0.05502  0.04248  -0.02652 247 VAL E CG2 
6239 N N   . SER E 234 ? 0.41734 0.54572 0.52270 0.04491  0.07603  -0.02658 248 SER E N   
6240 C CA  . SER E 234 ? 0.40659 0.54048 0.50329 0.04032  0.08528  -0.02477 248 SER E CA  
6241 C C   . SER E 234 ? 0.35236 0.48921 0.44502 0.04628  0.09173  -0.03220 248 SER E C   
6242 O O   . SER E 234 ? 0.43451 0.57299 0.53553 0.05388  0.09023  -0.03887 248 SER E O   
6243 C CB  . SER E 234 ? 0.29209 0.44170 0.40195 0.03496  0.09178  -0.02045 248 SER E CB  
6244 O OG  . SER E 234 ? 0.59206 0.75504 0.72260 0.03964  0.09360  -0.02492 248 SER E OG  
6245 N N   . ALA E 235 ? 0.42327 0.56027 0.50230 0.04288  0.09871  -0.03102 249 ALA E N   
6246 C CA  . ALA E 235 ? 0.45705 0.59833 0.53087 0.04727  0.10666  -0.03738 249 ALA E CA  
6247 C C   . ALA E 235 ? 0.52113 0.67031 0.58851 0.04128  0.11661  -0.03331 249 ALA E C   
6248 O O   . ALA E 235 ? 0.46412 0.61089 0.52602 0.03412  0.11564  -0.02578 249 ALA E O   
6249 C CB  . ALA E 235 ? 0.44485 0.57084 0.50143 0.05116  0.10234  -0.04174 249 ALA E CB  
6250 N N   . GLU E 236 ? 0.57081 0.72916 0.63868 0.04431  0.12638  -0.03830 250 GLU E N   
6251 C CA  . GLU E 236 ? 0.47933 0.64675 0.54344 0.03898  0.13711  -0.03455 250 GLU E CA  
6252 C C   . GLU E 236 ? 0.58973 0.75755 0.64048 0.04225  0.14546  -0.03998 250 GLU E C   
6253 O O   . GLU E 236 ? 0.60264 0.76723 0.65185 0.04927  0.14411  -0.04770 250 GLU E O   
6254 C CB  . GLU E 236 ? 0.68040 0.86497 0.76704 0.03739  0.14327  -0.03364 250 GLU E CB  
6255 C CG  . GLU E 236 ? 0.75632 0.95058 0.86178 0.04508  0.14435  -0.04212 250 GLU E CG  
6256 C CD  . GLU E 236 ? 0.97668 1.18531 1.10699 0.04349  0.14552  -0.04087 250 GLU E CD  
6257 O OE1 . GLU E 236 ? 0.85658 1.06720 0.98907 0.03618  0.14568  -0.03325 250 GLU E OE1 
6258 O OE2 . GLU E 236 ? 0.81944 1.03734 0.96747 0.04969  0.14599  -0.04778 250 GLU E OE2 
6259 N N   . ALA E 237 ? 0.49827 0.66951 0.53863 0.03706  0.15412  -0.03570 251 ALA E N   
6260 C CA  . ALA E 237 ? 0.57347 0.74629 0.60026 0.03919  0.16366  -0.03988 251 ALA E CA  
6261 C C   . ALA E 237 ? 0.58566 0.76829 0.61190 0.03314  0.17513  -0.03448 251 ALA E C   
6262 O O   . ALA E 237 ? 0.65264 0.83673 0.68313 0.02664  0.17403  -0.02659 251 ALA E O   
6263 C CB  . ALA E 237 ? 0.43842 0.59556 0.44026 0.03979  0.15876  -0.04041 251 ALA E CB  
6264 N N   . TRP E 238 ? 0.75188 0.94075 0.77244 0.03525  0.18648  -0.03882 252 TRP E N   
6265 C CA  . TRP E 238 ? 0.65651 0.85523 0.67735 0.03000  0.19909  -0.03451 252 TRP E CA  
6266 C C   . TRP E 238 ? 0.60329 0.79526 0.59763 0.02802  0.20577  -0.03246 252 TRP E C   
6267 O O   . TRP E 238 ? 0.80170 0.99496 0.78956 0.02161  0.21180  -0.02503 252 TRP E O   
6268 C CB  . TRP E 238 ? 0.54326 0.75862 0.58469 0.03332  0.20928  -0.04101 252 TRP E CB  
6269 C CG  . TRP E 238 ? 0.51577 0.74069 0.58444 0.03284  0.20514  -0.04053 252 TRP E CG  
6270 C CD1 . TRP E 238 ? 0.62261 0.84794 0.70656 0.03868  0.19595  -0.04592 252 TRP E CD1 
6271 C CD2 . TRP E 238 ? 0.53002 0.76463 0.61328 0.02618  0.20942  -0.03422 252 TRP E CD2 
6272 N NE1 . TRP E 238 ? 0.51913 0.75418 0.62611 0.03631  0.19400  -0.04355 252 TRP E NE1 
6273 C CE2 . TRP E 238 ? 0.54259 0.78381 0.65019 0.02853  0.20224  -0.03657 252 TRP E CE2 
6274 C CE3 . TRP E 238 ? 0.55451 0.79242 0.63241 0.01854  0.21860  -0.02685 252 TRP E CE3 
6275 C CZ2 . TRP E 238 ? 0.53768 0.78933 0.66495 0.02345  0.20385  -0.03226 252 TRP E CZ2 
6276 C CZ3 . TRP E 238 ? 0.59218 0.84011 0.68989 0.01330  0.22057  -0.02236 252 TRP E CZ3 
6277 C CH2 . TRP E 238 ? 0.57219 0.82720 0.69462 0.01574  0.21316  -0.02529 252 TRP E CH2 
6278 N N   . GLY E 239 ? 0.64902 0.83339 0.62743 0.03337  0.20475  -0.03874 253 GLY E N   
6279 C CA  . GLY E 239 ? 0.82791 1.00588 0.78045 0.03182  0.21088  -0.03708 253 GLY E CA  
6280 C C   . GLY E 239 ? 0.80054 0.98706 0.75079 0.03541  0.22431  -0.04368 253 GLY E C   
6281 O O   . GLY E 239 ? 0.65962 0.86027 0.62890 0.03530  0.23328  -0.04557 253 GLY E O   
6282 N N   . ARG E 240 ? 0.82702 1.00528 0.75444 0.03861  0.22585  -0.04762 254 ARG E N   
6283 C CA  . ARG E 240 ? 0.80061 0.98537 0.72360 0.04290  0.23785  -0.05510 254 ARG E CA  
6284 C C   . ARG E 240 ? 0.93337 1.11510 0.83256 0.03895  0.24785  -0.05037 254 ARG E C   
6285 O O   . ARG E 240 ? 0.91545 1.08839 0.79963 0.03377  0.24399  -0.04194 254 ARG E O   
6286 C CB  . ARG E 240 ? 0.77184 0.94966 0.68789 0.05087  0.23202  -0.06501 254 ARG E CB  
6287 N N   . ALA E 241 ? 1.14274 1.33195 1.03919 0.04181  0.25862  -0.05553 255 ALA E N   
6288 C CA  . ALA E 241 ? 1.01516 1.20290 0.89051 0.03884  0.26331  -0.05127 255 ALA E CA  
6289 C C   . ALA E 241 ? 0.98421 1.15864 0.83171 0.04230  0.25984  -0.05602 255 ALA E C   
6290 O O   . ALA E 241 ? 0.81580 0.97674 0.64609 0.04004  0.25231  -0.05171 255 ALA E O   
6291 C CB  . ALA E 241 ? 1.07420 1.27626 0.96027 0.04044  0.27378  -0.05367 255 ALA E CB  
# 
