data_8GSQ
# 
_entry.id   8GSQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.379 
_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   8GSQ         pdb_00008gsq 10.2210/pdb8gsq/pdb 
WWPDB D_1300031633 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8GSQ 
_pdbx_database_status.recvd_initial_deposition_date   2022-09-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Aouti, S.'       1 0000-0003-2731-3528 
'Padmanabhan, B.' 2 0000-0001-8434-828X 
# 
_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            'Acta Crystallogr D Struct Biol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2059-7983 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            79 
_citation.language                  ? 
_citation.page_first                531 
_citation.page_last                 544 
_citation.title                     
;Structure-based discovery of an antipsychotic drug, paliperidone, as a modulator of human superoxide dismutase 1: a potential therapeutic target in amyotrophic lateral sclerosis.
;
_citation.year                      2023 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1107/S2059798323003649 
_citation.pdbx_database_id_PubMed   37204819 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Aouti, S.'       1 ?                   
primary 'Padavattan, S.'  2 0000-0002-1732-5421 
primary 'Padmanabhan, B.' 3 ?                   
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8GSQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     163.793 
_cell.length_a_esd                 ? 
_cell.length_b                     202.455 
_cell.length_b_esd                 ? 
_cell.length_c                     143.996 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        48 
_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                         8GSQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
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 'Superoxide dismutase [Cu-Zn]' 15958.757 6   1.15.1.1 ? ? ? 
2 polymer     man 'Superoxide dismutase [Cu-Zn]' 16029.835 1   1.15.1.1 ? ? ? 
3 polymer     man 'Superoxide dismutase [Cu-Zn]' 15840.603 2   1.15.1.1 ? ? ? 
4 polymer     man 'Superoxide dismutase [Cu-Zn]' 15770.510 1   1.15.1.1 ? ? ? 
5 non-polymer syn 'ZINC ION' 65.409    9   ?        ? ? ? 
6 non-polymer syn GLYCEROL 92.094    6   ?        ? ? ? 
7 non-polymer syn 
;(9~{R})-3-[2-[4-(6-fluoranyl-1,2-benzoxazol-3-yl)piperidin-1-yl]ethyl]-2-methyl-9-oxidanyl-6,7,8,9-tetrahydropyrido[1,2-a]pyrimidin-4-one
;
426.484   1   ?        ? ? ? 
8 water       nat water 18.015    991 ?        ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Superoxide dismutase 1,hSod1' 
2 'Superoxide dismutase 1,hSod1' 
3 'Superoxide dismutase 1,hSod1' 
# 
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 
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
A,B,D,F,I,J ? 
2 'polypeptide(L)' no no 
;AMATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEE
RHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
;AMATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEE
RHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
C           ? 
3 'polypeptide(L)' no no 
;AATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDAER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
;AATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDAER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
E,G         ? 
4 'polypeptide(L)' no no 
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAA
;
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAA
;
H           ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   THR n 
1 4   LYS n 
1 5   ALA n 
1 6   VAL n 
1 7   CYS n 
1 8   VAL n 
1 9   LEU n 
1 10  LYS n 
1 11  GLY n 
1 12  ASP n 
1 13  GLY n 
1 14  PRO n 
1 15  VAL n 
1 16  GLN n 
1 17  GLY n 
1 18  ILE n 
1 19  ILE n 
1 20  ASN n 
1 21  PHE n 
1 22  GLU n 
1 23  GLN n 
1 24  LYS n 
1 25  GLU n 
1 26  SER n 
1 27  ASN n 
1 28  GLY n 
1 29  PRO n 
1 30  VAL n 
1 31  LYS n 
1 32  VAL n 
1 33  TRP n 
1 34  GLY n 
1 35  SER n 
1 36  ILE n 
1 37  LYS n 
1 38  GLY n 
1 39  LEU n 
1 40  THR n 
1 41  GLU n 
1 42  GLY n 
1 43  LEU n 
1 44  HIS n 
1 45  GLY n 
1 46  PHE n 
1 47  HIS n 
1 48  VAL n 
1 49  HIS n 
1 50  GLU n 
1 51  PHE n 
1 52  GLY n 
1 53  ASP n 
1 54  ASN n 
1 55  THR n 
1 56  ALA n 
1 57  GLY n 
1 58  CYS n 
1 59  THR n 
1 60  SER n 
1 61  ALA n 
1 62  GLY n 
1 63  PRO n 
1 64  HIS n 
1 65  PHE n 
1 66  ASN n 
1 67  PRO n 
1 68  LEU n 
1 69  SER n 
1 70  ARG n 
1 71  LYS n 
1 72  HIS n 
1 73  GLY n 
1 74  GLY n 
1 75  PRO n 
1 76  LYS n 
1 77  ASP n 
1 78  GLU n 
1 79  GLU n 
1 80  ARG n 
1 81  HIS n 
1 82  VAL n 
1 83  GLY n 
1 84  ASP n 
1 85  LEU n 
1 86  GLY n 
1 87  ASN n 
1 88  VAL n 
1 89  THR n 
1 90  ALA n 
1 91  ASP n 
1 92  LYS n 
1 93  ASP n 
1 94  GLY n 
1 95  VAL n 
1 96  ALA n 
1 97  ASP n 
1 98  VAL n 
1 99  SER n 
1 100 ILE n 
1 101 GLU n 
1 102 ASP n 
1 103 SER n 
1 104 VAL n 
1 105 ILE n 
1 106 SER n 
1 107 LEU n 
1 108 SER n 
1 109 GLY n 
1 110 ASP n 
1 111 HIS n 
1 112 CYS n 
1 113 ILE n 
1 114 ILE n 
1 115 GLY n 
1 116 ARG n 
1 117 THR n 
1 118 LEU n 
1 119 VAL n 
1 120 VAL n 
1 121 HIS n 
1 122 GLU n 
1 123 LYS n 
1 124 ALA n 
1 125 ASP n 
1 126 ASP n 
1 127 LEU n 
1 128 GLY n 
1 129 LYS n 
1 130 GLY n 
1 131 GLY n 
1 132 ASN n 
1 133 GLU n 
1 134 GLU n 
1 135 SER n 
1 136 THR n 
1 137 LYS n 
1 138 THR n 
1 139 GLY n 
1 140 ASN n 
1 141 ALA n 
1 142 GLY n 
1 143 SER n 
1 144 ARG n 
1 145 LEU n 
1 146 ALA n 
1 147 CYS n 
1 148 GLY n 
1 149 VAL n 
1 150 ILE n 
1 151 GLY n 
1 152 ILE n 
1 153 ALA n 
1 154 GLN n 
2 1   ALA n 
2 2   MET n 
2 3   ALA n 
2 4   THR n 
2 5   LYS n 
2 6   ALA n 
2 7   VAL n 
2 8   CYS n 
2 9   VAL n 
2 10  LEU n 
2 11  LYS n 
2 12  GLY n 
2 13  ASP n 
2 14  GLY n 
2 15  PRO n 
2 16  VAL n 
2 17  GLN n 
2 18  GLY n 
2 19  ILE n 
2 20  ILE n 
2 21  ASN n 
2 22  PHE n 
2 23  GLU n 
2 24  GLN n 
2 25  LYS n 
2 26  GLU n 
2 27  SER n 
2 28  ASN n 
2 29  GLY n 
2 30  PRO n 
2 31  VAL n 
2 32  LYS n 
2 33  VAL n 
2 34  TRP n 
2 35  GLY n 
2 36  SER n 
2 37  ILE n 
2 38  LYS n 
2 39  GLY n 
2 40  LEU n 
2 41  THR n 
2 42  GLU n 
2 43  GLY n 
2 44  LEU n 
2 45  HIS n 
2 46  GLY n 
2 47  PHE n 
2 48  HIS n 
2 49  VAL n 
2 50  HIS n 
2 51  GLU n 
2 52  PHE n 
2 53  GLY n 
2 54  ASP n 
2 55  ASN n 
2 56  THR n 
2 57  ALA n 
2 58  GLY n 
2 59  CYS n 
2 60  THR n 
2 61  SER n 
2 62  ALA n 
2 63  GLY n 
2 64  PRO n 
2 65  HIS n 
2 66  PHE n 
2 67  ASN n 
2 68  PRO n 
2 69  LEU n 
2 70  SER n 
2 71  ARG n 
2 72  LYS n 
2 73  HIS n 
2 74  GLY n 
2 75  GLY n 
2 76  PRO n 
2 77  LYS n 
2 78  ASP n 
2 79  GLU n 
2 80  GLU n 
2 81  ARG n 
2 82  HIS n 
2 83  VAL n 
2 84  GLY n 
2 85  ASP n 
2 86  LEU n 
2 87  GLY n 
2 88  ASN n 
2 89  VAL n 
2 90  THR n 
2 91  ALA n 
2 92  ASP n 
2 93  LYS n 
2 94  ASP n 
2 95  GLY n 
2 96  VAL n 
2 97  ALA n 
2 98  ASP n 
2 99  VAL n 
2 100 SER n 
2 101 ILE n 
2 102 GLU n 
2 103 ASP n 
2 104 SER n 
2 105 VAL n 
2 106 ILE n 
2 107 SER n 
2 108 LEU n 
2 109 SER n 
2 110 GLY n 
2 111 ASP n 
2 112 HIS n 
2 113 CYS n 
2 114 ILE n 
2 115 ILE n 
2 116 GLY n 
2 117 ARG n 
2 118 THR n 
2 119 LEU n 
2 120 VAL n 
2 121 VAL n 
2 122 HIS n 
2 123 GLU n 
2 124 LYS n 
2 125 ALA n 
2 126 ASP n 
2 127 ASP n 
2 128 LEU n 
2 129 GLY n 
2 130 LYS n 
2 131 GLY n 
2 132 GLY n 
2 133 ASN n 
2 134 GLU n 
2 135 GLU n 
2 136 SER n 
2 137 THR n 
2 138 LYS n 
2 139 THR n 
2 140 GLY n 
2 141 ASN n 
2 142 ALA n 
2 143 GLY n 
2 144 SER n 
2 145 ARG n 
2 146 LEU n 
2 147 ALA n 
2 148 CYS n 
2 149 GLY n 
2 150 VAL n 
2 151 ILE n 
2 152 GLY n 
2 153 ILE n 
2 154 ALA n 
2 155 GLN n 
3 1   ALA n 
3 2   ALA n 
3 3   THR n 
3 4   LYS n 
3 5   ALA n 
3 6   VAL n 
3 7   CYS n 
3 8   VAL n 
3 9   LEU n 
3 10  LYS n 
3 11  GLY n 
3 12  ASP n 
3 13  GLY n 
3 14  PRO n 
3 15  VAL n 
3 16  GLN n 
3 17  GLY n 
3 18  ILE n 
3 19  ILE n 
3 20  ASN n 
3 21  PHE n 
3 22  GLU n 
3 23  GLN n 
3 24  LYS n 
3 25  GLU n 
3 26  SER n 
3 27  ASN n 
3 28  GLY n 
3 29  PRO n 
3 30  VAL n 
3 31  LYS n 
3 32  VAL n 
3 33  TRP n 
3 34  GLY n 
3 35  SER n 
3 36  ILE n 
3 37  LYS n 
3 38  GLY n 
3 39  LEU n 
3 40  THR n 
3 41  GLU n 
3 42  GLY n 
3 43  LEU n 
3 44  HIS n 
3 45  GLY n 
3 46  PHE n 
3 47  HIS n 
3 48  VAL n 
3 49  HIS n 
3 50  GLU n 
3 51  PHE n 
3 52  GLY n 
3 53  ASP n 
3 54  ASN n 
3 55  THR n 
3 56  ALA n 
3 57  GLY n 
3 58  CYS n 
3 59  THR n 
3 60  SER n 
3 61  ALA n 
3 62  GLY n 
3 63  PRO n 
3 64  HIS n 
3 65  PHE n 
3 66  ASN n 
3 67  PRO n 
3 68  LEU n 
3 69  SER n 
3 70  ARG n 
3 71  LYS n 
3 72  HIS n 
3 73  GLY n 
3 74  GLY n 
3 75  PRO n 
3 76  LYS n 
3 77  ASP n 
3 78  ALA n 
3 79  GLU n 
3 80  ARG n 
3 81  HIS n 
3 82  VAL n 
3 83  GLY n 
3 84  ASP n 
3 85  LEU n 
3 86  GLY n 
3 87  ASN n 
3 88  VAL n 
3 89  THR n 
3 90  ALA n 
3 91  ASP n 
3 92  LYS n 
3 93  ASP n 
3 94  GLY n 
3 95  VAL n 
3 96  ALA n 
3 97  ASP n 
3 98  VAL n 
3 99  SER n 
3 100 ILE n 
3 101 GLU n 
3 102 ASP n 
3 103 SER n 
3 104 VAL n 
3 105 ILE n 
3 106 SER n 
3 107 LEU n 
3 108 SER n 
3 109 GLY n 
3 110 ASP n 
3 111 HIS n 
3 112 CYS n 
3 113 ILE n 
3 114 ILE n 
3 115 GLY n 
3 116 ARG n 
3 117 THR n 
3 118 LEU n 
3 119 VAL n 
3 120 VAL n 
3 121 HIS n 
3 122 GLU n 
3 123 LYS n 
3 124 ALA n 
3 125 ASP n 
3 126 ASP n 
3 127 LEU n 
3 128 GLY n 
3 129 LYS n 
3 130 GLY n 
3 131 GLY n 
3 132 ASN n 
3 133 GLU n 
3 134 GLU n 
3 135 SER n 
3 136 THR n 
3 137 LYS n 
3 138 THR n 
3 139 GLY n 
3 140 ASN n 
3 141 ALA n 
3 142 GLY n 
3 143 SER n 
3 144 ARG n 
3 145 LEU n 
3 146 ALA n 
3 147 CYS n 
3 148 GLY n 
3 149 VAL n 
3 150 ILE n 
3 151 GLY n 
3 152 ILE n 
3 153 ALA n 
3 154 GLN n 
4 1   ALA n 
4 2   THR n 
4 3   LYS n 
4 4   ALA n 
4 5   VAL n 
4 6   CYS n 
4 7   VAL n 
4 8   LEU n 
4 9   LYS n 
4 10  GLY n 
4 11  ASP n 
4 12  GLY n 
4 13  PRO n 
4 14  VAL n 
4 15  GLN n 
4 16  GLY n 
4 17  ILE n 
4 18  ILE n 
4 19  ASN n 
4 20  PHE n 
4 21  GLU n 
4 22  GLN n 
4 23  LYS n 
4 24  GLU n 
4 25  SER n 
4 26  ASN n 
4 27  GLY n 
4 28  PRO n 
4 29  VAL n 
4 30  LYS n 
4 31  VAL n 
4 32  TRP n 
4 33  GLY n 
4 34  SER n 
4 35  ILE n 
4 36  LYS n 
4 37  GLY n 
4 38  LEU n 
4 39  THR n 
4 40  GLU n 
4 41  GLY n 
4 42  LEU n 
4 43  HIS n 
4 44  GLY n 
4 45  PHE n 
4 46  HIS n 
4 47  VAL n 
4 48  HIS n 
4 49  GLU n 
4 50  PHE n 
4 51  GLY n 
4 52  ASP n 
4 53  ASN n 
4 54  THR n 
4 55  ALA n 
4 56  GLY n 
4 57  CYS n 
4 58  THR n 
4 59  SER n 
4 60  ALA n 
4 61  GLY n 
4 62  PRO n 
4 63  HIS n 
4 64  PHE n 
4 65  ASN n 
4 66  PRO n 
4 67  LEU n 
4 68  SER n 
4 69  ARG n 
4 70  LYS n 
4 71  HIS n 
4 72  GLY n 
4 73  GLY n 
4 74  PRO n 
4 75  LYS n 
4 76  ASP n 
4 77  GLU n 
4 78  GLU n 
4 79  ARG n 
4 80  HIS n 
4 81  VAL n 
4 82  GLY n 
4 83  ASP n 
4 84  LEU n 
4 85  GLY n 
4 86  ASN n 
4 87  VAL n 
4 88  THR n 
4 89  ALA n 
4 90  ASP n 
4 91  LYS n 
4 92  ASP n 
4 93  GLY n 
4 94  VAL n 
4 95  ALA n 
4 96  ASP n 
4 97  VAL n 
4 98  SER n 
4 99  ILE n 
4 100 GLU n 
4 101 ASP n 
4 102 SER n 
4 103 VAL n 
4 104 ILE n 
4 105 SER n 
4 106 LEU n 
4 107 SER n 
4 108 GLY n 
4 109 ASP n 
4 110 HIS n 
4 111 CYS n 
4 112 ILE n 
4 113 ILE n 
4 114 GLY n 
4 115 ARG n 
4 116 THR n 
4 117 LEU n 
4 118 VAL n 
4 119 VAL n 
4 120 HIS n 
4 121 GLU n 
4 122 LYS n 
4 123 ALA n 
4 124 ASP n 
4 125 ASP n 
4 126 LEU n 
4 127 GLY n 
4 128 LYS n 
4 129 GLY n 
4 130 GLY n 
4 131 ASN n 
4 132 GLU n 
4 133 GLU n 
4 134 SER n 
4 135 THR n 
4 136 LYS n 
4 137 THR n 
4 138 GLY n 
4 139 ASN n 
4 140 ALA n 
4 141 GLY n 
4 142 SER n 
4 143 ARG n 
4 144 LEU n 
4 145 ALA n 
4 146 CYS n 
4 147 GLY n 
4 148 VAL n 
4 149 ILE n 
4 150 GLY n 
4 151 ILE n 
4 152 ALA n 
4 153 ALA 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' 1 154 human ? SOD1     ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? 'BL21(DE3)' ? ? ? ? ? ? ? plasmid ? ? ? pETM11 ? ? 
2 1 sample 'Biological sequence' 1 155 human ? SOD1     ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? 'BL21(DE3)' ? ? ? ? ? ? ? plasmid ? ? ? pETM11 ? ? 
3 1 sample 'Biological sequence' 1 154 human ? HEL-S-44 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? 'BL21(DE3)' ? ? ? ? ? ? ? plasmid ? ? ? pETM11 ? ? 
4 1 sample 'Biological sequence' 1 153 human ? HEL-S-44 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? 'BL21(DE3)' ? ? ? ? ? ? ? plasmid ? ? ? pETM11 ? ? 
# 
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 SODC_HUMAN   P00441 ? 1 
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
1 
2 UNP SODC_HUMAN   P00441 ? 2 
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
1 
3 UNP V9HWC9_HUMAN V9HWC9 ? 3 
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
2 
4 UNP V9HWC9_HUMAN V9HWC9 ? 4 
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIA
;
2 
# 
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 8GSQ A 1 ? 154 ? P00441 1 ? 154 ? 0 153 
2  1 8GSQ B 1 ? 154 ? P00441 1 ? 154 ? 0 153 
3  2 8GSQ C 2 ? 155 ? P00441 1 ? 154 ? 0 153 
4  1 8GSQ D 1 ? 154 ? P00441 1 ? 154 ? 0 153 
5  3 8GSQ E 2 ? 154 ? V9HWC9 2 ? 154 ? 1 153 
6  1 8GSQ F 1 ? 154 ? P00441 1 ? 154 ? 0 153 
7  3 8GSQ G 2 ? 154 ? V9HWC9 2 ? 154 ? 1 153 
8  4 8GSQ H 1 ? 152 ? V9HWC9 2 ? 153 ? 1 152 
9  1 8GSQ I 1 ? 154 ? P00441 1 ? 154 ? 0 153 
10 1 8GSQ J 1 ? 154 ? P00441 1 ? 154 ? 0 153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
3 8GSQ ALA C 1   ? UNP P00441 ?   ?  'expression tag' -1  1 
5 8GSQ ALA E 1   ? UNP V9HWC9 ?   ?  'expression tag' 0   2 
5 8GSQ ALA E 78  ? UNP V9HWC9 GLU 78 conflict         77  3 
7 8GSQ ALA G 1   ? UNP V9HWC9 ?   ?  'expression tag' 0   4 
7 8GSQ ALA G 78  ? UNP V9HWC9 GLU 78 conflict         77  5 
8 8GSQ ALA H 153 ? UNP V9HWC9 ?   ?  'expression tag' 153 6 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE ?                               'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                               'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE ?                               'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE ?                               'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE ?                               'C2 H5 N O2'      75.067  
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 
K4I non-polymer         . 
;(9~{R})-3-[2-[4-(6-fluoranyl-1,2-benzoxazol-3-yl)piperidin-1-yl]ethyl]-2-methyl-9-oxidanyl-6,7,8,9-tetrahydropyrido[1,2-a]pyrimidin-4-one
;
?                               'C23 H27 F N4 O3' 426.484 
LEU 'L-peptide linking' y LEUCINE ?                               'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE ?                               'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE ?                               'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE ?                               'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE ?                               'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                               'C11 H12 N2 O2'   204.225 
VAL 'L-peptide linking' y VALINE ?                               'C5 H11 N O2'     117.146 
ZN  non-polymer         . 'ZINC ION' ?                               'Zn 2'            65.409  
# 
_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                   8GSQ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.78 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          67.45 
_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              6.5 
_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    'Sodium Citrate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_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 PILATUS3 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-02-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9655 
_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                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9655 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          33.81 
_reflns.entry_id                                       8GSQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.04 
_reflns.d_resolution_low                               101.23 
_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                                     142935 
_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                           94.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.103 
_reflns.pdbx_Rpim_I_all                                0.040 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.095 
_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                                    2.040 
_reflns_shell.d_res_low                                     2.076 
_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                             7478 
_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                               6.4 
_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                               0.994 
_reflns_shell.pdbx_Rpim_I_all                               0.393 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.769 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.911 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8GSQ 
_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                            2.10 
_refine.ls_d_res_low                             95.39 
_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                     130482 
_refine.ls_number_reflns_R_free                  6508 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.01 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1760 
_refine.ls_R_factor_R_free                       0.2078 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1744 
_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                          1.35 
_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                      6a9o 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.14 
_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                            0.21 
_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                       2.10 
_refine_hist.d_res_low                        95.39 
_refine_hist.number_atoms_solvent             991 
_refine_hist.number_atoms_total               12030 
_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        10963 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         76 
_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' ? 0.007 ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.857 ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.363 ? 1611 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.059 ? 1679 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005 ? 2072 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.10 2.12  . . 238 4310 100.00 . . . . 0.2175 . . . . . . . . . . . 0.2417 
'X-RAY DIFFRACTION' 2.12 2.15  . . 212 4389 100.00 . . . . 0.2128 . . . . . . . . . . . 0.2661 
'X-RAY DIFFRACTION' 2.15 2.18  . . 237 4356 100.00 . . . . 0.2189 . . . . . . . . . . . 0.2477 
'X-RAY DIFFRACTION' 2.18 2.20  . . 250 4353 100.00 . . . . 0.2185 . . . . . . . . . . . 0.2623 
'X-RAY DIFFRACTION' 2.20 2.23  . . 202 4020 93.00  . . . . 0.2248 . . . . . . . . . . . 0.2925 
'X-RAY DIFFRACTION' 2.23 2.23  . . 0   16   5.00   . . . . 0.2799 . . . . . . . . . . . .      
'X-RAY DIFFRACTION' 2.26 2.29  . . 220 4044 99.00  . . . . 0.2141 . . . . . . . . . . . 0.2519 
'X-RAY DIFFRACTION' 2.29 2.33  . . 205 4372 100.00 . . . . 0.2105 . . . . . . . . . . . 0.2232 
'X-RAY DIFFRACTION' 2.33 2.37  . . 228 4399 100.00 . . . . 0.2172 . . . . . . . . . . . 0.2617 
'X-RAY DIFFRACTION' 2.37 2.40  . . 203 4395 100.00 . . . . 0.2219 . . . . . . . . . . . 0.2644 
'X-RAY DIFFRACTION' 2.40 2.45  . . 242 4318 100.00 . . . . 0.2285 . . . . . . . . . . . 0.2572 
'X-RAY DIFFRACTION' 2.45 2.49  . . 231 4396 100.00 . . . . 0.2260 . . . . . . . . . . . 0.2900 
'X-RAY DIFFRACTION' 2.49 2.54  . . 217 4378 100.00 . . . . 0.2151 . . . . . . . . . . . 0.2860 
'X-RAY DIFFRACTION' 2.54 2.59  . . 231 4392 100.00 . . . . 0.2113 . . . . . . . . . . . 0.2677 
'X-RAY DIFFRACTION' 2.59 2.65  . . 227 4233 98.00  . . . . 0.2183 . . . . . . . . . . . 0.2786 
'X-RAY DIFFRACTION' 2.65 2.71  . . 92  1650 38.00  . . . . 0.2294 . . . . . . . . . . . 0.2419 
'X-RAY DIFFRACTION' 2.71 2.78  . . 243 4387 100.00 . . . . 0.2226 . . . . . . . . . . . 0.2530 
'X-RAY DIFFRACTION' 2.78 2.85  . . 248 4335 100.00 . . . . 0.2269 . . . . . . . . . . . 0.2588 
'X-RAY DIFFRACTION' 2.85 2.93  . . 256 4369 100.00 . . . . 0.2332 . . . . . . . . . . . 0.2446 
'X-RAY DIFFRACTION' 2.93 3.03  . . 232 4406 100.00 . . . . 0.2087 . . . . . . . . . . . 0.2549 
'X-RAY DIFFRACTION' 3.03 3.14  . . 229 4371 100.00 . . . . 0.1838 . . . . . . . . . . . 0.2035 
'X-RAY DIFFRACTION' 3.14 3.26  . . 223 4421 100.00 . . . . 0.1703 . . . . . . . . . . . 0.2102 
'X-RAY DIFFRACTION' 3.26 3.41  . . 254 4384 100.00 . . . . 0.1652 . . . . . . . . . . . 0.1999 
'X-RAY DIFFRACTION' 3.41 3.59  . . 232 4407 100.00 . . . . 0.1628 . . . . . . . . . . . 0.1858 
'X-RAY DIFFRACTION' 3.59 3.82  . . 213 4438 100.00 . . . . 0.1550 . . . . . . . . . . . 0.1797 
'X-RAY DIFFRACTION' 3.82 4.11  . . 232 4405 100.00 . . . . 0.1317 . . . . . . . . . . . 0.1586 
'X-RAY DIFFRACTION' 4.11 4.52  . . 215 4459 100.00 . . . . 0.1215 . . . . . . . . . . . 0.1542 
'X-RAY DIFFRACTION' 4.52 5.18  . . 233 4455 100.00 . . . . 0.1275 . . . . . . . . . . . 0.1499 
'X-RAY DIFFRACTION' 5.18 6.52  . . 231 4494 100.00 . . . . 0.1520 . . . . . . . . . . . 0.1756 
'X-RAY DIFFRACTION' 6.52 95.39 . . 232 4622 99.00  . . . . 0.1611 . . . . . . . . . . . 0.1949 
# 
_struct.entry_id                     8GSQ 
_struct.title                        
;Structure based studies reveal an atypical antipsychotic drug candidate - Paliperidone as a potent hSOD1 modulator with implications in ALS treatment.
;
_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        8GSQ 
_struct_keywords.text            
'Superoxide Dismutase, ALS, antipsychotic, oxidation, oxidoreductase-inhibitor complex, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 1 ? 
C  N N 2 ? 
D  N N 1 ? 
E  N N 3 ? 
F  N N 1 ? 
G  N N 3 ? 
H  N N 4 ? 
I  N N 1 ? 
J  N N 1 ? 
K  N N 5 ? 
L  N N 6 ? 
M  N N 5 ? 
N  N N 6 ? 
O  N N 5 ? 
P  N N 6 ? 
Q  N N 5 ? 
R  N N 6 ? 
S  N N 5 ? 
T  N N 6 ? 
U  N N 5 ? 
V  N N 6 ? 
W  N N 5 ? 
X  N N 7 ? 
Y  N N 5 ? 
Z  N N 5 ? 
AA N N 8 ? 
BA N N 8 ? 
CA N N 8 ? 
DA N N 8 ? 
EA N N 8 ? 
FA N N 8 ? 
GA N N 8 ? 
HA N N 8 ? 
IA N N 8 ? 
JA N N 8 ? 
# 
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 ALA A 56  ? GLY A 62  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2  AA2 GLU A 134 ? GLY A 139 ? GLU A 133 GLY A 138 1 ? 6 
HELX_P HELX_P3  AA3 ALA B 56  ? GLY B 62  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P4  AA4 GLU B 134 ? GLY B 139 ? GLU B 133 GLY B 138 1 ? 6 
HELX_P HELX_P5  AA5 ALA C 57  ? GLY C 63  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P6  AA6 ASN C 133 ? GLY C 140 ? ASN C 131 GLY C 138 1 ? 8 
HELX_P HELX_P7  AA7 ALA D 56  ? GLY D 62  ? ALA D 55  GLY D 61  5 ? 7 
HELX_P HELX_P8  AA8 SER D 108 ? CYS D 112 ? SER D 107 CYS D 111 5 ? 5 
HELX_P HELX_P9  AA9 GLU D 134 ? GLY D 139 ? GLU D 133 GLY D 138 1 ? 6 
HELX_P HELX_P10 AB1 ALA E 56  ? GLY E 62  ? ALA E 55  GLY E 61  5 ? 7 
HELX_P HELX_P11 AB2 ASN E 132 ? THR E 138 ? ASN E 131 THR E 137 1 ? 7 
HELX_P HELX_P12 AB3 ALA F 56  ? GLY F 62  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P13 AB4 GLU F 134 ? GLY F 139 ? GLU F 133 GLY F 138 1 ? 6 
HELX_P HELX_P14 AB5 CYS G 58  ? GLY G 62  ? CYS G 57  GLY G 61  5 ? 5 
HELX_P HELX_P15 AB6 ALA H 55  ? GLY H 61  ? ALA H 55  GLY H 61  5 ? 7 
HELX_P HELX_P16 AB7 ASN H 131 ? GLY H 138 ? ASN H 131 GLY H 138 1 ? 8 
HELX_P HELX_P17 AB8 ALA I 56  ? GLY I 62  ? ALA I 55  GLY I 61  5 ? 7 
HELX_P HELX_P18 AB9 ALA J 56  ? GLY J 62  ? ALA J 55  GLY J 61  5 ? 7 
HELX_P HELX_P19 AC1 GLU J 134 ? GLY J 139 ? GLU J 133 GLY J 138 1 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 58 SG  ? ? ? 1_555 A CYS 147 SG ? ? A CYS 57 A CYS 146 1_555 ? ? ? ? ? ? ? 2.116 ? ? 
disulf2  disulf ? ? B CYS 58 SG  ? ? ? 1_555 B CYS 147 SG ? ? B CYS 57 B CYS 146 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
disulf3  disulf ? ? C CYS 59 SG  ? ? ? 1_555 C CYS 148 SG ? ? C CYS 57 C CYS 146 1_555 ? ? ? ? ? ? ? 2.110 ? ? 
disulf4  disulf ? ? D CYS 58 SG  ? ? ? 1_555 D CYS 147 SG ? ? D CYS 57 D CYS 146 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
disulf5  disulf ? ? E CYS 58 SG  ? ? ? 1_555 E CYS 147 SG ? ? E CYS 57 E CYS 146 1_555 ? ? ? ? ? ? ? 2.113 ? ? 
disulf6  disulf ? ? F CYS 58 SG  ? ? ? 1_555 F CYS 147 SG ? ? F CYS 57 F CYS 146 1_555 ? ? ? ? ? ? ? 2.113 ? ? 
disulf7  disulf ? ? G CYS 58 SG  ? ? ? 1_555 G CYS 147 SG ? ? G CYS 57 G CYS 146 1_555 ? ? ? ? ? ? ? 2.091 ? ? 
disulf8  disulf ? ? H CYS 57 SG  ? ? ? 1_555 H CYS 146 SG ? ? H CYS 57 H CYS 146 1_555 ? ? ? ? ? ? ? 2.076 ? ? 
disulf9  disulf ? ? I CYS 58 SG  ? ? ? 1_555 I CYS 147 SG ? ? I CYS 57 I CYS 146 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
disulf10 disulf ? ? J CYS 58 SG  ? ? ? 1_555 J CYS 147 SG ? ? J CYS 57 J CYS 146 1_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc1  metalc ? ? A HIS 64 ND1 ? ? ? 1_555 K ZN  .   ZN ? ? A HIS 63 A ZN  201 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc2  metalc ? ? A HIS 72 ND1 ? ? ? 1_555 K ZN  .   ZN ? ? A HIS 71 A ZN  201 1_555 ? ? ? ? ? ? ? 2.284 ? ? 
metalc3  metalc ? ? A HIS 81 ND1 ? ? ? 1_555 K ZN  .   ZN ? ? A HIS 80 A ZN  201 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc4  metalc ? ? A ASP 84 OD1 ? ? ? 1_555 K ZN  .   ZN ? ? A ASP 83 A ZN  201 1_555 ? ? ? ? ? ? ? 1.913 ? ? 
metalc5  metalc ? ? B HIS 64 ND1 ? ? ? 1_555 M ZN  .   ZN ? ? B HIS 63 B ZN  201 1_555 ? ? ? ? ? ? ? 2.075 ? ? 
metalc6  metalc ? ? B HIS 72 ND1 ? ? ? 1_555 M ZN  .   ZN ? ? B HIS 71 B ZN  201 1_555 ? ? ? ? ? ? ? 2.170 ? ? 
metalc7  metalc ? ? B HIS 81 ND1 ? ? ? 1_555 M ZN  .   ZN ? ? B HIS 80 B ZN  201 1_555 ? ? ? ? ? ? ? 2.125 ? ? 
metalc8  metalc ? ? B ASP 84 OD1 ? ? ? 1_555 M ZN  .   ZN ? ? B ASP 83 B ZN  201 1_555 ? ? ? ? ? ? ? 1.906 ? ? 
metalc9  metalc ? ? C HIS 65 ND1 ? ? ? 1_555 O ZN  .   ZN ? ? C HIS 63 C ZN  201 1_555 ? ? ? ? ? ? ? 2.270 ? ? 
metalc10 metalc ? ? C HIS 73 ND1 ? ? ? 1_555 O ZN  .   ZN ? ? C HIS 71 C ZN  201 1_555 ? ? ? ? ? ? ? 2.226 ? ? 
metalc11 metalc ? ? C HIS 82 ND1 ? ? ? 1_555 O ZN  .   ZN ? ? C HIS 80 C ZN  201 1_555 ? ? ? ? ? ? ? 1.967 ? ? 
metalc12 metalc ? ? C ASP 85 OD1 ? ? ? 1_555 O ZN  .   ZN ? ? C ASP 83 C ZN  201 1_555 ? ? ? ? ? ? ? 1.932 ? ? 
metalc13 metalc ? ? D HIS 64 ND1 ? ? ? 1_555 Q ZN  .   ZN ? ? D HIS 63 D ZN  201 1_555 ? ? ? ? ? ? ? 2.054 ? ? 
metalc14 metalc ? ? D HIS 72 ND1 ? ? ? 1_555 Q ZN  .   ZN ? ? D HIS 71 D ZN  201 1_555 ? ? ? ? ? ? ? 2.164 ? ? 
metalc15 metalc ? ? D HIS 81 ND1 ? ? ? 1_555 Q ZN  .   ZN ? ? D HIS 80 D ZN  201 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
metalc16 metalc ? ? D ASP 84 OD1 ? ? ? 1_555 Q ZN  .   ZN ? ? D ASP 83 D ZN  201 1_555 ? ? ? ? ? ? ? 1.939 ? ? 
metalc17 metalc ? ? E HIS 64 ND1 ? ? ? 1_555 S ZN  .   ZN ? ? E HIS 63 E ZN  201 1_555 ? ? ? ? ? ? ? 2.203 ? ? 
metalc18 metalc ? ? E HIS 72 ND1 ? ? ? 1_555 S ZN  .   ZN ? ? E HIS 71 E ZN  201 1_555 ? ? ? ? ? ? ? 2.437 ? ? 
metalc19 metalc ? ? E HIS 81 ND1 ? ? ? 1_555 S ZN  .   ZN ? ? E HIS 80 E ZN  201 1_555 ? ? ? ? ? ? ? 2.097 ? ? 
metalc20 metalc ? ? E ASP 84 OD1 ? ? ? 1_555 S ZN  .   ZN ? ? E ASP 83 E ZN  201 1_555 ? ? ? ? ? ? ? 2.005 ? ? 
metalc21 metalc ? ? F HIS 64 ND1 ? ? ? 1_555 U ZN  .   ZN ? ? F HIS 63 F ZN  201 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc22 metalc ? ? F HIS 72 ND1 ? ? ? 1_555 U ZN  .   ZN ? ? F HIS 71 F ZN  201 1_555 ? ? ? ? ? ? ? 2.141 ? ? 
metalc23 metalc ? ? F HIS 81 ND1 ? ? ? 1_555 U ZN  .   ZN ? ? F HIS 80 F ZN  201 1_555 ? ? ? ? ? ? ? 2.136 ? ? 
metalc24 metalc ? ? F ASP 84 OD1 ? ? ? 1_555 U ZN  .   ZN ? ? F ASP 83 F ZN  201 1_555 ? ? ? ? ? ? ? 1.981 ? ? 
metalc25 metalc ? ? H HIS 63 ND1 ? ? ? 1_555 W ZN  .   ZN ? ? H HIS 63 H ZN  201 1_555 ? ? ? ? ? ? ? 2.208 ? ? 
metalc26 metalc ? ? H HIS 71 ND1 ? ? ? 1_555 W ZN  .   ZN ? ? H HIS 71 H ZN  201 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc27 metalc ? ? H HIS 80 ND1 ? ? ? 1_555 W ZN  .   ZN ? ? H HIS 80 H ZN  201 1_555 ? ? ? ? ? ? ? 2.203 ? ? 
metalc28 metalc ? ? H ASP 83 OD1 ? ? ? 1_555 W ZN  .   ZN ? ? H ASP 83 H ZN  201 1_555 ? ? ? ? ? ? ? 1.871 ? ? 
metalc29 metalc ? ? I HIS 64 ND1 ? ? ? 1_555 Y ZN  .   ZN ? ? I HIS 63 I ZN  201 1_555 ? ? ? ? ? ? ? 2.108 ? ? 
metalc30 metalc ? ? I HIS 72 ND1 ? ? ? 1_555 Y ZN  .   ZN ? ? I HIS 71 I ZN  201 1_555 ? ? ? ? ? ? ? 2.252 ? ? 
metalc31 metalc ? ? I HIS 81 ND1 ? ? ? 1_555 Y ZN  .   ZN ? ? I HIS 80 I ZN  201 1_555 ? ? ? ? ? ? ? 2.224 ? ? 
metalc32 metalc ? ? I ASP 84 OD1 ? ? ? 1_555 Y ZN  .   ZN ? ? I ASP 83 I ZN  201 1_555 ? ? ? ? ? ? ? 1.964 ? ? 
metalc33 metalc ? ? J HIS 64 ND1 ? ? ? 1_555 Z ZN  .   ZN ? ? J HIS 63 J ZN  201 1_555 ? ? ? ? ? ? ? 2.159 ? ? 
metalc34 metalc ? ? J HIS 72 ND1 ? ? ? 1_555 Z ZN  .   ZN ? ? J HIS 71 J ZN  201 1_555 ? ? ? ? ? ? ? 2.102 ? ? 
metalc35 metalc ? ? J HIS 81 ND1 ? ? ? 1_555 Z ZN  .   ZN ? ? J HIS 80 J ZN  201 1_555 ? ? ? ? ? ? ? 2.176 ? ? 
metalc36 metalc ? ? J ASP 84 OD1 ? ? ? 1_555 Z ZN  .   ZN ? ? J ASP 83 J ZN  201 1_555 ? ? ? ? ? ? ? 1.811 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 5 ? 
AA4 ? 4 ? 
AA5 ? 5 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 4 ? 
AA9 ? 5 ? 
AB1 ? 4 ? 
AB2 ? 5 ? 
AB3 ? 4 ? 
AB4 ? 5 ? 
AB5 ? 4 ? 
AB6 ? 5 ? 
AB7 ? 4 ? 
AB8 ? 5 ? 
AB9 ? 4 ? 
AC1 ? 5 ? 
AC2 ? 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 
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 
AA3 4 5 ? 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 
AA5 4 5 ? 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 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? 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 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? 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 
AB8 4 5 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC1 4 5 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 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 ALA A 96  ? ASP A 102 ? ALA A 95  ASP A 101 
AA1 2 VAL A 30  ? LYS A 37  ? VAL A 29  LYS A 36  
AA1 3 GLN A 16  ? GLU A 22  ? GLN A 15  GLU A 21  
AA1 4 LYS A 4   ? LEU A 9   ? LYS A 3   LEU A 8   
AA1 5 GLY A 151 ? ILE A 152 ? GLY A 150 ILE A 151 
AA2 1 ASP A 84  ? ALA A 90  ? ASP A 83  ALA A 89  
AA2 2 GLY A 42  ? HIS A 49  ? GLY A 41  HIS A 48  
AA2 3 THR A 117 ? HIS A 121 ? THR A 116 HIS A 120 
AA2 4 ARG A 144 ? VAL A 149 ? ARG A 143 VAL A 148 
AA3 1 ALA B 96  ? ASP B 102 ? ALA B 95  ASP B 101 
AA3 2 VAL B 30  ? LYS B 37  ? VAL B 29  LYS B 36  
AA3 3 GLN B 16  ? GLU B 22  ? GLN B 15  GLU B 21  
AA3 4 LYS B 4   ? LEU B 9   ? LYS B 3   LEU B 8   
AA3 5 GLY B 151 ? ILE B 152 ? GLY B 150 ILE B 151 
AA4 1 ASP B 84  ? ALA B 90  ? ASP B 83  ALA B 89  
AA4 2 GLY B 42  ? HIS B 49  ? GLY B 41  HIS B 48  
AA4 3 THR B 117 ? HIS B 121 ? THR B 116 HIS B 120 
AA4 4 ARG B 144 ? VAL B 149 ? ARG B 143 VAL B 148 
AA5 1 ALA C 97  ? ASP C 103 ? ALA C 95  ASP C 101 
AA5 2 VAL C 31  ? LYS C 38  ? VAL C 29  LYS C 36  
AA5 3 GLN C 17  ? GLU C 23  ? GLN C 15  GLU C 21  
AA5 4 LYS C 5   ? LEU C 10  ? LYS C 3   LEU C 8   
AA5 5 GLY C 152 ? ILE C 153 ? GLY C 150 ILE C 151 
AA6 1 ASP C 85  ? ALA C 91  ? ASP C 83  ALA C 89  
AA6 2 GLY C 43  ? HIS C 50  ? GLY C 41  HIS C 48  
AA6 3 THR C 118 ? HIS C 122 ? THR C 116 HIS C 120 
AA6 4 ARG C 145 ? VAL C 150 ? ARG C 143 VAL C 148 
AA7 1 ALA D 96  ? ASP D 102 ? ALA D 95  ASP D 101 
AA7 2 VAL D 30  ? LYS D 37  ? VAL D 29  LYS D 36  
AA7 3 GLN D 16  ? GLU D 22  ? GLN D 15  GLU D 21  
AA7 4 LYS D 4   ? LEU D 9   ? LYS D 3   LEU D 8   
AA7 5 GLY D 151 ? ILE D 152 ? GLY D 150 ILE D 151 
AA8 1 ASP D 84  ? ALA D 90  ? ASP D 83  ALA D 89  
AA8 2 GLY D 42  ? HIS D 49  ? GLY D 41  HIS D 48  
AA8 3 THR D 117 ? HIS D 121 ? THR D 116 HIS D 120 
AA8 4 ARG D 144 ? VAL D 149 ? ARG D 143 VAL D 148 
AA9 1 ALA E 96  ? ASP E 102 ? ALA E 95  ASP E 101 
AA9 2 VAL E 30  ? LYS E 37  ? VAL E 29  LYS E 36  
AA9 3 GLN E 16  ? GLU E 22  ? GLN E 15  GLU E 21  
AA9 4 LYS E 4   ? LEU E 9   ? LYS E 3   LEU E 8   
AA9 5 GLY E 151 ? ILE E 152 ? GLY E 150 ILE E 151 
AB1 1 ASP E 84  ? ALA E 90  ? ASP E 83  ALA E 89  
AB1 2 GLY E 42  ? HIS E 49  ? GLY E 41  HIS E 48  
AB1 3 THR E 117 ? HIS E 121 ? THR E 116 HIS E 120 
AB1 4 ARG E 144 ? VAL E 149 ? ARG E 143 VAL E 148 
AB2 1 ALA F 96  ? ASP F 102 ? ALA F 95  ASP F 101 
AB2 2 VAL F 30  ? LYS F 37  ? VAL F 29  LYS F 36  
AB2 3 GLN F 16  ? GLU F 22  ? GLN F 15  GLU F 21  
AB2 4 LYS F 4   ? LEU F 9   ? LYS F 3   LEU F 8   
AB2 5 GLY F 151 ? ILE F 152 ? GLY F 150 ILE F 151 
AB3 1 ASP F 84  ? ALA F 90  ? ASP F 83  ALA F 89  
AB3 2 GLY F 42  ? HIS F 49  ? GLY F 41  HIS F 48  
AB3 3 THR F 117 ? HIS F 121 ? THR F 116 HIS F 120 
AB3 4 ARG F 144 ? VAL F 149 ? ARG F 143 VAL F 148 
AB4 1 ALA G 96  ? ASP G 102 ? ALA G 95  ASP G 101 
AB4 2 VAL G 30  ? LYS G 37  ? VAL G 29  LYS G 36  
AB4 3 GLN G 16  ? GLU G 22  ? GLN G 15  GLU G 21  
AB4 4 LYS G 4   ? LEU G 9   ? LYS G 3   LEU G 8   
AB4 5 GLY G 151 ? ILE G 152 ? GLY G 150 ILE G 151 
AB5 1 ASP G 84  ? ALA G 90  ? ASP G 83  ALA G 89  
AB5 2 GLY G 42  ? HIS G 49  ? GLY G 41  HIS G 48  
AB5 3 THR G 117 ? HIS G 121 ? THR G 116 HIS G 120 
AB5 4 ARG G 144 ? VAL G 149 ? ARG G 143 VAL G 148 
AB6 1 ALA H 95  ? ASP H 101 ? ALA H 95  ASP H 101 
AB6 2 VAL H 29  ? LYS H 36  ? VAL H 29  LYS H 36  
AB6 3 GLN H 15  ? GLN H 22  ? GLN H 15  GLN H 22  
AB6 4 LYS H 3   ? LEU H 8   ? LYS H 3   LEU H 8   
AB6 5 GLY H 150 ? ILE H 151 ? GLY H 150 ILE H 151 
AB7 1 ASP H 83  ? ALA H 89  ? ASP H 83  ALA H 89  
AB7 2 GLY H 41  ? HIS H 48  ? GLY H 41  HIS H 48  
AB7 3 THR H 116 ? HIS H 120 ? THR H 116 HIS H 120 
AB7 4 ARG H 143 ? VAL H 148 ? ARG H 143 VAL H 148 
AB8 1 ALA I 96  ? ASP I 102 ? ALA I 95  ASP I 101 
AB8 2 VAL I 30  ? LYS I 37  ? VAL I 29  LYS I 36  
AB8 3 GLN I 16  ? GLU I 22  ? GLN I 15  GLU I 21  
AB8 4 LYS I 4   ? LEU I 9   ? LYS I 3   LEU I 8   
AB8 5 GLY I 151 ? ILE I 152 ? GLY I 150 ILE I 151 
AB9 1 ASP I 84  ? ALA I 90  ? ASP I 83  ALA I 89  
AB9 2 GLY I 42  ? HIS I 49  ? GLY I 41  HIS I 48  
AB9 3 THR I 117 ? HIS I 121 ? THR I 116 HIS I 120 
AB9 4 ARG I 144 ? VAL I 149 ? ARG I 143 VAL I 148 
AC1 1 ALA J 96  ? ASP J 102 ? ALA J 95  ASP J 101 
AC1 2 VAL J 30  ? LYS J 37  ? VAL J 29  LYS J 36  
AC1 3 GLN J 16  ? GLU J 22  ? GLN J 15  GLU J 21  
AC1 4 LYS J 4   ? LYS J 10  ? LYS J 3   LYS J 9   
AC1 5 GLY J 151 ? ILE J 152 ? GLY J 150 ILE J 151 
AC2 1 ASP J 84  ? ALA J 90  ? ASP J 83  ALA J 89  
AC2 2 GLY J 42  ? HIS J 49  ? GLY J 41  HIS J 48  
AC2 3 THR J 117 ? HIS J 121 ? THR J 116 HIS J 120 
AC2 4 ARG J 144 ? VAL J 149 ? ARG J 143 VAL J 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ASP A 102 ? O ASP A 101 N VAL A 30  ? N VAL A 29  
AA1 2 3 O TRP A 33  ? O TRP A 32  N ASN A 20  ? N ASN A 19  
AA1 3 4 O GLY A 17  ? O GLY A 16  N LEU A 9   ? N LEU A 8   
AA1 4 5 N VAL A 6   ? N VAL A 5   O GLY A 151 ? O GLY A 150 
AA2 1 2 O ALA A 90  ? O ALA A 89  N GLY A 42  ? N GLY A 41  
AA2 2 3 N HIS A 49  ? N HIS A 48  O THR A 117 ? O THR A 116 
AA2 3 4 N VAL A 120 ? N VAL A 119 O ALA A 146 ? O ALA A 145 
AA3 1 2 O ILE B 100 ? O ILE B 99  N VAL B 32  ? N VAL B 31  
AA3 2 3 O LYS B 37  ? O LYS B 36  N GLN B 16  ? N GLN B 15  
AA3 3 4 O PHE B 21  ? O PHE B 20  N ALA B 5   ? N ALA B 4   
AA3 4 5 N VAL B 6   ? N VAL B 5   O GLY B 151 ? O GLY B 150 
AA4 1 2 O ALA B 90  ? O ALA B 89  N GLY B 42  ? N GLY B 41  
AA4 2 3 N HIS B 49  ? N HIS B 48  O THR B 117 ? O THR B 116 
AA4 3 4 N VAL B 120 ? N VAL B 119 O ALA B 146 ? O ALA B 145 
AA5 1 2 O ASP C 103 ? O ASP C 101 N VAL C 31  ? N VAL C 29  
AA5 2 3 O TRP C 34  ? O TRP C 32  N ASN C 21  ? N ASN C 19  
AA5 3 4 O PHE C 22  ? O PHE C 20  N ALA C 6   ? N ALA C 4   
AA5 4 5 N VAL C 7   ? N VAL C 5   O GLY C 152 ? O GLY C 150 
AA6 1 2 O ALA C 91  ? O ALA C 89  N GLY C 43  ? N GLY C 41  
AA6 2 3 N HIS C 50  ? N HIS C 48  O THR C 118 ? O THR C 116 
AA6 3 4 N LEU C 119 ? N LEU C 117 O GLY C 149 ? O GLY C 147 
AA7 1 2 O ASP D 102 ? O ASP D 101 N VAL D 30  ? N VAL D 29  
AA7 2 3 O TRP D 33  ? O TRP D 32  N ASN D 20  ? N ASN D 19  
AA7 3 4 O GLY D 17  ? O GLY D 16  N LEU D 9   ? N LEU D 8   
AA7 4 5 N VAL D 6   ? N VAL D 5   O GLY D 151 ? O GLY D 150 
AA8 1 2 O ALA D 90  ? O ALA D 89  N GLY D 42  ? N GLY D 41  
AA8 2 3 N HIS D 49  ? N HIS D 48  O THR D 117 ? O THR D 116 
AA8 3 4 N LEU D 118 ? N LEU D 117 O GLY D 148 ? O GLY D 147 
AA9 1 2 O ASP E 102 ? O ASP E 101 N VAL E 30  ? N VAL E 29  
AA9 2 3 O TRP E 33  ? O TRP E 32  N ASN E 20  ? N ASN E 19  
AA9 3 4 O GLY E 17  ? O GLY E 16  N LEU E 9   ? N LEU E 8   
AA9 4 5 N VAL E 6   ? N VAL E 5   O GLY E 151 ? O GLY E 150 
AB1 1 2 O ALA E 90  ? O ALA E 89  N GLY E 42  ? N GLY E 41  
AB1 2 3 N HIS E 49  ? N HIS E 48  O THR E 117 ? O THR E 116 
AB1 3 4 N LEU E 118 ? N LEU E 117 O GLY E 148 ? O GLY E 147 
AB2 1 2 O ILE F 100 ? O ILE F 99  N VAL F 32  ? N VAL F 31  
AB2 2 3 O TRP F 33  ? O TRP F 32  N ASN F 20  ? N ASN F 19  
AB2 3 4 O PHE F 21  ? O PHE F 20  N ALA F 5   ? N ALA F 4   
AB2 4 5 N VAL F 6   ? N VAL F 5   O GLY F 151 ? O GLY F 150 
AB3 1 2 O ALA F 90  ? O ALA F 89  N GLY F 42  ? N GLY F 41  
AB3 2 3 N HIS F 49  ? N HIS F 48  O THR F 117 ? O THR F 116 
AB3 3 4 N VAL F 120 ? N VAL F 119 O ALA F 146 ? O ALA F 145 
AB4 1 2 O ASP G 102 ? O ASP G 101 N VAL G 30  ? N VAL G 29  
AB4 2 3 O TRP G 33  ? O TRP G 32  N ASN G 20  ? N ASN G 19  
AB4 3 4 O GLY G 17  ? O GLY G 16  N LEU G 9   ? N LEU G 8   
AB4 4 5 N VAL G 6   ? N VAL G 5   O GLY G 151 ? O GLY G 150 
AB5 1 2 O ALA G 90  ? O ALA G 89  N GLY G 42  ? N GLY G 41  
AB5 2 3 N HIS G 49  ? N HIS G 48  O THR G 117 ? O THR G 116 
AB5 3 4 N LEU G 118 ? N LEU G 117 O GLY G 148 ? O GLY G 147 
AB6 1 2 O ASP H 101 ? O ASP H 101 N VAL H 29  ? N VAL H 29  
AB6 2 3 O TRP H 32  ? O TRP H 32  N ASN H 19  ? N ASN H 19  
AB6 3 4 O PHE H 20  ? O PHE H 20  N ALA H 4   ? N ALA H 4   
AB6 4 5 N VAL H 5   ? N VAL H 5   O GLY H 150 ? O GLY H 150 
AB7 1 2 O VAL H 87  ? O VAL H 87  N HIS H 43  ? N HIS H 43  
AB7 2 3 N HIS H 48  ? N HIS H 48  O THR H 116 ? O THR H 116 
AB7 3 4 N VAL H 119 ? N VAL H 119 O ALA H 145 ? O ALA H 145 
AB8 1 2 O ASP I 102 ? O ASP I 101 N VAL I 30  ? N VAL I 29  
AB8 2 3 O TRP I 33  ? O TRP I 32  N ASN I 20  ? N ASN I 19  
AB8 3 4 O GLY I 17  ? O GLY I 16  N LEU I 9   ? N LEU I 8   
AB8 4 5 N VAL I 6   ? N VAL I 5   O GLY I 151 ? O GLY I 150 
AB9 1 2 O ALA I 90  ? O ALA I 89  N GLY I 42  ? N GLY I 41  
AB9 2 3 N HIS I 49  ? N HIS I 48  O THR I 117 ? O THR I 116 
AB9 3 4 N LEU I 118 ? N LEU I 117 O GLY I 148 ? O GLY I 147 
AC1 1 2 O ASP J 102 ? O ASP J 101 N VAL J 30  ? N VAL J 29  
AC1 2 3 O TRP J 33  ? O TRP J 32  N ASN J 20  ? N ASN J 19  
AC1 3 4 O GLY J 17  ? O GLY J 16  N LEU J 9   ? N LEU J 8   
AC1 4 5 N VAL J 6   ? N VAL J 5   O GLY J 151 ? O GLY J 150 
AC2 1 2 O ALA J 90  ? O ALA J 89  N GLY J 42  ? N GLY J 41  
AC2 2 3 N HIS J 49  ? N HIS J 48  O THR J 117 ? O THR J 116 
AC2 3 4 N LEU J 118 ? N LEU J 117 O GLY J 148 ? O GLY J 147 
# 
_atom_sites.entry_id                    8GSQ 
_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.fract_transf_matrix[1][1]   0.006105 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.004939 
_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]   0.006945 
_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.
;
? 
F  ? ? 4.90428  4.07044 ? ? 12.99538 1.63651  ? ? 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.
;
? 
ZN ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 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   . MET A  1 1   ? 31.583  246.151 33.936 1.00 58.46 ?  0   MET A N   1 
ATOM   2     C  CA  . MET A  1 1   ? 30.574  245.605 33.015 1.00 63.35 ?  0   MET A CA  1 
ATOM   3     C  C   . MET A  1 1   ? 31.165  245.200 31.640 1.00 67.21 ?  0   MET A C   1 
ATOM   4     O  O   . MET A  1 1   ? 31.880  244.191 31.538 1.00 64.63 ?  0   MET A O   1 
ATOM   5     C  CB  . MET A  1 1   ? 29.431  246.618 32.826 1.00 55.13 ?  0   MET A CB  1 
ATOM   6     N  N   . ALA A  1 2   ? 30.859  245.983 30.595 1.00 62.99 ?  1   ALA A N   1 
ATOM   7     C  CA  . ALA A  1 2   ? 31.316  245.684 29.238 1.00 53.00 ?  1   ALA A CA  1 
ATOM   8     C  C   . ALA A  1 2   ? 32.799  246.001 29.079 1.00 43.42 ?  1   ALA A C   1 
ATOM   9     O  O   . ALA A  1 2   ? 33.279  247.023 29.570 1.00 46.13 ?  1   ALA A O   1 
ATOM   10    C  CB  . ALA A  1 2   ? 30.500  246.481 28.218 1.00 45.64 ?  1   ALA A CB  1 
ATOM   11    N  N   . THR A  1 3   ? 33.534  245.121 28.392 1.00 37.64 ?  2   THR A N   1 
ATOM   12    C  CA  . THR A  1 3   ? 34.971  245.316 28.244 1.00 39.41 ?  2   THR A CA  1 
ATOM   13    C  C   . THR A  1 3   ? 35.406  245.563 26.810 1.00 39.27 ?  2   THR A C   1 
ATOM   14    O  O   . THR A  1 3   ? 36.567  245.922 26.589 1.00 36.55 ?  2   THR A O   1 
ATOM   15    C  CB  . THR A  1 3   ? 35.761  244.113 28.787 1.00 40.72 ?  2   THR A CB  1 
ATOM   16    O  OG1 . THR A  1 3   ? 35.612  242.988 27.904 1.00 42.00 ?  2   THR A OG1 1 
ATOM   17    C  CG2 . THR A  1 3   ? 35.315  243.754 30.214 1.00 45.68 ?  2   THR A CG2 1 
ATOM   18    N  N   . LYS A  1 4   ? 34.522  245.370 25.843 1.00 35.90 ?  3   LYS A N   1 
ATOM   19    C  CA  . LYS A  1 4   ? 34.844  245.523 24.436 1.00 36.86 ?  3   LYS A CA  1 
ATOM   20    C  C   . LYS A  1 4   ? 33.686  246.219 23.740 1.00 32.73 ?  3   LYS A C   1 
ATOM   21    O  O   . LYS A  1 4   ? 32.519  245.913 23.995 1.00 30.72 ?  3   LYS A O   1 
ATOM   22    C  CB  . LYS A  1 4   ? 35.119  244.159 23.784 1.00 42.48 ?  3   LYS A CB  1 
ATOM   23    C  CG  . LYS A  1 4   ? 36.605  243.823 23.646 1.00 50.43 ?  3   LYS A CG  1 
ATOM   24    C  CD  . LYS A  1 4   ? 36.854  242.725 22.610 1.00 56.34 ?  3   LYS A CD  1 
ATOM   25    C  CE  . LYS A  1 4   ? 36.867  243.295 21.190 1.00 58.61 ?  3   LYS A CE  1 
ATOM   26    N  NZ  . LYS A  1 4   ? 38.262  243.452 20.645 1.00 66.75 ?  3   LYS A NZ  1 
ATOM   27    N  N   . ALA A  1 5   ? 34.008  247.159 22.864 1.00 30.42 ?  4   ALA A N   1 
ATOM   28    C  CA  . ALA A  1 5   ? 33.004  247.846 22.073 1.00 28.05 ?  4   ALA A CA  1 
ATOM   29    C  C   . ALA A  1 5   ? 33.569  248.055 20.681 1.00 30.98 ?  4   ALA A C   1 
ATOM   30    O  O   . ALA A  1 5   ? 34.766  247.888 20.443 1.00 29.84 ?  4   ALA A O   1 
ATOM   31    C  CB  . ALA A  1 5   ? 32.598  249.185 22.702 1.00 27.74 ?  4   ALA A CB  1 
ATOM   32    N  N   . VAL A  1 6   ? 32.693  248.433 19.751 1.00 30.00 ?  5   VAL A N   1 
ATOM   33    C  CA  . VAL A  1 6   ? 33.075  248.606 18.362 1.00 30.36 ?  5   VAL A CA  1 
ATOM   34    C  C   . VAL A  1 6   ? 32.137  249.625 17.738 1.00 31.24 ?  5   VAL A C   1 
ATOM   35    O  O   . VAL A  1 6   ? 31.010  249.835 18.199 1.00 30.14 ?  5   VAL A O   1 
ATOM   36    C  CB  . VAL A  1 6   ? 33.040  247.271 17.585 1.00 33.47 ?  5   VAL A CB  1 
ATOM   37    C  CG1 . VAL A  1 6   ? 31.607  246.792 17.443 1.00 29.20 ?  5   VAL A CG1 1 
ATOM   38    C  CG2 . VAL A  1 6   ? 33.689  247.451 16.228 1.00 26.21 ?  5   VAL A CG2 1 
ATOM   39    N  N   . CYS A  1 7   ? 32.617  250.278 16.690 1.00 29.13 ?  6   CYS A N   1 
ATOM   40    C  CA  . CYS A  1 7   ? 31.864  251.332 16.039 1.00 27.22 ?  6   CYS A CA  1 
ATOM   41    C  C   . CYS A  1 7   ? 32.196  251.305 14.552 1.00 29.88 ?  6   CYS A C   1 
ATOM   42    O  O   . CYS A  1 7   ? 33.371  251.279 14.185 1.00 30.42 ?  6   CYS A O   1 
ATOM   43    C  CB  . CYS A  1 7   ? 32.209  252.690 16.664 1.00 28.98 ?  6   CYS A CB  1 
ATOM   44    S  SG  . CYS A  1 7   ? 31.262  254.056 15.942 1.00 33.03 ?  6   CYS A SG  1 
ATOM   45    N  N   . VAL A  1 8   ? 31.171  251.287 13.705 1.00 29.92 ?  7   VAL A N   1 
ATOM   46    C  CA  . VAL A  1 8   ? 31.347  251.340 12.256 1.00 27.64 ?  7   VAL A CA  1 
ATOM   47    C  C   . VAL A  1 8   ? 31.001  252.757 11.818 1.00 31.13 ?  7   VAL A C   1 
ATOM   48    O  O   . VAL A  1 8   ? 29.858  253.204 11.982 1.00 32.78 ?  7   VAL A O   1 
ATOM   49    C  CB  . VAL A  1 8   ? 30.477  250.290 11.537 1.00 27.84 ?  7   VAL A CB  1 
ATOM   50    C  CG1 . VAL A  1 8   ? 30.600  250.403 9.990  1.00 30.44 ?  7   VAL A CG1 1 
ATOM   51    C  CG2 . VAL A  1 8   ? 30.870  248.910 11.964 1.00 28.86 ?  7   VAL A CG2 1 
ATOM   52    N  N   . LEU A  1 9   ? 31.995  253.479 11.296 1.00 31.07 ?  8   LEU A N   1 
ATOM   53    C  CA  . LEU A  1 9   ? 31.804  254.862 10.871 1.00 31.58 ?  8   LEU A CA  1 
ATOM   54    C  C   . LEU A  1 9   ? 31.399  254.913 9.410  1.00 33.03 ?  8   LEU A C   1 
ATOM   55    O  O   . LEU A  1 9   ? 32.093  254.356 8.553  1.00 31.40 ?  8   LEU A O   1 
ATOM   56    C  CB  . LEU A  1 9   ? 33.083  255.680 11.064 1.00 33.83 ?  8   LEU A CB  1 
ATOM   57    C  CG  . LEU A  1 9   ? 33.627  255.735 12.484 1.00 33.59 ?  8   LEU A CG  1 
ATOM   58    C  CD1 . LEU A  1 9   ? 35.020  256.281 12.448 1.00 38.47 ?  8   LEU A CD1 1 
ATOM   59    C  CD2 . LEU A  1 9   ? 32.753  256.646 13.282 1.00 31.95 ?  8   LEU A CD2 1 
ATOM   60    N  N   . LYS A  1 10  ? 30.297  255.601 9.130  1.00 33.43 ?  9   LYS A N   1 
ATOM   61    C  CA  . LYS A  1 10  ? 29.839  255.825 7.767  1.00 36.47 ?  9   LYS A CA  1 
ATOM   62    C  C   . LYS A  1 10  ? 29.324  257.246 7.665  1.00 34.55 ?  9   LYS A C   1 
ATOM   63    O  O   . LYS A  1 10  ? 28.958  257.870 8.664  1.00 30.50 ?  9   LYS A O   1 
ATOM   64    C  CB  . LYS A  1 10  ? 28.717  254.859 7.350  1.00 37.40 ?  9   LYS A CB  1 
ATOM   65    C  CG  . LYS A  1 10  ? 29.046  253.395 7.464  1.00 42.01 ?  9   LYS A CG  1 
ATOM   66    C  CD  . LYS A  1 10  ? 27.829  252.566 7.012  1.00 56.04 ?  9   LYS A CD  1 
ATOM   67    C  CE  . LYS A  1 10  ? 27.892  251.094 7.476  1.00 59.48 ?  9   LYS A CE  1 
ATOM   68    N  NZ  . LYS A  1 10  ? 29.075  250.357 6.933  1.00 58.86 ?  9   LYS A NZ  1 
ATOM   69    N  N   . GLY A  1 11  ? 29.280  257.745 6.439  1.00 33.89 ?  10  GLY A N   1 
ATOM   70    C  CA  . GLY A  1 11  ? 28.802  259.085 6.192  1.00 35.18 ?  10  GLY A CA  1 
ATOM   71    C  C   . GLY A  1 11  ? 28.350  259.233 4.757  1.00 39.12 ?  10  GLY A C   1 
ATOM   72    O  O   . GLY A  1 11  ? 28.254  258.256 4.011  1.00 41.88 ?  10  GLY A O   1 
ATOM   73    N  N   . ASP A  1 12  ? 28.090  260.481 4.371  1.00 44.07 ?  11  ASP A N   1 
ATOM   74    C  CA  . ASP A  1 12  ? 27.627  260.754 3.016  1.00 46.93 ?  11  ASP A CA  1 
ATOM   75    C  C   . ASP A  1 12  ? 28.743  260.703 1.986  1.00 46.12 ?  11  ASP A C   1 
ATOM   76    O  O   . ASP A  1 12  ? 28.459  260.522 0.799  1.00 52.44 ?  11  ASP A O   1 
ATOM   77    C  CB  . ASP A  1 12  ? 26.941  262.116 2.962  1.00 42.62 ?  11  ASP A CB  1 
ATOM   78    C  CG  . ASP A  1 12  ? 25.687  262.157 3.803  1.00 58.20 ?  11  ASP A CG  1 
ATOM   79    O  OD1 . ASP A  1 12  ? 24.947  261.146 3.804  1.00 61.88 ?  11  ASP A OD1 1 
ATOM   80    O  OD2 . ASP A  1 12  ? 25.454  263.184 4.477  1.00 65.57 ?  11  ASP A OD2 1 
ATOM   81    N  N   . GLY A  1 13  ? 29.994  260.856 2.400  1.00 40.47 ?  12  GLY A N   1 
ATOM   82    C  CA  . GLY A  1 13  ? 31.098  260.834 1.472  1.00 39.72 ?  12  GLY A CA  1 
ATOM   83    C  C   . GLY A  1 13  ? 31.831  259.518 1.559  1.00 38.86 ?  12  GLY A C   1 
ATOM   84    O  O   . GLY A  1 13  ? 31.262  258.493 1.935  1.00 38.72 ?  12  GLY A O   1 
ATOM   85    N  N   . PRO A  1 14  ? 33.123  259.528 1.234  1.00 36.56 ?  13  PRO A N   1 
ATOM   86    C  CA  . PRO A  1 14  ? 33.918  258.293 1.231  1.00 37.58 ?  13  PRO A CA  1 
ATOM   87    C  C   . PRO A  1 14  ? 34.525  257.900 2.568  1.00 35.65 ?  13  PRO A C   1 
ATOM   88    O  O   . PRO A  1 14  ? 35.233  256.890 2.616  1.00 33.28 ?  13  PRO A O   1 
ATOM   89    C  CB  . PRO A  1 14  ? 35.035  258.630 0.239  1.00 36.60 ?  13  PRO A CB  1 
ATOM   90    C  CG  . PRO A  1 14  ? 35.249  260.092 0.439  1.00 32.76 ?  13  PRO A CG  1 
ATOM   91    C  CD  . PRO A  1 14  ? 33.902  260.696 0.786  1.00 36.95 ?  13  PRO A CD  1 
ATOM   92    N  N   . VAL A  1 15  ? 34.314  258.656 3.640  1.00 32.42 ?  14  VAL A N   1 
ATOM   93    C  CA  . VAL A  1 15  ? 34.944  258.308 4.907  1.00 33.63 ?  14  VAL A CA  1 
ATOM   94    C  C   . VAL A  1 15  ? 34.218  257.113 5.507  1.00 34.57 ?  14  VAL A C   1 
ATOM   95    O  O   . VAL A  1 15  ? 32.994  257.134 5.665  1.00 35.40 ?  14  VAL A O   1 
ATOM   96    C  CB  . VAL A  1 15  ? 34.932  259.500 5.868  1.00 32.63 ?  14  VAL A CB  1 
ATOM   97    C  CG1 . VAL A  1 15  ? 35.543  259.084 7.193  1.00 30.53 ?  14  VAL A CG1 1 
ATOM   98    C  CG2 . VAL A  1 15  ? 35.707  260.670 5.257  1.00 36.44 ?  14  VAL A CG2 1 
ATOM   99    N  N   . GLN A  1 16  ? 34.967  256.071 5.843  1.00 33.76 ?  15  GLN A N   1 
ATOM   100   C  CA  . GLN A  1 16  ? 34.390  254.927 6.521  1.00 36.98 ?  15  GLN A CA  1 
ATOM   101   C  C   . GLN A  1 16  ? 35.473  254.218 7.314  1.00 35.09 ?  15  GLN A C   1 
ATOM   102   O  O   . GLN A  1 16  ? 36.651  254.264 6.959  1.00 37.09 ?  15  GLN A O   1 
ATOM   103   C  CB  . GLN A  1 16  ? 33.728  253.953 5.539  1.00 37.50 ?  15  GLN A CB  1 
ATOM   104   C  CG  . GLN A  1 16  ? 34.648  253.413 4.457  1.00 43.74 ?  15  GLN A CG  1 
ATOM   105   C  CD  . GLN A  1 16  ? 33.889  252.529 3.459  1.00 53.83 ?  15  GLN A CD  1 
ATOM   106   O  OE1 . GLN A  1 16  ? 33.676  252.893 2.302  1.00 53.71 ?  15  GLN A OE1 1 
ATOM   107   N  NE2 . GLN A  1 16  ? 33.465  251.361 3.924  1.00 49.04 ?  15  GLN A NE2 1 
ATOM   108   N  N   . GLY A  1 17  ? 35.069  253.565 8.397  1.00 32.14 ?  16  GLY A N   1 
ATOM   109   C  CA  . GLY A  1 17  ? 36.054  252.871 9.203  1.00 32.62 ?  16  GLY A CA  1 
ATOM   110   C  C   . GLY A  1 17  ? 35.413  252.016 10.272 1.00 33.22 ?  16  GLY A C   1 
ATOM   111   O  O   . GLY A  1 17  ? 34.198  252.040 10.491 1.00 31.03 ?  16  GLY A O   1 
ATOM   112   N  N   . ILE A  1 18  ? 36.267  251.247 10.931 1.00 33.76 ?  17  ILE A N   1 
ATOM   113   C  CA  . ILE A  1 18  ? 35.900  250.430 12.077 1.00 32.17 ?  17  ILE A CA  1 
ATOM   114   C  C   . ILE A  1 18  ? 36.818  250.822 13.218 1.00 34.12 ?  17  ILE A C   1 
ATOM   115   O  O   . ILE A  1 18  ? 38.042  250.774 13.073 1.00 30.71 ?  17  ILE A O   1 
ATOM   116   C  CB  . ILE A  1 18  ? 36.030  248.927 11.780 1.00 32.55 ?  17  ILE A CB  1 
ATOM   117   C  CG1 . ILE A  1 18  ? 35.031  248.499 10.710 1.00 33.84 ?  17  ILE A CG1 1 
ATOM   118   C  CG2 . ILE A  1 18  ? 35.879  248.114 13.072 1.00 29.68 ?  17  ILE A CG2 1 
ATOM   119   C  CD1 . ILE A  1 18  ? 35.341  247.136 10.155 1.00 37.57 ?  17  ILE A CD1 1 
ATOM   120   N  N   . ILE A  1 19  ? 36.232  251.198 14.347 1.00 29.83 ?  18  ILE A N   1 
ATOM   121   C  CA  . ILE A  1 19  ? 36.991  251.583 15.528 1.00 27.35 ?  18  ILE A CA  1 
ATOM   122   C  C   . ILE A  1 19  ? 36.639  250.621 16.655 1.00 30.58 ?  18  ILE A C   1 
ATOM   123   O  O   . ILE A  1 19  ? 35.455  250.410 16.944 1.00 31.64 ?  18  ILE A O   1 
ATOM   124   C  CB  . ILE A  1 19  ? 36.694  253.041 15.923 1.00 27.61 ?  18  ILE A CB  1 
ATOM   125   C  CG1 . ILE A  1 19  ? 37.216  253.987 14.839 1.00 28.67 ?  18  ILE A CG1 1 
ATOM   126   C  CG2 . ILE A  1 19  ? 37.311  253.364 17.275 1.00 24.00 ?  18  ILE A CG2 1 
ATOM   127   C  CD1 . ILE A  1 19  ? 38.724  253.924 14.659 1.00 29.48 ?  18  ILE A CD1 1 
ATOM   128   N  N   . ASN A  1 20  ? 37.666  250.045 17.282 1.00 28.32 ?  19  ASN A N   1 
ATOM   129   C  CA  . ASN A  1 20  ? 37.539  249.148 18.420 1.00 30.42 ?  19  ASN A CA  1 
ATOM   130   C  C   . ASN A  1 20  ? 37.839  249.866 19.728 1.00 34.76 ?  19  ASN A C   1 
ATOM   131   O  O   . ASN A  1 20  ? 38.713  250.736 19.797 1.00 31.51 ?  19  ASN A O   1 
ATOM   132   C  CB  . ASN A  1 20  ? 38.497  247.968 18.280 1.00 29.83 ?  19  ASN A CB  1 
ATOM   133   C  CG  . ASN A  1 20  ? 38.381  247.299 16.936 1.00 40.53 ?  19  ASN A CG  1 
ATOM   134   O  OD1 . ASN A  1 20  ? 39.218  247.498 16.046 1.00 40.80 ?  19  ASN A OD1 1 
ATOM   135   N  ND2 . ASN A  1 20  ? 37.339  246.504 16.772 1.00 32.74 ?  19  ASN A ND2 1 
ATOM   136   N  N   . PHE A  1 21  ? 37.123  249.469 20.780 1.00 29.97 ?  20  PHE A N   1 
ATOM   137   C  CA  . PHE A  1 21  ? 37.364  249.952 22.133 1.00 29.70 ?  20  PHE A CA  1 
ATOM   138   C  C   . PHE A  1 21  ? 37.562  248.754 23.040 1.00 36.03 ?  20  PHE A C   1 
ATOM   139   O  O   . PHE A  1 21  ? 36.831  247.762 22.931 1.00 31.23 ?  20  PHE A O   1 
ATOM   140   C  CB  . PHE A  1 21  ? 36.210  250.757 22.695 1.00 29.16 ?  20  PHE A CB  1 
ATOM   141   C  CG  . PHE A  1 21  ? 35.787  251.891 21.851 1.00 31.15 ?  20  PHE A CG  1 
ATOM   142   C  CD1 . PHE A  1 21  ? 35.038  251.680 20.702 1.00 33.42 ?  20  PHE A CD1 1 
ATOM   143   C  CD2 . PHE A  1 21  ? 36.110  253.187 22.215 1.00 31.43 ?  20  PHE A CD2 1 
ATOM   144   C  CE1 . PHE A  1 21  ? 34.619  252.744 19.930 1.00 30.20 ?  20  PHE A CE1 1 
ATOM   145   C  CE2 . PHE A  1 21  ? 35.695  254.255 21.435 1.00 31.00 ?  20  PHE A CE2 1 
ATOM   146   C  CZ  . PHE A  1 21  ? 34.951  254.028 20.294 1.00 28.15 ?  20  PHE A CZ  1 
ATOM   147   N  N   . GLU A  1 22  ? 38.516  248.862 23.960 1.00 30.48 ?  21  GLU A N   1 
ATOM   148   C  CA  . GLU A  1 22  ? 38.771  247.769 24.889 1.00 33.22 ?  21  GLU A CA  1 
ATOM   149   C  C   . GLU A  1 22  ? 39.133  248.337 26.247 1.00 34.21 ?  21  GLU A C   1 
ATOM   150   O  O   . GLU A  1 22  ? 39.964  249.243 26.345 1.00 33.59 ?  21  GLU A O   1 
ATOM   151   C  CB  . GLU A  1 22  ? 39.885  246.864 24.377 1.00 36.54 ?  21  GLU A CB  1 
ATOM   152   C  CG  . GLU A  1 22  ? 39.914  245.507 25.026 1.00 51.23 ?  21  GLU A CG  1 
ATOM   153   C  CD  . GLU A  1 22  ? 40.857  244.566 24.305 1.00 69.02 ?  21  GLU A CD  1 
ATOM   154   O  OE1 . GLU A  1 22  ? 40.436  243.433 23.986 1.00 74.98 ?  21  GLU A OE1 1 
ATOM   155   O  OE2 . GLU A  1 22  ? 42.016  244.970 24.044 1.00 74.49 ?  21  GLU A OE2 1 
ATOM   156   N  N   . GLN A  1 23  ? 38.505  247.805 27.289 1.00 31.21 ?  22  GLN A N   1 
ATOM   157   C  CA  . GLN A  1 23  ? 38.720  248.278 28.653 1.00 30.99 ?  22  GLN A CA  1 
ATOM   158   C  C   . GLN A  1 23  ? 38.806  247.039 29.535 1.00 40.79 ?  22  GLN A C   1 
ATOM   159   O  O   . GLN A  1 23  ? 37.783  246.554 30.024 1.00 39.87 ?  22  GLN A O   1 
ATOM   160   C  CB  . GLN A  1 23  ? 37.593  249.203 29.087 1.00 30.06 ?  22  GLN A CB  1 
ATOM   161   C  CG  . GLN A  1 23  ? 37.883  249.945 30.349 1.00 30.50 ?  22  GLN A CG  1 
ATOM   162   C  CD  . GLN A  1 23  ? 36.730  250.817 30.781 1.00 30.03 ?  22  GLN A CD  1 
ATOM   163   O  OE1 . GLN A  1 23  ? 35.604  250.680 30.293 1.00 29.80 ?  22  GLN A OE1 1 
ATOM   164   N  NE2 . GLN A  1 23  ? 37.001  251.723 31.713 1.00 29.64 ?  22  GLN A NE2 1 
ATOM   165   N  N   . LYS A  1 24  ? 40.023  246.533 29.741 1.00 40.61 ?  23  LYS A N   1 
ATOM   166   C  CA  . LYS A  1 24  ? 40.159  245.291 30.499 1.00 43.26 ?  23  LYS A CA  1 
ATOM   167   C  C   . LYS A  1 24  ? 39.720  245.447 31.953 1.00 42.88 ?  23  LYS A C   1 
ATOM   168   O  O   . LYS A  1 24  ? 39.147  244.513 32.516 1.00 48.30 ?  23  LYS A O   1 
ATOM   169   C  CB  . LYS A  1 24  ? 41.595  244.773 30.413 1.00 46.94 ?  23  LYS A CB  1 
ATOM   170   C  CG  . LYS A  1 24  ? 41.863  243.922 29.159 1.00 51.65 ?  23  LYS A CG  1 
ATOM   171   C  CD  . LYS A  1 24  ? 41.208  242.536 29.266 1.00 59.96 ?  23  LYS A CD  1 
ATOM   172   C  CE  . LYS A  1 24  ? 39.899  242.433 28.454 1.00 63.11 ?  23  LYS A CE  1 
ATOM   173   N  NZ  . LYS A  1 24  ? 39.323  241.040 28.414 1.00 55.10 ?  23  LYS A NZ  1 
ATOM   174   N  N   . GLU A  1 25  ? 39.947  246.607 32.569 1.00 36.29 ?  24  GLU A N   1 
ATOM   175   C  CA  . GLU A  1 25  ? 39.505  246.879 33.935 1.00 39.78 ?  24  GLU A CA  1 
ATOM   176   C  C   . GLU A  1 25  ? 38.521  248.033 33.916 1.00 37.77 ?  24  GLU A C   1 
ATOM   177   O  O   . GLU A  1 25  ? 38.782  249.059 33.280 1.00 36.98 ?  24  GLU A O   1 
ATOM   178   C  CB  . GLU A  1 25  ? 40.668  247.247 34.863 1.00 42.86 ?  24  GLU A CB  1 
ATOM   179   C  CG  . GLU A  1 25  ? 41.991  246.642 34.487 1.00 48.72 ?  24  GLU A CG  1 
ATOM   180   C  CD  . GLU A  1 25  ? 42.070  245.168 34.817 1.00 63.10 ?  24  GLU A CD  1 
ATOM   181   O  OE1 . GLU A  1 25  ? 41.166  244.664 35.532 1.00 66.18 ?  24  GLU A OE1 1 
ATOM   182   O  OE2 . GLU A  1 25  ? 43.040  244.516 34.357 1.00 70.83 ?  24  GLU A OE2 1 
ATOM   183   N  N   . SER A  1 26  ? 37.404  247.878 34.633 1.00 31.29 ?  25  SER A N   1 
ATOM   184   C  CA  . SER A  1 26  ? 36.373  248.906 34.588 1.00 30.32 ?  25  SER A CA  1 
ATOM   185   C  C   . SER A  1 26  ? 36.854  250.239 35.142 1.00 30.61 ?  25  SER A C   1 
ATOM   186   O  O   . SER A  1 26  ? 36.220  251.268 34.879 1.00 32.40 ?  25  SER A O   1 
ATOM   187   C  CB  . SER A  1 26  ? 35.133  248.451 35.356 1.00 33.12 ?  25  SER A CB  1 
ATOM   188   O  OG  . SER A  1 26  ? 35.471  248.151 36.693 1.00 32.59 ?  25  SER A OG  1 
ATOM   189   N  N   . ASN A  1 27  ? 37.915  250.241 35.951 1.00 32.75 ?  26  ASN A N   1 
ATOM   190   C  CA  . ASN A  1 27  ? 38.445  251.480 36.505 1.00 38.06 ?  26  ASN A CA  1 
ATOM   191   C  C   . ASN A  1 27  ? 39.736  251.899 35.815 1.00 41.35 ?  26  ASN A C   1 
ATOM   192   O  O   . ASN A  1 27  ? 40.418  252.813 36.291 1.00 42.64 ?  26  ASN A O   1 
ATOM   193   C  CB  . ASN A  1 27  ? 38.660  251.365 38.017 1.00 33.17 ?  26  ASN A CB  1 
ATOM   194   C  CG  . ASN A  1 27  ? 39.692  250.321 38.391 1.00 37.54 ?  26  ASN A CG  1 
ATOM   195   O  OD1 . ASN A  1 27  ? 39.790  249.268 37.753 1.00 42.04 ?  26  ASN A OD1 1 
ATOM   196   N  ND2 . ASN A  1 27  ? 40.472  250.607 39.442 1.00 35.99 ?  26  ASN A ND2 1 
ATOM   197   N  N   . GLY A  1 28  ? 40.077  251.251 34.704 1.00 36.66 ?  27  GLY A N   1 
ATOM   198   C  CA  . GLY A  1 28  ? 41.272  251.560 33.963 1.00 37.54 ?  27  GLY A CA  1 
ATOM   199   C  C   . GLY A  1 28  ? 40.950  252.291 32.674 1.00 34.77 ?  27  GLY A C   1 
ATOM   200   O  O   . GLY A  1 28  ? 39.791  252.625 32.388 1.00 32.33 ?  27  GLY A O   1 
ATOM   201   N  N   . PRO A  1 29  ? 41.981  252.570 31.884 1.00 35.04 ?  28  PRO A N   1 
ATOM   202   C  CA  . PRO A  1 29  ? 41.790  253.316 30.637 1.00 36.14 ?  28  PRO A CA  1 
ATOM   203   C  C   . PRO A  1 29  ? 41.140  252.471 29.551 1.00 32.01 ?  28  PRO A C   1 
ATOM   204   O  O   . PRO A  1 29  ? 41.149  251.237 29.582 1.00 32.32 ?  28  PRO A O   1 
ATOM   205   C  CB  . PRO A  1 29  ? 43.222  253.696 30.240 1.00 37.13 ?  28  PRO A CB  1 
ATOM   206   C  CG  . PRO A  1 29  ? 44.055  252.604 30.811 1.00 42.82 ?  28  PRO A CG  1 
ATOM   207   C  CD  . PRO A  1 29  ? 43.404  252.291 32.143 1.00 38.32 ?  28  PRO A CD  1 
ATOM   208   N  N   . VAL A  1 30  ? 40.582  253.170 28.567 1.00 30.12 ?  29  VAL A N   1 
ATOM   209   C  CA  . VAL A  1 30  ? 40.041  252.540 27.359 1.00 27.79 ?  29  VAL A CA  1 
ATOM   210   C  C   . VAL A  1 30  ? 41.042  252.686 26.219 1.00 37.00 ?  29  VAL A C   1 
ATOM   211   O  O   . VAL A  1 30  ? 41.442  253.811 25.882 1.00 33.27 ?  29  VAL A O   1 
ATOM   212   C  CB  . VAL A  1 30  ? 38.695  253.174 26.973 1.00 27.53 ?  29  VAL A CB  1 
ATOM   213   C  CG1 . VAL A  1 30  ? 38.106  252.485 25.730 1.00 27.24 ?  29  VAL A CG1 1 
ATOM   214   C  CG2 . VAL A  1 30  ? 37.736  253.123 28.156 1.00 29.40 ?  29  VAL A CG2 1 
ATOM   215   N  N   . LYS A  1 31  ? 41.431  251.560 25.613 1.00 30.96 ?  30  LYS A N   1 
ATOM   216   C  CA  . LYS A  1 31  ? 42.176  251.575 24.360 1.00 32.32 ?  30  LYS A CA  1 
ATOM   217   C  C   . LYS A  1 31  ? 41.222  251.743 23.183 1.00 39.74 ?  30  LYS A C   1 
ATOM   218   O  O   . LYS A  1 31  ? 40.173  251.092 23.120 1.00 32.87 ?  30  LYS A O   1 
ATOM   219   C  CB  . LYS A  1 31  ? 42.979  250.288 24.184 1.00 34.37 ?  30  LYS A CB  1 
ATOM   220   C  CG  . LYS A  1 31  ? 44.224  250.216 25.050 1.00 43.85 ?  30  LYS A CG  1 
ATOM   221   C  CD  . LYS A  1 31  ? 45.025  248.924 24.835 1.00 45.08 ?  30  LYS A CD  1 
ATOM   222   C  CE  . LYS A  1 31  ? 46.001  248.699 25.998 1.00 54.23 ?  30  LYS A CE  1 
ATOM   223   N  NZ  . LYS A  1 31  ? 46.875  247.496 25.777 1.00 63.29 ?  30  LYS A NZ  1 
ATOM   224   N  N   . VAL A  1 32  ? 41.596  252.603 22.239 1.00 32.11 ?  31  VAL A N   1 
ATOM   225   C  CA  . VAL A  1 32  ? 40.783  252.922 21.072 1.00 32.78 ?  31  VAL A CA  1 
ATOM   226   C  C   . VAL A  1 32  ? 41.670  252.763 19.851 1.00 35.11 ?  31  VAL A C   1 
ATOM   227   O  O   . VAL A  1 32  ? 42.726  253.401 19.762 1.00 36.30 ?  31  VAL A O   1 
ATOM   228   C  CB  . VAL A  1 32  ? 40.217  254.350 21.150 1.00 30.83 ?  31  VAL A CB  1 
ATOM   229   C  CG1 . VAL A  1 32  ? 39.355  254.655 19.931 1.00 27.41 ?  31  VAL A CG1 1 
ATOM   230   C  CG2 . VAL A  1 32  ? 39.428  254.520 22.434 1.00 28.94 ?  31  VAL A CG2 1 
ATOM   231   N  N   . TRP A  1 33  ? 41.259  251.912 18.915 1.00 29.99 ?  32  TRP A N   1 
ATOM   232   C  CA  . TRP A  1 33  ? 42.133  251.647 17.783 1.00 30.85 ?  32  TRP A CA  1 
ATOM   233   C  C   . TRP A  1 33  ? 41.327  251.122 16.605 1.00 34.74 ?  32  TRP A C   1 
ATOM   234   O  O   . TRP A  1 33  ? 40.228  250.577 16.755 1.00 31.16 ?  32  TRP A O   1 
ATOM   235   C  CB  . TRP A  1 33  ? 43.248  250.658 18.158 1.00 30.91 ?  32  TRP A CB  1 
ATOM   236   C  CG  . TRP A  1 33  ? 42.839  249.213 18.071 1.00 34.16 ?  32  TRP A CG  1 
ATOM   237   C  CD1 . TRP A  1 33  ? 43.035  248.361 17.022 1.00 32.42 ?  32  TRP A CD1 1 
ATOM   238   C  CD2 . TRP A  1 33  ? 42.193  248.452 19.092 1.00 33.07 ?  32  TRP A CD2 1 
ATOM   239   N  NE1 . TRP A  1 33  ? 42.534  247.113 17.326 1.00 35.60 ?  32  TRP A NE1 1 
ATOM   240   C  CE2 . TRP A  1 33  ? 42.010  247.144 18.591 1.00 33.58 ?  32  TRP A CE2 1 
ATOM   241   C  CE3 . TRP A  1 33  ? 41.736  248.752 20.376 1.00 37.72 ?  32  TRP A CE3 1 
ATOM   242   C  CZ2 . TRP A  1 33  ? 41.392  246.137 19.332 1.00 38.33 ?  32  TRP A CZ2 1 
ATOM   243   C  CZ3 . TRP A  1 33  ? 41.128  247.739 21.120 1.00 45.81 ?  32  TRP A CZ3 1 
ATOM   244   C  CH2 . TRP A  1 33  ? 40.960  246.452 20.591 1.00 41.32 ?  32  TRP A CH2 1 
ATOM   245   N  N   . GLY A  1 34  ? 41.900  251.293 15.434 1.00 31.47 ?  33  GLY A N   1 
ATOM   246   C  CA  . GLY A  1 34  ? 41.302  250.819 14.216 1.00 33.99 ?  33  GLY A CA  1 
ATOM   247   C  C   . GLY A  1 34  ? 41.750  251.689 13.062 1.00 36.65 ?  33  GLY A C   1 
ATOM   248   O  O   . GLY A  1 34  ? 42.747  252.391 13.143 1.00 34.56 ?  33  GLY A O   1 
ATOM   249   N  N   . SER A  1 35  ? 40.977  251.653 11.993 1.00 37.15 ?  34  SER A N   1 
ATOM   250   C  CA  . SER A  1 35  ? 41.398  252.320 10.778 1.00 35.99 ?  34  SER A CA  1 
ATOM   251   C  C   . SER A  1 35  ? 40.222  253.078 10.196 1.00 38.44 ?  34  SER A C   1 
ATOM   252   O  O   . SER A  1 35  ? 39.113  252.543 10.109 1.00 35.90 ?  34  SER A O   1 
ATOM   253   C  CB  . SER A  1 35  ? 41.943  251.296 9.784  1.00 40.98 ?  34  SER A CB  1 
ATOM   254   O  OG  . SER A  1 35  ? 41.934  251.827 8.482  1.00 55.47 ?  34  SER A OG  1 
ATOM   255   N  N   . ILE A  1 36  ? 40.459  254.330 9.829  1.00 31.08 ?  35  ILE A N   1 
ATOM   256   C  CA  . ILE A  1 36  ? 39.493  255.130 9.090  1.00 32.27 ?  35  ILE A CA  1 
ATOM   257   C  C   . ILE A  1 36  ? 40.121  255.480 7.754  1.00 38.20 ?  35  ILE A C   1 
ATOM   258   O  O   . ILE A  1 36  ? 41.268  255.938 7.707  1.00 36.72 ?  35  ILE A O   1 
ATOM   259   C  CB  . ILE A  1 36  ? 39.105  256.407 9.846  1.00 32.92 ?  35  ILE A CB  1 
ATOM   260   C  CG1 . ILE A  1 36  ? 38.724  256.095 11.289 1.00 34.31 ?  35  ILE A CG1 1 
ATOM   261   C  CG2 . ILE A  1 36  ? 37.995  257.138 9.116  1.00 31.47 ?  35  ILE A CG2 1 
ATOM   262   C  CD1 . ILE A  1 36  ? 38.391  257.347 12.059 1.00 29.62 ?  35  ILE A CD1 1 
ATOM   263   N  N   . LYS A  1 37  ? 39.389  255.259 6.675  1.00 36.76 ?  36  LYS A N   1 
ATOM   264   C  CA  . LYS A  1 37  ? 39.909  255.570 5.353  1.00 36.45 ?  36  LYS A CA  1 
ATOM   265   C  C   . LYS A  1 37  ? 38.999  256.583 4.680  1.00 32.26 ?  36  LYS A C   1 
ATOM   266   O  O   . LYS A  1 37  ? 37.943  256.957 5.205  1.00 34.64 ?  36  LYS A O   1 
ATOM   267   C  CB  . LYS A  1 37  ? 40.076  254.300 4.512  1.00 39.87 ?  36  LYS A CB  1 
ATOM   268   C  CG  . LYS A  1 37  ? 38.787  253.641 4.111  1.00 41.71 ?  36  LYS A CG  1 
ATOM   269   C  CD  . LYS A  1 37  ? 38.985  252.142 3.955  1.00 45.58 ?  36  LYS A CD  1 
ATOM   270   C  CE  . LYS A  1 37  ? 38.276  251.632 2.709  1.00 49.46 ?  36  LYS A CE  1 
ATOM   271   N  NZ  . LYS A  1 37  ? 38.381  250.136 2.576  1.00 59.89 ?  36  LYS A NZ  1 
ATOM   272   N  N   . GLY A  1 38  ? 39.446  257.067 3.526  1.00 36.92 ?  37  GLY A N   1 
ATOM   273   C  CA  . GLY A  1 38  ? 38.699  258.062 2.795  1.00 31.09 ?  37  GLY A CA  1 
ATOM   274   C  C   . GLY A  1 38  ? 38.854  259.481 3.295  1.00 35.51 ?  37  GLY A C   1 
ATOM   275   O  O   . GLY A  1 38  ? 38.057  260.349 2.912  1.00 39.14 ?  37  GLY A O   1 
ATOM   276   N  N   . LEU A  1 39  ? 39.857  259.758 4.124  1.00 33.79 ?  38  LEU A N   1 
ATOM   277   C  CA  . LEU A  1 39  ? 40.026  261.084 4.705  1.00 37.35 ?  38  LEU A CA  1 
ATOM   278   C  C   . LEU A  1 39  ? 41.058  261.903 3.934  1.00 39.27 ?  38  LEU A C   1 
ATOM   279   O  O   . LEU A  1 39  ? 41.979  261.366 3.318  1.00 37.58 ?  38  LEU A O   1 
ATOM   280   C  CB  . LEU A  1 39  ? 40.472  260.988 6.166  1.00 34.22 ?  38  LEU A CB  1 
ATOM   281   C  CG  . LEU A  1 39  ? 39.459  260.470 7.185  1.00 35.05 ?  38  LEU A CG  1 
ATOM   282   C  CD1 . LEU A  1 39  ? 40.198  259.960 8.422  1.00 31.75 ?  38  LEU A CD1 1 
ATOM   283   C  CD2 . LEU A  1 39  ? 38.472  261.577 7.542  1.00 33.40 ?  38  LEU A CD2 1 
ATOM   284   N  N   . THR A  1 40  ? 40.911  263.220 4.001  1.00 39.30 ?  39  THR A N   1 
ATOM   285   C  CA  . THR A  1 40  ? 41.984  264.082 3.529  1.00 44.71 ?  39  THR A CA  1 
ATOM   286   C  C   . THR A  1 40  ? 43.159  264.013 4.497  1.00 45.72 ?  39  THR A C   1 
ATOM   287   O  O   . THR A  1 40  ? 42.989  263.784 5.697  1.00 43.95 ?  39  THR A O   1 
ATOM   288   C  CB  . THR A  1 40  ? 41.494  265.513 3.394  1.00 40.99 ?  39  THR A CB  1 
ATOM   289   O  OG1 . THR A  1 40  ? 41.114  265.997 4.690  1.00 47.28 ?  39  THR A OG1 1 
ATOM   290   C  CG2 . THR A  1 40  ? 40.281  265.565 2.453  1.00 36.86 ?  39  THR A CG2 1 
ATOM   291   N  N   . GLU A  1 41  ? 44.365  264.187 3.957  1.00 44.97 ?  40  GLU A N   1 
ATOM   292   C  CA  . GLU A  1 41  ? 45.576  264.112 4.770  1.00 41.32 ?  40  GLU A CA  1 
ATOM   293   C  C   . GLU A  1 41  ? 45.541  265.113 5.918  1.00 43.89 ?  40  GLU A C   1 
ATOM   294   O  O   . GLU A  1 41  ? 45.004  266.217 5.788  1.00 37.84 ?  40  GLU A O   1 
ATOM   295   C  CB  . GLU A  1 41  ? 46.812  264.369 3.909  1.00 46.54 ?  40  GLU A CB  1 
ATOM   296   C  CG  . GLU A  1 41  ? 48.069  263.753 4.500  1.00 53.44 ?  40  GLU A CG  1 
ATOM   297   C  CD  . GLU A  1 41  ? 49.341  264.119 3.743  1.00 61.08 ?  40  GLU A CD  1 
ATOM   298   O  OE1 . GLU A  1 41  ? 50.433  263.706 4.198  1.00 66.17 ?  40  GLU A OE1 1 
ATOM   299   O  OE2 . GLU A  1 41  ? 49.252  264.808 2.702  1.00 60.94 ?  40  GLU A OE2 1 
ATOM   300   N  N   . GLY A  1 42  ? 46.101  264.713 7.060  1.00 37.70 ?  41  GLY A N   1 
ATOM   301   C  CA  . GLY A  1 42  ? 46.179  265.622 8.183  1.00 34.85 ?  41  GLY A CA  1 
ATOM   302   C  C   . GLY A  1 42  ? 45.327  265.249 9.383  1.00 42.10 ?  41  GLY A C   1 
ATOM   303   O  O   . GLY A  1 42  ? 44.857  264.108 9.502  1.00 39.14 ?  41  GLY A O   1 
ATOM   304   N  N   . LEU A  1 43  ? 45.111  266.225 10.264 1.00 40.09 ?  42  LEU A N   1 
ATOM   305   C  CA  . LEU A  1 43  ? 44.410  266.020 11.525 1.00 38.69 ?  42  LEU A CA  1 
ATOM   306   C  C   . LEU A  1 43  ? 42.901  266.091 11.336 1.00 42.05 ?  42  LEU A C   1 
ATOM   307   O  O   . LEU A  1 43  ? 42.399  266.896 10.547 1.00 35.11 ?  42  LEU A O   1 
ATOM   308   C  CB  . LEU A  1 43  ? 44.827  267.070 12.555 1.00 38.35 ?  42  LEU A CB  1 
ATOM   309   C  CG  . LEU A  1 43  ? 46.294  267.180 12.959 1.00 38.45 ?  42  LEU A CG  1 
ATOM   310   C  CD1 . LEU A  1 43  ? 46.566  268.573 13.567 1.00 41.08 ?  42  LEU A CD1 1 
ATOM   311   C  CD2 . LEU A  1 43  ? 46.667  266.068 13.933 1.00 39.87 ?  42  LEU A CD2 1 
ATOM   312   N  N   . HIS A  1 44  ? 42.177  265.256 12.085 1.00 35.39 ?  43  HIS A N   1 
ATOM   313   C  CA  . HIS A  1 44  ? 40.720  265.281 12.073 1.00 31.87 ?  43  HIS A CA  1 
ATOM   314   C  C   . HIS A  1 44  ? 40.194  265.117 13.488 1.00 32.84 ?  43  HIS A C   1 
ATOM   315   O  O   . HIS A  1 44  ? 40.610  264.202 14.209 1.00 32.52 ?  43  HIS A O   1 
ATOM   316   C  CB  . HIS A  1 44  ? 40.162  264.177 11.175 1.00 34.04 ?  43  HIS A CB  1 
ATOM   317   C  CG  . HIS A  1 44  ? 40.462  264.385 9.727  1.00 36.89 ?  43  HIS A CG  1 
ATOM   318   N  ND1 . HIS A  1 44  ? 39.613  265.071 8.886  1.00 38.34 ?  43  HIS A ND1 1 
ATOM   319   C  CD2 . HIS A  1 44  ? 41.526  264.016 8.974  1.00 34.40 ?  43  HIS A CD2 1 
ATOM   320   C  CE1 . HIS A  1 44  ? 40.130  265.095 7.669  1.00 38.22 ?  43  HIS A CE1 1 
ATOM   321   N  NE2 . HIS A  1 44  ? 41.289  264.463 7.695  1.00 39.09 ?  43  HIS A NE2 1 
ATOM   322   N  N   . GLY A  1 45  ? 39.286  266.012 13.874 1.00 34.29 ?  44  GLY A N   1 
ATOM   323   C  CA  . GLY A  1 45  ? 38.645  265.889 15.170 1.00 30.15 ?  44  GLY A CA  1 
ATOM   324   C  C   . GLY A  1 45  ? 37.952  264.545 15.310 1.00 34.53 ?  44  GLY A C   1 
ATOM   325   O  O   . GLY A  1 45  ? 37.352  264.030 14.362 1.00 30.02 ?  44  GLY A O   1 
ATOM   326   N  N   . PHE A  1 46  ? 38.031  263.985 16.512 1.00 28.99 ?  45  PHE A N   1 
ATOM   327   C  CA  . PHE A  1 46  ? 37.632  262.601 16.809 1.00 31.70 ?  45  PHE A CA  1 
ATOM   328   C  C   . PHE A  1 46  ? 36.951  262.665 18.171 1.00 31.04 ?  45  PHE A C   1 
ATOM   329   O  O   . PHE A  1 46  ? 37.634  262.806 19.188 1.00 30.68 ?  45  PHE A O   1 
ATOM   330   C  CB  . PHE A  1 46  ? 38.868  261.712 16.841 1.00 30.21 ?  45  PHE A CB  1 
ATOM   331   C  CG  . PHE A  1 46  ? 38.598  260.234 16.846 1.00 28.76 ?  45  PHE A CG  1 
ATOM   332   C  CD1 . PHE A  1 46  ? 37.978  259.615 15.759 1.00 32.18 ?  45  PHE A CD1 1 
ATOM   333   C  CD2 . PHE A  1 46  ? 39.051  259.443 17.896 1.00 30.91 ?  45  PHE A CD2 1 
ATOM   334   C  CE1 . PHE A  1 46  ? 37.769  258.236 15.739 1.00 30.97 ?  45  PHE A CE1 1 
ATOM   335   C  CE2 . PHE A  1 46  ? 38.844  258.042 17.885 1.00 33.36 ?  45  PHE A CE2 1 
ATOM   336   C  CZ  . PHE A  1 46  ? 38.201  257.447 16.811 1.00 29.46 ?  45  PHE A CZ  1 
ATOM   337   N  N   . HIS A  1 47  ? 35.617  262.617 18.189 1.00 30.24 ?  46  HIS A N   1 
ATOM   338   C  CA  . HIS A  1 47  ? 34.850  262.935 19.389 1.00 29.30 ?  46  HIS A CA  1 
ATOM   339   C  C   . HIS A  1 47  ? 33.703  261.954 19.583 1.00 32.29 ?  46  HIS A C   1 
ATOM   340   O  O   . HIS A  1 47  ? 33.080  261.505 18.618 1.00 31.15 ?  46  HIS A O   1 
ATOM   341   C  CB  . HIS A  1 47  ? 34.254  264.332 19.319 1.00 31.97 ?  46  HIS A CB  1 
ATOM   342   C  CG  . HIS A  1 47  ? 35.241  265.381 18.937 1.00 37.95 ?  46  HIS A CG  1 
ATOM   343   N  ND1 . HIS A  1 47  ? 35.041  266.238 17.879 1.00 35.82 ?  46  HIS A ND1 1 
ATOM   344   C  CD2 . HIS A  1 47  ? 36.432  265.723 19.487 1.00 37.10 ?  46  HIS A CD2 1 
ATOM   345   C  CE1 . HIS A  1 47  ? 36.075  267.058 17.781 1.00 39.31 ?  46  HIS A CE1 1 
ATOM   346   N  NE2 . HIS A  1 47  ? 36.933  266.767 18.743 1.00 38.62 ?  46  HIS A NE2 1 
ATOM   347   N  N   . VAL A  1 48  ? 33.399  261.665 20.842 1.00 30.67 ?  47  VAL A N   1 
ATOM   348   C  CA  . VAL A  1 48  ? 32.157  260.991 21.193 1.00 31.19 ?  47  VAL A CA  1 
ATOM   349   C  C   . VAL A  1 48  ? 31.101  262.062 21.425 1.00 28.21 ?  47  VAL A C   1 
ATOM   350   O  O   . VAL A  1 48  ? 31.244  262.910 22.315 1.00 32.35 ?  47  VAL A O   1 
ATOM   351   C  CB  . VAL A  1 48  ? 32.333  260.106 22.437 1.00 32.32 ?  47  VAL A CB  1 
ATOM   352   C  CG1 . VAL A  1 48  ? 31.016  259.421 22.786 1.00 22.40 ?  47  VAL A CG1 1 
ATOM   353   C  CG2 . VAL A  1 48  ? 33.448  259.088 22.208 1.00 30.85 ?  47  VAL A CG2 1 
ATOM   354   N  N   . HIS A  1 49  ? 30.055  262.041 20.613 1.00 26.53 ?  48  HIS A N   1 
ATOM   355   C  CA  . HIS A  1 49  ? 28.920  262.931 20.793 1.00 31.35 ?  48  HIS A CA  1 
ATOM   356   C  C   . HIS A  1 49  ? 27.838  262.262 21.642 1.00 33.03 ?  48  HIS A C   1 
ATOM   357   O  O   . HIS A  1 49  ? 27.817  261.042 21.811 1.00 30.27 ?  48  HIS A O   1 
ATOM   358   C  CB  . HIS A  1 49  ? 28.357  263.344 19.445 1.00 29.13 ?  48  HIS A CB  1 
ATOM   359   C  CG  . HIS A  1 49  ? 29.271  264.237 18.657 1.00 33.35 ?  48  HIS A CG  1 
ATOM   360   N  ND1 . HIS A  1 49  ? 28.907  265.502 18.248 1.00 33.75 ?  48  HIS A ND1 1 
ATOM   361   C  CD2 . HIS A  1 49  ? 30.542  264.053 18.228 1.00 31.81 ?  48  HIS A CD2 1 
ATOM   362   C  CE1 . HIS A  1 49  ? 29.908  266.050 17.576 1.00 33.01 ?  48  HIS A CE1 1 
ATOM   363   N  NE2 . HIS A  1 49  ? 30.912  265.193 17.553 1.00 33.09 ?  48  HIS A NE2 1 
ATOM   364   N  N   . GLU A  1 50  ? 26.897  263.077 22.133 1.00 31.24 ?  49  GLU A N   1 
ATOM   365   C  CA  . GLU A  1 50  ? 26.090  262.678 23.284 1.00 31.92 ?  49  GLU A CA  1 
ATOM   366   C  C   . GLU A  1 50  ? 25.073  261.588 22.940 1.00 31.38 ?  49  GLU A C   1 
ATOM   367   O  O   . GLU A  1 50  ? 24.824  260.698 23.755 1.00 31.12 ?  49  GLU A O   1 
ATOM   368   C  CB  . GLU A  1 50  ? 25.366  263.889 23.878 1.00 32.59 ?  49  GLU A CB  1 
ATOM   369   C  CG  . GLU A  1 50  ? 24.480  263.512 25.068 1.00 34.19 ?  49  GLU A CG  1 
ATOM   370   C  CD  . GLU A  1 50  ? 23.801  264.707 25.747 1.00 40.98 ?  49  GLU A CD  1 
ATOM   371   O  OE1 . GLU A  1 50  ? 23.895  265.840 25.226 1.00 42.05 ?  49  GLU A OE1 1 
ATOM   372   O  OE2 . GLU A  1 50  ? 23.174  264.498 26.811 1.00 47.36 ?  49  GLU A OE2 1 
ATOM   373   N  N   . PHE A  1 51  ? 24.450  261.649 21.767 1.00 31.10 ?  50  PHE A N   1 
ATOM   374   C  CA  . PHE A  1 51  ? 23.341  260.760 21.441 1.00 28.28 ?  50  PHE A CA  1 
ATOM   375   C  C   . PHE A  1 51  ? 23.751  259.750 20.383 1.00 30.88 ?  50  PHE A C   1 
ATOM   376   O  O   . PHE A  1 51  ? 24.489  260.079 19.450 1.00 32.48 ?  50  PHE A O   1 
ATOM   377   C  CB  . PHE A  1 51  ? 22.126  261.565 20.964 1.00 30.24 ?  50  PHE A CB  1 
ATOM   378   C  CG  . PHE A  1 51  ? 21.701  262.632 21.944 1.00 33.91 ?  50  PHE A CG  1 
ATOM   379   C  CD1 . PHE A  1 51  ? 21.278  262.286 23.214 1.00 34.90 ?  50  PHE A CD1 1 
ATOM   380   C  CD2 . PHE A  1 51  ? 21.767  263.975 21.615 1.00 37.50 ?  50  PHE A CD2 1 
ATOM   381   C  CE1 . PHE A  1 51  ? 20.907  263.266 24.139 1.00 36.82 ?  50  PHE A CE1 1 
ATOM   382   C  CE2 . PHE A  1 51  ? 21.392  264.954 22.541 1.00 40.26 ?  50  PHE A CE2 1 
ATOM   383   C  CZ  . PHE A  1 51  ? 20.969  264.591 23.794 1.00 35.77 ?  50  PHE A CZ  1 
ATOM   384   N  N   . GLY A  1 52  ? 23.277  258.517 20.540 1.00 29.61 ?  51  GLY A N   1 
ATOM   385   C  CA  . GLY A  1 52  ? 23.438  257.485 19.522 1.00 26.16 ?  51  GLY A CA  1 
ATOM   386   C  C   . GLY A  1 52  ? 22.274  257.531 18.548 1.00 31.16 ?  51  GLY A C   1 
ATOM   387   O  O   . GLY A  1 52  ? 21.590  256.530 18.307 1.00 31.90 ?  51  GLY A O   1 
ATOM   388   N  N   . ASP A  1 53  ? 22.039  258.719 18.007 1.00 30.78 ?  52  ASP A N   1 
ATOM   389   C  CA  . ASP A  1 53  ? 20.879  259.034 17.181 1.00 33.54 ?  52  ASP A CA  1 
ATOM   390   C  C   . ASP A  1 53  ? 21.384  259.399 15.792 1.00 33.28 ?  52  ASP A C   1 
ATOM   391   O  O   . ASP A  1 53  ? 22.039  260.434 15.621 1.00 31.17 ?  52  ASP A O   1 
ATOM   392   C  CB  . ASP A  1 53  ? 20.085  260.184 17.801 1.00 32.79 ?  52  ASP A CB  1 
ATOM   393   C  CG  . ASP A  1 53  ? 18.769  260.461 17.082 1.00 35.26 ?  52  ASP A CG  1 
ATOM   394   O  OD1 . ASP A  1 53  ? 18.686  260.226 15.854 1.00 33.66 ?  52  ASP A OD1 1 
ATOM   395   O  OD2 . ASP A  1 53  ? 17.821  260.923 17.762 1.00 31.73 ?  52  ASP A OD2 1 
ATOM   396   N  N   . ASN A  1 54  ? 21.088  258.549 14.812 1.00 31.55 ?  53  ASN A N   1 
ATOM   397   C  CA  . ASN A  1 54  ? 21.490  258.748 13.424 1.00 31.80 ?  53  ASN A CA  1 
ATOM   398   C  C   . ASN A  1 54  ? 20.282  258.973 12.518 1.00 35.29 ?  53  ASN A C   1 
ATOM   399   O  O   . ASN A  1 54  ? 20.378  258.796 11.297 1.00 33.71 ?  53  ASN A O   1 
ATOM   400   C  CB  . ASN A  1 54  ? 22.324  257.552 12.953 1.00 36.87 ?  53  ASN A CB  1 
ATOM   401   C  CG  . ASN A  1 54  ? 23.017  257.792 11.613 1.00 53.33 ?  53  ASN A CG  1 
ATOM   402   O  OD1 . ASN A  1 54  ? 23.895  258.652 11.497 1.00 50.53 ?  53  ASN A OD1 1 
ATOM   403   N  ND2 . ASN A  1 54  ? 22.625  257.026 10.591 1.00 53.37 ?  53  ASN A ND2 1 
ATOM   404   N  N   . THR A  1 55  ? 19.143  259.381 13.095 1.00 33.47 ?  54  THR A N   1 
ATOM   405   C  CA  . THR A  1 55  ? 17.918  259.509 12.308 1.00 34.04 ?  54  THR A CA  1 
ATOM   406   C  C   . THR A  1 55  ? 18.055  260.572 11.228 1.00 36.21 ?  54  THR A C   1 
ATOM   407   O  O   . THR A  1 55  ? 17.481  260.428 10.147 1.00 35.55 ?  54  THR A O   1 
ATOM   408   C  CB  . THR A  1 55  ? 16.723  259.845 13.202 1.00 31.08 ?  54  THR A CB  1 
ATOM   409   O  OG1 . THR A  1 55  ? 17.027  260.991 14.005 1.00 33.06 ?  54  THR A OG1 1 
ATOM   410   C  CG2 . THR A  1 55  ? 16.366  258.656 14.113 1.00 32.12 ?  54  THR A CG2 1 
ATOM   411   N  N   . ALA A  1 56  ? 18.805  261.641 11.500 1.00 34.45 ?  55  ALA A N   1 
ATOM   412   C  CA  . ALA A  1 56  ? 19.104  262.663 10.501 1.00 41.11 ?  55  ALA A CA  1 
ATOM   413   C  C   . ALA A  1 56  ? 20.593  262.689 10.175 1.00 39.74 ?  55  ALA A C   1 
ATOM   414   O  O   . ALA A  1 56  ? 21.201  263.757 10.067 1.00 45.64 ?  55  ALA A O   1 
ATOM   415   C  CB  . ALA A  1 56  ? 18.636  264.037 10.974 1.00 39.00 ?  55  ALA A CB  1 
ATOM   416   N  N   . GLY A  1 57  ? 21.202  261.510 10.018 1.00 36.78 ?  56  GLY A N   1 
ATOM   417   C  CA  . GLY A  1 57  ? 22.645  261.419 9.847  1.00 36.84 ?  56  GLY A CA  1 
ATOM   418   C  C   . GLY A  1 57  ? 23.388  261.824 11.119 1.00 37.14 ?  56  GLY A C   1 
ATOM   419   O  O   . GLY A  1 57  ? 22.851  261.804 12.227 1.00 37.61 ?  56  GLY A O   1 
ATOM   420   N  N   . CYS A  1 58  ? 24.647  262.229 10.935 1.00 35.24 ?  57  CYS A N   1 
ATOM   421   C  CA  . CYS A  1 58  ? 25.497  262.566 12.078 1.00 37.97 ?  57  CYS A CA  1 
ATOM   422   C  C   . CYS A  1 58  ? 25.021  263.792 12.851 1.00 34.19 ?  57  CYS A C   1 
ATOM   423   O  O   . CYS A  1 58  ? 25.385  263.949 14.025 1.00 31.67 ?  57  CYS A O   1 
ATOM   424   C  CB  . CYS A  1 58  ? 26.930  262.769 11.597 1.00 36.13 ?  57  CYS A CB  1 
ATOM   425   S  SG  . CYS A  1 58  ? 27.624  261.278 10.818 1.00 44.76 ?  57  CYS A SG  1 
ATOM   426   N  N   . THR A  1 59  ? 24.203  264.646 12.232 1.00 33.16 ?  58  THR A N   1 
ATOM   427   C  CA  . THR A  1 59  ? 23.697  265.832 12.918 1.00 35.48 ?  58  THR A CA  1 
ATOM   428   C  C   . THR A  1 59  ? 22.972  265.470 14.202 1.00 36.95 ?  58  THR A C   1 
ATOM   429   O  O   . THR A  1 59  ? 23.138  266.140 15.225 1.00 37.24 ?  58  THR A O   1 
ATOM   430   C  CB  . THR A  1 59  ? 22.752  266.605 12.003 1.00 35.89 ?  58  THR A CB  1 
ATOM   431   O  OG1 . THR A  1 59  ? 23.437  266.925 10.793 1.00 48.68 ?  58  THR A OG1 1 
ATOM   432   C  CG2 . THR A  1 59  ? 22.276  267.884 12.673 1.00 36.70 ?  58  THR A CG2 1 
ATOM   433   N  N   . SER A  1 60  ? 22.158  264.411 14.177 1.00 36.09 ?  59  SER A N   1 
ATOM   434   C  CA  . SER A  1 60  ? 21.327  264.135 15.340 1.00 32.85 ?  59  SER A CA  1 
ATOM   435   C  C   . SER A  1 60  ? 22.096  263.483 16.471 1.00 30.70 ?  59  SER A C   1 
ATOM   436   O  O   . SER A  1 60  ? 21.507  263.217 17.524 1.00 33.62 ?  59  SER A O   1 
ATOM   437   C  CB  . SER A  1 60  ? 20.142  263.261 14.949 1.00 38.43 ?  59  SER A CB  1 
ATOM   438   O  OG  . SER A  1 60  ? 20.429  262.565 13.778 1.00 38.25 ?  59  SER A OG  1 
ATOM   439   N  N   . ALA A  1 61  ? 23.392  263.234 16.299 1.00 30.96 ?  60  ALA A N   1 
ATOM   440   C  CA  . ALA A  1 61  ? 24.200  262.814 17.436 1.00 30.38 ?  60  ALA A CA  1 
ATOM   441   C  C   . ALA A  1 61  ? 24.323  263.903 18.504 1.00 34.04 ?  60  ALA A C   1 
ATOM   442   O  O   . ALA A  1 61  ? 24.762  263.609 19.622 1.00 32.12 ?  60  ALA A O   1 
ATOM   443   C  CB  . ALA A  1 61  ? 25.587  262.397 16.956 1.00 26.89 ?  60  ALA A CB  1 
ATOM   444   N  N   . GLY A  1 62  ? 23.972  265.147 18.195 1.00 35.00 ?  61  GLY A N   1 
ATOM   445   C  CA  . GLY A  1 62  ? 24.071  266.214 19.165 1.00 32.29 ?  61  GLY A CA  1 
ATOM   446   C  C   . GLY A  1 62  ? 25.492  266.675 19.420 1.00 29.45 ?  61  GLY A C   1 
ATOM   447   O  O   . GLY A  1 62  ? 26.399  266.472 18.601 1.00 32.79 ?  61  GLY A O   1 
ATOM   448   N  N   . PRO A  1 63  ? 25.708  267.314 20.564 1.00 33.73 ?  62  PRO A N   1 
ATOM   449   C  CA  . PRO A  1 63  ? 27.007  267.943 20.830 1.00 33.42 ?  62  PRO A CA  1 
ATOM   450   C  C   . PRO A  1 63  ? 27.965  266.948 21.445 1.00 34.93 ?  62  PRO A C   1 
ATOM   451   O  O   . PRO A  1 63  ? 27.643  265.761 21.517 1.00 34.01 ?  62  PRO A O   1 
ATOM   452   C  CB  . PRO A  1 63  ? 26.642  269.057 21.816 1.00 34.48 ?  62  PRO A CB  1 
ATOM   453   C  CG  . PRO A  1 63  ? 25.547  268.380 22.675 1.00 32.86 ?  62  PRO A CG  1 
ATOM   454   C  CD  . PRO A  1 63  ? 24.753  267.532 21.671 1.00 32.93 ?  62  PRO A CD  1 
ATOM   455   N  N   . HIS A  1 64  ? 29.128  267.392 21.912 1.00 33.09 ?  63  HIS A N   1 
ATOM   456   C  CA  . HIS A  1 64  ? 30.067  266.438 22.483 1.00 34.07 ?  63  HIS A CA  1 
ATOM   457   C  C   . HIS A  1 64  ? 29.483  265.865 23.771 1.00 35.78 ?  63  HIS A C   1 
ATOM   458   O  O   . HIS A  1 64  ? 28.748  266.546 24.486 1.00 29.65 ?  63  HIS A O   1 
ATOM   459   C  CB  . HIS A  1 64  ? 31.418  267.107 22.738 1.00 32.62 ?  63  HIS A CB  1 
ATOM   460   C  CG  . HIS A  1 64  ? 32.126  267.506 21.479 1.00 38.65 ?  63  HIS A CG  1 
ATOM   461   N  ND1 . HIS A  1 64  ? 33.386  268.064 21.469 1.00 37.59 ?  63  HIS A ND1 1 
ATOM   462   C  CD2 . HIS A  1 64  ? 31.747  267.410 20.183 1.00 36.36 ?  63  HIS A CD2 1 
ATOM   463   C  CE1 . HIS A  1 64  ? 33.751  268.299 20.220 1.00 35.88 ?  63  HIS A CE1 1 
ATOM   464   N  NE2 . HIS A  1 64  ? 32.770  267.918 19.422 1.00 40.86 ?  63  HIS A NE2 1 
ATOM   465   N  N   . PHE A  1 65  ? 29.761  264.589 24.031 1.00 33.81 ?  64  PHE A N   1 
ATOM   466   C  CA  . PHE A  1 65  ? 29.356  263.979 25.290 1.00 29.86 ?  64  PHE A CA  1 
ATOM   467   C  C   . PHE A  1 65  ? 30.017  264.732 26.451 1.00 32.66 ?  64  PHE A C   1 
ATOM   468   O  O   . PHE A  1 65  ? 31.246  264.785 26.551 1.00 31.61 ?  64  PHE A O   1 
ATOM   469   C  CB  . PHE A  1 65  ? 29.739  262.501 25.290 1.00 27.38 ?  64  PHE A CB  1 
ATOM   470   C  CG  . PHE A  1 65  ? 29.301  261.746 26.528 1.00 30.25 ?  64  PHE A CG  1 
ATOM   471   C  CD1 . PHE A  1 65  ? 28.055  261.967 27.095 1.00 28.92 ?  64  PHE A CD1 1 
ATOM   472   C  CD2 . PHE A  1 65  ? 30.153  260.837 27.123 1.00 27.30 ?  64  PHE A CD2 1 
ATOM   473   C  CE1 . PHE A  1 65  ? 27.667  261.286 28.248 1.00 28.35 ?  64  PHE A CE1 1 
ATOM   474   C  CE2 . PHE A  1 65  ? 29.781  260.150 28.268 1.00 30.62 ?  64  PHE A CE2 1 
ATOM   475   C  CZ  . PHE A  1 65  ? 28.534  260.381 28.833 1.00 30.14 ?  64  PHE A CZ  1 
ATOM   476   N  N   . ASN A  1 66  ? 29.193  265.319 27.323 1.00 30.91 ?  65  ASN A N   1 
ATOM   477   C  CA  . ASN A  1 66  ? 29.660  266.287 28.324 1.00 37.02 ?  65  ASN A CA  1 
ATOM   478   C  C   . ASN A  1 66  ? 28.850  266.161 29.605 1.00 39.48 ?  65  ASN A C   1 
ATOM   479   O  O   . ASN A  1 66  ? 28.171  267.110 30.023 1.00 36.61 ?  65  ASN A O   1 
ATOM   480   C  CB  . ASN A  1 66  ? 29.562  267.698 27.754 1.00 31.96 ?  65  ASN A CB  1 
ATOM   481   C  CG  . ASN A  1 66  ? 30.291  268.750 28.603 1.00 39.27 ?  65  ASN A CG  1 
ATOM   482   O  OD1 . ASN A  1 66  ? 31.182  268.431 29.397 1.00 32.37 ?  65  ASN A OD1 1 
ATOM   483   N  ND2 . ASN A  1 66  ? 29.938  270.017 28.392 1.00 36.22 ?  65  ASN A ND2 1 
ATOM   484   N  N   . PRO A  1 67  ? 28.893  265.009 30.274 1.00 34.96 ?  66  PRO A N   1 
ATOM   485   C  CA  . PRO A  1 67  ? 28.094  264.834 31.496 1.00 36.37 ?  66  PRO A CA  1 
ATOM   486   C  C   . PRO A  1 67  ? 28.500  265.770 32.617 1.00 43.92 ?  66  PRO A C   1 
ATOM   487   O  O   . PRO A  1 67  ? 27.671  266.071 33.479 1.00 43.96 ?  66  PRO A O   1 
ATOM   488   C  CB  . PRO A  1 67  ? 28.353  263.375 31.873 1.00 36.01 ?  66  PRO A CB  1 
ATOM   489   C  CG  . PRO A  1 67  ? 29.713  263.113 31.355 1.00 37.86 ?  66  PRO A CG  1 
ATOM   490   C  CD  . PRO A  1 67  ? 29.833  263.890 30.072 1.00 33.50 ?  66  PRO A CD  1 
ATOM   491   N  N   . LEU A  1 68  ? 29.741  266.252 32.629 1.00 42.43 ?  67  LEU A N   1 
ATOM   492   C  CA  . LEU A  1 68  ? 30.226  267.121 33.697 1.00 44.57 ?  67  LEU A CA  1 
ATOM   493   C  C   . LEU A  1 68  ? 30.058  268.601 33.381 1.00 45.13 ?  67  LEU A C   1 
ATOM   494   O  O   . LEU A  1 68  ? 30.500  269.444 34.172 1.00 48.11 ?  67  LEU A O   1 
ATOM   495   C  CB  . LEU A  1 68  ? 31.697  266.817 33.989 1.00 38.48 ?  67  LEU A CB  1 
ATOM   496   C  CG  . LEU A  1 68  ? 32.006  265.387 34.425 1.00 43.88 ?  67  LEU A CG  1 
ATOM   497   C  CD1 . LEU A  1 68  ? 33.370  265.306 35.089 1.00 46.77 ?  67  LEU A CD1 1 
ATOM   498   C  CD2 . LEU A  1 68  ? 30.930  264.902 35.373 1.00 48.64 ?  67  LEU A CD2 1 
ATOM   499   N  N   . SER A  1 69  ? 29.435  268.933 32.255 1.00 42.10 ?  68  SER A N   1 
ATOM   500   C  CA  . SER A  1 69  ? 29.159  270.313 31.870 1.00 42.19 ?  68  SER A CA  1 
ATOM   501   C  C   . SER A  1 69  ? 30.424  271.169 31.923 1.00 45.10 ?  68  SER A C   1 
ATOM   502   O  O   . SER A  1 69  ? 30.504  272.168 32.633 1.00 45.39 ?  68  SER A O   1 
ATOM   503   C  CB  . SER A  1 69  ? 28.055  270.900 32.754 1.00 45.58 ?  68  SER A CB  1 
ATOM   504   O  OG  . SER A  1 69  ? 26.806  270.304 32.432 1.00 51.12 ?  68  SER A OG  1 
ATOM   505   N  N   . ARG A  1 70  ? 31.425  270.753 31.162 1.00 39.92 ?  69  ARG A N   1 
ATOM   506   C  CA  . ARG A  1 70  ? 32.692  271.464 31.083 1.00 43.07 ?  69  ARG A CA  1 
ATOM   507   C  C   . ARG A  1 70  ? 32.867  272.064 29.692 1.00 46.30 ?  69  ARG A C   1 
ATOM   508   O  O   . ARG A  1 70  ? 31.990  271.960 28.824 1.00 42.66 ?  69  ARG A O   1 
ATOM   509   C  CB  . ARG A  1 70  ? 33.854  270.532 31.432 1.00 40.73 ?  69  ARG A CB  1 
ATOM   510   C  CG  . ARG A  1 70  ? 33.864  270.146 32.894 1.00 42.98 ?  69  ARG A CG  1 
ATOM   511   C  CD  . ARG A  1 70  ? 35.200  269.578 33.334 1.00 47.84 ?  69  ARG A CD  1 
ATOM   512   N  NE  . ARG A  1 70  ? 35.166  269.224 34.751 1.00 51.08 ?  69  ARG A NE  1 
ATOM   513   C  CZ  . ARG A  1 70  ? 35.938  268.307 35.321 1.00 59.26 ?  69  ARG A CZ  1 
ATOM   514   N  NH1 . ARG A  1 70  ? 36.846  267.638 34.626 1.00 57.41 ?  69  ARG A NH1 1 
ATOM   515   N  NH2 . ARG A  1 70  ? 35.802  268.061 36.622 1.00 56.59 ?  69  ARG A NH2 1 
ATOM   516   N  N   . LYS A  1 71  ? 34.014  272.701 29.482 1.00 44.40 ?  70  LYS A N   1 
ATOM   517   C  CA  . LYS A  1 71  ? 34.342  273.306 28.200 1.00 45.10 ?  70  LYS A CA  1 
ATOM   518   C  C   . LYS A  1 71  ? 35.206  272.354 27.379 1.00 41.82 ?  70  LYS A C   1 
ATOM   519   O  O   . LYS A  1 71  ? 35.923  271.513 27.930 1.00 41.76 ?  70  LYS A O   1 
ATOM   520   C  CB  . LYS A  1 71  ? 35.065  274.641 28.396 1.00 47.76 ?  70  LYS A CB  1 
ATOM   521   C  CG  . LYS A  1 71  ? 34.195  275.722 29.025 1.00 49.61 ?  70  LYS A CG  1 
ATOM   522   C  CD  . LYS A  1 71  ? 34.907  277.061 29.005 1.00 53.73 ?  70  LYS A CD  1 
ATOM   523   C  CE  . LYS A  1 71  ? 33.985  278.175 29.484 1.00 68.86 ?  70  LYS A CE  1 
ATOM   524   N  NZ  . LYS A  1 71  ? 32.577  278.014 28.991 1.00 74.29 ?  70  LYS A NZ  1 
ATOM   525   N  N   . HIS A  1 72  ? 35.127  272.486 26.052 1.00 38.86 ?  71  HIS A N   1 
ATOM   526   C  CA  . HIS A  1 72  ? 35.893  271.599 25.186 1.00 38.97 ?  71  HIS A CA  1 
ATOM   527   C  C   . HIS A  1 72  ? 37.382  271.761 25.463 1.00 39.22 ?  71  HIS A C   1 
ATOM   528   O  O   . HIS A  1 72  ? 37.854  272.851 25.781 1.00 39.39 ?  71  HIS A O   1 
ATOM   529   C  CB  . HIS A  1 72  ? 35.575  271.884 23.715 1.00 36.69 ?  71  HIS A CB  1 
ATOM   530   C  CG  . HIS A  1 72  ? 36.440  271.134 22.748 1.00 38.87 ?  71  HIS A CG  1 
ATOM   531   N  ND1 . HIS A  1 72  ? 36.173  269.838 22.357 1.00 34.90 ?  71  HIS A ND1 1 
ATOM   532   C  CD2 . HIS A  1 72  ? 37.563  271.501 22.086 1.00 35.60 ?  71  HIS A CD2 1 
ATOM   533   C  CE1 . HIS A  1 72  ? 37.099  269.437 21.504 1.00 41.05 ?  71  HIS A CE1 1 
ATOM   534   N  NE2 . HIS A  1 72  ? 37.955  270.427 21.322 1.00 37.29 ?  71  HIS A NE2 1 
ATOM   535   N  N   . GLY A  1 73  ? 38.116  270.655 25.380 1.00 36.05 ?  72  GLY A N   1 
ATOM   536   C  CA  . GLY A  1 73  ? 39.544  270.655 25.614 1.00 33.23 ?  72  GLY A CA  1 
ATOM   537   C  C   . GLY A  1 73  ? 40.169  269.520 24.835 1.00 35.36 ?  72  GLY A C   1 
ATOM   538   O  O   . GLY A  1 73  ? 39.493  268.807 24.089 1.00 36.99 ?  72  GLY A O   1 
ATOM   539   N  N   . GLY A  1 74  ? 41.480  269.377 24.989 1.00 36.22 ?  73  GLY A N   1 
ATOM   540   C  CA  . GLY A  1 74  ? 42.175  268.231 24.458 1.00 34.42 ?  73  GLY A CA  1 
ATOM   541   C  C   . GLY A  1 74  ? 42.070  267.105 25.465 1.00 40.15 ?  73  GLY A C   1 
ATOM   542   O  O   . GLY A  1 74  ? 41.810  267.341 26.648 1.00 35.76 ?  73  GLY A O   1 
ATOM   543   N  N   . PRO A  1 75  ? 42.273  265.860 25.017 1.00 37.68 ?  74  PRO A N   1 
ATOM   544   C  CA  . PRO A  1 75  ? 42.153  264.719 25.941 1.00 37.26 ?  74  PRO A CA  1 
ATOM   545   C  C   . PRO A  1 75  ? 43.046  264.820 27.169 1.00 43.56 ?  74  PRO A C   1 
ATOM   546   O  O   . PRO A  1 75  ? 42.678  264.302 28.230 1.00 38.21 ?  74  PRO A O   1 
ATOM   547   C  CB  . PRO A  1 75  ? 42.539  263.515 25.068 1.00 33.36 ?  74  PRO A CB  1 
ATOM   548   C  CG  . PRO A  1 75  ? 43.262  264.084 23.889 1.00 33.83 ?  74  PRO A CG  1 
ATOM   549   C  CD  . PRO A  1 75  ? 42.668  265.441 23.662 1.00 32.68 ?  74  PRO A CD  1 
ATOM   550   N  N   . LYS A  1 76  ? 44.205  265.475 27.068 1.00 42.70 ?  75  LYS A N   1 
ATOM   551   C  CA  . LYS A  1 76  ? 45.100  265.587 28.214 1.00 43.91 ?  75  LYS A CA  1 
ATOM   552   C  C   . LYS A  1 76  ? 44.726  266.721 29.169 1.00 39.22 ?  75  LYS A C   1 
ATOM   553   O  O   . LYS A  1 76  ? 45.290  266.793 30.265 1.00 43.75 ?  75  LYS A O   1 
ATOM   554   C  CB  . LYS A  1 76  ? 46.535  265.758 27.724 1.00 44.94 ?  75  LYS A CB  1 
ATOM   555   C  CG  . LYS A  1 76  ? 47.043  264.548 26.953 1.00 45.05 ?  75  LYS A CG  1 
ATOM   556   C  CD  . LYS A  1 76  ? 48.192  264.937 26.036 1.00 54.34 ?  75  LYS A CD  1 
ATOM   557   C  CE  . LYS A  1 76  ? 49.515  264.990 26.807 1.00 62.54 ?  75  LYS A CE  1 
ATOM   558   N  NZ  . LYS A  1 76  ? 50.314  266.199 26.434 1.00 53.35 ?  75  LYS A NZ  1 
ATOM   559   N  N   . ASP A  1 77  ? 43.774  267.579 28.813 1.00 39.53 ?  76  ASP A N   1 
ATOM   560   C  CA  . ASP A  1 77  ? 43.362  268.649 29.712 1.00 41.32 ?  76  ASP A CA  1 
ATOM   561   C  C   . ASP A  1 77  ? 42.434  268.133 30.802 1.00 46.76 ?  76  ASP A C   1 
ATOM   562   O  O   . ASP A  1 77  ? 41.685  267.174 30.607 1.00 41.75 ?  76  ASP A O   1 
ATOM   563   C  CB  . ASP A  1 77  ? 42.653  269.754 28.940 1.00 38.74 ?  76  ASP A CB  1 
ATOM   564   C  CG  . ASP A  1 77  ? 43.567  270.437 27.968 1.00 45.66 ?  76  ASP A CG  1 
ATOM   565   O  OD1 . ASP A  1 77  ? 44.715  270.731 28.371 1.00 46.61 ?  76  ASP A OD1 1 
ATOM   566   O  OD2 . ASP A  1 77  ? 43.155  270.643 26.799 1.00 47.80 ?  76  ASP A OD2 1 
ATOM   567   N  N   . GLU A  1 78  ? 42.474  268.799 31.962 1.00 42.96 ?  77  GLU A N   1 
ATOM   568   C  CA  . GLU A  1 78  ? 41.489  268.515 32.996 1.00 41.23 ?  77  GLU A CA  1 
ATOM   569   C  C   . GLU A  1 78  ? 40.130  269.076 32.614 1.00 44.13 ?  77  GLU A C   1 
ATOM   570   O  O   . GLU A  1 78  ? 39.099  268.412 32.791 1.00 43.76 ?  77  GLU A O   1 
ATOM   571   C  CB  . GLU A  1 78  ? 41.939  269.097 34.333 1.00 49.12 ?  77  GLU A CB  1 
ATOM   572   C  CG  . GLU A  1 78  ? 40.939  268.875 35.444 1.00 55.58 ?  77  GLU A CG  1 
ATOM   573   C  CD  . GLU A  1 78  ? 40.933  267.428 35.915 1.00 74.33 ?  77  GLU A CD  1 
ATOM   574   O  OE1 . GLU A  1 78  ? 39.910  266.983 36.493 1.00 80.01 ?  77  GLU A OE1 1 
ATOM   575   O  OE2 . GLU A  1 78  ? 41.958  266.734 35.695 1.00 74.32 ?  77  GLU A OE2 1 
ATOM   576   N  N   . GLU A  1 79  ? 40.109  270.303 32.102 1.00 36.55 ?  78  GLU A N   1 
ATOM   577   C  CA  . GLU A  1 79  ? 38.900  270.915 31.559 1.00 42.29 ?  78  GLU A CA  1 
ATOM   578   C  C   . GLU A  1 79  ? 38.679  270.361 30.158 1.00 40.67 ?  78  GLU A C   1 
ATOM   579   O  O   . GLU A  1 79  ? 39.255  270.848 29.186 1.00 41.07 ?  78  GLU A O   1 
ATOM   580   C  CB  . GLU A  1 79  ? 39.023  272.434 31.539 1.00 37.97 ?  78  GLU A CB  1 
ATOM   581   C  CG  . GLU A  1 79  ? 37.788  273.129 31.009 1.00 42.39 ?  78  GLU A CG  1 
ATOM   582   C  CD  . GLU A  1 79  ? 36.666  273.167 32.041 1.00 52.69 ?  78  GLU A CD  1 
ATOM   583   O  OE1 . GLU A  1 79  ? 36.896  272.724 33.190 1.00 55.20 ?  78  GLU A OE1 1 
ATOM   584   O  OE2 . GLU A  1 79  ? 35.550  273.629 31.703 1.00 48.66 ?  78  GLU A OE2 1 
ATOM   585   N  N   . ARG A  1 80  ? 37.851  269.323 30.052 1.00 43.04 ?  79  ARG A N   1 
ATOM   586   C  CA  . ARG A  1 80  ? 37.528  268.723 28.763 1.00 36.69 ?  79  ARG A CA  1 
ATOM   587   C  C   . ARG A  1 80  ? 36.143  268.106 28.846 1.00 40.56 ?  79  ARG A C   1 
ATOM   588   O  O   . ARG A  1 80  ? 35.642  267.801 29.929 1.00 39.51 ?  79  ARG A O   1 
ATOM   589   C  CB  . ARG A  1 80  ? 38.553  267.653 28.372 1.00 35.33 ?  79  ARG A CB  1 
ATOM   590   C  CG  . ARG A  1 80  ? 38.590  266.484 29.351 1.00 36.11 ?  79  ARG A CG  1 
ATOM   591   C  CD  . ARG A  1 80  ? 39.463  265.361 28.845 1.00 37.56 ?  79  ARG A CD  1 
ATOM   592   N  NE  . ARG A  1 80  ? 38.686  264.380 28.086 1.00 32.88 ?  79  ARG A NE  1 
ATOM   593   C  CZ  . ARG A  1 80  ? 39.147  263.188 27.738 1.00 32.11 ?  79  ARG A CZ  1 
ATOM   594   N  NH1 . ARG A  1 80  ? 40.385  262.817 28.024 1.00 32.22 ?  79  ARG A NH1 1 
ATOM   595   N  NH2 . ARG A  1 80  ? 38.353  262.348 27.075 1.00 35.39 ?  79  ARG A NH2 1 
ATOM   596   N  N   . HIS A  1 81  ? 35.516  267.942 27.690 1.00 39.81 ?  80  HIS A N   1 
ATOM   597   C  CA  . HIS A  1 81  ? 34.359  267.062 27.603 1.00 36.22 ?  80  HIS A CA  1 
ATOM   598   C  C   . HIS A  1 81  ? 34.818  265.619 27.769 1.00 33.78 ?  80  HIS A C   1 
ATOM   599   O  O   . HIS A  1 81  ? 35.936  265.259 27.390 1.00 32.46 ?  80  HIS A O   1 
ATOM   600   C  CB  . HIS A  1 81  ? 33.660  267.242 26.256 1.00 34.60 ?  80  HIS A CB  1 
ATOM   601   C  CG  . HIS A  1 81  ? 33.185  268.640 26.000 1.00 37.76 ?  80  HIS A CG  1 
ATOM   602   N  ND1 . HIS A  1 81  ? 33.222  269.223 24.752 1.00 37.26 ?  80  HIS A ND1 1 
ATOM   603   C  CD2 . HIS A  1 81  ? 32.632  269.557 26.826 1.00 36.48 ?  80  HIS A CD2 1 
ATOM   604   C  CE1 . HIS A  1 81  ? 32.715  270.439 24.822 1.00 34.97 ?  80  HIS A CE1 1 
ATOM   605   N  NE2 . HIS A  1 81  ? 32.341  270.663 26.069 1.00 34.69 ?  80  HIS A NE2 1 
ATOM   606   N  N   . VAL A  1 82  ? 33.954  264.783 28.356 1.00 34.59 ?  81  VAL A N   1 
ATOM   607   C  CA  . VAL A  1 82  ? 34.269  263.356 28.400 1.00 30.19 ?  81  VAL A CA  1 
ATOM   608   C  C   . VAL A  1 82  ? 34.517  262.834 26.989 1.00 28.57 ?  81  VAL A C   1 
ATOM   609   O  O   . VAL A  1 82  ? 35.440  262.048 26.753 1.00 29.76 ?  81  VAL A O   1 
ATOM   610   C  CB  . VAL A  1 82  ? 33.155  262.565 29.117 1.00 36.42 ?  81  VAL A CB  1 
ATOM   611   C  CG1 . VAL A  1 82  ? 33.339  261.085 28.876 1.00 30.85 ?  81  VAL A CG1 1 
ATOM   612   C  CG2 . VAL A  1 82  ? 33.200  262.816 30.625 1.00 30.48 ?  81  VAL A CG2 1 
ATOM   613   N  N   . GLY A  1 83  ? 33.723  263.291 26.023 1.00 27.24 ?  82  GLY A N   1 
ATOM   614   C  CA  . GLY A  1 83  ? 33.897  262.817 24.661 1.00 33.05 ?  82  GLY A CA  1 
ATOM   615   C  C   . GLY A  1 83  ? 35.075  263.403 23.896 1.00 34.48 ?  82  GLY A C   1 
ATOM   616   O  O   . GLY A  1 83  ? 35.216  263.095 22.709 1.00 32.45 ?  82  GLY A O   1 
ATOM   617   N  N   . ASP A  1 84  ? 35.937  264.203 24.539 1.00 31.82 ?  83  ASP A N   1 
ATOM   618   C  CA  . ASP A  1 84  ? 37.027  264.923 23.866 1.00 31.73 ?  83  ASP A CA  1 
ATOM   619   C  C   . ASP A  1 84  ? 38.213  263.993 23.680 1.00 31.51 ?  83  ASP A C   1 
ATOM   620   O  O   . ASP A  1 84  ? 39.099  263.915 24.526 1.00 33.82 ?  83  ASP A O   1 
ATOM   621   C  CB  . ASP A  1 84  ? 37.442  266.149 24.675 1.00 29.65 ?  83  ASP A CB  1 
ATOM   622   C  CG  . ASP A  1 84  ? 36.492  267.309 24.501 1.00 33.87 ?  83  ASP A CG  1 
ATOM   623   O  OD1 . ASP A  1 84  ? 35.671  267.233 23.573 1.00 33.09 ?  83  ASP A OD1 1 
ATOM   624   O  OD2 . ASP A  1 84  ? 36.550  268.287 25.287 1.00 34.87 ?  83  ASP A OD2 1 
ATOM   625   N  N   . LEU A  1 85  ? 38.245  263.281 22.559 1.00 30.49 ?  84  LEU A N   1 
ATOM   626   C  CA  . LEU A  1 85  ? 39.345  262.371 22.264 1.00 32.01 ?  84  LEU A CA  1 
ATOM   627   C  C   . LEU A  1 85  ? 40.406  263.004 21.360 1.00 32.17 ?  84  LEU A C   1 
ATOM   628   O  O   . LEU A  1 85  ? 41.313  262.302 20.908 1.00 33.63 ?  84  LEU A O   1 
ATOM   629   C  CB  . LEU A  1 85  ? 38.819  261.079 21.623 1.00 32.55 ?  84  LEU A CB  1 
ATOM   630   C  CG  . LEU A  1 85  ? 37.951  260.180 22.524 1.00 34.73 ?  84  LEU A CG  1 
ATOM   631   C  CD1 . LEU A  1 85  ? 37.475  258.922 21.775 1.00 34.71 ?  84  LEU A CD1 1 
ATOM   632   C  CD2 . LEU A  1 85  ? 38.647  259.826 23.846 1.00 30.19 ?  84  LEU A CD2 1 
ATOM   633   N  N   . GLY A  1 86  ? 40.311  264.305 21.087 1.00 32.60 ?  85  GLY A N   1 
ATOM   634   C  CA  . GLY A  1 86  ? 41.385  264.991 20.381 1.00 34.26 ?  85  GLY A CA  1 
ATOM   635   C  C   . GLY A  1 86  ? 41.283  264.799 18.888 1.00 32.91 ?  85  GLY A C   1 
ATOM   636   O  O   . GLY A  1 86  ? 40.204  264.941 18.303 1.00 33.15 ?  85  GLY A O   1 
ATOM   637   N  N   . ASN A  1 87  ? 42.409  264.453 18.267 1.00 32.76 ?  86  ASN A N   1 
ATOM   638   C  CA  . ASN A  1 87  ? 42.515  264.334 16.820 1.00 33.06 ?  86  ASN A CA  1 
ATOM   639   C  C   . ASN A  1 87  ? 43.009  262.951 16.433 1.00 32.56 ?  86  ASN A C   1 
ATOM   640   O  O   . ASN A  1 87  ? 43.715  262.286 17.198 1.00 33.78 ?  86  ASN A O   1 
ATOM   641   C  CB  . ASN A  1 87  ? 43.508  265.355 16.227 1.00 35.52 ?  86  ASN A CB  1 
ATOM   642   C  CG  . ASN A  1 87  ? 42.970  266.755 16.208 1.00 36.10 ?  86  ASN A CG  1 
ATOM   643   O  OD1 . ASN A  1 87  ? 41.997  267.057 15.513 1.00 37.50 ?  86  ASN A OD1 1 
ATOM   644   N  ND2 . ASN A  1 87  ? 43.616  267.638 16.962 1.00 35.37 ?  86  ASN A ND2 1 
ATOM   645   N  N   . VAL A  1 88  ? 42.669  262.550 15.210 1.00 30.64 ?  87  VAL A N   1 
ATOM   646   C  CA  . VAL A  1 88  ? 43.353  261.454 14.542 1.00 32.48 ?  87  VAL A CA  1 
ATOM   647   C  C   . VAL A  1 88  ? 44.001  262.008 13.277 1.00 34.16 ?  87  VAL A C   1 
ATOM   648   O  O   . VAL A  1 88  ? 43.526  262.986 12.696 1.00 32.04 ?  87  VAL A O   1 
ATOM   649   C  CB  . VAL A  1 88  ? 42.403  260.281 14.211 1.00 30.67 ?  87  VAL A CB  1 
ATOM   650   C  CG1 . VAL A  1 88  ? 41.914  259.603 15.512 1.00 30.40 ?  87  VAL A CG1 1 
ATOM   651   C  CG2 . VAL A  1 88  ? 41.242  260.754 13.352 1.00 30.33 ?  87  VAL A CG2 1 
ATOM   652   N  N   . THR A  1 89  ? 45.101  261.385 12.861 1.00 35.03 ?  88  THR A N   1 
ATOM   653   C  CA  . THR A  1 89  ? 45.886  261.853 11.724 1.00 38.65 ?  88  THR A CA  1 
ATOM   654   C  C   . THR A  1 89  ? 45.751  260.882 10.563 1.00 37.61 ?  88  THR A C   1 
ATOM   655   O  O   . THR A  1 89  ? 46.093  259.703 10.690 1.00 36.33 ?  88  THR A O   1 
ATOM   656   C  CB  . THR A  1 89  ? 47.360  262.008 12.091 1.00 39.48 ?  88  THR A CB  1 
ATOM   657   O  OG1 . THR A  1 89  ? 47.473  262.755 13.309 1.00 37.57 ?  88  THR A OG1 1 
ATOM   658   C  CG2 . THR A  1 89  ? 48.098  262.739 10.985 1.00 42.56 ?  88  THR A CG2 1 
ATOM   659   N  N   . ALA A  1 90  ? 45.266  261.385 9.436  1.00 36.36 ?  89  ALA A N   1 
ATOM   660   C  CA  . ALA A  1 90  ? 45.215  260.616 8.207  1.00 39.04 ?  89  ALA A CA  1 
ATOM   661   C  C   . ALA A  1 90  ? 46.505  260.843 7.430  1.00 41.15 ?  89  ALA A C   1 
ATOM   662   O  O   . ALA A  1 90  ? 47.010  261.967 7.355  1.00 42.73 ?  89  ALA A O   1 
ATOM   663   C  CB  . ALA A  1 90  ? 44.007  261.025 7.364  1.00 37.88 ?  89  ALA A CB  1 
ATOM   664   N  N   . ASP A  1 91  ? 47.040  259.773 6.866  1.00 41.77 ?  90  ASP A N   1 
ATOM   665   C  CA  . ASP A  1 91  ? 48.309  259.854 6.165  1.00 45.83 ?  90  ASP A CA  1 
ATOM   666   C  C   . ASP A  1 91  ? 48.078  260.292 4.718  1.00 49.88 ?  90  ASP A C   1 
ATOM   667   O  O   . ASP A  1 91  ? 46.987  260.731 4.337  1.00 42.34 ?  90  ASP A O   1 
ATOM   668   C  CB  . ASP A  1 91  ? 49.049  258.523 6.256  1.00 38.05 ?  90  ASP A CB  1 
ATOM   669   C  CG  . ASP A  1 91  ? 48.279  257.349 5.620  1.00 41.12 ?  90  ASP A CG  1 
ATOM   670   O  OD1 . ASP A  1 91  ? 47.389  257.552 4.770  1.00 44.45 ?  90  ASP A OD1 1 
ATOM   671   O  OD2 . ASP A  1 91  ? 48.599  256.193 5.967  1.00 41.87 ?  90  ASP A OD2 1 
ATOM   672   N  N   . LYS A  1 92  ? 49.122  260.160 3.893  1.00 52.92 ?  91  LYS A N   1 
ATOM   673   C  CA  . LYS A  1 92  ? 49.045  260.595 2.504  1.00 52.55 ?  91  LYS A CA  1 
ATOM   674   C  C   . LYS A  1 92  ? 48.080  259.748 1.685  1.00 49.17 ?  91  LYS A C   1 
ATOM   675   O  O   . LYS A  1 92  ? 47.556  260.232 0.675  1.00 55.75 ?  91  LYS A O   1 
ATOM   676   C  CB  . LYS A  1 92  ? 50.440  260.565 1.872  1.00 53.83 ?  91  LYS A CB  1 
ATOM   677   C  CG  . LYS A  1 92  ? 51.146  259.208 1.991  1.00 58.50 ?  91  LYS A CG  1 
ATOM   678   C  CD  . LYS A  1 92  ? 52.444  259.152 1.186  1.00 61.02 ?  91  LYS A CD  1 
ATOM   679   C  CE  . LYS A  1 92  ? 52.396  260.083 -0.027 1.00 66.67 ?  91  LYS A CE  1 
ATOM   680   N  NZ  . LYS A  1 92  ? 53.315  259.645 -1.122 1.00 70.65 ?  91  LYS A NZ  1 
ATOM   681   N  N   . ASP A  1 93  ? 47.838  258.501 2.091  1.00 45.78 ?  92  ASP A N   1 
ATOM   682   C  CA  . ASP A  1 93  ? 46.896  257.617 1.415  1.00 46.16 ?  92  ASP A CA  1 
ATOM   683   C  C   . ASP A  1 93  ? 45.454  257.776 1.906  1.00 43.54 ?  92  ASP A C   1 
ATOM   684   O  O   . ASP A  1 93  ? 44.594  256.979 1.516  1.00 50.01 ?  92  ASP A O   1 
ATOM   685   C  CB  . ASP A  1 93  ? 47.334  256.160 1.581  1.00 49.56 ?  92  ASP A CB  1 
ATOM   686   C  CG  . ASP A  1 93  ? 48.667  255.870 0.914  1.00 58.81 ?  92  ASP A CG  1 
ATOM   687   O  OD1 . ASP A  1 93  ? 48.971  256.500 -0.128 1.00 63.15 ?  92  ASP A OD1 1 
ATOM   688   O  OD2 . ASP A  1 93  ? 49.418  255.021 1.442  1.00 65.55 ?  92  ASP A OD2 1 
ATOM   689   N  N   . GLY A  1 94  ? 45.173  258.775 2.741  1.00 38.58 ?  93  GLY A N   1 
ATOM   690   C  CA  . GLY A  1 94  ? 43.846  258.961 3.302  1.00 44.75 ?  93  GLY A CA  1 
ATOM   691   C  C   . GLY A  1 94  ? 43.451  258.033 4.438  1.00 38.58 ?  93  GLY A C   1 
ATOM   692   O  O   . GLY A  1 94  ? 42.263  257.944 4.760  1.00 39.85 ?  93  GLY A O   1 
ATOM   693   N  N   . VAL A  1 95  ? 44.402  257.351 5.067  1.00 36.92 ?  94  VAL A N   1 
ATOM   694   C  CA  . VAL A  1 95  ? 44.112  256.362 6.099  1.00 37.37 ?  94  VAL A CA  1 
ATOM   695   C  C   . VAL A  1 95  ? 44.588  256.876 7.450  1.00 37.56 ?  94  VAL A C   1 
ATOM   696   O  O   . VAL A  1 95  ? 45.761  257.239 7.615  1.00 41.67 ?  94  VAL A O   1 
ATOM   697   C  CB  . VAL A  1 95  ? 44.763  255.011 5.773  1.00 39.32 ?  94  VAL A CB  1 
ATOM   698   C  CG1 . VAL A  1 95  ? 44.583  254.056 6.945  1.00 37.60 ?  94  VAL A CG1 1 
ATOM   699   C  CG2 . VAL A  1 95  ? 44.166  254.433 4.462  1.00 39.38 ?  94  VAL A CG2 1 
ATOM   700   N  N   . ALA A  1 96  ? 43.686  256.890 8.424  1.00 36.55 ?  95  ALA A N   1 
ATOM   701   C  CA  . ALA A  1 96  ? 44.041  257.197 9.807  1.00 33.93 ?  95  ALA A CA  1 
ATOM   702   C  C   . ALA A  1 96  ? 44.065  255.881 10.580 1.00 36.60 ?  95  ALA A C   1 
ATOM   703   O  O   . ALA A  1 96  ? 43.016  255.272 10.818 1.00 33.73 ?  95  ALA A O   1 
ATOM   704   C  CB  . ALA A  1 96  ? 43.061  258.202 10.412 1.00 31.04 ?  95  ALA A CB  1 
ATOM   705   N  N   . ASP A  1 97  ? 45.260  255.422 10.939 1.00 32.72 ?  96  ASP A N   1 
ATOM   706   C  CA  . ASP A  1 97  ? 45.409  254.218 11.749 1.00 33.27 ?  96  ASP A CA  1 
ATOM   707   C  C   . ASP A  1 97  ? 45.326  254.639 13.211 1.00 34.91 ?  96  ASP A C   1 
ATOM   708   O  O   . ASP A  1 97  ? 46.333  254.923 13.858 1.00 37.63 ?  96  ASP A O   1 
ATOM   709   C  CB  . ASP A  1 97  ? 46.715  253.511 11.433 1.00 40.47 ?  96  ASP A CB  1 
ATOM   710   C  CG  . ASP A  1 97  ? 46.670  252.777 10.099 1.00 51.73 ?  96  ASP A CG  1 
ATOM   711   O  OD1 . ASP A  1 97  ? 45.578  252.301 9.704  1.00 46.64 ?  96  ASP A OD1 1 
ATOM   712   O  OD2 . ASP A  1 97  ? 47.725  252.702 9.432  1.00 60.34 ?  96  ASP A OD2 1 
ATOM   713   N  N   . VAL A  1 98  ? 44.105  254.662 13.742 1.00 30.22 ?  97  VAL A N   1 
ATOM   714   C  CA  . VAL A  1 98  ? 43.871  255.232 15.063 1.00 32.25 ?  97  VAL A CA  1 
ATOM   715   C  C   . VAL A  1 98  ? 44.527  254.393 16.146 1.00 32.21 ?  97  VAL A C   1 
ATOM   716   O  O   . VAL A  1 98  ? 44.475  253.156 16.130 1.00 35.41 ?  97  VAL A O   1 
ATOM   717   C  CB  . VAL A  1 98  ? 42.367  255.373 15.317 1.00 28.69 ?  97  VAL A CB  1 
ATOM   718   C  CG1 . VAL A  1 98  ? 42.128  256.009 16.684 1.00 30.11 ?  97  VAL A CG1 1 
ATOM   719   C  CG2 . VAL A  1 98  ? 41.737  256.182 14.192 1.00 30.06 ?  97  VAL A CG2 1 
ATOM   720   N  N   . SER A  1 99  ? 45.143  255.078 17.112 1.00 35.56 ?  98  SER A N   1 
ATOM   721   C  CA  . SER A  1 99  ? 45.689  254.433 18.306 1.00 34.18 ?  98  SER A CA  1 
ATOM   722   C  C   . SER A  1 99  ? 45.656  255.467 19.420 1.00 37.32 ?  98  SER A C   1 
ATOM   723   O  O   . SER A  1 99  ? 46.487  256.376 19.462 1.00 40.20 ?  98  SER A O   1 
ATOM   724   C  CB  . SER A  1 99  ? 47.097  253.910 18.078 1.00 42.43 ?  98  SER A CB  1 
ATOM   725   O  OG  . SER A  1 99  ? 47.485  253.130 19.189 1.00 44.97 ?  98  SER A OG  1 
ATOM   726   N  N   . ILE A  1 100 ? 44.687  255.326 20.300 1.00 34.06 ?  99  ILE A N   1 
ATOM   727   C  CA  . ILE A  1 100 ? 44.426  256.267 21.372 1.00 31.00 ?  99  ILE A CA  1 
ATOM   728   C  C   . ILE A  1 100 ? 44.243  255.454 22.642 1.00 34.36 ?  99  ILE A C   1 
ATOM   729   O  O   . ILE A  1 100 ? 43.664  254.363 22.605 1.00 33.66 ?  99  ILE A O   1 
ATOM   730   C  CB  . ILE A  1 100 ? 43.169  257.112 21.077 1.00 34.00 ?  99  ILE A CB  1 
ATOM   731   C  CG1 . ILE A  1 100 ? 43.477  258.193 20.047 1.00 34.69 ?  99  ILE A CG1 1 
ATOM   732   C  CG2 . ILE A  1 100 ? 42.587  257.714 22.366 1.00 33.45 ?  99  ILE A CG2 1 
ATOM   733   C  CD1 . ILE A  1 100 ? 42.278  259.045 19.691 1.00 32.15 ?  99  ILE A CD1 1 
ATOM   734   N  N   . GLU A  1 101 ? 44.750  255.961 23.757 1.00 35.41 ?  100 GLU A N   1 
ATOM   735   C  CA  . GLU A  1 101 ? 44.402  255.430 25.067 1.00 33.67 ?  100 GLU A CA  1 
ATOM   736   C  C   . GLU A  1 101 ? 43.862  256.569 25.908 1.00 36.70 ?  100 GLU A C   1 
ATOM   737   O  O   . GLU A  1 101 ? 44.509  257.612 26.030 1.00 38.08 ?  100 GLU A O   1 
ATOM   738   C  CB  . GLU A  1 101 ? 45.596  254.767 25.756 1.00 37.25 ?  100 GLU A CB  1 
ATOM   739   C  CG  . GLU A  1 101 ? 45.201  254.145 27.082 1.00 44.33 ?  100 GLU A CG  1 
ATOM   740   C  CD  . GLU A  1 101 ? 46.378  253.598 27.888 1.00 61.56 ?  100 GLU A CD  1 
ATOM   741   O  OE1 . GLU A  1 101 ? 46.975  252.594 27.420 1.00 53.19 ?  100 GLU A OE1 1 
ATOM   742   O  OE2 . GLU A  1 101 ? 46.684  254.163 28.984 1.00 49.53 ?  100 GLU A OE2 1 
ATOM   743   N  N   . ASP A  1 102 ? 42.670  256.386 26.465 1.00 33.26 ?  101 ASP A N   1 
ATOM   744   C  CA  . ASP A  1 102 ? 42.027  257.463 27.202 1.00 31.83 ?  101 ASP A CA  1 
ATOM   745   C  C   . ASP A  1 102 ? 41.514  256.958 28.539 1.00 39.26 ?  101 ASP A C   1 
ATOM   746   O  O   . ASP A  1 102 ? 40.975  255.852 28.628 1.00 32.07 ?  101 ASP A O   1 
ATOM   747   C  CB  . ASP A  1 102 ? 40.872  258.070 26.409 1.00 33.31 ?  101 ASP A CB  1 
ATOM   748   C  CG  . ASP A  1 102 ? 40.421  259.391 26.987 1.00 38.14 ?  101 ASP A CG  1 
ATOM   749   O  OD1 . ASP A  1 102 ? 41.075  260.418 26.711 1.00 41.32 ?  101 ASP A OD1 1 
ATOM   750   O  OD2 . ASP A  1 102 ? 39.417  259.409 27.740 1.00 39.10 ?  101 ASP A OD2 1 
ATOM   751   N  N   . SER A  1 103 ? 41.676  257.771 29.582 1.00 32.95 ?  102 SER A N   1 
ATOM   752   C  CA  . SER A  1 103 ? 41.285  257.350 30.916 1.00 35.97 ?  102 SER A CA  1 
ATOM   753   C  C   . SER A  1 103 ? 40.091  258.133 31.440 1.00 33.05 ?  102 SER A C   1 
ATOM   754   O  O   . SER A  1 103 ? 39.755  258.013 32.620 1.00 34.60 ?  102 SER A O   1 
ATOM   755   C  CB  . SER A  1 103 ? 42.477  257.443 31.872 1.00 34.33 ?  102 SER A CB  1 
ATOM   756   O  OG  . SER A  1 103 ? 42.900  258.782 32.004 1.00 41.54 ?  102 SER A OG  1 
ATOM   757   N  N   . VAL A  1 104 ? 39.417  258.889 30.582 1.00 33.05 ?  103 VAL A N   1 
ATOM   758   C  CA  . VAL A  1 104 ? 38.224  259.634 30.966 1.00 34.27 ?  103 VAL A CA  1 
ATOM   759   C  C   . VAL A  1 104 ? 36.950  258.977 30.438 1.00 38.87 ?  103 VAL A C   1 
ATOM   760   O  O   . VAL A  1 104 ? 35.944  258.911 31.152 1.00 32.48 ?  103 VAL A O   1 
ATOM   761   C  CB  . VAL A  1 104 ? 38.338  261.100 30.494 1.00 32.81 ?  103 VAL A CB  1 
ATOM   762   C  CG1 . VAL A  1 104 ? 37.006  261.821 30.680 1.00 33.27 ?  103 VAL A CG1 1 
ATOM   763   C  CG2 . VAL A  1 104 ? 39.454  261.809 31.277 1.00 33.26 ?  103 VAL A CG2 1 
ATOM   764   N  N   . ILE A  1 105 ? 36.964  258.497 29.186 1.00 32.04 ?  104 ILE A N   1 
ATOM   765   C  CA  . ILE A  1 105 ? 35.847  257.698 28.694 1.00 29.08 ?  104 ILE A CA  1 
ATOM   766   C  C   . ILE A  1 105 ? 35.850  256.349 29.405 1.00 32.26 ?  104 ILE A C   1 
ATOM   767   O  O   . ILE A  1 105 ? 36.886  255.874 29.890 1.00 34.12 ?  104 ILE A O   1 
ATOM   768   C  CB  . ILE A  1 105 ? 35.909  257.507 27.165 1.00 30.58 ?  104 ILE A CB  1 
ATOM   769   C  CG1 . ILE A  1 105 ? 37.235  256.871 26.759 1.00 25.53 ?  104 ILE A CG1 1 
ATOM   770   C  CG2 . ILE A  1 105 ? 35.681  258.834 26.424 1.00 33.47 ?  104 ILE A CG2 1 
ATOM   771   C  CD1 . ILE A  1 105 ? 37.208  256.186 25.390 1.00 28.51 ?  104 ILE A CD1 1 
ATOM   772   N  N   . SER A  1 106 ? 34.687  255.707 29.444 1.00 28.52 ?  105 SER A N   1 
ATOM   773   C  CA  . SER A  1 106 ? 34.590  254.362 29.994 1.00 29.41 ?  105 SER A CA  1 
ATOM   774   C  C   . SER A  1 106 ? 33.593  253.565 29.171 1.00 26.06 ?  105 SER A C   1 
ATOM   775   O  O   . SER A  1 106 ? 32.731  254.129 28.500 1.00 30.45 ?  105 SER A O   1 
ATOM   776   C  CB  . SER A  1 106 ? 34.162  254.382 31.474 1.00 27.56 ?  105 SER A CB  1 
ATOM   777   O  OG  . SER A  1 106 ? 34.434  253.135 32.109 1.00 33.09 ?  105 SER A OG  1 
ATOM   778   N  N   . LEU A  1 107 ? 33.713  252.241 29.230 1.00 31.46 ?  106 LEU A N   1 
ATOM   779   C  CA  . LEU A  1 107 ? 32.700  251.367 28.661 1.00 29.88 ?  106 LEU A CA  1 
ATOM   780   C  C   . LEU A  1 107 ? 31.652  250.958 29.693 1.00 36.80 ?  106 LEU A C   1 
ATOM   781   O  O   . LEU A  1 107 ? 30.825  250.101 29.396 1.00 36.08 ?  106 LEU A O   1 
ATOM   782   C  CB  . LEU A  1 107 ? 33.351  250.122 28.039 1.00 28.11 ?  106 LEU A CB  1 
ATOM   783   C  CG  . LEU A  1 107 ? 34.377  250.448 26.940 1.00 32.45 ?  106 LEU A CG  1 
ATOM   784   C  CD1 . LEU A  1 107 ? 34.852  249.214 26.179 1.00 28.93 ?  106 LEU A CD1 1 
ATOM   785   C  CD2 . LEU A  1 107 ? 33.810  251.460 25.964 1.00 30.28 ?  106 LEU A CD2 1 
ATOM   786   N  N   . SER A  1 108 ? 31.673  251.551 30.892 1.00 33.18 ?  107 SER A N   1 
ATOM   787   C  CA  . SER A  1 108 ? 30.650  251.320 31.909 1.00 39.23 ?  107 SER A CA  1 
ATOM   788   C  C   . SER A  1 108 ? 30.551  252.545 32.806 1.00 36.99 ?  107 SER A C   1 
ATOM   789   O  O   . SER A  1 108 ? 31.393  253.441 32.756 1.00 35.24 ?  107 SER A O   1 
ATOM   790   C  CB  . SER A  1 108 ? 30.959  250.082 32.755 1.00 38.82 ?  107 SER A CB  1 
ATOM   791   O  OG  . SER A  1 108 ? 32.299  250.105 33.221 1.00 36.47 ?  107 SER A OG  1 
ATOM   792   N  N   . GLY A  1 109 ? 29.509  252.573 33.646 1.00 33.16 ?  108 GLY A N   1 
ATOM   793   C  CA  . GLY A  1 109 ? 29.351  253.648 34.608 1.00 33.00 ?  108 GLY A CA  1 
ATOM   794   C  C   . GLY A  1 109 ? 28.835  254.935 33.981 1.00 46.02 ?  108 GLY A C   1 
ATOM   795   O  O   . GLY A  1 109 ? 28.288  254.953 32.878 1.00 45.14 ?  108 GLY A O   1 
ATOM   796   N  N   . ASP A  1 110 ? 29.031  256.039 34.708 1.00 44.62 ?  109 ASP A N   1 
ATOM   797   C  CA  . ASP A  1 110 ? 28.441  257.317 34.314 1.00 42.79 ?  109 ASP A CA  1 
ATOM   798   C  C   . ASP A  1 110 ? 29.116  257.910 33.081 1.00 50.15 ?  109 ASP A C   1 
ATOM   799   O  O   . ASP A  1 110 ? 28.459  258.591 32.291 1.00 46.18 ?  109 ASP A O   1 
ATOM   800   C  CB  . ASP A  1 110 ? 28.517  258.310 35.478 1.00 51.98 ?  109 ASP A CB  1 
ATOM   801   C  CG  . ASP A  1 110 ? 27.396  258.107 36.503 1.00 56.59 ?  109 ASP A CG  1 
ATOM   802   O  OD1 . ASP A  1 110 ? 26.516  257.247 36.259 1.00 59.38 ?  109 ASP A OD1 1 
ATOM   803   O  OD2 . ASP A  1 110 ? 27.398  258.804 37.549 1.00 62.89 ?  109 ASP A OD2 1 
ATOM   804   N  N   . HIS A  1 111 ? 30.417  257.698 32.904 1.00 43.67 ?  110 HIS A N   1 
ATOM   805   C  CA  . HIS A  1 111 ? 31.086  258.172 31.696 1.00 45.00 ?  110 HIS A CA  1 
ATOM   806   C  C   . HIS A  1 111 ? 30.961  257.193 30.544 1.00 41.76 ?  110 HIS A C   1 
ATOM   807   O  O   . HIS A  1 111 ? 31.775  257.256 29.609 1.00 36.98 ?  110 HIS A O   1 
ATOM   808   C  CB  . HIS A  1 111 ? 32.568  258.454 31.977 1.00 41.03 ?  110 HIS A CB  1 
ATOM   809   C  CG  . HIS A  1 111 ? 32.800  259.631 32.873 1.00 47.70 ?  110 HIS A CG  1 
ATOM   810   N  ND1 . HIS A  1 111 ? 34.062  260.070 33.222 1.00 46.91 ?  110 HIS A ND1 1 
ATOM   811   C  CD2 . HIS A  1 111 ? 31.927  260.466 33.489 1.00 47.69 ?  110 HIS A CD2 1 
ATOM   812   C  CE1 . HIS A  1 111 ? 33.956  261.117 34.021 1.00 47.26 ?  110 HIS A CE1 1 
ATOM   813   N  NE2 . HIS A  1 111 ? 32.672  261.381 34.196 1.00 43.68 ?  110 HIS A NE2 1 
ATOM   814   N  N   . CYS A  1 112 ? 29.987  256.278 30.606 1.00 37.95 ?  111 CYS A N   1 
ATOM   815   C  CA  . CYS A  1 112 ? 29.894  255.205 29.622 1.00 32.51 ?  111 CYS A CA  1 
ATOM   816   C  C   . CYS A  1 112 ? 29.582  255.748 28.235 1.00 24.74 ?  111 CYS A C   1 
ATOM   817   O  O   . CYS A  1 112 ? 28.637  256.515 28.056 1.00 32.29 ?  111 CYS A O   1 
ATOM   818   C  CB  . CYS A  1 112 ? 28.808  254.223 30.049 1.00 35.90 ?  111 CYS A CB  1 
ATOM   819   S  SG  . CYS A  1 112 ? 28.559  252.850 28.933 1.00 37.52 ?  111 CYS A SG  1 
ATOM   820   N  N   . ILE A  1 113 ? 30.354  255.323 27.234 1.00 30.27 ?  112 ILE A N   1 
ATOM   821   C  CA  . ILE A  1 113 ? 30.106  255.788 25.873 1.00 30.31 ?  112 ILE A CA  1 
ATOM   822   C  C   . ILE A  1 113 ? 29.352  254.768 25.025 1.00 33.29 ?  112 ILE A C   1 
ATOM   823   O  O   . ILE A  1 113 ? 29.061  255.056 23.858 1.00 27.76 ?  112 ILE A O   1 
ATOM   824   C  CB  . ILE A  1 113 ? 31.418  256.204 25.177 1.00 36.12 ?  112 ILE A CB  1 
ATOM   825   C  CG1 . ILE A  1 113 ? 32.394  255.023 25.110 1.00 29.99 ?  112 ILE A CG1 1 
ATOM   826   C  CG2 . ILE A  1 113 ? 32.045  257.399 25.913 1.00 31.29 ?  112 ILE A CG2 1 
ATOM   827   C  CD1 . ILE A  1 113 ? 33.573  255.243 24.156 1.00 29.83 ?  112 ILE A CD1 1 
ATOM   828   N  N   . ILE A  1 114 ? 29.010  253.597 25.571 1.00 31.05 ?  113 ILE A N   1 
ATOM   829   C  CA  . ILE A  1 114 ? 28.205  252.640 24.816 1.00 28.68 ?  113 ILE A CA  1 
ATOM   830   C  C   . ILE A  1 114 ? 26.871  253.276 24.457 1.00 26.91 ?  113 ILE A C   1 
ATOM   831   O  O   . ILE A  1 114 ? 26.193  253.850 25.317 1.00 26.60 ?  113 ILE A O   1 
ATOM   832   C  CB  . ILE A  1 114 ? 27.973  251.351 25.618 1.00 30.04 ?  113 ILE A CB  1 
ATOM   833   C  CG1 . ILE A  1 114 ? 29.280  250.616 25.873 1.00 33.59 ?  113 ILE A CG1 1 
ATOM   834   C  CG2 . ILE A  1 114 ? 27.001  250.437 24.864 1.00 27.91 ?  113 ILE A CG2 1 
ATOM   835   C  CD1 . ILE A  1 114 ? 30.191  250.704 24.749 1.00 36.18 ?  113 ILE A CD1 1 
ATOM   836   N  N   . GLY A  1 115 ? 26.480  253.165 23.188 1.00 27.45 ?  114 GLY A N   1 
ATOM   837   C  CA  . GLY A  1 115 ? 25.222  253.732 22.757 1.00 24.11 ?  114 GLY A CA  1 
ATOM   838   C  C   . GLY A  1 115 ? 25.261  255.208 22.437 1.00 27.48 ?  114 GLY A C   1 
ATOM   839   O  O   . GLY A  1 115 ? 24.200  255.812 22.231 1.00 25.82 ?  114 GLY A O   1 
ATOM   840   N  N   . ARG A  1 116 ? 26.440  255.815 22.410 1.00 27.50 ?  115 ARG A N   1 
ATOM   841   C  CA  . ARG A  1 116 ? 26.600  257.173 21.921 1.00 26.97 ?  115 ARG A CA  1 
ATOM   842   C  C   . ARG A  1 116 ? 27.253  257.087 20.545 1.00 25.82 ?  115 ARG A C   1 
ATOM   843   O  O   . ARG A  1 116 ? 27.423  255.999 19.992 1.00 31.66 ?  115 ARG A O   1 
ATOM   844   C  CB  . ARG A  1 116 ? 27.400  257.997 22.933 1.00 26.83 ?  115 ARG A CB  1 
ATOM   845   C  CG  . ARG A  1 116 ? 26.928  257.733 24.379 1.00 29.35 ?  115 ARG A CG  1 
ATOM   846   C  CD  . ARG A  1 116 ? 27.143  258.896 25.315 1.00 32.48 ?  115 ARG A CD  1 
ATOM   847   N  NE  . ARG A  1 116 ? 26.661  258.640 26.675 1.00 31.89 ?  115 ARG A NE  1 
ATOM   848   C  CZ  . ARG A  1 116 ? 25.547  259.162 27.172 1.00 27.55 ?  115 ARG A CZ  1 
ATOM   849   N  NH1 . ARG A  1 116 ? 24.747  259.918 26.429 1.00 30.65 ?  115 ARG A NH1 1 
ATOM   850   N  NH2 . ARG A  1 116 ? 25.231  258.934 28.445 1.00 31.05 ?  115 ARG A NH2 1 
ATOM   851   N  N   . THR A  1 117 ? 27.605  258.234 19.976 1.00 30.92 ?  116 THR A N   1 
ATOM   852   C  CA  . THR A  1 117 ? 28.056  258.289 18.588 1.00 27.84 ?  116 THR A CA  1 
ATOM   853   C  C   . THR A  1 117 ? 29.494  258.769 18.548 1.00 29.90 ?  116 THR A C   1 
ATOM   854   O  O   . THR A  1 117 ? 29.819  259.822 19.106 1.00 31.59 ?  116 THR A O   1 
ATOM   855   C  CB  . THR A  1 117 ? 27.176  259.222 17.766 1.00 30.13 ?  116 THR A CB  1 
ATOM   856   O  OG1 . THR A  1 117 ? 25.849  258.704 17.707 1.00 33.07 ?  116 THR A OG1 1 
ATOM   857   C  CG2 . THR A  1 117 ? 27.714  259.391 16.350 1.00 28.18 ?  116 THR A CG2 1 
ATOM   858   N  N   . LEU A  1 118 ? 30.345  257.992 17.908 1.00 25.32 ?  117 LEU A N   1 
ATOM   859   C  CA  . LEU A  1 118 ? 31.690  258.425 17.572 1.00 29.45 ?  117 LEU A CA  1 
ATOM   860   C  C   . LEU A  1 118 ? 31.629  259.182 16.248 1.00 32.95 ?  117 LEU A C   1 
ATOM   861   O  O   . LEU A  1 118 ? 31.015  258.703 15.298 1.00 32.20 ?  117 LEU A O   1 
ATOM   862   C  CB  . LEU A  1 118 ? 32.606  257.205 17.466 1.00 27.80 ?  117 LEU A CB  1 
ATOM   863   C  CG  . LEU A  1 118 ? 34.073  257.481 17.165 1.00 32.38 ?  117 LEU A CG  1 
ATOM   864   C  CD1 . LEU A  1 118 ? 34.669  258.179 18.364 1.00 29.36 ?  117 LEU A CD1 1 
ATOM   865   C  CD2 . LEU A  1 118 ? 34.830  256.182 16.845 1.00 28.26 ?  117 LEU A CD2 1 
ATOM   866   N  N   . VAL A  1 119 ? 32.241  260.367 16.185 1.00 31.78 ?  118 VAL A N   1 
ATOM   867   C  CA  . VAL A  1 119 ? 32.222  261.189 14.974 1.00 33.57 ?  118 VAL A CA  1 
ATOM   868   C  C   . VAL A  1 119 ? 33.655  261.543 14.605 1.00 33.33 ?  118 VAL A C   1 
ATOM   869   O  O   . VAL A  1 119 ? 34.455  261.900 15.476 1.00 31.16 ?  118 VAL A O   1 
ATOM   870   C  CB  . VAL A  1 119 ? 31.391  262.480 15.143 1.00 34.17 ?  118 VAL A CB  1 
ATOM   871   C  CG1 . VAL A  1 119 ? 31.482  263.359 13.873 1.00 31.93 ?  118 VAL A CG1 1 
ATOM   872   C  CG2 . VAL A  1 119 ? 29.945  262.169 15.454 1.00 29.12 ?  118 VAL A CG2 1 
ATOM   873   N  N   . VAL A  1 120 ? 33.989  261.424 13.326 1.00 30.53 ?  119 VAL A N   1 
ATOM   874   C  CA  . VAL A  1 120 ? 35.256  261.925 12.800 1.00 33.19 ?  119 VAL A CA  1 
ATOM   875   C  C   . VAL A  1 120 ? 34.950  263.173 11.977 1.00 32.54 ?  119 VAL A C   1 
ATOM   876   O  O   . VAL A  1 120 ? 34.019  263.179 11.162 1.00 32.61 ?  119 VAL A O   1 
ATOM   877   C  CB  . VAL A  1 120 ? 36.006  260.845 11.996 1.00 35.45 ?  119 VAL A CB  1 
ATOM   878   C  CG1 . VAL A  1 120 ? 35.186  260.362 10.803 1.00 32.56 ?  119 VAL A CG1 1 
ATOM   879   C  CG2 . VAL A  1 120 ? 37.384  261.356 11.564 1.00 33.12 ?  119 VAL A CG2 1 
ATOM   880   N  N   . HIS A  1 121 ? 35.703  264.245 12.223 1.00 32.18 ?  120 HIS A N   1 
ATOM   881   C  CA  . HIS A  1 121 ? 35.321  265.574 11.764 1.00 35.30 ?  120 HIS A CA  1 
ATOM   882   C  C   . HIS A  1 121 ? 36.154  266.034 10.566 1.00 30.11 ?  120 HIS A C   1 
ATOM   883   O  O   . HIS A  1 121 ? 37.178  265.450 10.203 1.00 33.40 ?  120 HIS A O   1 
ATOM   884   C  CB  . HIS A  1 121 ? 35.435  266.602 12.894 1.00 29.62 ?  120 HIS A CB  1 
ATOM   885   C  CG  . HIS A  1 121 ? 34.338  266.517 13.911 1.00 32.13 ?  120 HIS A CG  1 
ATOM   886   N  ND1 . HIS A  1 121 ? 33.230  267.336 13.885 1.00 32.28 ?  120 HIS A ND1 1 
ATOM   887   C  CD2 . HIS A  1 121 ? 34.182  265.704 14.988 1.00 29.41 ?  120 HIS A CD2 1 
ATOM   888   C  CE1 . HIS A  1 121 ? 32.437  267.031 14.900 1.00 33.93 ?  120 HIS A CE1 1 
ATOM   889   N  NE2 . HIS A  1 121 ? 32.993  266.047 15.586 1.00 33.36 ?  120 HIS A NE2 1 
ATOM   890   N  N   . GLU A  1 122 ? 35.686  267.120 9.956  1.00 35.54 ?  121 GLU A N   1 
ATOM   891   C  CA  . GLU A  1 122 ? 36.257  267.580 8.693  1.00 38.54 ?  121 GLU A CA  1 
ATOM   892   C  C   . GLU A  1 122 ? 37.637  268.214 8.892  1.00 40.02 ?  121 GLU A C   1 
ATOM   893   O  O   . GLU A  1 122 ? 38.543  268.007 8.075  1.00 39.78 ?  121 GLU A O   1 
ATOM   894   C  CB  . GLU A  1 122 ? 35.272  268.552 8.046  1.00 40.87 ?  121 GLU A CB  1 
ATOM   895   C  CG  . GLU A  1 122 ? 35.825  269.438 6.952  1.00 46.70 ?  121 GLU A CG  1 
ATOM   896   C  CD  . GLU A  1 122 ? 35.011  270.718 6.803  1.00 52.60 ?  121 GLU A CD  1 
ATOM   897   O  OE1 . GLU A  1 122 ? 34.926  271.232 5.667  1.00 63.42 ?  121 GLU A OE1 1 
ATOM   898   O  OE2 . GLU A  1 122 ? 34.450  271.202 7.822  1.00 51.60 ?  121 GLU A OE2 1 
ATOM   899   N  N   . LYS A  1 123 ? 37.828  268.943 9.993  1.00 36.61 ?  122 LYS A N   1 
ATOM   900   C  CA  . LYS A  1 123 ? 39.029  269.729 10.272 1.00 40.98 ?  122 LYS A CA  1 
ATOM   901   C  C   . LYS A  1 123 ? 39.668  269.292 11.591 1.00 42.96 ?  122 LYS A C   1 
ATOM   902   O  O   . LYS A  1 123 ? 39.123  268.478 12.338 1.00 36.21 ?  122 LYS A O   1 
ATOM   903   C  CB  . LYS A  1 123 ? 38.702  271.224 10.331 1.00 37.34 ?  122 LYS A CB  1 
ATOM   904   C  CG  . LYS A  1 123 ? 37.938  271.761 9.146  1.00 43.66 ?  122 LYS A CG  1 
ATOM   905   C  CD  . LYS A  1 123 ? 37.758  273.263 9.305  1.00 47.68 ?  122 LYS A CD  1 
ATOM   906   C  CE  . LYS A  1 123 ? 36.378  273.609 9.856  1.00 52.23 ?  122 LYS A CE  1 
ATOM   907   N  NZ  . LYS A  1 123 ? 36.410  274.752 10.824 1.00 51.66 ?  122 LYS A NZ  1 
ATOM   908   N  N   . ALA A  1 124 ? 40.829  269.875 11.887 1.00 40.40 ?  123 ALA A N   1 
ATOM   909   C  CA  . ALA A  1 124 ? 41.517  269.594 13.137 1.00 36.39 ?  123 ALA A CA  1 
ATOM   910   C  C   . ALA A  1 124 ? 40.748  270.154 14.319 1.00 36.80 ?  123 ALA A C   1 
ATOM   911   O  O   . ALA A  1 124 ? 40.090  271.195 14.237 1.00 36.94 ?  123 ALA A O   1 
ATOM   912   C  CB  . ALA A  1 124 ? 42.930  270.178 13.127 1.00 35.07 ?  123 ALA A CB  1 
ATOM   913   N  N   . ASP A  1 125 ? 40.828  269.439 15.433 1.00 34.62 ?  124 ASP A N   1 
ATOM   914   C  CA  . ASP A  1 125 ? 40.381  269.959 16.716 1.00 33.59 ?  124 ASP A CA  1 
ATOM   915   C  C   . ASP A  1 125 ? 41.472  270.876 17.260 1.00 31.92 ?  124 ASP A C   1 
ATOM   916   O  O   . ASP A  1 125 ? 42.627  270.453 17.372 1.00 32.49 ?  124 ASP A O   1 
ATOM   917   C  CB  . ASP A  1 125 ? 40.123  268.781 17.661 1.00 34.27 ?  124 ASP A CB  1 
ATOM   918   C  CG  . ASP A  1 125 ? 39.503  269.185 18.988 1.00 38.74 ?  124 ASP A CG  1 
ATOM   919   O  OD1 . ASP A  1 125 ? 39.488  270.382 19.357 1.00 35.53 ?  124 ASP A OD1 1 
ATOM   920   O  OD2 . ASP A  1 125 ? 39.031  268.266 19.693 1.00 40.85 ?  124 ASP A OD2 1 
ATOM   921   N  N   . ASP A  1 126 ? 41.121  272.123 17.600 1.00 37.44 ?  125 ASP A N   1 
ATOM   922   C  CA  . ASP A  1 126 ? 42.114  273.036 18.169 1.00 35.44 ?  125 ASP A CA  1 
ATOM   923   C  C   . ASP A  1 126 ? 42.270  272.870 19.679 1.00 41.67 ?  125 ASP A C   1 
ATOM   924   O  O   . ASP A  1 126 ? 42.985  273.655 20.312 1.00 35.94 ?  125 ASP A O   1 
ATOM   925   C  CB  . ASP A  1 126 ? 41.779  274.491 17.802 1.00 34.46 ?  125 ASP A CB  1 
ATOM   926   C  CG  . ASP A  1 126 ? 40.499  275.002 18.449 1.00 41.04 ?  125 ASP A CG  1 
ATOM   927   O  OD1 . ASP A  1 126 ? 40.034  274.443 19.471 1.00 38.59 ?  125 ASP A OD1 1 
ATOM   928   O  OD2 . ASP A  1 126 ? 39.956  276.001 17.936 1.00 38.39 ?  125 ASP A OD2 1 
ATOM   929   N  N   . LEU A  1 127 ? 41.608  271.866 20.253 1.00 36.28 ?  126 LEU A N   1 
ATOM   930   C  CA  . LEU A  1 127 ? 41.761  271.486 21.655 1.00 35.14 ?  126 LEU A CA  1 
ATOM   931   C  C   . LEU A  1 127 ? 41.381  272.625 22.588 1.00 39.17 ?  126 LEU A C   1 
ATOM   932   O  O   . LEU A  1 127 ? 41.918  272.746 23.690 1.00 40.93 ?  126 LEU A O   1 
ATOM   933   C  CB  . LEU A  1 127 ? 43.180  270.988 21.948 1.00 37.02 ?  126 LEU A CB  1 
ATOM   934   C  CG  . LEU A  1 127 ? 43.674  269.917 20.975 1.00 40.05 ?  126 LEU A CG  1 
ATOM   935   C  CD1 . LEU A  1 127 ? 45.025  269.345 21.404 1.00 42.75 ?  126 LEU A CD1 1 
ATOM   936   C  CD2 . LEU A  1 127 ? 42.639  268.798 20.824 1.00 35.49 ?  126 LEU A CD2 1 
ATOM   937   N  N   . GLY A  1 128 ? 40.430  273.450 22.160 1.00 35.47 ?  127 GLY A N   1 
ATOM   938   C  CA  . GLY A  1 128 ? 39.947  274.529 22.987 1.00 38.21 ?  127 GLY A CA  1 
ATOM   939   C  C   . GLY A  1 128 ? 40.850  275.743 23.053 1.00 44.01 ?  127 GLY A C   1 
ATOM   940   O  O   . GLY A  1 128 ? 40.543  276.679 23.802 1.00 43.66 ?  127 GLY A O   1 
ATOM   941   N  N   . LYS A  1 129 ? 41.941  275.769 22.281 1.00 40.54 ?  128 LYS A N   1 
ATOM   942   C  CA  . LYS A  1 129 ? 42.915  276.857 22.313 1.00 46.41 ?  128 LYS A CA  1 
ATOM   943   C  C   . LYS A  1 129 ? 42.807  277.797 21.108 1.00 43.80 ?  128 LYS A C   1 
ATOM   944   O  O   . LYS A  1 129 ? 43.794  278.444 20.742 1.00 45.72 ?  128 LYS A O   1 
ATOM   945   C  CB  . LYS A  1 129 ? 44.321  276.273 22.420 1.00 42.17 ?  128 LYS A CB  1 
ATOM   946   C  CG  . LYS A  1 129 ? 44.547  275.553 23.754 1.00 41.79 ?  128 LYS A CG  1 
ATOM   947   C  CD  . LYS A  1 129 ? 45.680  274.558 23.687 1.00 46.78 ?  128 LYS A CD  1 
ATOM   948   C  CE  . LYS A  1 129 ? 47.010  275.247 23.406 1.00 54.18 ?  128 LYS A CE  1 
ATOM   949   N  NZ  . LYS A  1 129 ? 48.185  274.310 23.467 1.00 57.88 ?  128 LYS A NZ  1 
ATOM   950   N  N   . GLY A  1 130 ? 41.624  277.915 20.503 1.00 38.18 ?  129 GLY A N   1 
ATOM   951   C  CA  . GLY A  1 130 ? 41.438  278.681 19.289 1.00 41.16 ?  129 GLY A CA  1 
ATOM   952   C  C   . GLY A  1 130 ? 40.901  280.092 19.451 1.00 43.52 ?  129 GLY A C   1 
ATOM   953   O  O   . GLY A  1 130 ? 40.654  280.770 18.445 1.00 42.69 ?  129 GLY A O   1 
ATOM   954   N  N   . GLY A  1 131 ? 40.694  280.552 20.678 1.00 39.01 ?  130 GLY A N   1 
ATOM   955   C  CA  . GLY A  1 131 ? 40.335  281.930 20.929 1.00 38.44 ?  130 GLY A CA  1 
ATOM   956   C  C   . GLY A  1 131 ? 38.934  282.356 20.546 1.00 47.92 ?  130 GLY A C   1 
ATOM   957   O  O   . GLY A  1 131 ? 38.590  283.524 20.766 1.00 46.61 ?  130 GLY A O   1 
ATOM   958   N  N   . ASN A  1 132 ? 38.112  281.479 19.971 1.00 47.62 ?  131 ASN A N   1 
ATOM   959   C  CA  . ASN A  1 132 ? 36.724  281.825 19.675 1.00 42.81 ?  131 ASN A CA  1 
ATOM   960   C  C   . ASN A  1 132 ? 35.768  280.969 20.493 1.00 46.84 ?  131 ASN A C   1 
ATOM   961   O  O   . ASN A  1 132 ? 36.158  279.995 21.144 1.00 49.07 ?  131 ASN A O   1 
ATOM   962   C  CB  . ASN A  1 132 ? 36.404  281.695 18.177 1.00 47.03 ?  131 ASN A CB  1 
ATOM   963   C  CG  . ASN A  1 132 ? 36.776  280.366 17.593 1.00 49.02 ?  131 ASN A CG  1 
ATOM   964   O  OD1 . ASN A  1 132 ? 37.049  279.411 18.313 1.00 48.87 ?  131 ASN A OD1 1 
ATOM   965   N  ND2 . ASN A  1 132 ? 36.762  280.285 16.258 1.00 49.18 ?  131 ASN A ND2 1 
ATOM   966   N  N   . GLU A  1 133 ? 34.488  281.350 20.457 1.00 51.08 ?  132 GLU A N   1 
ATOM   967   C  CA  . GLU A  1 133 ? 33.488  280.618 21.228 1.00 51.41 ?  132 GLU A CA  1 
ATOM   968   C  C   . GLU A  1 133 ? 33.347  279.191 20.714 1.00 49.23 ?  132 GLU A C   1 
ATOM   969   O  O   . GLU A  1 133 ? 33.137  278.254 21.496 1.00 50.80 ?  132 GLU A O   1 
ATOM   970   C  CB  . GLU A  1 133 ? 32.146  281.356 21.179 1.00 61.27 ?  132 GLU A CB  1 
ATOM   971   C  CG  . GLU A  1 133 ? 30.973  280.584 21.786 1.00 68.15 ?  132 GLU A CG  1 
ATOM   972   C  CD  . GLU A  1 133 ? 29.608  281.154 21.396 1.00 80.95 ?  132 GLU A CD  1 
ATOM   973   O  OE1 . GLU A  1 133 ? 29.233  281.060 20.202 1.00 77.51 ?  132 GLU A OE1 1 
ATOM   974   O  OE2 . GLU A  1 133 ? 28.907  281.681 22.290 1.00 84.81 ?  132 GLU A OE2 1 
ATOM   975   N  N   . GLU A  1 134 ? 33.483  279.008 19.399 1.00 48.76 ?  133 GLU A N   1 
ATOM   976   C  CA  . GLU A  1 134 ? 33.401  277.679 18.805 1.00 44.83 ?  133 GLU A CA  1 
ATOM   977   C  C   . GLU A  1 134 ? 34.493  276.761 19.339 1.00 46.86 ?  133 GLU A C   1 
ATOM   978   O  O   . GLU A  1 134 ? 34.285  275.544 19.453 1.00 41.52 ?  133 GLU A O   1 
ATOM   979   C  CB  . GLU A  1 134 ? 33.495  277.798 17.285 1.00 49.79 ?  133 GLU A CB  1 
ATOM   980   C  CG  . GLU A  1 134 ? 32.854  276.657 16.518 1.00 55.46 ?  133 GLU A CG  1 
ATOM   981   C  CD  . GLU A  1 134 ? 31.437  276.363 16.987 1.00 62.58 ?  133 GLU A CD  1 
ATOM   982   O  OE1 . GLU A  1 134 ? 31.194  275.228 17.451 1.00 60.71 ?  133 GLU A OE1 1 
ATOM   983   O  OE2 . GLU A  1 134 ? 30.573  277.265 16.895 1.00 59.87 ?  133 GLU A OE2 1 
ATOM   984   N  N   . SER A  1 135 ? 35.651  277.327 19.698 1.00 36.99 ?  134 SER A N   1 
ATOM   985   C  CA  . SER A  1 135 ? 36.755  276.507 20.185 1.00 37.44 ?  134 SER A CA  1 
ATOM   986   C  C   . SER A  1 135 ? 36.393  275.811 21.487 1.00 38.46 ?  134 SER A C   1 
ATOM   987   O  O   . SER A  1 135 ? 36.819  274.678 21.725 1.00 37.30 ?  134 SER A O   1 
ATOM   988   C  CB  . SER A  1 135 ? 38.008  277.362 20.390 1.00 39.78 ?  134 SER A CB  1 
ATOM   989   O  OG  . SER A  1 135 ? 39.106  276.574 20.821 1.00 41.04 ?  134 SER A OG  1 
ATOM   990   N  N   . THR A  1 136 ? 35.631  276.478 22.341 1.00 36.35 ?  135 THR A N   1 
ATOM   991   C  CA  . THR A  1 136 ? 35.284  275.939 23.647 1.00 41.76 ?  135 THR A CA  1 
ATOM   992   C  C   . THR A  1 136 ? 34.088  275.000 23.593 1.00 40.45 ?  135 THR A C   1 
ATOM   993   O  O   . THR A  1 136 ? 33.717  274.435 24.628 1.00 42.35 ?  135 THR A O   1 
ATOM   994   C  CB  . THR A  1 136 ? 35.022  277.094 24.622 1.00 44.77 ?  135 THR A CB  1 
ATOM   995   O  OG1 . THR A  1 136 ? 33.870  277.828 24.184 1.00 51.73 ?  135 THR A OG1 1 
ATOM   996   C  CG2 . THR A  1 136 ? 36.208  278.022 24.651 1.00 43.79 ?  135 THR A CG2 1 
ATOM   997   N  N   . LYS A  1 137 ? 33.495  274.815 22.411 1.00 42.09 ?  136 LYS A N   1 
ATOM   998   C  CA  . LYS A  1 137 ? 32.382  273.905 22.190 1.00 43.60 ?  136 LYS A CA  1 
ATOM   999   C  C   . LYS A  1 137 ? 32.760  272.716 21.320 1.00 39.37 ?  136 LYS A C   1 
ATOM   1000  O  O   . LYS A  1 137 ? 32.505  271.568 21.691 1.00 39.31 ?  136 LYS A O   1 
ATOM   1001  C  CB  . LYS A  1 137 ? 31.208  274.666 21.559 1.00 44.44 ?  136 LYS A CB  1 
ATOM   1002  C  CG  . LYS A  1 137 ? 30.714  275.828 22.413 1.00 48.74 ?  136 LYS A CG  1 
ATOM   1003  C  CD  . LYS A  1 137 ? 29.302  276.271 22.008 1.00 55.50 ?  136 LYS A CD  1 
ATOM   1004  C  CE  . LYS A  1 137 ? 29.258  276.760 20.561 1.00 60.18 ?  136 LYS A CE  1 
ATOM   1005  N  NZ  . LYS A  1 137 ? 29.108  278.244 20.436 1.00 63.56 ?  136 LYS A NZ  1 
ATOM   1006  N  N   . THR A  1 138 ? 33.396  272.961 20.183 1.00 34.10 ?  137 THR A N   1 
ATOM   1007  C  CA  . THR A  1 138 ? 33.676  271.928 19.205 1.00 40.52 ?  137 THR A CA  1 
ATOM   1008  C  C   . THR A  1 138 ? 35.135  271.846 18.805 1.00 38.29 ?  137 THR A C   1 
ATOM   1009  O  O   . THR A  1 138 ? 35.489  270.962 18.018 1.00 39.65 ?  137 THR A O   1 
ATOM   1010  C  CB  . THR A  1 138 ? 32.851  272.157 17.933 1.00 50.09 ?  137 THR A CB  1 
ATOM   1011  O  OG1 . THR A  1 138 ? 33.299  273.363 17.294 1.00 47.18 ?  137 THR A OG1 1 
ATOM   1012  C  CG2 . THR A  1 138 ? 31.369  272.259 18.255 1.00 44.92 ?  137 THR A CG2 1 
ATOM   1013  N  N   . GLY A  1 139 ? 35.987  272.735 19.305 1.00 35.77 ?  138 GLY A N   1 
ATOM   1014  C  CA  . GLY A  1 139 ? 37.352  272.786 18.826 1.00 34.62 ?  138 GLY A CA  1 
ATOM   1015  C  C   . GLY A  1 139 ? 37.513  273.231 17.382 1.00 34.46 ?  138 GLY A C   1 
ATOM   1016  O  O   . GLY A  1 139 ? 38.589  273.039 16.811 1.00 34.06 ?  138 GLY A O   1 
ATOM   1017  N  N   . ASN A  1 140 ? 36.477  273.806 16.774 1.00 34.89 ?  139 ASN A N   1 
ATOM   1018  C  CA  . ASN A  1 140 ? 36.496  274.196 15.358 1.00 39.11 ?  139 ASN A CA  1 
ATOM   1019  C  C   . ASN A  1 140 ? 36.789  273.022 14.425 1.00 40.61 ?  139 ASN A C   1 
ATOM   1020  O  O   . ASN A  1 140 ? 37.301  273.213 13.318 1.00 39.03 ?  139 ASN A O   1 
ATOM   1021  C  CB  . ASN A  1 140 ? 37.500  275.321 15.107 1.00 34.05 ?  139 ASN A CB  1 
ATOM   1022  C  CG  . ASN A  1 140 ? 37.039  276.620 15.687 1.00 37.65 ?  139 ASN A CG  1 
ATOM   1023  O  OD1 . ASN A  1 140 ? 36.103  277.227 15.177 1.00 44.32 ?  139 ASN A OD1 1 
ATOM   1024  N  ND2 . ASN A  1 140 ? 37.657  277.037 16.789 1.00 38.25 ?  139 ASN A ND2 1 
ATOM   1025  N  N   . ALA A  1 141 ? 36.462  271.797 14.844 1.00 37.47 ?  140 ALA A N   1 
ATOM   1026  C  CA  . ALA A  1 141 ? 36.719  270.647 13.986 1.00 35.01 ?  140 ALA A CA  1 
ATOM   1027  C  C   . ALA A  1 141 ? 35.786  270.592 12.787 1.00 34.06 ?  140 ALA A C   1 
ATOM   1028  O  O   . ALA A  1 141 ? 35.977  269.738 11.912 1.00 37.95 ?  140 ALA A O   1 
ATOM   1029  C  CB  . ALA A  1 141 ? 36.611  269.344 14.793 1.00 36.20 ?  140 ALA A CB  1 
ATOM   1030  N  N   . GLY A  1 142 ? 34.782  271.462 12.728 1.00 38.41 ?  141 GLY A N   1 
ATOM   1031  C  CA  . GLY A  1 142 ? 33.964  271.533 11.534 1.00 38.59 ?  141 GLY A CA  1 
ATOM   1032  C  C   . GLY A  1 142 ? 32.957  270.398 11.435 1.00 42.13 ?  141 GLY A C   1 
ATOM   1033  O  O   . GLY A  1 142 ? 32.559  269.786 12.427 1.00 43.60 ?  141 GLY A O   1 
ATOM   1034  N  N   . SER A  1 143 ? 32.577  270.093 10.201 1.00 36.03 ?  142 SER A N   1 
ATOM   1035  C  CA  . SER A  1 143 ? 31.424  269.254 9.946  1.00 40.16 ?  142 SER A CA  1 
ATOM   1036  C  C   . SER A  1 143 ? 31.738  267.777 10.193 1.00 37.46 ?  142 SER A C   1 
ATOM   1037  O  O   . SER A  1 143 ? 32.893  267.349 10.328 1.00 36.23 ?  142 SER A O   1 
ATOM   1038  C  CB  . SER A  1 143 ? 30.948  269.456 8.518  1.00 45.36 ?  142 SER A CB  1 
ATOM   1039  O  OG  . SER A  1 143 ? 31.849  268.805 7.658  1.00 44.91 ?  142 SER A OG  1 
ATOM   1040  N  N   . ARG A  1 144 ? 30.675  266.988 10.231 1.00 37.91 ?  143 ARG A N   1 
ATOM   1041  C  CA  . ARG A  1 144 ? 30.757  265.586 10.623 1.00 36.03 ?  143 ARG A CA  1 
ATOM   1042  C  C   . ARG A  1 144 ? 30.919  264.740 9.369  1.00 30.30 ?  143 ARG A C   1 
ATOM   1043  O  O   . ARG A  1 144 ? 29.992  264.632 8.563  1.00 34.36 ?  143 ARG A O   1 
ATOM   1044  C  CB  . ARG A  1 144 ? 29.511  265.204 11.421 1.00 32.86 ?  143 ARG A CB  1 
ATOM   1045  C  CG  . ARG A  1 144 ? 29.396  266.013 12.711 1.00 31.93 ?  143 ARG A CG  1 
ATOM   1046  C  CD  . ARG A  1 144 ? 27.973  266.174 13.229 1.00 34.55 ?  143 ARG A CD  1 
ATOM   1047  N  NE  . ARG A  1 144 ? 27.940  267.135 14.324 1.00 30.48 ?  143 ARG A NE  1 
ATOM   1048  C  CZ  . ARG A  1 144 ? 27.266  266.986 15.454 1.00 38.92 ?  143 ARG A CZ  1 
ATOM   1049  N  NH1 . ARG A  1 144 ? 26.527  265.911 15.685 1.00 35.69 ?  143 ARG A NH1 1 
ATOM   1050  N  NH2 . ARG A  1 144 ? 27.324  267.946 16.375 1.00 33.65 ?  143 ARG A NH2 1 
ATOM   1051  N  N   . LEU A  1 145 ? 32.096  264.141 9.196  1.00 31.92 ?  144 LEU A N   1 
ATOM   1052  C  CA  . LEU A  1 145 ? 32.343  263.386 7.972  1.00 30.06 ?  144 LEU A CA  1 
ATOM   1053  C  C   . LEU A  1 145 ? 31.744  261.990 8.041  1.00 37.15 ?  144 LEU A C   1 
ATOM   1054  O  O   . LEU A  1 145 ? 31.205  261.496 7.046  1.00 31.08 ?  144 LEU A O   1 
ATOM   1055  C  CB  . LEU A  1 145 ? 33.840  263.288 7.697  1.00 31.38 ?  144 LEU A CB  1 
ATOM   1056  C  CG  . LEU A  1 145 ? 34.555  264.626 7.442  1.00 37.49 ?  144 LEU A CG  1 
ATOM   1057  C  CD1 . LEU A  1 145 ? 35.952  264.362 6.943  1.00 38.41 ?  144 LEU A CD1 1 
ATOM   1058  C  CD2 . LEU A  1 145 ? 33.798  265.492 6.446  1.00 35.03 ?  144 LEU A CD2 1 
ATOM   1059  N  N   . ALA A  1 146 ? 31.847  261.333 9.192  1.00 31.16 ?  145 ALA A N   1 
ATOM   1060  C  CA  . ALA A  1 146 ? 31.292  259.996 9.356  1.00 33.47 ?  145 ALA A CA  1 
ATOM   1061  C  C   . ALA A  1 146 ? 31.011  259.768 10.833 1.00 34.53 ?  145 ALA A C   1 
ATOM   1062  O  O   . ALA A  1 146 ? 31.599  260.422 11.699 1.00 32.02 ?  145 ALA A O   1 
ATOM   1063  C  CB  . ALA A  1 146 ? 32.241  258.925 8.808  1.00 30.40 ?  145 ALA A CB  1 
ATOM   1064  N  N   . CYS A  1 147 ? 30.113  258.827 11.114 1.00 30.51 ?  146 CYS A N   1 
ATOM   1065  C  CA  . CYS A  1 147 ? 29.767  258.528 12.496 1.00 29.13 ?  146 CYS A CA  1 
ATOM   1066  C  C   . CYS A  1 147 ? 29.175  257.130 12.583 1.00 33.38 ?  146 CYS A C   1 
ATOM   1067  O  O   . CYS A  1 147 ? 28.842  256.503 11.575 1.00 29.23 ?  146 CYS A O   1 
ATOM   1068  C  CB  . CYS A  1 147 ? 28.791  259.556 13.059 1.00 28.37 ?  146 CYS A CB  1 
ATOM   1069  S  SG  . CYS A  1 147 ? 27.271  259.670 12.147 1.00 35.80 ?  146 CYS A SG  1 
ATOM   1070  N  N   . GLY A  1 148 ? 29.055  256.649 13.813 1.00 31.08 ?  147 GLY A N   1 
ATOM   1071  C  CA  . GLY A  1 148 ? 28.432  255.366 14.078 1.00 28.43 ?  147 GLY A CA  1 
ATOM   1072  C  C   . GLY A  1 148 ? 28.088  255.307 15.547 1.00 31.99 ?  147 GLY A C   1 
ATOM   1073  O  O   . GLY A  1 148 ? 28.655  256.041 16.367 1.00 30.58 ?  147 GLY A O   1 
ATOM   1074  N  N   . VAL A  1 149 ? 27.134  254.463 15.868 1.00 30.04 ?  148 VAL A N   1 
ATOM   1075  C  CA  . VAL A  1 149 ? 26.803  254.236 17.269 1.00 29.11 ?  148 VAL A CA  1 
ATOM   1076  C  C   . VAL A  1 149 ? 27.806  253.259 17.852 1.00 26.19 ?  148 VAL A C   1 
ATOM   1077  O  O   . VAL A  1 149 ? 28.243  252.314 17.188 1.00 30.75 ?  148 VAL A O   1 
ATOM   1078  C  CB  . VAL A  1 149 ? 25.355  253.737 17.407 1.00 30.62 ?  148 VAL A CB  1 
ATOM   1079  C  CG1 . VAL A  1 149 ? 25.000  253.508 18.892 1.00 27.50 ?  148 VAL A CG1 1 
ATOM   1080  C  CG2 . VAL A  1 149 ? 24.425  254.762 16.771 1.00 27.55 ?  148 VAL A CG2 1 
ATOM   1081  N  N   . ILE A  1 150 ? 28.219  253.507 19.088 1.00 26.42 ?  149 ILE A N   1 
ATOM   1082  C  CA  . ILE A  1 150 ? 29.198  252.646 19.729 1.00 24.74 ?  149 ILE A CA  1 
ATOM   1083  C  C   . ILE A  1 150 ? 28.458  251.473 20.354 1.00 27.97 ?  149 ILE A C   1 
ATOM   1084  O  O   . ILE A  1 150 ? 27.626  251.657 21.255 1.00 28.94 ?  149 ILE A O   1 
ATOM   1085  C  CB  . ILE A  1 150 ? 30.005  253.418 20.781 1.00 25.81 ?  149 ILE A CB  1 
ATOM   1086  C  CG1 . ILE A  1 150 ? 30.798  254.554 20.124 1.00 29.98 ?  149 ILE A CG1 1 
ATOM   1087  C  CG2 . ILE A  1 150 ? 30.921  252.489 21.546 1.00 27.70 ?  149 ILE A CG2 1 
ATOM   1088  C  CD1 . ILE A  1 150 ? 31.248  255.607 21.128 1.00 28.79 ?  149 ILE A CD1 1 
ATOM   1089  N  N   . GLY A  1 151 ? 28.756  250.268 19.880 1.00 27.86 ?  150 GLY A N   1 
ATOM   1090  C  CA  . GLY A  1 151 ? 28.028  249.096 20.332 1.00 26.71 ?  150 GLY A CA  1 
ATOM   1091  C  C   . GLY A  1 151 ? 28.869  248.111 21.114 1.00 30.08 ?  150 GLY A C   1 
ATOM   1092  O  O   . GLY A  1 151 ? 30.106  248.100 21.017 1.00 29.31 ?  150 GLY A O   1 
ATOM   1093  N  N   . ILE A  1 152 ? 28.191  247.279 21.903 1.00 29.60 ?  151 ILE A N   1 
ATOM   1094  C  CA  . ILE A  1 152 ? 28.867  246.252 22.687 1.00 27.99 ?  151 ILE A CA  1 
ATOM   1095  C  C   . ILE A  1 152 ? 29.418  245.207 21.737 1.00 28.05 ?  151 ILE A C   1 
ATOM   1096  O  O   . ILE A  1 152 ? 28.739  244.778 20.792 1.00 31.52 ?  151 ILE A O   1 
ATOM   1097  C  CB  . ILE A  1 152 ? 27.898  245.625 23.701 1.00 28.63 ?  151 ILE A CB  1 
ATOM   1098  C  CG1 . ILE A  1 152 ? 27.573  246.612 24.810 1.00 36.29 ?  151 ILE A CG1 1 
ATOM   1099  C  CG2 . ILE A  1 152 ? 28.482  244.366 24.325 1.00 32.28 ?  151 ILE A CG2 1 
ATOM   1100  C  CD1 . ILE A  1 152 ? 26.211  246.351 25.468 1.00 35.23 ?  151 ILE A CD1 1 
ATOM   1101  N  N   . ALA A  1 153 ? 30.665  244.810 21.957 1.00 29.39 ?  152 ALA A N   1 
ATOM   1102  C  CA  . ALA A  1 153 ? 31.311  243.853 21.076 1.00 31.50 ?  152 ALA A CA  1 
ATOM   1103  C  C   . ALA A  1 153 ? 31.695  242.599 21.850 1.00 34.11 ?  152 ALA A C   1 
ATOM   1104  O  O   . ALA A  1 153 ? 31.825  242.611 23.077 1.00 33.19 ?  152 ALA A O   1 
ATOM   1105  C  CB  . ALA A  1 153 ? 32.553  244.442 20.412 1.00 32.60 ?  152 ALA A CB  1 
ATOM   1106  N  N   . GLN A  1 154 ? 31.865  241.516 21.100 1.00 38.50 ?  153 GLN A N   1 
ATOM   1107  C  CA  . GLN A  1 154 ? 32.346  240.248 21.639 1.00 43.56 ?  153 GLN A CA  1 
ATOM   1108  C  C   . GLN A  1 154 ? 33.866  240.239 21.884 1.00 56.60 ?  153 GLN A C   1 
ATOM   1109  O  O   . GLN A  1 154 ? 34.676  240.558 20.995 1.00 51.55 ?  153 GLN A O   1 
ATOM   1110  C  CB  . GLN A  1 154 ? 31.980  239.109 20.691 1.00 41.31 ?  153 GLN A CB  1 
ATOM   1111  C  CG  . GLN A  1 154 ? 32.298  237.733 21.263 1.00 51.36 ?  153 GLN A CG  1 
ATOM   1112  C  CD  . GLN A  1 154 ? 31.824  236.620 20.363 1.00 53.42 ?  153 GLN A CD  1 
ATOM   1113  O  OE1 . GLN A  1 154 ? 31.920  236.715 19.134 1.00 56.26 ?  153 GLN A OE1 1 
ATOM   1114  N  NE2 . GLN A  1 154 ? 31.295  235.555 20.967 1.00 58.49 ?  153 GLN A NE2 1 
ATOM   1115  O  OXT . GLN A  1 154 ? 34.322  239.887 22.980 1.00 63.06 ?  153 GLN A OXT 1 
ATOM   1116  N  N   . MET B  1 1   ? 18.711  255.128 34.094 1.00 62.84 ?  0   MET B N   1 
ATOM   1117  C  CA  . MET B  1 1   ? 19.452  256.322 33.671 1.00 67.47 ?  0   MET B CA  1 
ATOM   1118  C  C   . MET B  1 1   ? 18.967  256.825 32.302 1.00 67.52 ?  0   MET B C   1 
ATOM   1119  O  O   . MET B  1 1   ? 18.389  257.913 32.205 1.00 61.88 ?  0   MET B O   1 
ATOM   1120  C  CB  . MET B  1 1   ? 20.961  256.045 33.631 1.00 61.51 ?  0   MET B CB  1 
ATOM   1121  N  N   . ALA B  1 2   ? 19.202  256.042 31.245 1.00 64.37 ?  1   ALA B N   1 
ATOM   1122  C  CA  . ALA B  1 2   ? 18.643  256.363 29.935 1.00 53.33 ?  1   ALA B CA  1 
ATOM   1123  C  C   . ALA B  1 2   ? 17.149  256.048 29.916 1.00 44.40 ?  1   ALA B C   1 
ATOM   1124  O  O   . ALA B  1 2   ? 16.728  254.962 30.326 1.00 48.88 ?  1   ALA B O   1 
ATOM   1125  C  CB  . ALA B  1 2   ? 19.365  255.585 28.837 1.00 47.41 ?  1   ALA B CB  1 
ATOM   1126  N  N   . THR B  1 3   ? 16.342  257.010 29.464 1.00 37.19 ?  2   THR B N   1 
ATOM   1127  C  CA  . THR B  1 3   ? 14.908  256.812 29.364 1.00 36.17 ?  2   THR B CA  1 
ATOM   1128  C  C   . THR B  1 3   ? 14.404  256.783 27.931 1.00 36.95 ?  2   THR B C   1 
ATOM   1129  O  O   . THR B  1 3   ? 13.228  256.469 27.711 1.00 32.26 ?  2   THR B O   1 
ATOM   1130  C  CB  . THR B  1 3   ? 14.165  257.910 30.134 1.00 36.19 ?  2   THR B CB  1 
ATOM   1131  O  OG1 . THR B  1 3   ? 14.242  259.143 29.409 1.00 42.54 ?  2   THR B OG1 1 
ATOM   1132  C  CG2 . THR B  1 3   ? 14.776  258.096 31.524 1.00 42.65 ?  2   THR B CG2 1 
ATOM   1133  N  N   . LYS B  1 4   ? 15.252  257.105 26.958 1.00 32.07 ?  3   LYS B N   1 
ATOM   1134  C  CA  . LYS B  1 4   ? 14.877  257.102 25.556 1.00 30.54 ?  3   LYS B CA  1 
ATOM   1135  C  C   . LYS B  1 4   ? 16.015  256.514 24.753 1.00 33.39 ?  3   LYS B C   1 
ATOM   1136  O  O   . LYS B  1 4   ? 17.184  256.719 25.083 1.00 31.76 ?  3   LYS B O   1 
ATOM   1137  C  CB  . LYS B  1 4   ? 14.584  258.503 25.015 1.00 37.37 ?  3   LYS B CB  1 
ATOM   1138  C  CG  . LYS B  1 4   ? 13.307  259.134 25.488 1.00 42.72 ?  3   LYS B CG  1 
ATOM   1139  C  CD  . LYS B  1 4   ? 12.541  259.650 24.285 1.00 52.72 ?  3   LYS B CD  1 
ATOM   1140  C  CE  . LYS B  1 4   ? 11.850  260.970 24.588 1.00 57.46 ?  3   LYS B CE  1 
ATOM   1141  N  NZ  . LYS B  1 4   ? 11.304  261.037 25.975 1.00 57.80 ?  3   LYS B NZ  1 
ATOM   1142  N  N   . ALA B  1 5   ? 15.672  255.795 23.693 1.00 27.82 ?  4   ALA B N   1 
ATOM   1143  C  CA  . ALA B  1 5   ? 16.681  255.268 22.792 1.00 27.67 ?  4   ALA B CA  1 
ATOM   1144  C  C   . ALA B  1 5   ? 16.094  255.260 21.394 1.00 27.51 ?  4   ALA B C   1 
ATOM   1145  O  O   . ALA B  1 5   ? 14.889  255.442 21.202 1.00 28.28 ?  4   ALA B O   1 
ATOM   1146  C  CB  . ALA B  1 5   ? 17.136  253.875 23.218 1.00 22.45 ?  4   ALA B CB  1 
ATOM   1147  N  N   . VAL B  1 6   ? 16.952  255.027 20.409 1.00 25.03 ?  5   VAL B N   1 
ATOM   1148  C  CA  . VAL B  1 6   ? 16.515  255.064 19.026 1.00 25.21 ?  5   VAL B CA  1 
ATOM   1149  C  C   . VAL B  1 6   ? 17.413  254.143 18.219 1.00 26.76 ?  5   VAL B C   1 
ATOM   1150  O  O   . VAL B  1 6   ? 18.562  253.882 18.583 1.00 26.57 ?  5   VAL B O   1 
ATOM   1151  C  CB  . VAL B  1 6   ? 16.531  256.498 18.452 1.00 28.47 ?  5   VAL B CB  1 
ATOM   1152  C  CG1 . VAL B  1 6   ? 17.956  256.947 18.207 1.00 29.56 ?  5   VAL B CG1 1 
ATOM   1153  C  CG2 . VAL B  1 6   ? 15.736  256.551 17.144 1.00 28.09 ?  5   VAL B CG2 1 
ATOM   1154  N  N   . CYS B  1 7   ? 16.874  253.636 17.123 1.00 25.40 ?  6   CYS B N   1 
ATOM   1155  C  CA  . CYS B  1 7   ? 17.618  252.718 16.291 1.00 24.85 ?  6   CYS B CA  1 
ATOM   1156  C  C   . CYS B  1 7   ? 17.269  252.980 14.840 1.00 26.98 ?  6   CYS B C   1 
ATOM   1157  O  O   . CYS B  1 7   ? 16.087  253.082 14.486 1.00 29.82 ?  6   CYS B O   1 
ATOM   1158  C  CB  . CYS B  1 7   ? 17.303  251.269 16.673 1.00 27.19 ?  6   CYS B CB  1 
ATOM   1159  S  SG  . CYS B  1 7   ? 18.183  250.096 15.673 1.00 30.85 ?  6   CYS B SG  1 
ATOM   1160  N  N   . VAL B  1 8   ? 18.288  253.095 14.003 1.00 27.78 ?  7   VAL B N   1 
ATOM   1161  C  CA  . VAL B  1 8   ? 18.088  253.283 12.572 1.00 25.87 ?  7   VAL B CA  1 
ATOM   1162  C  C   . VAL B  1 8   ? 18.407  251.958 11.893 1.00 28.00 ?  7   VAL B C   1 
ATOM   1163  O  O   . VAL B  1 8   ? 19.544  251.481 11.959 1.00 25.06 ?  7   VAL B O   1 
ATOM   1164  C  CB  . VAL B  1 8   ? 18.965  254.419 12.032 1.00 30.12 ?  7   VAL B CB  1 
ATOM   1165  C  CG1 . VAL B  1 8   ? 18.897  254.449 10.513 1.00 28.53 ?  7   VAL B CG1 1 
ATOM   1166  C  CG2 . VAL B  1 8   ? 18.515  255.754 12.645 1.00 30.39 ?  7   VAL B CG2 1 
ATOM   1167  N  N   . LEU B  1 9   ? 17.401  251.341 11.288 1.00 29.91 ?  8   LEU B N   1 
ATOM   1168  C  CA  . LEU B  1 9   ? 17.558  250.050 10.637 1.00 25.62 ?  8   LEU B CA  1 
ATOM   1169  C  C   . LEU B  1 9   ? 17.944  250.267 9.179  1.00 31.75 ?  8   LEU B C   1 
ATOM   1170  O  O   . LEU B  1 9   ? 17.222  250.941 8.438  1.00 29.23 ?  8   LEU B O   1 
ATOM   1171  C  CB  . LEU B  1 9   ? 16.249  249.259 10.721 1.00 26.38 ?  8   LEU B CB  1 
ATOM   1172  C  CG  . LEU B  1 9   ? 15.822  248.860 12.149 1.00 34.10 ?  8   LEU B CG  1 
ATOM   1173  C  CD1 . LEU B  1 9   ? 14.531  248.084 12.124 1.00 33.23 ?  8   LEU B CD1 1 
ATOM   1174  C  CD2 . LEU B  1 9   ? 16.875  247.978 12.743 1.00 29.83 ?  8   LEU B CD2 1 
ATOM   1175  N  N   . LYS B  1 10  ? 19.068  249.686 8.777  1.00 31.15 ?  9   LYS B N   1 
ATOM   1176  C  CA  . LYS B  1 10  ? 19.538  249.692 7.398  1.00 35.03 ?  9   LYS B CA  1 
ATOM   1177  C  C   . LYS B  1 10  ? 20.011  248.291 7.065  1.00 32.12 ?  9   LYS B C   1 
ATOM   1178  O  O   . LYS B  1 10  ? 20.427  247.537 7.949  1.00 32.80 ?  9   LYS B O   1 
ATOM   1179  C  CB  . LYS B  1 10  ? 20.714  250.665 7.168  1.00 39.62 ?  9   LYS B CB  1 
ATOM   1180  C  CG  . LYS B  1 10  ? 20.385  252.062 6.648  1.00 49.52 ?  9   LYS B CG  1 
ATOM   1181  C  CD  . LYS B  1 10  ? 19.402  252.812 7.517  1.00 51.32 ?  9   LYS B CD  1 
ATOM   1182  C  CE  . LYS B  1 10  ? 18.420  253.674 6.698  1.00 54.03 ?  9   LYS B CE  1 
ATOM   1183  N  NZ  . LYS B  1 10  ? 17.220  254.095 7.506  1.00 46.67 ?  9   LYS B NZ  1 
ATOM   1184  N  N   . GLY B  1 11  ? 19.995  247.968 5.777  1.00 31.72 ?  10  GLY B N   1 
ATOM   1185  C  CA  . GLY B  1 11  ? 20.521  246.700 5.307  1.00 34.41 ?  10  GLY B CA  1 
ATOM   1186  C  C   . GLY B  1 11  ? 20.998  246.742 3.864  1.00 33.89 ?  10  GLY B C   1 
ATOM   1187  O  O   . GLY B  1 11  ? 21.127  247.820 3.280  1.00 32.13 ?  10  GLY B O   1 
ATOM   1188  N  N   . ASP B  1 12  ? 21.257  245.563 3.288  1.00 34.65 ?  11  ASP B N   1 
ATOM   1189  C  CA  . ASP B  1 12  ? 21.699  245.451 1.898  1.00 39.58 ?  11  ASP B CA  1 
ATOM   1190  C  C   . ASP B  1 12  ? 20.556  245.644 0.921  1.00 41.40 ?  11  ASP B C   1 
ATOM   1191  O  O   . ASP B  1 12  ? 20.789  245.973 -0.242 1.00 43.98 ?  11  ASP B O   1 
ATOM   1192  C  CB  . ASP B  1 12  ? 22.316  244.075 1.626  1.00 36.54 ?  11  ASP B CB  1 
ATOM   1193  C  CG  . ASP B  1 12  ? 23.532  243.787 2.486  1.00 58.72 ?  11  ASP B CG  1 
ATOM   1194  O  OD1 . ASP B  1 12  ? 23.542  242.717 3.146  1.00 61.20 ?  11  ASP B OD1 1 
ATOM   1195  O  OD2 . ASP B  1 12  ? 24.477  244.612 2.487  1.00 58.31 ?  11  ASP B OD2 1 
ATOM   1196  N  N   . GLY B  1 13  ? 19.333  245.394 1.353  1.00 34.27 ?  12  GLY B N   1 
ATOM   1197  C  CA  . GLY B  1 13  ? 18.193  245.505 0.489  1.00 29.15 ?  12  GLY B CA  1 
ATOM   1198  C  C   . GLY B  1 13  ? 17.451  246.782 0.772  1.00 30.41 ?  12  GLY B C   1 
ATOM   1199  O  O   . GLY B  1 13  ? 17.996  247.755 1.307  1.00 31.38 ?  12  GLY B O   1 
ATOM   1200  N  N   . PRO B  1 14  ? 16.166  246.797 0.422  1.00 29.51 ?  13  PRO B N   1 
ATOM   1201  C  CA  . PRO B  1 14  ? 15.376  248.021 0.560  1.00 30.60 ?  13  PRO B CA  1 
ATOM   1202  C  C   . PRO B  1 14  ? 14.832  248.265 1.954  1.00 29.39 ?  13  PRO B C   1 
ATOM   1203  O  O   . PRO B  1 14  ? 14.211  249.307 2.170  1.00 28.46 ?  13  PRO B O   1 
ATOM   1204  C  CB  . PRO B  1 14  ? 14.231  247.779 -0.428 1.00 33.99 ?  13  PRO B CB  1 
ATOM   1205  C  CG  . PRO B  1 14  ? 14.019  246.308 -0.369 1.00 30.31 ?  13  PRO B CG  1 
ATOM   1206  C  CD  . PRO B  1 14  ? 15.383  245.684 -0.146 1.00 28.98 ?  13  PRO B CD  1 
ATOM   1207  N  N   . VAL B  1 15  ? 15.025  247.350 2.907  1.00 29.97 ?  14  VAL B N   1 
ATOM   1208  C  CA  . VAL B  1 15  ? 14.366  247.496 4.200  1.00 28.10 ?  14  VAL B CA  1 
ATOM   1209  C  C   . VAL B  1 15  ? 15.051  248.582 5.014  1.00 27.93 ?  14  VAL B C   1 
ATOM   1210  O  O   . VAL B  1 15  ? 16.271  248.554 5.210  1.00 32.63 ?  14  VAL B O   1 
ATOM   1211  C  CB  . VAL B  1 15  ? 14.378  246.163 4.957  1.00 30.81 ?  14  VAL B CB  1 
ATOM   1212  C  CG1 . VAL B  1 15  ? 13.818  246.378 6.356  1.00 28.09 ?  14  VAL B CG1 1 
ATOM   1213  C  CG2 . VAL B  1 15  ? 13.545  245.134 4.200  1.00 30.30 ?  14  VAL B CG2 1 
ATOM   1214  N  N   . GLN B  1 16  ? 14.269  249.527 5.526  1.00 27.22 ?  15  GLN B N   1 
ATOM   1215  C  CA  . GLN B  1 16  ? 14.852  250.542 6.388  1.00 33.46 ?  15  GLN B CA  1 
ATOM   1216  C  C   . GLN B  1 16  ? 13.777  251.099 7.309  1.00 30.86 ?  15  GLN B C   1 
ATOM   1217  O  O   . GLN B  1 16  ? 12.584  251.031 7.004  1.00 32.92 ?  15  GLN B O   1 
ATOM   1218  C  CB  . GLN B  1 16  ? 15.489  251.653 5.547  1.00 35.47 ?  15  GLN B CB  1 
ATOM   1219  C  CG  . GLN B  1 16  ? 14.536  252.269 4.556  1.00 35.63 ?  15  GLN B CG  1 
ATOM   1220  C  CD  . GLN B  1 16  ? 15.103  253.530 3.924  1.00 52.04 ?  15  GLN B CD  1 
ATOM   1221  O  OE1 . GLN B  1 16  ? 15.850  253.453 2.949  1.00 47.59 ?  15  GLN B OE1 1 
ATOM   1222  N  NE2 . GLN B  1 16  ? 14.769  254.696 4.486  1.00 55.07 ?  15  GLN B NE2 1 
ATOM   1223  N  N   . GLY B  1 17  ? 14.199  251.653 8.442  1.00 29.65 ?  16  GLY B N   1 
ATOM   1224  C  CA  . GLY B  1 17  ? 13.213  252.241 9.331  1.00 29.75 ?  16  GLY B CA  1 
ATOM   1225  C  C   . GLY B  1 17  ? 13.845  252.891 10.541 1.00 29.50 ?  16  GLY B C   1 
ATOM   1226  O  O   . GLY B  1 17  ? 15.062  252.864 10.735 1.00 29.54 ?  16  GLY B O   1 
ATOM   1227  N  N   . ILE B  1 18  ? 12.987  253.471 11.375 1.00 26.06 ?  17  ILE B N   1 
ATOM   1228  C  CA  . ILE B  1 18  ? 13.418  254.101 12.613 1.00 28.26 ?  17  ILE B CA  1 
ATOM   1229  C  C   . ILE B  1 18  ? 12.563  253.550 13.745 1.00 26.33 ?  17  ILE B C   1 
ATOM   1230  O  O   . ILE B  1 18  ? 11.331  253.633 13.697 1.00 29.98 ?  17  ILE B O   1 
ATOM   1231  C  CB  . ILE B  1 18  ? 13.302  255.634 12.557 1.00 28.24 ?  17  ILE B CB  1 
ATOM   1232  C  CG1 . ILE B  1 18  ? 14.278  256.204 11.515 1.00 34.68 ?  17  ILE B CG1 1 
ATOM   1233  C  CG2 . ILE B  1 18  ? 13.500  256.227 13.978 1.00 26.56 ?  17  ILE B CG2 1 
ATOM   1234  C  CD1 . ILE B  1 18  ? 13.976  257.650 11.121 1.00 31.02 ?  17  ILE B CD1 1 
ATOM   1235  N  N   . ILE B  1 19  ? 13.202  253.008 14.771 1.00 26.57 ?  18  ILE B N   1 
ATOM   1236  C  CA  . ILE B  1 19  ? 12.477  252.491 15.919 1.00 24.50 ?  18  ILE B CA  1 
ATOM   1237  C  C   . ILE B  1 19  ? 12.882  253.296 17.143 1.00 28.41 ?  18  ILE B C   1 
ATOM   1238  O  O   . ILE B  1 19  ? 14.078  253.454 17.411 1.00 27.96 ?  18  ILE B O   1 
ATOM   1239  C  CB  . ILE B  1 19  ? 12.762  251.000 16.149 1.00 26.66 ?  18  ILE B CB  1 
ATOM   1240  C  CG1 . ILE B  1 19  ? 12.296  250.145 14.955 1.00 28.85 ?  18  ILE B CG1 1 
ATOM   1241  C  CG2 . ILE B  1 19  ? 12.138  250.584 17.438 1.00 24.22 ?  18  ILE B CG2 1 
ATOM   1242  C  CD1 . ILE B  1 19  ? 10.817  250.240 14.639 1.00 22.91 ?  18  ILE B CD1 1 
ATOM   1243  N  N   . ASN B  1 20  ? 11.887  253.766 17.899 1.00 28.30 ?  19  ASN B N   1 
ATOM   1244  C  CA  . ASN B  1 20  ? 12.070  254.497 19.140 1.00 25.81 ?  19  ASN B CA  1 
ATOM   1245  C  C   . ASN B  1 20  ? 11.810  253.595 20.334 1.00 30.85 ?  19  ASN B C   1 
ATOM   1246  O  O   . ASN B  1 20  ? 10.972  252.694 20.283 1.00 29.78 ?  19  ASN B O   1 
ATOM   1247  C  CB  . ASN B  1 20  ? 11.124  255.698 19.204 1.00 29.99 ?  19  ASN B CB  1 
ATOM   1248  C  CG  . ASN B  1 20  ? 11.222  256.555 17.966 1.00 33.36 ?  19  ASN B CG  1 
ATOM   1249  O  OD1 . ASN B  1 20  ? 10.395  256.455 17.061 1.00 33.68 ?  19  ASN B OD1 1 
ATOM   1250  N  ND2 . ASN B  1 20  ? 12.265  257.362 17.894 1.00 30.80 ?  19  ASN B ND2 1 
ATOM   1251  N  N   . PHE B  1 21  ? 12.523  253.863 21.422 1.00 24.99 ?  20  PHE B N   1 
ATOM   1252  C  CA  . PHE B  1 21  ? 12.313  253.157 22.679 1.00 28.60 ?  20  PHE B CA  1 
ATOM   1253  C  C   . PHE B  1 21  ? 12.080  254.196 23.764 1.00 31.85 ?  20  PHE B C   1 
ATOM   1254  O  O   . PHE B  1 21  ? 12.698  255.263 23.752 1.00 31.34 ?  20  PHE B O   1 
ATOM   1255  C  CB  . PHE B  1 21  ? 13.508  252.260 23.056 1.00 26.60 ?  20  PHE B CB  1 
ATOM   1256  C  CG  . PHE B  1 21  ? 13.898  251.244 21.996 1.00 29.77 ?  20  PHE B CG  1 
ATOM   1257  C  CD1 . PHE B  1 21  ? 14.630  251.624 20.871 1.00 29.19 ?  20  PHE B CD1 1 
ATOM   1258  C  CD2 . PHE B  1 21  ? 13.564  249.904 22.144 1.00 30.47 ?  20  PHE B CD2 1 
ATOM   1259  C  CE1 . PHE B  1 21  ? 15.000  250.686 19.915 1.00 26.97 ?  20  PHE B CE1 1 
ATOM   1260  C  CE2 . PHE B  1 21  ? 13.932  248.963 21.178 1.00 30.75 ?  20  PHE B CE2 1 
ATOM   1261  C  CZ  . PHE B  1 21  ? 14.645  249.356 20.076 1.00 28.23 ?  20  PHE B CZ  1 
ATOM   1262  N  N   . GLU B  1 22  ? 11.204  253.889 24.710 1.00 30.66 ?  21  GLU B N   1 
ATOM   1263  C  CA  . GLU B  1 22  ? 10.974  254.820 25.806 1.00 32.18 ?  21  GLU B CA  1 
ATOM   1264  C  C   . GLU B  1 22  ? 10.628  254.043 27.055 1.00 34.84 ?  21  GLU B C   1 
ATOM   1265  O  O   . GLU B  1 22  ? 9.767   253.160 27.021 1.00 32.88 ?  21  GLU B O   1 
ATOM   1266  C  CB  . GLU B  1 22  ? 9.852   255.798 25.478 1.00 33.76 ?  21  GLU B CB  1 
ATOM   1267  C  CG  . GLU B  1 22  ? 9.375   256.614 26.646 1.00 44.49 ?  21  GLU B CG  1 
ATOM   1268  C  CD  . GLU B  1 22  ? 8.870   257.977 26.205 1.00 53.32 ?  21  GLU B CD  1 
ATOM   1269  O  OE1 . GLU B  1 22  ? 9.693   258.900 26.026 1.00 67.96 ?  21  GLU B OE1 1 
ATOM   1270  O  OE2 . GLU B  1 22  ? 7.645   258.106 25.998 1.00 57.34 ?  21  GLU B OE2 1 
ATOM   1271  N  N   . GLN B  1 23  ? 11.304  254.380 28.147 1.00 29.41 ?  22  GLN B N   1 
ATOM   1272  C  CA  . GLN B  1 23  ? 11.128  253.710 29.428 1.00 35.37 ?  22  GLN B CA  1 
ATOM   1273  C  C   . GLN B  1 23  ? 11.090  254.794 30.500 1.00 38.36 ?  22  GLN B C   1 
ATOM   1274  O  O   . GLN B  1 23  ? 12.139  255.272 30.940 1.00 36.17 ?  22  GLN B O   1 
ATOM   1275  C  CB  . GLN B  1 23  ? 12.251  252.719 29.683 1.00 32.04 ?  22  GLN B CB  1 
ATOM   1276  C  CG  . GLN B  1 23  ? 11.968  251.788 30.848 1.00 29.98 ?  22  GLN B CG  1 
ATOM   1277  C  CD  . GLN B  1 23  ? 13.134  250.912 31.121 1.00 29.55 ?  22  GLN B CD  1 
ATOM   1278  O  OE1 . GLN B  1 23  ? 14.254  251.229 30.716 1.00 30.66 ?  22  GLN B OE1 1 
ATOM   1279  N  NE2 . GLN B  1 23  ? 12.890  249.766 31.762 1.00 26.21 ?  22  GLN B NE2 1 
ATOM   1280  N  N   . LYS B  1 24  ? 9.877   255.165 30.914 1.00 43.39 ?  23  LYS B N   1 
ATOM   1281  C  CA  . LYS B  1 24  ? 9.710   256.247 31.880 1.00 44.63 ?  23  LYS B CA  1 
ATOM   1282  C  C   . LYS B  1 24  ? 10.295  255.883 33.235 1.00 47.44 ?  23  LYS B C   1 
ATOM   1283  O  O   . LYS B  1 24  ? 10.912  256.728 33.892 1.00 48.33 ?  23  LYS B O   1 
ATOM   1284  C  CB  . LYS B  1 24  ? 8.232   256.606 32.026 1.00 48.66 ?  23  LYS B CB  1 
ATOM   1285  C  CG  . LYS B  1 24  ? 7.684   257.461 30.883 1.00 52.54 ?  23  LYS B CG  1 
ATOM   1286  C  CD  . LYS B  1 24  ? 8.672   258.558 30.454 1.00 52.57 ?  23  LYS B CD  1 
ATOM   1287  C  CE  . LYS B  1 24  ? 8.029   259.566 29.463 1.00 61.20 ?  23  LYS B CE  1 
ATOM   1288  N  NZ  . LYS B  1 24  ? 6.526   259.628 29.536 1.00 52.90 ?  23  LYS B NZ  1 
ATOM   1289  N  N   . GLU B  1 25  ? 10.119  254.637 33.673 1.00 39.77 ?  24  GLU B N   1 
ATOM   1290  C  CA  . GLU B  1 25  ? 10.633  254.171 34.958 1.00 44.91 ?  24  GLU B CA  1 
ATOM   1291  C  C   . GLU B  1 25  ? 11.555  252.985 34.745 1.00 43.57 ?  24  GLU B C   1 
ATOM   1292  O  O   . GLU B  1 25  ? 11.257  252.099 33.936 1.00 38.61 ?  24  GLU B O   1 
ATOM   1293  C  CB  . GLU B  1 25  ? 9.496   253.752 35.891 1.00 47.06 ?  24  GLU B CB  1 
ATOM   1294  C  CG  . GLU B  1 25  ? 8.540   254.871 36.254 1.00 56.11 ?  24  GLU B CG  1 
ATOM   1295  C  CD  . GLU B  1 25  ? 9.217   256.008 37.010 1.00 64.04 ?  24  GLU B CD  1 
ATOM   1296  O  OE1 . GLU B  1 25  ? 8.667   257.133 36.988 1.00 67.10 ?  24  GLU B OE1 1 
ATOM   1297  O  OE2 . GLU B  1 25  ? 10.287  255.777 37.634 1.00 66.35 ?  24  GLU B OE2 1 
ATOM   1298  N  N   . SER B  1 26  ? 12.659  252.937 35.496 1.00 40.02 ?  25  SER B N   1 
ATOM   1299  C  CA  . SER B  1 26  ? 13.582  251.820 35.304 1.00 44.58 ?  25  SER B CA  1 
ATOM   1300  C  C   . SER B  1 26  ? 12.965  250.482 35.701 1.00 46.22 ?  25  SER B C   1 
ATOM   1301  O  O   . SER B  1 26  ? 13.434  249.432 35.245 1.00 44.88 ?  25  SER B O   1 
ATOM   1302  C  CB  . SER B  1 26  ? 14.879  252.046 36.083 1.00 46.94 ?  25  SER B CB  1 
ATOM   1303  O  OG  . SER B  1 26  ? 14.672  251.992 37.485 1.00 51.36 ?  25  SER B OG  1 
ATOM   1304  N  N   . ASN B  1 27  ? 11.928  250.485 36.532 1.00 40.96 ?  26  ASN B N   1 
ATOM   1305  C  CA  . ASN B  1 27  ? 11.254  249.246 36.896 1.00 42.46 ?  26  ASN B CA  1 
ATOM   1306  C  C   . ASN B  1 27  ? 10.016  248.996 36.041 1.00 47.94 ?  26  ASN B C   1 
ATOM   1307  O  O   . ASN B  1 27  ? 9.151   248.193 36.422 1.00 45.96 ?  26  ASN B O   1 
ATOM   1308  C  CB  . ASN B  1 27  ? 10.889  249.259 38.384 1.00 42.59 ?  26  ASN B CB  1 
ATOM   1309  C  CG  . ASN B  1 27  ? 9.857   250.327 38.726 1.00 50.88 ?  26  ASN B CG  1 
ATOM   1310  O  OD1 . ASN B  1 27  ? 9.586   251.227 37.925 1.00 49.71 ?  26  ASN B OD1 1 
ATOM   1311  N  ND2 . ASN B  1 27  ? 9.266   250.227 39.912 1.00 45.00 ?  26  ASN B ND2 1 
ATOM   1312  N  N   . GLY B  1 28  ? 9.912   249.671 34.895 1.00 40.36 ?  27  GLY B N   1 
ATOM   1313  C  CA  . GLY B  1 28  ? 8.697   249.670 34.123 1.00 36.38 ?  27  GLY B CA  1 
ATOM   1314  C  C   . GLY B  1 28  ? 8.918   249.203 32.704 1.00 33.44 ?  27  GLY B C   1 
ATOM   1315  O  O   . GLY B  1 28  ? 10.053  249.023 32.254 1.00 31.84 ?  27  GLY B O   1 
ATOM   1316  N  N   . PRO B  1 29  ? 7.826   249.010 31.971 1.00 34.45 ?  28  PRO B N   1 
ATOM   1317  C  CA  . PRO B  1 29  ? 7.927   248.541 30.587 1.00 33.97 ?  28  PRO B CA  1 
ATOM   1318  C  C   . PRO B  1 29  ? 8.603   249.541 29.658 1.00 35.07 ?  28  PRO B C   1 
ATOM   1319  O  O   . PRO B  1 29  ? 8.614   250.754 29.883 1.00 30.06 ?  28  PRO B O   1 
ATOM   1320  C  CB  . PRO B  1 29  ? 6.466   248.326 30.171 1.00 34.88 ?  28  PRO B CB  1 
ATOM   1321  C  CG  . PRO B  1 29  ? 5.655   249.059 31.146 1.00 44.31 ?  28  PRO B CG  1 
ATOM   1322  C  CD  . PRO B  1 29  ? 6.436   249.201 32.407 1.00 33.49 ?  28  PRO B CD  1 
ATOM   1323  N  N   . VAL B  1 30  ? 9.151   249.000 28.570 1.00 30.21 ?  29  VAL B N   1 
ATOM   1324  C  CA  . VAL B  1 30  ? 9.694   249.802 27.472 1.00 29.23 ?  29  VAL B CA  1 
ATOM   1325  C  C   . VAL B  1 30  ? 8.672   249.845 26.348 1.00 31.36 ?  29  VAL B C   1 
ATOM   1326  O  O   . VAL B  1 30  ? 8.223   248.794 25.871 1.00 34.11 ?  29  VAL B O   1 
ATOM   1327  C  CB  . VAL B  1 30  ? 11.024  249.222 26.968 1.00 27.92 ?  29  VAL B CB  1 
ATOM   1328  C  CG1 . VAL B  1 30  ? 11.584  250.076 25.803 1.00 29.03 ?  29  VAL B CG1 1 
ATOM   1329  C  CG2 . VAL B  1 30  ? 12.022  249.130 28.130 1.00 29.91 ?  29  VAL B CG2 1 
ATOM   1330  N  N   . LYS B  1 31  ? 8.302   251.049 25.921 1.00 30.71 ?  30  LYS B N   1 
ATOM   1331  C  CA  . LYS B  1 31  ? 7.485   251.202 24.727 1.00 32.11 ?  30  LYS B CA  1 
ATOM   1332  C  C   . LYS B  1 31  ? 8.392   251.233 23.507 1.00 31.41 ?  30  LYS B C   1 
ATOM   1333  O  O   . LYS B  1 31  ? 9.423   251.908 23.512 1.00 30.91 ?  30  LYS B O   1 
ATOM   1334  C  CB  . LYS B  1 31  ? 6.643   252.477 24.788 1.00 36.29 ?  30  LYS B CB  1 
ATOM   1335  C  CG  . LYS B  1 31  ? 5.965   252.732 26.127 1.00 53.59 ?  30  LYS B CG  1 
ATOM   1336  C  CD  . LYS B  1 31  ? 4.436   252.652 26.033 1.00 60.44 ?  30  LYS B CD  1 
ATOM   1337  C  CE  . LYS B  1 31  ? 3.763   253.539 27.097 1.00 61.84 ?  30  LYS B CE  1 
ATOM   1338  N  NZ  . LYS B  1 31  ? 2.659   254.400 26.545 1.00 60.81 ?  30  LYS B NZ  1 
ATOM   1339  N  N   . VAL B  1 32  ? 8.012   250.492 22.472 1.00 29.73 ?  31  VAL B N   1 
ATOM   1340  C  CA  . VAL B  1 32  ? 8.785   250.357 21.239 1.00 29.22 ?  31  VAL B CA  1 
ATOM   1341  C  C   . VAL B  1 32  ? 7.859   250.724 20.095 1.00 27.35 ?  31  VAL B C   1 
ATOM   1342  O  O   . VAL B  1 32  ? 6.822   250.077 19.909 1.00 31.68 ?  31  VAL B O   1 
ATOM   1343  C  CB  . VAL B  1 32  ? 9.321   248.928 21.065 1.00 27.17 ?  31  VAL B CB  1 
ATOM   1344  C  CG1 . VAL B  1 32  ? 10.213  248.830 19.831 1.00 28.41 ?  31  VAL B CG1 1 
ATOM   1345  C  CG2 . VAL B  1 32  ? 10.067  248.500 22.287 1.00 29.33 ?  31  VAL B CG2 1 
ATOM   1346  N  N   . TRP B  1 33  ? 8.214   251.757 19.333 1.00 28.75 ?  32  TRP B N   1 
ATOM   1347  C  CA  . TRP B  1 33  ? 7.335   252.184 18.251 1.00 27.41 ?  32  TRP B CA  1 
ATOM   1348  C  C   . TRP B  1 33  ? 8.138   252.810 17.126 1.00 29.56 ?  32  TRP B C   1 
ATOM   1349  O  O   . TRP B  1 33  ? 9.256   253.287 17.315 1.00 30.26 ?  32  TRP B O   1 
ATOM   1350  C  CB  . TRP B  1 33  ? 6.265   253.168 18.745 1.00 29.48 ?  32  TRP B CB  1 
ATOM   1351  C  CG  . TRP B  1 33  ? 6.751   254.584 18.943 1.00 31.79 ?  32  TRP B CG  1 
ATOM   1352  C  CD1 . TRP B  1 33  ? 6.579   255.632 18.094 1.00 29.10 ?  32  TRP B CD1 1 
ATOM   1353  C  CD2 . TRP B  1 33  ? 7.464   255.100 20.081 1.00 31.28 ?  32  TRP B CD2 1 
ATOM   1354  N  NE1 . TRP B  1 33  ? 7.146   256.774 18.624 1.00 33.25 ?  32  TRP B NE1 1 
ATOM   1355  C  CE2 . TRP B  1 33  ? 7.696   256.471 19.842 1.00 32.53 ?  32  TRP B CE2 1 
ATOM   1356  C  CE3 . TRP B  1 33  ? 7.939   254.531 21.271 1.00 35.71 ?  32  TRP B CE3 1 
ATOM   1357  C  CZ2 . TRP B  1 33  ? 8.375   257.290 20.756 1.00 38.60 ?  32  TRP B CZ2 1 
ATOM   1358  C  CZ3 . TRP B  1 33  ? 8.618   255.347 22.179 1.00 36.31 ?  32  TRP B CZ3 1 
ATOM   1359  C  CH2 . TRP B  1 33  ? 8.824   256.713 21.914 1.00 34.98 ?  32  TRP B CH2 1 
ATOM   1360  N  N   . GLY B  1 34  ? 7.547   252.818 15.958 1.00 28.98 ?  33  GLY B N   1 
ATOM   1361  C  CA  . GLY B  1 34  ? 8.188   253.424 14.815 1.00 29.93 ?  33  GLY B CA  1 
ATOM   1362  C  C   . GLY B  1 34  ? 7.678   252.795 13.543 1.00 31.10 ?  33  GLY B C   1 
ATOM   1363  O  O   . GLY B  1 34  ? 6.648   252.138 13.532 1.00 33.92 ?  33  GLY B O   1 
ATOM   1364  N  N   . SER B  1 35  ? 8.440   252.995 12.479 1.00 32.96 ?  34  SER B N   1 
ATOM   1365  C  CA  . SER B  1 35  ? 8.036   252.580 11.151 1.00 30.13 ?  34  SER B CA  1 
ATOM   1366  C  C   . SER B  1 35  ? 9.193   251.896 10.450 1.00 33.20 ?  34  SER B C   1 
ATOM   1367  O  O   . SER B  1 35  ? 10.325  252.375 10.505 1.00 33.67 ?  34  SER B O   1 
ATOM   1368  C  CB  . SER B  1 35  ? 7.579   253.776 10.327 1.00 35.00 ?  34  SER B CB  1 
ATOM   1369  O  OG  . SER B  1 35  ? 6.670   253.346 9.351  1.00 52.37 ?  34  SER B OG  1 
ATOM   1370  N  N   . ILE B  1 36  ? 8.903   250.776 9.796  1.00 30.04 ?  35  ILE B N   1 
ATOM   1371  C  CA  . ILE B  1 36  ? 9.856   250.085 8.933  1.00 30.38 ?  35  ILE B CA  1 
ATOM   1372  C  C   . ILE B  1 36  ? 9.226   249.975 7.548  1.00 35.68 ?  35  ILE B C   1 
ATOM   1373  O  O   . ILE B  1 36  ? 8.045   249.618 7.431  1.00 34.41 ?  35  ILE B O   1 
ATOM   1374  C  CB  . ILE B  1 36  ? 10.221  248.694 9.488  1.00 30.52 ?  35  ILE B CB  1 
ATOM   1375  C  CG1 . ILE B  1 36  ? 10.661  248.786 10.951 1.00 28.11 ?  35  ILE B CG1 1 
ATOM   1376  C  CG2 . ILE B  1 36  ? 11.308  248.057 8.636  1.00 32.05 ?  35  ILE B CG2 1 
ATOM   1377  C  CD1 . ILE B  1 36  ? 10.923  247.418 11.606 1.00 25.25 ?  35  ILE B CD1 1 
ATOM   1378  N  N   . LYS B  1 37  ? 10.003  250.293 6.506  1.00 31.98 ?  36  LYS B N   1 
ATOM   1379  C  CA  . LYS B  1 37  ? 9.528   250.279 5.128  1.00 31.12 ?  36  LYS B CA  1 
ATOM   1380  C  C   . LYS B  1 37  ? 10.311  249.257 4.325  1.00 30.05 ?  36  LYS B C   1 
ATOM   1381  O  O   . LYS B  1 37  ? 11.391  248.820 4.727  1.00 30.60 ?  36  LYS B O   1 
ATOM   1382  C  CB  . LYS B  1 37  ? 9.684   251.656 4.450  1.00 32.75 ?  36  LYS B CB  1 
ATOM   1383  C  CG  . LYS B  1 37  ? 8.956   252.793 5.151  1.00 47.14 ?  36  LYS B CG  1 
ATOM   1384  C  CD  . LYS B  1 37  ? 9.641   254.168 4.948  1.00 49.18 ?  36  LYS B CD  1 
ATOM   1385  C  CE  . LYS B  1 37  ? 10.752  254.144 3.887  1.00 54.71 ?  36  LYS B CE  1 
ATOM   1386  N  NZ  . LYS B  1 37  ? 11.294  255.525 3.625  1.00 53.99 ?  36  LYS B NZ  1 
ATOM   1387  N  N   . GLY B  1 38  ? 9.775   248.913 3.154  1.00 30.14 ?  37  GLY B N   1 
ATOM   1388  C  CA  . GLY B  1 38  ? 10.472  248.019 2.251  1.00 29.33 ?  37  GLY B CA  1 
ATOM   1389  C  C   . GLY B  1 38  ? 10.334  246.549 2.580  1.00 30.76 ?  37  GLY B C   1 
ATOM   1390  O  O   . GLY B  1 38  ? 11.124  245.743 2.084  1.00 32.61 ?  37  GLY B O   1 
ATOM   1391  N  N   . LEU B  1 39  ? 9.348   246.174 3.390  1.00 29.43 ?  38  LEU B N   1 
ATOM   1392  C  CA  . LEU B  1 39  ? 9.130   244.791 3.807  1.00 30.27 ?  38  LEU B CA  1 
ATOM   1393  C  C   . LEU B  1 39  ? 8.099   244.120 2.910  1.00 31.14 ?  38  LEU B C   1 
ATOM   1394  O  O   . LEU B  1 39  ? 7.176   244.763 2.419  1.00 33.66 ?  38  LEU B O   1 
ATOM   1395  C  CB  . LEU B  1 39  ? 8.637   244.743 5.262  1.00 27.93 ?  38  LEU B CB  1 
ATOM   1396  C  CG  . LEU B  1 39  ? 9.668   245.077 6.335  1.00 26.03 ?  38  LEU B CG  1 
ATOM   1397  C  CD1 . LEU B  1 39  ? 9.002   245.479 7.658  1.00 29.51 ?  38  LEU B CD1 1 
ATOM   1398  C  CD2 . LEU B  1 39  ? 10.566  243.889 6.547  1.00 27.32 ?  38  LEU B CD2 1 
ATOM   1399  N  N   . THR B  1 40  ? 8.244   242.814 2.718  1.00 34.41 ?  39  THR B N   1 
ATOM   1400  C  CA  . THR B  1 40  ? 7.146   242.060 2.131  1.00 32.43 ?  39  THR B CA  1 
ATOM   1401  C  C   . THR B  1 40  ? 5.983   241.981 3.122  1.00 39.11 ?  39  THR B C   1 
ATOM   1402  O  O   . THR B  1 40  ? 6.177   241.977 4.347  1.00 34.41 ?  39  THR B O   1 
ATOM   1403  C  CB  . THR B  1 40  ? 7.609   240.654 1.736  1.00 40.88 ?  39  THR B CB  1 
ATOM   1404  O  OG1 . THR B  1 40  ? 8.136   239.988 2.889  1.00 39.50 ?  39  THR B OG1 1 
ATOM   1405  C  CG2 . THR B  1 40  ? 8.705   240.723 0.690  1.00 37.57 ?  39  THR B CG2 1 
ATOM   1406  N  N   . GLU B  1 41  ? 4.762   241.905 2.579  1.00 33.82 ?  40  GLU B N   1 
ATOM   1407  C  CA  . GLU B  1 41  ? 3.564   241.881 3.415  1.00 37.99 ?  40  GLU B CA  1 
ATOM   1408  C  C   . GLU B  1 41  ? 3.580   240.687 4.371  1.00 35.95 ?  40  GLU B C   1 
ATOM   1409  O  O   . GLU B  1 41  ? 3.955   239.576 3.999  1.00 36.17 ?  40  GLU B O   1 
ATOM   1410  C  CB  . GLU B  1 41  ? 2.302   241.838 2.543  1.00 39.96 ?  40  GLU B CB  1 
ATOM   1411  C  CG  . GLU B  1 41  ? 1.007   241.866 3.353  1.00 46.49 ?  40  GLU B CG  1 
ATOM   1412  C  CD  . GLU B  1 41  ? -0.243  242.001 2.488  1.00 53.39 ?  40  GLU B CD  1 
ATOM   1413  O  OE1 . GLU B  1 41  ? -1.350  242.097 3.066  1.00 60.11 ?  40  GLU B OE1 1 
ATOM   1414  O  OE2 . GLU B  1 41  ? -0.123  242.024 1.243  1.00 51.68 ?  40  GLU B OE2 1 
ATOM   1415  N  N   . GLY B  1 42  ? 3.191   240.929 5.617  1.00 36.21 ?  41  GLY B N   1 
ATOM   1416  C  CA  . GLY B  1 42  ? 3.049   239.870 6.601  1.00 31.78 ?  41  GLY B CA  1 
ATOM   1417  C  C   . GLY B  1 42  ? 4.013   239.994 7.763  1.00 31.86 ?  41  GLY B C   1 
ATOM   1418  O  O   . GLY B  1 42  ? 4.605   241.047 8.023  1.00 30.84 ?  41  GLY B O   1 
ATOM   1419  N  N   . LEU B  1 43  ? 4.196   238.861 8.459  1.00 31.11 ?  42  LEU B N   1 
ATOM   1420  C  CA  . LEU B  1 43  ? 4.946   238.804 9.712  1.00 28.80 ?  42  LEU B CA  1 
ATOM   1421  C  C   . LEU B  1 43  ? 6.454   238.761 9.491  1.00 30.98 ?  42  LEU B C   1 
ATOM   1422  O  O   . LEU B  1 43  ? 6.948   238.060 8.606  1.00 30.53 ?  42  LEU B O   1 
ATOM   1423  C  CB  . LEU B  1 43  ? 4.546   237.567 10.514 1.00 21.43 ?  42  LEU B CB  1 
ATOM   1424  C  CG  . LEU B  1 43  ? 3.114   237.556 11.023 1.00 33.87 ?  42  LEU B CG  1 
ATOM   1425  C  CD1 . LEU B  1 43  ? 2.755   236.160 11.528 1.00 35.73 ?  42  LEU B CD1 1 
ATOM   1426  C  CD2 . LEU B  1 43  ? 2.991   238.592 12.138 1.00 32.39 ?  42  LEU B CD2 1 
ATOM   1427  N  N   . HIS B  1 44  ? 7.191   239.481 10.341 1.00 28.98 ?  43  HIS B N   1 
ATOM   1428  C  CA  . HIS B  1 44  ? 8.649   239.509 10.293 1.00 29.18 ?  43  HIS B CA  1 
ATOM   1429  C  C   . HIS B  1 44  ? 9.192   239.443 11.708 1.00 24.54 ?  43  HIS B C   1 
ATOM   1430  O  O   . HIS B  1 44  ? 8.831   240.277 12.545 1.00 23.05 ?  43  HIS B O   1 
ATOM   1431  C  CB  . HIS B  1 44  ? 9.162   240.781 9.599  1.00 26.74 ?  43  HIS B CB  1 
ATOM   1432  C  CG  . HIS B  1 44  ? 8.865   240.818 8.132  1.00 30.00 ?  43  HIS B CG  1 
ATOM   1433  N  ND1 . HIS B  1 44  ? 9.697   240.242 7.193  1.00 30.26 ?  43  HIS B ND1 1 
ATOM   1434  C  CD2 . HIS B  1 44  ? 7.811   241.323 7.444  1.00 29.19 ?  43  HIS B CD2 1 
ATOM   1435  C  CE1 . HIS B  1 44  ? 9.179   240.406 5.989  1.00 30.72 ?  43  HIS B CE1 1 
ATOM   1436  N  NE2 . HIS B  1 44  ? 8.035   241.061 6.112  1.00 29.50 ?  43  HIS B NE2 1 
ATOM   1437  N  N   . GLY B  1 45  ? 10.052  238.467 11.971 1.00 21.90 ?  44  GLY B N   1 
ATOM   1438  C  CA  . GLY B  1 45  ? 10.687  238.402 13.277 1.00 24.33 ?  44  GLY B CA  1 
ATOM   1439  C  C   . GLY B  1 45  ? 11.444  239.682 13.580 1.00 25.41 ?  44  GLY B C   1 
ATOM   1440  O  O   . GLY B  1 45  ? 12.011  240.326 12.688 1.00 27.07 ?  44  GLY B O   1 
ATOM   1441  N  N   . PHE B  1 46  ? 11.476  240.036 14.860 1.00 24.53 ?  45  PHE B N   1 
ATOM   1442  C  CA  . PHE B  1 46  ? 11.894  241.367 15.312 1.00 24.08 ?  45  PHE B CA  1 
ATOM   1443  C  C   . PHE B  1 46  ? 12.589  241.139 16.645 1.00 24.35 ?  45  PHE B C   1 
ATOM   1444  O  O   . PHE B  1 46  ? 11.914  240.856 17.638 1.00 26.65 ?  45  PHE B O   1 
ATOM   1445  C  CB  . PHE B  1 46  ? 10.660  242.253 15.448 1.00 20.56 ?  45  PHE B CB  1 
ATOM   1446  C  CG  . PHE B  1 46  ? 10.923  243.693 15.777 1.00 24.33 ?  45  PHE B CG  1 
ATOM   1447  C  CD1 . PHE B  1 46  ? 11.470  244.553 14.839 1.00 27.40 ?  45  PHE B CD1 1 
ATOM   1448  C  CD2 . PHE B  1 46  ? 10.511  244.216 16.998 1.00 23.63 ?  45  PHE B CD2 1 
ATOM   1449  C  CE1 . PHE B  1 46  ? 11.656  245.928 15.139 1.00 24.73 ?  45  PHE B CE1 1 
ATOM   1450  C  CE2 . PHE B  1 46  ? 10.696  245.564 17.300 1.00 26.48 ?  45  PHE B CE2 1 
ATOM   1451  C  CZ  . PHE B  1 46  ? 11.275  246.417 16.359 1.00 27.05 ?  45  PHE B CZ  1 
ATOM   1452  N  N   . HIS B  1 47  ? 13.921  241.213 16.672 1.00 22.18 ?  46  HIS B N   1 
ATOM   1453  C  CA  . HIS B  1 47  ? 14.692  240.710 17.802 1.00 20.34 ?  46  HIS B CA  1 
ATOM   1454  C  C   . HIS B  1 47  ? 15.838  241.646 18.145 1.00 27.23 ?  46  HIS B C   1 
ATOM   1455  O  O   . HIS B  1 47  ? 16.437  242.264 17.261 1.00 22.93 ?  46  HIS B O   1 
ATOM   1456  C  CB  . HIS B  1 47  ? 15.281  239.326 17.502 1.00 24.46 ?  46  HIS B CB  1 
ATOM   1457  C  CG  . HIS B  1 47  ? 14.275  238.350 16.979 1.00 27.17 ?  46  HIS B CG  1 
ATOM   1458  N  ND1 . HIS B  1 47  ? 14.394  237.745 15.749 1.00 29.99 ?  46  HIS B ND1 1 
ATOM   1459  C  CD2 . HIS B  1 47  ? 13.137  237.864 17.534 1.00 29.09 ?  46  HIS B CD2 1 
ATOM   1460  C  CE1 . HIS B  1 47  ? 13.369  236.932 15.564 1.00 33.72 ?  46  HIS B CE1 1 
ATOM   1461  N  NE2 . HIS B  1 47  ? 12.589  236.989 16.629 1.00 28.81 ?  46  HIS B NE2 1 
ATOM   1462  N  N   . VAL B  1 48  ? 16.158  241.733 19.437 1.00 20.88 ?  47  VAL B N   1 
ATOM   1463  C  CA  . VAL B  1 48  ? 17.405  242.353 19.860 1.00 20.34 ?  47  VAL B CA  1 
ATOM   1464  C  C   . VAL B  1 48  ? 18.468  241.270 19.877 1.00 26.03 ?  47  VAL B C   1 
ATOM   1465  O  O   . VAL B  1 48  ? 18.326  240.254 20.568 1.00 28.15 ?  47  VAL B O   1 
ATOM   1466  C  CB  . VAL B  1 48  ? 17.288  243.022 21.235 1.00 26.09 ?  47  VAL B CB  1 
ATOM   1467  C  CG1 . VAL B  1 48  ? 18.651  243.589 21.634 1.00 27.04 ?  47  VAL B CG1 1 
ATOM   1468  C  CG2 . VAL B  1 48  ? 16.235  244.113 21.206 1.00 25.09 ?  47  VAL B CG2 1 
ATOM   1469  N  N   . HIS B  1 49  ? 19.519  241.474 19.102 1.00 20.92 ?  48  HIS B N   1 
ATOM   1470  C  CA  . HIS B  1 49  ? 20.653  240.574 19.093 1.00 20.58 ?  48  HIS B CA  1 
ATOM   1471  C  C   . HIS B  1 49  ? 21.744  241.111 20.007 1.00 28.08 ?  48  HIS B C   1 
ATOM   1472  O  O   . HIS B  1 49  ? 21.763  242.290 20.366 1.00 29.21 ?  48  HIS B O   1 
ATOM   1473  C  CB  . HIS B  1 49  ? 21.187  240.396 17.678 1.00 21.14 ?  48  HIS B CB  1 
ATOM   1474  C  CG  . HIS B  1 49  ? 20.261  239.633 16.785 1.00 24.27 ?  48  HIS B CG  1 
ATOM   1475  N  ND1 . HIS B  1 49  ? 20.633  238.463 16.158 1.00 22.62 ?  48  HIS B ND1 1 
ATOM   1476  C  CD2 . HIS B  1 49  ? 18.981  239.874 16.411 1.00 24.99 ?  48  HIS B CD2 1 
ATOM   1477  C  CE1 . HIS B  1 49  ? 19.625  238.021 15.422 1.00 28.66 ?  48  HIS B CE1 1 
ATOM   1478  N  NE2 . HIS B  1 49  ? 18.611  238.860 15.556 1.00 28.25 ?  48  HIS B NE2 1 
ATOM   1479  N  N   . GLU B  1 50  ? 22.687  240.234 20.339 1.00 24.82 ?  49  GLU B N   1 
ATOM   1480  C  CA  . GLU B  1 50  ? 23.536  240.464 21.500 1.00 25.86 ?  49  GLU B CA  1 
ATOM   1481  C  C   . GLU B  1 50  ? 24.537  241.598 21.291 1.00 28.46 ?  49  GLU B C   1 
ATOM   1482  O  O   . GLU B  1 50  ? 24.805  242.364 22.225 1.00 28.90 ?  49  GLU B O   1 
ATOM   1483  C  CB  . GLU B  1 50  ? 24.278  239.180 21.857 1.00 30.60 ?  49  GLU B CB  1 
ATOM   1484  C  CG  . GLU B  1 50  ? 25.232  239.367 23.010 1.00 31.56 ?  49  GLU B CG  1 
ATOM   1485  C  CD  . GLU B  1 50  ? 25.828  238.062 23.493 1.00 37.82 ?  49  GLU B CD  1 
ATOM   1486  O  OE1 . GLU B  1 50  ? 25.598  237.004 22.855 1.00 34.88 ?  49  GLU B OE1 1 
ATOM   1487  O  OE2 . GLU B  1 50  ? 26.536  238.106 24.516 1.00 42.25 ?  49  GLU B OE2 1 
ATOM   1488  N  N   . PHE B  1 51  ? 25.130  241.707 20.108 1.00 26.45 ?  50  PHE B N   1 
ATOM   1489  C  CA  . PHE B  1 51  ? 26.251  242.618 19.895 1.00 29.44 ?  50  PHE B CA  1 
ATOM   1490  C  C   . PHE B  1 51  ? 25.862  243.796 19.023 1.00 30.55 ?  50  PHE B C   1 
ATOM   1491  O  O   . PHE B  1 51  ? 25.188  243.630 18.002 1.00 28.47 ?  50  PHE B O   1 
ATOM   1492  C  CB  . PHE B  1 51  ? 27.436  241.886 19.264 1.00 30.73 ?  50  PHE B CB  1 
ATOM   1493  C  CG  . PHE B  1 51  ? 27.874  240.701 20.068 1.00 30.21 ?  50  PHE B CG  1 
ATOM   1494  C  CD1 . PHE B  1 51  ? 28.250  240.866 21.394 1.00 33.17 ?  50  PHE B CD1 1 
ATOM   1495  C  CD2 . PHE B  1 51  ? 27.878  239.427 19.519 1.00 36.88 ?  50  PHE B CD2 1 
ATOM   1496  C  CE1 . PHE B  1 51  ? 28.635  239.778 22.166 1.00 37.84 ?  50  PHE B CE1 1 
ATOM   1497  C  CE2 . PHE B  1 51  ? 28.269  238.331 20.278 1.00 39.42 ?  50  PHE B CE2 1 
ATOM   1498  C  CZ  . PHE B  1 51  ? 28.642  238.514 21.613 1.00 38.10 ?  50  PHE B CZ  1 
ATOM   1499  N  N   . GLY B  1 52  ? 26.327  244.984 19.417 1.00 25.88 ?  51  GLY B N   1 
ATOM   1500  C  CA  . GLY B  1 52  ? 26.160  246.175 18.614 1.00 27.20 ?  51  GLY B CA  1 
ATOM   1501  C  C   . GLY B  1 52  ? 27.296  246.282 17.619 1.00 35.85 ?  51  GLY B C   1 
ATOM   1502  O  O   . GLY B  1 52  ? 27.956  247.320 17.507 1.00 32.08 ?  51  GLY B O   1 
ATOM   1503  N  N   . ASP B  1 53  ? 27.524  245.185 16.900 1.00 33.13 ?  52  ASP B N   1 
ATOM   1504  C  CA  . ASP B  1 53  ? 28.657  245.005 16.001 1.00 32.80 ?  52  ASP B CA  1 
ATOM   1505  C  C   . ASP B  1 53  ? 28.101  244.827 14.598 1.00 32.22 ?  52  ASP B C   1 
ATOM   1506  O  O   . ASP B  1 53  ? 27.512  243.785 14.283 1.00 31.36 ?  52  ASP B O   1 
ATOM   1507  C  CB  . ASP B  1 53  ? 29.492  243.798 16.432 1.00 32.67 ?  52  ASP B CB  1 
ATOM   1508  C  CG  . ASP B  1 53  ? 30.751  243.606 15.582 1.00 33.66 ?  52  ASP B CG  1 
ATOM   1509  O  OD1 . ASP B  1 53  ? 30.784  244.084 14.431 1.00 31.79 ?  52  ASP B OD1 1 
ATOM   1510  O  OD2 . ASP B  1 53  ? 31.704  242.970 16.078 1.00 35.38 ?  52  ASP B OD2 1 
ATOM   1511  N  N   . ASN B  1 54  ? 28.276  245.850 13.765 1.00 29.04 ?  53  ASN B N   1 
ATOM   1512  C  CA  . ASN B  1 54  ? 27.872  245.820 12.367 1.00 30.86 ?  53  ASN B CA  1 
ATOM   1513  C  C   . ASN B  1 54  ? 29.065  245.739 11.411 1.00 31.25 ?  53  ASN B C   1 
ATOM   1514  O  O   . ASN B  1 54  ? 28.931  246.082 10.231 1.00 32.59 ?  53  ASN B O   1 
ATOM   1515  C  CB  . ASN B  1 54  ? 27.022  247.056 12.056 1.00 31.71 ?  53  ASN B CB  1 
ATOM   1516  C  CG  . ASN B  1 54  ? 26.338  246.973 10.697 1.00 50.71 ?  53  ASN B CG  1 
ATOM   1517  O  OD1 . ASN B  1 54  ? 25.625  246.004 10.406 1.00 54.20 ?  53  ASN B OD1 1 
ATOM   1518  N  ND2 . ASN B  1 54  ? 26.564  247.985 9.847  1.00 43.64 ?  53  ASN B ND2 1 
ATOM   1519  N  N   . THR B  1 55  ? 30.229  245.281 11.881 1.00 32.27 ?  54  THR B N   1 
ATOM   1520  C  CA  . THR B  1 55  ? 31.422  245.306 11.032 1.00 31.08 ?  54  THR B CA  1 
ATOM   1521  C  C   . THR B  1 55  ? 31.271  244.428 9.798  1.00 37.41 ?  54  THR B C   1 
ATOM   1522  O  O   . THR B  1 55  ? 31.816  244.750 8.742  1.00 35.06 ?  54  THR B O   1 
ATOM   1523  C  CB  . THR B  1 55  ? 32.648  244.862 11.817 1.00 30.43 ?  54  THR B CB  1 
ATOM   1524  O  OG1 . THR B  1 55  ? 32.367  243.594 12.396 1.00 31.32 ?  54  THR B OG1 1 
ATOM   1525  C  CG2 . THR B  1 55  ? 32.979  245.859 12.931 1.00 30.15 ?  54  THR B CG2 1 
ATOM   1526  N  N   . ALA B  1 56  ? 30.561  243.310 9.904  1.00 34.09 ?  55  ALA B N   1 
ATOM   1527  C  CA  . ALA B  1 56  ? 30.275  242.543 8.700  1.00 34.10 ?  55  ALA B CA  1 
ATOM   1528  C  C   . ALA B  1 56  ? 28.779  242.554 8.425  1.00 41.01 ?  55  ALA B C   1 
ATOM   1529  O  O   . ALA B  1 56  ? 28.182  241.504 8.173  1.00 42.38 ?  55  ALA B O   1 
ATOM   1530  C  CB  . ALA B  1 56  ? 30.791  241.105 8.832  1.00 34.19 ?  55  ALA B CB  1 
ATOM   1531  N  N   . GLY B  1 57  ? 28.153  243.726 8.493  1.00 33.19 ?  56  GLY B N   1 
ATOM   1532  C  CA  . GLY B  1 57  ? 26.715  243.727 8.300  1.00 37.54 ?  56  GLY B CA  1 
ATOM   1533  C  C   . GLY B  1 57  ? 26.002  243.164 9.529  1.00 38.09 ?  56  GLY B C   1 
ATOM   1534  O  O   . GLY B  1 57  ? 26.576  243.029 10.608 1.00 32.41 ?  56  GLY B O   1 
ATOM   1535  N  N   . CYS B  1 58  ? 24.730  242.802 9.331  1.00 35.50 ?  57  CYS B N   1 
ATOM   1536  C  CA  . CYS B  1 58  ? 23.892  242.302 10.424 1.00 35.62 ?  57  CYS B CA  1 
ATOM   1537  C  C   . CYS B  1 58  ? 24.372  240.973 10.995 1.00 35.72 ?  57  CYS B C   1 
ATOM   1538  O  O   . CYS B  1 58  ? 24.070  240.671 12.157 1.00 31.68 ?  57  CYS B O   1 
ATOM   1539  C  CB  . CYS B  1 58  ? 22.444  242.177 9.950  1.00 32.73 ?  57  CYS B CB  1 
ATOM   1540  S  SG  . CYS B  1 58  ? 21.724  243.794 9.420  1.00 43.26 ?  57  CYS B SG  1 
ATOM   1541  N  N   . THR B  1 59  ? 25.109  240.179 10.213 1.00 31.47 ?  58  THR B N   1 
ATOM   1542  C  CA  . THR B  1 59  ? 25.601  238.891 10.699 1.00 31.90 ?  58  THR B CA  1 
ATOM   1543  C  C   . THR B  1 59  ? 26.433  239.030 11.967 1.00 30.98 ?  58  THR B C   1 
ATOM   1544  O  O   . THR B  1 59  ? 26.379  238.163 12.851 1.00 30.37 ?  58  THR B O   1 
ATOM   1545  C  CB  . THR B  1 59  ? 26.439  238.214 9.621  1.00 41.07 ?  58  THR B CB  1 
ATOM   1546  O  OG1 . THR B  1 59  ? 25.730  238.249 8.385  1.00 48.18 ?  58  THR B OG1 1 
ATOM   1547  C  CG2 . THR B  1 59  ? 26.739  236.773 10.017 1.00 39.84 ?  58  THR B CG2 1 
ATOM   1548  N  N   . SER B  1 60  ? 27.240  240.091 12.072 1.00 30.57 ?  59  SER B N   1 
ATOM   1549  C  CA  . SER B  1 60  ? 28.124  240.215 13.232 1.00 29.16 ?  59  SER B CA  1 
ATOM   1550  C  C   . SER B  1 60  ? 27.395  240.639 14.499 1.00 25.27 ?  59  SER B C   1 
ATOM   1551  O  O   . SER B  1 60  ? 28.024  240.712 15.561 1.00 31.36 ?  59  SER B O   1 
ATOM   1552  C  CB  . SER B  1 60  ? 29.258  241.211 12.951 1.00 34.84 ?  59  SER B CB  1 
ATOM   1553  O  OG  . SER B  1 60  ? 28.889  242.112 11.954 1.00 35.12 ?  59  SER B OG  1 
ATOM   1554  N  N   . ALA B  1 61  ? 26.096  240.921 14.428 1.00 28.78 ?  60  ALA B N   1 
ATOM   1555  C  CA  . ALA B  1 61  ? 25.380  241.209 15.669 1.00 28.39 ?  60  ALA B CA  1 
ATOM   1556  C  C   . ALA B  1 61  ? 25.210  239.978 16.554 1.00 28.55 ?  60  ALA B C   1 
ATOM   1557  O  O   . ALA B  1 61  ? 24.789  240.119 17.709 1.00 29.23 ?  60  ALA B O   1 
ATOM   1558  C  CB  . ALA B  1 61  ? 24.019  241.809 15.362 1.00 25.31 ?  60  ALA B CB  1 
ATOM   1559  N  N   . GLY B  1 62  ? 25.529  238.787 16.057 1.00 29.66 ?  61  GLY B N   1 
ATOM   1560  C  CA  . GLY B  1 62  ? 25.489  237.601 16.883 1.00 31.03 ?  61  GLY B CA  1 
ATOM   1561  C  C   . GLY B  1 62  ? 24.079  237.081 17.052 1.00 30.41 ?  61  GLY B C   1 
ATOM   1562  O  O   . GLY B  1 62  ? 23.170  237.439 16.285 1.00 27.48 ?  61  GLY B O   1 
ATOM   1563  N  N   . PRO B  1 63  ? 23.867  236.241 18.064 1.00 30.52 ?  62  PRO B N   1 
ATOM   1564  C  CA  . PRO B  1 63  ? 22.560  235.609 18.280 1.00 29.31 ?  62  PRO B CA  1 
ATOM   1565  C  C   . PRO B  1 63  ? 21.639  236.535 19.066 1.00 32.40 ?  62  PRO B C   1 
ATOM   1566  O  O   . PRO B  1 63  ? 22.001  237.656 19.410 1.00 27.56 ?  62  PRO B O   1 
ATOM   1567  C  CB  . PRO B  1 63  ? 22.927  234.363 19.087 1.00 32.28 ?  62  PRO B CB  1 
ATOM   1568  C  CG  . PRO B  1 63  ? 24.072  234.838 19.936 1.00 33.60 ?  62  PRO B CG  1 
ATOM   1569  C  CD  . PRO B  1 63  ? 24.868  235.766 19.035 1.00 31.26 ?  62  PRO B CD  1 
ATOM   1570  N  N   . HIS B  1 64  ? 20.430  236.055 19.360 1.00 27.69 ?  63  HIS B N   1 
ATOM   1571  C  CA  . HIS B  1 64  ? 19.522  236.879 20.148 1.00 28.35 ?  63  HIS B CA  1 
ATOM   1572  C  C   . HIS B  1 64  ? 20.141  237.183 21.504 1.00 30.84 ?  63  HIS B C   1 
ATOM   1573  O  O   . HIS B  1 64  ? 20.851  236.355 22.081 1.00 30.07 ?  63  HIS B O   1 
ATOM   1574  C  CB  . HIS B  1 64  ? 18.152  236.188 20.319 1.00 28.20 ?  63  HIS B CB  1 
ATOM   1575  C  CG  . HIS B  1 64  ? 17.431  235.971 19.025 1.00 27.51 ?  63  HIS B CG  1 
ATOM   1576  N  ND1 . HIS B  1 64  ? 16.252  235.276 18.940 1.00 24.97 ?  63  HIS B ND1 1 
ATOM   1577  C  CD2 . HIS B  1 64  ? 17.726  236.365 17.757 1.00 30.84 ?  63  HIS B CD2 1 
ATOM   1578  C  CE1 . HIS B  1 64  ? 15.844  235.238 17.682 1.00 28.37 ?  63  HIS B CE1 1 
ATOM   1579  N  NE2 . HIS B  1 64  ? 16.721  235.893 16.942 1.00 33.25 ?  63  HIS B NE2 1 
ATOM   1580  N  N   . PHE B  1 65  ? 19.913  238.401 21.986 1.00 27.16 ?  64  PHE B N   1 
ATOM   1581  C  CA  . PHE B  1 65  ? 20.377  238.793 23.310 1.00 29.53 ?  64  PHE B CA  1 
ATOM   1582  C  C   . PHE B  1 65  ? 19.700  237.905 24.352 1.00 28.21 ?  64  PHE B C   1 
ATOM   1583  O  O   . PHE B  1 65  ? 18.470  237.903 24.465 1.00 31.14 ?  64  PHE B O   1 
ATOM   1584  C  CB  . PHE B  1 65  ? 20.049  240.270 23.536 1.00 25.21 ?  64  PHE B CB  1 
ATOM   1585  C  CG  . PHE B  1 65  ? 20.456  240.808 24.876 1.00 28.44 ?  64  PHE B CG  1 
ATOM   1586  C  CD1 . PHE B  1 65  ? 21.642  240.426 25.473 1.00 27.55 ?  64  PHE B CD1 1 
ATOM   1587  C  CD2 . PHE B  1 65  ? 19.650  241.732 25.526 1.00 27.02 ?  64  PHE B CD2 1 
ATOM   1588  C  CE1 . PHE B  1 65  ? 22.011  240.930 26.722 1.00 27.56 ?  64  PHE B CE1 1 
ATOM   1589  C  CE2 . PHE B  1 65  ? 20.010  242.243 26.754 1.00 29.77 ?  64  PHE B CE2 1 
ATOM   1590  C  CZ  . PHE B  1 65  ? 21.203  241.836 27.359 1.00 29.89 ?  64  PHE B CZ  1 
ATOM   1591  N  N   . ASN B  1 66  ? 20.509  237.163 25.113 1.00 29.77 ?  65  ASN B N   1 
ATOM   1592  C  CA  . ASN B  1 66  ? 20.049  236.032 25.907 1.00 33.43 ?  65  ASN B CA  1 
ATOM   1593  C  C   . ASN B  1 66  ? 20.910  235.880 27.157 1.00 33.26 ?  65  ASN B C   1 
ATOM   1594  O  O   . ASN B  1 66  ? 21.578  234.852 27.332 1.00 36.04 ?  65  ASN B O   1 
ATOM   1595  C  CB  . ASN B  1 66  ? 20.095  234.752 25.054 1.00 31.61 ?  65  ASN B CB  1 
ATOM   1596  C  CG  . ASN B  1 66  ? 19.496  233.526 25.763 1.00 35.40 ?  65  ASN B CG  1 
ATOM   1597  O  OD1 . ASN B  1 66  ? 18.632  233.638 26.635 1.00 31.42 ?  65  ASN B OD1 1 
ATOM   1598  N  ND2 . ASN B  1 66  ? 19.946  232.347 25.352 1.00 30.58 ?  65  ASN B ND2 1 
ATOM   1599  N  N   . PRO B  1 67  ? 20.930  236.872 28.046 1.00 33.20 ?  66  PRO B N   1 
ATOM   1600  C  CA  . PRO B  1 67  ? 21.796  236.764 29.228 1.00 34.54 ?  66  PRO B CA  1 
ATOM   1601  C  C   . PRO B  1 67  ? 21.392  235.645 30.172 1.00 40.01 ?  66  PRO B C   1 
ATOM   1602  O  O   . PRO B  1 67  ? 22.245  235.125 30.894 1.00 43.26 ?  66  PRO B O   1 
ATOM   1603  C  CB  . PRO B  1 67  ? 21.640  238.135 29.896 1.00 36.35 ?  66  PRO B CB  1 
ATOM   1604  C  CG  . PRO B  1 67  ? 20.298  238.588 29.478 1.00 35.13 ?  66  PRO B CG  1 
ATOM   1605  C  CD  . PRO B  1 67  ? 20.136  238.112 28.063 1.00 29.43 ?  66  PRO B CD  1 
ATOM   1606  N  N   . LEU B  1 68  ? 20.128  235.238 30.178 1.00 37.34 ?  67  LEU B N   1 
ATOM   1607  C  CA  . LEU B  1 68  ? 19.678  234.172 31.064 1.00 38.03 ?  67  LEU B CA  1 
ATOM   1608  C  C   . LEU B  1 68  ? 19.799  232.786 30.439 1.00 41.05 ?  67  LEU B C   1 
ATOM   1609  O  O   . LEU B  1 68  ? 19.331  231.814 31.032 1.00 45.45 ?  67  LEU B O   1 
ATOM   1610  C  CB  . LEU B  1 68  ? 18.246  234.452 31.487 1.00 34.81 ?  67  LEU B CB  1 
ATOM   1611  C  CG  . LEU B  1 68  ? 18.217  235.662 32.426 1.00 41.98 ?  67  LEU B CG  1 
ATOM   1612  C  CD1 . LEU B  1 68  ? 16.814  235.961 32.909 1.00 42.17 ?  67  LEU B CD1 1 
ATOM   1613  C  CD2 . LEU B  1 68  ? 19.162  235.405 33.621 1.00 46.26 ?  67  LEU B CD2 1 
ATOM   1614  N  N   . SER B  1 69  ? 20.396  232.681 29.253 1.00 39.13 ?  68  SER B N   1 
ATOM   1615  C  CA  . SER B  1 69  ? 20.619  231.404 28.565 1.00 41.16 ?  68  SER B CA  1 
ATOM   1616  C  C   . SER B  1 69  ? 19.353  230.544 28.525 1.00 38.20 ?  68  SER B C   1 
ATOM   1617  O  O   . SER B  1 69  ? 19.353  229.371 28.895 1.00 43.73 ?  68  SER B O   1 
ATOM   1618  C  CB  . SER B  1 69  ? 21.782  230.645 29.207 1.00 43.19 ?  68  SER B CB  1 
ATOM   1619  O  OG  . SER B  1 69  ? 22.884  231.509 29.417 1.00 52.47 ?  68  SER B OG  1 
ATOM   1620  N  N   . ARG B  1 70  ? 18.266  231.144 28.069 1.00 38.32 ?  69  ARG B N   1 
ATOM   1621  C  CA  . ARG B  1 70  ? 17.003  230.450 27.896 1.00 33.74 ?  69  ARG B CA  1 
ATOM   1622  C  C   . ARG B  1 70  ? 16.821  230.086 26.433 1.00 39.10 ?  69  ARG B C   1 
ATOM   1623  O  O   . ARG B  1 70  ? 17.609  230.475 25.569 1.00 40.61 ?  69  ARG B O   1 
ATOM   1624  C  CB  . ARG B  1 70  ? 15.847  231.322 28.381 1.00 34.39 ?  69  ARG B CB  1 
ATOM   1625  C  CG  . ARG B  1 70  ? 16.070  231.898 29.767 1.00 42.77 ?  69  ARG B CG  1 
ATOM   1626  C  CD  . ARG B  1 70  ? 15.111  231.308 30.774 1.00 44.72 ?  69  ARG B CD  1 
ATOM   1627  N  NE  . ARG B  1 70  ? 15.287  231.855 32.121 1.00 53.47 ?  69  ARG B NE  1 
ATOM   1628  C  CZ  . ARG B  1 70  ? 14.526  232.795 32.671 1.00 56.66 ?  69  ARG B CZ  1 
ATOM   1629  N  NH1 . ARG B  1 70  ? 13.552  233.381 31.993 1.00 56.40 ?  69  ARG B NH1 1 
ATOM   1630  N  NH2 . ARG B  1 70  ? 14.753  233.161 33.932 1.00 57.97 ?  69  ARG B NH2 1 
ATOM   1631  N  N   . LYS B  1 71  ? 15.780  229.310 26.161 1.00 36.61 ?  70  LYS B N   1 
ATOM   1632  C  CA  . LYS B  1 71  ? 15.428  228.992 24.790 1.00 35.01 ?  70  LYS B CA  1 
ATOM   1633  C  C   . LYS B  1 71  ? 14.589  230.126 24.211 1.00 32.58 ?  70  LYS B C   1 
ATOM   1634  O  O   . LYS B  1 71  ? 13.994  230.930 24.933 1.00 31.03 ?  70  LYS B O   1 
ATOM   1635  C  CB  . LYS B  1 71  ? 14.667  227.662 24.719 1.00 35.89 ?  70  LYS B CB  1 
ATOM   1636  C  CG  . LYS B  1 71  ? 15.551  226.445 25.011 1.00 39.92 ?  70  LYS B CG  1 
ATOM   1637  C  CD  . LYS B  1 71  ? 14.930  225.155 24.505 1.00 49.09 ?  70  LYS B CD  1 
ATOM   1638  C  CE  . LYS B  1 71  ? 15.021  224.048 25.559 1.00 60.03 ?  70  LYS B CE  1 
ATOM   1639  N  NZ  . LYS B  1 71  ? 13.820  223.143 25.585 1.00 62.28 ?  70  LYS B NZ  1 
ATOM   1640  N  N   . HIS B  1 72  ? 14.561  230.185 22.888 1.00 29.74 ?  71  HIS B N   1 
ATOM   1641  C  CA  . HIS B  1 72  ? 13.812  231.222 22.191 1.00 31.14 ?  71  HIS B CA  1 
ATOM   1642  C  C   . HIS B  1 72  ? 12.313  231.052 22.436 1.00 31.44 ?  71  HIS B C   1 
ATOM   1643  O  O   . HIS B  1 72  ? 11.799  229.935 22.505 1.00 29.56 ?  71  HIS B O   1 
ATOM   1644  C  CB  . HIS B  1 72  ? 14.129  231.150 20.694 1.00 24.96 ?  71  HIS B CB  1 
ATOM   1645  C  CG  . HIS B  1 72  ? 13.307  232.074 19.852 1.00 29.90 ?  71  HIS B CG  1 
ATOM   1646  N  ND1 . HIS B  1 72  ? 13.630  233.399 19.661 1.00 28.08 ?  71  HIS B ND1 1 
ATOM   1647  C  CD2 . HIS B  1 72  ? 12.176  231.858 19.137 1.00 27.32 ?  71  HIS B CD2 1 
ATOM   1648  C  CE1 . HIS B  1 72  ? 12.728  233.967 18.881 1.00 30.22 ?  71  HIS B CE1 1 
ATOM   1649  N  NE2 . HIS B  1 72  ? 11.832  233.055 18.552 1.00 30.27 ?  71  HIS B NE2 1 
ATOM   1650  N  N   . GLY B  1 73  ? 11.615  232.171 22.569 1.00 31.88 ?  72  GLY B N   1 
ATOM   1651  C  CA  . GLY B  1 73  ? 10.177  232.158 22.737 1.00 28.28 ?  72  GLY B CA  1 
ATOM   1652  C  C   . GLY B  1 73  ? 9.584   233.423 22.151 1.00 29.35 ?  72  GLY B C   1 
ATOM   1653  O  O   . GLY B  1 73  ? 10.274  234.224 21.510 1.00 31.93 ?  72  GLY B O   1 
ATOM   1654  N  N   . GLY B  1 74  ? 8.285   233.575 22.339 1.00 26.28 ?  73  GLY B N   1 
ATOM   1655  C  CA  . GLY B  1 74  ? 7.632   234.815 21.999 1.00 26.75 ?  73  GLY B CA  1 
ATOM   1656  C  C   . GLY B  1 74  ? 7.695   235.733 23.198 1.00 29.14 ?  73  GLY B C   1 
ATOM   1657  O  O   . GLY B  1 74  ? 8.015   235.300 24.308 1.00 29.86 ?  73  GLY B O   1 
ATOM   1658  N  N   . PRO B  1 75  ? 7.371   237.013 23.002 1.00 28.26 ?  74  PRO B N   1 
ATOM   1659  C  CA  . PRO B  1 75  ? 7.509   237.979 24.108 1.00 27.76 ?  74  PRO B CA  1 
ATOM   1660  C  C   . PRO B  1 75  ? 6.673   237.644 25.317 1.00 35.59 ?  74  PRO B C   1 
ATOM   1661  O  O   . PRO B  1 75  ? 7.058   238.008 26.434 1.00 32.60 ?  74  PRO B O   1 
ATOM   1662  C  CB  . PRO B  1 75  ? 7.066   239.312 23.485 1.00 27.69 ?  74  PRO B CB  1 
ATOM   1663  C  CG  . PRO B  1 75  ? 6.437   238.955 22.132 1.00 29.52 ?  74  PRO B CG  1 
ATOM   1664  C  CD  . PRO B  1 75  ? 7.053   237.664 21.718 1.00 26.99 ?  74  PRO B CD  1 
ATOM   1665  N  N   . LYS B  1 76  ? 5.541   236.960 25.137 1.00 31.99 ?  75  LYS B N   1 
ATOM   1666  C  CA  . LYS B  1 76  ? 4.657   236.641 26.248 1.00 34.57 ?  75  LYS B CA  1 
ATOM   1667  C  C   . LYS B  1 76  ? 5.106   235.435 27.054 1.00 32.36 ?  75  LYS B C   1 
ATOM   1668  O  O   . LYS B  1 76  ? 4.550   235.189 28.127 1.00 37.16 ?  75  LYS B O   1 
ATOM   1669  C  CB  . LYS B  1 76  ? 3.246   236.407 25.727 1.00 35.87 ?  75  LYS B CB  1 
ATOM   1670  C  CG  . LYS B  1 76  ? 2.702   237.603 24.976 1.00 38.09 ?  75  LYS B CG  1 
ATOM   1671  C  CD  . LYS B  1 76  ? 1.602   237.163 24.036 1.00 42.14 ?  75  LYS B CD  1 
ATOM   1672  C  CE  . LYS B  1 76  ? 0.250   237.190 24.754 1.00 46.94 ?  75  LYS B CE  1 
ATOM   1673  N  NZ  . LYS B  1 76  ? -0.578  235.982 24.420 1.00 50.27 ?  75  LYS B NZ  1 
ATOM   1674  N  N   . ASP B  1 77  ? 6.090   234.685 26.583 1.00 30.53 ?  76  ASP B N   1 
ATOM   1675  C  CA  . ASP B  1 77  ? 6.502   233.472 27.260 1.00 35.89 ?  76  ASP B CA  1 
ATOM   1676  C  C   . ASP B  1 77  ? 7.448   233.793 28.410 1.00 37.86 ?  76  ASP B C   1 
ATOM   1677  O  O   . ASP B  1 77  ? 8.221   234.748 28.355 1.00 36.22 ?  76  ASP B O   1 
ATOM   1678  C  CB  . ASP B  1 77  ? 7.207   232.529 26.282 1.00 36.11 ?  76  ASP B CB  1 
ATOM   1679  C  CG  . ASP B  1 77  ? 6.293   232.043 25.176 1.00 38.45 ?  76  ASP B CG  1 
ATOM   1680  O  OD1 . ASP B  1 77  ? 5.092   231.856 25.454 1.00 50.75 ?  76  ASP B OD1 1 
ATOM   1681  O  OD2 . ASP B  1 77  ? 6.760   231.870 24.023 1.00 45.27 ?  76  ASP B OD2 1 
ATOM   1682  N  N   . GLU B  1 78  ? 7.415   232.955 29.445 1.00 36.74 ?  77  GLU B N   1 
ATOM   1683  C  CA  . GLU B  1 78  ? 8.424   233.063 30.495 1.00 38.07 ?  77  GLU B CA  1 
ATOM   1684  C  C   . GLU B  1 78  ? 9.763   232.519 30.020 1.00 37.59 ?  77  GLU B C   1 
ATOM   1685  O  O   . GLU B  1 78  ? 10.821  233.040 30.400 1.00 41.41 ?  77  GLU B O   1 
ATOM   1686  C  CB  . GLU B  1 78  ? 7.964   232.319 31.757 1.00 41.32 ?  77  GLU B CB  1 
ATOM   1687  C  CG  . GLU B  1 78  ? 8.511   232.895 33.073 1.00 54.95 ?  77  GLU B CG  1 
ATOM   1688  C  CD  . GLU B  1 78  ? 8.451   231.907 34.245 1.00 71.58 ?  77  GLU B CD  1 
ATOM   1689  O  OE1 . GLU B  1 78  ? 8.672   232.345 35.401 1.00 74.50 ?  77  GLU B OE1 1 
ATOM   1690  O  OE2 . GLU B  1 78  ? 8.196   230.699 34.016 1.00 80.50 ?  77  GLU B OE2 1 
ATOM   1691  N  N   . GLU B  1 79  ? 9.734   231.486 29.187 1.00 32.46 ?  78  GLU B N   1 
ATOM   1692  C  CA  . GLU B  1 79  ? 10.936  230.955 28.559 1.00 36.59 ?  78  GLU B CA  1 
ATOM   1693  C  C   . GLU B  1 79  ? 11.124  231.713 27.252 1.00 36.03 ?  78  GLU B C   1 
ATOM   1694  O  O   . GLU B  1 79  ? 10.441  231.450 26.257 1.00 36.82 ?  78  GLU B O   1 
ATOM   1695  C  CB  . GLU B  1 79  ? 10.812  229.450 28.356 1.00 32.06 ?  78  GLU B CB  1 
ATOM   1696  C  CG  . GLU B  1 79  ? 12.055  228.771 27.795 1.00 41.41 ?  78  GLU B CG  1 
ATOM   1697  C  CD  . GLU B  1 79  ? 13.146  228.648 28.832 1.00 42.74 ?  78  GLU B CD  1 
ATOM   1698  O  OE1 . GLU B  1 79  ? 12.832  228.898 30.019 1.00 53.54 ?  78  GLU B OE1 1 
ATOM   1699  O  OE2 . GLU B  1 79  ? 14.294  228.276 28.491 1.00 45.98 ?  78  GLU B OE2 1 
ATOM   1700  N  N   . ARG B  1 80  ? 12.027  232.689 27.267 1.00 33.51 ?  79  ARG B N   1 
ATOM   1701  C  CA  . ARG B  1 80  ? 12.312  233.502 26.088 1.00 30.30 ?  79  ARG B CA  1 
ATOM   1702  C  C   . ARG B  1 80  ? 13.670  234.142 26.290 1.00 33.23 ?  79  ARG B C   1 
ATOM   1703  O  O   . ARG B  1 80  ? 14.146  234.266 27.418 1.00 31.75 ?  79  ARG B O   1 
ATOM   1704  C  CB  . ARG B  1 80  ? 11.263  234.587 25.879 1.00 26.63 ?  79  ARG B CB  1 
ATOM   1705  C  CG  . ARG B  1 80  ? 11.200  235.553 27.047 1.00 27.66 ?  79  ARG B CG  1 
ATOM   1706  C  CD  . ARG B  1 80  ? 10.354  236.750 26.721 1.00 29.56 ?  79  ARG B CD  1 
ATOM   1707  N  NE  . ARG B  1 80  ? 11.157  237.841 26.168 1.00 30.52 ?  79  ARG B NE  1 
ATOM   1708  C  CZ  . ARG B  1 80  ? 10.728  239.090 26.083 1.00 25.98 ?  79  ARG B CZ  1 
ATOM   1709  N  NH1 . ARG B  1 80  ? 9.518   239.428 26.501 1.00 24.92 ?  79  ARG B NH1 1 
ATOM   1710  N  NH2 . ARG B  1 80  ? 11.529  240.021 25.567 1.00 27.87 ?  79  ARG B NH2 1 
ATOM   1711  N  N   . HIS B  1 81  ? 14.292  234.528 25.188 1.00 31.37 ?  80  HIS B N   1 
ATOM   1712  C  CA  . HIS B  1 81  ? 15.449  235.406 25.270 1.00 28.39 ?  80  HIS B CA  1 
ATOM   1713  C  C   . HIS B  1 81  ? 14.996  236.805 25.646 1.00 23.15 ?  80  HIS B C   1 
ATOM   1714  O  O   . HIS B  1 81  ? 13.873  237.215 25.348 1.00 29.56 ?  80  HIS B O   1 
ATOM   1715  C  CB  . HIS B  1 81  ? 16.181  235.451 23.921 1.00 24.17 ?  80  HIS B CB  1 
ATOM   1716  C  CG  . HIS B  1 81  ? 16.575  234.108 23.403 1.00 30.04 ?  80  HIS B CG  1 
ATOM   1717  N  ND1 . HIS B  1 81  ? 16.594  233.807 22.060 1.00 27.64 ?  80  HIS B ND1 1 
ATOM   1718  C  CD2 . HIS B  1 81  ? 17.000  232.993 24.045 1.00 30.36 ?  80  HIS B CD2 1 
ATOM   1719  C  CE1 . HIS B  1 81  ? 17.011  232.565 21.896 1.00 32.20 ?  80  HIS B CE1 1 
ATOM   1720  N  NE2 . HIS B  1 81  ? 17.270  232.052 23.086 1.00 31.33 ?  80  HIS B NE2 1 
ATOM   1721  N  N   . VAL B  1 82  ? 15.880  237.554 26.303 1.00 28.65 ?  81  VAL B N   1 
ATOM   1722  C  CA  . VAL B  1 82  ? 15.557  238.951 26.567 1.00 26.05 ?  81  VAL B CA  1 
ATOM   1723  C  C   . VAL B  1 82  ? 15.246  239.664 25.257 1.00 23.83 ?  81  VAL B C   1 
ATOM   1724  O  O   . VAL B  1 82  ? 14.298  240.446 25.169 1.00 26.76 ?  81  VAL B O   1 
ATOM   1725  C  CB  . VAL B  1 82  ? 16.706  239.634 27.340 1.00 30.60 ?  81  VAL B CB  1 
ATOM   1726  C  CG1 . VAL B  1 82  ? 16.519  241.127 27.375 1.00 26.79 ?  81  VAL B CG1 1 
ATOM   1727  C  CG2 . VAL B  1 82  ? 16.796  239.105 28.758 1.00 28.67 ?  81  VAL B CG2 1 
ATOM   1728  N  N   . GLY B  1 83  ? 15.992  239.356 24.205 1.00 26.11 ?  82  GLY B N   1 
ATOM   1729  C  CA  . GLY B  1 83  ? 15.767  240.048 22.946 1.00 24.17 ?  82  GLY B CA  1 
ATOM   1730  C  C   . GLY B  1 83  ? 14.552  239.615 22.134 1.00 30.52 ?  82  GLY B C   1 
ATOM   1731  O  O   . GLY B  1 83  ? 14.362  240.144 21.031 1.00 22.54 ?  82  GLY B O   1 
ATOM   1732  N  N   . ASP B  1 84  ? 13.711  238.704 22.635 1.00 26.27 ?  83  ASP B N   1 
ATOM   1733  C  CA  . ASP B  1 84  ? 12.613  238.139 21.839 1.00 26.91 ?  83  ASP B CA  1 
ATOM   1734  C  C   . ASP B  1 84  ? 11.415  239.074 21.861 1.00 27.66 ?  83  ASP B C   1 
ATOM   1735  O  O   . ASP B  1 84  ? 10.552  238.987 22.736 1.00 30.88 ?  83  ASP B O   1 
ATOM   1736  C  CB  . ASP B  1 84  ? 12.210  236.765 22.376 1.00 25.82 ?  83  ASP B CB  1 
ATOM   1737  C  CG  . ASP B  1 84  ? 13.249  235.688 22.096 1.00 29.63 ?  83  ASP B CG  1 
ATOM   1738  O  OD1 . ASP B  1 84  ? 14.091  235.915 21.198 1.00 24.44 ?  83  ASP B OD1 1 
ATOM   1739  O  OD2 . ASP B  1 84  ? 13.230  234.613 22.767 1.00 24.78 ?  83  ASP B OD2 1 
ATOM   1740  N  N   . LEU B  1 85  ? 11.318  239.951 20.867 1.00 25.86 ?  84  LEU B N   1 
ATOM   1741  C  CA  . LEU B  1 85  ? 10.182  240.852 20.755 1.00 25.07 ?  84  LEU B CA  1 
ATOM   1742  C  C   . LEU B  1 85  ? 9.142   240.357 19.754 1.00 28.10 ?  84  LEU B C   1 
ATOM   1743  O  O   . LEU B  1 85  ? 8.254   241.122 19.366 1.00 31.79 ?  84  LEU B O   1 
ATOM   1744  C  CB  . LEU B  1 85  ? 10.661  242.263 20.378 1.00 23.78 ?  84  LEU B CB  1 
ATOM   1745  C  CG  . LEU B  1 85  ? 11.641  242.905 21.372 1.00 28.21 ?  84  LEU B CG  1 
ATOM   1746  C  CD1 . LEU B  1 85  ? 12.028  244.314 20.930 1.00 28.29 ?  84  LEU B CD1 1 
ATOM   1747  C  CD2 . LEU B  1 85  ? 11.070  242.938 22.777 1.00 28.17 ?  84  LEU B CD2 1 
ATOM   1748  N  N   . GLY B  1 86  ? 9.242   239.109 19.311 1.00 20.40 ?  85  GLY B N   1 
ATOM   1749  C  CA  . GLY B  1 86  ? 8.201   238.511 18.500 1.00 21.50 ?  85  GLY B CA  1 
ATOM   1750  C  C   . GLY B  1 86  ? 8.231   238.966 17.049 1.00 29.66 ?  85  GLY B C   1 
ATOM   1751  O  O   . GLY B  1 86  ? 9.298   239.076 16.440 1.00 29.70 ?  85  GLY B O   1 
ATOM   1752  N  N   . ASN B  1 87  ? 7.060   239.250 16.496 1.00 24.05 ?  86  ASN B N   1 
ATOM   1753  C  CA  . ASN B  1 87  ? 6.918   239.648 15.106 1.00 26.08 ?  86  ASN B CA  1 
ATOM   1754  C  C   . ASN B  1 87  ? 6.441   241.083 15.009 1.00 27.90 ?  86  ASN B C   1 
ATOM   1755  O  O   . ASN B  1 87  ? 5.781   241.596 15.919 1.00 27.98 ?  86  ASN B O   1 
ATOM   1756  C  CB  . ASN B  1 87  ? 5.911   238.755 14.390 1.00 24.21 ?  86  ASN B CB  1 
ATOM   1757  C  CG  . ASN B  1 87  ? 6.442   237.377 14.172 1.00 29.62 ?  86  ASN B CG  1 
ATOM   1758  O  OD1 . ASN B  1 87  ? 7.477   237.201 13.514 1.00 29.80 ?  86  ASN B OD1 1 
ATOM   1759  N  ND2 . ASN B  1 87  ? 5.764   236.382 14.728 1.00 23.86 ?  86  ASN B ND2 1 
ATOM   1760  N  N   . VAL B  1 88  ? 6.760   241.712 13.889 1.00 21.69 ?  87  VAL B N   1 
ATOM   1761  C  CA  . VAL B  1 88  ? 6.057   242.898 13.444 1.00 24.64 ?  87  VAL B CA  1 
ATOM   1762  C  C   . VAL B  1 88  ? 5.385   242.553 12.126 1.00 26.93 ?  87  VAL B C   1 
ATOM   1763  O  O   . VAL B  1 88  ? 5.769   241.613 11.425 1.00 31.88 ?  87  VAL B O   1 
ATOM   1764  C  CB  . VAL B  1 88  ? 6.978   244.122 13.298 1.00 27.20 ?  87  VAL B CB  1 
ATOM   1765  C  CG1 . VAL B  1 88  ? 7.553   244.499 14.667 1.00 28.54 ?  87  VAL B CG1 1 
ATOM   1766  C  CG2 . VAL B  1 88  ? 8.073   243.822 12.295 1.00 25.93 ?  87  VAL B CG2 1 
ATOM   1767  N  N   . THR B  1 89  ? 4.344   243.307 11.807 1.00 25.86 ?  88  THR B N   1 
ATOM   1768  C  CA  . THR B  1 89  ? 3.473   242.994 10.687 1.00 30.28 ?  88  THR B CA  1 
ATOM   1769  C  C   . THR B  1 89  ? 3.569   244.110 9.661  1.00 29.69 ?  88  THR B C   1 
ATOM   1770  O  O   . THR B  1 89  ? 3.304   245.266 9.981  1.00 31.56 ?  88  THR B O   1 
ATOM   1771  C  CB  . THR B  1 89  ? 2.026   242.814 11.141 1.00 31.87 ?  88  THR B CB  1 
ATOM   1772  O  OG1 . THR B  1 89  ? 1.935   241.646 11.966 1.00 28.81 ?  88  THR B OG1 1 
ATOM   1773  C  CG2 . THR B  1 89  ? 1.106   242.664 9.927  1.00 31.81 ?  88  THR B CG2 1 
ATOM   1774  N  N   . ALA B  1 90  ? 3.951   243.755 8.437  1.00 30.97 ?  89  ALA B N   1 
ATOM   1775  C  CA  . ALA B  1 90  ? 4.022   244.712 7.346  1.00 33.27 ?  89  ALA B CA  1 
ATOM   1776  C  C   . ALA B  1 90  ? 2.712   244.677 6.572  1.00 36.23 ?  89  ALA B C   1 
ATOM   1777  O  O   . ALA B  1 90  ? 2.203   243.596 6.256  1.00 33.26 ?  89  ALA B O   1 
ATOM   1778  C  CB  . ALA B  1 90  ? 5.195   244.389 6.417  1.00 31.51 ?  89  ALA B CB  1 
ATOM   1779  N  N   . ASP B  1 91  ? 2.164   245.857 6.284  1.00 34.19 ?  90  ASP B N   1 
ATOM   1780  C  CA  . ASP B  1 91  ? 0.918   245.944 5.536  1.00 37.30 ?  90  ASP B CA  1 
ATOM   1781  C  C   . ASP B  1 91  ? 1.208   245.749 4.048  1.00 39.48 ?  90  ASP B C   1 
ATOM   1782  O  O   . ASP B  1 91  ? 2.334   245.441 3.642  1.00 36.61 ?  90  ASP B O   1 
ATOM   1783  C  CB  . ASP B  1 91  ? 0.190   247.254 5.848  1.00 34.93 ?  90  ASP B CB  1 
ATOM   1784  C  CG  . ASP B  1 91  ? 0.939   248.525 5.367  1.00 41.31 ?  90  ASP B CG  1 
ATOM   1785  O  OD1 . ASP B  1 91  ? 1.728   248.482 4.392  1.00 38.90 ?  90  ASP B OD1 1 
ATOM   1786  O  OD2 . ASP B  1 91  ? 0.686   249.600 5.970  1.00 40.82 ?  90  ASP B OD2 1 
ATOM   1787  N  N   . LYS B  1 92  ? 0.181   245.936 3.210  1.00 40.41 ?  91  LYS B N   1 
ATOM   1788  C  CA  . LYS B  1 92  ? 0.333   245.661 1.786  1.00 39.06 ?  91  LYS B CA  1 
ATOM   1789  C  C   . LYS B  1 92  ? 1.195   246.696 1.074  1.00 44.41 ?  91  LYS B C   1 
ATOM   1790  O  O   . LYS B  1 92  ? 1.641   246.437 -0.047 1.00 47.22 ?  91  LYS B O   1 
ATOM   1791  C  CB  . LYS B  1 92  ? -1.039  245.568 1.115  1.00 49.95 ?  91  LYS B CB  1 
ATOM   1792  C  CG  . LYS B  1 92  ? -1.546  246.874 0.530  1.00 54.63 ?  91  LYS B CG  1 
ATOM   1793  C  CD  . LYS B  1 92  ? -3.015  246.773 0.096  1.00 63.80 ?  91  LYS B CD  1 
ATOM   1794  C  CE  . LYS B  1 92  ? -3.779  248.082 0.306  1.00 57.40 ?  91  LYS B CE  1 
ATOM   1795  N  NZ  . LYS B  1 92  ? -4.149  248.299 1.733  1.00 62.70 ?  91  LYS B NZ  1 
ATOM   1796  N  N   . ASP B  1 93  ? 1.435   247.855 1.689  1.00 40.47 ?  92  ASP B N   1 
ATOM   1797  C  CA  . ASP B  1 93  ? 2.396   248.822 1.172  1.00 45.11 ?  92  ASP B CA  1 
ATOM   1798  C  C   . ASP B  1 93  ? 3.819   248.559 1.644  1.00 44.61 ?  92  ASP B C   1 
ATOM   1799  O  O   . ASP B  1 93  ? 4.703   249.381 1.386  1.00 43.70 ?  92  ASP B O   1 
ATOM   1800  C  CB  . ASP B  1 93  ? 2.006   250.240 1.580  1.00 46.75 ?  92  ASP B CB  1 
ATOM   1801  C  CG  . ASP B  1 93  ? 0.703   250.682 0.964  1.00 56.92 ?  92  ASP B CG  1 
ATOM   1802  O  OD1 . ASP B  1 93  ? 0.271   250.052 -0.033 1.00 52.70 ?  92  ASP B OD1 1 
ATOM   1803  O  OD2 . ASP B  1 93  ? 0.119   251.666 1.477  1.00 60.25 ?  92  ASP B OD2 1 
ATOM   1804  N  N   . GLY B  1 94  ? 4.059   247.455 2.338  1.00 39.84 ?  93  GLY B N   1 
ATOM   1805  C  CA  . GLY B  1 94  ? 5.399   247.155 2.793  1.00 41.67 ?  93  GLY B CA  1 
ATOM   1806  C  C   . GLY B  1 94  ? 5.812   247.859 4.063  1.00 36.21 ?  93  GLY B C   1 
ATOM   1807  O  O   . GLY B  1 94  ? 7.003   247.858 4.396  1.00 35.68 ?  93  GLY B O   1 
ATOM   1808  N  N   . VAL B  1 95  ? 4.869   248.442 4.799  1.00 34.60 ?  94  VAL B N   1 
ATOM   1809  C  CA  . VAL B  1 95  ? 5.174   249.225 5.991  1.00 31.66 ?  94  VAL B CA  1 
ATOM   1810  C  C   . VAL B  1 95  ? 4.729   248.456 7.229  1.00 34.56 ?  94  VAL B C   1 
ATOM   1811  O  O   . VAL B  1 95  ? 3.565   248.056 7.333  1.00 36.71 ?  94  VAL B O   1 
ATOM   1812  C  CB  . VAL B  1 95  ? 4.495   250.601 5.940  1.00 34.40 ?  94  VAL B CB  1 
ATOM   1813  C  CG1 . VAL B  1 95  ? 4.659   251.308 7.264  1.00 33.88 ?  94  VAL B CG1 1 
ATOM   1814  C  CG2 . VAL B  1 95  ? 5.059   251.432 4.785  1.00 34.57 ?  94  VAL B CG2 1 
ATOM   1815  N  N   . ALA B  1 96  ? 5.648   248.276 8.177  1.00 30.90 ?  95  ALA B N   1 
ATOM   1816  C  CA  . ALA B  1 96  ? 5.324   247.823 9.527  1.00 30.14 ?  95  ALA B CA  1 
ATOM   1817  C  C   . ALA B  1 96  ? 5.293   249.035 10.455 1.00 33.39 ?  95  ALA B C   1 
ATOM   1818  O  O   . ALA B  1 96  ? 6.340   249.624 10.754 1.00 30.54 ?  95  ALA B O   1 
ATOM   1819  C  CB  . ALA B  1 96  ? 6.341   246.796 10.023 1.00 28.87 ?  95  ALA B CB  1 
ATOM   1820  N  N   . ASP B  1 97  ? 4.096   249.412 10.908 1.00 31.63 ?  96  ASP B N   1 
ATOM   1821  C  CA  . ASP B  1 97  ? 3.929   250.464 11.913 1.00 32.83 ?  96  ASP B CA  1 
ATOM   1822  C  C   . ASP B  1 97  ? 4.071   249.843 13.300 1.00 34.45 ?  96  ASP B C   1 
ATOM   1823  O  O   . ASP B  1 97  ? 3.092   249.454 13.941 1.00 36.56 ?  96  ASP B O   1 
ATOM   1824  C  CB  . ASP B  1 97  ? 2.583   251.148 11.727 1.00 31.29 ?  96  ASP B CB  1 
ATOM   1825  C  CG  . ASP B  1 97  ? 2.581   252.091 10.540 1.00 43.72 ?  96  ASP B CG  1 
ATOM   1826  O  OD1 . ASP B  1 97  ? 1.621   252.045 9.739  1.00 42.90 ?  96  ASP B OD1 1 
ATOM   1827  O  OD2 . ASP B  1 97  ? 3.533   252.900 10.432 1.00 45.77 ?  96  ASP B OD2 1 
ATOM   1828  N  N   . VAL B  1 98  ? 5.306   249.777 13.790 1.00 31.64 ?  97  VAL B N   1 
ATOM   1829  C  CA  . VAL B  1 98  ? 5.581   248.997 14.991 1.00 28.60 ?  97  VAL B CA  1 
ATOM   1830  C  C   . VAL B  1 98  ? 5.009   249.680 16.220 1.00 31.12 ?  97  VAL B C   1 
ATOM   1831  O  O   . VAL B  1 98  ? 5.075   250.907 16.358 1.00 31.32 ?  97  VAL B O   1 
ATOM   1832  C  CB  . VAL B  1 98  ? 7.091   248.764 15.145 1.00 27.16 ?  97  VAL B CB  1 
ATOM   1833  C  CG1 . VAL B  1 98  ? 7.368   247.977 16.421 1.00 28.17 ?  97  VAL B CG1 1 
ATOM   1834  C  CG2 . VAL B  1 98  ? 7.622   248.015 13.915 1.00 25.57 ?  97  VAL B CG2 1 
ATOM   1835  N  N   . SER B  1 99  ? 4.437   248.871 17.123 1.00 28.23 ?  98  SER B N   1 
ATOM   1836  C  CA  . SER B  1 99  ? 3.896   249.343 18.400 1.00 33.82 ?  98  SER B CA  1 
ATOM   1837  C  C   . SER B  1 99  ? 3.927   248.154 19.353 1.00 33.78 ?  98  SER B C   1 
ATOM   1838  O  O   . SER B  1 99  ? 3.060   247.276 19.301 1.00 35.18 ?  98  SER B O   1 
ATOM   1839  C  CB  . SER B  1 99  ? 2.489   249.906 18.258 1.00 41.37 ?  98  SER B CB  1 
ATOM   1840  O  OG  . SER B  1 99  ? 2.040   250.455 19.492 1.00 45.67 ?  98  SER B OG  1 
ATOM   1841  N  N   . ILE B  1 100 ? 4.931   248.131 20.211 1.00 34.66 ?  99  ILE B N   1 
ATOM   1842  C  CA  . ILE B  1 100 ? 5.180   247.018 21.112 1.00 30.88 ?  99  ILE B CA  1 
ATOM   1843  C  C   . ILE B  1 100 ? 5.466   247.594 22.487 1.00 35.31 ?  99  ILE B C   1 
ATOM   1844  O  O   . ILE B  1 100 ? 6.019   248.692 22.618 1.00 32.99 ?  99  ILE B O   1 
ATOM   1845  C  CB  . ILE B  1 100 ? 6.352   246.145 20.605 1.00 30.36 ?  99  ILE B CB  1 
ATOM   1846  C  CG1 . ILE B  1 100 ? 5.842   245.099 19.622 1.00 32.41 ?  99  ILE B CG1 1 
ATOM   1847  C  CG2 . ILE B  1 100 ? 7.076   245.430 21.730 1.00 32.61 ?  99  ILE B CG2 1 
ATOM   1848  C  CD1 . ILE B  1 100 ? 6.952   244.552 18.733 1.00 36.52 ?  99  ILE B CD1 1 
ATOM   1849  N  N   . GLU B  1 101 ? 5.050   246.871 23.516 1.00 35.02 ?  100 GLU B N   1 
ATOM   1850  C  CA  . GLU B  1 101 ? 5.412   247.198 24.882 1.00 37.80 ?  100 GLU B CA  1 
ATOM   1851  C  C   . GLU B  1 101 ? 5.960   245.934 25.521 1.00 37.19 ?  100 GLU B C   1 
ATOM   1852  O  O   . GLU B  1 101 ? 5.337   244.872 25.437 1.00 34.15 ?  100 GLU B O   1 
ATOM   1853  C  CB  . GLU B  1 101 ? 4.201   247.753 25.637 1.00 39.74 ?  100 GLU B CB  1 
ATOM   1854  C  CG  . GLU B  1 101 ? 4.451   248.042 27.090 1.00 50.24 ?  100 GLU B CG  1 
ATOM   1855  C  CD  . GLU B  1 101 ? 3.191   248.528 27.814 1.00 60.50 ?  100 GLU B CD  1 
ATOM   1856  O  OE1 . GLU B  1 101 ? 2.599   249.544 27.370 1.00 61.25 ?  100 GLU B OE1 1 
ATOM   1857  O  OE2 . GLU B  1 101 ? 2.809   247.897 28.825 1.00 57.96 ?  100 GLU B OE2 1 
ATOM   1858  N  N   . ASP B  1 102 ? 7.136   246.032 26.124 1.00 31.12 ?  101 ASP B N   1 
ATOM   1859  C  CA  . ASP B  1 102 ? 7.776   244.849 26.667 1.00 31.73 ?  101 ASP B CA  1 
ATOM   1860  C  C   . ASP B  1 102 ? 8.426   245.186 27.997 1.00 32.57 ?  101 ASP B C   1 
ATOM   1861  O  O   . ASP B  1 102 ? 9.037   246.250 28.139 1.00 34.11 ?  101 ASP B O   1 
ATOM   1862  C  CB  . ASP B  1 102 ? 8.829   244.304 25.696 1.00 28.96 ?  101 ASP B CB  1 
ATOM   1863  C  CG  . ASP B  1 102 ? 9.299   242.934 26.093 1.00 32.73 ?  101 ASP B CG  1 
ATOM   1864  O  OD1 . ASP B  1 102 ? 8.505   241.974 25.934 1.00 37.64 ?  101 ASP B OD1 1 
ATOM   1865  O  OD2 . ASP B  1 102 ? 10.445  242.809 26.583 1.00 30.93 ?  101 ASP B OD2 1 
ATOM   1866  N  N   A SER B  1 103 ? 8.308   244.272 28.961 0.50 32.11 ?  102 SER B N   1 
ATOM   1867  N  N   B SER B  1 103 ? 8.302   244.281 28.969 0.50 32.16 ?  102 SER B N   1 
ATOM   1868  C  CA  A SER B  1 103 ? 8.835   244.484 30.305 0.50 33.84 ?  102 SER B CA  1 
ATOM   1869  C  CA  B SER B  1 103 ? 8.853   244.504 30.301 0.50 33.88 ?  102 SER B CA  1 
ATOM   1870  C  C   A SER B  1 103 ? 10.048  243.615 30.605 0.50 33.07 ?  102 SER B C   1 
ATOM   1871  C  C   B SER B  1 103 ? 10.038  243.601 30.609 0.50 32.88 ?  102 SER B C   1 
ATOM   1872  O  O   A SER B  1 103 ? 10.522  243.604 31.745 0.50 31.65 ?  102 SER B O   1 
ATOM   1873  O  O   B SER B  1 103 ? 10.482  243.554 31.760 0.50 31.64 ?  102 SER B O   1 
ATOM   1874  C  CB  A SER B  1 103 ? 7.746   244.239 31.351 0.50 35.40 ?  102 SER B CB  1 
ATOM   1875  C  CB  B SER B  1 103 ? 7.768   244.324 31.367 0.50 35.39 ?  102 SER B CB  1 
ATOM   1876  O  OG  A SER B  1 103 ? 6.508   244.795 30.941 0.50 37.11 ?  102 SER B OG  1 
ATOM   1877  O  OG  B SER B  1 103 ? 7.375   242.966 31.467 0.50 34.05 ?  102 SER B OG  1 
ATOM   1878  N  N   . VAL B  1 104 ? 10.560  242.881 29.622 1.00 31.52 ?  103 VAL B N   1 
ATOM   1879  C  CA  . VAL B  1 104 ? 11.771  242.098 29.807 1.00 29.06 ?  103 VAL B CA  1 
ATOM   1880  C  C   . VAL B  1 104 ? 13.005  242.845 29.296 1.00 31.67 ?  103 VAL B C   1 
ATOM   1881  O  O   . VAL B  1 104 ? 14.042  242.860 29.962 1.00 31.11 ?  103 VAL B O   1 
ATOM   1882  C  CB  . VAL B  1 104 ? 11.623  240.710 29.153 1.00 30.34 ?  103 VAL B CB  1 
ATOM   1883  C  CG1 . VAL B  1 104 ? 12.894  239.908 29.338 1.00 29.26 ?  103 VAL B CG1 1 
ATOM   1884  C  CG2 . VAL B  1 104 ? 10.449  239.971 29.787 1.00 32.97 ?  103 VAL B CG2 1 
ATOM   1885  N  N   . ILE B  1 105 ? 12.913  243.496 28.131 1.00 30.00 ?  104 ILE B N   1 
ATOM   1886  C  CA  . ILE B  1 105 ? 13.975  244.418 27.727 1.00 27.17 ?  104 ILE B CA  1 
ATOM   1887  C  C   . ILE B  1 105 ? 13.970  245.626 28.658 1.00 30.34 ?  104 ILE B C   1 
ATOM   1888  O  O   . ILE B  1 105 ? 12.945  245.983 29.246 1.00 28.74 ?  104 ILE B O   1 
ATOM   1889  C  CB  . ILE B  1 105 ? 13.807  244.866 26.262 1.00 22.46 ?  104 ILE B CB  1 
ATOM   1890  C  CG1 . ILE B  1 105 ? 12.441  245.509 26.045 1.00 26.16 ?  104 ILE B CG1 1 
ATOM   1891  C  CG2 . ILE B  1 105 ? 14.041  243.697 25.282 1.00 24.21 ?  104 ILE B CG2 1 
ATOM   1892  C  CD1 . ILE B  1 105 ? 12.385  246.403 24.783 1.00 23.89 ?  104 ILE B CD1 1 
ATOM   1893  N  N   . SER B  1 106 ? 15.124  246.268 28.798 1.00 26.87 ?  105 SER B N   1 
ATOM   1894  C  CA  . SER B  1 106 ? 15.220  247.493 29.570 1.00 28.56 ?  105 SER B CA  1 
ATOM   1895  C  C   . SER B  1 106 ? 16.210  248.425 28.885 1.00 29.78 ?  105 SER B C   1 
ATOM   1896  O  O   . SER B  1 106 ? 17.041  247.993 28.080 1.00 29.93 ?  105 SER B O   1 
ATOM   1897  C  CB  . SER B  1 106 ? 15.668  247.206 31.013 1.00 27.98 ?  105 SER B CB  1 
ATOM   1898  O  OG  . SER B  1 106 ? 15.534  248.368 31.813 1.00 30.96 ?  105 SER B OG  1 
ATOM   1899  N  N   . LEU B  1 107 ? 16.117  249.717 29.207 1.00 30.95 ?  106 LEU B N   1 
ATOM   1900  C  CA  . LEU B  1 107 ? 17.136  250.686 28.823 1.00 32.07 ?  106 LEU B CA  1 
ATOM   1901  C  C   . LEU B  1 107 ? 18.178  250.904 29.925 1.00 37.74 ?  106 LEU B C   1 
ATOM   1902  O  O   . LEU B  1 107 ? 18.942  251.876 29.868 1.00 34.18 ?  106 LEU B O   1 
ATOM   1903  C  CB  . LEU B  1 107 ? 16.482  252.015 28.433 1.00 29.37 ?  106 LEU B CB  1 
ATOM   1904  C  CG  . LEU B  1 107 ? 15.436  251.929 27.314 1.00 26.63 ?  106 LEU B CG  1 
ATOM   1905  C  CD1 . LEU B  1 107 ? 14.917  253.316 26.898 1.00 27.59 ?  106 LEU B CD1 1 
ATOM   1906  C  CD2 . LEU B  1 107 ? 15.999  251.194 26.107 1.00 25.20 ?  106 LEU B CD2 1 
ATOM   1907  N  N   . SER B  1 108 ? 18.240  250.008 30.910 1.00 33.14 ?  107 SER B N   1 
ATOM   1908  C  CA  . SER B  1 108 ? 19.260  250.067 31.948 1.00 32.79 ?  107 SER B CA  1 
ATOM   1909  C  C   . SER B  1 108 ? 19.349  248.702 32.609 1.00 35.07 ?  107 SER B C   1 
ATOM   1910  O  O   . SER B  1 108 ? 18.476  247.856 32.437 1.00 35.41 ?  107 SER B O   1 
ATOM   1911  C  CB  . SER B  1 108 ? 18.945  251.162 32.977 1.00 40.74 ?  107 SER B CB  1 
ATOM   1912  O  OG  . SER B  1 108 ? 17.891  250.750 33.829 1.00 42.37 ?  107 SER B OG  1 
ATOM   1913  N  N   . GLY B  1 109 ? 20.425  248.492 33.353 1.00 33.31 ?  108 GLY B N   1 
ATOM   1914  C  CA  . GLY B  1 109 ? 20.551  247.276 34.128 1.00 36.44 ?  108 GLY B CA  1 
ATOM   1915  C  C   . GLY B  1 109 ? 20.971  246.078 33.294 1.00 33.73 ?  108 GLY B C   1 
ATOM   1916  O  O   . GLY B  1 109 ? 21.434  246.189 32.163 1.00 35.69 ?  108 GLY B O   1 
ATOM   1917  N  N   . ASP B  1 110 ? 20.777  244.903 33.904 1.00 32.67 ?  109 ASP B N   1 
ATOM   1918  C  CA  . ASP B  1 110 ? 21.204  243.626 33.325 1.00 33.44 ?  109 ASP B CA  1 
ATOM   1919  C  C   . ASP B  1 110 ? 20.617  243.409 31.937 1.00 36.52 ?  109 ASP B C   1 
ATOM   1920  O  O   . ASP B  1 110 ? 21.260  242.804 31.071 1.00 33.86 ?  109 ASP B O   1 
ATOM   1921  C  CB  . ASP B  1 110 ? 20.752  242.476 34.227 1.00 40.96 ?  109 ASP B CB  1 
ATOM   1922  C  CG  . ASP B  1 110 ? 21.698  242.218 35.367 1.00 43.66 ?  109 ASP B CG  1 
ATOM   1923  O  OD1 . ASP B  1 110 ? 22.663  242.997 35.521 1.00 48.61 ?  109 ASP B OD1 1 
ATOM   1924  O  OD2 . ASP B  1 110 ? 21.477  241.234 36.107 1.00 46.64 ?  109 ASP B OD2 1 
ATOM   1925  N  N   . HIS B  1 111 ? 19.374  243.834 31.733 1.00 30.20 ?  110 HIS B N   1 
ATOM   1926  C  CA  . HIS B  1 111 ? 18.646  243.581 30.506 1.00 32.61 ?  110 HIS B CA  1 
ATOM   1927  C  C   . HIS B  1 111 ? 18.743  244.748 29.542 1.00 31.32 ?  110 HIS B C   1 
ATOM   1928  O  O   . HIS B  1 111 ? 17.950  244.832 28.598 1.00 30.20 ?  110 HIS B O   1 
ATOM   1929  C  CB  . HIS B  1 111 ? 17.183  243.277 30.831 1.00 32.87 ?  110 HIS B CB  1 
ATOM   1930  C  CG  . HIS B  1 111 ? 16.989  241.972 31.545 1.00 38.26 ?  110 HIS B CG  1 
ATOM   1931  N  ND1 . HIS B  1 111 ? 15.744  241.411 31.749 1.00 39.62 ?  110 HIS B ND1 1 
ATOM   1932  C  CD2 . HIS B  1 111 ? 17.882  241.117 32.099 1.00 40.54 ?  110 HIS B CD2 1 
ATOM   1933  C  CE1 . HIS B  1 111 ? 15.881  240.266 32.399 1.00 42.33 ?  110 HIS B CE1 1 
ATOM   1934  N  NE2 . HIS B  1 111 ? 17.168  240.065 32.624 1.00 36.11 ?  110 HIS B NE2 1 
ATOM   1935  N  N   . CYS B  1 112 ? 19.688  245.654 29.771 1.00 30.08 ?  111 CYS B N   1 
ATOM   1936  C  CA  . CYS B  1 112 ? 19.817  246.839 28.945 1.00 28.14 ?  111 CYS B CA  1 
ATOM   1937  C  C   . CYS B  1 112 ? 20.140  246.468 27.503 1.00 22.55 ?  111 CYS B C   1 
ATOM   1938  O  O   . CYS B  1 112 ? 21.094  245.739 27.241 1.00 28.20 ?  111 CYS B O   1 
ATOM   1939  C  CB  . CYS B  1 112 ? 20.916  247.726 29.507 1.00 33.83 ?  111 CYS B CB  1 
ATOM   1940  S  SG  . CYS B  1 112 ? 21.064  249.265 28.607 1.00 32.33 ?  111 CYS B SG  1 
ATOM   1941  N  N   . ILE B  1 113 ? 19.354  246.998 26.566 1.00 27.19 ?  112 ILE B N   1 
ATOM   1942  C  CA  . ILE B  1 113 ? 19.547  246.733 25.142 1.00 24.96 ?  112 ILE B CA  1 
ATOM   1943  C  C   . ILE B  1 113 ? 20.279  247.866 24.435 1.00 28.14 ?  112 ILE B C   1 
ATOM   1944  O  O   . ILE B  1 113 ? 20.515  247.778 23.222 1.00 22.86 ?  112 ILE B O   1 
ATOM   1945  C  CB  . ILE B  1 113 ? 18.198  246.468 24.441 1.00 24.14 ?  112 ILE B CB  1 
ATOM   1946  C  CG1 . ILE B  1 113 ? 17.290  247.683 24.592 1.00 24.27 ?  112 ILE B CG1 1 
ATOM   1947  C  CG2 . ILE B  1 113 ? 17.520  245.168 24.974 1.00 26.01 ?  112 ILE B CG2 1 
ATOM   1948  C  CD1 . ILE B  1 113 ? 16.105  247.715 23.644 1.00 24.21 ?  112 ILE B CD1 1 
ATOM   1949  N  N   . ILE B  1 114 ? 20.640  248.933 25.148 1.00 30.24 ?  113 ILE B N   1 
ATOM   1950  C  CA  . ILE B  1 114 ? 21.367  250.030 24.521 1.00 25.44 ?  113 ILE B CA  1 
ATOM   1951  C  C   . ILE B  1 114 ? 22.763  249.553 24.144 1.00 26.35 ?  113 ILE B C   1 
ATOM   1952  O  O   . ILE B  1 114 ? 23.431  248.850 24.916 1.00 26.28 ?  113 ILE B O   1 
ATOM   1953  C  CB  . ILE B  1 114 ? 21.407  251.245 25.456 1.00 29.70 ?  113 ILE B CB  1 
ATOM   1954  C  CG1 . ILE B  1 114 ? 20.058  251.975 25.389 1.00 26.29 ?  113 ILE B CG1 1 
ATOM   1955  C  CG2 . ILE B  1 114 ? 22.519  252.186 25.059 1.00 26.62 ?  113 ILE B CG2 1 
ATOM   1956  C  CD1 . ILE B  1 114 ? 19.806  252.859 26.584 1.00 35.11 ?  113 ILE B CD1 1 
ATOM   1957  N  N   . GLY B  1 115 ? 23.196  249.883 22.934 1.00 22.77 ?  114 GLY B N   1 
ATOM   1958  C  CA  . GLY B  1 115 ? 24.450  249.337 22.457 1.00 23.87 ?  114 GLY B CA  1 
ATOM   1959  C  C   . GLY B  1 115 ? 24.364  247.947 21.866 1.00 27.94 ?  114 GLY B C   1 
ATOM   1960  O  O   . GLY B  1 115 ? 25.408  247.359 21.532 1.00 23.50 ?  114 GLY B O   1 
ATOM   1961  N  N   . ARG B  1 116 ? 23.164  247.394 21.737 1.00 25.40 ?  115 ARG B N   1 
ATOM   1962  C  CA  . ARG B  1 116 ? 22.945  246.115 21.077 1.00 26.73 ?  115 ARG B CA  1 
ATOM   1963  C  C   . ARG B  1 116 ? 22.234  246.368 19.751 1.00 25.63 ?  115 ARG B C   1 
ATOM   1964  O  O   . ARG B  1 116 ? 22.000  247.512 19.364 1.00 27.62 ?  115 ARG B O   1 
ATOM   1965  C  CB  . ARG B  1 116 ? 22.178  245.173 22.020 1.00 26.94 ?  115 ARG B CB  1 
ATOM   1966  C  CG  . ARG B  1 116 ? 22.831  245.143 23.416 1.00 28.03 ?  115 ARG B CG  1 
ATOM   1967  C  CD  . ARG B  1 116 ? 22.504  243.911 24.216 1.00 30.37 ?  115 ARG B CD  1 
ATOM   1968  N  NE  . ARG B  1 116 ? 23.104  243.935 25.549 1.00 29.89 ?  115 ARG B NE  1 
ATOM   1969  C  CZ  . ARG B  1 116 ? 24.171  243.225 25.900 1.00 27.50 ?  115 ARG B CZ  1 
ATOM   1970  N  NH1 . ARG B  1 116 ? 24.818  242.475 25.027 1.00 26.92 ?  115 ARG B NH1 1 
ATOM   1971  N  NH2 . ARG B  1 116 ? 24.611  243.282 27.152 1.00 26.94 ?  115 ARG B NH2 1 
ATOM   1972  N  N   . THR B  1 117 ? 21.920  245.308 19.022 1.00 23.11 ?  116 THR B N   1 
ATOM   1973  C  CA  . THR B  1 117 ? 21.443  245.464 17.656 1.00 27.46 ?  116 THR B CA  1 
ATOM   1974  C  C   . THR B  1 117 ? 20.009  244.987 17.536 1.00 27.78 ?  116 THR B C   1 
ATOM   1975  O  O   . THR B  1 117 ? 19.688  243.849 17.903 1.00 30.23 ?  116 THR B O   1 
ATOM   1976  C  CB  . THR B  1 117 ? 22.321  244.700 16.663 1.00 30.19 ?  116 THR B CB  1 
ATOM   1977  O  OG1 . THR B  1 117 ? 23.643  245.245 16.684 1.00 27.17 ?  116 THR B OG1 1 
ATOM   1978  C  CG2 . THR B  1 117 ? 21.760  244.823 15.245 1.00 25.24 ?  116 THR B CG2 1 
ATOM   1979  N  N   . LEU B  1 118 ? 19.160  245.859 17.011 1.00 27.03 ?  117 LEU B N   1 
ATOM   1980  C  CA  . LEU B  1 118 ? 17.813  245.485 16.616 1.00 27.10 ?  117 LEU B CA  1 
ATOM   1981  C  C   . LEU B  1 118 ? 17.857  244.968 15.186 1.00 26.46 ?  117 LEU B C   1 
ATOM   1982  O  O   . LEU B  1 118 ? 18.430  245.621 14.317 1.00 28.46 ?  117 LEU B O   1 
ATOM   1983  C  CB  . LEU B  1 118 ? 16.891  246.694 16.729 1.00 25.06 ?  117 LEU B CB  1 
ATOM   1984  C  CG  . LEU B  1 118 ? 15.404  246.462 16.461 1.00 27.77 ?  117 LEU B CG  1 
ATOM   1985  C  CD1 . LEU B  1 118 ? 14.832  245.555 17.532 1.00 26.45 ?  117 LEU B CD1 1 
ATOM   1986  C  CD2 . LEU B  1 118 ? 14.684  247.825 16.446 1.00 26.61 ?  117 LEU B CD2 1 
ATOM   1987  N  N   . VAL B  1 119 ? 17.256  243.805 14.941 1.00 23.35 ?  118 VAL B N   1 
ATOM   1988  C  CA  . VAL B  1 119 ? 17.253  243.176 13.623 1.00 24.95 ?  118 VAL B CA  1 
ATOM   1989  C  C   . VAL B  1 119 ? 15.814  242.872 13.231 1.00 25.48 ?  118 VAL B C   1 
ATOM   1990  O  O   . VAL B  1 119 ? 15.059  242.313 14.032 1.00 24.97 ?  118 VAL B O   1 
ATOM   1991  C  CB  . VAL B  1 119 ? 18.077  241.876 13.619 1.00 25.39 ?  118 VAL B CB  1 
ATOM   1992  C  CG1 . VAL B  1 119 ? 18.028  241.199 12.239 1.00 26.17 ?  118 VAL B CG1 1 
ATOM   1993  C  CG2 . VAL B  1 119 ? 19.503  242.141 14.043 1.00 22.13 ?  118 VAL B CG2 1 
ATOM   1994  N  N   . VAL B  1 120 ? 15.431  243.218 12.011 1.00 25.34 ?  119 VAL B N   1 
ATOM   1995  C  CA  . VAL B  1 120 ? 14.172  242.747 11.446 1.00 20.65 ?  119 VAL B CA  1 
ATOM   1996  C  C   . VAL B  1 120 ? 14.489  241.655 10.424 1.00 28.23 ?  119 VAL B C   1 
ATOM   1997  O  O   . VAL B  1 120 ? 15.402  241.804 9.587  1.00 29.69 ?  119 VAL B O   1 
ATOM   1998  C  CB  . VAL B  1 120 ? 13.344  243.902 10.848 1.00 28.18 ?  119 VAL B CB  1 
ATOM   1999  C  CG1 . VAL B  1 120 ? 14.055  244.604 9.684  1.00 30.76 ?  119 VAL B CG1 1 
ATOM   2000  C  CG2 . VAL B  1 120 ? 11.969  243.401 10.408 1.00 29.08 ?  119 VAL B CG2 1 
ATOM   2001  N  N   . HIS B  1 121 ? 13.765  240.541 10.511 1.00 25.17 ?  120 HIS B N   1 
ATOM   2002  C  CA  . HIS B  1 121 ? 14.118  239.305 9.820  1.00 21.34 ?  120 HIS B CA  1 
ATOM   2003  C  C   . HIS B  1 121 ? 13.237  239.047 8.606  1.00 23.60 ?  120 HIS B C   1 
ATOM   2004  O  O   . HIS B  1 121 ? 12.187  239.655 8.408  1.00 24.21 ?  120 HIS B O   1 
ATOM   2005  C  CB  . HIS B  1 121 ? 14.035  238.108 10.770 1.00 21.82 ?  120 HIS B CB  1 
ATOM   2006  C  CG  . HIS B  1 121 ? 15.158  238.052 11.756 1.00 28.66 ?  120 HIS B CG  1 
ATOM   2007  N  ND1 . HIS B  1 121 ? 16.285  237.285 11.556 1.00 27.34 ?  120 HIS B ND1 1 
ATOM   2008  C  CD2 . HIS B  1 121 ? 15.316  238.653 12.962 1.00 24.86 ?  120 HIS B CD2 1 
ATOM   2009  C  CE1 . HIS B  1 121 ? 17.097  237.428 12.592 1.00 29.12 ?  120 HIS B CE1 1 
ATOM   2010  N  NE2 . HIS B  1 121 ? 16.531  238.251 13.456 1.00 25.68 ?  120 HIS B NE2 1 
ATOM   2011  N  N   . GLU B  1 122 ? 13.683  238.076 7.811  1.00 29.74 ?  121 GLU B N   1 
ATOM   2012  C  CA  . GLU B  1 122 ? 13.069  237.769 6.520  1.00 30.42 ?  121 GLU B CA  1 
ATOM   2013  C  C   . GLU B  1 122 ? 11.677  237.157 6.670  1.00 30.76 ?  121 GLU B C   1 
ATOM   2014  O  O   . GLU B  1 122 ? 10.750  237.528 5.944  1.00 30.44 ?  121 GLU B O   1 
ATOM   2015  C  CB  . GLU B  1 122 ? 14.010  236.808 5.777  1.00 31.74 ?  121 GLU B CB  1 
ATOM   2016  C  CG  . GLU B  1 122 ? 13.600  236.330 4.403  1.00 38.12 ?  121 GLU B CG  1 
ATOM   2017  C  CD  . GLU B  1 122 ? 14.453  235.129 3.946  1.00 41.90 ?  121 GLU B CD  1 
ATOM   2018  O  OE1 . GLU B  1 122 ? 15.066  234.435 4.805  1.00 42.35 ?  121 GLU B OE1 1 
ATOM   2019  O  OE2 . GLU B  1 122 ? 14.529  234.903 2.720  1.00 55.34 ?  121 GLU B OE2 1 
ATOM   2020  N  N   . LYS B  1 123 ? 11.512  236.236 7.611  1.00 28.81 ?  122 LYS B N   1 
ATOM   2021  C  CA  . LYS B  1 123 ? 10.322  235.399 7.761  1.00 30.90 ?  122 LYS B CA  1 
ATOM   2022  C  C   . LYS B  1 123 ? 9.665   235.652 9.122  1.00 33.84 ?  122 LYS B C   1 
ATOM   2023  O  O   . LYS B  1 123 ? 10.200  236.356 9.985  1.00 23.89 ?  122 LYS B O   1 
ATOM   2024  C  CB  . LYS B  1 123 ? 10.691  233.915 7.647  1.00 29.27 ?  122 LYS B CB  1 
ATOM   2025  C  CG  . LYS B  1 123 ? 11.223  233.457 6.311  1.00 37.23 ?  122 LYS B CG  1 
ATOM   2026  C  CD  . LYS B  1 123 ? 12.192  232.276 6.502  1.00 42.06 ?  122 LYS B CD  1 
ATOM   2027  C  CE  . LYS B  1 123 ? 11.474  230.979 6.866  1.00 51.73 ?  122 LYS B CE  1 
ATOM   2028  N  NZ  . LYS B  1 123 ? 12.349  229.970 7.585  1.00 54.97 ?  122 LYS B NZ  1 
ATOM   2029  N  N   . ALA B  1 124 ? 8.512   235.018 9.328  1.00 30.40 ?  123 ALA B N   1 
ATOM   2030  C  CA  . ALA B  1 124 ? 7.841   235.092 10.616 1.00 30.16 ?  123 ALA B CA  1 
ATOM   2031  C  C   . ALA B  1 124 ? 8.635   234.352 11.684 1.00 28.76 ?  123 ALA B C   1 
ATOM   2032  O  O   . ALA B  1 124 ? 9.250   233.315 11.430 1.00 27.35 ?  123 ALA B O   1 
ATOM   2033  C  CB  . ALA B  1 124 ? 6.438   234.504 10.516 1.00 32.21 ?  123 ALA B CB  1 
ATOM   2034  N  N   . ASP B  1 125 ? 8.619   234.898 12.900 1.00 27.60 ?  124 ASP B N   1 
ATOM   2035  C  CA  . ASP B  1 125 ? 9.131   234.203 14.078 1.00 27.25 ?  124 ASP B CA  1 
ATOM   2036  C  C   . ASP B  1 125 ? 8.083   233.192 14.541 1.00 28.76 ?  124 ASP B C   1 
ATOM   2037  O  O   . ASP B  1 125 ? 6.930   233.570 14.774 1.00 29.59 ?  124 ASP B O   1 
ATOM   2038  C  CB  . ASP B  1 125 ? 9.430   235.236 15.160 1.00 23.40 ?  124 ASP B CB  1 
ATOM   2039  C  CG  . ASP B  1 125 ? 10.053  234.656 16.412 1.00 31.33 ?  124 ASP B CG  1 
ATOM   2040  O  OD1 . ASP B  1 125 ? 9.978   233.423 16.678 1.00 29.29 ?  124 ASP B OD1 1 
ATOM   2041  O  OD2 . ASP B  1 125 ? 10.597  235.487 17.177 1.00 31.60 ?  124 ASP B OD2 1 
ATOM   2042  N  N   . ASP B  1 126 ? 8.457   231.911 14.675 1.00 28.42 ?  125 ASP B N   1 
ATOM   2043  C  CA  . ASP B  1 126 ? 7.453   230.945 15.138 1.00 25.80 ?  125 ASP B CA  1 
ATOM   2044  C  C   . ASP B  1 126 ? 7.315   230.918 16.662 1.00 28.47 ?  125 ASP B C   1 
ATOM   2045  O  O   . ASP B  1 126 ? 6.596   230.061 17.212 1.00 28.58 ?  125 ASP B O   1 
ATOM   2046  C  CB  . ASP B  1 126 ? 7.729   229.544 14.548 1.00 28.39 ?  125 ASP B CB  1 
ATOM   2047  C  CG  . ASP B  1 126 ? 8.966   228.859 15.116 1.00 25.02 ?  125 ASP B CG  1 
ATOM   2048  O  OD1 . ASP B  1 126 ? 9.486   229.240 16.184 1.00 29.16 ?  125 ASP B OD1 1 
ATOM   2049  O  OD2 . ASP B  1 126 ? 9.454   227.906 14.461 1.00 30.39 ?  125 ASP B OD2 1 
ATOM   2050  N  N   . LEU B  1 127 ? 7.957   231.861 17.353 1.00 24.60 ?  126 LEU B N   1 
ATOM   2051  C  CA  . LEU B  1 127 ? 7.804   232.050 18.796 1.00 26.99 ?  126 LEU B CA  1 
ATOM   2052  C  C   . LEU B  1 127 ? 8.256   230.820 19.567 1.00 28.87 ?  126 LEU B C   1 
ATOM   2053  O  O   . LEU B  1 127 ? 7.828   230.582 20.701 1.00 29.08 ?  126 LEU B O   1 
ATOM   2054  C  CB  . LEU B  1 127 ? 6.370   232.452 19.157 1.00 23.90 ?  126 LEU B CB  1 
ATOM   2055  C  CG  . LEU B  1 127 ? 5.810   233.609 18.289 1.00 30.02 ?  126 LEU B CG  1 
ATOM   2056  C  CD1 . LEU B  1 127 ? 4.423   234.051 18.716 1.00 33.76 ?  126 LEU B CD1 1 
ATOM   2057  C  CD2 . LEU B  1 127 ? 6.731   234.815 18.336 1.00 26.56 ?  126 LEU B CD2 1 
ATOM   2058  N  N   . GLY B  1 128 ? 9.143   230.041 18.959 1.00 23.91 ?  127 GLY B N   1 
ATOM   2059  C  CA  . GLY B  1 128 ? 9.745   228.911 19.636 1.00 27.00 ?  127 GLY B CA  1 
ATOM   2060  C  C   . GLY B  1 128 ? 8.897   227.657 19.643 1.00 27.02 ?  127 GLY B C   1 
ATOM   2061  O  O   . GLY B  1 128 ? 9.234   226.700 20.352 1.00 20.97 ?  127 GLY B O   1 
ATOM   2062  N  N   . LYS B  1 129 ? 7.826   227.630 18.848 1.00 26.10 ?  128 LYS B N   1 
ATOM   2063  C  CA  . LYS B  1 129 ? 6.874   226.527 18.824 1.00 30.03 ?  128 LYS B CA  1 
ATOM   2064  C  C   . LYS B  1 129 ? 6.996   225.683 17.564 1.00 28.51 ?  128 LYS B C   1 
ATOM   2065  O  O   . LYS B  1 129 ? 6.080   224.923 17.242 1.00 29.91 ?  128 LYS B O   1 
ATOM   2066  C  CB  . LYS B  1 129 ? 5.457   227.085 18.970 1.00 26.08 ?  128 LYS B CB  1 
ATOM   2067  C  CG  . LYS B  1 129 ? 5.284   227.804 20.344 1.00 26.00 ?  128 LYS B CG  1 
ATOM   2068  C  CD  . LYS B  1 129 ? 4.095   228.741 20.358 1.00 34.44 ?  128 LYS B CD  1 
ATOM   2069  C  CE  . LYS B  1 129 ? 2.781   227.989 20.465 1.00 38.03 ?  128 LYS B CE  1 
ATOM   2070  N  NZ  . LYS B  1 129 ? 1.584   228.903 20.472 1.00 52.95 ?  128 LYS B NZ  1 
ATOM   2071  N  N   . GLY B  1 130 ? 8.104   225.806 16.843 1.00 25.38 ?  129 GLY B N   1 
ATOM   2072  C  CA  . GLY B  1 130 ? 8.253   225.110 15.576 1.00 27.92 ?  129 GLY B CA  1 
ATOM   2073  C  C   . GLY B  1 130 ? 8.692   223.660 15.650 1.00 28.88 ?  129 GLY B C   1 
ATOM   2074  O  O   . GLY B  1 130 ? 8.643   222.961 14.628 1.00 28.82 ?  129 GLY B O   1 
ATOM   2075  N  N   . GLY B  1 131 ? 9.136   223.192 16.816 1.00 25.89 ?  130 GLY B N   1 
ATOM   2076  C  CA  . GLY B  1 131 ? 9.479   221.792 16.997 1.00 22.95 ?  130 GLY B CA  1 
ATOM   2077  C  C   . GLY B  1 131 ? 10.785  221.343 16.377 1.00 30.78 ?  130 GLY B C   1 
ATOM   2078  O  O   . GLY B  1 131 ? 11.060  220.137 16.355 1.00 27.76 ?  130 GLY B O   1 
ATOM   2079  N  N   . ASN B  1 132 ? 11.598  222.255 15.853 1.00 30.88 ?  131 ASN B N   1 
ATOM   2080  C  CA  . ASN B  1 132 ? 12.951  221.920 15.430 1.00 31.25 ?  131 ASN B CA  1 
ATOM   2081  C  C   . ASN B  1 132 ? 13.948  222.719 16.269 1.00 35.76 ?  131 ASN B C   1 
ATOM   2082  O  O   . ASN B  1 132 ? 13.586  223.636 17.020 1.00 32.01 ?  131 ASN B O   1 
ATOM   2083  C  CB  . ASN B  1 132 ? 13.144  222.151 13.912 1.00 32.52 ?  131 ASN B CB  1 
ATOM   2084  C  CG  . ASN B  1 132 ? 12.909  223.595 13.483 1.00 38.81 ?  131 ASN B CG  1 
ATOM   2085  O  OD1 . ASN B  1 132 ? 12.722  224.488 14.316 1.00 32.07 ?  131 ASN B OD1 1 
ATOM   2086  N  ND2 . ASN B  1 132 ? 12.945  223.832 12.163 1.00 32.09 ?  131 ASN B ND2 1 
ATOM   2087  N  N   A GLU B  1 133 ? 15.220  222.337 16.155 0.50 35.98 ?  132 GLU B N   1 
ATOM   2088  N  N   B GLU B  1 133 ? 15.226  222.353 16.140 0.50 35.86 ?  132 GLU B N   1 
ATOM   2089  C  CA  A GLU B  1 133 ? 16.276  222.995 16.924 0.50 39.67 ?  132 GLU B CA  1 
ATOM   2090  C  CA  B GLU B  1 133 ? 16.262  223.004 16.938 0.50 39.63 ?  132 GLU B CA  1 
ATOM   2091  C  C   A GLU B  1 133 ? 16.352  224.485 16.609 0.50 41.23 ?  132 GLU B C   1 
ATOM   2092  C  C   B GLU B  1 133 ? 16.359  224.491 16.610 0.50 41.24 ?  132 GLU B C   1 
ATOM   2093  O  O   A GLU B  1 133 ? 16.609  225.305 17.497 0.50 53.39 ?  132 GLU B O   1 
ATOM   2094  O  O   B GLU B  1 133 ? 16.613  225.317 17.494 0.50 51.04 ?  132 GLU B O   1 
ATOM   2095  C  CB  A GLU B  1 133 ? 17.623  222.327 16.634 0.50 42.29 ?  132 GLU B CB  1 
ATOM   2096  C  CB  B GLU B  1 133 ? 17.608  222.311 16.704 0.50 42.40 ?  132 GLU B CB  1 
ATOM   2097  C  CG  A GLU B  1 133 ? 18.123  222.530 15.204 0.50 42.43 ?  132 GLU B CG  1 
ATOM   2098  C  CG  B GLU B  1 133 ? 18.806  223.019 17.337 0.50 40.65 ?  132 GLU B CG  1 
ATOM   2099  C  CD  A GLU B  1 133 ? 17.178  221.933 14.180 0.50 44.79 ?  132 GLU B CD  1 
ATOM   2100  C  CD  B GLU B  1 133 ? 19.746  222.058 18.032 0.50 44.45 ?  132 GLU B CD  1 
ATOM   2101  O  OE1 A GLU B  1 133 ? 16.764  220.776 14.437 0.50 40.71 ?  132 GLU B OE1 1 
ATOM   2102  O  OE1 B GLU B  1 133 ? 19.787  220.873 17.632 0.50 47.39 ?  132 GLU B OE1 1 
ATOM   2103  O  OE2 A GLU B  1 133 ? 16.814  222.618 13.179 0.50 33.99 ?  132 GLU B OE2 1 
ATOM   2104  O  OE2 B GLU B  1 133 ? 20.435  222.480 18.990 0.50 45.65 ?  132 GLU B OE2 1 
ATOM   2105  N  N   . GLU B  1 134 ? 16.145  224.846 15.341 1.00 36.79 ?  133 GLU B N   1 
ATOM   2106  C  CA  . GLU B  1 134 ? 16.234  226.242 14.937 1.00 38.88 ?  133 GLU B CA  1 
ATOM   2107  C  C   . GLU B  1 134 ? 15.153  227.075 15.608 1.00 36.59 ?  133 GLU B C   1 
ATOM   2108  O  O   . GLU B  1 134 ? 15.380  228.244 15.947 1.00 32.24 ?  133 GLU B O   1 
ATOM   2109  C  CB  . GLU B  1 134 ? 16.127  226.339 13.414 1.00 39.70 ?  133 GLU B CB  1 
ATOM   2110  C  CG  . GLU B  1 134 ? 16.578  227.662 12.837 1.00 42.60 ?  133 GLU B CG  1 
ATOM   2111  C  CD  . GLU B  1 134 ? 18.045  227.915 13.120 1.00 48.62 ?  133 GLU B CD  1 
ATOM   2112  O  OE1 . GLU B  1 134 ? 18.331  228.903 13.823 1.00 50.73 ?  133 GLU B OE1 1 
ATOM   2113  O  OE2 . GLU B  1 134 ? 18.904  227.112 12.683 1.00 53.06 ?  133 GLU B OE2 1 
ATOM   2114  N  N   . SER B  1 135 ? 13.964  226.496 15.796 1.00 31.08 ?  134 SER B N   1 
ATOM   2115  C  CA  . SER B  1 135 ? 12.894  227.234 16.461 1.00 30.54 ?  134 SER B CA  1 
ATOM   2116  C  C   . SER B  1 135 ? 13.337  227.698 17.838 1.00 30.96 ?  134 SER B C   1 
ATOM   2117  O  O   . SER B  1 135 ? 13.057  228.835 18.231 1.00 27.56 ?  134 SER B O   1 
ATOM   2118  C  CB  . SER B  1 135 ? 11.628  226.385 16.557 1.00 31.20 ?  134 SER B CB  1 
ATOM   2119  O  OG  . SER B  1 135 ? 10.605  227.040 17.298 1.00 29.83 ?  134 SER B OG  1 
ATOM   2120  N  N   . THR B  1 136 ? 14.063  226.850 18.573 1.00 30.37 ?  135 THR B N   1 
ATOM   2121  C  CA  . THR B  1 136 ? 14.473  227.204 19.926 1.00 34.44 ?  135 THR B CA  1 
ATOM   2122  C  C   . THR B  1 136 ? 15.642  228.169 19.957 1.00 35.90 ?  135 THR B C   1 
ATOM   2123  O  O   . THR B  1 136 ? 16.042  228.586 21.050 1.00 34.08 ?  135 THR B O   1 
ATOM   2124  C  CB  . THR B  1 136 ? 14.880  225.963 20.732 1.00 37.06 ?  135 THR B CB  1 
ATOM   2125  O  OG1 . THR B  1 136 ? 15.955  225.303 20.048 1.00 39.80 ?  135 THR B OG1 1 
ATOM   2126  C  CG2 . THR B  1 136 ? 13.723  225.010 20.875 1.00 36.51 ?  135 THR B CG2 1 
ATOM   2127  N  N   . LYS B  1 137 ? 16.219  228.505 18.803 1.00 32.66 ?  136 LYS B N   1 
ATOM   2128  C  CA  . LYS B  1 137 ? 17.323  229.463 18.731 1.00 38.16 ?  136 LYS B CA  1 
ATOM   2129  C  C   . LYS B  1 137 ? 16.917  230.785 18.093 1.00 31.15 ?  136 LYS B C   1 
ATOM   2130  O  O   . LYS B  1 137 ? 17.171  231.862 18.649 1.00 30.54 ?  136 LYS B O   1 
ATOM   2131  C  CB  . LYS B  1 137 ? 18.495  228.835 17.957 1.00 39.96 ?  136 LYS B CB  1 
ATOM   2132  C  CG  . LYS B  1 137 ? 19.325  227.887 18.832 1.00 41.89 ?  136 LYS B CG  1 
ATOM   2133  C  CD  . LYS B  1 137 ? 19.814  226.645 18.090 1.00 51.83 ?  136 LYS B CD  1 
ATOM   2134  C  CE  . LYS B  1 137 ? 20.433  226.975 16.730 1.00 57.83 ?  136 LYS B CE  1 
ATOM   2135  N  NZ  . LYS B  1 137 ? 20.819  225.721 15.979 1.00 61.32 ?  136 LYS B NZ  1 
ATOM   2136  N  N   . THR B  1 138 ? 16.242  230.728 16.952 1.00 28.68 ?  137 THR B N   1 
ATOM   2137  C  CA  . THR B  1 138 ? 15.906  231.911 16.177 1.00 31.48 ?  137 THR B CA  1 
ATOM   2138  C  C   . THR B  1 138 ? 14.435  232.015 15.844 1.00 28.11 ?  137 THR B C   1 
ATOM   2139  O  O   . THR B  1 138 ? 14.038  232.994 15.208 1.00 30.07 ?  137 THR B O   1 
ATOM   2140  C  CB  . THR B  1 138 ? 16.678  231.925 14.857 1.00 33.77 ?  137 THR B CB  1 
ATOM   2141  O  OG1 . THR B  1 138 ? 16.202  230.837 14.055 1.00 32.83 ?  137 THR B OG1 1 
ATOM   2142  C  CG2 . THR B  1 138 ? 18.180  231.766 15.095 1.00 36.73 ?  137 THR B CG2 1 
ATOM   2143  N  N   . GLY B  1 139 ? 13.623  231.028 16.217 1.00 29.76 ?  138 GLY B N   1 
ATOM   2144  C  CA  . GLY B  1 139 ? 12.243  230.992 15.749 1.00 25.40 ?  138 GLY B CA  1 
ATOM   2145  C  C   . GLY B  1 139 ? 12.073  230.801 14.252 1.00 29.73 ?  138 GLY B C   1 
ATOM   2146  O  O   . GLY B  1 139 ? 10.999  231.101 13.724 1.00 27.96 ?  138 GLY B O   1 
ATOM   2147  N  N   . ASN B  1 140 ? 13.098  230.298 13.551 1.00 23.90 ?  139 ASN B N   1 
ATOM   2148  C  CA  . ASN B  1 140 ? 13.044  230.119 12.098 1.00 26.39 ?  139 ASN B CA  1 
ATOM   2149  C  C   . ASN B  1 140 ? 12.704  231.428 11.365 1.00 29.57 ?  139 ASN B C   1 
ATOM   2150  O  O   . ASN B  1 140 ? 12.032  231.421 10.321 1.00 25.68 ?  139 ASN B O   1 
ATOM   2151  C  CB  . ASN B  1 140 ? 12.049  229.012 11.723 1.00 27.16 ?  139 ASN B CB  1 
ATOM   2152  C  CG  . ASN B  1 140 ? 12.536  227.630 12.134 1.00 32.33 ?  139 ASN B CG  1 
ATOM   2153  O  OD1 . ASN B  1 140 ? 13.475  227.091 11.555 1.00 38.14 ?  139 ASN B OD1 1 
ATOM   2154  N  ND2 . ASN B  1 140 ? 11.913  227.069 13.149 1.00 31.89 ?  139 ASN B ND2 1 
ATOM   2155  N  N   . ALA B  1 141 ? 13.152  232.575 11.905 1.00 23.22 ?  140 ALA B N   1 
ATOM   2156  C  CA  . ALA B  1 141 ? 12.807  233.861 11.304 1.00 25.07 ?  140 ALA B CA  1 
ATOM   2157  C  C   . ALA B  1 141 ? 13.630  234.185 10.056 1.00 26.18 ?  140 ALA B C   1 
ATOM   2158  O  O   . ALA B  1 141 ? 13.371  235.201 9.401  1.00 30.73 ?  140 ALA B O   1 
ATOM   2159  C  CB  . ALA B  1 141 ? 12.950  234.990 12.344 1.00 23.20 ?  140 ALA B CB  1 
ATOM   2160  N  N   . GLY B  1 142 ? 14.610  233.363 9.711  1.00 33.12 ?  141 GLY B N   1 
ATOM   2161  C  CA  . GLY B  1 142 ? 15.322  233.587 8.466  1.00 33.57 ?  141 GLY B CA  1 
ATOM   2162  C  C   . GLY B  1 142 ? 16.355  234.697 8.550  1.00 34.06 ?  141 GLY B C   1 
ATOM   2163  O  O   . GLY B  1 142 ? 16.811  235.102 9.629  1.00 29.75 ?  141 GLY B O   1 
ATOM   2164  N  N   . SER B  1 143 ? 16.711  235.214 7.378  1.00 29.36 ?  142 SER B N   1 
ATOM   2165  C  CA  . SER B  1 143 ? 17.885  236.061 7.285  1.00 30.18 ?  142 SER B CA  1 
ATOM   2166  C  C   . SER B  1 143 ? 17.586  237.456 7.838  1.00 31.07 ?  142 SER B C   1 
ATOM   2167  O  O   . SER B  1 143 ? 16.440  237.818 8.139  1.00 26.54 ?  142 SER B O   1 
ATOM   2168  C  CB  . SER B  1 143 ? 18.372  236.133 5.838  1.00 30.55 ?  142 SER B CB  1 
ATOM   2169  O  OG  . SER B  1 143 ? 17.480  236.908 5.087  1.00 36.10 ?  142 SER B OG  1 
ATOM   2170  N  N   . ARG B  1 144 ? 18.645  238.238 7.991  1.00 31.06 ?  143 ARG B N   1 
ATOM   2171  C  CA  . ARG B  1 144 ? 18.563  239.563 8.601  1.00 31.84 ?  143 ARG B CA  1 
ATOM   2172  C  C   . ARG B  1 144 ? 18.418  240.604 7.495  1.00 30.96 ?  143 ARG B C   1 
ATOM   2173  O  O   . ARG B  1 144 ? 19.350  240.825 6.711  1.00 30.24 ?  143 ARG B O   1 
ATOM   2174  C  CB  . ARG B  1 144 ? 19.795  239.802 9.471  1.00 28.96 ?  143 ARG B CB  1 
ATOM   2175  C  CG  . ARG B  1 144 ? 20.163  238.545 10.271 1.00 28.48 ?  143 ARG B CG  1 
ATOM   2176  C  CD  . ARG B  1 144 ? 21.334  238.709 11.227 1.00 29.54 ?  143 ARG B CD  1 
ATOM   2177  N  NE  . ARG B  1 144 ? 21.472  237.504 12.033 1.00 30.21 ?  143 ARG B NE  1 
ATOM   2178  C  CZ  . ARG B  1 144 ? 22.181  237.403 13.146 1.00 31.84 ?  143 ARG B CZ  1 
ATOM   2179  N  NH1 . ARG B  1 144 ? 22.871  238.428 13.629 1.00 25.98 ?  143 ARG B NH1 1 
ATOM   2180  N  NH2 . ARG B  1 144 ? 22.194  236.247 13.799 1.00 25.97 ?  143 ARG B NH2 1 
ATOM   2181  N  N   . LEU B  1 145 ? 17.240  241.232 7.425  1.00 29.85 ?  144 LEU B N   1 
ATOM   2182  C  CA  . LEU B  1 145 ? 16.951  242.177 6.351  1.00 29.11 ?  144 LEU B CA  1 
ATOM   2183  C  C   . LEU B  1 145 ? 17.544  243.550 6.625  1.00 32.44 ?  144 LEU B C   1 
ATOM   2184  O  O   . LEU B  1 145 ? 18.005  244.218 5.693  1.00 28.70 ?  144 LEU B O   1 
ATOM   2185  C  CB  . LEU B  1 145 ? 15.441  242.313 6.137  1.00 22.61 ?  144 LEU B CB  1 
ATOM   2186  C  CG  . LEU B  1 145 ? 14.720  241.041 5.677  1.00 32.19 ?  144 LEU B CG  1 
ATOM   2187  C  CD1 . LEU B  1 145 ? 13.249  241.348 5.444  1.00 33.47 ?  144 LEU B CD1 1 
ATOM   2188  C  CD2 . LEU B  1 145 ? 15.365  240.431 4.410  1.00 30.87 ?  144 LEU B CD2 1 
ATOM   2189  N  N   . ALA B  1 146 ? 17.513  243.994 7.882  1.00 26.39 ?  145 ALA B N   1 
ATOM   2190  C  CA  . ALA B  1 146 ? 18.057  245.289 8.273  1.00 29.11 ?  145 ALA B CA  1 
ATOM   2191  C  C   . ALA B  1 146 ? 18.298  245.285 9.777  1.00 32.59 ?  145 ALA B C   1 
ATOM   2192  O  O   . ALA B  1 146 ? 17.650  244.542 10.530 1.00 25.45 ?  145 ALA B O   1 
ATOM   2193  C  CB  . ALA B  1 146 ? 17.125  246.449 7.889  1.00 23.82 ?  145 ALA B CB  1 
ATOM   2194  N  N   . CYS B  1 147 ? 19.230  246.131 10.202 1.00 27.93 ?  146 CYS B N   1 
ATOM   2195  C  CA  . CYS B  1 147 ? 19.617  246.196 11.601 1.00 30.89 ?  146 CYS B CA  1 
ATOM   2196  C  C   . CYS B  1 147 ? 20.213  247.570 11.873 1.00 31.05 ?  146 CYS B C   1 
ATOM   2197  O  O   . CYS B  1 147 ? 20.540  248.324 10.952 1.00 30.81 ?  146 CYS B O   1 
ATOM   2198  C  CB  . CYS B  1 147 ? 20.609  245.092 11.969 1.00 30.20 ?  146 CYS B CB  1 
ATOM   2199  S  SG  . CYS B  1 147 ? 22.136  245.146 10.999 1.00 34.70 ?  146 CYS B SG  1 
ATOM   2200  N  N   . GLY B  1 148 ? 20.325  247.887 13.155 1.00 28.62 ?  147 GLY B N   1 
ATOM   2201  C  CA  . GLY B  1 148 ? 20.995  249.093 13.604 1.00 28.21 ?  147 GLY B CA  1 
ATOM   2202  C  C   . GLY B  1 148 ? 21.392  248.903 15.049 1.00 29.61 ?  147 GLY B C   1 
ATOM   2203  O  O   . GLY B  1 148 ? 20.807  248.086 15.770 1.00 25.23 ?  147 GLY B O   1 
ATOM   2204  N  N   . VAL B  1 149 ? 22.388  249.669 15.476 1.00 27.22 ?  148 VAL B N   1 
ATOM   2205  C  CA  . VAL B  1 149 ? 22.750  249.671 16.888 1.00 27.19 ?  148 VAL B CA  1 
ATOM   2206  C  C   . VAL B  1 149 ? 21.778  250.571 17.639 1.00 26.29 ?  148 VAL B C   1 
ATOM   2207  O  O   . VAL B  1 149 ? 21.441  251.669 17.181 1.00 29.88 ?  148 VAL B O   1 
ATOM   2208  C  CB  . VAL B  1 149 ? 24.208  250.121 17.081 1.00 28.81 ?  148 VAL B CB  1 
ATOM   2209  C  CG1 . VAL B  1 149 ? 24.590  250.060 18.549 1.00 20.76 ?  148 VAL B CG1 1 
ATOM   2210  C  CG2 . VAL B  1 149 ? 25.126  249.232 16.268 1.00 29.85 ?  148 VAL B CG2 1 
ATOM   2211  N  N   . ILE B  1 150 ? 21.331  250.118 18.805 1.00 26.36 ?  149 ILE B N   1 
ATOM   2212  C  CA  . ILE B  1 150 ? 20.380  250.890 19.602 1.00 24.60 ?  149 ILE B CA  1 
ATOM   2213  C  C   . ILE B  1 150 ? 21.159  251.939 20.378 1.00 28.33 ?  149 ILE B C   1 
ATOM   2214  O  O   . ILE B  1 150 ? 22.060  251.604 21.161 1.00 28.45 ?  149 ILE B O   1 
ATOM   2215  C  CB  . ILE B  1 150 ? 19.575  249.972 20.542 1.00 20.43 ?  149 ILE B CB  1 
ATOM   2216  C  CG1 . ILE B  1 150 ? 18.790  248.944 19.719 1.00 24.58 ?  149 ILE B CG1 1 
ATOM   2217  C  CG2 . ILE B  1 150 ? 18.627  250.777 21.438 1.00 24.53 ?  149 ILE B CG2 1 
ATOM   2218  C  CD1 . ILE B  1 150 ? 18.395  247.711 20.533 1.00 24.07 ?  149 ILE B CD1 1 
ATOM   2219  N  N   . GLY B  1 151 ? 20.821  253.212 20.164 1.00 29.93 ?  150 GLY B N   1 
ATOM   2220  C  CA  . GLY B  1 151 ? 21.585  254.275 20.781 1.00 24.21 ?  150 GLY B CA  1 
ATOM   2221  C  C   . GLY B  1 151 ? 20.762  255.147 21.693 1.00 28.72 ?  150 GLY B C   1 
ATOM   2222  O  O   . GLY B  1 151 ? 19.534  255.211 21.553 1.00 30.06 ?  150 GLY B O   1 
ATOM   2223  N  N   . ILE B  1 152 ? 21.434  255.833 22.623 1.00 28.90 ?  151 ILE B N   1 
ATOM   2224  C  CA  . ILE B  1 152 ? 20.767  256.743 23.548 1.00 29.83 ?  151 ILE B CA  1 
ATOM   2225  C  C   . ILE B  1 152 ? 20.161  257.906 22.778 1.00 30.46 ?  151 ILE B C   1 
ATOM   2226  O  O   . ILE B  1 152 ? 20.809  258.511 21.915 1.00 29.29 ?  151 ILE B O   1 
ATOM   2227  C  CB  . ILE B  1 152 ? 21.753  257.230 24.621 1.00 32.45 ?  151 ILE B CB  1 
ATOM   2228  C  CG1 . ILE B  1 152 ? 22.174  256.049 25.494 1.00 32.35 ?  151 ILE B CG1 1 
ATOM   2229  C  CG2 . ILE B  1 152 ? 21.133  258.355 25.462 1.00 34.46 ?  151 ILE B CG2 1 
ATOM   2230  C  CD1 . ILE B  1 152 ? 23.519  256.233 26.179 1.00 38.19 ?  151 ILE B CD1 1 
ATOM   2231  N  N   . ALA B  1 153 ? 18.905  258.224 23.081 1.00 29.29 ?  152 ALA B N   1 
ATOM   2232  C  CA  . ALA B  1 153 ? 18.197  259.286 22.379 1.00 30.34 ?  152 ALA B CA  1 
ATOM   2233  C  C   . ALA B  1 153 ? 17.889  260.425 23.341 1.00 36.67 ?  152 ALA B C   1 
ATOM   2234  O  O   . ALA B  1 153 ? 17.736  260.217 24.551 1.00 34.66 ?  152 ALA B O   1 
ATOM   2235  C  CB  . ALA B  1 153 ? 16.895  258.777 21.755 1.00 33.14 ?  152 ALA B CB  1 
ATOM   2236  N  N   . GLN B  1 154 ? 17.794  261.625 22.787 1.00 42.36 ?  153 GLN B N   1 
ATOM   2237  C  CA  . GLN B  1 154 ? 17.494  262.829 23.561 1.00 46.43 ?  153 GLN B CA  1 
ATOM   2238  C  C   . GLN B  1 154 ? 16.061  262.832 24.089 1.00 52.79 ?  153 GLN B C   1 
ATOM   2239  O  O   . GLN B  1 154 ? 15.105  262.815 23.304 1.00 61.87 ?  153 GLN B O   1 
ATOM   2240  C  CB  . GLN B  1 154 ? 17.722  264.070 22.695 1.00 41.08 ?  153 GLN B CB  1 
ATOM   2241  C  CG  . GLN B  1 154 ? 17.051  265.331 23.209 1.00 50.15 ?  153 GLN B CG  1 
ATOM   2242  C  CD  . GLN B  1 154 ? 17.644  266.570 22.582 1.00 53.80 ?  153 GLN B CD  1 
ATOM   2243  O  OE1 . GLN B  1 154 ? 18.329  267.352 23.247 1.00 59.49 ?  153 GLN B OE1 1 
ATOM   2244  N  NE2 . GLN B  1 154 ? 17.403  266.749 21.282 1.00 52.94 ?  153 GLN B NE2 1 
ATOM   2245  O  OXT . GLN B  1 154 ? 15.820  262.866 25.302 1.00 58.42 ?  153 GLN B OXT 1 
ATOM   2246  N  N   . ALA C  2 1   ? -1.033  195.570 35.153 1.00 54.94 ?  -1  ALA C N   1 
ATOM   2247  C  CA  . ALA C  2 1   ? -2.481  195.674 35.104 1.00 53.56 ?  -1  ALA C CA  1 
ATOM   2248  C  C   . ALA C  2 1   ? -2.986  196.033 33.704 1.00 65.15 ?  -1  ALA C C   1 
ATOM   2249  O  O   . ALA C  2 1   ? -3.911  195.389 33.195 1.00 70.84 ?  -1  ALA C O   1 
ATOM   2250  C  CB  . ALA C  2 1   ? -2.954  196.706 36.102 1.00 58.18 ?  -1  ALA C CB  1 
ATOM   2251  N  N   . MET C  2 2   ? -2.340  197.041 33.096 1.00 61.41 ?  0   MET C N   1 
ATOM   2252  C  CA  . MET C  2 2   ? -2.845  197.816 31.960 1.00 61.10 ?  0   MET C CA  1 
ATOM   2253  C  C   . MET C  2 2   ? -3.317  197.008 30.747 1.00 57.46 ?  0   MET C C   1 
ATOM   2254  O  O   . MET C  2 2   ? -4.447  196.502 30.733 1.00 58.08 ?  0   MET C O   1 
ATOM   2255  C  CB  . MET C  2 2   ? -1.774  198.832 31.505 1.00 64.95 ?  0   MET C CB  1 
ATOM   2256  C  CG  . MET C  2 2   ? -0.300  198.341 31.550 1.00 68.80 ?  0   MET C CG  1 
ATOM   2257  S  SD  . MET C  2 2   ? 0.313   197.490 30.056 1.00 95.29 ?  0   MET C SD  1 
ATOM   2258  C  CE  . MET C  2 2   ? 1.078   198.807 29.097 1.00 62.75 ?  0   MET C CE  1 
ATOM   2259  N  N   . ALA C  2 3   ? -2.476  196.923 29.712 1.00 54.16 ?  1   ALA C N   1 
ATOM   2260  C  CA  . ALA C  2 3   ? -2.921  196.504 28.388 1.00 42.66 ?  1   ALA C CA  1 
ATOM   2261  C  C   . ALA C  2 3   ? -3.493  195.094 28.403 1.00 36.51 ?  1   ALA C C   1 
ATOM   2262  O  O   . ALA C  2 3   ? -2.881  194.166 28.933 1.00 41.20 ?  1   ALA C O   1 
ATOM   2263  C  CB  . ALA C  2 3   ? -1.757  196.576 27.406 1.00 42.40 ?  1   ALA C CB  1 
ATOM   2264  N  N   . THR C  2 4   ? -4.680  194.936 27.824 1.00 30.55 ?  2   THR C N   1 
ATOM   2265  C  CA  . THR C  2 4   ? -5.273  193.613 27.668 1.00 33.21 ?  2   THR C CA  1 
ATOM   2266  C  C   . THR C  2 4   ? -5.170  193.075 26.245 1.00 34.21 ?  2   THR C C   1 
ATOM   2267  O  O   . THR C  2 4   ? -5.338  191.869 26.043 1.00 33.37 ?  2   THR C O   1 
ATOM   2268  C  CB  . THR C  2 4   ? -6.745  193.648 28.082 1.00 34.72 ?  2   THR C CB  1 
ATOM   2269  O  OG1 . THR C  2 4   ? -7.416  194.671 27.340 1.00 39.41 ?  2   THR C OG1 1 
ATOM   2270  C  CG2 . THR C  2 4   ? -6.874  193.923 29.607 1.00 36.81 ?  2   THR C CG2 1 
ATOM   2271  N  N   . LYS C  2 5   ? -4.873  193.932 25.273 1.00 30.41 ?  3   LYS C N   1 
ATOM   2272  C  CA  . LYS C  2 5   ? -4.792  193.553 23.869 1.00 28.68 ?  3   LYS C CA  1 
ATOM   2273  C  C   . LYS C  2 5   ? -3.603  194.226 23.197 1.00 21.12 ?  3   LYS C C   1 
ATOM   2274  O  O   . LYS C  2 5   ? -3.275  195.382 23.478 1.00 23.54 ?  3   LYS C O   1 
ATOM   2275  C  CB  . LYS C  2 5   ? -6.082  193.915 23.120 1.00 31.78 ?  3   LYS C CB  1 
ATOM   2276  C  CG  . LYS C  2 5   ? -7.261  193.008 23.482 1.00 44.75 ?  3   LYS C CG  1 
ATOM   2277  C  CD  . LYS C  2 5   ? -8.619  193.638 23.163 1.00 50.32 ?  3   LYS C CD  1 
ATOM   2278  C  CE  . LYS C  2 5   ? -9.273  194.290 24.404 1.00 58.75 ?  3   LYS C CE  1 
ATOM   2279  N  NZ  . LYS C  2 5   ? -9.679  193.307 25.476 1.00 56.67 ?  3   LYS C NZ  1 
ATOM   2280  N  N   . ALA C  2 6   ? -2.963  193.498 22.295 1.00 26.21 ?  4   ALA C N   1 
ATOM   2281  C  CA  . ALA C  2 6   ? -1.839  194.028 21.543 1.00 25.58 ?  4   ALA C CA  1 
ATOM   2282  C  C   . ALA C  2 6   ? -1.880  193.427 20.149 1.00 29.39 ?  4   ALA C C   1 
ATOM   2283  O  O   . ALA C  2 6   ? -2.589  192.448 19.893 1.00 24.00 ?  4   ALA C O   1 
ATOM   2284  C  CB  . ALA C  2 6   ? -0.504  193.717 22.226 1.00 20.34 ?  4   ALA C CB  1 
ATOM   2285  N  N   . VAL C  2 7   ? -1.103  194.017 19.248 1.00 22.88 ?  5   VAL C N   1 
ATOM   2286  C  CA  . VAL C  2 7   ? -1.098  193.599 17.857 1.00 24.92 ?  5   VAL C CA  1 
ATOM   2287  C  C   . VAL C  2 7   ? 0.281   193.906 17.292 1.00 28.63 ?  5   VAL C C   1 
ATOM   2288  O  O   . VAL C  2 7   ? 0.991   194.792 17.784 1.00 28.08 ?  5   VAL C O   1 
ATOM   2289  C  CB  . VAL C  2 7   ? -2.238  194.290 17.065 1.00 27.94 ?  5   VAL C CB  1 
ATOM   2290  C  CG1 . VAL C  2 7   ? -1.927  195.767 16.858 1.00 23.87 ?  5   VAL C CG1 1 
ATOM   2291  C  CG2 . VAL C  2 7   ? -2.473  193.589 15.721 1.00 28.03 ?  5   VAL C CG2 1 
ATOM   2292  N  N   . CYS C  2 8   ? 0.666   193.147 16.277 1.00 21.96 ?  6   CYS C N   1 
ATOM   2293  C  CA  . CYS C  2 8   ? 1.961   193.269 15.637 1.00 22.69 ?  6   CYS C CA  1 
ATOM   2294  C  C   . CYS C  2 8   ? 1.809   193.031 14.142 1.00 28.84 ?  6   CYS C C   1 
ATOM   2295  O  O   . CYS C  2 8   ? 1.272   192.001 13.732 1.00 30.37 ?  6   CYS C O   1 
ATOM   2296  C  CB  . CYS C  2 8   ? 2.937   192.264 16.225 1.00 25.23 ?  6   CYS C CB  1 
ATOM   2297  S  SG  . CYS C  2 8   ? 4.630   192.457 15.624 1.00 27.56 ?  6   CYS C SG  1 
ATOM   2298  N  N   . VAL C  2 9   ? 2.284   193.967 13.332 1.00 27.70 ?  7   VAL C N   1 
ATOM   2299  C  CA  . VAL C  2 9   ? 2.308   193.809 11.882 1.00 24.80 ?  7   VAL C CA  1 
ATOM   2300  C  C   . VAL C  2 9   ? 3.719   193.400 11.495 1.00 24.74 ?  7   VAL C C   1 
ATOM   2301  O  O   . VAL C  2 9   ? 4.663   194.178 11.650 1.00 27.84 ?  7   VAL C O   1 
ATOM   2302  C  CB  . VAL C  2 9   ? 1.893   195.090 11.147 1.00 30.29 ?  7   VAL C CB  1 
ATOM   2303  C  CG1 . VAL C  2 9   ? 1.981   194.862 9.602  1.00 27.56 ?  7   VAL C CG1 1 
ATOM   2304  C  CG2 . VAL C  2 9   ? 0.508   195.536 11.573 1.00 22.20 ?  7   VAL C CG2 1 
ATOM   2305  N  N   . LEU C  2 10  ? 3.863   192.184 10.969 1.00 27.79 ?  8   LEU C N   1 
ATOM   2306  C  CA  . LEU C  2 10  ? 5.159   191.656 10.580 1.00 20.34 ?  8   LEU C CA  1 
ATOM   2307  C  C   . LEU C  2 10  ? 5.449   192.056 9.138  1.00 24.63 ?  8   LEU C C   1 
ATOM   2308  O  O   . LEU C  2 10  ? 4.613   191.845 8.258  1.00 26.76 ?  8   LEU C O   1 
ATOM   2309  C  CB  . LEU C  2 10  ? 5.169   190.134 10.723 1.00 22.84 ?  8   LEU C CB  1 
ATOM   2310  C  CG  . LEU C  2 10  ? 4.982   189.549 12.143 1.00 30.40 ?  8   LEU C CG  1 
ATOM   2311  C  CD1 . LEU C  2 10  ? 4.739   188.057 12.079 1.00 31.97 ?  8   LEU C CD1 1 
ATOM   2312  C  CD2 . LEU C  2 10  ? 6.216   189.805 12.953 1.00 25.55 ?  8   LEU C CD2 1 
ATOM   2313  N  N   . LYS C  2 11  ? 6.637   192.609 8.902  1.00 27.94 ?  9   LYS C N   1 
ATOM   2314  C  CA  . LYS C  2 11  ? 7.077   193.044 7.580  1.00 29.38 ?  9   LYS C CA  1 
ATOM   2315  C  C   . LYS C  2 11  ? 8.573   192.796 7.486  1.00 29.38 ?  9   LYS C C   1 
ATOM   2316  O  O   . LYS C  2 11  ? 9.276   192.785 8.499  1.00 23.62 ?  9   LYS C O   1 
ATOM   2317  C  CB  . LYS C  2 11  ? 6.796   194.541 7.348  1.00 31.84 ?  9   LYS C CB  1 
ATOM   2318  C  CG  . LYS C  2 11  ? 5.331   194.866 7.079  1.00 39.02 ?  9   LYS C CG  1 
ATOM   2319  C  CD  . LYS C  2 11  ? 5.188   196.314 6.566  1.00 52.83 ?  9   LYS C CD  1 
ATOM   2320  C  CE  . LYS C  2 11  ? 3.740   196.851 6.621  1.00 50.44 ?  9   LYS C CE  1 
ATOM   2321  N  NZ  . LYS C  2 11  ? 2.838   196.141 5.650  1.00 52.01 ?  9   LYS C NZ  1 
ATOM   2322  N  N   . GLY C  2 12  ? 9.062   192.618 6.267  1.00 28.19 ?  10  GLY C N   1 
ATOM   2323  C  CA  . GLY C  2 12  ? 10.484  192.404 6.105  1.00 28.60 ?  10  GLY C CA  1 
ATOM   2324  C  C   . GLY C  2 12  ? 10.946  192.797 4.722  1.00 33.52 ?  10  GLY C C   1 
ATOM   2325  O  O   . GLY C  2 12  ? 10.214  193.458 3.988  1.00 27.41 ?  10  GLY C O   1 
ATOM   2326  N  N   . ASP C  2 13  ? 12.156  192.405 4.356  1.00 35.24 ?  11  ASP C N   1 
ATOM   2327  C  CA  . ASP C  2 13  ? 12.667  192.731 3.030  1.00 39.54 ?  11  ASP C CA  1 
ATOM   2328  C  C   . ASP C  2 13  ? 12.062  191.857 1.937  1.00 38.77 ?  11  ASP C C   1 
ATOM   2329  O  O   . ASP C  2 13  ? 11.915  192.305 0.797  1.00 44.46 ?  11  ASP C O   1 
ATOM   2330  C  CB  . ASP C  2 13  ? 14.181  192.583 3.024  1.00 46.70 ?  11  ASP C CB  1 
ATOM   2331  C  CG  . ASP C  2 13  ? 14.852  193.669 2.241  1.00 63.72 ?  11  ASP C CG  1 
ATOM   2332  O  OD1 . ASP C  2 13  ? 14.838  193.598 0.987  1.00 67.17 ?  11  ASP C OD1 1 
ATOM   2333  O  OD2 . ASP C  2 13  ? 15.375  194.599 2.891  1.00 71.02 ?  11  ASP C OD2 1 
ATOM   2334  N  N   . GLY C  2 14  ? 11.740  190.615 2.249  1.00 32.33 ?  12  GLY C N   1 
ATOM   2335  C  CA  . GLY C  2 14  ? 11.174  189.694 1.297  1.00 26.99 ?  12  GLY C CA  1 
ATOM   2336  C  C   . GLY C  2 14  ? 9.675   189.648 1.402  1.00 25.71 ?  12  GLY C C   1 
ATOM   2337  O  O   . GLY C  2 14  ? 9.021   190.606 1.829  1.00 27.96 ?  12  GLY C O   1 
ATOM   2338  N  N   . PRO C  2 15  ? 9.100   188.493 1.047  1.00 25.18 ?  13  PRO C N   1 
ATOM   2339  C  CA  . PRO C  2 15  ? 7.645   188.355 0.948  1.00 27.26 ?  13  PRO C CA  1 
ATOM   2340  C  C   . PRO C  2 15  ? 6.925   188.041 2.250  1.00 31.16 ?  13  PRO C C   1 
ATOM   2341  O  O   . PRO C  2 15  ? 5.690   187.950 2.238  1.00 32.32 ?  13  PRO C O   1 
ATOM   2342  C  CB  . PRO C  2 15  ? 7.503   187.170 -0.018 1.00 22.64 ?  13  PRO C CB  1 
ATOM   2343  C  CG  . PRO C  2 15  ? 8.716   186.312 0.302  1.00 27.55 ?  13  PRO C CG  1 
ATOM   2344  C  CD  . PRO C  2 15  ? 9.815   187.239 0.758  1.00 23.99 ?  13  PRO C CD  1 
ATOM   2345  N  N   . VAL C  2 16  ? 7.632   187.847 3.355  1.00 29.84 ?  14  VAL C N   1 
ATOM   2346  C  CA  . VAL C  2 16  ? 6.972   187.394 4.582  1.00 28.33 ?  14  VAL C CA  1 
ATOM   2347  C  C   . VAL C  2 16  ? 6.225   188.556 5.211  1.00 28.87 ?  14  VAL C C   1 
ATOM   2348  O  O   . VAL C  2 16  ? 6.823   189.598 5.514  1.00 28.21 ?  14  VAL C O   1 
ATOM   2349  C  CB  . VAL C  2 16  ? 7.974   186.795 5.571  1.00 29.17 ?  14  VAL C CB  1 
ATOM   2350  C  CG1 . VAL C  2 16  ? 7.240   186.370 6.878  1.00 27.04 ?  14  VAL C CG1 1 
ATOM   2351  C  CG2 . VAL C  2 16  ? 8.695   185.619 4.941  1.00 28.20 ?  14  VAL C CG2 1 
ATOM   2352  N  N   . GLN C  2 17  ? 4.927   188.382 5.427  1.00 24.35 ?  15  GLN C N   1 
ATOM   2353  C  CA  . GLN C  2 17  ? 4.165   189.392 6.137  1.00 31.18 ?  15  GLN C CA  1 
ATOM   2354  C  C   . GLN C  2 17  ? 3.050   188.716 6.912  1.00 35.48 ?  15  GLN C C   1 
ATOM   2355  O  O   . GLN C  2 17  ? 2.613   187.607 6.574  1.00 29.61 ?  15  GLN C O   1 
ATOM   2356  C  CB  . GLN C  2 17  ? 3.605   190.471 5.203  1.00 34.24 ?  15  GLN C CB  1 
ATOM   2357  C  CG  . GLN C  2 17  ? 3.418   190.077 3.783  1.00 41.80 ?  15  GLN C CG  1 
ATOM   2358  C  CD  . GLN C  2 17  ? 3.007   191.243 2.915  1.00 43.34 ?  15  GLN C CD  1 
ATOM   2359  O  OE1 . GLN C  2 17  ? 2.783   192.352 3.401  1.00 50.69 ?  15  GLN C OE1 1 
ATOM   2360  N  NE2 . GLN C  2 17  ? 2.887   190.996 1.624  1.00 39.14 ?  15  GLN C NE2 1 
ATOM   2361  N  N   . GLY C  2 18  ? 2.606   189.396 7.971  1.00 30.23 ?  16  GLY C N   1 
ATOM   2362  C  CA  . GLY C  2 18  ? 1.575   188.829 8.820  1.00 29.54 ?  16  GLY C CA  1 
ATOM   2363  C  C   . GLY C  2 18  ? 1.064   189.821 9.840  1.00 31.83 ?  16  GLY C C   1 
ATOM   2364  O  O   . GLY C  2 18  ? 1.610   190.915 10.026 1.00 28.10 ?  16  GLY C O   1 
ATOM   2365  N  N   . ILE C  2 19  ? -0.016  189.416 10.500 1.00 27.82 ?  17  ILE C N   1 
ATOM   2366  C  CA  . ILE C  2 19  ? -0.601  190.162 11.603 1.00 28.87 ?  17  ILE C CA  1 
ATOM   2367  C  C   . ILE C  2 19  ? -0.803  189.188 12.752 1.00 29.99 ?  17  ILE C C   1 
ATOM   2368  O  O   . ILE C  2 19  ? -1.515  188.193 12.601 1.00 26.51 ?  17  ILE C O   1 
ATOM   2369  C  CB  . ILE C  2 19  ? -1.933  190.822 11.216 1.00 28.99 ?  17  ILE C CB  1 
ATOM   2370  C  CG1 . ILE C  2 19  ? -1.695  191.965 10.223 1.00 28.91 ?  17  ILE C CG1 1 
ATOM   2371  C  CG2 . ILE C  2 19  ? -2.634  191.325 12.476 1.00 28.29 ?  17  ILE C CG2 1 
ATOM   2372  C  CD1 . ILE C  2 19  ? -2.966  192.517 9.652  1.00 35.38 ?  17  ILE C CD1 1 
ATOM   2373  N  N   . ILE C  2 20  ? -0.184  189.468 13.890 1.00 27.43 ?  18  ILE C N   1 
ATOM   2374  C  CA  . ILE C  2 20  ? -0.296  188.631 15.077 1.00 26.62 ?  18  ILE C CA  1 
ATOM   2375  C  C   . ILE C  2 20  ? -0.990  189.439 16.164 1.00 29.10 ?  18  ILE C C   1 
ATOM   2376  O  O   . ILE C  2 20  ? -0.574  190.564 16.467 1.00 30.02 ?  18  ILE C O   1 
ATOM   2377  C  CB  . ILE C  2 20  ? 1.086   188.146 15.540 1.00 22.19 ?  18  ILE C CB  1 
ATOM   2378  C  CG1 . ILE C  2 20  ? 1.722   187.294 14.425 1.00 29.87 ?  18  ILE C CG1 1 
ATOM   2379  C  CG2 . ILE C  2 20  ? 0.997   187.399 16.892 1.00 20.34 ?  18  ILE C CG2 1 
ATOM   2380  C  CD1 . ILE C  2 20  ? 0.950   186.017 14.124 1.00 25.08 ?  18  ILE C CD1 1 
ATOM   2381  N  N   . ASN C  2 21  ? -2.045  188.866 16.736 1.00 26.21 ?  19  ASN C N   1 
ATOM   2382  C  CA  . ASN C  2 21  ? -2.815  189.464 17.816 1.00 29.83 ?  19  ASN C CA  1 
ATOM   2383  C  C   . ASN C  2 21  ? -2.439  188.835 19.149 1.00 29.97 ?  19  ASN C C   1 
ATOM   2384  O  O   . ASN C  2 21  ? -2.072  187.658 19.223 1.00 27.33 ?  19  ASN C O   1 
ATOM   2385  C  CB  . ASN C  2 21  ? -4.311  189.267 17.591 1.00 28.68 ?  19  ASN C CB  1 
ATOM   2386  C  CG  . ASN C  2 21  ? -4.757  189.779 16.260 1.00 32.45 ?  19  ASN C CG  1 
ATOM   2387  O  OD1 . ASN C  2 21  ? -4.876  190.977 16.073 1.00 30.77 ?  19  ASN C OD1 1 
ATOM   2388  N  ND2 . ASN C  2 21  ? -5.009  188.873 15.324 1.00 31.29 ?  19  ASN C ND2 1 
ATOM   2389  N  N   . PHE C  2 22  ? -2.552  189.631 20.205 1.00 29.48 ?  20  PHE C N   1 
ATOM   2390  C  CA  . PHE C  2 22  ? -2.278  189.202 21.569 1.00 28.17 ?  20  PHE C CA  1 
ATOM   2391  C  C   . PHE C  2 22  ? -3.449  189.621 22.430 1.00 30.05 ?  20  PHE C C   1 
ATOM   2392  O  O   . PHE C  2 22  ? -3.963  190.737 22.280 1.00 21.85 ?  20  PHE C O   1 
ATOM   2393  C  CB  . PHE C  2 22  ? -1.030  189.838 22.157 1.00 27.05 ?  20  PHE C CB  1 
ATOM   2394  C  CG  . PHE C  2 22  ? 0.206   189.616 21.360 1.00 26.44 ?  20  PHE C CG  1 
ATOM   2395  C  CD1 . PHE C  2 22  ? 0.438   190.333 20.184 1.00 28.35 ?  20  PHE C CD1 1 
ATOM   2396  C  CD2 . PHE C  2 22  ? 1.169   188.742 21.811 1.00 24.64 ?  20  PHE C CD2 1 
ATOM   2397  C  CE1 . PHE C  2 22  ? 1.603   190.143 19.459 1.00 24.47 ?  20  PHE C CE1 1 
ATOM   2398  C  CE2 . PHE C  2 22  ? 2.342   188.551 21.096 1.00 30.49 ?  20  PHE C CE2 1 
ATOM   2399  C  CZ  . PHE C  2 22  ? 2.555   189.242 19.920 1.00 27.68 ?  20  PHE C CZ  1 
ATOM   2400  N  N   . GLU C  2 23  ? -3.852  188.742 23.345 1.00 26.53 ?  21  GLU C N   1 
ATOM   2401  C  CA  . GLU C  2 23  ? -4.927  189.069 24.268 1.00 27.36 ?  21  GLU C CA  1 
ATOM   2402  C  C   . GLU C  2 23  ? -4.676  188.413 25.613 1.00 30.00 ?  21  GLU C C   1 
ATOM   2403  O  O   . GLU C  2 23  ? -4.346  187.226 25.684 1.00 31.65 ?  21  GLU C O   1 
ATOM   2404  C  CB  . GLU C  2 23  ? -6.277  188.626 23.726 1.00 32.16 ?  21  GLU C CB  1 
ATOM   2405  C  CG  . GLU C  2 23  ? -7.451  189.134 24.552 1.00 43.20 ?  21  GLU C CG  1 
ATOM   2406  C  CD  . GLU C  2 23  ? -8.770  188.664 23.976 1.00 62.03 ?  21  GLU C CD  1 
ATOM   2407  O  OE1 . GLU C  2 23  ? -9.381  187.736 24.555 1.00 66.10 ?  21  GLU C OE1 1 
ATOM   2408  O  OE2 . GLU C  2 23  ? -9.172  189.207 22.920 1.00 68.96 ?  21  GLU C OE2 1 
ATOM   2409  N  N   . GLN C  2 24  ? -4.859  189.193 26.675 1.00 30.64 ?  22  GLN C N   1 
ATOM   2410  C  CA  . GLN C  2 24  ? -4.623  188.755 28.050 1.00 31.56 ?  22  GLN C CA  1 
ATOM   2411  C  C   . GLN C  2 24  ? -5.753  189.329 28.902 1.00 33.93 ?  22  GLN C C   1 
ATOM   2412  O  O   . GLN C  2 24  ? -5.674  190.471 29.354 1.00 31.89 ?  22  GLN C O   1 
ATOM   2413  C  CB  . GLN C  2 24  ? -3.262  189.221 28.529 1.00 28.99 ?  22  GLN C CB  1 
ATOM   2414  C  CG  . GLN C  2 24  ? -2.818  188.622 29.867 1.00 26.30 ?  22  GLN C CG  1 
ATOM   2415  C  CD  . GLN C  2 24  ? -1.501  189.219 30.312 1.00 26.88 ?  22  GLN C CD  1 
ATOM   2416  O  OE1 . GLN C  2 24  ? -1.100  190.298 29.842 1.00 26.74 ?  22  GLN C OE1 1 
ATOM   2417  N  NE2 . GLN C  2 24  ? -0.805  188.529 31.195 1.00 28.98 ?  22  GLN C NE2 1 
ATOM   2418  N  N   . LYS C  2 25  ? -6.803  188.532 29.102 1.00 32.13 ?  23  LYS C N   1 
ATOM   2419  C  CA  . LYS C  2 25  ? -7.951  188.985 29.883 1.00 34.17 ?  23  LYS C CA  1 
ATOM   2420  C  C   . LYS C  2 25  ? -7.545  189.341 31.308 1.00 39.25 ?  23  LYS C C   1 
ATOM   2421  O  O   . LYS C  2 25  ? -8.039  190.323 31.874 1.00 38.89 ?  23  LYS C O   1 
ATOM   2422  C  CB  . LYS C  2 25  ? -9.032  187.900 29.909 1.00 47.95 ?  23  LYS C CB  1 
ATOM   2423  C  CG  . LYS C  2 25  ? -9.694  187.606 28.560 1.00 57.77 ?  23  LYS C CG  1 
ATOM   2424  C  CD  . LYS C  2 25  ? -10.442 188.823 28.006 1.00 57.36 ?  23  LYS C CD  1 
ATOM   2425  C  CE  . LYS C  2 25  ? -11.847 188.448 27.489 1.00 66.40 ?  23  LYS C CE  1 
ATOM   2426  N  NZ  . LYS C  2 25  ? -11.870 187.246 26.579 1.00 68.88 ?  23  LYS C NZ  1 
ATOM   2427  N  N   . GLU C  2 26  ? -6.652  188.556 31.909 1.00 35.30 ?  24  GLU C N   1 
ATOM   2428  C  CA  . GLU C  2 26  ? -6.245  188.753 33.294 1.00 34.97 ?  24  GLU C CA  1 
ATOM   2429  C  C   . GLU C  2 26  ? -4.750  189.021 33.359 1.00 33.08 ?  24  GLU C C   1 
ATOM   2430  O  O   . GLU C  2 26  ? -3.957  188.298 32.747 1.00 29.55 ?  24  GLU C O   1 
ATOM   2431  C  CB  . GLU C  2 26  ? -6.598  187.531 34.139 1.00 39.64 ?  24  GLU C CB  1 
ATOM   2432  C  CG  . GLU C  2 26  ? -8.059  187.168 34.060 1.00 49.39 ?  24  GLU C CG  1 
ATOM   2433  C  CD  . GLU C  2 26  ? -8.912  188.018 34.996 1.00 66.99 ?  24  GLU C CD  1 
ATOM   2434  O  OE1 . GLU C  2 26  ? -8.341  188.881 35.711 1.00 58.52 ?  24  GLU C OE1 1 
ATOM   2435  O  OE2 . GLU C  2 26  ? -10.152 187.819 35.016 1.00 67.18 ?  24  GLU C OE2 1 
ATOM   2436  N  N   . SER C  2 27  ? -4.363  190.045 34.118 1.00 32.66 ?  25  SER C N   1 
ATOM   2437  C  CA  . SER C  2 27  ? -2.958  190.427 34.155 1.00 29.97 ?  25  SER C CA  1 
ATOM   2438  C  C   . SER C  2 27  ? -2.067  189.348 34.762 1.00 29.57 ?  25  SER C C   1 
ATOM   2439  O  O   . SER C  2 27  ? -0.864  189.326 34.481 1.00 30.60 ?  25  SER C O   1 
ATOM   2440  C  CB  . SER C  2 27  ? -2.799  191.739 34.910 1.00 35.46 ?  25  SER C CB  1 
ATOM   2441  O  OG  . SER C  2 27  ? -3.049  191.561 36.294 1.00 32.68 ?  25  SER C OG  1 
ATOM   2442  N  N   . ASN C  2 28  ? -2.614  188.438 35.571 1.00 29.25 ?  26  ASN C N   1 
ATOM   2443  C  CA  . ASN C  2 28  ? -1.818  187.333 36.101 1.00 33.05 ?  26  ASN C CA  1 
ATOM   2444  C  C   . ASN C  2 28  ? -2.141  186.016 35.408 1.00 37.38 ?  26  ASN C C   1 
ATOM   2445  O  O   . ASN C  2 28  ? -1.844  184.946 35.949 1.00 41.44 ?  26  ASN C O   1 
ATOM   2446  C  CB  . ASN C  2 28  ? -1.996  187.212 37.618 1.00 34.09 ?  26  ASN C CB  1 
ATOM   2447  C  CG  . ASN C  2 28  ? -3.399  186.798 38.013 1.00 39.58 ?  26  ASN C CG  1 
ATOM   2448  O  OD1 . ASN C  2 28  ? -4.374  187.136 37.334 1.00 38.10 ?  26  ASN C OD1 1 
ATOM   2449  N  ND2 . ASN C  2 28  ? -3.509  186.056 39.125 1.00 35.81 ?  26  ASN C ND2 1 
ATOM   2450  N  N   . GLY C  2 29  ? -2.754  186.083 34.224 1.00 33.56 ?  27  GLY C N   1 
ATOM   2451  C  CA  . GLY C  2 29  ? -3.076  184.916 33.425 1.00 37.79 ?  27  GLY C CA  1 
ATOM   2452  C  C   . GLY C  2 29  ? -2.284  184.850 32.125 1.00 36.29 ?  27  GLY C C   1 
ATOM   2453  O  O   . GLY C  2 29  ? -1.401  185.678 31.868 1.00 30.46 ?  27  GLY C O   1 
ATOM   2454  N  N   . PRO C  2 30  ? -2.564  183.851 31.290 1.00 36.21 ?  28  PRO C N   1 
ATOM   2455  C  CA  . PRO C  2 30  ? -1.777  183.665 30.069 1.00 35.00 ?  28  PRO C CA  1 
ATOM   2456  C  C   . PRO C  2 30  ? -2.200  184.623 28.960 1.00 30.97 ?  28  PRO C C   1 
ATOM   2457  O  O   . PRO C  2 30  ? -3.254  185.258 28.995 1.00 32.23 ?  28  PRO C O   1 
ATOM   2458  C  CB  . PRO C  2 30  ? -2.075  182.212 29.678 1.00 32.63 ?  28  PRO C CB  1 
ATOM   2459  C  CG  . PRO C  2 30  ? -3.441  181.986 30.179 1.00 43.85 ?  28  PRO C CG  1 
ATOM   2460  C  CD  . PRO C  2 30  ? -3.511  182.738 31.496 1.00 34.08 ?  28  PRO C CD  1 
ATOM   2461  N  N   . VAL C  2 31  ? -1.344  184.697 27.947 1.00 30.38 ?  29  VAL C N   1 
ATOM   2462  C  CA  . VAL C  2 31  ? -1.573  185.523 26.766 1.00 28.40 ?  29  VAL C CA  1 
ATOM   2463  C  C   . VAL C  2 31  ? -1.957  184.616 25.609 1.00 29.85 ?  29  VAL C C   1 
ATOM   2464  O  O   . VAL C  2 31  ? -1.237  183.661 25.298 1.00 31.47 ?  29  VAL C O   1 
ATOM   2465  C  CB  . VAL C  2 31  ? -0.329  186.355 26.433 1.00 26.07 ?  29  VAL C CB  1 
ATOM   2466  C  CG1 . VAL C  2 31  ? -0.558  187.196 25.163 1.00 23.13 ?  29  VAL C CG1 1 
ATOM   2467  C  CG2 . VAL C  2 31  ? 0.028   187.241 27.647 1.00 26.97 ?  29  VAL C CG2 1 
ATOM   2468  N  N   . LYS C  2 32  ? -3.092  184.904 24.983 1.00 27.46 ?  30  LYS C N   1 
ATOM   2469  C  CA  . LYS C  2 32  ? -3.452  184.239 23.737 1.00 31.54 ?  30  LYS C CA  1 
ATOM   2470  C  C   . LYS C  2 32  ? -2.791  184.959 22.567 1.00 33.33 ?  30  LYS C C   1 
ATOM   2471  O  O   . LYS C  2 32  ? -2.857  186.184 22.469 1.00 30.09 ?  30  LYS C O   1 
ATOM   2472  C  CB  . LYS C  2 32  ? -4.971  184.211 23.564 1.00 30.36 ?  30  LYS C CB  1 
ATOM   2473  C  CG  . LYS C  2 32  ? -5.702  183.651 24.790 1.00 41.45 ?  30  LYS C CG  1 
ATOM   2474  C  CD  . LYS C  2 32  ? -7.092  184.270 24.950 1.00 54.66 ?  30  LYS C CD  1 
ATOM   2475  C  CE  . LYS C  2 32  ? -8.186  183.219 25.119 1.00 53.58 ?  30  LYS C CE  1 
ATOM   2476  N  NZ  . LYS C  2 32  ? -8.115  182.590 26.480 1.00 55.90 ?  30  LYS C NZ  1 
ATOM   2477  N  N   . VAL C  2 33  ? -2.145  184.195 21.690 1.00 30.76 ?  31  VAL C N   1 
ATOM   2478  C  CA  . VAL C  2 33  ? -1.393  184.726 20.557 1.00 31.22 ?  31  VAL C CA  1 
ATOM   2479  C  C   . VAL C  2 33  ? -1.951  184.065 19.307 1.00 32.17 ?  31  VAL C C   1 
ATOM   2480  O  O   . VAL C  2 33  ? -1.926  182.832 19.194 1.00 32.12 ?  31  VAL C O   1 
ATOM   2481  C  CB  . VAL C  2 33  ? 0.116   184.447 20.692 1.00 31.39 ?  31  VAL C CB  1 
ATOM   2482  C  CG1 . VAL C  2 33  ? 0.917   185.125 19.580 1.00 27.57 ?  31  VAL C CG1 1 
ATOM   2483  C  CG2 . VAL C  2 33  ? 0.636   184.890 22.026 1.00 27.48 ?  31  VAL C CG2 1 
ATOM   2484  N  N   . TRP C  2 34  ? -2.452  184.866 18.371 1.00 30.32 ?  32  TRP C N   1 
ATOM   2485  C  CA  . TRP C  2 34  ? -3.038  184.249 17.194 1.00 30.19 ?  32  TRP C CA  1 
ATOM   2486  C  C   . TRP C  2 34  ? -3.014  185.206 16.020 1.00 29.27 ?  32  TRP C C   1 
ATOM   2487  O  O   . TRP C  2 34  ? -3.006  186.427 16.179 1.00 29.83 ?  32  TRP C O   1 
ATOM   2488  C  CB  . TRP C  2 34  ? -4.473  183.780 17.445 1.00 31.82 ?  32  TRP C CB  1 
ATOM   2489  C  CG  . TRP C  2 34  ? -5.495  184.871 17.339 1.00 33.50 ?  32  TRP C CG  1 
ATOM   2490  C  CD1 . TRP C  2 34  ? -6.251  185.197 16.242 1.00 31.49 ?  32  TRP C CD1 1 
ATOM   2491  C  CD2 . TRP C  2 34  ? -5.895  185.758 18.378 1.00 31.48 ?  32  TRP C CD2 1 
ATOM   2492  N  NE1 . TRP C  2 34  ? -7.091  186.246 16.541 1.00 35.12 ?  32  TRP C NE1 1 
ATOM   2493  C  CE2 . TRP C  2 34  ? -6.893  186.602 17.851 1.00 34.32 ?  32  TRP C CE2 1 
ATOM   2494  C  CE3 . TRP C  2 34  ? -5.512  185.917 19.709 1.00 36.89 ?  32  TRP C CE3 1 
ATOM   2495  C  CZ2 . TRP C  2 34  ? -7.503  187.589 18.609 1.00 37.17 ?  32  TRP C CZ2 1 
ATOM   2496  C  CZ3 . TRP C  2 34  ? -6.119  186.901 20.460 1.00 38.47 ?  32  TRP C CZ3 1 
ATOM   2497  C  CH2 . TRP C  2 34  ? -7.102  187.729 19.908 1.00 40.02 ?  32  TRP C CH2 1 
ATOM   2498  N  N   . GLY C  2 35  ? -3.010  184.617 14.834 1.00 27.40 ?  33  GLY C N   1 
ATOM   2499  C  CA  . GLY C  2 35  ? -2.969  185.386 13.606 1.00 30.73 ?  33  GLY C CA  1 
ATOM   2500  C  C   . GLY C  2 35  ? -2.450  184.520 12.472 1.00 31.41 ?  33  GLY C C   1 
ATOM   2501  O  O   . GLY C  2 35  ? -2.509  183.298 12.532 1.00 30.45 ?  33  GLY C O   1 
ATOM   2502  N  N   . SER C  2 36  ? -1.926  185.187 11.452 1.00 29.24 ?  34  SER C N   1 
ATOM   2503  C  CA  . SER C  2 36  ? -1.542  184.519 10.224 1.00 33.87 ?  34  SER C CA  1 
ATOM   2504  C  C   . SER C  2 36  ? -0.292  185.186 9.679  1.00 32.52 ?  34  SER C C   1 
ATOM   2505  O  O   . SER C  2 36  ? -0.166  186.412 9.729  1.00 30.58 ?  34  SER C O   1 
ATOM   2506  C  CB  . SER C  2 36  ? -2.675  184.580 9.195  1.00 31.23 ?  34  SER C CB  1 
ATOM   2507  O  OG  . SER C  2 36  ? -2.206  184.143 7.941  1.00 53.74 ?  34  SER C OG  1 
ATOM   2508  N  N   . ILE C  2 37  ? 0.642   184.372 9.197  1.00 26.12 ?  35  ILE C N   1 
ATOM   2509  C  CA  . ILE C  2 37  ? 1.834   184.842 8.504  1.00 23.22 ?  35  ILE C CA  1 
ATOM   2510  C  C   . ILE C  2 37  ? 1.853   184.177 7.136  1.00 36.62 ?  35  ILE C C   1 
ATOM   2511  O  O   . ILE C  2 37  ? 1.681   182.957 7.039  1.00 32.41 ?  35  ILE C O   1 
ATOM   2512  C  CB  . ILE C  2 37  ? 3.130   184.502 9.260  1.00 26.05 ?  35  ILE C CB  1 
ATOM   2513  C  CG1 . ILE C  2 37  ? 3.059   184.934 10.725 1.00 29.23 ?  35  ILE C CG1 1 
ATOM   2514  C  CG2 . ILE C  2 37  ? 4.327   185.147 8.554  1.00 26.83 ?  35  ILE C CG2 1 
ATOM   2515  C  CD1 . ILE C  2 37  ? 4.283   184.527 11.503 1.00 31.20 ?  35  ILE C CD1 1 
ATOM   2516  N  N   . LYS C  2 38  ? 2.088   184.962 6.090  1.00 32.73 ?  36  LYS C N   1 
ATOM   2517  C  CA  . LYS C  2 38  ? 2.170   184.426 4.743  1.00 33.61 ?  36  LYS C CA  1 
ATOM   2518  C  C   . LYS C  2 38  ? 3.550   184.695 4.158  1.00 32.89 ?  36  LYS C C   1 
ATOM   2519  O  O   . LYS C  2 38  ? 4.335   185.489 4.684  1.00 31.90 ?  36  LYS C O   1 
ATOM   2520  C  CB  . LYS C  2 38  ? 1.077   185.012 3.855  1.00 33.55 ?  36  LYS C CB  1 
ATOM   2521  C  CG  . LYS C  2 38  ? 1.273   186.476 3.504  1.00 37.44 ?  36  LYS C CG  1 
ATOM   2522  C  CD  . LYS C  2 38  ? -0.029  187.057 2.993  1.00 48.30 ?  36  LYS C CD  1 
ATOM   2523  C  CE  . LYS C  2 38  ? -0.018  188.581 2.945  1.00 43.83 ?  36  LYS C CE  1 
ATOM   2524  N  NZ  . LYS C  2 38  ? -1.039  189.082 1.964  1.00 51.90 ?  36  LYS C NZ  1 
ATOM   2525  N  N   . GLY C  2 39  ? 3.863   183.980 3.087  1.00 29.66 ?  37  GLY C N   1 
ATOM   2526  C  CA  . GLY C  2 39  ? 5.114   184.174 2.405  1.00 27.48 ?  37  GLY C CA  1 
ATOM   2527  C  C   . GLY C  2 39  ? 6.255   183.338 2.905  1.00 29.49 ?  37  GLY C C   1 
ATOM   2528  O  O   . GLY C  2 39  ? 7.408   183.600 2.530  1.00 31.13 ?  37  GLY C O   1 
ATOM   2529  N  N   . LEU C  2 40  ? 5.978   182.349 3.742  1.00 29.85 ?  38  LEU C N   1 
ATOM   2530  C  CA  . LEU C  2 40  ? 7.011   181.524 4.337  1.00 33.30 ?  38  LEU C CA  1 
ATOM   2531  C  C   . LEU C  2 40  ? 7.280   180.300 3.474  1.00 32.52 ?  38  LEU C C   1 
ATOM   2532  O  O   . LEU C  2 40  ? 6.398   179.808 2.770  1.00 34.30 ?  38  LEU C O   1 
ATOM   2533  C  CB  . LEU C  2 40  ? 6.588   181.068 5.735  1.00 29.97 ?  38  LEU C CB  1 
ATOM   2534  C  CG  . LEU C  2 40  ? 6.460   182.178 6.789  1.00 32.09 ?  38  LEU C CG  1 
ATOM   2535  C  CD1 . LEU C  2 40  ? 5.701   181.673 7.994  1.00 27.87 ?  38  LEU C CD1 1 
ATOM   2536  C  CD2 . LEU C  2 40  ? 7.829   182.630 7.177  1.00 30.89 ?  38  LEU C CD2 1 
ATOM   2537  N  N   . THR C  2 41  ? 8.503   179.796 3.559  1.00 32.80 ?  39  THR C N   1 
ATOM   2538  C  CA  . THR C  2 41  ? 8.758   178.466 3.039  1.00 39.80 ?  39  THR C CA  1 
ATOM   2539  C  C   . THR C  2 41  ? 8.002   177.455 3.893  1.00 42.17 ?  39  THR C C   1 
ATOM   2540  O  O   . THR C  2 41  ? 7.828   177.640 5.104  1.00 36.36 ?  39  THR C O   1 
ATOM   2541  C  CB  . THR C  2 41  ? 10.252  178.165 3.047  1.00 40.38 ?  39  THR C CB  1 
ATOM   2542  O  OG1 . THR C  2 41  ? 10.735  178.218 4.392  1.00 36.30 ?  39  THR C OG1 1 
ATOM   2543  C  CG2 . THR C  2 41  ? 11.008  179.200 2.236  1.00 43.15 ?  39  THR C CG2 1 
ATOM   2544  N  N   . GLU C  2 42  ? 7.511   176.404 3.242  1.00 39.78 ?  40  GLU C N   1 
ATOM   2545  C  CA  . GLU C  2 42  ? 6.764   175.365 3.941  1.00 35.34 ?  40  GLU C CA  1 
ATOM   2546  C  C   . GLU C  2 42  ? 7.629   174.769 5.039  1.00 35.13 ?  40  GLU C C   1 
ATOM   2547  O  O   . GLU C  2 42  ? 8.839   174.593 4.870  1.00 37.25 ?  40  GLU C O   1 
ATOM   2548  C  CB  . GLU C  2 42  ? 6.318   174.287 2.953  1.00 39.03 ?  40  GLU C CB  1 
ATOM   2549  C  CG  . GLU C  2 42  ? 5.508   173.139 3.559  1.00 41.79 ?  40  GLU C CG  1 
ATOM   2550  C  CD  . GLU C  2 42  ? 5.059   172.133 2.488  1.00 49.52 ?  40  GLU C CD  1 
ATOM   2551  O  OE1 . GLU C  2 42  ? 4.212   171.266 2.784  1.00 53.33 ?  40  GLU C OE1 1 
ATOM   2552  O  OE2 . GLU C  2 42  ? 5.538   172.234 1.334  1.00 49.46 ?  40  GLU C OE2 1 
ATOM   2553  N  N   . GLY C  2 43  ? 7.022   174.511 6.189  1.00 35.66 ?  41  GLY C N   1 
ATOM   2554  C  CA  . GLY C  2 43  ? 7.762   173.981 7.309  1.00 34.00 ?  41  GLY C CA  1 
ATOM   2555  C  C   . GLY C  2 43  ? 7.781   174.927 8.497  1.00 34.53 ?  41  GLY C C   1 
ATOM   2556  O  O   . GLY C  2 43  ? 6.969   175.849 8.616  1.00 32.86 ?  41  GLY C O   1 
ATOM   2557  N  N   . LEU C  2 44  ? 8.747   174.690 9.380  1.00 35.08 ?  42  LEU C N   1 
ATOM   2558  C  CA  . LEU C  2 44  ? 8.797   175.315 10.692 1.00 37.98 ?  42  LEU C CA  1 
ATOM   2559  C  C   . LEU C  2 44  ? 9.635   176.586 10.672 1.00 37.36 ?  42  LEU C C   1 
ATOM   2560  O  O   . LEU C  2 44  ? 10.653  176.673 9.980  1.00 35.17 ?  42  LEU C O   1 
ATOM   2561  C  CB  . LEU C  2 44  ? 9.385   174.355 11.723 1.00 34.66 ?  42  LEU C CB  1 
ATOM   2562  C  CG  . LEU C  2 44  ? 8.710   173.001 11.916 1.00 41.86 ?  42  LEU C CG  1 
ATOM   2563  C  CD1 . LEU C  2 44  ? 9.217   172.387 13.204 1.00 37.13 ?  42  LEU C CD1 1 
ATOM   2564  C  CD2 . LEU C  2 44  ? 7.219   173.157 11.954 1.00 41.34 ?  42  LEU C CD2 1 
ATOM   2565  N  N   . HIS C  2 45  ? 9.230   177.560 11.484 1.00 31.75 ?  43  HIS C N   1 
ATOM   2566  C  CA  . HIS C  2 45  ? 9.987   178.803 11.589 1.00 29.00 ?  43  HIS C CA  1 
ATOM   2567  C  C   . HIS C  2 45  ? 10.003  179.251 13.034 1.00 30.62 ?  43  HIS C C   1 
ATOM   2568  O  O   . HIS C  2 45  ? 8.944   179.331 13.663 1.00 32.63 ?  43  HIS C O   1 
ATOM   2569  C  CB  . HIS C  2 45  ? 9.365   179.883 10.709 1.00 29.49 ?  43  HIS C CB  1 
ATOM   2570  C  CG  . HIS C  2 45  ? 9.397   179.550 9.252  1.00 30.57 ?  43  HIS C CG  1 
ATOM   2571  N  ND1 . HIS C  2 45  ? 10.494  179.812 8.469  1.00 30.50 ?  43  HIS C ND1 1 
ATOM   2572  C  CD2 . HIS C  2 45  ? 8.482   178.958 8.445  1.00 31.65 ?  43  HIS C CD2 1 
ATOM   2573  C  CE1 . HIS C  2 45  ? 10.250  179.408 7.233  1.00 36.71 ?  43  HIS C CE1 1 
ATOM   2574  N  NE2 . HIS C  2 45  ? 9.040   178.879 7.195  1.00 31.70 ?  43  HIS C NE2 1 
ATOM   2575  N  N   . GLY C  2 46  ? 11.195  179.530 13.550 1.00 29.81 ?  44  GLY C N   1 
ATOM   2576  C  CA  . GLY C  2 46  ? 11.333  180.135 14.859 1.00 32.05 ?  44  GLY C CA  1 
ATOM   2577  C  C   . GLY C  2 46  ? 10.512  181.408 14.959 1.00 32.03 ?  44  GLY C C   1 
ATOM   2578  O  O   . GLY C  2 46  ? 10.389  182.162 13.976 1.00 28.33 ?  44  GLY C O   1 
ATOM   2579  N  N   . PHE C  2 47  ? 9.955   181.639 16.144 1.00 29.37 ?  45  PHE C N   1 
ATOM   2580  C  CA  . PHE C  2 47  ? 8.963   182.680 16.413 1.00 25.65 ?  45  PHE C CA  1 
ATOM   2581  C  C   . PHE C  2 47  ? 9.282   183.240 17.789 1.00 29.06 ?  45  PHE C C   1 
ATOM   2582  O  O   . PHE C  2 47  ? 9.007   182.581 18.802 1.00 30.69 ?  45  PHE C O   1 
ATOM   2583  C  CB  . PHE C  2 47  ? 7.553   182.077 16.367 1.00 30.69 ?  45  PHE C CB  1 
ATOM   2584  C  CG  . PHE C  2 47  ? 6.431   183.073 16.293 1.00 29.73 ?  45  PHE C CG  1 
ATOM   2585  C  CD1 . PHE C  2 47  ? 6.341   183.985 15.250 1.00 30.99 ?  45  PHE C CD1 1 
ATOM   2586  C  CD2 . PHE C  2 47  ? 5.418   183.051 17.242 1.00 29.39 ?  45  PHE C CD2 1 
ATOM   2587  C  CE1 . PHE C  2 47  ? 5.268   184.870 15.177 1.00 30.47 ?  45  PHE C CE1 1 
ATOM   2588  C  CE2 . PHE C  2 47  ? 4.357   183.935 17.177 1.00 33.50 ?  45  PHE C CE2 1 
ATOM   2589  C  CZ  . PHE C  2 47  ? 4.280   184.848 16.131 1.00 30.95 ?  45  PHE C CZ  1 
ATOM   2590  N  N   . HIS C  2 48  ? 9.865   184.439 17.840 1.00 26.23 ?  46  HIS C N   1 
ATOM   2591  C  CA  . HIS C  2 48  ? 10.408  184.972 19.081 1.00 22.54 ?  46  HIS C CA  1 
ATOM   2592  C  C   . HIS C  2 48  ? 10.093  186.448 19.254 1.00 29.62 ?  46  HIS C C   1 
ATOM   2593  O  O   . HIS C  2 48  ? 9.978   187.203 18.278 1.00 24.67 ?  46  HIS C O   1 
ATOM   2594  C  CB  . HIS C  2 48  ? 11.922  184.794 19.138 1.00 30.62 ?  46  HIS C CB  1 
ATOM   2595  C  CG  . HIS C  2 48  ? 12.370  183.437 18.722 1.00 33.41 ?  46  HIS C CG  1 
ATOM   2596  N  ND1 . HIS C  2 48  ? 13.165  183.227 17.618 1.00 35.76 ?  46  HIS C ND1 1 
ATOM   2597  C  CD2 . HIS C  2 48  ? 12.119  182.214 19.248 1.00 38.64 ?  46  HIS C CD2 1 
ATOM   2598  C  CE1 . HIS C  2 48  ? 13.385  181.931 17.478 1.00 36.43 ?  46  HIS C CE1 1 
ATOM   2599  N  NE2 . HIS C  2 48  ? 12.763  181.293 18.455 1.00 36.95 ?  46  HIS C NE2 1 
ATOM   2600  N  N   . VAL C  2 49  ? 9.971   186.846 20.522 1.00 26.98 ?  47  VAL C N   1 
ATOM   2601  C  CA  . VAL C  2 49  ? 9.978   188.247 20.911 1.00 24.05 ?  47  VAL C CA  1 
ATOM   2602  C  C   . VAL C  2 49  ? 11.414  188.627 21.201 1.00 27.83 ?  47  VAL C C   1 
ATOM   2603  O  O   . VAL C  2 49  ? 12.068  188.007 22.048 1.00 29.08 ?  47  VAL C O   1 
ATOM   2604  C  CB  . VAL C  2 49  ? 9.102   188.504 22.139 1.00 25.98 ?  47  VAL C CB  1 
ATOM   2605  C  CG1 . VAL C  2 49  ? 9.197   189.977 22.509 1.00 26.12 ?  47  VAL C CG1 1 
ATOM   2606  C  CG2 . VAL C  2 49  ? 7.666   188.077 21.873 1.00 26.37 ?  47  VAL C CG2 1 
ATOM   2607  N  N   . HIS C  2 50  ? 11.918  189.610 20.478 1.00 24.77 ?  48  HIS C N   1 
ATOM   2608  C  CA  . HIS C  2 50  ? 13.258  190.111 20.703 1.00 23.05 ?  48  HIS C CA  1 
ATOM   2609  C  C   . HIS C  2 50  ? 13.196  191.346 21.572 1.00 27.69 ?  48  HIS C C   1 
ATOM   2610  O  O   . HIS C  2 50  ? 12.140  191.973 21.723 1.00 28.27 ?  48  HIS C O   1 
ATOM   2611  C  CB  . HIS C  2 50  ? 13.954  190.422 19.374 1.00 28.15 ?  48  HIS C CB  1 
ATOM   2612  C  CG  . HIS C  2 50  ? 14.303  189.189 18.590 1.00 26.25 ?  48  HIS C CG  1 
ATOM   2613  N  ND1 . HIS C  2 50  ? 15.594  188.871 18.237 1.00 27.50 ?  48  HIS C ND1 1 
ATOM   2614  C  CD2 . HIS C  2 50  ? 13.531  188.169 18.146 1.00 28.42 ?  48  HIS C CD2 1 
ATOM   2615  C  CE1 . HIS C  2 50  ? 15.601  187.725 17.573 1.00 28.05 ?  48  HIS C CE1 1 
ATOM   2616  N  NE2 . HIS C  2 50  ? 14.360  187.281 17.496 1.00 29.02 ?  48  HIS C NE2 1 
ATOM   2617  N  N   . GLU C  2 51  ? 14.360  191.702 22.126 1.00 24.56 ?  49  GLU C N   1 
ATOM   2618  C  CA  . GLU C  2 51  ? 14.414  192.660 23.228 1.00 27.78 ?  49  GLU C CA  1 
ATOM   2619  C  C   . GLU C  2 51  ? 13.958  194.068 22.830 1.00 27.61 ?  49  GLU C C   1 
ATOM   2620  O  O   . GLU C  2 51  ? 13.244  194.724 23.595 1.00 29.67 ?  49  GLU C O   1 
ATOM   2621  C  CB  . GLU C  2 51  ? 15.832  192.712 23.799 1.00 28.81 ?  49  GLU C CB  1 
ATOM   2622  C  CG  . GLU C  2 51  ? 15.914  193.609 25.025 1.00 31.38 ?  49  GLU C CG  1 
ATOM   2623  C  CD  . GLU C  2 51  ? 17.273  193.599 25.677 1.00 35.09 ?  49  GLU C CD  1 
ATOM   2624  O  OE1 . GLU C  2 51  ? 18.165  192.860 25.194 1.00 35.52 ?  49  GLU C OE1 1 
ATOM   2625  O  OE2 . GLU C  2 51  ? 17.437  194.325 26.678 1.00 40.57 ?  49  GLU C OE2 1 
ATOM   2626  N  N   . PHE C  2 52  ? 14.372  194.577 21.667 1.00 25.99 ?  50  PHE C N   1 
ATOM   2627  C  CA  . PHE C  2 52  ? 14.136  195.984 21.340 1.00 27.88 ?  50  PHE C CA  1 
ATOM   2628  C  C   . PHE C  2 52  ? 13.094  196.153 20.239 1.00 30.09 ?  50  PHE C C   1 
ATOM   2629  O  O   . PHE C  2 52  ? 13.071  195.397 19.262 1.00 28.70 ?  50  PHE C O   1 
ATOM   2630  C  CB  . PHE C  2 52  ? 15.444  196.679 20.917 1.00 28.82 ?  50  PHE C CB  1 
ATOM   2631  C  CG  . PHE C  2 52  ? 16.554  196.471 21.895 1.00 31.35 ?  50  PHE C CG  1 
ATOM   2632  C  CD1 . PHE C  2 52  ? 16.461  196.994 23.179 1.00 30.67 ?  50  PHE C CD1 1 
ATOM   2633  C  CD2 . PHE C  2 52  ? 17.664  195.726 21.552 1.00 33.63 ?  50  PHE C CD2 1 
ATOM   2634  C  CE1 . PHE C  2 52  ? 17.466  196.776 24.105 1.00 37.88 ?  50  PHE C CE1 1 
ATOM   2635  C  CE2 . PHE C  2 52  ? 18.669  195.501 22.463 1.00 34.75 ?  50  PHE C CE2 1 
ATOM   2636  C  CZ  . PHE C  2 52  ? 18.571  196.024 23.745 1.00 35.98 ?  50  PHE C CZ  1 
ATOM   2637  N  N   . GLY C  2 53  ? 12.245  197.161 20.401 1.00 23.76 ?  51  GLY C N   1 
ATOM   2638  C  CA  . GLY C  2 53  ? 11.299  197.541 19.377 1.00 25.19 ?  51  GLY C CA  1 
ATOM   2639  C  C   . GLY C  2 53  ? 11.943  198.568 18.476 1.00 26.92 ?  51  GLY C C   1 
ATOM   2640  O  O   . GLY C  2 53  ? 11.374  199.629 18.211 1.00 29.06 ?  51  GLY C O   1 
ATOM   2641  N  N   . ASP C  2 54  ? 13.161  198.257 18.047 1.00 29.51 ?  52  ASP C N   1 
ATOM   2642  C  CA  . ASP C  2 54  ? 14.001  199.118 17.227 1.00 21.66 ?  52  ASP C CA  1 
ATOM   2643  C  C   . ASP C  2 54  ? 14.096  198.478 15.850 1.00 31.18 ?  52  ASP C C   1 
ATOM   2644  O  O   . ASP C  2 54  ? 14.742  197.434 15.687 1.00 30.95 ?  52  ASP C O   1 
ATOM   2645  C  CB  . ASP C  2 54  ? 15.381  199.277 17.860 1.00 27.98 ?  52  ASP C CB  1 
ATOM   2646  C  CG  . ASP C  2 54  ? 16.284  200.236 17.082 1.00 31.02 ?  52  ASP C CG  1 
ATOM   2647  O  OD1 . ASP C  2 54  ? 16.054  200.438 15.872 1.00 31.13 ?  52  ASP C OD1 1 
ATOM   2648  O  OD2 . ASP C  2 54  ? 17.226  200.794 17.685 1.00 33.41 ?  52  ASP C OD2 1 
ATOM   2649  N  N   . ASN C  2 55  ? 13.448  199.102 14.867 1.00 29.71 ?  53  ASN C N   1 
ATOM   2650  C  CA  . ASN C  2 55  ? 13.465  198.666 13.475 1.00 31.28 ?  53  ASN C CA  1 
ATOM   2651  C  C   . ASN C  2 55  ? 14.307  199.589 12.590 1.00 29.78 ?  53  ASN C C   1 
ATOM   2652  O  O   . ASN C  2 55  ? 14.151  199.580 11.372 1.00 29.82 ?  53  ASN C O   1 
ATOM   2653  C  CB  . ASN C  2 55  ? 12.026  198.597 12.950 1.00 31.01 ?  53  ASN C CB  1 
ATOM   2654  C  CG  . ASN C  2 55  ? 11.900  197.895 11.611 1.00 45.66 ?  53  ASN C CG  1 
ATOM   2655  O  OD1 . ASN C  2 55  ? 11.292  198.437 10.678 1.00 51.33 ?  53  ASN C OD1 1 
ATOM   2656  N  ND2 . ASN C  2 55  ? 12.430  196.671 11.513 1.00 43.66 ?  53  ASN C ND2 1 
ATOM   2657  N  N   . THR C  2 56  ? 15.197  200.394 13.174 1.00 28.96 ?  54  THR C N   1 
ATOM   2658  C  CA  . THR C  2 56  ? 15.920  201.384 12.375 1.00 27.74 ?  54  THR C CA  1 
ATOM   2659  C  C   . THR C  2 56  ? 16.887  200.746 11.395 1.00 31.03 ?  54  THR C C   1 
ATOM   2660  O  O   . THR C  2 56  ? 17.254  201.386 10.410 1.00 37.61 ?  54  THR C O   1 
ATOM   2661  C  CB  . THR C  2 56  ? 16.692  202.355 13.270 1.00 29.65 ?  54  THR C CB  1 
ATOM   2662  O  OG1 . THR C  2 56  ? 17.545  201.620 14.151 1.00 32.23 ?  54  THR C OG1 1 
ATOM   2663  C  CG2 . THR C  2 56  ? 15.736  203.206 14.088 1.00 26.02 ?  54  THR C CG2 1 
ATOM   2664  N  N   . ALA C  2 57  ? 17.301  199.506 11.633 1.00 31.87 ?  55  ALA C N   1 
ATOM   2665  C  CA  . ALA C  2 57  ? 18.096  198.742 10.682 1.00 35.81 ?  55  ALA C CA  1 
ATOM   2666  C  C   . ALA C  2 57  ? 17.356  197.478 10.295 1.00 34.45 ?  55  ALA C C   1 
ATOM   2667  O  O   . ALA C  2 57  ? 17.943  196.401 10.196 1.00 37.44 ?  55  ALA C O   1 
ATOM   2668  C  CB  . ALA C  2 57  ? 19.468  198.403 11.253 1.00 37.46 ?  55  ALA C CB  1 
ATOM   2669  N  N   . GLY C  2 58  ? 16.046  197.599 10.083 1.00 32.89 ?  56  GLY C N   1 
ATOM   2670  C  CA  . GLY C  2 58  ? 15.253  196.404 9.877  1.00 31.58 ?  56  GLY C CA  1 
ATOM   2671  C  C   . GLY C  2 58  ? 15.241  195.553 11.142 1.00 36.35 ?  56  GLY C C   1 
ATOM   2672  O  O   . GLY C  2 58  ? 15.388  196.045 12.270 1.00 33.00 ?  56  GLY C O   1 
ATOM   2673  N  N   . CYS C  2 59  ? 15.092  194.245 10.942 1.00 30.54 ?  57  CYS C N   1 
ATOM   2674  C  CA  . CYS C  2 59  ? 14.947  193.298 12.047 1.00 29.68 ?  57  CYS C CA  1 
ATOM   2675  C  C   . CYS C  2 59  ? 16.241  193.107 12.830 1.00 35.03 ?  57  CYS C C   1 
ATOM   2676  O  O   . CYS C  2 59  ? 16.200  192.646 13.984 1.00 30.48 ?  57  CYS C O   1 
ATOM   2677  C  CB  . CYS C  2 59  ? 14.449  191.963 11.487 1.00 29.44 ?  57  CYS C CB  1 
ATOM   2678  S  SG  . CYS C  2 59  ? 12.822  192.126 10.698 1.00 40.40 ?  57  CYS C SG  1 
ATOM   2679  N  N   . THR C  2 60  ? 17.378  193.473 12.234 1.00 33.10 ?  58  THR C N   1 
ATOM   2680  C  CA  . THR C  2 60  ? 18.674  193.333 12.894 1.00 30.77 ?  58  THR C CA  1 
ATOM   2681  C  C   . THR C  2 60  ? 18.730  194.125 14.192 1.00 30.91 ?  58  THR C C   1 
ATOM   2682  O  O   . THR C  2 60  ? 19.326  193.676 15.178 1.00 34.26 ?  58  THR C O   1 
ATOM   2683  C  CB  . THR C  2 60  ? 19.784  193.805 11.941 1.00 37.55 ?  58  THR C CB  1 
ATOM   2684  O  OG1 . THR C  2 60  ? 19.905  192.883 10.853 1.00 41.75 ?  58  THR C OG1 1 
ATOM   2685  C  CG2 . THR C  2 60  ? 21.125  193.908 12.657 1.00 41.76 ?  58  THR C CG2 1 
ATOM   2686  N  N   . SER C  2 61  ? 18.118  195.310 14.219 1.00 28.74 ?  59  SER C N   1 
ATOM   2687  C  CA  . SER C  2 61  ? 18.253  196.158 15.391 1.00 30.06 ?  59  SER C CA  1 
ATOM   2688  C  C   . SER C  2 61  ? 17.308  195.769 16.529 1.00 27.54 ?  59  SER C C   1 
ATOM   2689  O  O   . SER C  2 61  ? 17.312  196.436 17.571 1.00 29.93 ?  59  SER C O   1 
ATOM   2690  C  CB  . SER C  2 61  ? 18.065  197.633 15.005 1.00 34.54 ?  59  SER C CB  1 
ATOM   2691  O  OG  . SER C  2 61  ? 17.140  197.789 13.937 1.00 33.66 ?  59  SER C OG  1 
ATOM   2692  N  N   . ALA C  2 62  ? 16.531  194.702 16.376 1.00 26.97 ?  60  ALA C N   1 
ATOM   2693  C  CA  . ALA C  2 62  ? 15.684  194.249 17.476 1.00 28.15 ?  60  ALA C CA  1 
ATOM   2694  C  C   . ALA C  2 62  ? 16.479  193.561 18.584 1.00 29.31 ?  60  ALA C C   1 
ATOM   2695  O  O   . ALA C  2 62  ? 15.933  193.325 19.671 1.00 29.99 ?  60  ALA C O   1 
ATOM   2696  C  CB  . ALA C  2 62  ? 14.604  193.310 16.941 1.00 31.00 ?  60  ALA C CB  1 
ATOM   2697  N  N   . GLY C  2 63  ? 17.751  193.254 18.348 1.00 30.84 ?  61  GLY C N   1 
ATOM   2698  C  CA  . GLY C  2 63  ? 18.592  192.646 19.352 1.00 27.67 ?  61  GLY C CA  1 
ATOM   2699  C  C   . GLY C  2 63  ? 18.275  191.177 19.529 1.00 29.13 ?  61  GLY C C   1 
ATOM   2700  O  O   . GLY C  2 63  ? 17.666  190.543 18.660 1.00 31.29 ?  61  GLY C O   1 
ATOM   2701  N  N   . PRO C  2 64  ? 18.677  190.610 20.666 1.00 33.43 ?  62  PRO C N   1 
ATOM   2702  C  CA  . PRO C  2 64  ? 18.527  189.172 20.901 1.00 30.84 ?  62  PRO C CA  1 
ATOM   2703  C  C   . PRO C  2 64  ? 17.125  188.849 21.409 1.00 33.33 ?  62  PRO C C   1 
ATOM   2704  O  O   . PRO C  2 64  ? 16.260  189.714 21.528 1.00 29.45 ?  62  PRO C O   1 
ATOM   2705  C  CB  . PRO C  2 64  ? 19.572  188.908 21.983 1.00 32.85 ?  62  PRO C CB  1 
ATOM   2706  C  CG  . PRO C  2 64  ? 19.493  190.151 22.816 1.00 32.49 ?  62  PRO C CG  1 
ATOM   2707  C  CD  . PRO C  2 64  ? 19.278  191.286 21.833 1.00 31.57 ?  62  PRO C CD  1 
ATOM   2708  N  N   . HIS C  2 65  ? 16.915  187.576 21.732 1.00 30.58 ?  63  HIS C N   1 
ATOM   2709  C  CA  . HIS C  2 65  ? 15.637  187.167 22.292 1.00 28.50 ?  63  HIS C CA  1 
ATOM   2710  C  C   . HIS C  2 65  ? 15.403  187.903 23.610 1.00 29.87 ?  63  HIS C C   1 
ATOM   2711  O  O   . HIS C  2 65  ? 16.341  188.159 24.368 1.00 31.61 ?  63  HIS C O   1 
ATOM   2712  C  CB  . HIS C  2 65  ? 15.608  185.646 22.472 1.00 32.60 ?  63  HIS C CB  1 
ATOM   2713  C  CG  . HIS C  2 65  ? 15.655  184.896 21.173 1.00 36.19 ?  63  HIS C CG  1 
ATOM   2714  N  ND1 . HIS C  2 65  ? 15.587  183.525 21.092 1.00 34.67 ?  63  HIS C ND1 1 
ATOM   2715  C  CD2 . HIS C  2 65  ? 15.752  185.335 19.895 1.00 39.69 ?  63  HIS C CD2 1 
ATOM   2716  C  CE1 . HIS C  2 65  ? 15.640  183.147 19.830 1.00 36.70 ?  63  HIS C CE1 1 
ATOM   2717  N  NE2 . HIS C  2 65  ? 15.735  184.228 19.079 1.00 40.54 ?  63  HIS C NE2 1 
ATOM   2718  N  N   . PHE C  2 66  ? 14.157  188.324 23.839 1.00 30.96 ?  64  PHE C N   1 
ATOM   2719  C  CA  . PHE C  2 66  ? 13.822  189.015 25.080 1.00 28.94 ?  64  PHE C CA  1 
ATOM   2720  C  C   . PHE C  2 66  ? 14.046  188.072 26.258 1.00 29.53 ?  64  PHE C C   1 
ATOM   2721  O  O   . PHE C  2 66  ? 13.398  187.019 26.349 1.00 30.44 ?  64  PHE C O   1 
ATOM   2722  C  CB  . PHE C  2 66  ? 12.374  189.487 25.049 1.00 28.62 ?  64  PHE C CB  1 
ATOM   2723  C  CG  . PHE C  2 66  ? 11.944  190.241 26.300 1.00 30.12 ?  64  PHE C CG  1 
ATOM   2724  C  CD1 . PHE C  2 66  ? 12.781  191.163 26.910 1.00 24.67 ?  64  PHE C CD1 1 
ATOM   2725  C  CD2 . PHE C  2 66  ? 10.685  190.017 26.846 1.00 27.33 ?  64  PHE C CD2 1 
ATOM   2726  C  CE1 . PHE C  2 66  ? 12.373  191.852 28.054 1.00 29.28 ?  64  PHE C CE1 1 
ATOM   2727  C  CE2 . PHE C  2 66  ? 10.264  190.691 27.965 1.00 27.30 ?  64  PHE C CE2 1 
ATOM   2728  C  CZ  . PHE C  2 66  ? 11.109  191.607 28.586 1.00 31.26 ?  64  PHE C CZ  1 
ATOM   2729  N  N   . ASN C  2 67  ? 14.964  188.446 27.151 1.00 31.30 ?  65  ASN C N   1 
ATOM   2730  C  CA  . ASN C  2 67  ? 15.498  187.525 28.152 1.00 32.77 ?  65  ASN C CA  1 
ATOM   2731  C  C   . ASN C  2 67  ? 15.790  188.261 29.456 1.00 34.19 ?  65  ASN C C   1 
ATOM   2732  O  O   . ASN C  2 67  ? 16.933  188.283 29.917 1.00 38.25 ?  65  ASN C O   1 
ATOM   2733  C  CB  . ASN C  2 67  ? 16.772  186.862 27.600 1.00 36.75 ?  65  ASN C CB  1 
ATOM   2734  C  CG  . ASN C  2 67  ? 17.315  185.743 28.492 1.00 44.65 ?  65  ASN C CG  1 
ATOM   2735  O  OD1 . ASN C  2 67  ? 16.566  185.097 29.236 1.00 36.77 ?  65  ASN C OD1 1 
ATOM   2736  N  ND2 . ASN C  2 67  ? 18.623  185.495 28.392 1.00 35.15 ?  65  ASN C ND2 1 
ATOM   2737  N  N   . PRO C  2 68  ? 14.785  188.866 30.089 1.00 32.59 ?  66  PRO C N   1 
ATOM   2738  C  CA  . PRO C  2 68  ? 15.047  189.623 31.323 1.00 38.25 ?  66  PRO C CA  1 
ATOM   2739  C  C   . PRO C  2 68  ? 15.471  188.760 32.511 1.00 42.93 ?  66  PRO C C   1 
ATOM   2740  O  O   . PRO C  2 68  ? 15.977  189.314 33.492 1.00 44.56 ?  66  PRO C O   1 
ATOM   2741  C  CB  . PRO C  2 68  ? 13.704  190.302 31.598 1.00 32.90 ?  66  PRO C CB  1 
ATOM   2742  C  CG  . PRO C  2 68  ? 12.720  189.273 31.110 1.00 34.23 ?  66  PRO C CG  1 
ATOM   2743  C  CD  . PRO C  2 68  ? 13.340  188.701 29.847 1.00 31.55 ?  66  PRO C CD  1 
ATOM   2744  N  N   . LEU C  2 69  ? 15.275  187.441 32.467 1.00 40.04 ?  67  LEU C N   1 
ATOM   2745  C  CA  . LEU C  2 69  ? 15.715  186.549 33.536 1.00 43.04 ?  67  LEU C CA  1 
ATOM   2746  C  C   . LEU C  2 69  ? 17.075  185.914 33.265 1.00 44.36 ?  67  LEU C C   1 
ATOM   2747  O  O   . LEU C  2 69  ? 17.485  185.032 34.021 1.00 52.02 ?  67  LEU C O   1 
ATOM   2748  C  CB  . LEU C  2 69  ? 14.678  185.455 33.777 1.00 41.47 ?  67  LEU C CB  1 
ATOM   2749  C  CG  . LEU C  2 69  ? 13.263  185.937 34.107 1.00 47.93 ?  67  LEU C CG  1 
ATOM   2750  C  CD1 . LEU C  2 69  ? 12.348  184.772 34.523 1.00 44.49 ?  67  LEU C CD1 1 
ATOM   2751  C  CD2 . LEU C  2 69  ? 13.310  187.007 35.177 1.00 45.41 ?  67  LEU C CD2 1 
ATOM   2752  N  N   . SER C  2 70  ? 17.780  186.345 32.217 1.00 46.37 ?  68  SER C N   1 
ATOM   2753  C  CA  . SER C  2 70  ? 19.113  185.837 31.875 1.00 45.31 ?  68  SER C CA  1 
ATOM   2754  C  C   . SER C  2 70  ? 19.170  184.309 31.949 1.00 51.34 ?  68  SER C C   1 
ATOM   2755  O  O   . SER C  2 70  ? 19.929  183.724 32.722 1.00 51.60 ?  68  SER C O   1 
ATOM   2756  C  CB  . SER C  2 70  ? 20.183  186.452 32.782 1.00 45.80 ?  68  SER C CB  1 
ATOM   2757  O  OG  . SER C  2 70  ? 19.920  187.820 33.026 1.00 50.65 ?  68  SER C OG  1 
ATOM   2758  N  N   . ARG C  2 71  ? 18.338  183.668 31.136 1.00 45.38 ?  69  ARG C N   1 
ATOM   2759  C  CA  . ARG C  2 71  ? 18.260  182.220 31.044 1.00 43.87 ?  69  ARG C CA  1 
ATOM   2760  C  C   . ARG C  2 71  ? 18.756  181.762 29.677 1.00 49.69 ?  69  ARG C C   1 
ATOM   2761  O  O   . ARG C  2 71  ? 19.103  182.568 28.813 1.00 47.52 ?  69  ARG C O   1 
ATOM   2762  C  CB  . ARG C  2 71  ? 16.829  181.754 31.297 1.00 42.23 ?  69  ARG C CB  1 
ATOM   2763  C  CG  . ARG C  2 71  ? 16.490  181.734 32.767 1.00 46.92 ?  69  ARG C CG  1 
ATOM   2764  C  CD  . ARG C  2 71  ? 15.097  181.216 32.997 1.00 51.16 ?  69  ARG C CD  1 
ATOM   2765  N  NE  . ARG C  2 71  ? 14.561  181.687 34.267 1.00 60.75 ?  69  ARG C NE  1 
ATOM   2766  C  CZ  . ARG C  2 71  ? 13.453  181.227 34.831 1.00 61.73 ?  69  ARG C CZ  1 
ATOM   2767  N  NH1 . ARG C  2 71  ? 12.729  180.274 34.261 1.00 55.21 ?  69  ARG C NH1 1 
ATOM   2768  N  NH2 . ARG C  2 71  ? 13.054  181.743 35.991 1.00 58.69 ?  69  ARG C NH2 1 
ATOM   2769  N  N   . LYS C  2 72  ? 18.787  180.451 29.487 1.00 41.95 ?  70  LYS C N   1 
ATOM   2770  C  CA  . LYS C  2 72  ? 19.192  179.879 28.216 1.00 44.74 ?  70  LYS C CA  1 
ATOM   2771  C  C   . LYS C  2 72  ? 17.967  179.706 27.321 1.00 44.95 ?  70  LYS C C   1 
ATOM   2772  O  O   . LYS C  2 72  ? 16.830  179.629 27.791 1.00 42.02 ?  70  LYS C O   1 
ATOM   2773  C  CB  . LYS C  2 72  ? 19.893  178.532 28.439 1.00 46.50 ?  70  LYS C CB  1 
ATOM   2774  C  CG  . LYS C  2 72  ? 21.299  178.616 29.066 1.00 48.86 ?  70  LYS C CG  1 
ATOM   2775  C  CD  . LYS C  2 72  ? 22.178  179.616 28.324 1.00 58.34 ?  70  LYS C CD  1 
ATOM   2776  C  CE  . LYS C  2 72  ? 23.680  179.387 28.561 1.00 61.85 ?  70  LYS C CE  1 
ATOM   2777  N  NZ  . LYS C  2 72  ? 24.512  180.085 27.504 1.00 64.98 ?  70  LYS C NZ  1 
ATOM   2778  N  N   . HIS C  2 73  ? 18.208  179.638 26.016 1.00 41.80 ?  71  HIS C N   1 
ATOM   2779  C  CA  . HIS C  2 73  ? 17.107  179.490 25.076 1.00 38.10 ?  71  HIS C CA  1 
ATOM   2780  C  C   . HIS C  2 73  ? 16.458  178.116 25.244 1.00 43.04 ?  71  HIS C C   1 
ATOM   2781  O  O   . HIS C  2 73  ? 17.131  177.118 25.522 1.00 43.57 ?  71  HIS C O   1 
ATOM   2782  C  CB  . HIS C  2 73  ? 17.621  179.693 23.650 1.00 40.42 ?  71  HIS C CB  1 
ATOM   2783  C  CG  . HIS C  2 73  ? 16.613  179.404 22.584 1.00 42.09 ?  71  HIS C CG  1 
ATOM   2784  N  ND1 . HIS C  2 73  ? 15.555  180.242 22.309 1.00 38.92 ?  71  HIS C ND1 1 
ATOM   2785  C  CD2 . HIS C  2 73  ? 16.511  178.371 21.717 1.00 37.84 ?  71  HIS C CD2 1 
ATOM   2786  C  CE1 . HIS C  2 73  ? 14.833  179.727 21.333 1.00 34.75 ?  71  HIS C CE1 1 
ATOM   2787  N  NE2 . HIS C  2 73  ? 15.394  178.594 20.951 1.00 39.41 ?  71  HIS C NE2 1 
ATOM   2788  N  N   . GLY C  2 74  ? 15.135  178.069 25.100 1.00 39.46 ?  72  GLY C N   1 
ATOM   2789  C  CA  . GLY C  2 74  ? 14.403  176.821 25.111 1.00 36.34 ?  72  GLY C CA  1 
ATOM   2790  C  C   . GLY C  2 74  ? 13.124  176.987 24.323 1.00 37.05 ?  72  GLY C C   1 
ATOM   2791  O  O   . GLY C  2 74  ? 12.876  178.039 23.736 1.00 43.19 ?  72  GLY C O   1 
ATOM   2792  N  N   . GLY C  2 75  ? 12.323  175.925 24.283 1.00 35.08 ?  73  GLY C N   1 
ATOM   2793  C  CA  . GLY C  2 75  ? 10.980  176.006 23.748 1.00 36.13 ?  73  GLY C CA  1 
ATOM   2794  C  C   . GLY C  2 75  ? 10.027  176.631 24.743 1.00 38.96 ?  73  GLY C C   1 
ATOM   2795  O  O   . GLY C  2 75  ? 10.337  176.822 25.929 1.00 39.91 ?  73  GLY C O   1 
ATOM   2796  N  N   . PRO C  2 76  ? 8.822   176.958 24.271 1.00 33.82 ?  74  PRO C N   1 
ATOM   2797  C  CA  . PRO C  2 76  ? 7.844   177.597 25.162 1.00 34.27 ?  74  PRO C CA  1 
ATOM   2798  C  C   . PRO C  2 76  ? 7.383   176.704 26.309 1.00 42.60 ?  74  PRO C C   1 
ATOM   2799  O  O   . PRO C  2 76  ? 6.948   177.236 27.339 1.00 38.68 ?  74  PRO C O   1 
ATOM   2800  C  CB  . PRO C  2 76  ? 6.684   177.945 24.221 1.00 37.15 ?  74  PRO C CB  1 
ATOM   2801  C  CG  . PRO C  2 76  ? 6.831   176.995 23.061 1.00 39.39 ?  74  PRO C CG  1 
ATOM   2802  C  CD  . PRO C  2 76  ? 8.303   176.764 22.906 1.00 38.28 ?  74  PRO C CD  1 
ATOM   2803  N  N   . LYS C  2 77  ? 7.461   175.373 26.156 1.00 45.55 ?  75  LYS C N   1 
ATOM   2804  C  CA  . LYS C  2 77  ? 7.076   174.413 27.192 1.00 44.15 ?  75  LYS C CA  1 
ATOM   2805  C  C   . LYS C  2 77  ? 8.129   174.265 28.279 1.00 47.09 ?  75  LYS C C   1 
ATOM   2806  O  O   . LYS C  2 77  ? 7.831   173.693 29.337 1.00 46.60 ?  75  LYS C O   1 
ATOM   2807  C  CB  . LYS C  2 77  ? 6.854   173.012 26.594 1.00 47.96 ?  75  LYS C CB  1 
ATOM   2808  C  CG  . LYS C  2 77  ? 5.818   172.839 25.466 1.00 55.00 ?  75  LYS C CG  1 
ATOM   2809  C  CD  . LYS C  2 77  ? 5.964   171.409 24.866 1.00 59.38 ?  75  LYS C CD  1 
ATOM   2810  C  CE  . LYS C  2 77  ? 5.139   171.162 23.573 1.00 63.75 ?  75  LYS C CE  1 
ATOM   2811  N  NZ  . LYS C  2 77  ? 4.136   170.029 23.679 1.00 53.77 ?  75  LYS C NZ  1 
ATOM   2812  N  N   . ASP C  2 78  ? 9.362   174.692 28.020 1.00 39.64 ?  76  ASP C N   1 
ATOM   2813  C  CA  . ASP C  2 78  ? 10.441  174.508 28.978 1.00 40.61 ?  76  ASP C CA  1 
ATOM   2814  C  C   . ASP C  2 78  ? 10.416  175.578 30.054 1.00 47.37 ?  76  ASP C C   1 
ATOM   2815  O  O   . ASP C  2 78  ? 10.037  176.724 29.817 1.00 43.92 ?  76  ASP C O   1 
ATOM   2816  C  CB  . ASP C  2 78  ? 11.805  174.517 28.282 1.00 41.06 ?  76  ASP C CB  1 
ATOM   2817  C  CG  . ASP C  2 78  ? 11.842  173.587 27.084 1.00 50.37 ?  76  ASP C CG  1 
ATOM   2818  O  OD1 . ASP C  2 78  ? 11.320  172.455 27.222 1.00 48.31 ?  76  ASP C OD1 1 
ATOM   2819  O  OD2 . ASP C  2 78  ? 12.388  173.971 26.019 1.00 49.42 ?  76  ASP C OD2 1 
ATOM   2820  N  N   . GLU C  2 79  ? 10.819  175.178 31.258 1.00 45.50 ?  77  GLU C N   1 
ATOM   2821  C  CA  . GLU C  2 79  ? 11.005  176.137 32.333 1.00 43.47 ?  77  GLU C CA  1 
ATOM   2822  C  C   . GLU C  2 79  ? 12.222  177.009 32.066 1.00 45.26 ?  77  GLU C C   1 
ATOM   2823  O  O   . GLU C  2 79  ? 12.189  178.222 32.308 1.00 43.56 ?  77  GLU C O   1 
ATOM   2824  C  CB  . GLU C  2 79  ? 11.136  175.399 33.668 1.00 49.63 ?  77  GLU C CB  1 
ATOM   2825  C  CG  . GLU C  2 79  ? 10.787  176.222 34.900 1.00 59.43 ?  77  GLU C CG  1 
ATOM   2826  C  CD  . GLU C  2 79  ? 11.938  177.101 35.367 1.00 70.68 ?  77  GLU C CD  1 
ATOM   2827  O  OE1 . GLU C  2 79  ? 13.112  176.769 35.062 1.00 71.24 ?  77  GLU C OE1 1 
ATOM   2828  O  OE2 . GLU C  2 79  ? 11.660  178.119 36.045 1.00 75.74 ?  77  GLU C OE2 1 
ATOM   2829  N  N   . GLU C  2 80  ? 13.303  176.411 31.560 1.00 39.85 ?  78  GLU C N   1 
ATOM   2830  C  CA  . GLU C  2 80  ? 14.502  177.149 31.154 1.00 43.61 ?  78  GLU C CA  1 
ATOM   2831  C  C   . GLU C  2 80  ? 14.282  177.698 29.740 1.00 40.30 ?  78  GLU C C   1 
ATOM   2832  O  O   . GLU C  2 80  ? 14.519  177.024 28.736 1.00 39.40 ?  78  GLU C O   1 
ATOM   2833  C  CB  . GLU C  2 80  ? 15.740  176.255 31.224 1.00 42.75 ?  78  GLU C CB  1 
ATOM   2834  C  CG  . GLU C  2 80  ? 17.071  176.970 30.912 1.00 43.15 ?  78  GLU C CG  1 
ATOM   2835  C  CD  . GLU C  2 80  ? 17.524  177.906 32.015 1.00 49.56 ?  78  GLU C CD  1 
ATOM   2836  O  OE1 . GLU C  2 80  ? 18.521  178.638 31.800 1.00 51.55 ?  78  GLU C OE1 1 
ATOM   2837  O  OE2 . GLU C  2 80  ? 16.893  177.908 33.103 1.00 57.84 ?  78  GLU C OE2 1 
ATOM   2838  N  N   . ARG C  2 81  ? 13.820  178.940 29.656 1.00 39.09 ?  79  ARG C N   1 
ATOM   2839  C  CA  . ARG C  2 81  ? 13.612  179.574 28.362 1.00 39.13 ?  79  ARG C CA  1 
ATOM   2840  C  C   . ARG C  2 81  ? 13.774  181.070 28.539 1.00 38.31 ?  79  ARG C C   1 
ATOM   2841  O  O   . ARG C  2 81  ? 13.677  181.594 29.657 1.00 35.48 ?  79  ARG C O   1 
ATOM   2842  C  CB  . ARG C  2 81  ? 12.224  179.265 27.787 1.00 39.77 ?  79  ARG C CB  1 
ATOM   2843  C  CG  . ARG C  2 81  ? 11.096  179.586 28.749 1.00 37.74 ?  79  ARG C CG  1 
ATOM   2844  C  CD  . ARG C  2 81  ? 9.734   179.479 28.097 1.00 34.30 ?  79  ARG C CD  1 
ATOM   2845  N  NE  . ARG C  2 81  ? 9.327   180.753 27.521 1.00 30.82 ?  79  ARG C NE  1 
ATOM   2846  C  CZ  . ARG C  2 81  ? 8.098   181.035 27.113 1.00 36.21 ?  79  ARG C CZ  1 
ATOM   2847  N  NH1 . ARG C  2 81  ? 7.118   180.158 27.220 1.00 34.03 ?  79  ARG C NH1 1 
ATOM   2848  N  NH2 . ARG C  2 81  ? 7.844   182.236 26.597 1.00 30.37 ?  79  ARG C NH2 1 
ATOM   2849  N  N   . HIS C  2 82  ? 14.059  181.748 27.428 1.00 36.00 ?  80  HIS C N   1 
ATOM   2850  C  CA  . HIS C  2 82  ? 13.897  183.196 27.378 1.00 31.58 ?  80  HIS C CA  1 
ATOM   2851  C  C   . HIS C  2 82  ? 12.411  183.512 27.470 1.00 30.01 ?  80  HIS C C   1 
ATOM   2852  O  O   . HIS C  2 82  ? 11.567  182.741 26.999 1.00 32.60 ?  80  HIS C O   1 
ATOM   2853  C  CB  . HIS C  2 82  ? 14.461  183.766 26.068 1.00 34.25 ?  80  HIS C CB  1 
ATOM   2854  C  CG  . HIS C  2 82  ? 15.893  183.401 25.802 1.00 39.89 ?  80  HIS C CG  1 
ATOM   2855  N  ND1 . HIS C  2 82  ? 16.382  183.173 24.529 1.00 42.73 ?  80  HIS C ND1 1 
ATOM   2856  C  CD2 . HIS C  2 82  ? 16.949  183.263 26.637 1.00 39.84 ?  80  HIS C CD2 1 
ATOM   2857  C  CE1 . HIS C  2 82  ? 17.671  182.897 24.599 1.00 41.62 ?  80  HIS C CE1 1 
ATOM   2858  N  NE2 . HIS C  2 82  ? 18.040  182.948 25.867 1.00 42.27 ?  80  HIS C NE2 1 
ATOM   2859  N  N   . VAL C  2 83  ? 12.082  184.649 28.091 1.00 27.49 ?  81  VAL C N   1 
ATOM   2860  C  CA  . VAL C  2 83  ? 10.692  185.104 28.067 1.00 27.48 ?  81  VAL C CA  1 
ATOM   2861  C  C   . VAL C  2 83  ? 10.170  185.157 26.633 1.00 30.80 ?  81  VAL C C   1 
ATOM   2862  O  O   . VAL C  2 83  ? 9.037   184.742 26.348 1.00 32.49 ?  81  VAL C O   1 
ATOM   2863  C  CB  . VAL C  2 83  ? 10.562  186.468 28.776 1.00 33.93 ?  81  VAL C CB  1 
ATOM   2864  C  CG1 . VAL C  2 83  ? 9.221   187.115 28.450 1.00 28.55 ?  81  VAL C CG1 1 
ATOM   2865  C  CG2 . VAL C  2 83  ? 10.712  186.284 30.284 1.00 34.15 ?  81  VAL C CG2 1 
ATOM   2866  N  N   . GLY C  2 84  ? 11.000  185.605 25.700 1.00 28.55 ?  82  GLY C N   1 
ATOM   2867  C  CA  . GLY C  2 84  ? 10.549  185.719 24.315 1.00 27.85 ?  82  GLY C CA  1 
ATOM   2868  C  C   . GLY C  2 84  ? 10.452  184.446 23.488 1.00 34.09 ?  82  GLY C C   1 
ATOM   2869  O  O   . GLY C  2 84  ? 10.174  184.519 22.283 1.00 29.97 ?  82  GLY C O   1 
ATOM   2870  N  N   . ASP C  2 85  ? 10.635  183.264 24.080 1.00 31.07 ?  83  ASP C N   1 
ATOM   2871  C  CA  . ASP C  2 85  ? 10.767  182.030 23.305 1.00 33.16 ?  83  ASP C CA  1 
ATOM   2872  C  C   . ASP C  2 85  ? 9.387   181.445 23.027 1.00 34.00 ?  83  ASP C C   1 
ATOM   2873  O  O   . ASP C  2 85  ? 8.851   180.688 23.835 1.00 33.53 ?  83  ASP C O   1 
ATOM   2874  C  CB  . ASP C  2 85  ? 11.620  181.015 24.058 1.00 35.14 ?  83  ASP C CB  1 
ATOM   2875  C  CG  . ASP C  2 85  ? 13.098  181.305 23.977 1.00 39.90 ?  83  ASP C CG  1 
ATOM   2876  O  OD1 . ASP C  2 85  ? 13.507  182.097 23.090 1.00 41.61 ?  83  ASP C OD1 1 
ATOM   2877  O  OD2 . ASP C  2 85  ? 13.866  180.741 24.803 1.00 36.83 ?  83  ASP C OD2 1 
ATOM   2878  N  N   . LEU C  2 86  ? 8.811   181.750 21.870 1.00 30.36 ?  84  LEU C N   1 
ATOM   2879  C  CA  . LEU C  2 86  ? 7.495   181.212 21.546 1.00 31.23 ?  84  LEU C CA  1 
ATOM   2880  C  C   . LEU C  2 86  ? 7.557   180.020 20.610 1.00 31.19 ?  84  LEU C C   1 
ATOM   2881  O  O   . LEU C  2 86  ? 6.522   179.618 20.072 1.00 36.35 ?  84  LEU C O   1 
ATOM   2882  C  CB  . LEU C  2 86  ? 6.605   182.306 20.953 1.00 29.64 ?  84  LEU C CB  1 
ATOM   2883  C  CG  . LEU C  2 86  ? 6.481   183.471 21.949 1.00 29.82 ?  84  LEU C CG  1 
ATOM   2884  C  CD1 . LEU C  2 86  ? 5.689   184.608 21.354 1.00 32.40 ?  84  LEU C CD1 1 
ATOM   2885  C  CD2 . LEU C  2 86  ? 5.860   182.972 23.265 1.00 33.90 ?  84  LEU C CD2 1 
ATOM   2886  N  N   . GLY C  2 87  ? 8.737   179.439 20.400 1.00 31.39 ?  85  GLY C N   1 
ATOM   2887  C  CA  . GLY C  2 87  ? 8.804   178.166 19.692 1.00 31.40 ?  85  GLY C CA  1 
ATOM   2888  C  C   . GLY C  2 87  ? 8.757   178.273 18.183 1.00 32.38 ?  85  GLY C C   1 
ATOM   2889  O  O   . GLY C  2 87  ? 9.417   179.147 17.612 1.00 31.88 ?  85  GLY C O   1 
ATOM   2890  N  N   . ASN C  2 88  ? 7.982   177.397 17.527 1.00 29.52 ?  86  ASN C N   1 
ATOM   2891  C  CA  . ASN C  2 88  ? 7.915   177.331 16.070 1.00 30.77 ?  86  ASN C CA  1 
ATOM   2892  C  C   . ASN C  2 88  ? 6.488   177.552 15.609 1.00 34.11 ?  86  ASN C C   1 
ATOM   2893  O  O   . ASN C  2 88  ? 5.545   177.044 16.221 1.00 31.06 ?  86  ASN C O   1 
ATOM   2894  C  CB  . ASN C  2 88  ? 8.368   175.957 15.538 1.00 34.13 ?  86  ASN C CB  1 
ATOM   2895  C  CG  . ASN C  2 88  ? 9.844   175.730 15.676 1.00 33.40 ?  86  ASN C CG  1 
ATOM   2896  O  OD1 . ASN C  2 88  ? 10.662  176.478 15.140 1.00 37.40 ?  86  ASN C OD1 1 
ATOM   2897  N  ND2 . ASN C  2 88  ? 10.200  174.700 16.413 1.00 35.95 ?  86  ASN C ND2 1 
ATOM   2898  N  N   . VAL C  2 89  ? 6.331   178.291 14.517 1.00 30.37 ?  87  VAL C N   1 
ATOM   2899  C  CA  . VAL C  2 89  ? 5.082   178.292 13.774 1.00 31.83 ?  87  VAL C CA  1 
ATOM   2900  C  C   . VAL C  2 89  ? 5.305   177.462 12.518 1.00 30.27 ?  87  VAL C C   1 
ATOM   2901  O  O   . VAL C  2 89  ? 6.439   177.242 12.085 1.00 32.90 ?  87  VAL C O   1 
ATOM   2902  C  CB  . VAL C  2 89  ? 4.606   179.715 13.432 1.00 29.89 ?  87  VAL C CB  1 
ATOM   2903  C  CG1 . VAL C  2 89  ? 4.447   180.516 14.728 1.00 29.74 ?  87  VAL C CG1 1 
ATOM   2904  C  CG2 . VAL C  2 89  ? 5.592   180.389 12.468 1.00 30.44 ?  87  VAL C CG2 1 
ATOM   2905  N  N   . THR C  2 90  ? 4.204   176.978 11.941 1.00 31.08 ?  88  THR C N   1 
ATOM   2906  C  CA  . THR C  2 90  ? 4.241   176.014 10.845 1.00 32.12 ?  88  THR C CA  1 
ATOM   2907  C  C   . THR C  2 90  ? 3.569   176.594 9.614  1.00 31.01 ?  88  THR C C   1 
ATOM   2908  O  O   . THR C  2 90  ? 2.370   176.890 9.640  1.00 33.41 ?  88  THR C O   1 
ATOM   2909  C  CB  . THR C  2 90  ? 3.548   174.702 11.229 1.00 31.09 ?  88  THR C CB  1 
ATOM   2910  O  OG1 . THR C  2 90  ? 4.288   174.074 12.279 1.00 39.36 ?  88  THR C OG1 1 
ATOM   2911  C  CG2 . THR C  2 90  ? 3.513   173.760 10.011 1.00 42.79 ?  88  THR C CG2 1 
ATOM   2912  N  N   . ALA C  2 91  ? 4.326   176.718 8.529  1.00 31.05 ?  89  ALA C N   1 
ATOM   2913  C  CA  . ALA C  2 91  ? 3.767   177.146 7.258  1.00 33.49 ?  89  ALA C CA  1 
ATOM   2914  C  C   . ALA C  2 91  ? 3.338   175.923 6.463  1.00 32.74 ?  89  ALA C C   1 
ATOM   2915  O  O   . ALA C  2 91  ? 4.081   174.942 6.380  1.00 35.40 ?  89  ALA C O   1 
ATOM   2916  C  CB  . ALA C  2 91  ? 4.784   177.968 6.466  1.00 31.33 ?  89  ALA C CB  1 
ATOM   2917  N  N   . ASP C  2 92  ? 2.137   175.987 5.899  1.00 37.20 ?  90  ASP C N   1 
ATOM   2918  C  CA  . ASP C  2 92  ? 1.624   174.940 5.027  1.00 44.71 ?  90  ASP C CA  1 
ATOM   2919  C  C   . ASP C  2 92  ? 2.309   175.048 3.661  1.00 42.66 ?  90  ASP C C   1 
ATOM   2920  O  O   . ASP C  2 92  ? 3.251   175.820 3.463  1.00 39.66 ?  90  ASP C O   1 
ATOM   2921  C  CB  . ASP C  2 92  ? 0.101   175.016 4.940  1.00 39.42 ?  90  ASP C CB  1 
ATOM   2922  C  CG  . ASP C  2 92  ? -0.410  176.304 4.283  1.00 40.30 ?  90  ASP C CG  1 
ATOM   2923  O  OD1 . ASP C  2 92  ? 0.319   176.942 3.486  1.00 42.51 ?  90  ASP C OD1 1 
ATOM   2924  O  OD2 . ASP C  2 92  ? -1.581  176.666 4.544  1.00 43.24 ?  90  ASP C OD2 1 
ATOM   2925  N  N   . LYS C  2 93  ? 1.823   174.273 2.687  1.00 45.28 ?  91  LYS C N   1 
ATOM   2926  C  CA  . LYS C  2 93  ? 2.459   174.262 1.374  1.00 41.30 ?  91  LYS C CA  1 
ATOM   2927  C  C   . LYS C  2 93  ? 2.198   175.546 0.604  1.00 42.03 ?  91  LYS C C   1 
ATOM   2928  O  O   . LYS C  2 93  ? 2.964   175.878 -0.308 1.00 40.80 ?  91  LYS C O   1 
ATOM   2929  C  CB  . LYS C  2 93  ? 1.991   173.039 0.571  1.00 42.49 ?  91  LYS C CB  1 
ATOM   2930  C  CG  . LYS C  2 93  ? 0.486   172.890 0.436  1.00 48.51 ?  91  LYS C CG  1 
ATOM   2931  C  CD  . LYS C  2 93  ? -0.032  173.658 -0.789 1.00 57.31 ?  91  LYS C CD  1 
ATOM   2932  C  CE  . LYS C  2 93  ? -1.267  173.018 -1.437 1.00 61.39 ?  91  LYS C CE  1 
ATOM   2933  N  NZ  . LYS C  2 93  ? -1.406  173.467 -2.869 1.00 56.30 ?  91  LYS C NZ  1 
ATOM   2934  N  N   . ASP C  2 94  ? 1.145   176.278 0.955  1.00 39.76 ?  92  ASP C N   1 
ATOM   2935  C  CA  . ASP C  2 94  ? 0.890   177.580 0.364  1.00 39.32 ?  92  ASP C CA  1 
ATOM   2936  C  C   . ASP C  2 94  ? 1.706   178.705 0.999  1.00 39.61 ?  92  ASP C C   1 
ATOM   2937  O  O   . ASP C  2 94  ? 1.541   179.859 0.598  1.00 38.92 ?  92  ASP C O   1 
ATOM   2938  C  CB  . ASP C  2 94  ? -0.593  177.907 0.479  1.00 41.25 ?  92  ASP C CB  1 
ATOM   2939  C  CG  . ASP C  2 94  ? -1.450  176.991 -0.358 1.00 56.10 ?  92  ASP C CG  1 
ATOM   2940  O  OD1 . ASP C  2 94  ? -1.000  176.606 -1.466 1.00 49.93 ?  92  ASP C OD1 1 
ATOM   2941  O  OD2 . ASP C  2 94  ? -2.567  176.656 0.106  1.00 62.18 ?  92  ASP C OD2 1 
ATOM   2942  N  N   . GLY C  2 95  ? 2.566   178.416 1.967  1.00 34.39 ?  93  GLY C N   1 
ATOM   2943  C  CA  . GLY C  2 95  ? 3.374   179.453 2.584  1.00 38.16 ?  93  GLY C CA  1 
ATOM   2944  C  C   . GLY C  2 95  ? 2.741   180.136 3.777  1.00 37.82 ?  93  GLY C C   1 
ATOM   2945  O  O   . GLY C  2 95  ? 3.296   181.125 4.273  1.00 34.28 ?  93  GLY C O   1 
ATOM   2946  N  N   . VAL C  2 96  ? 1.616   179.624 4.267  1.00 34.39 ?  94  VAL C N   1 
ATOM   2947  C  CA  . VAL C  2 96  ? 0.789   180.296 5.257  1.00 34.41 ?  94  VAL C CA  1 
ATOM   2948  C  C   . VAL C  2 96  ? 0.902   179.558 6.582  1.00 39.44 ?  94  VAL C C   1 
ATOM   2949  O  O   . VAL C  2 96  ? 0.738   178.333 6.638  1.00 36.27 ?  94  VAL C O   1 
ATOM   2950  C  CB  . VAL C  2 96  ? -0.674  180.359 4.804  1.00 39.17 ?  94  VAL C CB  1 
ATOM   2951  C  CG1 . VAL C  2 96  ? -1.538  180.956 5.914  1.00 40.52 ?  94  VAL C CG1 1 
ATOM   2952  C  CG2 . VAL C  2 96  ? -0.782  181.152 3.514  1.00 38.41 ?  94  VAL C CG2 1 
ATOM   2953  N  N   . ALA C  2 97  ? 1.157   180.312 7.648  1.00 38.24 ?  95  ALA C N   1 
ATOM   2954  C  CA  . ALA C  2 97  ? 1.237   179.786 9.004  1.00 35.63 ?  95  ALA C CA  1 
ATOM   2955  C  C   . ALA C  2 97  ? 0.086   180.362 9.821  1.00 38.18 ?  95  ALA C C   1 
ATOM   2956  O  O   . ALA C  2 97  ? 0.011   181.582 10.016 1.00 32.66 ?  95  ALA C O   1 
ATOM   2957  C  CB  . ALA C  2 97  ? 2.579   180.138 9.641  1.00 32.02 ?  95  ALA C CB  1 
ATOM   2958  N  N   . ASP C  2 98  ? -0.806  179.483 10.286 1.00 33.66 ?  96  ASP C N   1 
ATOM   2959  C  CA  . ASP C  2 98  ? -1.893  179.849 11.194 1.00 38.09 ?  96  ASP C CA  1 
ATOM   2960  C  C   . ASP C  2 98  ? -1.360  179.785 12.618 1.00 34.38 ?  96  ASP C C   1 
ATOM   2961  O  O   . ASP C  2 98  ? -1.133  178.697 13.157 1.00 35.06 ?  96  ASP C O   1 
ATOM   2962  C  CB  . ASP C  2 98  ? -3.097  178.927 11.025 1.00 43.75 ?  96  ASP C CB  1 
ATOM   2963  C  CG  . ASP C  2 98  ? -3.658  178.947 9.604  1.00 58.54 ?  96  ASP C CG  1 
ATOM   2964  O  OD1 . ASP C  2 98  ? -4.114  177.880 9.123  1.00 60.47 ?  96  ASP C OD1 1 
ATOM   2965  O  OD2 . ASP C  2 98  ? -3.647  180.033 8.972  1.00 60.56 ?  96  ASP C OD2 1 
ATOM   2966  N  N   . VAL C  2 99  ? -1.147  180.943 13.223 1.00 32.04 ?  97  VAL C N   1 
ATOM   2967  C  CA  . VAL C  2 99  ? -0.523  181.014 14.534 1.00 27.58 ?  97  VAL C CA  1 
ATOM   2968  C  C   . VAL C  2 99  ? -1.617  180.911 15.579 1.00 30.36 ?  97  VAL C C   1 
ATOM   2969  O  O   . VAL C  2 99  ? -2.643  181.605 15.498 1.00 30.18 ?  97  VAL C O   1 
ATOM   2970  C  CB  . VAL C  2 99  ? 0.291   182.307 14.690 1.00 34.36 ?  97  VAL C CB  1 
ATOM   2971  C  CG1 . VAL C  2 99  ? 0.890   182.398 16.078 1.00 26.95 ?  97  VAL C CG1 1 
ATOM   2972  C  CG2 . VAL C  2 99  ? 1.394   182.344 13.631 1.00 31.20 ?  97  VAL C CG2 1 
ATOM   2973  N  N   . SER C  2 100 ? -1.417  180.019 16.541 1.00 32.97 ?  98  SER C N   1 
ATOM   2974  C  CA  . SER C  2 100 ? -2.378  179.841 17.624 1.00 36.68 ?  98  SER C CA  1 
ATOM   2975  C  C   . SER C  2 100 ? -1.590  179.308 18.812 1.00 39.77 ?  98  SER C C   1 
ATOM   2976  O  O   . SER C  2 100 ? -1.211  178.133 18.848 1.00 40.38 ?  98  SER C O   1 
ATOM   2977  C  CB  . SER C  2 100 ? -3.508  178.907 17.233 1.00 42.56 ?  98  SER C CB  1 
ATOM   2978  O  OG  . SER C  2 100 ? -4.351  178.706 18.350 1.00 47.78 ?  98  SER C OG  1 
ATOM   2979  N  N   . ILE C  2 101 ? -1.321  180.194 19.751 1.00 32.30 ?  99  ILE C N   1 
ATOM   2980  C  CA  . ILE C  2 101 ? -0.436  179.942 20.877 1.00 31.66 ?  99  ILE C CA  1 
ATOM   2981  C  C   . ILE C  2 101 ? -1.143  180.468 22.112 1.00 34.74 ?  99  ILE C C   1 
ATOM   2982  O  O   . ILE C  2 101 ? -1.820  181.495 22.045 1.00 28.85 ?  99  ILE C O   1 
ATOM   2983  C  CB  . ILE C  2 101 ? 0.922   180.654 20.679 1.00 33.50 ?  99  ILE C CB  1 
ATOM   2984  C  CG1 . ILE C  2 101 ? 1.640   180.106 19.449 1.00 35.33 ?  99  ILE C CG1 1 
ATOM   2985  C  CG2 . ILE C  2 101 ? 1.805   180.585 21.917 1.00 33.03 ?  99  ILE C CG2 1 
ATOM   2986  C  CD1 . ILE C  2 101 ? 2.892   180.881 19.105 1.00 39.64 ?  99  ILE C CD1 1 
ATOM   2987  N  N   . GLU C  2 102 ? -1.030  179.747 23.223 1.00 31.22 ?  100 GLU C N   1 
ATOM   2988  C  CA  . GLU C  2 102 ? -1.343  180.296 24.529 1.00 33.81 ?  100 GLU C CA  1 
ATOM   2989  C  C   . GLU C  2 102 ? -0.072  180.218 25.340 1.00 30.07 ?  100 GLU C C   1 
ATOM   2990  O  O   . GLU C  2 102 ? 0.575   179.169 25.364 1.00 34.95 ?  100 GLU C O   1 
ATOM   2991  C  CB  . GLU C  2 102 ? -2.477  179.540 25.217 1.00 38.69 ?  100 GLU C CB  1 
ATOM   2992  C  CG  . GLU C  2 102 ? -3.011  180.291 26.417 1.00 45.80 ?  100 GLU C CG  1 
ATOM   2993  C  CD  . GLU C  2 102 ? -3.994  179.466 27.234 1.00 52.48 ?  100 GLU C CD  1 
ATOM   2994  O  OE1 . GLU C  2 102 ? -3.533  178.591 28.008 1.00 59.96 ?  100 GLU C OE1 1 
ATOM   2995  O  OE2 . GLU C  2 102 ? -5.216  179.700 27.106 1.00 56.28 ?  100 GLU C OE2 1 
ATOM   2996  N  N   . ASP C  2 103 ? 0.325   181.329 25.949 1.00 25.50 ?  101 ASP C N   1 
ATOM   2997  C  CA  . ASP C  2 103 ? 1.593   181.350 26.663 1.00 28.64 ?  101 ASP C CA  1 
ATOM   2998  C  C   . ASP C  2 103 ? 1.450   182.019 28.022 1.00 33.43 ?  101 ASP C C   1 
ATOM   2999  O  O   . ASP C  2 103 ? 0.812   183.072 28.155 1.00 30.21 ?  101 ASP C O   1 
ATOM   3000  C  CB  . ASP C  2 103 ? 2.672   182.066 25.853 1.00 29.59 ?  101 ASP C CB  1 
ATOM   3001  C  CG  . ASP C  2 103 ? 4.073   181.832 26.411 1.00 32.50 ?  101 ASP C CG  1 
ATOM   3002  O  OD1 . ASP C  2 103 ? 4.635   180.733 26.188 1.00 33.73 ?  101 ASP C OD1 1 
ATOM   3003  O  OD2 . ASP C  2 103 ? 4.608   182.748 27.083 1.00 30.01 ?  101 ASP C OD2 1 
ATOM   3004  N  N   . SER C  2 104 ? 2.101   181.421 29.013 1.00 31.70 ?  102 SER C N   1 
ATOM   3005  C  CA  . SER C  2 104 ? 2.002   181.829 30.403 1.00 33.53 ?  102 SER C CA  1 
ATOM   3006  C  C   . SER C  2 104 ? 3.224   182.581 30.896 1.00 32.74 ?  102 SER C C   1 
ATOM   3007  O  O   . SER C  2 104 ? 3.239   182.997 32.056 1.00 31.39 ?  102 SER C O   1 
ATOM   3008  C  CB  . SER C  2 104 ? 1.795   180.594 31.291 1.00 35.42 ?  102 SER C CB  1 
ATOM   3009  O  OG  . SER C  2 104 ? 0.410   180.363 31.473 1.00 51.15 ?  102 SER C OG  1 
ATOM   3010  N  N   . VAL C  2 105 ? 4.255   182.737 30.074 1.00 32.11 ?  103 VAL C N   1 
ATOM   3011  C  CA  . VAL C  2 105 ? 5.468   183.434 30.486 1.00 25.49 ?  103 VAL C CA  1 
ATOM   3012  C  C   . VAL C  2 105 ? 5.484   184.868 29.985 1.00 33.21 ?  103 VAL C C   1 
ATOM   3013  O  O   . VAL C  2 105 ? 5.816   185.781 30.736 1.00 32.22 ?  103 VAL C O   1 
ATOM   3014  C  CB  . VAL C  2 105 ? 6.723   182.657 30.028 1.00 31.12 ?  103 VAL C CB  1 
ATOM   3015  C  CG1 . VAL C  2 105 ? 7.978   183.422 30.394 1.00 28.86 ?  103 VAL C CG1 1 
ATOM   3016  C  CG2 . VAL C  2 105 ? 6.735   181.279 30.680 1.00 33.10 ?  103 VAL C CG2 1 
ATOM   3017  N  N   . ILE C  2 106 ? 5.137   185.090 28.708 1.00 29.93 ?  104 ILE C N   1 
ATOM   3018  C  CA  . ILE C  2 106 ? 5.018   186.477 28.228 1.00 26.98 ?  104 ILE C CA  1 
ATOM   3019  C  C   . ILE C  2 106 ? 3.856   187.161 28.936 1.00 26.49 ?  104 ILE C C   1 
ATOM   3020  O  O   . ILE C  2 106 ? 2.915   186.524 29.410 1.00 23.88 ?  104 ILE C O   1 
ATOM   3021  C  CB  . ILE C  2 106 ? 4.826   186.544 26.704 1.00 27.53 ?  104 ILE C CB  1 
ATOM   3022  C  CG1 . ILE C  2 106 ? 3.577   185.764 26.284 1.00 26.34 ?  104 ILE C CG1 1 
ATOM   3023  C  CG2 . ILE C  2 106 ? 6.045   186.015 25.952 1.00 26.46 ?  104 ILE C CG2 1 
ATOM   3024  C  CD1 . ILE C  2 106 ? 3.220   185.967 24.807 1.00 26.14 ?  104 ILE C CD1 1 
ATOM   3025  N  N   . SER C  2 107 ? 3.907   188.487 28.980 1.00 22.22 ?  105 SER C N   1 
ATOM   3026  C  CA  . SER C  2 107 ? 2.802   189.246 29.528 1.00 26.72 ?  105 SER C CA  1 
ATOM   3027  C  C   . SER C  2 107 ? 2.645   190.536 28.745 1.00 27.56 ?  105 SER C C   1 
ATOM   3028  O  O   . SER C  2 107 ? 3.581   191.010 28.102 1.00 28.57 ?  105 SER C O   1 
ATOM   3029  C  CB  . SER C  2 107 ? 3.008   189.567 31.020 1.00 27.25 ?  105 SER C CB  1 
ATOM   3030  O  OG  . SER C  2 107 ? 1.791   190.059 31.584 1.00 29.27 ?  105 SER C OG  1 
ATOM   3031  N  N   . LEU C  2 108 ? 1.440   191.090 28.795 1.00 27.39 ?  106 LEU C N   1 
ATOM   3032  C  CA  . LEU C  2 108 ? 1.174   192.405 28.244 1.00 29.46 ?  106 LEU C CA  1 
ATOM   3033  C  C   . LEU C  2 108 ? 1.307   193.515 29.287 1.00 31.43 ?  106 LEU C C   1 
ATOM   3034  O  O   . LEU C  2 108 ? 1.025   194.663 28.964 1.00 28.83 ?  106 LEU C O   1 
ATOM   3035  C  CB  . LEU C  2 108 ? -0.213  192.437 27.598 1.00 22.89 ?  106 LEU C CB  1 
ATOM   3036  C  CG  . LEU C  2 108 ? -0.422  191.386 26.489 1.00 27.97 ?  106 LEU C CG  1 
ATOM   3037  C  CD1 . LEU C  2 108 ? -1.677  191.667 25.676 1.00 28.59 ?  106 LEU C CD1 1 
ATOM   3038  C  CD2 . LEU C  2 108 ? 0.770   191.323 25.547 1.00 22.81 ?  106 LEU C CD2 1 
ATOM   3039  N  N   . SER C  2 109 ? 1.757   193.202 30.509 1.00 29.53 ?  107 SER C N   1 
ATOM   3040  C  CA  . SER C  2 109 ? 1.990   194.202 31.551 1.00 33.99 ?  107 SER C CA  1 
ATOM   3041  C  C   . SER C  2 109 ? 3.046   193.670 32.512 1.00 31.72 ?  107 SER C C   1 
ATOM   3042  O  O   . SER C  2 109 ? 3.375   192.484 32.486 1.00 31.08 ?  107 SER C O   1 
ATOM   3043  C  CB  . SER C  2 109 ? 0.701   194.546 32.306 1.00 35.88 ?  107 SER C CB  1 
ATOM   3044  O  OG  . SER C  2 109 ? 0.003   193.379 32.696 1.00 37.32 ?  107 SER C OG  1 
ATOM   3045  N  N   . GLY C  2 110 ? 3.608   194.562 33.346 1.00 34.56 ?  108 GLY C N   1 
ATOM   3046  C  CA  . GLY C  2 110 ? 4.659   194.156 34.284 1.00 37.92 ?  108 GLY C CA  1 
ATOM   3047  C  C   . GLY C  2 110 ? 6.053   194.092 33.672 1.00 46.52 ?  108 GLY C C   1 
ATOM   3048  O  O   . GLY C  2 110 ? 6.328   194.687 32.642 1.00 42.55 ?  108 GLY C O   1 
ATOM   3049  N  N   . ASP C  2 111 ? 6.939   193.326 34.323 1.00 50.25 ?  109 ASP C N   1 
ATOM   3050  C  CA  . ASP C  2 111 ? 8.346   193.247 33.915 1.00 47.82 ?  109 ASP C CA  1 
ATOM   3051  C  C   . ASP C  2 111 ? 8.583   192.262 32.771 1.00 47.18 ?  109 ASP C C   1 
ATOM   3052  O  O   . ASP C  2 111 ? 9.539   192.425 32.005 1.00 46.41 ?  109 ASP C O   1 
ATOM   3053  C  CB  . ASP C  2 111 ? 9.237   192.842 35.105 1.00 56.86 ?  109 ASP C CB  1 
ATOM   3054  C  CG  . ASP C  2 111 ? 9.330   193.934 36.195 1.00 64.76 ?  109 ASP C CG  1 
ATOM   3055  O  OD1 . ASP C  2 111 ? 8.998   195.117 35.917 1.00 63.51 ?  109 ASP C OD1 1 
ATOM   3056  O  OD2 . ASP C  2 111 ? 9.749   193.601 37.330 1.00 65.86 ?  109 ASP C OD2 1 
ATOM   3057  N  N   . HIS C  2 112 ? 7.776   191.220 32.657 1.00 46.48 ?  110 HIS C N   1 
ATOM   3058  C  CA  . HIS C  2 112 ? 7.800   190.396 31.454 1.00 47.55 ?  110 HIS C CA  1 
ATOM   3059  C  C   . HIS C  2 112 ? 7.035   191.018 30.296 1.00 38.29 ?  110 HIS C C   1 
ATOM   3060  O  O   . HIS C  2 112 ? 6.660   190.275 29.369 1.00 40.88 ?  110 HIS C O   1 
ATOM   3061  C  CB  . HIS C  2 112 ? 7.208   189.008 31.729 1.00 45.78 ?  110 HIS C CB  1 
ATOM   3062  C  CG  . HIS C  2 112 ? 8.106   188.105 32.511 1.00 52.23 ?  110 HIS C CG  1 
ATOM   3063  N  ND1 . HIS C  2 112 ? 7.805   186.777 32.736 1.00 53.05 ?  110 HIS C ND1 1 
ATOM   3064  C  CD2 . HIS C  2 112 ? 9.293   188.335 33.121 1.00 44.74 ?  110 HIS C CD2 1 
ATOM   3065  C  CE1 . HIS C  2 112 ? 8.772   186.227 33.450 1.00 49.42 ?  110 HIS C CE1 1 
ATOM   3066  N  NE2 . HIS C  2 112 ? 9.686   187.151 33.696 1.00 54.85 ?  110 HIS C NE2 1 
ATOM   3067  N  N   . CYS C  2 113 ? 6.749   192.319 30.338 1.00 35.89 ?  111 CYS C N   1 
ATOM   3068  C  CA  . CYS C  2 113 ? 5.844   192.907 29.355 1.00 34.36 ?  111 CYS C CA  1 
ATOM   3069  C  C   . CYS C  2 113 ? 6.513   192.962 27.985 1.00 30.57 ?  111 CYS C C   1 
ATOM   3070  O  O   . CYS C  2 113 ? 7.665   193.388 27.860 1.00 24.33 ?  111 CYS C O   1 
ATOM   3071  C  CB  . CYS C  2 113 ? 5.433   194.296 29.815 1.00 33.86 ?  111 CYS C CB  1 
ATOM   3072  S  SG  . CYS C  2 113 ? 4.557   195.324 28.644 1.00 38.23 ?  111 CYS C SG  1 
ATOM   3073  N  N   . ILE C  2 114 ? 5.785   192.537 26.950 1.00 27.24 ?  112 ILE C N   1 
ATOM   3074  C  CA  . ILE C  2 114 ? 6.357   192.525 25.615 1.00 27.17 ?  112 ILE C CA  1 
ATOM   3075  C  C   . ILE C  2 114 ? 5.902   193.704 24.760 1.00 27.43 ?  112 ILE C C   1 
ATOM   3076  O  O   . ILE C  2 114 ? 6.350   193.818 23.616 1.00 25.99 ?  112 ILE C O   1 
ATOM   3077  C  CB  . ILE C  2 114 ? 6.068   191.182 24.921 1.00 26.52 ?  112 ILE C CB  1 
ATOM   3078  C  CG1 . ILE C  2 114 ? 4.569   190.987 24.744 1.00 20.34 ?  112 ILE C CG1 1 
ATOM   3079  C  CG2 . ILE C  2 114 ? 6.684   190.027 25.749 1.00 24.37 ?  112 ILE C CG2 1 
ATOM   3080  C  CD1 . ILE C  2 114 ? 4.204   189.780 23.950 1.00 20.34 ?  112 ILE C CD1 1 
ATOM   3081  N  N   . ILE C  2 115 ? 5.060   194.602 25.286 1.00 29.59 ?  113 ILE C N   1 
ATOM   3082  C  CA  . ILE C  2 115 ? 4.655   195.784 24.525 1.00 28.22 ?  113 ILE C CA  1 
ATOM   3083  C  C   . ILE C  2 115 ? 5.879   196.612 24.167 1.00 28.61 ?  113 ILE C C   1 
ATOM   3084  O  O   . ILE C  2 115 ? 6.745   196.860 25.009 1.00 22.20 ?  113 ILE C O   1 
ATOM   3085  C  CB  . ILE C  2 115 ? 3.670   196.644 25.331 1.00 34.17 ?  113 ILE C CB  1 
ATOM   3086  C  CG1 . ILE C  2 115 ? 2.474   195.823 25.793 1.00 35.33 ?  113 ILE C CG1 1 
ATOM   3087  C  CG2 . ILE C  2 115 ? 3.241   197.876 24.524 1.00 27.71 ?  113 ILE C CG2 1 
ATOM   3088  C  CD1 . ILE C  2 115 ? 1.579   195.447 24.707 1.00 33.86 ?  113 ILE C CD1 1 
ATOM   3089  N  N   . GLY C  2 116 ? 5.966   197.038 22.912 1.00 23.89 ?  114 GLY C N   1 
ATOM   3090  C  CA  . GLY C  2 116 ? 7.107   197.825 22.505 1.00 23.93 ?  114 GLY C CA  1 
ATOM   3091  C  C   . GLY C  2 116 ? 8.371   197.039 22.233 1.00 23.87 ?  114 GLY C C   1 
ATOM   3092  O  O   . GLY C  2 116 ? 9.421   197.649 22.012 1.00 23.29 ?  114 GLY C O   1 
ATOM   3093  N  N   . ARG C  2 117 ? 8.323   195.710 22.277 1.00 24.16 ?  115 ARG C N   1 
ATOM   3094  C  CA  . ARG C  2 117 ? 9.433   194.882 21.825 1.00 23.57 ?  115 ARG C CA  1 
ATOM   3095  C  C   . ARG C  2 117 ? 9.115   194.410 20.414 1.00 22.18 ?  115 ARG C C   1 
ATOM   3096  O  O   . ARG C  2 117 ? 8.105   194.807 19.838 1.00 24.46 ?  115 ARG C O   1 
ATOM   3097  C  CB  . ARG C  2 117 ? 9.671   193.748 22.830 1.00 22.51 ?  115 ARG C CB  1 
ATOM   3098  C  CG  . ARG C  2 117 ? 9.796   194.358 24.245 1.00 25.64 ?  115 ARG C CG  1 
ATOM   3099  C  CD  . ARG C  2 117 ? 10.559  193.519 25.226 1.00 27.91 ?  115 ARG C CD  1 
ATOM   3100  N  NE  . ARG C  2 117 ? 10.579  194.144 26.548 1.00 27.01 ?  115 ARG C NE  1 
ATOM   3101  C  CZ  . ARG C  2 117 ? 11.591  194.861 27.025 1.00 30.67 ?  115 ARG C CZ  1 
ATOM   3102  N  NH1 . ARG C  2 117 ? 12.682  195.088 26.306 1.00 23.85 ?  115 ARG C NH1 1 
ATOM   3103  N  NH2 . ARG C  2 117 ? 11.515  195.349 28.262 1.00 27.97 ?  115 ARG C NH2 1 
ATOM   3104  N  N   . THR C  2 118 ? 9.973   193.571 19.840 1.00 22.71 ?  116 THR C N   1 
ATOM   3105  C  CA  . THR C  2 118 ? 9.802   193.139 18.456 1.00 24.20 ?  116 THR C CA  1 
ATOM   3106  C  C   . THR C  2 118 ? 9.497   191.649 18.369 1.00 25.69 ?  116 THR C C   1 
ATOM   3107  O  O   . THR C  2 118 ? 10.233  190.823 18.916 1.00 28.57 ?  116 THR C O   1 
ATOM   3108  C  CB  . THR C  2 118 ? 11.040  193.463 17.628 1.00 27.53 ?  116 THR C CB  1 
ATOM   3109  O  OG1 . THR C  2 118 ? 11.260  194.882 17.639 1.00 28.58 ?  116 THR C OG1 1 
ATOM   3110  C  CG2 . THR C  2 118 ? 10.855  193.014 16.190 1.00 26.04 ?  116 THR C CG2 1 
ATOM   3111  N  N   . LEU C  2 119 ? 8.421   191.309 17.669 1.00 25.21 ?  117 LEU C N   1 
ATOM   3112  C  CA  . LEU C  2 119 ? 8.131   189.922 17.316 1.00 24.94 ?  117 LEU C CA  1 
ATOM   3113  C  C   . LEU C  2 119 ? 8.840   189.621 16.006 1.00 27.53 ?  117 LEU C C   1 
ATOM   3114  O  O   . LEU C  2 119 ? 8.744   190.408 15.068 1.00 23.87 ?  117 LEU C O   1 
ATOM   3115  C  CB  . LEU C  2 119 ? 6.621   189.718 17.182 1.00 21.23 ?  117 LEU C CB  1 
ATOM   3116  C  CG  . LEU C  2 119 ? 6.120   188.312 16.897 1.00 26.90 ?  117 LEU C CG  1 
ATOM   3117  C  CD1 . LEU C  2 119 ? 6.427   187.365 18.078 1.00 27.67 ?  117 LEU C CD1 1 
ATOM   3118  C  CD2 . LEU C  2 119 ? 4.644   188.381 16.628 1.00 24.54 ?  117 LEU C CD2 1 
ATOM   3119  N  N   . VAL C  2 120 ? 9.576   188.512 15.944 1.00 27.01 ?  118 VAL C N   1 
ATOM   3120  C  CA  . VAL C  2 120 ? 10.354  188.170 14.752 1.00 28.20 ?  118 VAL C CA  1 
ATOM   3121  C  C   . VAL C  2 120 ? 10.018  186.745 14.321 1.00 29.02 ?  118 VAL C C   1 
ATOM   3122  O  O   . VAL C  2 120 ? 10.011  185.823 15.149 1.00 30.85 ?  118 VAL C O   1 
ATOM   3123  C  CB  . VAL C  2 120 ? 11.869  188.296 15.004 1.00 23.62 ?  118 VAL C CB  1 
ATOM   3124  C  CG1 . VAL C  2 120 ? 12.649  187.735 13.815 1.00 28.93 ?  118 VAL C CG1 1 
ATOM   3125  C  CG2 . VAL C  2 120 ? 12.261  189.725 15.277 1.00 23.18 ?  118 VAL C CG2 1 
ATOM   3126  N  N   . VAL C  2 121 ? 9.761   186.551 13.033 1.00 25.49 ?  119 VAL C N   1 
ATOM   3127  C  CA  . VAL C  2 121 ? 9.683   185.209 12.469 1.00 25.85 ?  119 VAL C CA  1 
ATOM   3128  C  C   . VAL C  2 121 ? 10.969  184.928 11.698 1.00 29.33 ?  119 VAL C C   1 
ATOM   3129  O  O   . VAL C  2 121 ? 11.442  185.762 10.907 1.00 29.20 ?  119 VAL C O   1 
ATOM   3130  C  CB  . VAL C  2 121 ? 8.428   185.013 11.600 1.00 25.68 ?  119 VAL C CB  1 
ATOM   3131  C  CG1 . VAL C  2 121 ? 8.374   185.984 10.406 1.00 22.60 ?  119 VAL C CG1 1 
ATOM   3132  C  CG2 . VAL C  2 121 ? 8.350   183.577 11.141 1.00 27.90 ?  119 VAL C CG2 1 
ATOM   3133  N  N   . HIS C  2 122 ? 11.552  183.766 11.953 1.00 31.12 ?  120 HIS C N   1 
ATOM   3134  C  CA  . HIS C  2 122 ? 12.896  183.445 11.500 1.00 30.76 ?  120 HIS C CA  1 
ATOM   3135  C  C   . HIS C  2 122 ? 12.882  182.477 10.318 1.00 29.59 ?  120 HIS C C   1 
ATOM   3136  O  O   . HIS C  2 122 ? 11.876  181.846 9.977  1.00 28.85 ?  120 HIS C O   1 
ATOM   3137  C  CB  . HIS C  2 122 ? 13.726  182.838 12.633 1.00 24.37 ?  120 HIS C CB  1 
ATOM   3138  C  CG  . HIS C  2 122 ? 14.144  183.816 13.685 1.00 29.32 ?  120 HIS C CG  1 
ATOM   3139  N  ND1 . HIS C  2 122 ? 15.422  184.326 13.768 1.00 32.37 ?  120 HIS C ND1 1 
ATOM   3140  C  CD2 . HIS C  2 122 ? 13.456  184.354 14.720 1.00 29.38 ?  120 HIS C CD2 1 
ATOM   3141  C  CE1 . HIS C  2 122 ? 15.502  185.143 14.802 1.00 32.36 ?  120 HIS C CE1 1 
ATOM   3142  N  NE2 . HIS C  2 122 ? 14.325  185.175 15.399 1.00 31.35 ?  120 HIS C NE2 1 
ATOM   3143  N  N   . GLU C  2 123 ? 14.060  182.350 9.716  1.00 30.31 ?  121 GLU C N   1 
ATOM   3144  C  CA  . GLU C  2 123 ? 14.204  181.633 8.456  1.00 31.76 ?  121 GLU C CA  1 
ATOM   3145  C  C   . GLU C  2 123 ? 14.043  180.122 8.627  1.00 32.48 ?  121 GLU C C   1 
ATOM   3146  O  O   . GLU C  2 123 ? 13.390  179.470 7.798  1.00 30.12 ?  121 GLU C O   1 
ATOM   3147  C  CB  . GLU C  2 123 ? 15.557  181.994 7.870  1.00 37.41 ?  121 GLU C CB  1 
ATOM   3148  C  CG  . GLU C  2 123 ? 16.188  180.943 7.036  1.00 49.53 ?  121 GLU C CG  1 
ATOM   3149  C  CD  . GLU C  2 123 ? 17.594  181.327 6.694  1.00 51.38 ?  121 GLU C CD  1 
ATOM   3150  O  OE1 . GLU C  2 123 ? 18.408  181.483 7.643  1.00 46.12 ?  121 GLU C OE1 1 
ATOM   3151  O  OE2 . GLU C  2 123 ? 17.870  181.492 5.486  1.00 66.67 ?  121 GLU C OE2 1 
ATOM   3152  N  N   . LYS C  2 124 ? 14.595  179.559 9.708  1.00 35.21 ?  122 LYS C N   1 
ATOM   3153  C  CA  . LYS C  2 124 ? 14.680  178.118 9.956  1.00 36.75 ?  122 LYS C CA  1 
ATOM   3154  C  C   . LYS C  2 124 ? 13.913  177.727 11.217 1.00 37.53 ?  122 LYS C C   1 
ATOM   3155  O  O   . LYS C  2 124 ? 13.541  178.564 12.043 1.00 34.19 ?  122 LYS C O   1 
ATOM   3156  C  CB  . LYS C  2 124 ? 16.137  177.670 10.150 1.00 34.57 ?  122 LYS C CB  1 
ATOM   3157  C  CG  . LYS C  2 124 ? 17.040  177.724 8.934  1.00 46.51 ?  122 LYS C CG  1 
ATOM   3158  C  CD  . LYS C  2 124 ? 18.504  177.670 9.390  1.00 49.36 ?  122 LYS C CD  1 
ATOM   3159  C  CE  . LYS C  2 124 ? 19.464  178.188 8.317  1.00 64.29 ?  122 LYS C CE  1 
ATOM   3160  N  NZ  . LYS C  2 124 ? 20.436  177.131 7.868  1.00 74.10 ?  122 LYS C NZ  1 
ATOM   3161  N  N   . ALA C  2 125 ? 13.752  176.416 11.397 1.00 36.30 ?  123 ALA C N   1 
ATOM   3162  C  CA  . ALA C  2 125 ? 13.127  175.892 12.605 1.00 37.37 ?  123 ALA C CA  1 
ATOM   3163  C  C   . ALA C  2 125 ? 13.963  176.233 13.830 1.00 34.85 ?  123 ALA C C   1 
ATOM   3164  O  O   . ALA C  2 125 ? 15.195  176.260 13.782 1.00 32.40 ?  123 ALA C O   1 
ATOM   3165  C  CB  . ALA C  2 125 ? 12.945  174.373 12.504 1.00 38.98 ?  123 ALA C CB  1 
ATOM   3166  N  N   . ASP C  2 126 ? 13.270  176.552 14.922 1.00 37.98 ?  124 ASP C N   1 
ATOM   3167  C  CA  . ASP C  2 126 ? 13.889  176.687 16.229 1.00 34.54 ?  124 ASP C CA  1 
ATOM   3168  C  C   . ASP C  2 126 ? 14.133  175.284 16.780 1.00 38.44 ?  124 ASP C C   1 
ATOM   3169  O  O   . ASP C  2 126 ? 13.207  174.471 16.820 1.00 33.48 ?  124 ASP C O   1 
ATOM   3170  C  CB  . ASP C  2 126 ? 12.945  177.474 17.145 1.00 37.82 ?  124 ASP C CB  1 
ATOM   3171  C  CG  . ASP C  2 126 ? 13.527  177.770 18.518 1.00 40.09 ?  124 ASP C CG  1 
ATOM   3172  O  OD1 . ASP C  2 126 ? 14.484  177.101 18.965 1.00 38.80 ?  124 ASP C OD1 1 
ATOM   3173  O  OD2 . ASP C  2 126 ? 12.999  178.704 19.157 1.00 41.09 ?  124 ASP C OD2 1 
ATOM   3174  N  N   . ASP C  2 127 ? 15.368  174.990 17.196 1.00 33.45 ?  125 ASP C N   1 
ATOM   3175  C  CA  . ASP C  2 127 ? 15.647  173.679 17.779 1.00 40.00 ?  125 ASP C CA  1 
ATOM   3176  C  C   . ASP C  2 127 ? 15.356  173.623 19.274 1.00 45.32 ?  125 ASP C C   1 
ATOM   3177  O  O   . ASP C  2 127 ? 15.764  172.657 19.938 1.00 42.39 ?  125 ASP C O   1 
ATOM   3178  C  CB  . ASP C  2 127 ? 17.092  173.227 17.492 1.00 35.27 ?  125 ASP C CB  1 
ATOM   3179  C  CG  . ASP C  2 127 ? 18.150  174.044 18.217 1.00 43.52 ?  125 ASP C CG  1 
ATOM   3180  O  OD1 . ASP C  2 127 ? 17.877  174.672 19.270 1.00 42.86 ?  125 ASP C OD1 1 
ATOM   3181  O  OD2 . ASP C  2 127 ? 19.303  174.023 17.718 1.00 42.59 ?  125 ASP C OD2 1 
ATOM   3182  N  N   . LEU C  2 128 ? 14.663  174.634 19.806 1.00 37.58 ?  126 LEU C N   1 
ATOM   3183  C  CA  . LEU C  2 128 ? 14.191  174.648 21.188 1.00 37.29 ?  126 LEU C CA  1 
ATOM   3184  C  C   . LEU C  2 128 ? 15.343  174.512 22.173 1.00 39.21 ?  126 LEU C C   1 
ATOM   3185  O  O   . LEU C  2 128 ? 15.152  174.090 23.311 1.00 43.73 ?  126 LEU C O   1 
ATOM   3186  C  CB  . LEU C  2 128 ? 13.137  173.566 21.432 1.00 36.57 ?  126 LEU C CB  1 
ATOM   3187  C  CG  . LEU C  2 128 ? 12.083  173.457 20.333 1.00 42.53 ?  126 LEU C CG  1 
ATOM   3188  C  CD1 . LEU C  2 128 ? 11.168  172.237 20.513 1.00 38.20 ?  126 LEU C CD1 1 
ATOM   3189  C  CD2 . LEU C  2 128 ? 11.279  174.746 20.261 1.00 40.86 ?  126 LEU C CD2 1 
ATOM   3190  N  N   . GLY C  2 129 ? 16.544  174.907 21.757 1.00 40.11 ?  127 GLY C N   1 
ATOM   3191  C  CA  . GLY C  2 129 ? 17.677  174.889 22.661 1.00 41.92 ?  127 GLY C CA  1 
ATOM   3192  C  C   . GLY C  2 129 ? 18.325  173.532 22.827 1.00 48.94 ?  127 GLY C C   1 
ATOM   3193  O  O   . GLY C  2 129 ? 19.228  173.393 23.661 1.00 49.21 ?  127 GLY C O   1 
ATOM   3194  N  N   . LYS C  2 130 ? 17.901  172.534 22.046 1.00 46.36 ?  128 LYS C N   1 
ATOM   3195  C  CA  . LYS C  2 130 ? 18.341  171.151 22.193 1.00 51.10 ?  128 LYS C CA  1 
ATOM   3196  C  C   . LYS C  2 130 ? 19.213  170.696 21.029 1.00 54.11 ?  128 LYS C C   1 
ATOM   3197  O  O   . LYS C  2 130 ? 19.199  169.519 20.662 1.00 52.22 ?  128 LYS C O   1 
ATOM   3198  C  CB  . LYS C  2 130 ? 17.134  170.223 22.330 1.00 48.24 ?  128 LYS C CB  1 
ATOM   3199  C  CG  . LYS C  2 130 ? 16.735  169.963 23.768 1.00 51.09 ?  128 LYS C CG  1 
ATOM   3200  C  CD  . LYS C  2 130 ? 15.795  171.022 24.304 1.00 53.23 ?  128 LYS C CD  1 
ATOM   3201  C  CE  . LYS C  2 130 ? 14.335  170.556 24.288 1.00 55.66 ?  128 LYS C CE  1 
ATOM   3202  N  NZ  . LYS C  2 130 ? 13.405  171.710 24.522 1.00 50.77 ?  128 LYS C NZ  1 
ATOM   3203  N  N   . GLY C  2 131 ? 19.965  171.621 20.429 1.00 52.80 ?  129 GLY C N   1 
ATOM   3204  C  CA  . GLY C  2 131 ? 20.832  171.292 19.315 1.00 50.00 ?  129 GLY C CA  1 
ATOM   3205  C  C   . GLY C  2 131 ? 22.243  170.907 19.695 1.00 54.68 ?  129 GLY C C   1 
ATOM   3206  O  O   . GLY C  2 131 ? 23.013  170.478 18.827 1.00 62.95 ?  129 GLY C O   1 
ATOM   3207  N  N   . GLY C  2 132 ? 22.612  171.064 20.963 1.00 47.54 ?  130 GLY C N   1 
ATOM   3208  C  CA  . GLY C  2 132 ? 23.929  170.656 21.416 1.00 52.44 ?  130 GLY C CA  1 
ATOM   3209  C  C   . GLY C  2 132 ? 25.071  171.484 20.872 1.00 57.42 ?  130 GLY C C   1 
ATOM   3210  O  O   . GLY C  2 132 ? 26.133  170.937 20.550 1.00 59.75 ?  130 GLY C O   1 
ATOM   3211  N  N   . ASN C  2 133 ? 24.872  172.790 20.739 1.00 54.95 ?  131 ASN C N   1 
ATOM   3212  C  CA  . ASN C  2 133 ? 25.955  173.718 20.448 1.00 52.54 ?  131 ASN C CA  1 
ATOM   3213  C  C   . ASN C  2 133 ? 25.570  175.060 21.051 1.00 51.54 ?  131 ASN C C   1 
ATOM   3214  O  O   . ASN C  2 133 ? 24.410  175.281 21.410 1.00 52.79 ?  131 ASN C O   1 
ATOM   3215  C  CB  . ASN C  2 133 ? 26.217  173.823 18.942 1.00 49.90 ?  131 ASN C CB  1 
ATOM   3216  C  CG  . ASN C  2 133 ? 24.968  174.183 18.160 1.00 57.03 ?  131 ASN C CG  1 
ATOM   3217  O  OD1 . ASN C  2 133 ? 24.401  175.258 18.353 1.00 55.97 ?  131 ASN C OD1 1 
ATOM   3218  N  ND2 . ASN C  2 133 ? 24.519  173.278 17.288 1.00 50.23 ?  131 ASN C ND2 1 
ATOM   3219  N  N   . GLU C  2 134 ? 26.554  175.954 21.174 1.00 54.10 ?  132 GLU C N   1 
ATOM   3220  C  CA  . GLU C  2 134 ? 26.312  177.219 21.864 1.00 48.46 ?  132 GLU C CA  1 
ATOM   3221  C  C   . GLU C  2 134 ? 25.173  178.000 21.215 1.00 52.62 ?  132 GLU C C   1 
ATOM   3222  O  O   . GLU C  2 134 ? 24.293  178.520 21.911 1.00 48.72 ?  132 GLU C O   1 
ATOM   3223  C  CB  . GLU C  2 134 ? 27.586  178.062 21.886 1.00 51.00 ?  132 GLU C CB  1 
ATOM   3224  C  CG  . GLU C  2 134 ? 27.648  179.058 23.045 1.00 59.51 ?  132 GLU C CG  1 
ATOM   3225  C  CD  . GLU C  2 134 ? 28.742  180.101 22.860 1.00 69.26 ?  132 GLU C CD  1 
ATOM   3226  O  OE1 . GLU C  2 134 ? 29.892  179.710 22.561 1.00 76.19 ?  132 GLU C OE1 1 
ATOM   3227  O  OE2 . GLU C  2 134 ? 28.451  181.310 23.007 1.00 71.67 ?  132 GLU C OE2 1 
ATOM   3228  N  N   . GLU C  2 135 ? 25.168  178.074 19.878 1.00 54.73 ?  133 GLU C N   1 
ATOM   3229  C  CA  . GLU C  2 135 ? 24.131  178.804 19.151 1.00 51.14 ?  133 GLU C CA  1 
ATOM   3230  C  C   . GLU C  2 135 ? 22.735  178.333 19.544 1.00 46.41 ?  133 GLU C C   1 
ATOM   3231  O  O   . GLU C  2 135 ? 21.813  179.147 19.685 1.00 45.50 ?  133 GLU C O   1 
ATOM   3232  C  CB  . GLU C  2 135 ? 24.343  178.639 17.641 1.00 48.53 ?  133 GLU C CB  1 
ATOM   3233  C  CG  . GLU C  2 135 ? 23.714  179.724 16.783 1.00 47.71 ?  133 GLU C CG  1 
ATOM   3234  C  CD  . GLU C  2 135 ? 23.994  181.127 17.316 1.00 59.44 ?  133 GLU C CD  1 
ATOM   3235  O  OE1 . GLU C  2 135 ? 23.027  181.903 17.487 1.00 55.91 ?  133 GLU C OE1 1 
ATOM   3236  O  OE2 . GLU C  2 135 ? 25.178  181.447 17.586 1.00 63.25 ?  133 GLU C OE2 1 
ATOM   3237  N  N   . SER C  2 136 ? 22.565  177.022 19.742 1.00 47.88 ?  134 SER C N   1 
ATOM   3238  C  CA  . SER C  2 136 ? 21.255  176.495 20.102 1.00 44.46 ?  134 SER C CA  1 
ATOM   3239  C  C   . SER C  2 136 ? 20.783  177.052 21.434 1.00 47.19 ?  134 SER C C   1 
ATOM   3240  O  O   . SER C  2 136 ? 19.580  177.239 21.633 1.00 48.36 ?  134 SER C O   1 
ATOM   3241  C  CB  . SER C  2 136 ? 21.285  174.967 20.151 1.00 49.66 ?  134 SER C CB  1 
ATOM   3242  O  OG  . SER C  2 136 ? 20.068  174.444 20.675 1.00 43.21 ?  134 SER C OG  1 
ATOM   3243  N  N   . THR C  2 137 ? 21.707  177.329 22.352 1.00 45.46 ?  135 THR C N   1 
ATOM   3244  C  CA  . THR C  2 137 ? 21.344  177.870 23.653 1.00 45.41 ?  135 THR C CA  1 
ATOM   3245  C  C   . THR C  2 137 ? 21.122  179.375 23.627 1.00 51.55 ?  135 THR C C   1 
ATOM   3246  O  O   . THR C  2 137 ? 20.726  179.942 24.654 1.00 45.91 ?  135 THR C O   1 
ATOM   3247  C  CB  . THR C  2 137 ? 22.424  177.541 24.687 1.00 50.48 ?  135 THR C CB  1 
ATOM   3248  O  OG1 . THR C  2 137 ? 23.508  178.480 24.569 1.00 53.85 ?  135 THR C OG1 1 
ATOM   3249  C  CG2 . THR C  2 137 ? 22.942  176.132 24.472 1.00 48.87 ?  135 THR C CG2 1 
ATOM   3250  N  N   . LYS C  2 138 ? 21.394  180.028 22.495 1.00 46.78 ?  136 LYS C N   1 
ATOM   3251  C  CA  . LYS C  2 138 ? 21.160  181.455 22.331 1.00 46.58 ?  136 LYS C CA  1 
ATOM   3252  C  C   . LYS C  2 138 ? 20.001  181.749 21.392 1.00 43.13 ?  136 LYS C C   1 
ATOM   3253  O  O   . LYS C  2 138 ? 19.137  182.569 21.717 1.00 40.27 ?  136 LYS C O   1 
ATOM   3254  C  CB  . LYS C  2 138 ? 22.430  182.140 21.810 1.00 46.62 ?  136 LYS C CB  1 
ATOM   3255  C  CG  . LYS C  2 138 ? 23.598  182.072 22.766 1.00 50.89 ?  136 LYS C CG  1 
ATOM   3256  C  CD  . LYS C  2 138 ? 24.663  183.111 22.406 1.00 56.37 ?  136 LYS C CD  1 
ATOM   3257  C  CE  . LYS C  2 138 ? 24.561  184.353 23.303 1.00 60.62 ?  136 LYS C CE  1 
ATOM   3258  N  NZ  . LYS C  2 138 ? 24.092  184.060 24.697 1.00 63.93 ?  136 LYS C NZ  1 
ATOM   3259  N  N   . THR C  2 139 ? 19.956  181.094 20.227 1.00 43.51 ?  137 THR C N   1 
ATOM   3260  C  CA  . THR C  2 139 ? 18.969  181.406 19.202 1.00 36.89 ?  137 THR C CA  1 
ATOM   3261  C  C   . THR C  2 139 ? 18.153  180.211 18.757 1.00 41.06 ?  137 THR C C   1 
ATOM   3262  O  O   . THR C  2 139 ? 17.245  180.383 17.939 1.00 35.69 ?  137 THR C O   1 
ATOM   3263  C  CB  . THR C  2 139 ? 19.633  182.007 17.957 1.00 43.22 ?  137 THR C CB  1 
ATOM   3264  O  OG1 . THR C  2 139 ? 20.569  181.065 17.424 1.00 46.49 ?  137 THR C OG1 1 
ATOM   3265  C  CG2 . THR C  2 139 ? 20.339  183.326 18.273 1.00 40.65 ?  137 THR C CG2 1 
ATOM   3266  N  N   . GLY C  2 140 ? 18.453  179.010 19.241 1.00 37.82 ?  138 GLY C N   1 
ATOM   3267  C  CA  . GLY C  2 140 ? 17.785  177.848 18.694 1.00 35.99 ?  138 GLY C CA  1 
ATOM   3268  C  C   . GLY C  2 140 ? 18.157  177.509 17.265 1.00 38.87 ?  138 GLY C C   1 
ATOM   3269  O  O   . GLY C  2 140 ? 17.475  176.684 16.644 1.00 34.26 ?  138 GLY C O   1 
ATOM   3270  N  N   . ASN C  2 141 ? 19.209  178.130 16.718 1.00 35.68 ?  139 ASN C N   1 
ATOM   3271  C  CA  . ASN C  2 141 ? 19.599  177.963 15.310 1.00 42.49 ?  139 ASN C CA  1 
ATOM   3272  C  C   . ASN C  2 141 ? 18.459  178.285 14.339 1.00 42.75 ?  139 ASN C C   1 
ATOM   3273  O  O   . ASN C  2 141 ? 18.393  177.724 13.242 1.00 39.08 ?  139 ASN C O   1 
ATOM   3274  C  CB  . ASN C  2 141 ? 20.136  176.552 15.040 1.00 39.46 ?  139 ASN C CB  1 
ATOM   3275  C  CG  . ASN C  2 141 ? 21.495  176.326 15.664 1.00 45.12 ?  139 ASN C CG  1 
ATOM   3276  O  OD1 . ASN C  2 141 ? 22.483  176.955 15.274 1.00 51.77 ?  139 ASN C OD1 1 
ATOM   3277  N  ND2 . ASN C  2 141 ? 21.547  175.453 16.669 1.00 46.58 ?  139 ASN C ND2 1 
ATOM   3278  N  N   . ALA C  2 142 ? 17.561  179.203 14.714 1.00 39.00 ?  140 ALA C N   1 
ATOM   3279  C  CA  . ALA C  2 142 ? 16.448  179.562 13.840 1.00 37.93 ?  140 ALA C CA  1 
ATOM   3280  C  C   . ALA C  2 142 ? 16.886  180.430 12.664 1.00 34.31 ?  140 ALA C C   1 
ATOM   3281  O  O   . ALA C  2 142 ? 16.091  180.651 11.739 1.00 33.91 ?  140 ALA C O   1 
ATOM   3282  C  CB  . ALA C  2 142 ? 15.357  180.278 14.642 1.00 36.61 ?  140 ALA C CB  1 
ATOM   3283  N  N   . GLY C  2 143 ? 18.121  180.919 12.668 1.00 34.23 ?  141 GLY C N   1 
ATOM   3284  C  CA  . GLY C  2 143 ? 18.640  181.548 11.472 1.00 40.25 ?  141 GLY C CA  1 
ATOM   3285  C  C   . GLY C  2 143 ? 18.229  183.007 11.344 1.00 42.12 ?  141 GLY C C   1 
ATOM   3286  O  O   . GLY C  2 143 ? 17.952  183.693 12.336 1.00 36.14 ?  141 GLY C O   1 
ATOM   3287  N  N   . SER C  2 144 ? 18.178  183.480 10.103 1.00 39.70 ?  142 SER C N   1 
ATOM   3288  C  CA  . SER C  2 144 ? 18.032  184.908 9.875  1.00 41.29 ?  142 SER C CA  1 
ATOM   3289  C  C   . SER C  2 144 ? 16.580  185.351 10.103 1.00 36.01 ?  142 SER C C   1 
ATOM   3290  O  O   . SER C  2 144 ? 15.645  184.547 10.198 1.00 30.92 ?  142 SER C O   1 
ATOM   3291  C  CB  . SER C  2 144 ? 18.510  185.274 8.469  1.00 38.77 ?  142 SER C CB  1 
ATOM   3292  O  OG  . SER C  2 144 ? 17.591  184.824 7.503  1.00 42.02 ?  142 SER C OG  1 
ATOM   3293  N  N   . ARG C  2 145 ? 16.400  186.663 10.172 1.00 34.70 ?  143 ARG C N   1 
ATOM   3294  C  CA  . ARG C  2 145 ? 15.119  187.257 10.527 1.00 35.15 ?  143 ARG C CA  1 
ATOM   3295  C  C   . ARG C  2 145 ? 14.348  187.610 9.255  1.00 34.25 ?  143 ARG C C   1 
ATOM   3296  O  O   . ARG C  2 145 ? 14.736  188.523 8.527  1.00 35.54 ?  143 ARG C O   1 
ATOM   3297  C  CB  . ARG C  2 145 ? 15.372  188.475 11.407 1.00 28.15 ?  143 ARG C CB  1 
ATOM   3298  C  CG  . ARG C  2 145 ? 16.238  188.124 12.628 1.00 31.17 ?  143 ARG C CG  1 
ATOM   3299  C  CD  . ARG C  2 145 ? 16.749  189.349 13.379 1.00 31.15 ?  143 ARG C CD  1 
ATOM   3300  N  NE  . ARG C  2 145 ? 17.644  188.920 14.444 1.00 31.41 ?  143 ARG C NE  1 
ATOM   3301  C  CZ  . ARG C  2 145 ? 17.857  189.570 15.576 1.00 32.13 ?  143 ARG C CZ  1 
ATOM   3302  N  NH1 . ARG C  2 145 ? 17.288  190.739 15.818 1.00 31.29 ?  143 ARG C NH1 1 
ATOM   3303  N  NH2 . ARG C  2 145 ? 18.670  189.042 16.484 1.00 31.86 ?  143 ARG C NH2 1 
ATOM   3304  N  N   . LEU C  2 146 ? 13.237  186.910 9.002  1.00 33.56 ?  144 LEU C N   1 
ATOM   3305  C  CA  . LEU C  2 146 ? 12.483  187.116 7.762  1.00 30.36 ?  144 LEU C CA  1 
ATOM   3306  C  C   . LEU C  2 146 ? 11.574  188.328 7.828  1.00 32.35 ?  144 LEU C C   1 
ATOM   3307  O  O   . LEU C  2 146 ? 11.431  189.058 6.839  1.00 29.54 ?  144 LEU C O   1 
ATOM   3308  C  CB  . LEU C  2 146 ? 11.636  185.891 7.441  1.00 31.52 ?  144 LEU C CB  1 
ATOM   3309  C  CG  . LEU C  2 146 ? 12.410  184.595 7.255  1.00 36.74 ?  144 LEU C CG  1 
ATOM   3310  C  CD1 . LEU C  2 146 ? 11.461  183.501 6.765  1.00 31.63 ?  144 LEU C CD1 1 
ATOM   3311  C  CD2 . LEU C  2 146 ? 13.539  184.843 6.281  1.00 36.44 ?  144 LEU C CD2 1 
ATOM   3312  N  N   . ALA C  2 147 ? 10.888  188.521 8.950  1.00 22.42 ?  145 ALA C N   1 
ATOM   3313  C  CA  . ALA C  2 147 ? 10.030  189.686 9.106  1.00 25.85 ?  145 ALA C CA  1 
ATOM   3314  C  C   . ALA C  2 147 ? 9.906   190.000 10.585 1.00 27.47 ?  145 ALA C C   1 
ATOM   3315  O  O   . ALA C  2 147 ? 10.153  189.146 11.449 1.00 27.11 ?  145 ALA C O   1 
ATOM   3316  C  CB  . ALA C  2 147 ? 8.652   189.473 8.488  1.00 20.34 ?  145 ALA C CB  1 
ATOM   3317  N  N   . CYS C  2 148 ? 9.507   191.231 10.876 1.00 25.35 ?  146 CYS C N   1 
ATOM   3318  C  CA  . CYS C  2 148 ? 9.368   191.641 12.268 1.00 27.54 ?  146 CYS C CA  1 
ATOM   3319  C  C   . CYS C  2 148 ? 8.453   192.852 12.339 1.00 28.39 ?  146 CYS C C   1 
ATOM   3320  O  O   . CYS C  2 148 ? 8.124   193.467 11.319 1.00 28.93 ?  146 CYS C O   1 
ATOM   3321  C  CB  . CYS C  2 148 ? 10.736  191.947 12.893 1.00 25.26 ?  146 CYS C CB  1 
ATOM   3322  S  SG  . CYS C  2 148 ? 11.668  193.260 12.052 1.00 33.75 ?  146 CYS C SG  1 
ATOM   3323  N  N   . GLY C  2 149 ? 8.042   193.176 13.561 1.00 26.34 ?  147 GLY C N   1 
ATOM   3324  C  CA  . GLY C  2 149 ? 7.273   194.384 13.823 1.00 23.70 ?  147 GLY C CA  1 
ATOM   3325  C  C   . GLY C  2 149 ? 7.253   194.670 15.311 1.00 26.60 ?  147 GLY C C   1 
ATOM   3326  O  O   . GLY C  2 149 ? 7.440   193.768 16.139 1.00 25.48 ?  147 GLY C O   1 
ATOM   3327  N  N   . VAL C  2 150 ? 7.015   195.932 15.645 1.00 24.64 ?  148 VAL C N   1 
ATOM   3328  C  CA  . VAL C  2 150 ? 6.901   196.310 17.053 1.00 22.49 ?  148 VAL C CA  1 
ATOM   3329  C  C   . VAL C  2 150 ? 5.539   195.879 17.592 1.00 26.50 ?  148 VAL C C   1 
ATOM   3330  O  O   . VAL C  2 150 ? 4.506   196.032 16.929 1.00 24.09 ?  148 VAL C O   1 
ATOM   3331  C  CB  . VAL C  2 150 ? 7.150   197.818 17.230 1.00 24.70 ?  148 VAL C CB  1 
ATOM   3332  C  CG1 . VAL C  2 150 ? 7.230   198.181 18.722 1.00 20.34 ?  148 VAL C CG1 1 
ATOM   3333  C  CG2 . VAL C  2 150 ? 8.469   198.227 16.535 1.00 22.92 ?  148 VAL C CG2 1 
ATOM   3334  N  N   . ILE C  2 151 ? 5.529   195.311 18.794 1.00 23.60 ?  149 ILE C N   1 
ATOM   3335  C  CA  . ILE C  2 151 ? 4.282   194.894 19.421 1.00 24.04 ?  149 ILE C CA  1 
ATOM   3336  C  C   . ILE C  2 151 ? 3.623   196.123 20.021 1.00 25.27 ?  149 ILE C C   1 
ATOM   3337  O  O   . ILE C  2 151 ? 4.191   196.773 20.910 1.00 26.22 ?  149 ILE C O   1 
ATOM   3338  C  CB  . ILE C  2 151 ? 4.528   193.819 20.487 1.00 26.39 ?  149 ILE C CB  1 
ATOM   3339  C  CG1 . ILE C  2 151 ? 5.166   192.587 19.848 1.00 26.24 ?  149 ILE C CG1 1 
ATOM   3340  C  CG2 . ILE C  2 151 ? 3.218   193.476 21.215 1.00 24.79 ?  149 ILE C CG2 1 
ATOM   3341  C  CD1 . ILE C  2 151 ? 5.830   191.647 20.882 1.00 25.65 ?  149 ILE C CD1 1 
ATOM   3342  N  N   . GLY C  2 152 ? 2.432   196.452 19.536 1.00 23.39 ?  150 GLY C N   1 
ATOM   3343  C  CA  . GLY C  2 152 ? 1.794   197.690 19.927 1.00 23.51 ?  150 GLY C CA  1 
ATOM   3344  C  C   . GLY C  2 152 ? 0.523   197.476 20.716 1.00 25.55 ?  150 GLY C C   1 
ATOM   3345  O  O   . GLY C  2 152 ? -0.090  196.408 20.606 1.00 22.73 ?  150 GLY C O   1 
ATOM   3346  N  N   . ILE C  2 153 ? 0.116   198.478 21.508 1.00 23.67 ?  151 ILE C N   1 
ATOM   3347  C  CA  . ILE C  2 153 ? -1.148  198.387 22.230 1.00 26.42 ?  151 ILE C CA  1 
ATOM   3348  C  C   . ILE C  2 153 ? -2.292  198.466 21.232 1.00 26.94 ?  151 ILE C C   1 
ATOM   3349  O  O   . ILE C  2 153 ? -2.280  199.297 20.315 1.00 25.03 ?  151 ILE C O   1 
ATOM   3350  C  CB  . ILE C  2 153 ? -1.253  199.489 23.297 1.00 24.27 ?  151 ILE C CB  1 
ATOM   3351  C  CG1 . ILE C  2 153 ? -0.143  199.318 24.335 1.00 30.97 ?  151 ILE C CG1 1 
ATOM   3352  C  CG2 . ILE C  2 153 ? -2.593  199.408 23.997 1.00 28.88 ?  151 ILE C CG2 1 
ATOM   3353  C  CD1 . ILE C  2 153 ? 0.250   200.611 25.032 1.00 37.73 ?  151 ILE C CD1 1 
ATOM   3354  N  N   . ALA C  2 154 ? -3.278  197.587 21.396 1.00 29.87 ?  152 ALA C N   1 
ATOM   3355  C  CA  . ALA C  2 154 ? -4.417  197.492 20.495 1.00 28.76 ?  152 ALA C CA  1 
ATOM   3356  C  C   . ALA C  2 154 ? -5.710  197.784 21.243 1.00 32.50 ?  152 ALA C C   1 
ATOM   3357  O  O   . ALA C  2 154 ? -5.798  197.624 22.463 1.00 30.52 ?  152 ALA C O   1 
ATOM   3358  C  CB  . ALA C  2 154 ? -4.512  196.104 19.859 1.00 28.83 ?  152 ALA C CB  1 
ATOM   3359  N  N   . GLN C  2 155 ? -6.713  198.217 20.491 1.00 35.47 ?  153 GLN C N   1 
ATOM   3360  C  CA  . GLN C  2 155 ? -8.020  198.530 21.057 1.00 37.14 ?  153 GLN C CA  1 
ATOM   3361  C  C   . GLN C  2 155 ? -8.810  197.263 21.383 1.00 54.62 ?  153 GLN C C   1 
ATOM   3362  O  O   . GLN C  2 155 ? -8.811  196.299 20.593 1.00 44.11 ?  153 GLN C O   1 
ATOM   3363  C  CB  . GLN C  2 155 ? -8.835  199.392 20.103 1.00 36.37 ?  153 GLN C CB  1 
ATOM   3364  C  CG  . GLN C  2 155 ? -10.142 199.862 20.723 1.00 45.35 ?  153 GLN C CG  1 
ATOM   3365  C  CD  . GLN C  2 155 ? -10.959 200.717 19.775 1.00 51.34 ?  153 GLN C CD  1 
ATOM   3366  O  OE1 . GLN C  2 155 ? -10.995 200.473 18.562 1.00 55.80 ?  153 GLN C OE1 1 
ATOM   3367  N  NE2 . GLN C  2 155 ? -11.618 201.733 20.322 1.00 50.04 ?  153 GLN C NE2 1 
ATOM   3368  O  OXT . GLN C  2 155 ? -9.469  197.199 22.434 1.00 60.29 ?  153 GLN C OXT 1 
ATOM   3369  N  N   . MET D  1 1   ? 11.032  200.413 33.185 1.00 67.75 ?  0   MET D N   1 
ATOM   3370  C  CA  . MET D  1 1   ? 12.184  201.257 33.488 1.00 63.86 ?  0   MET D CA  1 
ATOM   3371  C  C   . MET D  1 1   ? 12.896  201.736 32.206 1.00 68.35 ?  0   MET D C   1 
ATOM   3372  O  O   . MET D  1 1   ? 14.089  202.068 32.245 1.00 59.70 ?  0   MET D O   1 
ATOM   3373  C  CB  . MET D  1 1   ? 13.169  200.501 34.396 1.00 60.29 ?  0   MET D CB  1 
ATOM   3374  N  N   . ALA D  1 2   ? 12.166  201.780 31.082 1.00 63.02 ?  1   ALA D N   1 
ATOM   3375  C  CA  . ALA D  1 2   ? 12.758  202.187 29.806 1.00 52.30 ?  1   ALA D CA  1 
ATOM   3376  C  C   . ALA D  1 2   ? 13.201  203.648 29.853 1.00 36.26 ?  1   ALA D C   1 
ATOM   3377  O  O   . ALA D  1 2   ? 12.468  204.516 30.332 1.00 43.00 ?  1   ALA D O   1 
ATOM   3378  C  CB  . ALA D  1 2   ? 11.769  201.973 28.656 1.00 42.57 ?  1   ALA D CB  1 
ATOM   3379  N  N   . THR D  1 3   ? 14.421  203.910 29.386 1.00 29.79 ?  2   THR D N   1 
ATOM   3380  C  CA  . THR D  1 3   ? 14.938  205.267 29.294 1.00 34.95 ?  2   THR D CA  1 
ATOM   3381  C  C   . THR D  1 3   ? 15.143  205.728 27.857 1.00 29.05 ?  2   THR D C   1 
ATOM   3382  O  O   . THR D  1 3   ? 15.411  206.921 27.638 1.00 27.76 ?  2   THR D O   1 
ATOM   3383  C  CB  . THR D  1 3   ? 16.272  205.395 30.041 1.00 34.57 ?  2   THR D CB  1 
ATOM   3384  O  OG1 . THR D  1 3   ? 17.246  204.543 29.421 1.00 39.83 ?  2   THR D OG1 1 
ATOM   3385  C  CG2 . THR D  1 3   ? 16.119  205.004 31.519 1.00 35.26 ?  2   THR D CG2 1 
ATOM   3386  N  N   . LYS D  1 4   ? 15.018  204.822 26.883 1.00 30.31 ?  3   LYS D N   1 
ATOM   3387  C  CA  . LYS D  1 4   ? 15.187  205.138 25.472 1.00 32.30 ?  3   LYS D CA  1 
ATOM   3388  C  C   . LYS D  1 4   ? 14.123  204.434 24.647 1.00 28.01 ?  3   LYS D C   1 
ATOM   3389  O  O   . LYS D  1 4   ? 13.784  203.277 24.905 1.00 24.80 ?  3   LYS D O   1 
ATOM   3390  C  CB  . LYS D  1 4   ? 16.571  204.723 24.946 1.00 32.75 ?  3   LYS D CB  1 
ATOM   3391  C  CG  . LYS D  1 4   ? 17.697  205.682 25.340 1.00 42.88 ?  3   LYS D CG  1 
ATOM   3392  C  CD  . LYS D  1 4   ? 18.846  205.687 24.318 1.00 55.46 ?  3   LYS D CD  1 
ATOM   3393  C  CE  . LYS D  1 4   ? 18.678  206.806 23.255 1.00 59.36 ?  3   LYS D CE  1 
ATOM   3394  N  NZ  . LYS D  1 4   ? 17.397  206.765 22.449 1.00 51.36 ?  3   LYS D NZ  1 
ATOM   3395  N  N   . ALA D  1 5   ? 13.633  205.125 23.627 1.00 22.55 ?  4   ALA D N   1 
ATOM   3396  C  CA  . ALA D  1 5   ? 12.654  204.559 22.722 1.00 23.87 ?  4   ALA D CA  1 
ATOM   3397  C  C   . ALA D  1 5   ? 12.950  205.088 21.326 1.00 25.39 ?  4   ALA D C   1 
ATOM   3398  O  O   . ALA D  1 5   ? 13.698  206.049 21.148 1.00 25.30 ?  4   ALA D O   1 
ATOM   3399  C  CB  . ALA D  1 5   ? 11.229  204.902 23.157 1.00 23.11 ?  4   ALA D CB  1 
ATOM   3400  N  N   . VAL D  1 6   ? 12.358  204.454 20.324 1.00 22.50 ?  5   VAL D N   1 
ATOM   3401  C  CA  . VAL D  1 6   ? 12.629  204.826 18.943 1.00 22.66 ?  5   VAL D CA  1 
ATOM   3402  C  C   . VAL D  1 6   ? 11.403  204.481 18.118 1.00 29.23 ?  5   VAL D C   1 
ATOM   3403  O  O   . VAL D  1 6   ? 10.629  203.580 18.463 1.00 25.76 ?  5   VAL D O   1 
ATOM   3404  C  CB  . VAL D  1 6   ? 13.903  204.123 18.394 1.00 22.55 ?  5   VAL D CB  1 
ATOM   3405  C  CG1 . VAL D  1 6   ? 13.627  202.672 18.115 1.00 23.12 ?  5   VAL D CG1 1 
ATOM   3406  C  CG2 . VAL D  1 6   ? 14.399  204.829 17.106 1.00 26.87 ?  5   VAL D CG2 1 
ATOM   3407  N  N   . CYS D  1 7   ? 11.227  205.216 17.031 1.00 23.25 ?  6   CYS D N   1 
ATOM   3408  C  CA  . CYS D  1 7   ? 10.075  205.036 16.170 1.00 21.86 ?  6   CYS D CA  1 
ATOM   3409  C  C   . CYS D  1 7   ? 10.500  205.267 14.729 1.00 24.99 ?  6   CYS D C   1 
ATOM   3410  O  O   . CYS D  1 7   ? 11.071  206.319 14.420 1.00 22.73 ?  6   CYS D O   1 
ATOM   3411  C  CB  . CYS D  1 7   ? 8.972   206.012 16.560 1.00 21.09 ?  6   CYS D CB  1 
ATOM   3412  S  SG  . CYS D  1 7   ? 7.593   205.972 15.438 1.00 29.05 ?  6   CYS D SG  1 
ATOM   3413  N  N   . VAL D  1 8   ? 10.208  204.313 13.850 1.00 24.50 ?  7   VAL D N   1 
ATOM   3414  C  CA  . VAL D  1 8   ? 10.467  204.467 12.418 1.00 24.01 ?  7   VAL D CA  1 
ATOM   3415  C  C   . VAL D  1 8   ? 9.159   204.901 11.756 1.00 21.59 ?  7   VAL D C   1 
ATOM   3416  O  O   . VAL D  1 8   ? 8.162   204.173 11.782 1.00 24.33 ?  7   VAL D O   1 
ATOM   3417  C  CB  . VAL D  1 8   ? 11.030  203.178 11.797 1.00 24.72 ?  7   VAL D CB  1 
ATOM   3418  C  CG1 . VAL D  1 8   ? 11.233  203.336 10.255 1.00 23.54 ?  7   VAL D CG1 1 
ATOM   3419  C  CG2 . VAL D  1 8   ? 12.337  202.811 12.470 1.00 21.73 ?  7   VAL D CG2 1 
ATOM   3420  N  N   . LEU D  1 9   ? 9.138   206.107 11.205 1.00 20.34 ?  8   LEU D N   1 
ATOM   3421  C  CA  . LEU D  1 9   ? 7.947   206.631 10.561 1.00 20.60 ?  8   LEU D CA  1 
ATOM   3422  C  C   . LEU D  1 9   ? 7.946   206.233 9.091  1.00 25.65 ?  8   LEU D C   1 
ATOM   3423  O  O   . LEU D  1 9   ? 8.910   206.511 8.369  1.00 20.95 ?  8   LEU D O   1 
ATOM   3424  C  CB  . LEU D  1 9   ? 7.893   208.154 10.672 1.00 25.42 ?  8   LEU D CB  1 
ATOM   3425  C  CG  . LEU D  1 9   ? 7.839   208.725 12.093 1.00 28.06 ?  8   LEU D CG  1 
ATOM   3426  C  CD1 . LEU D  1 9   ? 7.848   210.244 12.025 1.00 32.57 ?  8   LEU D CD1 1 
ATOM   3427  C  CD2 . LEU D  1 9   ? 6.604   208.253 12.720 1.00 26.68 ?  8   LEU D CD2 1 
ATOM   3428  N  N   . LYS D  1 10  ? 6.855   205.615 8.648  1.00 27.21 ?  9   LYS D N   1 
ATOM   3429  C  CA  . LYS D  1 10  ? 6.688   205.231 7.248  1.00 26.58 ?  9   LYS D CA  1 
ATOM   3430  C  C   . LYS D  1 10  ? 5.260   205.529 6.822  1.00 28.94 ?  9   LYS D C   1 
ATOM   3431  O  O   . LYS D  1 10  ? 4.343   205.539 7.645  1.00 25.64 ?  9   LYS D O   1 
ATOM   3432  C  CB  . LYS D  1 10  ? 6.973   203.746 7.027  1.00 28.81 ?  9   LYS D CB  1 
ATOM   3433  C  CG  . LYS D  1 10  ? 8.440   203.409 6.974  1.00 37.22 ?  9   LYS D CG  1 
ATOM   3434  C  CD  . LYS D  1 10  ? 8.615   201.913 6.692  1.00 49.03 ?  9   LYS D CD  1 
ATOM   3435  C  CE  . LYS D  1 10  ? 9.916   201.380 7.276  1.00 46.47 ?  9   LYS D CE  1 
ATOM   3436  N  NZ  . LYS D  1 10  ? 11.095  201.945 6.579  1.00 53.13 ?  9   LYS D NZ  1 
ATOM   3437  N  N   . GLY D  1 11  ? 5.073   205.748 5.528  1.00 28.45 ?  10  GLY D N   1 
ATOM   3438  C  CA  . GLY D  1 11  ? 3.735   205.919 5.001  1.00 31.50 ?  10  GLY D CA  1 
ATOM   3439  C  C   . GLY D  1 11  ? 3.651   205.519 3.537  1.00 35.26 ?  10  GLY D C   1 
ATOM   3440  O  O   . GLY D  1 11  ? 4.587   204.922 2.996  1.00 33.23 ?  10  GLY D O   1 
ATOM   3441  N  N   . ASP D  1 12  ? 2.546   205.869 2.887  1.00 36.03 ?  11  ASP D N   1 
ATOM   3442  C  CA  . ASP D  1 12  ? 2.367   205.539 1.483  1.00 40.01 ?  11  ASP D CA  1 
ATOM   3443  C  C   . ASP D  1 12  ? 3.026   206.551 0.557  1.00 44.86 ?  11  ASP D C   1 
ATOM   3444  O  O   . ASP D  1 12  ? 3.285   206.232 -0.607 1.00 42.54 ?  11  ASP D O   1 
ATOM   3445  C  CB  . ASP D  1 12  ? 0.880   205.455 1.147  1.00 39.26 ?  11  ASP D CB  1 
ATOM   3446  C  CG  . ASP D  1 12  ? 0.213   204.258 1.787  1.00 54.32 ?  11  ASP D CG  1 
ATOM   3447  O  OD1 . ASP D  1 12  ? -0.839  204.472 2.441  1.00 58.55 ?  11  ASP D OD1 1 
ATOM   3448  O  OD2 . ASP D  1 12  ? 0.775   203.139 1.686  1.00 51.89 ?  11  ASP D OD2 1 
ATOM   3449  N  N   . GLY D  1 13  ? 3.293   207.760 1.034  1.00 32.41 ?  12  GLY D N   1 
ATOM   3450  C  CA  . GLY D  1 13  ? 3.913   208.767 0.211  1.00 30.37 ?  12  GLY D CA  1 
ATOM   3451  C  C   . GLY D  1 13  ? 5.395   208.881 0.476  1.00 28.06 ?  12  GLY D C   1 
ATOM   3452  O  O   . GLY D  1 13  ? 6.066   207.917 0.851  1.00 29.57 ?  12  GLY D O   1 
ATOM   3453  N  N   . PRO D  1 14  ? 5.943   210.081 0.282  1.00 30.21 ?  13  PRO D N   1 
ATOM   3454  C  CA  . PRO D  1 14  ? 7.385   210.268 0.453  1.00 29.64 ?  13  PRO D CA  1 
ATOM   3455  C  C   . PRO D  1 14  ? 7.826   210.518 1.890  1.00 25.31 ?  13  PRO D C   1 
ATOM   3456  O  O   . PRO D  1 14  ? 9.035   210.599 2.137  1.00 27.85 ?  13  PRO D O   1 
ATOM   3457  C  CB  . PRO D  1 14  ? 7.671   211.491 -0.429 1.00 27.21 ?  13  PRO D CB  1 
ATOM   3458  C  CG  . PRO D  1 14  ? 6.407   212.272 -0.418 1.00 25.80 ?  13  PRO D CG  1 
ATOM   3459  C  CD  . PRO D  1 14  ? 5.276   211.275 -0.261 1.00 29.27 ?  13  PRO D CD  1 
ATOM   3460  N  N   . VAL D  1 15  ? 6.910   210.629 2.846  1.00 27.44 ?  14  VAL D N   1 
ATOM   3461  C  CA  . VAL D  1 15  ? 7.292   211.004 4.209  1.00 24.77 ?  14  VAL D CA  1 
ATOM   3462  C  C   . VAL D  1 15  ? 7.853   209.784 4.929  1.00 26.14 ?  14  VAL D C   1 
ATOM   3463  O  O   . VAL D  1 15  ? 7.181   208.757 5.043  1.00 25.23 ?  14  VAL D O   1 
ATOM   3464  C  CB  . VAL D  1 15  ? 6.104   211.592 4.980  1.00 25.50 ?  14  VAL D CB  1 
ATOM   3465  C  CG1 . VAL D  1 15  ? 6.513   211.861 6.441  1.00 22.68 ?  14  VAL D CG1 1 
ATOM   3466  C  CG2 . VAL D  1 15  ? 5.634   212.895 4.320  1.00 21.76 ?  14  VAL D CG2 1 
ATOM   3467  N  N   . GLN D  1 16  ? 9.082   209.899 5.432  1.00 26.97 ?  15  GLN D N   1 
ATOM   3468  C  CA  . GLN D  1 16  ? 9.648   208.845 6.259  1.00 34.58 ?  15  GLN D CA  1 
ATOM   3469  C  C   . GLN D  1 16  ? 10.711  209.455 7.153  1.00 25.82 ?  15  GLN D C   1 
ATOM   3470  O  O   . GLN D  1 16  ? 11.273  210.508 6.846  1.00 29.23 ?  15  GLN D O   1 
ATOM   3471  C  CB  . GLN D  1 16  ? 10.232  207.715 5.402  1.00 33.68 ?  15  GLN D CB  1 
ATOM   3472  C  CG  . GLN D  1 16  ? 11.425  208.168 4.585  1.00 41.53 ?  15  GLN D CG  1 
ATOM   3473  C  CD  . GLN D  1 16  ? 12.206  207.007 3.977  1.00 57.67 ?  15  GLN D CD  1 
ATOM   3474  O  OE1 . GLN D  1 16  ? 13.440  207.002 3.986  1.00 57.10 ?  15  GLN D OE1 1 
ATOM   3475  N  NE2 . GLN D  1 16  ? 11.491  206.021 3.446  1.00 56.85 ?  15  GLN D NE2 1 
ATOM   3476  N  N   . GLY D  1 17  ? 10.971  208.801 8.280  1.00 26.25 ?  16  GLY D N   1 
ATOM   3477  C  CA  . GLY D  1 17  ? 11.999  209.309 9.169  1.00 25.40 ?  16  GLY D CA  1 
ATOM   3478  C  C   . GLY D  1 17  ? 12.174  208.426 10.390 1.00 22.90 ?  16  GLY D C   1 
ATOM   3479  O  O   . GLY D  1 17  ? 11.500  207.406 10.554 1.00 26.82 ?  16  GLY D O   1 
ATOM   3480  N  N   . ILE D  1 18  ? 13.099  208.843 11.253 1.00 26.13 ?  17  ILE D N   1 
ATOM   3481  C  CA  . ILE D  1 18  ? 13.413  208.139 12.493 1.00 25.89 ?  17  ILE D CA  1 
ATOM   3482  C  C   . ILE D  1 18  ? 13.370  209.148 13.631 1.00 25.54 ?  17  ILE D C   1 
ATOM   3483  O  O   . ILE D  1 18  ? 13.964  210.226 13.527 1.00 28.13 ?  17  ILE D O   1 
ATOM   3484  C  CB  . ILE D  1 18  ? 14.781  207.441 12.412 1.00 22.47 ?  17  ILE D CB  1 
ATOM   3485  C  CG1 . ILE D  1 18  ? 14.728  206.376 11.308 1.00 30.27 ?  17  ILE D CG1 1 
ATOM   3486  C  CG2 . ILE D  1 18  ? 15.178  206.861 13.794 1.00 26.85 ?  17  ILE D CG2 1 
ATOM   3487  C  CD1 . ILE D  1 18  ? 16.042  205.685 11.032 1.00 30.19 ?  17  ILE D CD1 1 
ATOM   3488  N  N   . ILE D  1 19  ? 12.640  208.817 14.698 1.00 24.05 ?  18  ILE D N   1 
ATOM   3489  C  CA  . ILE D  1 19  ? 12.470  209.694 15.850 1.00 20.34 ?  18  ILE D CA  1 
ATOM   3490  C  C   . ILE D  1 19  ? 12.919  208.936 17.097 1.00 25.89 ?  18  ILE D C   1 
ATOM   3491  O  O   . ILE D  1 19  ? 12.452  207.821 17.347 1.00 23.44 ?  18  ILE D O   1 
ATOM   3492  C  CB  . ILE D  1 19  ? 11.012  210.164 15.988 1.00 21.01 ?  18  ILE D CB  1 
ATOM   3493  C  CG1 . ILE D  1 19  ? 10.602  211.022 14.779 1.00 26.06 ?  18  ILE D CG1 1 
ATOM   3494  C  CG2 . ILE D  1 19  ? 10.802  210.928 17.302 1.00 20.34 ?  18  ILE D CG2 1 
ATOM   3495  C  CD1 . ILE D  1 19  ? 11.344  212.332 14.680 1.00 20.34 ?  18  ILE D CD1 1 
ATOM   3496  N  N   . ASN D  1 20  ? 13.827  209.541 17.866 1.00 27.81 ?  19  ASN D N   1 
ATOM   3497  C  CA  . ASN D  1 20  ? 14.354  208.982 19.102 1.00 28.74 ?  19  ASN D CA  1 
ATOM   3498  C  C   . ASN D  1 20  ? 13.703  209.640 20.314 1.00 24.29 ?  19  ASN D C   1 
ATOM   3499  O  O   . ASN D  1 20  ? 13.327  210.810 20.277 1.00 24.22 ?  19  ASN D O   1 
ATOM   3500  C  CB  . ASN D  1 20  ? 15.874  209.168 19.167 1.00 29.51 ?  19  ASN D CB  1 
ATOM   3501  C  CG  . ASN D  1 20  ? 16.566  208.643 17.932 1.00 28.58 ?  19  ASN D CG  1 
ATOM   3502  O  OD1 . ASN D  1 20  ? 16.757  207.453 17.792 1.00 32.75 ?  19  ASN D OD1 1 
ATOM   3503  N  ND2 . ASN D  1 20  ? 16.920  209.547 17.012 1.00 29.47 ?  19  ASN D ND2 1 
ATOM   3504  N  N   . PHE D  1 21  ? 13.568  208.873 21.397 1.00 24.76 ?  20  PHE D N   1 
ATOM   3505  C  CA  . PHE D  1 21  ? 13.065  209.399 22.661 1.00 25.01 ?  20  PHE D CA  1 
ATOM   3506  C  C   . PHE D  1 21  ? 14.064  209.079 23.752 1.00 25.76 ?  20  PHE D C   1 
ATOM   3507  O  O   . PHE D  1 21  ? 14.628  207.987 23.769 1.00 28.71 ?  20  PHE D O   1 
ATOM   3508  C  CB  . PHE D  1 21  ? 11.696  208.796 23.051 1.00 22.40 ?  20  PHE D CB  1 
ATOM   3509  C  CG  . PHE D  1 21  ? 10.618  209.001 22.028 1.00 26.48 ?  20  PHE D CG  1 
ATOM   3510  C  CD1 . PHE D  1 21  ? 10.551  208.195 20.895 1.00 22.90 ?  20  PHE D CD1 1 
ATOM   3511  C  CD2 . PHE D  1 21  ? 9.671   209.997 22.200 1.00 25.63 ?  20  PHE D CD2 1 
ATOM   3512  C  CE1 . PHE D  1 21  ? 9.533   208.372 19.950 1.00 23.77 ?  20  PHE D CE1 1 
ATOM   3513  C  CE2 . PHE D  1 21  ? 8.654   210.182 21.257 1.00 24.15 ?  20  PHE D CE2 1 
ATOM   3514  C  CZ  . PHE D  1 21  ? 8.594   209.369 20.136 1.00 22.69 ?  20  PHE D CZ  1 
ATOM   3515  N  N   . GLU D  1 22  ? 14.258  210.005 24.687 1.00 29.71 ?  21  GLU D N   1 
ATOM   3516  C  CA  . GLU D  1 22  ? 15.156  209.726 25.796 1.00 31.00 ?  21  GLU D CA  1 
ATOM   3517  C  C   . GLU D  1 22  ? 14.606  210.353 27.062 1.00 33.39 ?  21  GLU D C   1 
ATOM   3518  O  O   . GLU D  1 22  ? 14.299  211.546 27.084 1.00 27.77 ?  21  GLU D O   1 
ATOM   3519  C  CB  . GLU D  1 22  ? 16.566  210.252 25.532 1.00 37.06 ?  21  GLU D CB  1 
ATOM   3520  C  CG  . GLU D  1 22  ? 17.578  209.686 26.509 1.00 47.27 ?  21  GLU D CG  1 
ATOM   3521  C  CD  . GLU D  1 22  ? 18.978  210.215 26.293 1.00 58.29 ?  21  GLU D CD  1 
ATOM   3522  O  OE1 . GLU D  1 22  ? 19.131  211.249 25.606 1.00 61.86 ?  21  GLU D OE1 1 
ATOM   3523  O  OE2 . GLU D  1 22  ? 19.923  209.591 26.822 1.00 64.16 ?  21  GLU D OE2 1 
ATOM   3524  N  N   . GLN D  1 23  ? 14.504  209.551 28.120 1.00 28.04 ?  22  GLN D N   1 
ATOM   3525  C  CA  . GLN D  1 23  ? 14.012  210.021 29.411 1.00 28.72 ?  22  GLN D CA  1 
ATOM   3526  C  C   . GLN D  1 23  ? 14.989  209.531 30.476 1.00 30.55 ?  22  GLN D C   1 
ATOM   3527  O  O   . GLN D  1 23  ? 14.897  208.395 30.947 1.00 31.74 ?  22  GLN D O   1 
ATOM   3528  C  CB  . GLN D  1 23  ? 12.610  209.528 29.654 1.00 25.16 ?  22  GLN D CB  1 
ATOM   3529  C  CG  . GLN D  1 23  ? 11.947  210.238 30.792 1.00 26.91 ?  22  GLN D CG  1 
ATOM   3530  C  CD  . GLN D  1 23  ? 10.620  209.647 31.111 1.00 30.64 ?  22  GLN D CD  1 
ATOM   3531  O  OE1 . GLN D  1 23  ? 10.331  208.509 30.727 1.00 27.98 ?  22  GLN D OE1 1 
ATOM   3532  N  NE2 . GLN D  1 23  ? 9.783   210.408 31.801 1.00 29.53 ?  22  GLN D NE2 1 
ATOM   3533  N  N   . LYS D  1 24  ? 15.938  210.380 30.848 1.00 33.15 ?  23  LYS D N   1 
ATOM   3534  C  CA  . LYS D  1 24  ? 16.972  209.936 31.780 1.00 41.99 ?  23  LYS D CA  1 
ATOM   3535  C  C   . LYS D  1 24  ? 16.412  209.681 33.182 1.00 42.44 ?  23  LYS D C   1 
ATOM   3536  O  O   . LYS D  1 24  ? 16.884  208.776 33.876 1.00 45.17 ?  23  LYS D O   1 
ATOM   3537  C  CB  . LYS D  1 24  ? 18.108  210.961 31.818 1.00 46.38 ?  23  LYS D CB  1 
ATOM   3538  C  CG  . LYS D  1 24  ? 19.152  210.753 30.709 1.00 52.48 ?  23  LYS D CG  1 
ATOM   3539  C  CD  . LYS D  1 24  ? 20.046  209.533 30.986 1.00 61.26 ?  23  LYS D CD  1 
ATOM   3540  C  CE  . LYS D  1 24  ? 21.441  209.687 30.348 1.00 61.83 ?  23  LYS D CE  1 
ATOM   3541  N  NZ  . LYS D  1 24  ? 22.518  210.060 31.337 1.00 67.49 ?  23  LYS D NZ  1 
ATOM   3542  N  N   . GLU D  1 25  ? 15.392  210.426 33.605 1.00 36.63 ?  24  GLU D N   1 
ATOM   3543  C  CA  . GLU D  1 25  ? 14.760  210.229 34.905 1.00 45.49 ?  24  GLU D CA  1 
ATOM   3544  C  C   . GLU D  1 25  ? 13.264  210.023 34.729 1.00 41.75 ?  24  GLU D C   1 
ATOM   3545  O  O   . GLU D  1 25  ? 12.618  210.765 33.983 1.00 38.99 ?  24  GLU D O   1 
ATOM   3546  C  CB  . GLU D  1 25  ? 14.997  211.435 35.818 1.00 45.87 ?  24  GLU D CB  1 
ATOM   3547  C  CG  . GLU D  1 25  ? 16.388  212.014 35.725 1.00 55.99 ?  24  GLU D CG  1 
ATOM   3548  C  CD  . GLU D  1 25  ? 17.051  212.147 37.089 1.00 81.22 ?  24  GLU D CD  1 
ATOM   3549  O  OE1 . GLU D  1 25  ? 18.303  212.071 37.152 1.00 81.39 ?  24  GLU D OE1 1 
ATOM   3550  O  OE2 . GLU D  1 25  ? 16.320  212.330 38.093 1.00 85.00 ?  24  GLU D OE2 1 
ATOM   3551  N  N   . SER D  1 26  ? 12.693  209.062 35.466 1.00 35.09 ?  25  SER D N   1 
ATOM   3552  C  CA  . SER D  1 26  ? 11.289  208.719 35.241 1.00 39.54 ?  25  SER D CA  1 
ATOM   3553  C  C   . SER D  1 26  ? 10.334  209.864 35.578 1.00 40.32 ?  25  SER D C   1 
ATOM   3554  O  O   . SER D  1 26  ? 9.223   209.917 35.042 1.00 43.17 ?  25  SER D O   1 
ATOM   3555  C  CB  . SER D  1 26  ? 10.908  207.474 36.044 1.00 47.29 ?  25  SER D CB  1 
ATOM   3556  O  OG  . SER D  1 26  ? 11.262  207.621 37.402 1.00 47.32 ?  25  SER D OG  1 
ATOM   3557  N  N   . ASN D  1 27  ? 10.725  210.779 36.441 1.00 34.79 ?  26  ASN D N   1 
ATOM   3558  C  CA  . ASN D  1 27  ? 9.900   211.948 36.694 1.00 46.76 ?  26  ASN D CA  1 
ATOM   3559  C  C   . ASN D  1 27  ? 10.253  213.112 35.779 1.00 42.15 ?  26  ASN D C   1 
ATOM   3560  O  O   . ASN D  1 27  ? 9.703   214.206 35.941 1.00 48.94 ?  26  ASN D O   1 
ATOM   3561  C  CB  . ASN D  1 27  ? 10.032  212.360 38.170 1.00 42.53 ?  26  ASN D CB  1 
ATOM   3562  C  CG  . ASN D  1 27  ? 11.412  212.977 38.495 1.00 56.30 ?  26  ASN D CG  1 
ATOM   3563  O  OD1 . ASN D  1 27  ? 12.440  212.513 37.987 1.00 56.72 ?  26  ASN D OD1 1 
ATOM   3564  N  ND2 . ASN D  1 27  ? 11.439  213.979 39.383 1.00 51.61 ?  26  ASN D ND2 1 
ATOM   3565  N  N   . GLY D  1 28  ? 11.155  212.905 34.835 1.00 37.89 ?  27  GLY D N   1 
ATOM   3566  C  CA  . GLY D  1 28  ? 11.715  214.001 34.084 1.00 40.52 ?  27  GLY D CA  1 
ATOM   3567  C  C   . GLY D  1 28  ? 11.163  214.094 32.678 1.00 35.75 ?  27  GLY D C   1 
ATOM   3568  O  O   . GLY D  1 28  ? 10.369  213.259 32.229 1.00 31.75 ?  27  GLY D O   1 
ATOM   3569  N  N   . PRO D  1 29  ? 11.591  215.113 31.948 1.00 36.56 ?  28  PRO D N   1 
ATOM   3570  C  CA  . PRO D  1 29  ? 11.084  215.314 30.590 1.00 34.89 ?  28  PRO D CA  1 
ATOM   3571  C  C   . PRO D  1 29  ? 11.679  214.297 29.626 1.00 31.19 ?  28  PRO D C   1 
ATOM   3572  O  O   . PRO D  1 29  ? 12.708  213.667 29.889 1.00 31.35 ?  28  PRO D O   1 
ATOM   3573  C  CB  . PRO D  1 29  ? 11.540  216.736 30.247 1.00 35.20 ?  28  PRO D CB  1 
ATOM   3574  C  CG  . PRO D  1 29  ? 12.724  216.985 31.104 1.00 43.70 ?  28  PRO D CG  1 
ATOM   3575  C  CD  . PRO D  1 29  ? 12.678  216.044 32.288 1.00 33.60 ?  28  PRO D CD  1 
ATOM   3576  N  N   . VAL D  1 30  ? 10.992  214.134 28.498 1.00 30.02 ?  29  VAL D N   1 
ATOM   3577  C  CA  . VAL D  1 30  ? 11.419  213.247 27.424 1.00 27.39 ?  29  VAL D CA  1 
ATOM   3578  C  C   . VAL D  1 30  ? 11.973  214.117 26.303 1.00 28.49 ?  29  VAL D C   1 
ATOM   3579  O  O   . VAL D  1 30  ? 11.281  215.015 25.807 1.00 27.27 ?  29  VAL D O   1 
ATOM   3580  C  CB  . VAL D  1 30  ? 10.260  212.360 26.929 1.00 26.91 ?  29  VAL D CB  1 
ATOM   3581  C  CG1 . VAL D  1 30  ? 10.710  211.439 25.785 1.00 22.56 ?  29  VAL D CG1 1 
ATOM   3582  C  CG2 . VAL D  1 30  ? 9.691   211.533 28.081 1.00 24.87 ?  29  VAL D CG2 1 
ATOM   3583  N  N   . LYS D  1 31  ? 13.226  213.878 25.922 1.00 29.15 ?  30  LYS D N   1 
ATOM   3584  C  CA  . LYS D  1 31  ? 13.782  214.510 24.731 1.00 30.23 ?  30  LYS D CA  1 
ATOM   3585  C  C   . LYS D  1 31  ? 13.315  213.726 23.515 1.00 32.43 ?  30  LYS D C   1 
ATOM   3586  O  O   . LYS D  1 31  ? 13.337  212.496 23.534 1.00 27.74 ?  30  LYS D O   1 
ATOM   3587  C  CB  . LYS D  1 31  ? 15.311  214.541 24.772 1.00 29.72 ?  30  LYS D CB  1 
ATOM   3588  C  CG  . LYS D  1 31  ? 15.918  214.942 26.131 1.00 47.01 ?  30  LYS D CG  1 
ATOM   3589  C  CD  . LYS D  1 31  ? 17.074  213.979 26.549 1.00 59.65 ?  30  LYS D CD  1 
ATOM   3590  C  CE  . LYS D  1 31  ? 17.271  213.889 28.086 1.00 61.01 ?  30  LYS D CE  1 
ATOM   3591  N  NZ  . LYS D  1 31  ? 16.215  213.121 28.870 1.00 44.48 ?  30  LYS D NZ  1 
ATOM   3592  N  N   . VAL D  1 32  ? 12.868  214.436 22.476 1.00 25.67 ?  31  VAL D N   1 
ATOM   3593  C  CA  . VAL D  1 32  ? 12.364  213.834 21.241 1.00 25.85 ?  31  VAL D CA  1 
ATOM   3594  C  C   . VAL D  1 32  ? 13.144  214.459 20.089 1.00 22.15 ?  31  VAL D C   1 
ATOM   3595  O  O   . VAL D  1 32  ? 13.118  215.682 19.922 1.00 28.49 ?  31  VAL D O   1 
ATOM   3596  C  CB  . VAL D  1 32  ? 10.856  214.083 21.051 1.00 23.76 ?  31  VAL D CB  1 
ATOM   3597  C  CG1 . VAL D  1 32  ? 10.329  213.296 19.844 1.00 20.88 ?  31  VAL D CG1 1 
ATOM   3598  C  CG2 . VAL D  1 32  ? 10.061  213.713 22.297 1.00 26.10 ?  31  VAL D CG2 1 
ATOM   3599  N  N   . TRP D  1 33  ? 13.835  213.639 19.300 1.00 22.24 ?  32  TRP D N   1 
ATOM   3600  C  CA  . TRP D  1 33  ? 14.649  214.211 18.240 1.00 27.31 ?  32  TRP D CA  1 
ATOM   3601  C  C   . TRP D  1 33  ? 14.844  213.207 17.118 1.00 24.43 ?  32  TRP D C   1 
ATOM   3602  O  O   . TRP D  1 33  ? 14.776  211.988 17.315 1.00 25.61 ?  32  TRP D O   1 
ATOM   3603  C  CB  . TRP D  1 33  ? 16.018  214.694 18.757 1.00 25.23 ?  32  TRP D CB  1 
ATOM   3604  C  CG  . TRP D  1 33  ? 17.031  213.589 18.914 1.00 27.01 ?  32  TRP D CG  1 
ATOM   3605  C  CD1 . TRP D  1 33  ? 18.015  213.232 18.034 1.00 27.90 ?  32  TRP D CD1 1 
ATOM   3606  C  CD2 . TRP D  1 33  ? 17.142  212.697 20.021 1.00 26.87 ?  32  TRP D CD2 1 
ATOM   3607  N  NE1 . TRP D  1 33  ? 18.735  212.164 18.530 1.00 31.60 ?  32  TRP D NE1 1 
ATOM   3608  C  CE2 . TRP D  1 33  ? 18.225  211.828 19.757 1.00 28.76 ?  32  TRP D CE2 1 
ATOM   3609  C  CE3 . TRP D  1 33  ? 16.444  212.561 21.226 1.00 34.40 ?  32  TRP D CE3 1 
ATOM   3610  C  CZ2 . TRP D  1 33  ? 18.607  210.822 20.646 1.00 36.99 ?  32  TRP D CZ2 1 
ATOM   3611  C  CZ3 . TRP D  1 33  ? 16.830  211.549 22.114 1.00 32.54 ?  32  TRP D CZ3 1 
ATOM   3612  C  CH2 . TRP D  1 33  ? 17.899  210.701 21.819 1.00 31.04 ?  32  TRP D CH2 1 
ATOM   3613  N  N   . GLY D  1 34  ? 15.079  213.745 15.932 1.00 26.59 ?  33  GLY D N   1 
ATOM   3614  C  CA  . GLY D  1 34  ? 15.355  212.931 14.766 1.00 24.91 ?  33  GLY D CA  1 
ATOM   3615  C  C   . GLY D  1 34  ? 15.041  213.736 13.519 1.00 27.60 ?  33  GLY D C   1 
ATOM   3616  O  O   . GLY D  1 34  ? 14.934  214.957 13.564 1.00 31.96 ?  33  GLY D O   1 
ATOM   3617  N  N   . SER D  1 35  ? 14.877  213.025 12.421 1.00 30.72 ?  34  SER D N   1 
ATOM   3618  C  CA  . SER D  1 35  ? 14.744  213.686 11.136 1.00 31.81 ?  34  SER D CA  1 
ATOM   3619  C  C   . SER D  1 35  ? 13.631  213.003 10.367 1.00 28.85 ?  34  SER D C   1 
ATOM   3620  O  O   . SER D  1 35  ? 13.564  211.770 10.347 1.00 31.28 ?  34  SER D O   1 
ATOM   3621  C  CB  . SER D  1 35  ? 16.069  213.631 10.364 1.00 29.80 ?  34  SER D CB  1 
ATOM   3622  O  OG  . SER D  1 35  ? 15.923  214.164 9.068  1.00 48.79 ?  34  SER D OG  1 
ATOM   3623  N  N   . ILE D  1 36  ? 12.754  213.801 9.756  1.00 26.72 ?  35  ILE D N   1 
ATOM   3624  C  CA  . ILE D  1 36  ? 11.704  213.314 8.869  1.00 23.76 ?  35  ILE D CA  1 
ATOM   3625  C  C   . ILE D  1 36  ? 11.884  214.015 7.530  1.00 28.05 ?  35  ILE D C   1 
ATOM   3626  O  O   . ILE D  1 36  ? 11.955  215.250 7.480  1.00 26.06 ?  35  ILE D O   1 
ATOM   3627  C  CB  . ILE D  1 36  ? 10.294  213.599 9.427  1.00 26.46 ?  35  ILE D CB  1 
ATOM   3628  C  CG1 . ILE D  1 36  ? 10.119  213.114 10.866 1.00 25.83 ?  35  ILE D CG1 1 
ATOM   3629  C  CG2 . ILE D  1 36  ? 9.232   212.950 8.578  1.00 24.11 ?  35  ILE D CG2 1 
ATOM   3630  C  CD1 . ILE D  1 36  ? 8.849   213.685 11.492 1.00 23.80 ?  35  ILE D CD1 1 
ATOM   3631  N  N   . LYS D  1 37  ? 11.952  213.249 6.447  1.00 25.14 ?  36  LYS D N   1 
ATOM   3632  C  CA  . LYS D  1 37  ? 12.078  213.852 5.121  1.00 27.11 ?  36  LYS D CA  1 
ATOM   3633  C  C   . LYS D  1 37  ? 10.752  213.738 4.377  1.00 29.62 ?  36  LYS D C   1 
ATOM   3634  O  O   . LYS D  1 37  ? 9.844   213.014 4.790  1.00 29.08 ?  36  LYS D O   1 
ATOM   3635  C  CB  . LYS D  1 37  ? 13.196  213.178 4.305  1.00 28.41 ?  36  LYS D CB  1 
ATOM   3636  C  CG  . LYS D  1 37  ? 12.843  211.756 3.881  1.00 31.51 ?  36  LYS D CG  1 
ATOM   3637  C  CD  . LYS D  1 37  ? 13.611  211.297 2.632  1.00 45.70 ?  36  LYS D CD  1 
ATOM   3638  C  CE  . LYS D  1 37  ? 12.868  210.207 1.806  1.00 55.52 ?  36  LYS D CE  1 
ATOM   3639  N  NZ  . LYS D  1 37  ? 11.649  210.587 0.946  1.00 37.83 ?  36  LYS D NZ  1 
ATOM   3640  N  N   . GLY D  1 38  ? 10.645  214.451 3.259  1.00 28.60 ?  37  GLY D N   1 
ATOM   3641  C  CA  . GLY D  1 38  ? 9.484   214.315 2.390  1.00 24.85 ?  37  GLY D CA  1 
ATOM   3642  C  C   . GLY D  1 38  ? 8.272   215.143 2.758  1.00 27.59 ?  37  GLY D C   1 
ATOM   3643  O  O   . GLY D  1 38  ? 7.198   214.929 2.174  1.00 24.34 ?  37  GLY D O   1 
ATOM   3644  N  N   . LEU D  1 39  ? 8.413   216.094 3.683  1.00 23.19 ?  38  LEU D N   1 
ATOM   3645  C  CA  . LEU D  1 39  ? 7.305   216.909 4.176  1.00 20.37 ?  38  LEU D CA  1 
ATOM   3646  C  C   . LEU D  1 39  ? 7.227   218.234 3.429  1.00 24.50 ?  38  LEU D C   1 
ATOM   3647  O  O   . LEU D  1 39  ? 8.253   218.833 3.123  1.00 23.55 ?  38  LEU D O   1 
ATOM   3648  C  CB  . LEU D  1 39  ? 7.501   217.209 5.669  1.00 22.52 ?  38  LEU D CB  1 
ATOM   3649  C  CG  . LEU D  1 39  ? 7.367   216.027 6.642  1.00 24.15 ?  38  LEU D CG  1 
ATOM   3650  C  CD1 . LEU D  1 39  ? 7.959   216.381 7.998  1.00 26.14 ?  38  LEU D CD1 1 
ATOM   3651  C  CD2 . LEU D  1 39  ? 5.906   215.682 6.755  1.00 20.34 ?  38  LEU D CD2 1 
ATOM   3652  N  N   . THR D  1 40  ? 6.015   218.728 3.186  1.00 26.12 ?  39  THR D N   1 
ATOM   3653  C  CA  . THR D  1 40  ? 5.927   220.072 2.632  1.00 25.80 ?  39  THR D CA  1 
ATOM   3654  C  C   . THR D  1 40  ? 6.466   221.092 3.632  1.00 29.00 ?  39  THR D C   1 
ATOM   3655  O  O   . THR D  1 40  ? 6.295   220.951 4.845  1.00 23.72 ?  39  THR D O   1 
ATOM   3656  C  CB  . THR D  1 40  ? 4.494   220.438 2.262  1.00 30.36 ?  39  THR D CB  1 
ATOM   3657  O  OG1 . THR D  1 40  ? 3.676   220.403 3.436  1.00 29.64 ?  39  THR D OG1 1 
ATOM   3658  C  CG2 . THR D  1 40  ? 3.932   219.495 1.212  1.00 23.00 ?  39  THR D CG2 1 
ATOM   3659  N  N   . GLU D  1 41  ? 7.116   222.129 3.104  1.00 27.91 ?  40  GLU D N   1 
ATOM   3660  C  CA  . GLU D  1 41  ? 7.733   223.155 3.931  1.00 29.47 ?  40  GLU D CA  1 
ATOM   3661  C  C   . GLU D  1 41  ? 6.729   223.714 4.930  1.00 26.36 ?  40  GLU D C   1 
ATOM   3662  O  O   . GLU D  1 41  ? 5.572   223.970 4.593  1.00 22.97 ?  40  GLU D O   1 
ATOM   3663  C  CB  . GLU D  1 41  ? 8.262   224.280 3.039  1.00 31.72 ?  40  GLU D CB  1 
ATOM   3664  C  CG  . GLU D  1 41  ? 9.163   225.227 3.765  1.00 34.23 ?  40  GLU D CG  1 
ATOM   3665  C  CD  . GLU D  1 41  ? 9.718   226.342 2.868  1.00 52.58 ?  40  GLU D CD  1 
ATOM   3666  O  OE1 . GLU D  1 41  ? 9.504   226.318 1.625  1.00 48.86 ?  40  GLU D OE1 1 
ATOM   3667  O  OE2 . GLU D  1 41  ? 10.406  227.230 3.423  1.00 54.21 ?  40  GLU D OE2 1 
ATOM   3668  N  N   . GLY D  1 42  ? 7.169   223.916 6.162  1.00 23.42 ?  41  GLY D N   1 
ATOM   3669  C  CA  . GLY D  1 42  ? 6.301   224.512 7.149  1.00 21.80 ?  41  GLY D CA  1 
ATOM   3670  C  C   . GLY D  1 42  ? 5.896   223.537 8.242  1.00 24.75 ?  41  GLY D C   1 
ATOM   3671  O  O   . GLY D  1 42  ? 6.528   222.494 8.463  1.00 23.22 ?  41  GLY D O   1 
ATOM   3672  N  N   . LEU D  1 43  ? 4.810   223.892 8.929  1.00 24.05 ?  42  LEU D N   1 
ATOM   3673  C  CA  . LEU D  1 43  ? 4.404   223.217 10.157 1.00 26.96 ?  42  LEU D CA  1 
ATOM   3674  C  C   . LEU D  1 43  ? 3.600   221.959 9.865  1.00 25.37 ?  42  LEU D C   1 
ATOM   3675  O  O   . LEU D  1 43  ? 2.733   221.960 8.987  1.00 27.97 ?  42  LEU D O   1 
ATOM   3676  C  CB  . LEU D  1 43  ? 3.557   224.163 11.020 1.00 23.41 ?  42  LEU D CB  1 
ATOM   3677  C  CG  . LEU D  1 43  ? 4.249   225.416 11.542 1.00 28.12 ?  42  LEU D CG  1 
ATOM   3678  C  CD1 . LEU D  1 43  ? 3.233   226.376 12.141 1.00 31.85 ?  42  LEU D CD1 1 
ATOM   3679  C  CD2 . LEU D  1 43  ? 5.277   225.008 12.568 1.00 25.38 ?  42  LEU D CD2 1 
ATOM   3680  N  N   . HIS D  1 44  ? 3.841   220.910 10.655 1.00 20.40 ?  43  HIS D N   1 
ATOM   3681  C  CA  . HIS D  1 44  ? 3.091   219.657 10.583 1.00 21.29 ?  43  HIS D CA  1 
ATOM   3682  C  C   . HIS D  1 44  ? 2.744   219.170 11.981 1.00 24.57 ?  43  HIS D C   1 
ATOM   3683  O  O   . HIS D  1 44  ? 3.637   219.013 12.817 1.00 22.38 ?  43  HIS D O   1 
ATOM   3684  C  CB  . HIS D  1 44  ? 3.906   218.580 9.869  1.00 20.34 ?  43  HIS D CB  1 
ATOM   3685  C  CG  . HIS D  1 44  ? 4.119   218.875 8.423  1.00 25.86 ?  43  HIS D CG  1 
ATOM   3686  N  ND1 . HIS D  1 44  ? 3.268   218.409 7.444  1.00 26.30 ?  43  HIS D ND1 1 
ATOM   3687  C  CD2 . HIS D  1 44  ? 5.047   219.636 7.794  1.00 20.81 ?  43  HIS D CD2 1 
ATOM   3688  C  CE1 . HIS D  1 44  ? 3.673   218.863 6.266  1.00 30.68 ?  43  HIS D CE1 1 
ATOM   3689  N  NE2 . HIS D  1 44  ? 4.747   219.611 6.450  1.00 24.67 ?  43  HIS D NE2 1 
ATOM   3690  N  N   . GLY D  1 45  ? 1.470   218.888 12.222 1.00 22.94 ?  44  GLY D N   1 
ATOM   3691  C  CA  . GLY D  1 45  ? 1.071   218.228 13.454 1.00 22.40 ?  44  GLY D CA  1 
ATOM   3692  C  C   . GLY D  1 45  ? 1.864   216.964 13.747 1.00 26.31 ?  44  GLY D C   1 
ATOM   3693  O  O   . GLY D  1 45  ? 2.176   216.183 12.847 1.00 23.07 ?  44  GLY D O   1 
ATOM   3694  N  N   . PHE D  1 46  ? 2.171   216.742 15.025 1.00 22.72 ?  45  PHE D N   1 
ATOM   3695  C  CA  . PHE D  1 46  ? 3.135   215.714 15.433 1.00 20.34 ?  45  PHE D CA  1 
ATOM   3696  C  C   . PHE D  1 46  ? 2.601   215.143 16.747 1.00 25.51 ?  45  PHE D C   1 
ATOM   3697  O  O   . PHE D  1 46  ? 2.682   215.812 17.780 1.00 23.82 ?  45  PHE D O   1 
ATOM   3698  C  CB  . PHE D  1 46  ? 4.512   216.352 15.579 1.00 20.34 ?  45  PHE D CB  1 
ATOM   3699  C  CG  . PHE D  1 46  ? 5.640   215.395 15.864 1.00 22.22 ?  45  PHE D CG  1 
ATOM   3700  C  CD1 . PHE D  1 46  ? 6.092   214.505 14.899 1.00 25.55 ?  45  PHE D CD1 1 
ATOM   3701  C  CD2 . PHE D  1 46  ? 6.300   215.435 17.093 1.00 23.63 ?  45  PHE D CD2 1 
ATOM   3702  C  CE1 . PHE D  1 46  ? 7.159   213.651 15.168 1.00 20.34 ?  45  PHE D CE1 1 
ATOM   3703  C  CE2 . PHE D  1 46  ? 7.355   214.582 17.354 1.00 22.62 ?  45  PHE D CE2 1 
ATOM   3704  C  CZ  . PHE D  1 46  ? 7.779   213.689 16.386 1.00 24.45 ?  45  PHE D CZ  1 
ATOM   3705  N  N   . HIS D  1 47  ? 1.983   213.959 16.698 1.00 20.34 ?  46  HIS D N   1 
ATOM   3706  C  CA  . HIS D  1 47  ? 1.206   213.507 17.848 1.00 25.30 ?  46  HIS D CA  1 
ATOM   3707  C  C   . HIS D  1 47  ? 1.438   212.036 18.136 1.00 28.57 ?  46  HIS D C   1 
ATOM   3708  O  O   . HIS D  1 47  ? 1.707   211.240 17.223 1.00 23.30 ?  46  HIS D O   1 
ATOM   3709  C  CB  . HIS D  1 47  ? -0.302  213.702 17.650 1.00 24.74 ?  46  HIS D CB  1 
ATOM   3710  C  CG  . HIS D  1 47  ? -0.683  215.062 17.153 1.00 26.56 ?  46  HIS D CG  1 
ATOM   3711  N  ND1 . HIS D  1 47  ? -1.311  215.255 15.944 1.00 27.45 ?  46  HIS D ND1 1 
ATOM   3712  C  CD2 . HIS D  1 47  ? -0.527  216.290 17.699 1.00 26.91 ?  46  HIS D CD2 1 
ATOM   3713  C  CE1 . HIS D  1 47  ? -1.521  216.547 15.759 1.00 28.69 ?  46  HIS D CE1 1 
ATOM   3714  N  NE2 . HIS D  1 47  ? -1.047  217.200 16.804 1.00 24.30 ?  46  HIS D NE2 1 
ATOM   3715  N  N   . VAL D  1 48  ? 1.280   211.674 19.406 1.00 20.34 ?  47  VAL D N   1 
ATOM   3716  C  CA  . VAL D  1 48  ? 1.195   210.273 19.790 1.00 22.66 ?  47  VAL D CA  1 
ATOM   3717  C  C   . VAL D  1 48  ? -0.278  209.897 19.786 1.00 24.81 ?  47  VAL D C   1 
ATOM   3718  O  O   . VAL D  1 48  ? -1.101  210.546 20.441 1.00 27.93 ?  47  VAL D O   1 
ATOM   3719  C  CB  . VAL D  1 48  ? 1.839   210.000 21.162 1.00 20.34 ?  47  VAL D CB  1 
ATOM   3720  C  CG1 . VAL D  1 48  ? 1.734   208.499 21.471 1.00 24.89 ?  47  VAL D CG1 1 
ATOM   3721  C  CG2 . VAL D  1 48  ? 3.302   210.433 21.169 1.00 20.34 ?  47  VAL D CG2 1 
ATOM   3722  N  N   . HIS D  1 49  ? -0.620  208.901 19.000 1.00 21.33 ?  48  HIS D N   1 
ATOM   3723  C  CA  . HIS D  1 49  ? -1.979  208.394 18.947 1.00 24.00 ?  48  HIS D CA  1 
ATOM   3724  C  C   . HIS D  1 49  ? -2.078  207.171 19.851 1.00 22.62 ?  48  HIS D C   1 
ATOM   3725  O  O   . HIS D  1 49  ? -1.075  206.557 20.210 1.00 23.73 ?  48  HIS D O   1 
ATOM   3726  C  CB  . HIS D  1 49  ? -2.374  208.063 17.496 1.00 20.34 ?  48  HIS D CB  1 
ATOM   3727  C  CG  . HIS D  1 49  ? -2.577  209.275 16.630 1.00 24.91 ?  48  HIS D CG  1 
ATOM   3728  N  ND1 . HIS D  1 49  ? -3.786  209.572 16.037 1.00 23.19 ?  48  HIS D ND1 1 
ATOM   3729  C  CD2 . HIS D  1 49  ? -1.727  210.270 16.273 1.00 20.34 ?  48  HIS D CD2 1 
ATOM   3730  C  CE1 . HIS D  1 49  ? -3.671  210.694 15.343 1.00 22.16 ?  48  HIS D CE1 1 
ATOM   3731  N  NE2 . HIS D  1 49  ? -2.432  211.132 15.464 1.00 20.34 ?  48  HIS D NE2 1 
ATOM   3732  N  N   . GLU D  1 50  ? -3.314  206.796 20.179 1.00 24.80 ?  49  GLU D N   1 
ATOM   3733  C  CA  . GLU D  1 50  ? -3.546  205.874 21.290 1.00 22.49 ?  49  GLU D CA  1 
ATOM   3734  C  C   . GLU D  1 50  ? -3.027  204.456 21.021 1.00 23.66 ?  49  GLU D C   1 
ATOM   3735  O  O   . GLU D  1 50  ? -2.451  203.834 21.916 1.00 29.06 ?  49  GLU D O   1 
ATOM   3736  C  CB  . GLU D  1 50  ? -5.040  205.843 21.617 1.00 25.06 ?  49  GLU D CB  1 
ATOM   3737  C  CG  . GLU D  1 50  ? -5.381  204.891 22.766 1.00 30.12 ?  49  GLU D CG  1 
ATOM   3738  C  CD  . GLU D  1 50  ? -6.837  205.003 23.198 1.00 37.01 ?  49  GLU D CD  1 
ATOM   3739  O  OE1 . GLU D  1 50  ? -7.628  205.657 22.475 1.00 34.30 ?  49  GLU D OE1 1 
ATOM   3740  O  OE2 . GLU D  1 50  ? -7.180  204.428 24.254 1.00 40.38 ?  49  GLU D OE2 1 
ATOM   3741  N  N   . PHE D  1 51  ? -3.254  203.893 19.838 1.00 23.96 ?  50  PHE D N   1 
ATOM   3742  C  CA  . PHE D  1 51  ? -2.967  202.480 19.623 1.00 24.16 ?  50  PHE D CA  1 
ATOM   3743  C  C   . PHE D  1 51  ? -1.734  202.275 18.756 1.00 26.93 ?  50  PHE D C   1 
ATOM   3744  O  O   . PHE D  1 51  ? -1.541  202.980 17.765 1.00 24.71 ?  50  PHE D O   1 
ATOM   3745  C  CB  . PHE D  1 51  ? -4.172  201.774 18.992 1.00 27.03 ?  50  PHE D CB  1 
ATOM   3746  C  CG  . PHE D  1 51  ? -5.430  201.980 19.759 1.00 28.37 ?  50  PHE D CG  1 
ATOM   3747  C  CD1 . PHE D  1 51  ? -5.545  201.490 21.049 1.00 28.63 ?  50  PHE D CD1 1 
ATOM   3748  C  CD2 . PHE D  1 51  ? -6.480  202.708 19.223 1.00 33.93 ?  50  PHE D CD2 1 
ATOM   3749  C  CE1 . PHE D  1 51  ? -6.697  201.709 21.781 1.00 35.59 ?  50  PHE D CE1 1 
ATOM   3750  C  CE2 . PHE D  1 51  ? -7.634  202.929 19.956 1.00 32.22 ?  50  PHE D CE2 1 
ATOM   3751  C  CZ  . PHE D  1 51  ? -7.738  202.428 21.234 1.00 30.79 ?  50  PHE D CZ  1 
ATOM   3752  N  N   . GLY D  1 52  ? -0.914  201.288 19.130 1.00 23.96 ?  51  GLY D N   1 
ATOM   3753  C  CA  . GLY D  1 52  ? 0.218   200.863 18.327 1.00 22.22 ?  51  GLY D CA  1 
ATOM   3754  C  C   . GLY D  1 52  ? -0.227  199.837 17.305 1.00 27.29 ?  51  GLY D C   1 
ATOM   3755  O  O   . GLY D  1 52  ? 0.364   198.757 17.168 1.00 25.78 ?  51  GLY D O   1 
ATOM   3756  N  N   . ASP D  1 53  ? -1.304  200.165 16.604 1.00 27.49 ?  52  ASP D N   1 
ATOM   3757  C  CA  . ASP D  1 53  ? -1.981  199.261 15.678 1.00 22.60 ?  52  ASP D CA  1 
ATOM   3758  C  C   . ASP D  1 53  ? -1.803  199.836 14.288 1.00 27.62 ?  52  ASP D C   1 
ATOM   3759  O  O   . ASP D  1 53  ? -2.393  200.873 13.966 1.00 28.08 ?  52  ASP D O   1 
ATOM   3760  C  CB  . ASP D  1 53  ? -3.459  199.138 16.030 1.00 22.55 ?  52  ASP D CB  1 
ATOM   3761  C  CG  . ASP D  1 53  ? -4.220  198.142 15.138 1.00 29.08 ?  52  ASP D CG  1 
ATOM   3762  O  OD1 . ASP D  1 53  ? -3.810  197.882 13.983 1.00 29.02 ?  52  ASP D OD1 1 
ATOM   3763  O  OD2 . ASP D  1 53  ? -5.250  197.611 15.612 1.00 31.23 ?  52  ASP D OD2 1 
ATOM   3764  N  N   . ASN D  1 54  ? -1.006  199.157 13.465 1.00 26.14 ?  53  ASN D N   1 
ATOM   3765  C  CA  . ASN D  1 54  ? -0.758  199.562 12.085 1.00 25.55 ?  53  ASN D CA  1 
ATOM   3766  C  C   . ASN D  1 54  ? -1.450  198.641 11.077 1.00 31.55 ?  53  ASN D C   1 
ATOM   3767  O  O   . ASN D  1 54  ? -1.104  198.655 9.896  1.00 29.65 ?  53  ASN D O   1 
ATOM   3768  C  CB  . ASN D  1 54  ? 0.746   199.591 11.812 1.00 34.02 ?  53  ASN D CB  1 
ATOM   3769  C  CG  . ASN D  1 54  ? 1.096   200.304 10.496 1.00 48.77 ?  53  ASN D CG  1 
ATOM   3770  O  OD1 . ASN D  1 54  ? 0.527   201.346 10.160 1.00 51.18 ?  53  ASN D OD1 1 
ATOM   3771  N  ND2 . ASN D  1 54  ? 2.002   199.703 9.719  1.00 48.59 ?  53  ASN D ND2 1 
ATOM   3772  N  N   . THR D  1 55  ? -2.417  197.833 11.519 1.00 27.30 ?  54  THR D N   1 
ATOM   3773  C  CA  . THR D  1 55  ? -2.999  196.833 10.620 1.00 27.25 ?  54  THR D CA  1 
ATOM   3774  C  C   . THR D  1 55  ? -3.668  197.476 9.418  1.00 30.95 ?  54  THR D C   1 
ATOM   3775  O  O   . THR D  1 55  ? -3.665  196.898 8.338  1.00 30.98 ?  54  THR D O   1 
ATOM   3776  C  CB  . THR D  1 55  ? -4.008  195.950 11.355 1.00 27.99 ?  54  THR D CB  1 
ATOM   3777  O  OG1 . THR D  1 55  ? -5.029  196.764 11.944 1.00 29.64 ?  54  THR D OG1 1 
ATOM   3778  C  CG2 . THR D  1 55  ? -3.312  195.126 12.471 1.00 27.02 ?  54  THR D CG2 1 
ATOM   3779  N  N   . ALA D  1 56  ? -4.230  198.668 9.571  1.00 31.19 ?  55  ALA D N   1 
ATOM   3780  C  CA  . ALA D  1 56  ? -4.750  199.364 8.401  1.00 33.22 ?  55  ALA D CA  1 
ATOM   3781  C  C   . ALA D  1 56  ? -3.989  200.667 8.220  1.00 33.36 ?  55  ALA D C   1 
ATOM   3782  O  O   . ALA D  1 56  ? -4.593  201.729 8.064  1.00 37.07 ?  55  ALA D O   1 
ATOM   3783  C  CB  . ALA D  1 56  ? -6.255  199.615 8.550  1.00 33.62 ?  55  ALA D CB  1 
ATOM   3784  N  N   . GLY D  1 57  ? -2.663  200.607 8.286  1.00 35.63 ?  56  GLY D N   1 
ATOM   3785  C  CA  . GLY D  1 57  ? -1.922  201.851 8.170  1.00 36.99 ?  56  GLY D CA  1 
ATOM   3786  C  C   . GLY D  1 57  ? -2.154  202.767 9.371  1.00 35.77 ?  56  GLY D C   1 
ATOM   3787  O  O   . GLY D  1 57  ? -2.558  202.344 10.462 1.00 31.49 ?  56  GLY D O   1 
ATOM   3788  N  N   . CYS D  1 58  ? -1.896  204.056 9.145  1.00 32.76 ?  57  CYS D N   1 
ATOM   3789  C  CA  . CYS D  1 58  ? -1.957  205.034 10.226 1.00 28.97 ?  57  CYS D CA  1 
ATOM   3790  C  C   . CYS D  1 58  ? -3.364  205.189 10.785 1.00 30.10 ?  57  CYS D C   1 
ATOM   3791  O  O   . CYS D  1 58  ? -3.520  205.598 11.946 1.00 27.30 ?  57  CYS D O   1 
ATOM   3792  C  CB  . CYS D  1 58  ? -1.397  206.369 9.714  1.00 30.63 ?  57  CYS D CB  1 
ATOM   3793  S  SG  . CYS D  1 58  ? 0.365   206.210 9.212  1.00 39.45 ?  57  CYS D SG  1 
ATOM   3794  N  N   . THR D  1 59  ? -4.383  204.825 9.998  1.00 28.24 ?  58  THR D N   1 
ATOM   3795  C  CA  . THR D  1 59  ? -5.778  204.963 10.423 1.00 32.88 ?  58  THR D CA  1 
ATOM   3796  C  C   . THR D  1 59  ? -6.076  204.150 11.679 1.00 31.81 ?  58  THR D C   1 
ATOM   3797  O  O   . THR D  1 59  ? -6.820  204.595 12.567 1.00 32.27 ?  58  THR D O   1 
ATOM   3798  C  CB  . THR D  1 59  ? -6.698  204.505 9.293  1.00 34.56 ?  58  THR D CB  1 
ATOM   3799  O  OG1 . THR D  1 59  ? -6.164  204.965 8.053  1.00 43.26 ?  58  THR D OG1 1 
ATOM   3800  C  CG2 . THR D  1 59  ? -8.096  205.040 9.489  1.00 39.05 ?  58  THR D CG2 1 
ATOM   3801  N  N   . SER D  1 60  ? -5.523  202.954 11.771 1.00 28.01 ?  59  SER D N   1 
ATOM   3802  C  CA  . SER D  1 60  ? -5.856  202.115 12.914 1.00 28.52 ?  59  SER D CA  1 
ATOM   3803  C  C   . SER D  1 60  ? -5.141  202.546 14.187 1.00 25.73 ?  59  SER D C   1 
ATOM   3804  O  O   . SER D  1 60  ? -5.324  201.905 15.229 1.00 30.05 ?  59  SER D O   1 
ATOM   3805  C  CB  . SER D  1 60  ? -5.533  200.655 12.602 1.00 28.53 ?  59  SER D CB  1 
ATOM   3806  O  OG  . SER D  1 60  ? -4.355  200.578 11.851 1.00 32.58 ?  59  SER D OG  1 
ATOM   3807  N  N   . ALA D  1 61  ? -4.350  203.617 14.145 1.00 24.29 ?  60  ALA D N   1 
ATOM   3808  C  CA  . ALA D  1 61  ? -3.761  204.088 15.399 1.00 28.81 ?  60  ALA D CA  1 
ATOM   3809  C  C   . ALA D  1 61  ? -4.776  204.785 16.304 1.00 24.82 ?  60  ALA D C   1 
ATOM   3810  O  O   . ALA D  1 61  ? -4.466  205.074 17.465 1.00 25.67 ?  60  ALA D O   1 
ATOM   3811  C  CB  . ALA D  1 61  ? -2.587  205.019 15.111 1.00 23.94 ?  60  ALA D CB  1 
ATOM   3812  N  N   . GLY D  1 62  ? -5.980  205.056 15.820 1.00 27.82 ?  61  GLY D N   1 
ATOM   3813  C  CA  . GLY D  1 62  ? -6.984  205.690 16.648 1.00 24.17 ?  61  GLY D CA  1 
ATOM   3814  C  C   . GLY D  1 62  ? -6.717  207.171 16.857 1.00 25.95 ?  61  GLY D C   1 
ATOM   3815  O  O   . GLY D  1 62  ? -5.979  207.801 16.097 1.00 25.26 ?  61  GLY D O   1 
ATOM   3816  N  N   . PRO D  1 63  ? -7.309  207.745 17.894 1.00 25.63 ?  62  PRO D N   1 
ATOM   3817  C  CA  . PRO D  1 63  ? -7.179  209.181 18.139 1.00 27.81 ?  62  PRO D CA  1 
ATOM   3818  C  C   . PRO D  1 63  ? -5.898  209.490 18.910 1.00 25.95 ?  62  PRO D C   1 
ATOM   3819  O  O   . PRO D  1 63  ? -5.111  208.596 19.221 1.00 24.53 ?  62  PRO D O   1 
ATOM   3820  C  CB  . PRO D  1 63  ? -8.417  209.489 18.976 1.00 26.42 ?  62  PRO D CB  1 
ATOM   3821  C  CG  . PRO D  1 63  ? -8.570  208.222 19.826 1.00 28.77 ?  62  PRO D CG  1 
ATOM   3822  C  CD  . PRO D  1 63  ? -8.133  207.078 18.917 1.00 24.78 ?  62  PRO D CD  1 
ATOM   3823  N  N   . HIS D  1 64  ? -5.704  210.769 19.212 1.00 22.55 ?  63  HIS D N   1 
ATOM   3824  C  CA  . HIS D  1 64  ? -4.575  211.177 20.043 1.00 23.93 ?  63  HIS D CA  1 
ATOM   3825  C  C   . HIS D  1 64  ? -4.611  210.450 21.385 1.00 25.64 ?  63  HIS D C   1 
ATOM   3826  O  O   . HIS D  1 64  ? -5.671  210.270 21.978 1.00 27.30 ?  63  HIS D O   1 
ATOM   3827  C  CB  . HIS D  1 64  ? -4.613  212.684 20.270 1.00 25.37 ?  63  HIS D CB  1 
ATOM   3828  C  CG  . HIS D  1 64  ? -4.429  213.487 19.023 1.00 27.18 ?  63  HIS D CG  1 
ATOM   3829  N  ND1 . HIS D  1 64  ? -4.343  214.859 19.037 1.00 28.58 ?  63  HIS D ND1 1 
ATOM   3830  C  CD2 . HIS D  1 64  ? -4.299  213.115 17.726 1.00 29.21 ?  63  HIS D CD2 1 
ATOM   3831  C  CE1 . HIS D  1 64  ? -4.172  215.303 17.801 1.00 27.52 ?  63  HIS D CE1 1 
ATOM   3832  N  NE2 . HIS D  1 64  ? -4.137  214.263 16.987 1.00 23.86 ?  63  HIS D NE2 1 
ATOM   3833  N  N   . PHE D  1 65  ? -3.443  210.021 21.858 1.00 23.62 ?  64  PHE D N   1 
ATOM   3834  C  CA  . PHE D  1 65  ? -3.346  209.402 23.171 1.00 24.78 ?  64  PHE D CA  1 
ATOM   3835  C  C   . PHE D  1 65  ? -3.829  210.392 24.223 1.00 28.38 ?  64  PHE D C   1 
ATOM   3836  O  O   . PHE D  1 65  ? -3.242  211.468 24.392 1.00 25.50 ?  64  PHE D O   1 
ATOM   3837  C  CB  . PHE D  1 65  ? -1.895  208.989 23.430 1.00 20.49 ?  64  PHE D CB  1 
ATOM   3838  C  CG  . PHE D  1 65  ? -1.677  208.294 24.740 1.00 27.48 ?  64  PHE D CG  1 
ATOM   3839  C  CD1 . PHE D  1 65  ? -2.591  207.385 25.237 1.00 22.94 ?  64  PHE D CD1 1 
ATOM   3840  C  CD2 . PHE D  1 65  ? -0.538  208.578 25.497 1.00 28.06 ?  64  PHE D CD2 1 
ATOM   3841  C  CE1 . PHE D  1 65  ? -2.372  206.764 26.464 1.00 27.29 ?  64  PHE D CE1 1 
ATOM   3842  C  CE2 . PHE D  1 65  ? -0.308  207.962 26.703 1.00 26.77 ?  64  PHE D CE2 1 
ATOM   3843  C  CZ  . PHE D  1 65  ? -1.229  207.039 27.193 1.00 26.53 ?  64  PHE D CZ  1 
ATOM   3844  N  N   . ASN D  1 66  ? -4.921  210.053 24.903 1.00 25.06 ?  65  ASN D N   1 
ATOM   3845  C  CA  . ASN D  1 66  ? -5.621  211.009 25.768 1.00 27.53 ?  65  ASN D CA  1 
ATOM   3846  C  C   . ASN D  1 66  ? -6.155  210.307 27.010 1.00 30.23 ?  65  ASN D C   1 
ATOM   3847  O  O   . ASN D  1 66  ? -7.361  210.258 27.247 1.00 30.57 ?  65  ASN D O   1 
ATOM   3848  C  CB  . ASN D  1 66  ? -6.752  211.683 24.986 1.00 24.14 ?  65  ASN D CB  1 
ATOM   3849  C  CG  . ASN D  1 66  ? -7.465  212.778 25.782 1.00 29.12 ?  65  ASN D CG  1 
ATOM   3850  O  OD1 . ASN D  1 66  ? -6.932  213.323 26.750 1.00 29.47 ?  65  ASN D OD1 1 
ATOM   3851  N  ND2 . ASN D  1 66  ? -8.675  213.107 25.357 1.00 30.75 ?  65  ASN D ND2 1 
ATOM   3852  N  N   . PRO D  1 67  ? -5.274  209.767 27.846 1.00 27.86 ?  66  PRO D N   1 
ATOM   3853  C  CA  . PRO D  1 67  ? -5.760  209.005 29.005 1.00 36.09 ?  66  PRO D CA  1 
ATOM   3854  C  C   . PRO D  1 67  ? -6.490  209.846 30.030 1.00 38.08 ?  66  PRO D C   1 
ATOM   3855  O  O   . PRO D  1 67  ? -7.240  209.281 30.823 1.00 39.87 ?  66  PRO D O   1 
ATOM   3856  C  CB  . PRO D  1 67  ? -4.483  208.397 29.598 1.00 29.73 ?  66  PRO D CB  1 
ATOM   3857  C  CG  . PRO D  1 67  ? -3.391  209.295 29.151 1.00 30.02 ?  66  PRO D CG  1 
ATOM   3858  C  CD  . PRO D  1 67  ? -3.801  209.836 27.802 1.00 27.32 ?  66  PRO D CD  1 
ATOM   3859  N  N   . LEU D  1 68  ? -6.324  211.168 30.043 1.00 32.33 ?  67  LEU D N   1 
ATOM   3860  C  CA  . LEU D  1 68  ? -7.062  212.021 30.979 1.00 35.47 ?  67  LEU D CA  1 
ATOM   3861  C  C   . LEU D  1 68  ? -8.321  212.629 30.377 1.00 37.84 ?  67  LEU D C   1 
ATOM   3862  O  O   . LEU D  1 68  ? -8.933  213.499 31.003 1.00 40.68 ?  67  LEU D O   1 
ATOM   3863  C  CB  . LEU D  1 68  ? -6.153  213.135 31.507 1.00 34.14 ?  67  LEU D CB  1 
ATOM   3864  C  CG  . LEU D  1 68  ? -4.848  212.648 32.153 1.00 37.30 ?  67  LEU D CG  1 
ATOM   3865  C  CD1 . LEU D  1 68  ? -4.185  213.750 32.976 1.00 40.39 ?  67  LEU D CD1 1 
ATOM   3866  C  CD2 . LEU D  1 68  ? -5.132  211.452 33.046 1.00 43.21 ?  67  LEU D CD2 1 
ATOM   3867  N  N   . SER D  1 69  ? -8.705  212.219 29.173 1.00 31.95 ?  68  SER D N   1 
ATOM   3868  C  CA  . SER D  1 69  ? -9.921  212.712 28.512 1.00 38.48 ?  68  SER D CA  1 
ATOM   3869  C  C   . SER D  1 69  ? -10.007 214.245 28.496 1.00 40.35 ?  68  SER D C   1 
ATOM   3870  O  O   . SER D  1 69  ? -11.043 214.830 28.818 1.00 41.02 ?  68  SER D O   1 
ATOM   3871  C  CB  . SER D  1 69  ? -11.177 212.115 29.163 1.00 41.40 ?  68  SER D CB  1 
ATOM   3872  O  OG  . SER D  1 69  ? -11.270 210.722 28.925 1.00 55.37 ?  68  SER D OG  1 
ATOM   3873  N  N   . ARG D  1 70  ? -8.907  214.905 28.129 1.00 34.84 ?  69  ARG D N   1 
ATOM   3874  C  CA  A ARG D  1 70  ? -8.876  216.353 27.981 0.50 34.46 ?  69  ARG D CA  1 
ATOM   3875  C  CA  B ARG D  1 70  ? -8.915  216.353 27.993 0.50 34.28 ?  69  ARG D CA  1 
ATOM   3876  C  C   . ARG D  1 70  ? -9.151  216.735 26.535 1.00 33.60 ?  69  ARG D C   1 
ATOM   3877  O  O   . ARG D  1 70  ? -9.208  215.882 25.644 1.00 34.21 ?  69  ARG D O   1 
ATOM   3878  C  CB  A ARG D  1 70  ? -7.523  216.922 28.397 0.50 33.07 ?  69  ARG D CB  1 
ATOM   3879  C  CB  B ARG D  1 70  ? -7.605  216.957 28.522 0.50 33.14 ?  69  ARG D CB  1 
ATOM   3880  C  CG  A ARG D  1 70  ? -7.038  216.466 29.743 0.50 34.85 ?  69  ARG D CG  1 
ATOM   3881  C  CG  B ARG D  1 70  ? -7.277  216.540 29.960 0.50 34.88 ?  69  ARG D CG  1 
ATOM   3882  C  CD  A ARG D  1 70  ? -7.963  216.919 30.845 0.50 34.22 ?  69  ARG D CD  1 
ATOM   3883  C  CD  B ARG D  1 70  ? -6.224  217.433 30.650 0.50 33.99 ?  69  ARG D CD  1 
ATOM   3884  N  NE  A ARG D  1 70  ? -7.472  216.432 32.124 0.50 37.39 ?  69  ARG D NE  1 
ATOM   3885  N  NE  B ARG D  1 70  ? -6.156  217.149 32.083 0.50 32.69 ?  69  ARG D NE  1 
ATOM   3886  C  CZ  A ARG D  1 70  ? -8.244  215.966 33.094 0.50 35.77 ?  69  ARG D CZ  1 
ATOM   3887  C  CZ  B ARG D  1 70  ? -5.215  217.586 32.911 0.50 30.37 ?  69  ARG D CZ  1 
ATOM   3888  N  NH1 A ARG D  1 70  ? -9.564  215.981 32.994 0.50 35.02 ?  69  ARG D NH1 1 
ATOM   3889  N  NH1 B ARG D  1 70  ? -4.230  218.364 32.497 0.50 32.53 ?  69  ARG D NH1 1 
ATOM   3890  N  NH2 A ARG D  1 70  ? -7.678  215.466 34.184 0.50 30.50 ?  69  ARG D NH2 1 
ATOM   3891  N  NH2 B ARG D  1 70  ? -5.263  217.231 34.191 0.50 32.31 ?  69  ARG D NH2 1 
ATOM   3892  N  N   . LYS D  1 71  ? -9.322  218.039 26.306 1.00 31.16 ?  70  LYS D N   1 
ATOM   3893  C  CA  . LYS D  1 71  ? -9.441  218.548 24.946 1.00 33.64 ?  70  LYS D CA  1 
ATOM   3894  C  C   . LYS D  1 71  ? -8.045  218.683 24.323 1.00 33.31 ?  70  LYS D C   1 
ATOM   3895  O  O   . LYS D  1 71  ? -7.023  218.699 25.022 1.00 28.69 ?  70  LYS D O   1 
ATOM   3896  C  CB  . LYS D  1 71  ? -10.157 219.907 24.913 1.00 36.34 ?  70  LYS D CB  1 
ATOM   3897  C  CG  . LYS D  1 71  ? -11.634 219.903 25.347 1.00 44.10 ?  70  LYS D CG  1 
ATOM   3898  C  CD  . LYS D  1 71  ? -12.432 218.784 24.662 1.00 45.55 ?  70  LYS D CD  1 
ATOM   3899  C  CE  . LYS D  1 71  ? -13.654 218.351 25.506 1.00 50.40 ?  70  LYS D CE  1 
ATOM   3900  N  NZ  . LYS D  1 71  ? -13.545 216.920 26.007 1.00 57.16 ?  70  LYS D NZ  1 
ATOM   3901  N  N   . HIS D  1 72  ? -8.007  218.804 22.996 1.00 31.84 ?  71  HIS D N   1 
ATOM   3902  C  CA  . HIS D  1 72  ? -6.736  218.968 22.296 1.00 30.08 ?  71  HIS D CA  1 
ATOM   3903  C  C   . HIS D  1 72  ? -6.127  220.339 22.596 1.00 31.20 ?  71  HIS D C   1 
ATOM   3904  O  O   . HIS D  1 72  ? -6.832  221.347 22.665 1.00 28.75 ?  71  HIS D O   1 
ATOM   3905  C  CB  . HIS D  1 72  ? -6.942  218.807 20.786 1.00 29.76 ?  71  HIS D CB  1 
ATOM   3906  C  CG  . HIS D  1 72  ? -5.704  219.058 19.981 1.00 28.12 ?  71  HIS D CG  1 
ATOM   3907  N  ND1 . HIS D  1 72  ? -4.675  218.139 19.890 1.00 28.09 ?  71  HIS D ND1 1 
ATOM   3908  C  CD2 . HIS D  1 72  ? -5.321  220.124 19.243 1.00 28.69 ?  71  HIS D CD2 1 
ATOM   3909  C  CE1 . HIS D  1 72  ? -3.717  218.629 19.128 1.00 26.82 ?  71  HIS D CE1 1 
ATOM   3910  N  NE2 . HIS D  1 72  ? -4.079  219.839 18.731 1.00 30.08 ?  71  HIS D NE2 1 
ATOM   3911  N  N   . GLY D  1 73  ? -4.806  220.382 22.768 1.00 27.14 ?  72  GLY D N   1 
ATOM   3912  C  CA  . GLY D  1 73  ? -4.141  221.651 22.992 1.00 26.19 ?  72  GLY D CA  1 
ATOM   3913  C  C   . GLY D  1 73  ? -2.732  221.571 22.452 1.00 30.34 ?  72  GLY D C   1 
ATOM   3914  O  O   . GLY D  1 73  ? -2.337  220.569 21.852 1.00 26.53 ?  72  GLY D O   1 
ATOM   3915  N  N   . GLY D  1 74  ? -1.972  222.637 22.654 1.00 23.85 ?  73  GLY D N   1 
ATOM   3916  C  CA  . GLY D  1 74  ? -0.564  222.592 22.347 1.00 24.98 ?  73  GLY D CA  1 
ATOM   3917  C  C   . GLY D  1 74  ? 0.189   222.013 23.512 1.00 26.94 ?  73  GLY D C   1 
ATOM   3918  O  O   . GLY D  1 74  ? -0.344  221.868 24.621 1.00 30.00 ?  73  GLY D O   1 
ATOM   3919  N  N   . PRO D  1 75  ? 1.463   221.664 23.287 1.00 24.04 ?  74  PRO D N   1 
ATOM   3920  C  CA  . PRO D  1 75  ? 2.214   220.973 24.350 1.00 24.71 ?  74  PRO D CA  1 
ATOM   3921  C  C   . PRO D  1 75  ? 2.426   221.822 25.586 1.00 28.74 ?  74  PRO D C   1 
ATOM   3922  O  O   . PRO D  1 75  ? 2.594   221.267 26.673 1.00 28.27 ?  74  PRO D O   1 
ATOM   3923  C  CB  . PRO D  1 75  ? 3.550   220.608 23.676 1.00 24.55 ?  74  PRO D CB  1 
ATOM   3924  C  CG  . PRO D  1 75  ? 3.601   221.443 22.409 1.00 23.13 ?  74  PRO D CG  1 
ATOM   3925  C  CD  . PRO D  1 75  ? 2.183   221.654 21.998 1.00 21.76 ?  74  PRO D CD  1 
ATOM   3926  N  N   . LYS D  1 76  ? 2.392   223.147 25.453 1.00 26.11 ?  75  LYS D N   1 
ATOM   3927  C  CA  . LYS D  1 76  ? 2.539   224.075 26.576 1.00 31.24 ?  75  LYS D CA  1 
ATOM   3928  C  C   . LYS D  1 76  ? 1.250   224.293 27.356 1.00 32.24 ?  75  LYS D C   1 
ATOM   3929  O  O   . LYS D  1 76  ? 1.287   224.939 28.405 1.00 31.18 ?  75  LYS D O   1 
ATOM   3930  C  CB  . LYS D  1 76  ? 3.014   225.440 26.065 1.00 35.10 ?  75  LYS D CB  1 
ATOM   3931  C  CG  . LYS D  1 76  ? 4.492   225.508 25.766 1.00 37.28 ?  75  LYS D CG  1 
ATOM   3932  C  CD  . LYS D  1 76  ? 4.811   226.613 24.749 1.00 52.29 ?  75  LYS D CD  1 
ATOM   3933  C  CE  . LYS D  1 76  ? 5.269   227.897 25.458 1.00 47.33 ?  75  LYS D CE  1 
ATOM   3934  N  NZ  . LYS D  1 76  ? 4.975   229.131 24.668 1.00 47.96 ?  75  LYS D NZ  1 
ATOM   3935  N  N   . ASP D  1 77  ? 0.109   223.843 26.840 1.00 29.15 ?  76  ASP D N   1 
ATOM   3936  C  CA  . ASP D  1 77  ? -1.160  224.042 27.522 1.00 30.55 ?  76  ASP D CA  1 
ATOM   3937  C  C   . ASP D  1 77  ? -1.325  223.018 28.632 1.00 36.00 ?  76  ASP D C   1 
ATOM   3938  O  O   . ASP D  1 77  ? -0.870  221.876 28.521 1.00 30.30 ?  76  ASP D O   1 
ATOM   3939  C  CB  . ASP D  1 77  ? -2.333  223.913 26.542 1.00 32.04 ?  76  ASP D CB  1 
ATOM   3940  C  CG  . ASP D  1 77  ? -2.352  225.015 25.510 1.00 35.74 ?  76  ASP D CG  1 
ATOM   3941  O  OD1 . ASP D  1 77  ? -2.151  226.180 25.915 1.00 37.22 ?  76  ASP D OD1 1 
ATOM   3942  O  OD2 . ASP D  1 77  ? -2.561  224.729 24.303 1.00 33.62 ?  76  ASP D OD2 1 
ATOM   3943  N  N   . GLU D  1 78  ? -1.999  223.432 29.702 1.00 33.86 ?  77  GLU D N   1 
ATOM   3944  C  CA  . GLU D  1 78  ? -2.419  222.482 30.727 1.00 38.06 ?  77  GLU D CA  1 
ATOM   3945  C  C   . GLU D  1 78  ? -3.532  221.577 30.203 1.00 35.16 ?  77  GLU D C   1 
ATOM   3946  O  O   . GLU D  1 78  ? -3.493  220.355 30.387 1.00 33.46 ?  77  GLU D O   1 
ATOM   3947  C  CB  . GLU D  1 78  ? -2.875  223.239 31.973 1.00 40.52 ?  77  GLU D CB  1 
ATOM   3948  C  CG  . GLU D  1 78  ? -3.086  222.375 33.204 1.00 54.34 ?  77  GLU D CG  1 
ATOM   3949  C  CD  . GLU D  1 78  ? -3.590  223.192 34.394 1.00 68.29 ?  77  GLU D CD  1 
ATOM   3950  O  OE1 . GLU D  1 78  ? -2.989  224.254 34.680 1.00 72.21 ?  77  GLU D OE1 1 
ATOM   3951  O  OE2 . GLU D  1 78  ? -4.585  222.779 35.038 1.00 76.89 ?  77  GLU D OE2 1 
ATOM   3952  N  N   . GLU D  1 79  ? -4.520  222.160 29.532 1.00 30.43 ?  78  GLU D N   1 
ATOM   3953  C  CA  . GLU D  1 79  ? -5.548  221.403 28.837 1.00 29.87 ?  78  GLU D CA  1 
ATOM   3954  C  C   . GLU D  1 79  ? -4.946  220.886 27.529 1.00 32.71 ?  78  GLU D C   1 
ATOM   3955  O  O   . GLU D  1 79  ? -4.803  221.629 26.554 1.00 29.69 ?  78  GLU D O   1 
ATOM   3956  C  CB  . GLU D  1 79  ? -6.770  222.285 28.598 1.00 27.11 ?  78  GLU D CB  1 
ATOM   3957  C  CG  . GLU D  1 79  ? -7.991  221.564 28.005 1.00 33.24 ?  78  GLU D CG  1 
ATOM   3958  C  CD  . GLU D  1 79  ? -8.622  220.552 28.980 1.00 42.82 ?  78  GLU D CD  1 
ATOM   3959  O  OE1 . GLU D  1 79  ? -8.275  220.583 30.182 1.00 44.27 ?  78  GLU D OE1 1 
ATOM   3960  O  OE2 . GLU D  1 79  ? -9.463  219.713 28.548 1.00 41.30 ?  78  GLU D OE2 1 
ATOM   3961  N  N   . ARG D  1 80  ? -4.567  219.609 27.503 1.00 30.87 ?  79  ARG D N   1 
ATOM   3962  C  CA  . ARG D  1 80  ? -4.024  218.996 26.289 1.00 27.40 ?  79  ARG D CA  1 
ATOM   3963  C  C   . ARG D  1 80  ? -4.138  217.493 26.443 1.00 29.60 ?  79  ARG D C   1 
ATOM   3964  O  O   . ARG D  1 80  ? -4.295  216.981 27.554 1.00 29.15 ?  79  ARG D O   1 
ATOM   3965  C  CB  . ARG D  1 80  ? -2.559  219.388 26.052 1.00 27.05 ?  79  ARG D CB  1 
ATOM   3966  C  CG  . ARG D  1 80  ? -1.656  219.008 27.249 1.00 28.02 ?  79  ARG D CG  1 
ATOM   3967  C  CD  . ARG D  1 80  ? -0.181  219.107 26.933 1.00 27.24 ?  79  ARG D CD  1 
ATOM   3968  N  NE  . ARG D  1 80  ? 0.342   217.861 26.363 1.00 27.03 ?  79  ARG D NE  1 
ATOM   3969  C  CZ  . ARG D  1 80  ? 1.635   217.616 26.202 1.00 27.48 ?  79  ARG D CZ  1 
ATOM   3970  N  NH1 . ARG D  1 80  ? 2.552   218.530 26.490 1.00 25.20 ?  79  ARG D NH1 1 
ATOM   3971  N  NH2 . ARG D  1 80  ? 2.022   216.432 25.730 1.00 25.97 ?  79  ARG D NH2 1 
ATOM   3972  N  N   . HIS D  1 81  ? -4.080  216.797 25.310 1.00 26.98 ?  80  HIS D N   1 
ATOM   3973  C  CA  . HIS D  1 81  ? -3.889  215.353 25.300 1.00 24.55 ?  80  HIS D CA  1 
ATOM   3974  C  C   . HIS D  1 81  ? -2.454  215.027 25.696 1.00 25.82 ?  80  HIS D C   1 
ATOM   3975  O  O   . HIS D  1 81  ? -1.535  215.794 25.429 1.00 24.73 ?  80  HIS D O   1 
ATOM   3976  C  CB  . HIS D  1 81  ? -4.178  214.785 23.908 1.00 25.69 ?  80  HIS D CB  1 
ATOM   3977  C  CG  . HIS D  1 81  ? -5.548  215.109 23.384 1.00 23.11 ?  80  HIS D CG  1 
ATOM   3978  N  ND1 . HIS D  1 81  ? -5.807  215.307 22.049 1.00 28.56 ?  80  HIS D ND1 1 
ATOM   3979  C  CD2 . HIS D  1 81  ? -6.738  215.235 24.016 1.00 27.04 ?  80  HIS D CD2 1 
ATOM   3980  C  CE1 . HIS D  1 81  ? -7.093  215.557 21.877 1.00 26.93 ?  80  HIS D CE1 1 
ATOM   3981  N  NE2 . HIS D  1 81  ? -7.682  215.507 23.058 1.00 27.46 ?  80  HIS D NE2 1 
ATOM   3982  N  N   . VAL D  1 82  ? -2.254  213.865 26.326 1.00 26.34 ?  81  VAL D N   1 
ATOM   3983  C  CA  . VAL D  1 82  ? -0.878  213.438 26.573 1.00 23.44 ?  81  VAL D CA  1 
ATOM   3984  C  C   . VAL D  1 82  ? -0.099  213.404 25.264 1.00 29.01 ?  81  VAL D C   1 
ATOM   3985  O  O   . VAL D  1 82  ? 1.060   213.829 25.203 1.00 24.01 ?  81  VAL D O   1 
ATOM   3986  C  CB  . VAL D  1 82  ? -0.852  212.078 27.295 1.00 22.46 ?  81  VAL D CB  1 
ATOM   3987  C  CG1 . VAL D  1 82  ? 0.537   211.491 27.246 1.00 20.34 ?  81  VAL D CG1 1 
ATOM   3988  C  CG2 . VAL D  1 82  ? -1.292  212.268 28.760 1.00 23.61 ?  81  VAL D CG2 1 
ATOM   3989  N  N   . GLY D  1 83  ? -0.738  212.947 24.187 1.00 23.33 ?  82  GLY D N   1 
ATOM   3990  C  CA  . GLY D  1 83  ? -0.059  212.832 22.916 1.00 24.17 ?  82  GLY D CA  1 
ATOM   3991  C  C   . GLY D  1 83  ? 0.165   214.126 22.151 1.00 26.36 ?  82  GLY D C   1 
ATOM   3992  O  O   . GLY D  1 83  ? 0.719   214.076 21.053 1.00 26.12 ?  82  GLY D O   1 
ATOM   3993  N  N   . ASP D  1 84  ? -0.199  215.284 22.696 1.00 22.95 ?  83  ASP D N   1 
ATOM   3994  C  CA  . ASP D  1 84  ? -0.146  216.539 21.938 1.00 24.18 ?  83  ASP D CA  1 
ATOM   3995  C  C   . ASP D  1 84  ? 1.270   217.116 21.959 1.00 25.65 ?  83  ASP D C   1 
ATOM   3996  O  O   . ASP D  1 84  ? 1.618   217.935 22.813 1.00 26.94 ?  83  ASP D O   1 
ATOM   3997  C  CB  . ASP D  1 84  ? -1.137  217.541 22.514 1.00 24.87 ?  83  ASP D CB  1 
ATOM   3998  C  CG  . ASP D  1 84  ? -2.551  217.204 22.174 1.00 26.95 ?  83  ASP D CG  1 
ATOM   3999  O  OD1 . ASP D  1 84  ? -2.736  216.318 21.312 1.00 26.74 ?  83  ASP D OD1 1 
ATOM   4000  O  OD2 . ASP D  1 84  ? -3.489  217.788 22.774 1.00 22.81 ?  83  ASP D OD2 1 
ATOM   4001  N  N   . LEU D  1 85  ? 2.095   216.723 20.998 1.00 21.14 ?  84  LEU D N   1 
ATOM   4002  C  CA  . LEU D  1 85  ? 3.444   217.257 20.906 1.00 24.07 ?  84  LEU D CA  1 
ATOM   4003  C  C   . LEU D  1 85  ? 3.543   218.496 20.014 1.00 26.27 ?  84  LEU D C   1 
ATOM   4004  O  O   . LEU D  1 85  ? 4.651   218.961 19.752 1.00 26.99 ?  84  LEU D O   1 
ATOM   4005  C  CB  . LEU D  1 85  ? 4.402   216.179 20.402 1.00 20.34 ?  84  LEU D CB  1 
ATOM   4006  C  CG  . LEU D  1 85  ? 4.525   214.999 21.369 1.00 25.73 ?  84  LEU D CG  1 
ATOM   4007  C  CD1 . LEU D  1 85  ? 5.502   213.975 20.844 1.00 24.40 ?  84  LEU D CD1 1 
ATOM   4008  C  CD2 . LEU D  1 85  ? 4.947   215.501 22.768 1.00 29.63 ?  84  LEU D CD2 1 
ATOM   4009  N  N   . GLY D  1 86  ? 2.426   219.041 19.546 1.00 22.49 ?  85  GLY D N   1 
ATOM   4010  C  CA  . GLY D  1 86  ? 2.471   220.269 18.774 1.00 23.50 ?  85  GLY D CA  1 
ATOM   4011  C  C   . GLY D  1 86  ? 2.844   220.050 17.320 1.00 27.53 ?  85  GLY D C   1 
ATOM   4012  O  O   . GLY D  1 86  ? 2.382   219.085 16.704 1.00 25.90 ?  85  GLY D O   1 
ATOM   4013  N  N   . ASN D  1 87  ? 3.700   220.915 16.775 1.00 20.34 ?  86  ASN D N   1 
ATOM   4014  C  CA  . ASN D  1 87  ? 4.128   220.856 15.384 1.00 25.94 ?  86  ASN D CA  1 
ATOM   4015  C  C   . ASN D  1 87  ? 5.616   220.566 15.289 1.00 26.31 ?  86  ASN D C   1 
ATOM   4016  O  O   . ASN D  1 87  ? 6.387   220.872 16.206 1.00 23.27 ?  86  ASN D O   1 
ATOM   4017  C  CB  . ASN D  1 87  ? 3.859   222.178 14.661 1.00 25.71 ?  86  ASN D CB  1 
ATOM   4018  C  CG  . ASN D  1 87  ? 2.402   222.425 14.440 1.00 27.66 ?  86  ASN D CG  1 
ATOM   4019  O  OD1 . ASN D  1 87  ? 1.745   221.681 13.712 1.00 23.55 ?  86  ASN D OD1 1 
ATOM   4020  N  ND2 . ASN D  1 87  ? 1.876   223.480 15.054 1.00 22.90 ?  86  ASN D ND2 1 
ATOM   4021  N  N   . VAL D  1 88  ? 6.016   220.007 14.154 1.00 20.34 ?  87  VAL D N   1 
ATOM   4022  C  CA  . VAL D  1 88  ? 7.414   220.016 13.750 1.00 21.62 ?  87  VAL D CA  1 
ATOM   4023  C  C   . VAL D  1 88  ? 7.491   220.814 12.459 1.00 20.34 ?  87  VAL D C   1 
ATOM   4024  O  O   . VAL D  1 88  ? 6.499   220.969 11.747 1.00 29.27 ?  87  VAL D O   1 
ATOM   4025  C  CB  . VAL D  1 88  ? 8.005   218.603 13.568 1.00 23.97 ?  87  VAL D CB  1 
ATOM   4026  C  CG1 . VAL D  1 88  ? 8.005   217.838 14.908 1.00 20.34 ?  87  VAL D CG1 1 
ATOM   4027  C  CG2 . VAL D  1 88  ? 7.234   217.836 12.495 1.00 20.34 ?  87  VAL D CG2 1 
ATOM   4028  N  N   . THR D  1 89  ? 8.677   221.320 12.147 1.00 21.20 ?  88  THR D N   1 
ATOM   4029  C  CA  . THR D  1 89  ? 8.844   222.247 11.029 1.00 22.23 ?  88  THR D CA  1 
ATOM   4030  C  C   . THR D  1 89  ? 9.734   221.632 9.964  1.00 20.34 ?  88  THR D C   1 
ATOM   4031  O  O   . THR D  1 89  ? 10.869  221.256 10.247 1.00 27.77 ?  88  THR D O   1 
ATOM   4032  C  CB  . THR D  1 89  ? 9.448   223.578 11.491 1.00 26.25 ?  88  THR D CB  1 
ATOM   4033  O  OG1 . THR D  1 89  ? 8.544   224.207 12.403 1.00 25.38 ?  88  THR D OG1 1 
ATOM   4034  C  CG2 . THR D  1 89  ? 9.680   224.504 10.280 1.00 26.13 ?  88  THR D CG2 1 
ATOM   4035  N  N   . ALA D  1 90  ? 9.235   221.555 8.743  1.00 21.68 ?  89  ALA D N   1 
ATOM   4036  C  CA  . ALA D  1 90  ? 10.042  221.098 7.632  1.00 25.66 ?  89  ALA D CA  1 
ATOM   4037  C  C   . ALA D  1 90  ? 10.652  222.307 6.926  1.00 24.59 ?  89  ALA D C   1 
ATOM   4038  O  O   . ALA D  1 90  ? 9.994   223.335 6.749  1.00 24.82 ?  89  ALA D O   1 
ATOM   4039  C  CB  . ALA D  1 90  ? 9.200   220.273 6.656  1.00 27.02 ?  89  ALA D CB  1 
ATOM   4040  N  N   . ASP D  1 91  ? 11.923  222.179 6.544  1.00 28.61 ?  90  ASP D N   1 
ATOM   4041  C  CA  . ASP D  1 91  ? 12.630  223.259 5.884  1.00 29.60 ?  90  ASP D CA  1 
ATOM   4042  C  C   . ASP D  1 91  ? 12.293  223.226 4.397  1.00 32.72 ?  90  ASP D C   1 
ATOM   4043  O  O   . ASP D  1 91  ? 11.460  222.433 3.950  1.00 28.21 ?  90  ASP D O   1 
ATOM   4044  C  CB  . ASP D  1 91  ? 14.128  223.158 6.153  1.00 28.67 ?  90  ASP D CB  1 
ATOM   4045  C  CG  . ASP D  1 91  ? 14.781  221.908 5.540  1.00 32.27 ?  90  ASP D CG  1 
ATOM   4046  O  OD1 . ASP D  1 91  ? 14.231  221.285 4.599  1.00 30.25 ?  90  ASP D OD1 1 
ATOM   4047  O  OD2 . ASP D  1 91  ? 15.896  221.570 5.991  1.00 38.59 ?  90  ASP D OD2 1 
ATOM   4048  N  N   . LYS D  1 92  ? 12.941  224.095 3.612  1.00 30.00 ?  91  LYS D N   1 
ATOM   4049  C  CA  . LYS D  1 92  ? 12.582  224.223 2.201  1.00 36.46 ?  91  LYS D CA  1 
ATOM   4050  C  C   . LYS D  1 92  ? 12.907  222.967 1.393  1.00 33.66 ?  91  LYS D C   1 
ATOM   4051  O  O   . LYS D  1 92  ? 12.354  222.786 0.301  1.00 34.89 ?  91  LYS D O   1 
ATOM   4052  C  CB  . LYS D  1 92  ? 13.271  225.452 1.594  1.00 44.03 ?  91  LYS D CB  1 
ATOM   4053  C  CG  . LYS D  1 92  ? 14.779  225.349 1.500  1.00 41.85 ?  91  LYS D CG  1 
ATOM   4054  C  CD  . LYS D  1 92  ? 15.358  226.441 0.596  1.00 52.87 ?  91  LYS D CD  1 
ATOM   4055  C  CE  . LYS D  1 92  ? 14.847  226.321 -0.855 1.00 69.07 ?  91  LYS D CE  1 
ATOM   4056  N  NZ  . LYS D  1 92  ? 15.508  225.228 -1.671 1.00 64.65 ?  91  LYS D NZ  1 
ATOM   4057  N  N   . ASP D  1 93  ? 13.774  222.101 1.910  1.00 28.50 ?  92  ASP D N   1 
ATOM   4058  C  CA  . ASP D  1 93  ? 14.067  220.808 1.308  1.00 29.81 ?  92  ASP D CA  1 
ATOM   4059  C  C   . ASP D  1 93  ? 13.080  219.726 1.717  1.00 31.59 ?  92  ASP D C   1 
ATOM   4060  O  O   . ASP D  1 93  ? 13.212  218.586 1.263  1.00 31.97 ?  92  ASP D O   1 
ATOM   4061  C  CB  . ASP D  1 93  ? 15.481  220.358 1.692  1.00 32.87 ?  92  ASP D CB  1 
ATOM   4062  C  CG  . ASP D  1 93  ? 16.557  221.255 1.095  1.00 46.89 ?  92  ASP D CG  1 
ATOM   4063  O  OD1 . ASP D  1 93  ? 16.384  221.681 -0.071 1.00 44.23 ?  92  ASP D OD1 1 
ATOM   4064  O  OD2 . ASP D  1 93  ? 17.568  221.526 1.786  1.00 49.03 ?  92  ASP D OD2 1 
ATOM   4065  N  N   . GLY D  1 94  ? 12.110  220.043 2.564  1.00 28.76 ?  93  GLY D N   1 
ATOM   4066  C  CA  . GLY D  1 94  ? 11.188  219.042 3.061  1.00 26.63 ?  93  GLY D CA  1 
ATOM   4067  C  C   . GLY D  1 94  ? 11.663  218.237 4.252  1.00 24.46 ?  93  GLY D C   1 
ATOM   4068  O  O   . GLY D  1 94  ? 11.058  217.205 4.560  1.00 30.57 ?  93  GLY D O   1 
ATOM   4069  N  N   . VAL D  1 95  ? 12.700  218.679 4.953  1.00 25.53 ?  94  VAL D N   1 
ATOM   4070  C  CA  . VAL D  1 95  ? 13.277  217.910 6.053  1.00 28.10 ?  94  VAL D CA  1 
ATOM   4071  C  C   . VAL D  1 95  ? 12.939  218.601 7.366  1.00 26.31 ?  94  VAL D C   1 
ATOM   4072  O  O   . VAL D  1 95  ? 13.185  219.804 7.527  1.00 29.35 ?  94  VAL D O   1 
ATOM   4073  C  CB  . VAL D  1 95  ? 14.799  217.757 5.897  1.00 28.79 ?  94  VAL D CB  1 
ATOM   4074  C  CG1 . VAL D  1 95  ? 15.390  217.060 7.141  1.00 28.41 ?  94  VAL D CG1 1 
ATOM   4075  C  CG2 . VAL D  1 95  ? 15.132  217.008 4.603  1.00 27.69 ?  94  VAL D CG2 1 
ATOM   4076  N  N   . ALA D  1 96  ? 12.368  217.847 8.299  1.00 25.86 ?  95  ALA D N   1 
ATOM   4077  C  CA  . ALA D  1 96  ? 12.092  218.338 9.644  1.00 29.00 ?  95  ALA D CA  1 
ATOM   4078  C  C   . ALA D  1 96  ? 13.137  217.737 10.582 1.00 31.02 ?  95  ALA D C   1 
ATOM   4079  O  O   . ALA D  1 96  ? 13.148  216.524 10.820 1.00 29.84 ?  95  ALA D O   1 
ATOM   4080  C  CB  . ALA D  1 96  ? 10.674  217.987 10.089 1.00 20.34 ?  95  ALA D CB  1 
ATOM   4081  N  N   . ASP D  1 97  ? 14.027  218.582 11.096 1.00 23.87 ?  96  ASP D N   1 
ATOM   4082  C  CA  . ASP D  1 97  ? 14.999  218.142 12.085 1.00 29.67 ?  96  ASP D CA  1 
ATOM   4083  C  C   . ASP D  1 97  ? 14.338  218.361 13.437 1.00 28.86 ?  96  ASP D C   1 
ATOM   4084  O  O   . ASP D  1 97  ? 14.377  219.440 14.015 1.00 30.28 ?  96  ASP D O   1 
ATOM   4085  C  CB  . ASP D  1 97  ? 16.315  218.887 11.934 1.00 30.62 ?  96  ASP D CB  1 
ATOM   4086  C  CG  . ASP D  1 97  ? 17.062  218.484 10.651 1.00 49.30 ?  96  ASP D CG  1 
ATOM   4087  O  OD1 . ASP D  1 97  ? 17.298  217.262 10.422 1.00 41.82 ?  96  ASP D OD1 1 
ATOM   4088  O  OD2 . ASP D  1 97  ? 17.400  219.396 9.870  1.00 51.68 ?  96  ASP D OD2 1 
ATOM   4089  N  N   . VAL D  1 98  ? 13.686  217.314 13.925 1.00 28.77 ?  97  VAL D N   1 
ATOM   4090  C  CA  . VAL D  1 98  ? 12.841  217.421 15.102 1.00 21.51 ?  97  VAL D CA  1 
ATOM   4091  C  C   . VAL D  1 98  ? 13.713  217.567 16.333 1.00 30.35 ?  97  VAL D C   1 
ATOM   4092  O  O   . VAL D  1 98  ? 14.745  216.889 16.468 1.00 26.99 ?  97  VAL D O   1 
ATOM   4093  C  CB  . VAL D  1 98  ? 11.932  216.185 15.200 1.00 27.20 ?  97  VAL D CB  1 
ATOM   4094  C  CG1 . VAL D  1 98  ? 11.088  216.232 16.453 1.00 21.82 ?  97  VAL D CG1 1 
ATOM   4095  C  CG2 . VAL D  1 98  ? 11.033  216.103 13.953 1.00 25.65 ?  97  VAL D CG2 1 
ATOM   4096  N  N   . SER D  1 99  ? 13.307  218.459 17.231 1.00 28.11 ?  98  SER D N   1 
ATOM   4097  C  CA  . SER D  1 99  ? 13.937  218.555 18.549 1.00 30.14 ?  98  SER D CA  1 
ATOM   4098  C  C   . SER D  1 99  ? 12.891  219.110 19.501 1.00 30.25 ?  98  SER D C   1 
ATOM   4099  O  O   . SER D  1 99  ? 12.542  220.293 19.435 1.00 32.26 ?  98  SER D O   1 
ATOM   4100  C  CB  . SER D  1 99  ? 15.183  219.441 18.514 1.00 37.87 ?  98  SER D CB  1 
ATOM   4101  O  OG  . SER D  1 99  ? 15.878  219.358 19.749 1.00 45.36 ?  98  SER D OG  1 
ATOM   4102  N  N   . ILE D  1 100 ? 12.361  218.254 20.357 1.00 29.32 ?  99  ILE D N   1 
ATOM   4103  C  CA  . ILE D  1 100 ? 11.272  218.619 21.246 1.00 28.13 ?  99  ILE D CA  1 
ATOM   4104  C  C   . ILE D  1 100 ? 11.648  218.111 22.630 1.00 29.41 ?  99  ILE D C   1 
ATOM   4105  O  O   . ILE D  1 100 ? 12.335  217.094 22.774 1.00 27.15 ?  99  ILE D O   1 
ATOM   4106  C  CB  . ILE D  1 100 ? 9.931   218.020 20.741 1.00 30.99 ?  99  ILE D CB  1 
ATOM   4107  C  CG1 . ILE D  1 100 ? 9.348   218.863 19.594 1.00 26.85 ?  99  ILE D CG1 1 
ATOM   4108  C  CG2 . ILE D  1 100 ? 8.903   217.873 21.833 1.00 28.72 ?  99  ILE D CG2 1 
ATOM   4109  C  CD1 . ILE D  1 100 ? 8.333   218.053 18.753 1.00 24.98 ?  99  ILE D CD1 1 
ATOM   4110  N  N   . GLU D  1 101 ? 11.242  218.842 23.652 1.00 31.40 ?  100 GLU D N   1 
ATOM   4111  C  CA  . GLU D  1 101 ? 11.370  218.337 25.010 1.00 34.34 ?  100 GLU D CA  1 
ATOM   4112  C  C   . GLU D  1 101 ? 9.996   218.425 25.650 1.00 29.35 ?  100 GLU D C   1 
ATOM   4113  O  O   . GLU D  1 101 ? 9.357   219.477 25.607 1.00 28.04 ?  100 GLU D O   1 
ATOM   4114  C  CB  . GLU D  1 101 ? 12.420  219.124 25.802 1.00 36.09 ?  100 GLU D CB  1 
ATOM   4115  C  CG  . GLU D  1 101 ? 12.614  218.595 27.210 1.00 48.83 ?  100 GLU D CG  1 
ATOM   4116  C  CD  . GLU D  1 101 ? 13.278  219.599 28.139 1.00 58.65 ?  100 GLU D CD  1 
ATOM   4117  O  OE1 . GLU D  1 101 ? 14.500  219.818 27.988 1.00 61.05 ?  100 GLU D OE1 1 
ATOM   4118  O  OE2 . GLU D  1 101 ? 12.580  220.152 29.022 1.00 63.02 ?  100 GLU D OE2 1 
ATOM   4119  N  N   . ASP D  1 102 ? 9.498   217.313 26.170 1.00 28.92 ?  101 ASP D N   1 
ATOM   4120  C  CA  . ASP D  1 102 ? 8.139   217.329 26.695 1.00 30.34 ?  101 ASP D CA  1 
ATOM   4121  C  C   . ASP D  1 102 ? 8.100   216.627 28.040 1.00 31.76 ?  101 ASP D C   1 
ATOM   4122  O  O   . ASP D  1 102 ? 8.740   215.584 28.212 1.00 29.75 ?  101 ASP D O   1 
ATOM   4123  C  CB  . ASP D  1 102 ? 7.164   216.646 25.726 1.00 25.82 ?  101 ASP D CB  1 
ATOM   4124  C  CG  . ASP D  1 102 ? 5.726   216.909 26.080 1.00 31.41 ?  101 ASP D CG  1 
ATOM   4125  O  OD1 . ASP D  1 102 ? 5.264   218.060 25.912 1.00 30.65 ?  101 ASP D OD1 1 
ATOM   4126  O  OD2 . ASP D  1 102 ? 5.050   215.968 26.553 1.00 26.76 ?  101 ASP D OD2 1 
ATOM   4127  N  N   A SER D  1 103 ? 7.335   217.188 28.982 0.50 31.62 ?  102 SER D N   1 
ATOM   4128  N  N   B SER D  1 103 ? 7.338   217.193 28.981 0.50 31.57 ?  102 SER D N   1 
ATOM   4129  C  CA  A SER D  1 103 ? 7.238   216.650 30.335 0.50 33.30 ?  102 SER D CA  1 
ATOM   4130  C  CA  B SER D  1 103 ? 7.234   216.662 30.337 0.50 33.27 ?  102 SER D CA  1 
ATOM   4131  C  C   A SER D  1 103 ? 5.888   216.004 30.626 0.50 32.46 ?  102 SER D C   1 
ATOM   4132  C  C   B SER D  1 103 ? 5.887   216.008 30.626 0.50 32.45 ?  102 SER D C   1 
ATOM   4133  O  O   A SER D  1 103 ? 5.635   215.616 31.769 0.50 33.39 ?  102 SER D O   1 
ATOM   4134  O  O   B SER D  1 103 ? 5.635   215.619 31.769 0.50 33.34 ?  102 SER D O   1 
ATOM   4135  C  CB  A SER D  1 103 ? 7.519   217.748 31.363 0.50 35.08 ?  102 SER D CB  1 
ATOM   4136  C  CB  B SER D  1 103 ? 7.496   217.770 31.362 0.50 35.16 ?  102 SER D CB  1 
ATOM   4137  O  OG  A SER D  1 103 ? 8.911   217.988 31.466 0.50 36.46 ?  102 SER D OG  1 
ATOM   4138  O  OG  B SER D  1 103 ? 6.619   218.868 31.163 0.50 31.56 ?  102 SER D OG  1 
ATOM   4139  N  N   . VAL D  1 104 ? 5.016   215.879 29.631 1.00 30.05 ?  103 VAL D N   1 
ATOM   4140  C  CA  . VAL D  1 104 ? 3.726   215.219 29.806 1.00 25.03 ?  103 VAL D CA  1 
ATOM   4141  C  C   . VAL D  1 104 ? 3.749   213.789 29.267 1.00 30.87 ?  103 VAL D C   1 
ATOM   4142  O  O   . VAL D  1 104 ? 3.242   212.874 29.919 1.00 25.29 ?  103 VAL D O   1 
ATOM   4143  C  CB  . VAL D  1 104 ? 2.600   216.059 29.158 1.00 26.85 ?  103 VAL D CB  1 
ATOM   4144  C  CG1 . VAL D  1 104 ? 1.262   215.321 29.229 1.00 27.42 ?  103 VAL D CG1 1 
ATOM   4145  C  CG2 . VAL D  1 104 ? 2.496   217.433 29.845 1.00 30.74 ?  103 VAL D CG2 1 
ATOM   4146  N  N   . ILE D  1 105 ? 4.353   213.555 28.091 1.00 20.34 ?  104 ILE D N   1 
ATOM   4147  C  CA  . ILE D  1 105 ? 4.599   212.158 27.685 1.00 20.34 ?  104 ILE D CA  1 
ATOM   4148  C  C   . ILE D  1 105 ? 5.646   211.555 28.610 1.00 23.51 ?  104 ILE D C   1 
ATOM   4149  O  O   . ILE D  1 105 ? 6.449   212.259 29.221 1.00 28.06 ?  104 ILE D O   1 
ATOM   4150  C  CB  . ILE D  1 105 ? 5.052   212.053 26.219 1.00 23.57 ?  104 ILE D CB  1 
ATOM   4151  C  CG1 . ILE D  1 105 ? 6.363   212.823 26.017 1.00 24.36 ?  104 ILE D CG1 1 
ATOM   4152  C  CG2 . ILE D  1 105 ? 4.002   212.579 25.274 1.00 20.34 ?  104 ILE D CG2 1 
ATOM   4153  C  CD1 . ILE D  1 105 ? 7.077   212.462 24.688 1.00 22.83 ?  104 ILE D CD1 1 
ATOM   4154  N  N   . SER D  1 106 ? 5.652   210.231 28.694 1.00 23.88 ?  105 SER D N   1 
ATOM   4155  C  CA  . SER D  1 106 ? 6.650   209.547 29.492 1.00 24.49 ?  105 SER D CA  1 
ATOM   4156  C  C   . SER D  1 106 ? 6.972   208.211 28.833 1.00 27.15 ?  105 SER D C   1 
ATOM   4157  O  O   . SER D  1 106 ? 6.235   207.731 27.963 1.00 27.74 ?  105 SER D O   1 
ATOM   4158  C  CB  . SER D  1 106 ? 6.150   209.358 30.932 1.00 23.67 ?  105 SER D CB  1 
ATOM   4159  O  OG  . SER D  1 106 ? 7.171   208.805 31.745 1.00 27.45 ?  105 SER D OG  1 
ATOM   4160  N  N   . LEU D  1 107 ? 8.102   207.628 29.225 1.00 22.09 ?  106 LEU D N   1 
ATOM   4161  C  CA  . LEU D  1 107 ? 8.439   206.282 28.787 1.00 24.45 ?  106 LEU D CA  1 
ATOM   4162  C  C   . LEU D  1 107 ? 8.086   205.237 29.850 1.00 33.02 ?  106 LEU D C   1 
ATOM   4163  O  O   . LEU D  1 107 ? 8.432   204.071 29.697 1.00 33.14 ?  106 LEU D O   1 
ATOM   4164  C  CB  . LEU D  1 107 ? 9.925   206.195 28.398 1.00 27.25 ?  106 LEU D CB  1 
ATOM   4165  C  CG  . LEU D  1 107 ? 10.407  207.192 27.332 1.00 27.19 ?  106 LEU D CG  1 
ATOM   4166  C  CD1 . LEU D  1 107 ? 11.841  206.899 26.906 1.00 28.60 ?  106 LEU D CD1 1 
ATOM   4167  C  CD2 . LEU D  1 107 ? 9.473   207.246 26.103 1.00 26.97 ?  106 LEU D CD2 1 
ATOM   4168  N  N   . SER D  1 108 ? 7.386   205.638 30.914 1.00 28.37 ?  107 SER D N   1 
ATOM   4169  C  CA  . SER D  1 108 ? 6.888   204.713 31.924 1.00 31.63 ?  107 SER D CA  1 
ATOM   4170  C  C   . SER D  1 108 ? 5.612   205.296 32.523 1.00 29.53 ?  107 SER D C   1 
ATOM   4171  O  O   . SER D  1 108 ? 5.290   206.479 32.331 1.00 28.37 ?  107 SER D O   1 
ATOM   4172  C  CB  . SER D  1 108 ? 7.946   204.458 33.011 1.00 30.08 ?  107 SER D CB  1 
ATOM   4173  O  OG  . SER D  1 108 ? 8.463   205.685 33.516 1.00 40.13 ?  107 SER D OG  1 
ATOM   4174  N  N   . GLY D  1 109 ? 4.872   204.454 33.241 1.00 31.34 ?  108 GLY D N   1 
ATOM   4175  C  CA  . GLY D  1 109 ? 3.701   204.919 33.965 1.00 31.41 ?  108 GLY D CA  1 
ATOM   4176  C  C   . GLY D  1 109 ? 2.461   205.069 33.097 1.00 33.27 ?  108 GLY D C   1 
ATOM   4177  O  O   . GLY D  1 109 ? 2.389   204.601 31.968 1.00 31.90 ?  108 GLY D O   1 
ATOM   4178  N  N   . ASP D  1 110 ? 1.470   205.762 33.675 1.00 29.43 ?  109 ASP D N   1 
ATOM   4179  C  CA  . ASP D  1 110 ? 0.185   206.083 33.045 1.00 30.19 ?  109 ASP D CA  1 
ATOM   4180  C  C   . ASP D  1 110 ? 0.331   206.780 31.686 1.00 31.62 ?  109 ASP D C   1 
ATOM   4181  O  O   . ASP D  1 110 ? -0.518  206.607 30.802 1.00 30.84 ?  109 ASP D O   1 
ATOM   4182  C  CB  . ASP D  1 110 ? -0.599  207.027 33.979 1.00 33.31 ?  109 ASP D CB  1 
ATOM   4183  C  CG  . ASP D  1 110 ? -1.442  206.292 35.011 1.00 47.11 ?  109 ASP D CG  1 
ATOM   4184  O  OD1 . ASP D  1 110 ? -1.190  205.080 35.238 1.00 49.61 ?  109 ASP D OD1 1 
ATOM   4185  O  OD2 . ASP D  1 110 ? -2.350  206.937 35.600 1.00 43.02 ?  109 ASP D OD2 1 
ATOM   4186  N  N   . HIS D  1 111 ? 1.347   207.630 31.541 1.00 26.50 ?  110 HIS D N   1 
ATOM   4187  C  CA  . HIS D  1 111 ? 1.571   208.481 30.375 1.00 29.29 ?  110 HIS D CA  1 
ATOM   4188  C  C   . HIS D  1 111 ? 2.533   207.850 29.378 1.00 24.81 ?  110 HIS D C   1 
ATOM   4189  O  O   . HIS D  1 111 ? 3.000   208.530 28.442 1.00 28.82 ?  110 HIS D O   1 
ATOM   4190  C  CB  . HIS D  1 111 ? 2.128   209.830 30.817 1.00 28.89 ?  110 HIS D CB  1 
ATOM   4191  C  CG  . HIS D  1 111 ? 1.128   210.715 31.502 1.00 38.41 ?  110 HIS D CG  1 
ATOM   4192  N  ND1 . HIS D  1 111 ? -0.166  210.317 31.770 1.00 45.68 ?  110 HIS D ND1 1 
ATOM   4193  C  CD2 . HIS D  1 111 ? 1.241   211.981 31.985 1.00 36.25 ?  110 HIS D CD2 1 
ATOM   4194  C  CE1 . HIS D  1 111 ? -0.805  211.295 32.393 1.00 35.49 ?  110 HIS D CE1 1 
ATOM   4195  N  NE2 . HIS D  1 111 ? 0.025   212.313 32.535 1.00 37.44 ?  110 HIS D NE2 1 
ATOM   4196  N  N   . CYS D  1 112 ? 2.868   206.587 29.584 1.00 22.23 ?  111 CYS D N   1 
ATOM   4197  C  CA  . CYS D  1 112 ? 3.844   205.911 28.753 1.00 24.88 ?  111 CYS D CA  1 
ATOM   4198  C  C   . CYS D  1 112 ? 3.363   205.847 27.309 1.00 26.26 ?  111 CYS D C   1 
ATOM   4199  O  O   . CYS D  1 112 ? 2.215   205.490 27.035 1.00 23.08 ?  111 CYS D O   1 
ATOM   4200  C  CB  . CYS D  1 112 ? 4.075   204.509 29.286 1.00 27.56 ?  111 CYS D CB  1 
ATOM   4201  S  SG  . CYS D  1 112 ? 5.373   203.647 28.428 1.00 31.48 ?  111 CYS D SG  1 
ATOM   4202  N  N   . ILE D  1 113 ? 4.249   206.208 26.385 1.00 22.26 ?  112 ILE D N   1 
ATOM   4203  C  CA  . ILE D  1 113 ? 3.932   206.166 24.968 1.00 24.11 ?  112 ILE D CA  1 
ATOM   4204  C  C   . ILE D  1 113 ? 4.538   204.953 24.271 1.00 24.19 ?  112 ILE D C   1 
ATOM   4205  O  O   . ILE D  1 113 ? 4.331   204.785 23.065 1.00 20.34 ?  112 ILE D O   1 
ATOM   4206  C  CB  . ILE D  1 113 ? 4.392   207.464 24.272 1.00 23.73 ?  112 ILE D CB  1 
ATOM   4207  C  CG1 . ILE D  1 113 ? 5.905   207.639 24.389 1.00 22.51 ?  112 ILE D CG1 1 
ATOM   4208  C  CG2 . ILE D  1 113 ? 3.717   208.678 24.884 1.00 20.67 ?  112 ILE D CG2 1 
ATOM   4209  C  CD1 . ILE D  1 113 ? 6.400   208.917 23.707 1.00 23.93 ?  112 ILE D CD1 1 
ATOM   4210  N  N   . ILE D  1 114 ? 5.278   204.103 24.992 1.00 24.94 ?  113 ILE D N   1 
ATOM   4211  C  CA  . ILE D  1 114 ? 5.823   202.896 24.377 1.00 20.34 ?  113 ILE D CA  1 
ATOM   4212  C  C   . ILE D  1 114 ? 4.683   202.015 23.894 1.00 24.79 ?  113 ILE D C   1 
ATOM   4213  O  O   . ILE D  1 114 ? 3.688   201.830 24.595 1.00 22.18 ?  113 ILE D O   1 
ATOM   4214  C  CB  . ILE D  1 114 ? 6.695   202.111 25.369 1.00 28.69 ?  113 ILE D CB  1 
ATOM   4215  C  CG1 . ILE D  1 114 ? 7.763   203.011 25.992 1.00 36.15 ?  113 ILE D CG1 1 
ATOM   4216  C  CG2 . ILE D  1 114 ? 7.261   200.831 24.708 1.00 21.06 ?  113 ILE D CG2 1 
ATOM   4217  C  CD1 . ILE D  1 114 ? 9.033   203.067 25.259 1.00 35.71 ?  113 ILE D CD1 1 
ATOM   4218  N  N   . GLY D  1 115 ? 4.813   201.479 22.682 1.00 22.48 ?  114 GLY D N   1 
ATOM   4219  C  CA  . GLY D  1 115 ? 3.762   200.663 22.109 1.00 20.95 ?  114 GLY D CA  1 
ATOM   4220  C  C   . GLY D  1 115 ? 2.586   201.437 21.540 1.00 23.88 ?  114 GLY D C   1 
ATOM   4221  O  O   . GLY D  1 115 ? 1.589   200.817 21.153 1.00 22.80 ?  114 GLY D O   1 
ATOM   4222  N  N   . ARG D  1 116 ? 2.654   202.768 21.508 1.00 20.34 ?  115 ARG D N   1 
ATOM   4223  C  CA  . ARG D  1 116 ? 1.658   203.600 20.853 1.00 20.34 ?  115 ARG D CA  1 
ATOM   4224  C  C   . ARG D  1 116 ? 2.251   204.100 19.538 1.00 20.34 ?  115 ARG D C   1 
ATOM   4225  O  O   . ARG D  1 116 ? 3.372   203.743 19.184 1.00 26.49 ?  115 ARG D O   1 
ATOM   4226  C  CB  . ARG D  1 116 ? 1.226   204.730 21.801 1.00 23.21 ?  115 ARG D CB  1 
ATOM   4227  C  CG  . ARG D  1 116 ? 0.776   204.155 23.150 1.00 24.48 ?  115 ARG D CG  1 
ATOM   4228  C  CD  . ARG D  1 116 ? -0.061  205.114 23.997 1.00 30.78 ?  115 ARG D CD  1 
ATOM   4229  N  NE  . ARG D  1 116 ? -0.300  204.557 25.328 1.00 30.26 ?  115 ARG D NE  1 
ATOM   4230  C  CZ  . ARG D  1 116 ? -1.375  203.850 25.664 1.00 29.75 ?  115 ARG D CZ  1 
ATOM   4231  N  NH1 . ARG D  1 116 ? -2.326  203.578 24.787 1.00 22.40 ?  115 ARG D NH1 1 
ATOM   4232  N  NH2 . ARG D  1 116 ? -1.516  203.431 26.924 1.00 28.41 ?  115 ARG D NH2 1 
ATOM   4233  N  N   . THR D  1 117 ? 1.493   204.885 18.773 1.00 20.94 ?  116 THR D N   1 
ATOM   4234  C  CA  . THR D  1 117 ? 1.905   205.267 17.422 1.00 30.14 ?  116 THR D CA  1 
ATOM   4235  C  C   . THR D  1 117 ? 2.235   206.753 17.359 1.00 20.34 ?  116 THR D C   1 
ATOM   4236  O  O   . THR D  1 117 ? 1.423   207.592 17.752 1.00 23.42 ?  116 THR D O   1 
ATOM   4237  C  CB  . THR D  1 117 ? 0.824   204.931 16.391 1.00 25.50 ?  116 THR D CB  1 
ATOM   4238  O  OG1 . THR D  1 117 ? 0.637   203.512 16.322 1.00 23.50 ?  116 THR D OG1 1 
ATOM   4239  C  CG2 . THR D  1 117 ? 1.227   205.449 14.988 1.00 23.81 ?  116 THR D CG2 1 
ATOM   4240  N  N   . LEU D  1 118 ? 3.417   207.075 16.865 1.00 20.34 ?  117 LEU D N   1 
ATOM   4241  C  CA  . LEU D  1 118 ? 3.763   208.449 16.557 1.00 20.34 ?  117 LEU D CA  1 
ATOM   4242  C  C   . LEU D  1 118 ? 3.322   208.742 15.124 1.00 23.50 ?  117 LEU D C   1 
ATOM   4243  O  O   . LEU D  1 118 ? 3.586   207.937 14.233 1.00 22.09 ?  117 LEU D O   1 
ATOM   4244  C  CB  . LEU D  1 118 ? 5.262   208.654 16.709 1.00 20.34 ?  117 LEU D CB  1 
ATOM   4245  C  CG  . LEU D  1 118 ? 5.731   210.076 16.428 1.00 22.04 ?  117 LEU D CG  1 
ATOM   4246  C  CD1 . LEU D  1 118 ? 5.223   210.966 17.523 1.00 24.02 ?  117 LEU D CD1 1 
ATOM   4247  C  CD2 . LEU D  1 118 ? 7.253   210.111 16.345 1.00 20.34 ?  117 LEU D CD2 1 
ATOM   4248  N  N   . VAL D  1 119 ? 2.638   209.872 14.907 1.00 20.34 ?  118 VAL D N   1 
ATOM   4249  C  CA  . VAL D  1 119 ? 2.100   210.230 13.592 1.00 21.72 ?  118 VAL D CA  1 
ATOM   4250  C  C   . VAL D  1 119 ? 2.515   211.660 13.260 1.00 23.18 ?  118 VAL D C   1 
ATOM   4251  O  O   . VAL D  1 119 ? 2.358   212.568 14.089 1.00 22.83 ?  118 VAL D O   1 
ATOM   4252  C  CB  . VAL D  1 119 ? 0.561   210.114 13.543 1.00 22.84 ?  118 VAL D CB  1 
ATOM   4253  C  CG1 . VAL D  1 119 ? 0.043   210.463 12.159 1.00 20.34 ?  118 VAL D CG1 1 
ATOM   4254  C  CG2 . VAL D  1 119 ? 0.100   208.721 13.949 1.00 21.79 ?  118 VAL D CG2 1 
ATOM   4255  N  N   . VAL D  1 120 ? 3.041   211.865 12.061 1.00 20.34 ?  119 VAL D N   1 
ATOM   4256  C  CA  . VAL D  1 120 ? 3.211   213.209 11.523 1.00 20.34 ?  119 VAL D CA  1 
ATOM   4257  C  C   . VAL D  1 120 ? 2.099   213.469 10.516 1.00 24.11 ?  119 VAL D C   1 
ATOM   4258  O  O   . VAL D  1 120 ? 1.776   212.608 9.680  1.00 20.34 ?  119 VAL D O   1 
ATOM   4259  C  CB  . VAL D  1 120 ? 4.604   213.410 10.906 1.00 21.62 ?  119 VAL D CB  1 
ATOM   4260  C  CG1 . VAL D  1 120 ? 4.866   212.413 9.766  1.00 21.85 ?  119 VAL D CG1 1 
ATOM   4261  C  CG2 . VAL D  1 120 ? 4.758   214.858 10.429 1.00 23.48 ?  119 VAL D CG2 1 
ATOM   4262  N  N   . HIS D  1 121 ? 1.497   214.649 10.611 1.00 21.40 ?  120 HIS D N   1 
ATOM   4263  C  CA  . HIS D  1 121 ? 0.252   214.954 9.919  1.00 22.39 ?  120 HIS D CA  1 
ATOM   4264  C  C   . HIS D  1 121 ? 0.461   215.891 8.732  1.00 20.34 ?  120 HIS D C   1 
ATOM   4265  O  O   . HIS D  1 121 ? 1.506   216.513 8.563  1.00 22.37 ?  120 HIS D O   1 
ATOM   4266  C  CB  . HIS D  1 121 ? -0.753  215.574 10.886 1.00 20.34 ?  120 HIS D CB  1 
ATOM   4267  C  CG  . HIS D  1 121 ? -1.333  214.588 11.839 1.00 25.19 ?  120 HIS D CG  1 
ATOM   4268  N  ND1 . HIS D  1 121 ? -2.555  213.991 11.626 1.00 21.45 ?  120 HIS D ND1 1 
ATOM   4269  C  CD2 . HIS D  1 121 ? -0.847  214.073 12.996 1.00 20.96 ?  120 HIS D CD2 1 
ATOM   4270  C  CE1 . HIS D  1 121 ? -2.807  213.158 12.624 1.00 27.38 ?  120 HIS D CE1 1 
ATOM   4271  N  NE2 . HIS D  1 121 ? -1.787  213.192 13.468 1.00 25.08 ?  120 HIS D NE2 1 
ATOM   4272  N  N   . GLU D  1 122 ? -0.602  215.995 7.936  1.00 20.91 ?  121 GLU D N   1 
ATOM   4273  C  CA  . GLU D  1 122 ? -0.574  216.706 6.660  1.00 24.57 ?  121 GLU D CA  1 
ATOM   4274  C  C   . GLU D  1 122 ? -0.425  218.210 6.863  1.00 27.30 ?  121 GLU D C   1 
ATOM   4275  O  O   . GLU D  1 122 ? 0.321   218.869 6.133  1.00 25.69 ?  121 GLU D O   1 
ATOM   4276  C  CB  . GLU D  1 122 ? -1.867  216.365 5.907  1.00 28.86 ?  121 GLU D CB  1 
ATOM   4277  C  CG  . GLU D  1 122 ? -2.190  217.085 4.594  1.00 40.73 ?  121 GLU D CG  1 
ATOM   4278  C  CD  . GLU D  1 122 ? -3.718  217.262 4.388  1.00 50.79 ?  121 GLU D CD  1 
ATOM   4279  O  OE1 . GLU D  1 122 ? -4.534  216.657 5.149  1.00 37.75 ?  121 GLU D OE1 1 
ATOM   4280  O  OE2 . GLU D  1 122 ? -4.106  217.992 3.447  1.00 56.23 ?  121 GLU D OE2 1 
ATOM   4281  N  N   . LYS D  1 123 ? -1.109  218.762 7.861  1.00 22.47 ?  122 LYS D N   1 
ATOM   4282  C  CA  . LYS D  1 123 ? -1.247  220.199 8.038  1.00 28.34 ?  122 LYS D CA  1 
ATOM   4283  C  C   . LYS D  1 123 ? -0.706  220.620 9.397  1.00 27.62 ?  122 LYS D C   1 
ATOM   4284  O  O   . LYS D  1 123 ? -0.369  219.787 10.244 1.00 25.23 ?  122 LYS D O   1 
ATOM   4285  C  CB  . LYS D  1 123 ? -2.722  220.625 7.949  1.00 28.96 ?  122 LYS D CB  1 
ATOM   4286  C  CG  . LYS D  1 123 ? -3.384  220.448 6.603  1.00 33.26 ?  122 LYS D CG  1 
ATOM   4287  C  CD  . LYS D  1 123 ? -4.837  220.837 6.791  1.00 41.58 ?  122 LYS D CD  1 
ATOM   4288  C  CE  . LYS D  1 123 ? -5.742  220.334 5.683  1.00 51.64 ?  122 LYS D CE  1 
ATOM   4289  N  NZ  . LYS D  1 123 ? -7.050  219.913 6.287  1.00 59.69 ?  122 LYS D NZ  1 
ATOM   4290  N  N   . ALA D  1 124 ? -0.671  221.937 9.607  1.00 25.29 ?  123 ALA D N   1 
ATOM   4291  C  CA  . ALA D  1 124 ? -0.316  222.480 10.914 1.00 27.36 ?  123 ALA D CA  1 
ATOM   4292  C  C   . ALA D  1 124 ? -1.365  222.104 11.954 1.00 27.29 ?  123 ALA D C   1 
ATOM   4293  O  O   . ALA D  1 124 ? -2.568  222.112 11.677 1.00 24.61 ?  123 ALA D O   1 
ATOM   4294  C  CB  . ALA D  1 124 ? -0.190  224.006 10.840 1.00 21.40 ?  123 ALA D CB  1 
ATOM   4295  N  N   . ASP D  1 125 ? -0.894  221.735 13.146 1.00 22.54 ?  124 ASP D N   1 
ATOM   4296  C  CA  . ASP D  1 125 ? -1.742  221.662 14.325 1.00 23.53 ?  124 ASP D CA  1 
ATOM   4297  C  C   . ASP D  1 125 ? -2.062  223.088 14.786 1.00 20.34 ?  124 ASP D C   1 
ATOM   4298  O  O   . ASP D  1 125 ? -1.145  223.870 15.045 1.00 22.58 ?  124 ASP D O   1 
ATOM   4299  C  CB  . ASP D  1 125 ? -1.003  220.877 15.407 1.00 20.34 ?  124 ASP D CB  1 
ATOM   4300  C  CG  . ASP D  1 125 ? -1.851  220.583 16.648 1.00 28.28 ?  124 ASP D CG  1 
ATOM   4301  O  OD1 . ASP D  1 125 ? -2.903  221.242 16.892 1.00 25.73 ?  124 ASP D OD1 1 
ATOM   4302  O  OD2 . ASP D  1 125 ? -1.443  219.658 17.397 1.00 28.88 ?  124 ASP D OD2 1 
ATOM   4303  N  N   . ASP D  1 126 ? -3.343  223.434 14.889 1.00 23.03 ?  125 ASP D N   1 
ATOM   4304  C  CA  . ASP D  1 126 ? -3.675  224.772 15.394 1.00 23.38 ?  125 ASP D CA  1 
ATOM   4305  C  C   . ASP D  1 126 ? -3.644  224.862 16.926 1.00 28.67 ?  125 ASP D C   1 
ATOM   4306  O  O   . ASP D  1 126 ? -4.062  225.881 17.486 1.00 24.52 ?  125 ASP D O   1 
ATOM   4307  C  CB  . ASP D  1 126 ? -5.030  225.261 14.841 1.00 20.34 ?  125 ASP D CB  1 
ATOM   4308  C  CG  . ASP D  1 126 ? -6.241  224.485 15.382 1.00 28.51 ?  125 ASP D CG  1 
ATOM   4309  O  OD1 . ASP D  1 126 ? -6.176  223.821 16.433 1.00 29.12 ?  125 ASP D OD1 1 
ATOM   4310  O  OD2 . ASP D  1 126 ? -7.292  224.527 14.716 1.00 28.70 ?  125 ASP D OD2 1 
ATOM   4311  N  N   . LEU D  1 127 ? -3.165  223.817 17.608 1.00 27.66 ?  126 LEU D N   1 
ATOM   4312  C  CA  . LEU D  1 127 ? -2.954  223.840 19.060 1.00 23.74 ?  126 LEU D CA  1 
ATOM   4313  C  C   . LEU D  1 127 ? -4.253  224.084 19.816 1.00 28.06 ?  126 LEU D C   1 
ATOM   4314  O  O   . LEU D  1 127 ? -4.255  224.584 20.950 1.00 24.58 ?  126 LEU D O   1 
ATOM   4315  C  CB  . LEU D  1 127 ? -1.882  224.873 19.447 1.00 25.03 ?  126 LEU D CB  1 
ATOM   4316  C  CG  . LEU D  1 127 ? -0.614  224.810 18.568 1.00 30.78 ?  126 LEU D CG  1 
ATOM   4317  C  CD1 . LEU D  1 127 ? 0.428   225.826 19.019 1.00 31.56 ?  126 LEU D CD1 1 
ATOM   4318  C  CD2 . LEU D  1 127 ? -0.008  223.410 18.530 1.00 20.34 ?  126 LEU D CD2 1 
ATOM   4319  N  N   . GLY D  1 128 ? -5.368  223.706 19.201 1.00 27.11 ?  127 GLY D N   1 
ATOM   4320  C  CA  . GLY D  1 128 ? -6.651  223.866 19.852 1.00 28.68 ?  127 GLY D CA  1 
ATOM   4321  C  C   . GLY D  1 128 ? -7.217  225.263 19.804 1.00 29.57 ?  127 GLY D C   1 
ATOM   4322  O  O   . GLY D  1 128 ? -8.195  225.545 20.508 1.00 20.34 ?  127 GLY D O   1 
ATOM   4323  N  N   . LYS D  1 129 ? -6.650  226.142 18.976 1.00 23.30 ?  128 LYS D N   1 
ATOM   4324  C  CA  . LYS D  1 129 ? -7.064  227.534 18.936 1.00 22.99 ?  128 LYS D CA  1 
ATOM   4325  C  C   . LYS D  1 129 ? -7.875  227.852 17.696 1.00 26.61 ?  128 LYS D C   1 
ATOM   4326  O  O   . LYS D  1 129 ? -8.060  229.029 17.375 1.00 26.59 ?  128 LYS D O   1 
ATOM   4327  C  CB  . LYS D  1 129 ? -5.838  228.446 19.008 1.00 26.86 ?  128 LYS D CB  1 
ATOM   4328  C  CG  . LYS D  1 129 ? -5.126  228.374 20.342 1.00 32.66 ?  128 LYS D CG  1 
ATOM   4329  C  CD  . LYS D  1 129 ? -3.721  228.926 20.249 1.00 37.95 ?  128 LYS D CD  1 
ATOM   4330  C  CE  . LYS D  1 129 ? -3.710  230.447 20.267 1.00 42.75 ?  128 LYS D CE  1 
ATOM   4331  N  NZ  . LYS D  1 129 ? -2.365  230.996 20.624 1.00 49.82 ?  128 LYS D NZ  1 
ATOM   4332  N  N   . GLY D  1 130 ? -8.347  226.826 16.987 1.00 21.80 ?  129 GLY D N   1 
ATOM   4333  C  CA  . GLY D  1 130 ? -9.037  227.006 15.724 1.00 25.67 ?  129 GLY D CA  1 
ATOM   4334  C  C   . GLY D  1 130 ? -10.498 227.392 15.813 1.00 24.73 ?  129 GLY D C   1 
ATOM   4335  O  O   . GLY D  1 130 ? -11.063 227.793 14.790 1.00 23.63 ?  129 GLY D O   1 
ATOM   4336  N  N   . GLY D  1 131 ? -11.133 227.259 16.986 1.00 23.84 ?  130 GLY D N   1 
ATOM   4337  C  CA  . GLY D  1 131 ? -12.513 227.693 17.172 1.00 20.34 ?  130 GLY D CA  1 
ATOM   4338  C  C   . GLY D  1 131 ? -13.597 226.825 16.548 1.00 27.32 ?  130 GLY D C   1 
ATOM   4339  O  O   . GLY D  1 131 ? -14.781 227.176 16.650 1.00 24.79 ?  130 GLY D O   1 
ATOM   4340  N  N   . ASN D  1 132 ? -13.247 225.725 15.882 1.00 27.55 ?  131 ASN D N   1 
ATOM   4341  C  CA  . ASN D  1 132 ? -14.228 224.770 15.377 1.00 27.55 ?  131 ASN D CA  1 
ATOM   4342  C  C   . ASN D  1 132 ? -14.132 223.466 16.165 1.00 30.32 ?  131 ASN D C   1 
ATOM   4343  O  O   . ASN D  1 132 ? -13.221 223.268 16.973 1.00 29.16 ?  131 ASN D O   1 
ATOM   4344  C  CB  . ASN D  1 132 ? -14.051 224.534 13.866 1.00 22.29 ?  131 ASN D CB  1 
ATOM   4345  C  CG  . ASN D  1 132 ? -12.759 223.809 13.521 1.00 27.45 ?  131 ASN D CG  1 
ATOM   4346  O  OD1 . ASN D  1 132 ? -11.842 223.724 14.327 1.00 30.73 ?  131 ASN D OD1 1 
ATOM   4347  N  ND2 . ASN D  1 132 ? -12.679 223.300 12.293 1.00 24.90 ?  131 ASN D ND2 1 
ATOM   4348  N  N   . GLU D  1 133 ? -15.103 222.574 15.955 1.00 30.46 ?  132 GLU D N   1 
ATOM   4349  C  CA  . GLU D  1 133 ? -15.106 221.331 16.719 1.00 31.82 ?  132 GLU D CA  1 
ATOM   4350  C  C   . GLU D  1 133 ? -13.834 220.546 16.478 1.00 27.88 ?  132 GLU D C   1 
ATOM   4351  O  O   . GLU D  1 133 ? -13.282 219.943 17.405 1.00 29.78 ?  132 GLU D O   1 
ATOM   4352  C  CB  . GLU D  1 133 ? -16.301 220.456 16.350 1.00 40.89 ?  132 GLU D CB  1 
ATOM   4353  C  CG  . GLU D  1 133 ? -17.565 221.198 15.998 1.00 45.85 ?  132 GLU D CG  1 
ATOM   4354  C  CD  . GLU D  1 133 ? -18.704 220.254 15.623 1.00 54.29 ?  132 GLU D CD  1 
ATOM   4355  O  OE1 . GLU D  1 133 ? -19.873 220.586 15.923 1.00 56.47 ?  132 GLU D OE1 1 
ATOM   4356  O  OE2 . GLU D  1 133 ? -18.425 219.192 15.014 1.00 58.51 ?  132 GLU D OE2 1 
ATOM   4357  N  N   . GLU D  1 134 ? -13.368 220.514 15.230 1.00 28.54 ?  133 GLU D N   1 
ATOM   4358  C  CA  . GLU D  1 134 ? -12.181 219.721 14.920 1.00 28.13 ?  133 GLU D CA  1 
ATOM   4359  C  C   . GLU D  1 134 ? -10.967 220.189 15.720 1.00 29.50 ?  133 GLU D C   1 
ATOM   4360  O  O   . GLU D  1 134 ? -10.135 219.371 16.126 1.00 29.97 ?  133 GLU D O   1 
ATOM   4361  C  CB  . GLU D  1 134 ? -11.905 219.780 13.416 1.00 27.90 ?  133 GLU D CB  1 
ATOM   4362  C  CG  . GLU D  1 134 ? -11.052 218.642 12.900 1.00 39.10 ?  133 GLU D CG  1 
ATOM   4363  C  CD  . GLU D  1 134 ? -11.707 217.291 13.127 1.00 45.06 ?  133 GLU D CD  1 
ATOM   4364  O  OE1 . GLU D  1 134 ? -12.739 216.999 12.487 1.00 51.89 ?  133 GLU D OE1 1 
ATOM   4365  O  OE2 . GLU D  1 134 ? -11.200 216.535 13.980 1.00 41.50 ?  133 GLU D OE2 1 
ATOM   4366  N  N   . SER D  1 135 ? -10.870 221.492 15.987 1.00 28.25 ?  134 SER D N   1 
ATOM   4367  C  CA  . SER D  1 135 ? -9.697  222.019 16.675 1.00 26.60 ?  134 SER D CA  1 
ATOM   4368  C  C   . SER D  1 135 ? -9.499  221.368 18.039 1.00 30.42 ?  134 SER D C   1 
ATOM   4369  O  O   . SER D  1 135 ? -8.364  221.137 18.465 1.00 29.97 ?  134 SER D O   1 
ATOM   4370  C  CB  . SER D  1 135 ? -9.831  223.533 16.831 1.00 23.53 ?  134 SER D CB  1 
ATOM   4371  O  OG  . SER D  1 135 ? -8.671  224.072 17.440 1.00 24.10 ?  134 SER D OG  1 
ATOM   4372  N  N   . THR D  1 136 ? -10.592 221.086 18.750 1.00 30.52 ?  135 THR D N   1 
ATOM   4373  C  CA  . THR D  1 136 ? -10.553 220.512 20.094 1.00 27.96 ?  135 THR D CA  1 
ATOM   4374  C  C   . THR D  1 136 ? -10.284 219.013 20.113 1.00 33.45 ?  135 THR D C   1 
ATOM   4375  O  O   . THR D  1 136 ? -10.090 218.447 21.202 1.00 32.17 ?  135 THR D O   1 
ATOM   4376  C  CB  . THR D  1 136 ? -11.896 220.784 20.791 1.00 29.07 ?  135 THR D CB  1 
ATOM   4377  O  OG1 . THR D  1 136 ? -12.865 219.858 20.280 1.00 39.86 ?  135 THR D OG1 1 
ATOM   4378  C  CG2 . THR D  1 136 ? -12.380 222.165 20.473 1.00 38.73 ?  135 THR D CG2 1 
ATOM   4379  N  N   . LYS D  1 137 ? -10.268 218.365 18.948 1.00 29.31 ?  136 LYS D N   1 
ATOM   4380  C  CA  . LYS D  1 137 ? -9.965  216.948 18.801 1.00 30.07 ?  136 LYS D CA  1 
ATOM   4381  C  C   . LYS D  1 137 ? -8.626  216.687 18.126 1.00 30.18 ?  136 LYS D C   1 
ATOM   4382  O  O   . LYS D  1 137 ? -7.808  215.928 18.650 1.00 28.55 ?  136 LYS D O   1 
ATOM   4383  C  CB  . LYS D  1 137 ? -11.081 216.276 17.990 1.00 32.44 ?  136 LYS D CB  1 
ATOM   4384  C  CG  . LYS D  1 137 ? -12.454 216.591 18.509 1.00 37.89 ?  136 LYS D CG  1 
ATOM   4385  C  CD  . LYS D  1 137 ? -13.492 215.633 17.948 1.00 47.49 ?  136 LYS D CD  1 
ATOM   4386  C  CE  . LYS D  1 137 ? -14.904 216.121 18.275 1.00 53.27 ?  136 LYS D CE  1 
ATOM   4387  N  NZ  . LYS D  1 137 ? -15.730 216.326 17.038 1.00 57.58 ?  136 LYS D NZ  1 
ATOM   4388  N  N   . THR D  1 138 ? -8.388  217.255 16.941 1.00 27.41 ?  137 THR D N   1 
ATOM   4389  C  CA  . THR D  1 138 ? -7.169  216.970 16.201 1.00 28.32 ?  137 THR D CA  1 
ATOM   4390  C  C   . THR D  1 138 ? -6.320  218.194 15.921 1.00 27.49 ?  137 THR D C   1 
ATOM   4391  O  O   . THR D  1 138 ? -5.289  218.057 15.257 1.00 27.25 ?  137 THR D O   1 
ATOM   4392  C  CB  . THR D  1 138 ? -7.491  216.307 14.855 1.00 33.16 ?  137 THR D CB  1 
ATOM   4393  O  OG1 . THR D  1 138 ? -8.206  217.239 14.032 1.00 30.22 ?  137 THR D OG1 1 
ATOM   4394  C  CG2 . THR D  1 138 ? -8.340  215.042 15.046 1.00 33.38 ?  137 THR D CG2 1 
ATOM   4395  N  N   . GLY D  1 139 ? -6.732  219.380 16.364 1.00 24.22 ?  138 GLY D N   1 
ATOM   4396  C  CA  . GLY D  1 139 ? -6.040  220.588 15.941 1.00 21.04 ?  138 GLY D CA  1 
ATOM   4397  C  C   . GLY D  1 139 ? -6.143  220.896 14.454 1.00 25.01 ?  138 GLY D C   1 
ATOM   4398  O  O   . GLY D  1 139 ? -5.372  221.702 13.950 1.00 21.40 ?  138 GLY D O   1 
ATOM   4399  N  N   . ASN D  1 140 ? -7.088  220.277 13.743 1.00 27.80 ?  139 ASN D N   1 
ATOM   4400  C  CA  . ASN D  1 140 ? -7.218  220.427 12.286 1.00 22.81 ?  139 ASN D CA  1 
ATOM   4401  C  C   . ASN D  1 140 ? -5.933  220.046 11.563 1.00 25.70 ?  139 ASN D C   1 
ATOM   4402  O  O   . ASN D  1 140 ? -5.616  220.615 10.520 1.00 27.28 ?  139 ASN D O   1 
ATOM   4403  C  CB  . ASN D  1 140 ? -7.611  221.866 11.889 1.00 23.44 ?  139 ASN D CB  1 
ATOM   4404  C  CG  . ASN D  1 140 ? -9.010  222.225 12.321 1.00 28.34 ?  139 ASN D CG  1 
ATOM   4405  O  OD1 . ASN D  1 140 ? -9.992  221.791 11.717 1.00 28.71 ?  139 ASN D OD1 1 
ATOM   4406  N  ND2 . ASN D  1 140 ? -9.114  223.015 13.384 1.00 26.43 ?  139 ASN D ND2 1 
ATOM   4407  N  N   . ALA D  1 141 ? -5.149  219.116 12.113 1.00 26.60 ?  140 ALA D N   1 
ATOM   4408  C  CA  . ALA D  1 141 ? -3.875  218.786 11.484 1.00 24.06 ?  140 ALA D CA  1 
ATOM   4409  C  C   . ALA D  1 141 ? -4.030  217.916 10.233 1.00 22.09 ?  140 ALA D C   1 
ATOM   4410  O  O   . ALA D  1 141 ? -3.038  217.693 9.524  1.00 25.52 ?  140 ALA D O   1 
ATOM   4411  C  CB  . ALA D  1 141 ? -2.948  218.092 12.495 1.00 20.34 ?  140 ALA D CB  1 
ATOM   4412  N  N   . GLY D  1 142 ? -5.218  217.396 9.962  1.00 22.75 ?  141 GLY D N   1 
ATOM   4413  C  CA  . GLY D  1 142 ? -5.454  216.754 8.682  1.00 26.88 ?  141 GLY D CA  1 
ATOM   4414  C  C   . GLY D  1 142 ? -4.949  215.320 8.645  1.00 27.39 ?  141 GLY D C   1 
ATOM   4415  O  O   . GLY D  1 142 ? -4.841  214.640 9.661  1.00 26.27 ?  141 GLY D O   1 
ATOM   4416  N  N   . SER D  1 143 ? -4.607  214.864 7.447  1.00 26.66 ?  142 SER D N   1 
ATOM   4417  C  CA  . SER D  1 143 ? -4.429  213.430 7.294  1.00 28.75 ?  142 SER D CA  1 
ATOM   4418  C  C   . SER D  1 143 ? -3.060  212.970 7.823  1.00 23.19 ?  142 SER D C   1 
ATOM   4419  O  O   . SER D  1 143 ? -2.150  213.761 8.098  1.00 22.81 ?  142 SER D O   1 
ATOM   4420  C  CB  . SER D  1 143 ? -4.635  213.039 5.829  1.00 30.79 ?  142 SER D CB  1 
ATOM   4421  O  OG  . SER D  1 143 ? -3.664  213.660 5.035  1.00 40.46 ?  142 SER D OG  1 
ATOM   4422  N  N   . ARG D  1 144 ? -2.929  211.656 7.958  1.00 23.15 ?  143 ARG D N   1 
ATOM   4423  C  CA  . ARG D  1 144 ? -1.754  211.031 8.552  1.00 27.19 ?  143 ARG D CA  1 
ATOM   4424  C  C   . ARG D  1 144 ? -0.770  210.670 7.443  1.00 28.12 ?  143 ARG D C   1 
ATOM   4425  O  O   . ARG D  1 144 ? -1.006  209.733 6.674  1.00 32.16 ?  143 ARG D O   1 
ATOM   4426  C  CB  . ARG D  1 144 ? -2.188  209.808 9.356  1.00 22.33 ?  143 ARG D CB  1 
ATOM   4427  C  CG  . ARG D  1 144 ? -3.331  210.151 10.329 1.00 21.50 ?  143 ARG D CG  1 
ATOM   4428  C  CD  . ARG D  1 144 ? -3.911  208.958 11.081 1.00 20.90 ?  143 ARG D CD  1 
ATOM   4429  N  NE  . ARG D  1 144 ? -5.007  209.417 11.925 1.00 27.29 ?  143 ARG D NE  1 
ATOM   4430  C  CZ  . ARG D  1 144 ? -5.477  208.797 12.998 1.00 30.94 ?  143 ARG D CZ  1 
ATOM   4431  N  NH1 . ARG D  1 144 ? -4.968  207.648 13.414 1.00 28.89 ?  143 ARG D NH1 1 
ATOM   4432  N  NH2 . ARG D  1 144 ? -6.480  209.349 13.679 1.00 23.88 ?  143 ARG D NH2 1 
ATOM   4433  N  N   . LEU D  1 145 ? 0.342   211.403 7.368  1.00 24.18 ?  144 LEU D N   1 
ATOM   4434  C  CA  . LEU D  1 145 ? 1.309   211.186 6.294  1.00 23.50 ?  144 LEU D CA  1 
ATOM   4435  C  C   . LEU D  1 145 ? 2.192   209.971 6.555  1.00 27.86 ?  144 LEU D C   1 
ATOM   4436  O  O   . LEU D  1 145 ? 2.524   209.237 5.622  1.00 29.93 ?  144 LEU D O   1 
ATOM   4437  C  CB  . LEU D  1 145 ? 2.164   212.438 6.115  1.00 21.45 ?  144 LEU D CB  1 
ATOM   4438  C  CG  . LEU D  1 145 ? 1.376   213.680 5.674  1.00 24.78 ?  144 LEU D CG  1 
ATOM   4439  C  CD1 . LEU D  1 145 ? 2.339   214.829 5.331  1.00 25.71 ?  144 LEU D CD1 1 
ATOM   4440  C  CD2 . LEU D  1 145 ? 0.495   213.335 4.475  1.00 30.20 ?  144 LEU D CD2 1 
ATOM   4441  N  N   . ALA D  1 146 ? 2.582   209.738 7.805  1.00 21.40 ?  145 ALA D N   1 
ATOM   4442  C  CA  . ALA D  1 146 ? 3.481   208.643 8.143  1.00 21.56 ?  145 ALA D CA  1 
ATOM   4443  C  C   . ALA D  1 146 ? 3.357   208.397 9.632  1.00 26.05 ?  145 ALA D C   1 
ATOM   4444  O  O   . ALA D  1 146 ? 2.981   209.296 10.389 1.00 22.51 ?  145 ALA D O   1 
ATOM   4445  C  CB  . ALA D  1 146 ? 4.932   208.952 7.775  1.00 20.34 ?  145 ALA D CB  1 
ATOM   4446  N  N   . CYS D  1 147 ? 3.669   207.169 10.040 1.00 21.39 ?  146 CYS D N   1 
ATOM   4447  C  CA  . CYS D  1 147 ? 3.532   206.773 11.435 1.00 24.84 ?  146 CYS D CA  1 
ATOM   4448  C  C   . CYS D  1 147 ? 4.402   205.553 11.702 1.00 25.09 ?  146 CYS D C   1 
ATOM   4449  O  O   . CYS D  1 147 ? 4.931   204.913 10.782 1.00 21.59 ?  146 CYS D O   1 
ATOM   4450  C  CB  . CYS D  1 147 ? 2.075   206.468 11.780 1.00 22.79 ?  146 CYS D CB  1 
ATOM   4451  S  SG  . CYS D  1 147 ? 1.327   205.115 10.765 1.00 35.00 ?  146 CYS D SG  1 
ATOM   4452  N  N   . GLY D  1 148 ? 4.540   205.237 12.987 1.00 25.95 ?  147 GLY D N   1 
ATOM   4453  C  CA  . GLY D  1 148 ? 5.205   204.010 13.387 1.00 24.44 ?  147 GLY D CA  1 
ATOM   4454  C  C   . GLY D  1 148 ? 4.895   203.721 14.835 1.00 24.75 ?  147 GLY D C   1 
ATOM   4455  O  O   . GLY D  1 148 ? 4.447   204.597 15.579 1.00 23.57 ?  147 GLY D O   1 
ATOM   4456  N  N   . VAL D  1 149 ? 5.124   202.482 15.226 1.00 23.02 ?  148 VAL D N   1 
ATOM   4457  C  CA  . VAL D  1 149 ? 4.946   202.097 16.617 1.00 20.34 ?  148 VAL D CA  1 
ATOM   4458  C  C   . VAL D  1 149 ? 6.203   202.466 17.390 1.00 23.80 ?  148 VAL D C   1 
ATOM   4459  O  O   . VAL D  1 149 ? 7.331   202.221 16.935 1.00 26.10 ?  148 VAL D O   1 
ATOM   4460  C  CB  . VAL D  1 149 ? 4.626   200.599 16.730 1.00 25.21 ?  148 VAL D CB  1 
ATOM   4461  C  CG1 . VAL D  1 149 ? 4.373   200.222 18.180 1.00 20.34 ?  148 VAL D CG1 1 
ATOM   4462  C  CG2 . VAL D  1 149 ? 3.421   200.233 15.833 1.00 22.14 ?  148 VAL D CG2 1 
ATOM   4463  N  N   . ILE D  1 150 ? 6.013   203.097 18.547 1.00 21.65 ?  149 ILE D N   1 
ATOM   4464  C  CA  . ILE D  1 150 ? 7.119   203.504 19.407 1.00 21.11 ?  149 ILE D CA  1 
ATOM   4465  C  C   . ILE D  1 150 ? 7.643   202.291 20.162 1.00 23.68 ?  149 ILE D C   1 
ATOM   4466  O  O   . ILE D  1 150 ? 6.920   201.683 20.963 1.00 23.25 ?  149 ILE D O   1 
ATOM   4467  C  CB  . ILE D  1 150 ? 6.664   204.594 20.386 1.00 24.06 ?  149 ILE D CB  1 
ATOM   4468  C  CG1 . ILE D  1 150 ? 6.155   205.825 19.640 1.00 20.65 ?  149 ILE D CG1 1 
ATOM   4469  C  CG2 . ILE D  1 150 ? 7.780   204.951 21.365 1.00 26.26 ?  149 ILE D CG2 1 
ATOM   4470  C  CD1 . ILE D  1 150 ? 5.386   206.770 20.544 1.00 25.55 ?  149 ILE D CD1 1 
ATOM   4471  N  N   . GLY D  1 151 ? 8.912   201.959 19.957 1.00 21.66 ?  150 GLY D N   1 
ATOM   4472  C  CA  . GLY D  1 151 ? 9.435   200.759 20.597 1.00 24.75 ?  150 GLY D CA  1 
ATOM   4473  C  C   . GLY D  1 151 ? 10.552  201.038 21.584 1.00 24.87 ?  150 GLY D C   1 
ATOM   4474  O  O   . GLY D  1 151 ? 11.199  202.080 21.492 1.00 23.35 ?  150 GLY D O   1 
ATOM   4475  N  N   . ILE D  1 152 ? 10.782  200.118 22.528 1.00 26.12 ?  151 ILE D N   1 
ATOM   4476  C  CA  . ILE D  1 152 ? 11.888  200.256 23.470 1.00 26.59 ?  151 ILE D CA  1 
ATOM   4477  C  C   . ILE D  1 152 ? 13.198  200.191 22.714 1.00 27.52 ?  151 ILE D C   1 
ATOM   4478  O  O   . ILE D  1 152 ? 13.403  199.297 21.884 1.00 28.37 ?  151 ILE D O   1 
ATOM   4479  C  CB  . ILE D  1 152 ? 11.837  199.157 24.541 1.00 29.74 ?  151 ILE D CB  1 
ATOM   4480  C  CG1 . ILE D  1 152 ? 10.525  199.227 25.310 1.00 30.41 ?  151 ILE D CG1 1 
ATOM   4481  C  CG2 . ILE D  1 152 ? 13.009  199.320 25.530 1.00 31.84 ?  151 ILE D CG2 1 
ATOM   4482  C  CD1 . ILE D  1 152 ? 10.191  197.927 26.025 1.00 37.31 ?  151 ILE D CD1 1 
ATOM   4483  N  N   . ALA D  1 153 ? 14.095  201.135 22.993 1.00 25.26 ?  152 ALA D N   1 
ATOM   4484  C  CA  . ALA D  1 153 ? 15.400  201.144 22.350 1.00 28.01 ?  152 ALA D CA  1 
ATOM   4485  C  C   . ALA D  1 153 ? 16.497  200.844 23.364 1.00 30.08 ?  152 ALA D C   1 
ATOM   4486  O  O   . ALA D  1 153 ? 16.314  200.983 24.576 1.00 31.16 ?  152 ALA D O   1 
ATOM   4487  C  CB  . ALA D  1 153 ? 15.672  202.493 21.665 1.00 25.98 ?  152 ALA D CB  1 
ATOM   4488  N  N   . GLN D  1 154 ? 17.655  200.453 22.848 1.00 32.47 ?  153 GLN D N   1 
ATOM   4489  C  CA  . GLN D  1 154 ? 18.800  200.100 23.693 1.00 38.70 ?  153 GLN D CA  1 
ATOM   4490  C  C   . GLN D  1 154 ? 19.408  201.317 24.369 1.00 48.82 ?  153 GLN D C   1 
ATOM   4491  O  O   . GLN D  1 154 ? 19.647  202.338 23.715 1.00 57.57 ?  153 GLN D O   1 
ATOM   4492  C  CB  . GLN D  1 154 ? 19.864  199.392 22.868 1.00 35.25 ?  153 GLN D CB  1 
ATOM   4493  C  CG  . GLN D  1 154 ? 20.833  198.556 23.669 1.00 46.42 ?  153 GLN D CG  1 
ATOM   4494  C  CD  . GLN D  1 154 ? 21.967  198.024 22.816 1.00 50.45 ?  153 GLN D CD  1 
ATOM   4495  O  OE1 . GLN D  1 154 ? 22.351  196.865 22.948 1.00 55.82 ?  153 GLN D OE1 1 
ATOM   4496  N  NE2 . GLN D  1 154 ? 22.513  198.867 21.940 1.00 51.31 ?  153 GLN D NE2 1 
ATOM   4497  O  OXT . GLN D  1 154 ? 19.675  201.296 25.573 1.00 61.31 ?  153 GLN D OXT 1 
ATOM   4498  N  N   . ALA E  3 1   ? 28.288  251.006 39.186 1.00 60.52 ?  0   ALA E N   1 
ATOM   4499  C  CA  . ALA E  3 1   ? 27.335  250.467 40.165 1.00 65.21 ?  0   ALA E CA  1 
ATOM   4500  C  C   . ALA E  3 1   ? 27.426  251.179 41.524 1.00 56.26 ?  0   ALA E C   1 
ATOM   4501  O  O   . ALA E  3 1   ? 26.821  252.235 41.728 1.00 59.10 ?  0   ALA E O   1 
ATOM   4502  C  CB  . ALA E  3 1   ? 27.546  248.949 40.350 1.00 55.21 ?  0   ALA E CB  1 
ATOM   4503  N  N   . ALA E  3 2   ? 28.178  250.591 42.453 1.00 53.21 ?  1   ALA E N   1 
ATOM   4504  C  CA  . ALA E  3 2   ? 28.271  251.134 43.803 1.00 50.61 ?  1   ALA E CA  1 
ATOM   4505  C  C   . ALA E  3 2   ? 29.215  252.334 43.837 1.00 36.87 ?  1   ALA E C   1 
ATOM   4506  O  O   . ALA E  3 2   ? 30.233  252.365 43.141 1.00 45.14 ?  1   ALA E O   1 
ATOM   4507  C  CB  . ALA E  3 2   ? 28.744  250.051 44.774 1.00 38.50 ?  1   ALA E CB  1 
ATOM   4508  N  N   . THR E  3 3   ? 28.855  253.342 44.622 1.00 37.23 ?  2   THR E N   1 
ATOM   4509  C  CA  . THR E  3 3   ? 29.710  254.502 44.791 1.00 35.03 ?  2   THR E CA  1 
ATOM   4510  C  C   . THR E  3 3   ? 30.181  254.692 46.225 1.00 36.57 ?  2   THR E C   1 
ATOM   4511  O  O   . THR E  3 3   ? 31.105  255.479 46.452 1.00 34.28 ?  2   THR E O   1 
ATOM   4512  C  CB  . THR E  3 3   ? 28.998  255.784 44.330 1.00 40.56 ?  2   THR E CB  1 
ATOM   4513  O  OG1 . THR E  3 3   ? 27.822  255.985 45.121 1.00 41.98 ?  2   THR E OG1 1 
ATOM   4514  C  CG2 . THR E  3 3   ? 28.629  255.702 42.835 1.00 41.23 ?  2   THR E CG2 1 
ATOM   4515  N  N   . LYS E  3 4   ? 29.581  253.996 47.185 1.00 33.51 ?  3   LYS E N   1 
ATOM   4516  C  CA  . LYS E  3 4   ? 29.896  254.130 48.596 1.00 31.99 ?  3   LYS E CA  1 
ATOM   4517  C  C   . LYS E  3 4   ? 29.911  252.744 49.215 1.00 31.05 ?  3   LYS E C   1 
ATOM   4518  O  O   . LYS E  3 4   ? 29.060  251.908 48.896 1.00 30.11 ?  3   LYS E O   1 
ATOM   4519  C  CB  . LYS E  3 4   ? 28.873  255.010 49.312 1.00 38.19 ?  3   LYS E CB  1 
ATOM   4520  C  CG  . LYS E  3 4   ? 29.160  256.509 49.245 1.00 49.87 ?  3   LYS E CG  1 
ATOM   4521  C  CD  . LYS E  3 4   ? 29.092  257.114 50.654 1.00 59.76 ?  3   LYS E CD  1 
ATOM   4522  C  CE  . LYS E  3 4   ? 30.316  256.715 51.505 1.00 53.38 ?  3   LYS E CE  1 
ATOM   4523  N  NZ  . LYS E  3 4   ? 30.584  257.754 52.538 1.00 59.79 ?  3   LYS E NZ  1 
ATOM   4524  N  N   . ALA E  3 5   ? 30.880  252.492 50.093 1.00 28.66 ?  4   ALA E N   1 
ATOM   4525  C  CA  . ALA E  3 5   ? 30.928  251.233 50.821 1.00 29.41 ?  4   ALA E CA  1 
ATOM   4526  C  C   . ALA E  3 5   ? 31.410  251.525 52.232 1.00 32.05 ?  4   ALA E C   1 
ATOM   4527  O  O   . ALA E  3 5   ? 31.835  252.635 52.539 1.00 29.49 ?  4   ALA E O   1 
ATOM   4528  C  CB  . ALA E  3 5   ? 31.822  250.195 50.128 1.00 22.43 ?  4   ALA E CB  1 
ATOM   4529  N  N   . VAL E  3 6   ? 31.335  250.519 53.102 1.00 28.69 ?  5   VAL E N   1 
ATOM   4530  C  CA  . VAL E  3 6   ? 31.711  250.696 54.501 1.00 29.61 ?  5   VAL E CA  1 
ATOM   4531  C  C   . VAL E  3 6   ? 32.159  249.350 55.043 1.00 33.04 ?  5   VAL E C   1 
ATOM   4532  O  O   . VAL E  3 6   ? 31.728  248.293 54.573 1.00 32.21 ?  5   VAL E O   1 
ATOM   4533  C  CB  . VAL E  3 6   ? 30.555  251.282 55.344 1.00 32.90 ?  5   VAL E CB  1 
ATOM   4534  C  CG1 . VAL E  3 6   ? 29.469  250.247 55.547 1.00 33.66 ?  5   VAL E CG1 1 
ATOM   4535  C  CG2 . VAL E  3 6   ? 31.064  251.799 56.693 1.00 30.27 ?  5   VAL E CG2 1 
ATOM   4536  N  N   . CYS E  3 7   ? 33.040  249.394 56.031 1.00 31.35 ?  6   CYS E N   1 
ATOM   4537  C  CA  . CYS E  3 7   ? 33.572  248.178 56.613 1.00 30.58 ?  6   CYS E CA  1 
ATOM   4538  C  C   . CYS E  3 7   ? 33.742  248.395 58.108 1.00 33.06 ?  6   CYS E C   1 
ATOM   4539  O  O   . CYS E  3 7   ? 34.360  249.375 58.531 1.00 29.72 ?  6   CYS E O   1 
ATOM   4540  C  CB  . CYS E  3 7   ? 34.903  247.804 55.968 1.00 31.01 ?  6   CYS E CB  1 
ATOM   4541  S  SG  . CYS E  3 7   ? 35.631  246.305 56.657 1.00 34.52 ?  6   CYS E SG  1 
ATOM   4542  N  N   . VAL E  3 8   ? 33.170  247.505 58.896 1.00 27.69 ?  7   VAL E N   1 
ATOM   4543  C  CA  . VAL E  3 8   ? 33.322  247.510 60.338 1.00 32.80 ?  7   VAL E CA  1 
ATOM   4544  C  C   . VAL E  3 8   ? 34.372  246.464 60.676 1.00 31.00 ?  7   VAL E C   1 
ATOM   4545  O  O   . VAL E  3 8   ? 34.174  245.270 60.428 1.00 31.39 ?  7   VAL E O   1 
ATOM   4546  C  CB  . VAL E  3 8   ? 31.993  247.218 61.042 1.00 31.78 ?  7   VAL E CB  1 
ATOM   4547  C  CG1 . VAL E  3 8   ? 32.216  247.165 62.555 1.00 34.23 ?  7   VAL E CG1 1 
ATOM   4548  C  CG2 . VAL E  3 8   ? 30.974  248.288 60.690 1.00 32.37 ?  7   VAL E CG2 1 
ATOM   4549  N  N   . LEU E  3 9   ? 35.511  246.901 61.198 1.00 29.63 ?  8   LEU E N   1 
ATOM   4550  C  CA  . LEU E  3 9   ? 36.576  245.979 61.563 1.00 31.20 ?  8   LEU E CA  1 
ATOM   4551  C  C   . LEU E  3 9   ? 36.396  245.547 63.013 1.00 32.71 ?  8   LEU E C   1 
ATOM   4552  O  O   . LEU E  3 9   ? 36.189  246.389 63.895 1.00 31.56 ?  8   LEU E O   1 
ATOM   4553  C  CB  . LEU E  3 9   ? 37.942  246.630 61.383 1.00 35.36 ?  8   LEU E CB  1 
ATOM   4554  C  CG  . LEU E  3 9   ? 38.311  247.151 59.997 1.00 36.20 ?  8   LEU E CG  1 
ATOM   4555  C  CD1 . LEU E  3 9   ? 39.343  248.246 60.157 1.00 39.66 ?  8   LEU E CD1 1 
ATOM   4556  C  CD2 . LEU E  3 9   ? 38.879  246.032 59.189 1.00 36.36 ?  8   LEU E CD2 1 
ATOM   4557  N  N   . LYS E  3 10  ? 36.509  244.236 63.244 1.00 32.97 ?  9   LYS E N   1 
ATOM   4558  C  CA  . LYS E  3 10  ? 36.377  243.593 64.546 1.00 33.44 ?  9   LYS E CA  1 
ATOM   4559  C  C   . LYS E  3 10  ? 37.350  242.425 64.577 1.00 32.94 ?  9   LYS E C   1 
ATOM   4560  O  O   . LYS E  3 10  ? 37.670  241.841 63.534 1.00 30.77 ?  9   LYS E O   1 
ATOM   4561  C  CB  . LYS E  3 10  ? 34.953  243.055 64.793 1.00 35.79 ?  9   LYS E CB  1 
ATOM   4562  C  CG  . LYS E  3 10  ? 33.875  244.118 64.949 1.00 42.25 ?  9   LYS E CG  1 
ATOM   4563  C  CD  . LYS E  3 10  ? 34.282  245.213 65.925 1.00 52.75 ?  9   LYS E CD  1 
ATOM   4564  C  CE  . LYS E  3 10  ? 33.260  246.370 65.964 1.00 51.87 ?  9   LYS E CE  1 
ATOM   4565  N  NZ  . LYS E  3 10  ? 33.862  247.651 65.474 1.00 47.05 ?  9   LYS E NZ  1 
ATOM   4566  N  N   . GLY E  3 11  ? 37.787  242.049 65.776 1.00 35.10 ?  10  GLY E N   1 
ATOM   4567  C  CA  . GLY E  3 11  ? 38.722  240.945 65.888 1.00 31.87 ?  10  GLY E CA  1 
ATOM   4568  C  C   . GLY E  3 11  ? 38.616  240.255 67.230 1.00 39.21 ?  10  GLY E C   1 
ATOM   4569  O  O   . GLY E  3 11  ? 37.733  240.551 68.038 1.00 35.87 ?  10  GLY E O   1 
ATOM   4570  N  N   . ASP E  3 12  ? 39.542  239.325 67.464 1.00 41.64 ?  11  ASP E N   1 
ATOM   4571  C  CA  . ASP E  3 12  ? 39.559  238.622 68.742 1.00 42.59 ?  11  ASP E CA  1 
ATOM   4572  C  C   . ASP E  3 12  ? 39.929  239.553 69.888 1.00 51.35 ?  11  ASP E C   1 
ATOM   4573  O  O   . ASP E  3 12  ? 39.497  239.336 71.025 1.00 55.05 ?  11  ASP E O   1 
ATOM   4574  C  CB  . ASP E  3 12  ? 40.534  237.454 68.678 1.00 50.34 ?  11  ASP E CB  1 
ATOM   4575  C  CG  . ASP E  3 12  ? 39.927  236.236 68.011 1.00 63.13 ?  11  ASP E CG  1 
ATOM   4576  O  OD1 . ASP E  3 12  ? 38.683  236.104 68.060 1.00 65.33 ?  11  ASP E OD1 1 
ATOM   4577  O  OD2 . ASP E  3 12  ? 40.686  235.429 67.422 1.00 69.33 ?  11  ASP E OD2 1 
ATOM   4578  N  N   . GLY E  3 13  ? 40.695  240.605 69.606 1.00 46.76 ?  12  GLY E N   1 
ATOM   4579  C  CA  . GLY E  3 13  ? 41.204  241.474 70.632 1.00 39.07 ?  12  GLY E CA  1 
ATOM   4580  C  C   . GLY E  3 13  ? 40.527  242.820 70.645 1.00 42.70 ?  12  GLY E C   1 
ATOM   4581  O  O   . GLY E  3 13  ? 39.339  242.957 70.336 1.00 44.71 ?  12  GLY E O   1 
ATOM   4582  N  N   . PRO E  3 14  ? 41.286  243.852 71.025 1.00 40.31 ?  13  PRO E N   1 
ATOM   4583  C  CA  . PRO E  3 14  ? 40.699  245.183 71.192 1.00 40.69 ?  13  PRO E CA  1 
ATOM   4584  C  C   . PRO E  3 14  ? 40.630  245.991 69.915 1.00 39.07 ?  13  PRO E C   1 
ATOM   4585  O  O   . PRO E  3 14  ? 40.045  247.079 69.941 1.00 37.93 ?  13  PRO E O   1 
ATOM   4586  C  CB  . PRO E  3 14  ? 41.647  245.843 72.196 1.00 40.02 ?  13  PRO E CB  1 
ATOM   4587  C  CG  . PRO E  3 14  ? 42.994  245.253 71.829 1.00 34.53 ?  13  PRO E CG  1 
ATOM   4588  C  CD  . PRO E  3 14  ? 42.724  243.836 71.363 1.00 39.06 ?  13  PRO E CD  1 
ATOM   4589  N  N   . VAL E  3 15  ? 41.222  245.519 68.814 1.00 38.32 ?  14  VAL E N   1 
ATOM   4590  C  CA  . VAL E  3 15  ? 41.272  246.322 67.594 1.00 34.07 ?  14  VAL E CA  1 
ATOM   4591  C  C   . VAL E  3 15  ? 39.881  246.414 66.984 1.00 38.40 ?  14  VAL E C   1 
ATOM   4592  O  O   . VAL E  3 15  ? 39.223  245.395 66.729 1.00 33.73 ?  14  VAL E O   1 
ATOM   4593  C  CB  . VAL E  3 15  ? 42.269  245.730 66.590 1.00 35.12 ?  14  VAL E CB  1 
ATOM   4594  C  CG1 . VAL E  3 15  ? 42.300  246.583 65.343 1.00 31.23 ?  14  VAL E CG1 1 
ATOM   4595  C  CG2 . VAL E  3 15  ? 43.654  245.672 67.198 1.00 34.15 ?  14  VAL E CG2 1 
ATOM   4596  N  N   . GLN E  3 16  ? 39.438  247.637 66.720 1.00 35.94 ?  15  GLN E N   1 
ATOM   4597  C  CA  . GLN E  3 16  ? 38.147  247.839 66.089 1.00 36.77 ?  15  GLN E CA  1 
ATOM   4598  C  C   . GLN E  3 16  ? 38.140  249.177 65.363 1.00 39.23 ?  15  GLN E C   1 
ATOM   4599  O  O   . GLN E  3 16  ? 38.918  250.083 65.677 1.00 32.94 ?  15  GLN E O   1 
ATOM   4600  C  CB  . GLN E  3 16  ? 37.020  247.743 67.117 1.00 38.31 ?  15  GLN E CB  1 
ATOM   4601  C  CG  . GLN E  3 16  ? 36.861  248.934 68.020 1.00 44.96 ?  15  GLN E CG  1 
ATOM   4602  C  CD  . GLN E  3 16  ? 35.708  248.739 69.003 1.00 55.42 ?  15  GLN E CD  1 
ATOM   4603  O  OE1 . GLN E  3 16  ? 35.796  247.924 69.928 1.00 55.43 ?  15  GLN E OE1 1 
ATOM   4604  N  NE2 . GLN E  3 16  ? 34.617  249.481 68.799 1.00 57.78 ?  15  GLN E NE2 1 
ATOM   4605  N  N   . GLY E  3 17  ? 37.255  249.289 64.384 1.00 35.74 ?  16  GLY E N   1 
ATOM   4606  C  CA  . GLY E  3 17  ? 37.245  250.495 63.575 1.00 36.33 ?  16  GLY E CA  1 
ATOM   4607  C  C   . GLY E  3 17  ? 36.191  250.448 62.491 1.00 35.25 ?  16  GLY E C   1 
ATOM   4608  O  O   . GLY E  3 17  ? 35.562  249.416 62.233 1.00 34.18 ?  16  GLY E O   1 
ATOM   4609  N  N   . ILE E  3 18  ? 36.023  251.602 61.850 1.00 33.68 ?  17  ILE E N   1 
ATOM   4610  C  CA  . ILE E  3 18  ? 35.038  251.825 60.800 1.00 32.53 ?  17  ILE E CA  1 
ATOM   4611  C  C   . ILE E  3 18  ? 35.754  252.505 59.637 1.00 36.69 ?  17  ILE E C   1 
ATOM   4612  O  O   . ILE E  3 18  ? 36.332  253.589 59.805 1.00 33.51 ?  17  ILE E O   1 
ATOM   4613  C  CB  . ILE E  3 18  ? 33.870  252.690 61.299 1.00 33.32 ?  17  ILE E CB  1 
ATOM   4614  C  CG1 . ILE E  3 18  ? 33.179  252.013 62.485 1.00 34.70 ?  17  ILE E CG1 1 
ATOM   4615  C  CG2 . ILE E  3 18  ? 32.893  253.008 60.158 1.00 33.43 ?  17  ILE E CG2 1 
ATOM   4616  C  CD1 . ILE E  3 18  ? 31.901  252.693 62.881 1.00 34.98 ?  17  ILE E CD1 1 
ATOM   4617  N  N   . ILE E  3 19  ? 35.722  251.873 58.470 1.00 31.17 ?  18  ILE E N   1 
ATOM   4618  C  CA  . ILE E  3 19  ? 36.418  252.364 57.292 1.00 31.51 ?  18  ILE E CA  1 
ATOM   4619  C  C   . ILE E  3 19  ? 35.377  252.639 56.221 1.00 38.62 ?  18  ILE E C   1 
ATOM   4620  O  O   . ILE E  3 19  ? 34.592  251.746 55.870 1.00 32.91 ?  18  ILE E O   1 
ATOM   4621  C  CB  . ILE E  3 19  ? 37.470  251.362 56.800 1.00 32.29 ?  18  ILE E CB  1 
ATOM   4622  C  CG1 . ILE E  3 19  ? 38.538  251.180 57.866 1.00 31.88 ?  18  ILE E CG1 1 
ATOM   4623  C  CG2 . ILE E  3 19  ? 38.135  251.869 55.529 1.00 31.82 ?  18  ILE E CG2 1 
ATOM   4624  C  CD1 . ILE E  3 19  ? 39.269  252.484 58.206 1.00 30.15 ?  18  ILE E CD1 1 
ATOM   4625  N  N   . ASN E  3 20  ? 35.366  253.872 55.714 1.00 32.02 ?  19  ASN E N   1 
ATOM   4626  C  CA  . ASN E  3 20  ? 34.477  254.316 54.650 1.00 33.15 ?  19  ASN E CA  1 
ATOM   4627  C  C   . ASN E  3 20  ? 35.194  254.320 53.304 1.00 34.91 ?  19  ASN E C   1 
ATOM   4628  O  O   . ASN E  3 20  ? 36.396  254.567 53.228 1.00 35.79 ?  19  ASN E O   1 
ATOM   4629  C  CB  . ASN E  3 20  ? 33.952  255.716 54.955 1.00 34.31 ?  19  ASN E CB  1 
ATOM   4630  C  CG  . ASN E  3 20  ? 33.294  255.793 56.303 1.00 39.96 ?  19  ASN E CG  1 
ATOM   4631  O  OD1 . ASN E  3 20  ? 33.878  256.305 57.263 1.00 43.47 ?  19  ASN E OD1 1 
ATOM   4632  N  ND2 . ASN E  3 20  ? 32.087  255.253 56.402 1.00 36.53 ?  19  ASN E ND2 1 
ATOM   4633  N  N   . PHE E  3 21  ? 34.444  254.019 52.244 1.00 31.07 ?  20  PHE E N   1 
ATOM   4634  C  CA  . PHE E  3 21  ? 34.947  254.053 50.873 1.00 32.92 ?  20  PHE E CA  1 
ATOM   4635  C  C   . PHE E  3 21  ? 33.987  254.867 50.021 1.00 30.47 ?  20  PHE E C   1 
ATOM   4636  O  O   . PHE E  3 21  ? 32.769  254.755 50.176 1.00 33.67 ?  20  PHE E O   1 
ATOM   4637  C  CB  . PHE E  3 21  ? 35.073  252.671 50.210 1.00 26.51 ?  20  PHE E CB  1 
ATOM   4638  C  CG  . PHE E  3 21  ? 35.840  251.657 51.004 1.00 29.34 ?  20  PHE E CG  1 
ATOM   4639  C  CD1 . PHE E  3 21  ? 35.313  251.113 52.167 1.00 31.36 ?  20  PHE E CD1 1 
ATOM   4640  C  CD2 . PHE E  3 21  ? 37.069  251.202 50.550 1.00 31.69 ?  20  PHE E CD2 1 
ATOM   4641  C  CE1 . PHE E  3 21  ? 36.014  250.144 52.886 1.00 31.10 ?  20  PHE E CE1 1 
ATOM   4642  C  CE2 . PHE E  3 21  ? 37.776  250.236 51.263 1.00 34.58 ?  20  PHE E CE2 1 
ATOM   4643  C  CZ  . PHE E  3 21  ? 37.243  249.704 52.431 1.00 29.83 ?  20  PHE E CZ  1 
ATOM   4644  N  N   . GLU E  3 22  ? 34.533  255.656 49.096 1.00 32.74 ?  21  GLU E N   1 
ATOM   4645  C  CA  . GLU E  3 22  ? 33.716  256.420 48.167 1.00 33.88 ?  21  GLU E CA  1 
ATOM   4646  C  C   . GLU E  3 22  ? 34.400  256.485 46.814 1.00 35.01 ?  21  GLU E C   1 
ATOM   4647  O  O   . GLU E  3 22  ? 35.604  256.729 46.719 1.00 34.61 ?  21  GLU E O   1 
ATOM   4648  C  CB  . GLU E  3 22  ? 33.447  257.835 48.672 1.00 34.96 ?  21  GLU E CB  1 
ATOM   4649  C  CG  . GLU E  3 22  ? 32.318  258.530 47.944 1.00 44.19 ?  21  GLU E CG  1 
ATOM   4650  C  CD  . GLU E  3 22  ? 32.077  259.937 48.470 1.00 66.92 ?  21  GLU E CD  1 
ATOM   4651  O  OE1 . GLU E  3 22  ? 33.064  260.627 48.837 1.00 63.55 ?  21  GLU E OE1 1 
ATOM   4652  O  OE2 . GLU E  3 22  ? 30.895  260.344 48.528 1.00 69.74 ?  21  GLU E OE2 1 
ATOM   4653  N  N   . GLN E  3 23  ? 33.615  256.279 45.770 1.00 29.70 ?  22  GLN E N   1 
ATOM   4654  C  CA  . GLN E  3 23  ? 34.123  256.274 44.403 1.00 34.64 ?  22  GLN E CA  1 
ATOM   4655  C  C   . GLN E  3 23  ? 33.077  256.995 43.569 1.00 33.82 ?  22  GLN E C   1 
ATOM   4656  O  O   . GLN E  3 23  ? 32.102  256.386 43.125 1.00 34.16 ?  22  GLN E O   1 
ATOM   4657  C  CB  . GLN E  3 23  ? 34.364  254.858 43.900 1.00 31.90 ?  22  GLN E CB  1 
ATOM   4658  C  CG  . GLN E  3 23  ? 35.109  254.835 42.579 1.00 30.85 ?  22  GLN E CG  1 
ATOM   4659  C  CD  . GLN E  3 23  ? 35.295  253.428 42.074 1.00 33.02 ?  22  GLN E CD  1 
ATOM   4660  O  OE1 . GLN E  3 23  ? 34.650  252.499 42.568 1.00 31.10 ?  22  GLN E OE1 1 
ATOM   4661  N  NE2 . GLN E  3 23  ? 36.184  253.252 41.097 1.00 31.07 ?  22  GLN E NE2 1 
ATOM   4662  N  N   . LYS E  3 24  ? 33.283  258.291 43.365 1.00 34.04 ?  23  LYS E N   1 
ATOM   4663  C  CA  . LYS E  3 24  ? 32.260  259.082 42.703 1.00 40.37 ?  23  LYS E CA  1 
ATOM   4664  C  C   . LYS E  3 24  ? 32.158  258.736 41.224 1.00 37.01 ?  23  LYS E C   1 
ATOM   4665  O  O   . LYS E  3 24  ? 31.064  258.785 40.659 1.00 41.85 ?  23  LYS E O   1 
ATOM   4666  C  CB  . LYS E  3 24  ? 32.532  260.574 42.923 1.00 45.03 ?  23  LYS E CB  1 
ATOM   4667  C  CG  . LYS E  3 24  ? 33.709  261.153 42.141 1.00 49.27 ?  23  LYS E CG  1 
ATOM   4668  C  CD  . LYS E  3 24  ? 33.781  262.692 42.295 1.00 59.15 ?  23  LYS E CD  1 
ATOM   4669  C  CE  . LYS E  3 24  ? 33.319  263.413 41.013 1.00 60.66 ?  23  LYS E CE  1 
ATOM   4670  N  NZ  . LYS E  3 24  ? 33.823  264.826 40.912 1.00 62.04 ?  23  LYS E NZ  1 
ATOM   4671  N  N   . GLU E  3 25  ? 33.253  258.331 40.596 1.00 35.16 ?  24  GLU E N   1 
ATOM   4672  C  CA  . GLU E  3 25  ? 33.225  257.896 39.206 1.00 40.65 ?  24  GLU E CA  1 
ATOM   4673  C  C   . GLU E  3 25  ? 33.779  256.485 39.101 1.00 37.98 ?  24  GLU E C   1 
ATOM   4674  O  O   . GLU E  3 25  ? 34.812  256.167 39.701 1.00 31.91 ?  24  GLU E O   1 
ATOM   4675  C  CB  . GLU E  3 25  ? 34.023  258.848 38.287 1.00 38.71 ?  24  GLU E CB  1 
ATOM   4676  C  CG  . GLU E  3 25  ? 33.526  260.302 38.283 1.00 49.08 ?  24  GLU E CG  1 
ATOM   4677  C  CD  . GLU E  3 25  ? 32.201  260.490 37.518 1.00 66.75 ?  24  GLU E CD  1 
ATOM   4678  O  OE1 . GLU E  3 25  ? 31.706  261.646 37.457 1.00 69.60 ?  24  GLU E OE1 1 
ATOM   4679  O  OE2 . GLU E  3 25  ? 31.646  259.487 36.994 1.00 62.54 ?  24  GLU E OE2 1 
ATOM   4680  N  N   . SER E  3 26  ? 33.100  255.650 38.309 1.00 32.83 ?  25  SER E N   1 
ATOM   4681  C  CA  . SER E  3 26  ? 33.416  254.227 38.258 1.00 32.96 ?  25  SER E CA  1 
ATOM   4682  C  C   . SER E  3 26  ? 34.794  253.947 37.677 1.00 32.87 ?  25  SER E C   1 
ATOM   4683  O  O   . SER E  3 26  ? 35.329  252.855 37.879 1.00 34.09 ?  25  SER E O   1 
ATOM   4684  C  CB  . SER E  3 26  ? 32.354  253.490 37.445 1.00 34.36 ?  25  SER E CB  1 
ATOM   4685  O  OG  . SER E  3 26  ? 32.548  253.691 36.057 1.00 34.46 ?  25  SER E OG  1 
ATOM   4686  N  N   . ASN E  3 27  ? 35.382  254.889 36.946 1.00 34.07 ?  26  ASN E N   1 
ATOM   4687  C  CA  . ASN E  3 27  ? 36.744  254.714 36.458 1.00 35.62 ?  26  ASN E CA  1 
ATOM   4688  C  C   . ASN E  3 27  ? 37.711  255.674 37.146 1.00 38.38 ?  26  ASN E C   1 
ATOM   4689  O  O   . ASN E  3 27  ? 38.813  255.920 36.641 1.00 42.30 ?  26  ASN E O   1 
ATOM   4690  C  CB  . ASN E  3 27  ? 36.796  254.863 34.936 1.00 37.14 ?  26  ASN E CB  1 
ATOM   4691  C  CG  . ASN E  3 27  ? 36.441  256.261 34.461 1.00 36.18 ?  26  ASN E CG  1 
ATOM   4692  O  OD1 . ASN E  3 27  ? 35.732  257.008 35.140 1.00 40.07 ?  26  ASN E OD1 1 
ATOM   4693  N  ND2 . ASN E  3 27  ? 36.920  256.612 33.270 1.00 37.43 ?  26  ASN E ND2 1 
ATOM   4694  N  N   . GLY E  3 28  ? 37.310  256.218 38.291 1.00 33.37 ?  27  GLY E N   1 
ATOM   4695  C  CA  . GLY E  3 28  ? 38.147  257.089 39.076 1.00 35.77 ?  27  GLY E CA  1 
ATOM   4696  C  C   . GLY E  3 28  ? 38.635  256.401 40.336 1.00 39.53 ?  27  GLY E C   1 
ATOM   4697  O  O   . GLY E  3 28  ? 38.328  255.233 40.603 1.00 35.82 ?  27  GLY E O   1 
ATOM   4698  N  N   . PRO E  3 29  ? 39.409  257.121 41.139 1.00 37.56 ?  28  PRO E N   1 
ATOM   4699  C  CA  . PRO E  3 29  ? 39.977  256.532 42.354 1.00 37.90 ?  28  PRO E CA  1 
ATOM   4700  C  C   . PRO E  3 29  ? 38.941  256.354 43.458 1.00 33.24 ?  28  PRO E C   1 
ATOM   4701  O  O   . PRO E  3 29  ? 37.885  256.994 43.485 1.00 34.40 ?  28  PRO E O   1 
ATOM   4702  C  CB  . PRO E  3 29  ? 41.043  257.552 42.770 1.00 39.24 ?  28  PRO E CB  1 
ATOM   4703  C  CG  . PRO E  3 29  ? 40.527  258.855 42.238 1.00 47.89 ?  28  PRO E CG  1 
ATOM   4704  C  CD  . PRO E  3 29  ? 39.817  258.522 40.939 1.00 36.97 ?  28  PRO E CD  1 
ATOM   4705  N  N   . VAL E  3 30  ? 39.275  255.461 44.388 1.00 34.97 ?  29  VAL E N   1 
ATOM   4706  C  CA  . VAL E  3 30  ? 38.470  255.210 45.585 1.00 34.31 ?  29  VAL E CA  1 
ATOM   4707  C  C   . VAL E  3 30  ? 39.072  255.985 46.749 1.00 29.69 ?  29  VAL E C   1 
ATOM   4708  O  O   . VAL E  3 30  ? 40.264  255.841 47.043 1.00 35.63 ?  29  VAL E O   1 
ATOM   4709  C  CB  . VAL E  3 30  ? 38.411  253.708 45.912 1.00 31.58 ?  29  VAL E CB  1 
ATOM   4710  C  CG1 . VAL E  3 30  ? 37.549  253.452 47.159 1.00 29.57 ?  29  VAL E CG1 1 
ATOM   4711  C  CG2 . VAL E  3 30  ? 37.896  252.936 44.731 1.00 31.78 ?  29  VAL E CG2 1 
ATOM   4712  N  N   . LYS E  3 31  ? 38.255  256.793 47.422 1.00 29.70 ?  30  LYS E N   1 
ATOM   4713  C  CA  . LYS E  3 31  ? 38.656  257.413 48.678 1.00 33.54 ?  30  LYS E CA  1 
ATOM   4714  C  C   . LYS E  3 31  ? 38.359  256.459 49.823 1.00 35.15 ?  30  LYS E C   1 
ATOM   4715  O  O   . LYS E  3 31  ? 37.257  255.907 49.902 1.00 34.21 ?  30  LYS E O   1 
ATOM   4716  C  CB  . LYS E  3 31  ? 37.921  258.729 48.912 1.00 33.29 ?  30  LYS E CB  1 
ATOM   4717  C  CG  . LYS E  3 31  ? 38.363  259.863 48.015 1.00 45.40 ?  30  LYS E CG  1 
ATOM   4718  C  CD  . LYS E  3 31  ? 37.775  261.196 48.502 1.00 49.07 ?  30  LYS E CD  1 
ATOM   4719  C  CE  . LYS E  3 31  ? 37.760  262.254 47.402 1.00 56.82 ?  30  LYS E CE  1 
ATOM   4720  N  NZ  . LYS E  3 31  ? 36.365  262.780 47.190 1.00 63.33 ?  30  LYS E NZ  1 
ATOM   4721  N  N   . VAL E  3 32  ? 39.337  256.282 50.708 1.00 32.06 ?  31  VAL E N   1 
ATOM   4722  C  CA  . VAL E  3 32  ? 39.253  255.376 51.850 1.00 33.28 ?  31  VAL E CA  1 
ATOM   4723  C  C   . VAL E  3 32  ? 39.611  256.173 53.100 1.00 39.74 ?  31  VAL E C   1 
ATOM   4724  O  O   . VAL E  3 32  ? 40.713  256.726 53.189 1.00 37.39 ?  31  VAL E O   1 
ATOM   4725  C  CB  . VAL E  3 32  ? 40.198  254.178 51.693 1.00 33.57 ?  31  VAL E CB  1 
ATOM   4726  C  CG1 . VAL E  3 32  ? 39.960  253.137 52.786 1.00 32.24 ?  31  VAL E CG1 1 
ATOM   4727  C  CG2 . VAL E  3 32  ? 40.039  253.560 50.339 1.00 32.73 ?  31  VAL E CG2 1 
ATOM   4728  N  N   . TRP E  3 33  ? 38.699  256.227 54.065 1.00 31.62 ?  32  TRP E N   1 
ATOM   4729  C  CA  . TRP E  3 33  ? 38.981  256.982 55.275 1.00 32.16 ?  32  TRP E CA  1 
ATOM   4730  C  C   . TRP E  3 33  ? 38.200  256.428 56.447 1.00 33.28 ?  32  TRP E C   1 
ATOM   4731  O  O   . TRP E  3 33  ? 37.122  255.856 56.285 1.00 34.76 ?  32  TRP E O   1 
ATOM   4732  C  CB  . TRP E  3 33  ? 38.644  258.464 55.116 1.00 34.56 ?  32  TRP E CB  1 
ATOM   4733  C  CG  . TRP E  3 33  ? 37.188  258.753 55.145 1.00 34.64 ?  32  TRP E CG  1 
ATOM   4734  C  CD1 . TRP E  3 33  ? 36.459  259.213 56.205 1.00 31.89 ?  32  TRP E CD1 1 
ATOM   4735  C  CD2 . TRP E  3 33  ? 36.267  258.618 54.052 1.00 35.94 ?  32  TRP E CD2 1 
ATOM   4736  N  NE1 . TRP E  3 33  ? 35.142  259.369 55.841 1.00 33.90 ?  32  TRP E NE1 1 
ATOM   4737  C  CE2 . TRP E  3 33  ? 35.002  259.018 54.521 1.00 33.94 ?  32  TRP E CE2 1 
ATOM   4738  C  CE3 . TRP E  3 33  ? 36.391  258.187 52.726 1.00 35.99 ?  32  TRP E CE3 1 
ATOM   4739  C  CZ2 . TRP E  3 33  ? 33.868  259.006 53.711 1.00 39.48 ?  32  TRP E CZ2 1 
ATOM   4740  C  CZ3 . TRP E  3 33  ? 35.262  258.177 51.919 1.00 38.32 ?  32  TRP E CZ3 1 
ATOM   4741  C  CH2 . TRP E  3 33  ? 34.018  258.581 52.416 1.00 40.11 ?  32  TRP E CH2 1 
ATOM   4742  N  N   . GLY E  3 34  ? 38.741  256.644 57.635 1.00 35.09 ?  33  GLY E N   1 
ATOM   4743  C  CA  . GLY E  3 34  ? 38.077  256.211 58.847 1.00 29.18 ?  33  GLY E CA  1 
ATOM   4744  C  C   . GLY E  3 34  ? 39.066  256.174 60.001 1.00 34.66 ?  33  GLY E C   1 
ATOM   4745  O  O   . GLY E  3 34  ? 40.116  256.810 59.960 1.00 32.95 ?  33  GLY E O   1 
ATOM   4746  N  N   . SER E  3 35  ? 38.712  255.395 61.009 1.00 33.76 ?  34  SER E N   1 
ATOM   4747  C  CA  . SER E  3 35  ? 39.480  255.357 62.238 1.00 38.43 ?  34  SER E CA  1 
ATOM   4748  C  C   . SER E  3 35  ? 39.556  253.928 62.755 1.00 38.66 ?  34  SER E C   1 
ATOM   4749  O  O   . SER E  3 35  ? 38.554  253.206 62.746 1.00 34.75 ?  34  SER E O   1 
ATOM   4750  C  CB  . SER E  3 35  ? 38.833  256.269 63.278 1.00 36.29 ?  34  SER E CB  1 
ATOM   4751  O  OG  . SER E  3 35  ? 39.761  256.558 64.300 1.00 63.46 ?  34  SER E OG  1 
ATOM   4752  N  N   . ILE E  3 36  ? 40.747  253.518 63.191 1.00 35.65 ?  35  ILE E N   1 
ATOM   4753  C  CA  . ILE E  3 36  ? 40.956  252.235 63.858 1.00 35.27 ?  35  ILE E CA  1 
ATOM   4754  C  C   . ILE E  3 36  ? 41.574  252.502 65.229 1.00 43.97 ?  35  ILE E C   1 
ATOM   4755  O  O   . ILE E  3 36  ? 42.484  253.331 65.351 1.00 39.34 ?  35  ILE E O   1 
ATOM   4756  C  CB  . ILE E  3 36  ? 41.867  251.313 63.029 1.00 33.66 ?  35  ILE E CB  1 
ATOM   4757  C  CG1 . ILE E  3 36  ? 41.381  251.251 61.581 1.00 37.03 ?  35  ILE E CG1 1 
ATOM   4758  C  CG2 . ILE E  3 36  ? 41.919  249.918 63.640 1.00 31.86 ?  35  ILE E CG2 1 
ATOM   4759  C  CD1 . ILE E  3 36  ? 42.292  250.469 60.695 1.00 31.18 ?  35  ILE E CD1 1 
ATOM   4760  N  N   . LYS E  3 37  ? 41.090  251.810 66.262 1.00 34.50 ?  36  LYS E N   1 
ATOM   4761  C  CA  . LYS E  3 37  ? 41.630  251.984 67.607 1.00 37.32 ?  36  LYS E CA  1 
ATOM   4762  C  C   . LYS E  3 37  ? 42.019  250.629 68.187 1.00 38.61 ?  36  LYS E C   1 
ATOM   4763  O  O   . LYS E  3 37  ? 41.737  249.570 67.613 1.00 32.33 ?  36  LYS E O   1 
ATOM   4764  C  CB  . LYS E  3 37  ? 40.635  252.708 68.523 1.00 38.21 ?  36  LYS E CB  1 
ATOM   4765  C  CG  . LYS E  3 37  ? 39.326  251.984 68.706 1.00 39.72 ?  36  LYS E CG  1 
ATOM   4766  C  CD  . LYS E  3 37  ? 38.345  252.852 69.465 1.00 43.23 ?  36  LYS E CD  1 
ATOM   4767  C  CE  . LYS E  3 37  ? 37.176  252.031 69.974 1.00 48.60 ?  36  LYS E CE  1 
ATOM   4768  N  NZ  . LYS E  3 37  ? 35.918  252.805 70.095 1.00 52.56 ?  36  LYS E NZ  1 
ATOM   4769  N  N   . GLY E  3 38  ? 42.713  250.664 69.323 1.00 34.00 ?  37  GLY E N   1 
ATOM   4770  C  CA  . GLY E  3 38  ? 43.172  249.430 69.949 1.00 32.95 ?  37  GLY E CA  1 
ATOM   4771  C  C   . GLY E  3 38  ? 44.440  248.858 69.360 1.00 33.90 ?  37  GLY E C   1 
ATOM   4772  O  O   . GLY E  3 38  ? 44.823  247.734 69.708 1.00 31.98 ?  37  GLY E O   1 
ATOM   4773  N  N   . LEU E  3 39  ? 45.109  249.598 68.485 1.00 32.93 ?  38  LEU E N   1 
ATOM   4774  C  CA  . LEU E  3 39  ? 46.356  249.165 67.882 1.00 33.48 ?  38  LEU E CA  1 
ATOM   4775  C  C   . LEU E  3 39  ? 47.546  249.544 68.762 1.00 39.07 ?  38  LEU E C   1 
ATOM   4776  O  O   . LEU E  3 39  ? 47.472  250.454 69.584 1.00 38.49 ?  38  LEU E O   1 
ATOM   4777  C  CB  . LEU E  3 39  ? 46.525  249.795 66.500 1.00 34.49 ?  38  LEU E CB  1 
ATOM   4778  C  CG  . LEU E  3 39  ? 45.508  249.385 65.439 1.00 39.05 ?  38  LEU E CG  1 
ATOM   4779  C  CD1 . LEU E  3 39  ? 45.447  250.420 64.314 1.00 38.69 ?  38  LEU E CD1 1 
ATOM   4780  C  CD2 . LEU E  3 39  ? 45.921  248.038 64.899 1.00 33.36 ?  38  LEU E CD2 1 
ATOM   4781  N  N   . THR E  3 40  ? 48.652  248.822 68.586 1.00 38.13 ?  39  THR E N   1 
ATOM   4782  C  CA  . THR E  3 40  ? 49.908  249.284 69.159 1.00 40.34 ?  39  THR E CA  1 
ATOM   4783  C  C   . THR E  3 40  ? 50.437  250.421 68.306 1.00 46.60 ?  39  THR E C   1 
ATOM   4784  O  O   . THR E  3 40  ? 50.301  250.399 67.077 1.00 38.84 ?  39  THR E O   1 
ATOM   4785  C  CB  . THR E  3 40  ? 50.941  248.163 69.216 1.00 41.02 ?  39  THR E CB  1 
ATOM   4786  O  OG1 . THR E  3 40  ? 51.129  247.619 67.905 1.00 41.25 ?  39  THR E OG1 1 
ATOM   4787  C  CG2 . THR E  3 40  ? 50.487  247.064 70.171 1.00 35.68 ?  39  THR E CG2 1 
ATOM   4788  N  N   . GLU E  3 41  ? 51.032  251.422 68.955 1.00 38.17 ?  40  GLU E N   1 
ATOM   4789  C  CA  . GLU E  3 41  ? 51.575  252.555 68.207 1.00 42.66 ?  40  GLU E CA  1 
ATOM   4790  C  C   . GLU E  3 41  ? 52.591  252.063 67.181 1.00 37.96 ?  40  GLU E C   1 
ATOM   4791  O  O   . GLU E  3 41  ? 53.422  251.197 67.476 1.00 44.32 ?  40  GLU E O   1 
ATOM   4792  C  CB  . GLU E  3 41  ? 52.198  253.564 69.174 1.00 44.26 ?  40  GLU E CB  1 
ATOM   4793  C  CG  . GLU E  3 41  ? 53.399  254.337 68.665 1.00 45.51 ?  40  GLU E CG  1 
ATOM   4794  C  CD  . GLU E  3 41  ? 53.948  255.283 69.743 1.00 55.52 ?  40  GLU E CD  1 
ATOM   4795  O  OE1 . GLU E  3 41  ? 54.105  254.842 70.915 1.00 47.62 ?  40  GLU E OE1 1 
ATOM   4796  O  OE2 . GLU E  3 41  ? 54.217  256.460 69.419 1.00 59.76 ?  40  GLU E OE2 1 
ATOM   4797  N  N   . GLY E  3 42  ? 52.475  252.560 65.950 1.00 42.66 ?  41  GLY E N   1 
ATOM   4798  C  CA  . GLY E  3 42  ? 53.352  252.151 64.879 1.00 40.72 ?  41  GLY E CA  1 
ATOM   4799  C  C   . GLY E  3 42  ? 52.584  251.819 63.605 1.00 40.57 ?  41  GLY E C   1 
ATOM   4800  O  O   . GLY E  3 42  ? 51.387  252.095 63.474 1.00 38.09 ?  41  GLY E O   1 
ATOM   4801  N  N   . LEU E  3 43  ? 53.287  251.219 62.650 1.00 41.15 ?  42  LEU E N   1 
ATOM   4802  C  CA  . LEU E  3 43  ? 52.719  250.904 61.350 1.00 40.88 ?  42  LEU E CA  1 
ATOM   4803  C  C   . LEU E  3 43  ? 52.017  249.546 61.373 1.00 40.17 ?  42  LEU E C   1 
ATOM   4804  O  O   . LEU E  3 43  ? 52.440  248.613 62.059 1.00 46.00 ?  42  LEU E O   1 
ATOM   4805  C  CB  . LEU E  3 43  ? 53.806  250.905 60.269 1.00 45.26 ?  42  LEU E CB  1 
ATOM   4806  C  CG  . LEU E  3 43  ? 54.526  252.210 59.898 1.00 39.87 ?  42  LEU E CG  1 
ATOM   4807  C  CD1 . LEU E  3 43  ? 55.565  251.913 58.838 1.00 46.18 ?  42  LEU E CD1 1 
ATOM   4808  C  CD2 . LEU E  3 43  ? 53.576  253.293 59.406 1.00 40.85 ?  42  LEU E CD2 1 
ATOM   4809  N  N   . HIS E  3 44  ? 50.933  249.446 60.603 1.00 41.42 ?  43  HIS E N   1 
ATOM   4810  C  CA  . HIS E  3 44  ? 50.159  248.215 60.509 1.00 40.80 ?  43  HIS E CA  1 
ATOM   4811  C  C   . HIS E  3 44  ? 49.742  247.987 59.065 1.00 39.60 ?  43  HIS E C   1 
ATOM   4812  O  O   . HIS E  3 44  ? 49.091  248.843 58.460 1.00 36.67 ?  43  HIS E O   1 
ATOM   4813  C  CB  . HIS E  3 44  ? 48.936  248.277 61.421 1.00 33.29 ?  43  HIS E CB  1 
ATOM   4814  C  CG  . HIS E  3 44  ? 49.281  248.310 62.876 1.00 36.81 ?  43  HIS E CG  1 
ATOM   4815  N  ND1 . HIS E  3 44  ? 49.646  247.181 63.577 1.00 42.99 ?  43  HIS E ND1 1 
ATOM   4816  C  CD2 . HIS E  3 44  ? 49.322  249.336 63.762 1.00 34.51 ?  43  HIS E CD2 1 
ATOM   4817  C  CE1 . HIS E  3 44  ? 49.892  247.508 64.836 1.00 42.59 ?  43  HIS E CE1 1 
ATOM   4818  N  NE2 . HIS E  3 44  ? 49.700  248.811 64.974 1.00 38.82 ?  43  HIS E NE2 1 
ATOM   4819  N  N   . GLY E  3 45  ? 50.125  246.836 58.522 1.00 37.47 ?  44  GLY E N   1 
ATOM   4820  C  CA  . GLY E  3 45  ? 49.638  246.405 57.227 1.00 40.94 ?  44  GLY E CA  1 
ATOM   4821  C  C   . GLY E  3 45  ? 48.130  246.516 57.116 1.00 42.13 ?  44  GLY E C   1 
ATOM   4822  O  O   . GLY E  3 45  ? 47.397  246.222 58.069 1.00 36.29 ?  44  GLY E O   1 
ATOM   4823  N  N   . PHE E  3 46  ? 47.663  246.931 55.941 1.00 38.32 ?  45  PHE E N   1 
ATOM   4824  C  CA  . PHE E  3 46  ? 46.260  247.270 55.698 1.00 36.89 ?  45  PHE E CA  1 
ATOM   4825  C  C   . PHE E  3 46  ? 45.931  246.718 54.316 1.00 40.84 ?  45  PHE E C   1 
ATOM   4826  O  O   . PHE E  3 46  ? 46.323  247.316 53.309 1.00 38.42 ?  45  PHE E O   1 
ATOM   4827  C  CB  . PHE E  3 46  ? 46.089  248.777 55.756 1.00 35.52 ?  45  PHE E CB  1 
ATOM   4828  C  CG  . PHE E  3 46  ? 44.671  249.260 55.853 1.00 37.84 ?  45  PHE E CG  1 
ATOM   4829  C  CD1 . PHE E  3 46  ? 43.840  248.862 56.883 1.00 37.98 ?  45  PHE E CD1 1 
ATOM   4830  C  CD2 . PHE E  3 46  ? 44.202  250.201 54.954 1.00 35.70 ?  45  PHE E CD2 1 
ATOM   4831  C  CE1 . PHE E  3 46  ? 42.541  249.376 56.990 1.00 31.40 ?  45  PHE E CE1 1 
ATOM   4832  C  CE2 . PHE E  3 46  ? 42.918  250.707 55.059 1.00 36.84 ?  45  PHE E CE2 1 
ATOM   4833  C  CZ  . PHE E  3 46  ? 42.093  250.293 56.082 1.00 30.71 ?  45  PHE E CZ  1 
ATOM   4834  N  N   . HIS E  3 47  ? 45.231  245.580 54.258 1.00 34.74 ?  46  HIS E N   1 
ATOM   4835  C  CA  . HIS E  3 47  ? 45.029  244.914 52.976 1.00 35.28 ?  46  HIS E CA  1 
ATOM   4836  C  C   . HIS E  3 47  ? 43.599  244.429 52.807 1.00 35.77 ?  46  HIS E C   1 
ATOM   4837  O  O   . HIS E  3 47  ? 42.926  244.062 53.775 1.00 32.65 ?  46  HIS E O   1 
ATOM   4838  C  CB  . HIS E  3 47  ? 45.946  243.710 52.802 1.00 38.22 ?  46  HIS E CB  1 
ATOM   4839  C  CG  . HIS E  3 47  ? 47.365  243.982 53.160 1.00 41.64 ?  46  HIS E CG  1 
ATOM   4840  N  ND1 . HIS E  3 47  ? 47.991  243.371 54.221 1.00 44.87 ?  46  HIS E ND1 1 
ATOM   4841  C  CD2 . HIS E  3 47  ? 48.282  244.805 52.601 1.00 46.10 ?  46  HIS E CD2 1 
ATOM   4842  C  CE1 . HIS E  3 47  ? 49.239  243.801 54.298 1.00 42.06 ?  46  HIS E CE1 1 
ATOM   4843  N  NE2 . HIS E  3 47  ? 49.438  244.677 53.332 1.00 47.37 ?  46  HIS E NE2 1 
ATOM   4844  N  N   . VAL E  3 48  ? 43.158  244.416 51.556 1.00 31.03 ?  47  VAL E N   1 
ATOM   4845  C  CA  . VAL E  3 48  ? 41.949  243.700 51.177 1.00 33.03 ?  47  VAL E CA  1 
ATOM   4846  C  C   . VAL E  3 48  ? 42.341  242.270 50.872 1.00 31.72 ?  47  VAL E C   1 
ATOM   4847  O  O   . VAL E  3 48  ? 43.223  242.025 50.041 1.00 32.76 ?  47  VAL E O   1 
ATOM   4848  C  CB  . VAL E  3 48  ? 41.269  244.342 49.960 1.00 34.64 ?  47  VAL E CB  1 
ATOM   4849  C  CG1 . VAL E  3 48  ? 40.081  243.491 49.532 1.00 30.85 ?  47  VAL E CG1 1 
ATOM   4850  C  CG2 . VAL E  3 48  ? 40.810  245.735 50.286 1.00 32.20 ?  47  VAL E CG2 1 
ATOM   4851  N  N   . HIS E  3 49  ? 41.695  241.325 51.540 1.00 30.66 ?  48  HIS E N   1 
ATOM   4852  C  CA  . HIS E  3 49  ? 41.892  239.911 51.271 1.00 32.97 ?  48  HIS E CA  1 
ATOM   4853  C  C   . HIS E  3 49  ? 40.764  239.369 50.400 1.00 29.06 ?  48  HIS E C   1 
ATOM   4854  O  O   . HIS E  3 49  ? 39.704  239.984 50.257 1.00 33.56 ?  48  HIS E O   1 
ATOM   4855  C  CB  . HIS E  3 49  ? 42.004  239.130 52.577 1.00 32.58 ?  48  HIS E CB  1 
ATOM   4856  C  CG  . HIS E  3 49  ? 43.245  239.454 53.356 1.00 34.07 ?  48  HIS E CG  1 
ATOM   4857  N  ND1 . HIS E  3 49  ? 44.200  238.510 53.663 1.00 33.36 ?  48  HIS E ND1 1 
ATOM   4858  C  CD2 . HIS E  3 49  ? 43.699  240.629 53.861 1.00 34.36 ?  48  HIS E CD2 1 
ATOM   4859  C  CE1 . HIS E  3 49  ? 45.180  239.085 54.340 1.00 36.26 ?  48  HIS E CE1 1 
ATOM   4860  N  NE2 . HIS E  3 49  ? 44.904  240.371 54.469 1.00 34.76 ?  48  HIS E NE2 1 
ATOM   4861  N  N   . GLU E  3 50  ? 41.013  238.203 49.810 1.00 30.60 ?  49  GLU E N   1 
ATOM   4862  C  CA  . GLU E  3 50  ? 40.209  237.761 48.675 1.00 31.87 ?  49  GLU E CA  1 
ATOM   4863  C  C   . GLU E  3 50  ? 38.764  237.447 49.065 1.00 30.93 ?  49  GLU E C   1 
ATOM   4864  O  O   . GLU E  3 50  ? 37.832  237.817 48.349 1.00 33.97 ?  49  GLU E O   1 
ATOM   4865  C  CB  . GLU E  3 50  ? 40.843  236.542 48.011 1.00 33.62 ?  49  GLU E CB  1 
ATOM   4866  C  CG  . GLU E  3 50  ? 40.053  236.159 46.768 1.00 37.30 ?  49  GLU E CG  1 
ATOM   4867  C  CD  . GLU E  3 50  ? 40.703  235.074 45.939 1.00 42.31 ?  49  GLU E CD  1 
ATOM   4868  O  OE1 . GLU E  3 50  ? 41.817  234.629 46.287 1.00 44.57 ?  49  GLU E OE1 1 
ATOM   4869  O  OE2 . GLU E  3 50  ? 40.082  234.666 44.937 1.00 43.72 ?  49  GLU E OE2 1 
ATOM   4870  N  N   . PHE E  3 51  ? 38.544  236.745 50.167 1.00 31.62 ?  50  PHE E N   1 
ATOM   4871  C  CA  . PHE E  3 51  ? 37.211  236.243 50.469 1.00 29.16 ?  50  PHE E CA  1 
ATOM   4872  C  C   . PHE E  3 51  ? 36.546  237.042 51.575 1.00 30.76 ?  50  PHE E C   1 
ATOM   4873  O  O   . PHE E  3 51  ? 37.160  237.342 52.602 1.00 32.28 ?  50  PHE E O   1 
ATOM   4874  C  CB  . PHE E  3 51  ? 37.278  234.760 50.829 1.00 30.15 ?  50  PHE E CB  1 
ATOM   4875  C  CG  . PHE E  3 51  ? 37.968  233.942 49.780 1.00 33.28 ?  50  PHE E CG  1 
ATOM   4876  C  CD1 . PHE E  3 51  ? 37.413  233.819 48.512 1.00 35.76 ?  50  PHE E CD1 1 
ATOM   4877  C  CD2 . PHE E  3 51  ? 39.192  233.349 50.032 1.00 38.99 ?  50  PHE E CD2 1 
ATOM   4878  C  CE1 . PHE E  3 51  ? 38.060  233.088 47.523 1.00 38.34 ?  50  PHE E CE1 1 
ATOM   4879  C  CE2 . PHE E  3 51  ? 39.843  232.610 49.046 1.00 38.12 ?  50  PHE E CE2 1 
ATOM   4880  C  CZ  . PHE E  3 51  ? 39.276  232.487 47.794 1.00 38.01 ?  50  PHE E CZ  1 
ATOM   4881  N  N   . GLY E  3 52  ? 35.277  237.369 51.365 1.00 31.30 ?  51  GLY E N   1 
ATOM   4882  C  CA  . GLY E  3 52  ? 34.495  237.952 52.434 1.00 29.76 ?  51  GLY E CA  1 
ATOM   4883  C  C   . GLY E  3 52  ? 33.951  236.889 53.373 1.00 30.38 ?  51  GLY E C   1 
ATOM   4884  O  O   . GLY E  3 52  ? 32.763  236.882 53.708 1.00 29.52 ?  51  GLY E O   1 
ATOM   4885  N  N   . ASP E  3 53  ? 34.814  235.992 53.815 1.00 30.20 ?  52  ASP E N   1 
ATOM   4886  C  CA  . ASP E  3 53  ? 34.426  234.828 54.611 1.00 27.58 ?  52  ASP E CA  1 
ATOM   4887  C  C   . ASP E  3 53  ? 34.905  235.034 56.041 1.00 30.82 ?  52  ASP E C   1 
ATOM   4888  O  O   . ASP E  3 53  ? 36.100  234.911 56.325 1.00 30.94 ?  52  ASP E O   1 
ATOM   4889  C  CB  . ASP E  3 53  ? 35.019  233.554 54.016 1.00 30.64 ?  52  ASP E CB  1 
ATOM   4890  C  CG  . ASP E  3 53  ? 34.532  232.290 54.728 1.00 32.74 ?  52  ASP E CG  1 
ATOM   4891  O  OD1 . ASP E  3 53  ? 34.204  232.370 55.931 1.00 31.96 ?  52  ASP E OD1 1 
ATOM   4892  O  OD2 . ASP E  3 53  ? 34.489  231.218 54.080 1.00 35.46 ?  52  ASP E OD2 1 
ATOM   4893  N  N   . ASN E  3 54  ? 33.977  235.339 56.937 1.00 28.83 ?  53  ASN E N   1 
ATOM   4894  C  CA  . ASN E  3 54  ? 34.305  235.561 58.336 1.00 34.02 ?  53  ASN E CA  1 
ATOM   4895  C  C   . ASN E  3 54  ? 34.008  234.349 59.224 1.00 31.53 ?  53  ASN E C   1 
ATOM   4896  O  O   . ASN E  3 54  ? 34.007  234.481 60.453 1.00 31.26 ?  53  ASN E O   1 
ATOM   4897  C  CB  . ASN E  3 54  ? 33.542  236.793 58.839 1.00 32.26 ?  53  ASN E CB  1 
ATOM   4898  C  CG  . ASN E  3 54  ? 34.229  237.467 59.995 1.00 48.71 ?  53  ASN E CG  1 
ATOM   4899  O  OD1 . ASN E  3 54  ? 33.765  237.395 61.144 1.00 49.21 ?  53  ASN E OD1 1 
ATOM   4900  N  ND2 . ASN E  3 54  ? 35.353  238.119 59.711 1.00 51.93 ?  53  ASN E ND2 1 
ATOM   4901  N  N   . THR E  3 55  ? 33.747  233.174 58.635 1.00 28.35 ?  54  THR E N   1 
ATOM   4902  C  CA  . THR E  3 55  ? 33.314  232.031 59.445 1.00 32.11 ?  54  THR E CA  1 
ATOM   4903  C  C   . THR E  3 55  ? 34.382  231.586 60.431 1.00 31.57 ?  54  THR E C   1 
ATOM   4904  O  O   . THR E  3 55  ? 34.055  231.017 61.478 1.00 34.79 ?  54  THR E O   1 
ATOM   4905  C  CB  . THR E  3 55  ? 32.926  230.848 58.555 1.00 30.59 ?  54  THR E CB  1 
ATOM   4906  O  OG1 . THR E  3 55  ? 34.053  230.446 57.769 1.00 30.42 ?  54  THR E OG1 1 
ATOM   4907  C  CG2 . THR E  3 55  ? 31.771  231.221 57.630 1.00 26.26 ?  54  THR E CG2 1 
ATOM   4908  N  N   . ALA E  3 56  ? 35.653  231.803 60.110 1.00 32.42 ?  55  ALA E N   1 
ATOM   4909  C  CA  . ALA E  3 56  ? 36.757  231.563 61.033 1.00 37.49 ?  55  ALA E CA  1 
ATOM   4910  C  C   . ALA E  3 56  ? 37.423  232.880 61.428 1.00 37.92 ?  55  ALA E C   1 
ATOM   4911  O  O   . ALA E  3 56  ? 38.646  232.972 61.550 1.00 37.83 ?  55  ALA E O   1 
ATOM   4912  C  CB  . ALA E  3 56  ? 37.773  230.599 60.427 1.00 32.85 ?  55  ALA E CB  1 
ATOM   4913  N  N   . GLY E  3 57  ? 36.617  233.918 61.630 1.00 37.99 ?  56  GLY E N   1 
ATOM   4914  C  CA  . GLY E  3 57  ? 37.177  235.240 61.841 1.00 35.70 ?  56  GLY E CA  1 
ATOM   4915  C  C   . GLY E  3 57  ? 37.948  235.714 60.626 1.00 39.05 ?  56  GLY E C   1 
ATOM   4916  O  O   . GLY E  3 57  ? 37.566  235.469 59.471 1.00 35.75 ?  56  GLY E O   1 
ATOM   4917  N  N   . CYS E  3 58  ? 39.069  236.392 60.883 1.00 37.04 ?  57  CYS E N   1 
ATOM   4918  C  CA  . CYS E  3 58  ? 39.905  236.894 59.798 1.00 34.32 ?  57  CYS E CA  1 
ATOM   4919  C  C   . CYS E  3 58  ? 40.640  235.782 59.070 1.00 35.89 ?  57  CYS E C   1 
ATOM   4920  O  O   . CYS E  3 58  ? 41.043  235.969 57.918 1.00 32.04 ?  57  CYS E O   1 
ATOM   4921  C  CB  . CYS E  3 58  ? 40.891  237.916 60.364 1.00 39.94 ?  57  CYS E CB  1 
ATOM   4922  S  SG  . CYS E  3 58  ? 40.014  239.240 61.221 1.00 46.15 ?  57  CYS E SG  1 
ATOM   4923  N  N   . THR E  3 59  ? 40.783  234.615 59.706 1.00 35.66 ?  58  THR E N   1 
ATOM   4924  C  CA  . THR E  3 59  ? 41.572  233.531 59.134 1.00 33.90 ?  58  THR E CA  1 
ATOM   4925  C  C   . THR E  3 59  ? 40.988  233.041 57.812 1.00 37.15 ?  58  THR E C   1 
ATOM   4926  O  O   . THR E  3 59  ? 41.730  232.672 56.899 1.00 44.92 ?  58  THR E O   1 
ATOM   4927  C  CB  . THR E  3 59  ? 41.652  232.382 60.135 1.00 40.03 ?  58  THR E CB  1 
ATOM   4928  O  OG1 . THR E  3 59  ? 42.181  232.875 61.371 1.00 47.96 ?  58  THR E OG1 1 
ATOM   4929  C  CG2 . THR E  3 59  ? 42.561  231.302 59.623 1.00 42.64 ?  58  THR E CG2 1 
ATOM   4930  N  N   . SER E  3 60  ? 39.664  233.040 57.684 1.00 34.87 ?  59  SER E N   1 
ATOM   4931  C  CA  . SER E  3 60  ? 39.017  232.486 56.501 1.00 34.83 ?  59  SER E CA  1 
ATOM   4932  C  C   . SER E  3 60  ? 38.998  233.447 55.315 1.00 32.89 ?  59  SER E C   1 
ATOM   4933  O  O   . SER E  3 60  ? 38.535  233.059 54.234 1.00 32.10 ?  59  SER E O   1 
ATOM   4934  C  CB  . SER E  3 60  ? 37.589  232.058 56.853 1.00 29.30 ?  59  SER E CB  1 
ATOM   4935  O  OG  . SER E  3 60  ? 37.021  232.954 57.799 1.00 31.15 ?  59  SER E OG  1 
ATOM   4936  N  N   . ALA E  3 61  ? 39.500  234.674 55.468 1.00 34.27 ?  60  ALA E N   1 
ATOM   4937  C  CA  . ALA E  3 61  ? 39.499  235.627 54.362 1.00 31.83 ?  60  ALA E CA  1 
ATOM   4938  C  C   . ALA E  3 61  ? 40.497  235.278 53.261 1.00 33.48 ?  60  ALA E C   1 
ATOM   4939  O  O   . ALA E  3 61  ? 40.465  235.914 52.199 1.00 34.20 ?  60  ALA E O   1 
ATOM   4940  C  CB  . ALA E  3 61  ? 39.797  237.035 54.875 1.00 30.85 ?  60  ALA E CB  1 
ATOM   4941  N  N   . GLY E  3 62  ? 41.380  234.309 53.477 1.00 33.19 ?  61  GLY E N   1 
ATOM   4942  C  CA  . GLY E  3 62  ? 42.325  233.908 52.459 1.00 33.84 ?  61  GLY E CA  1 
ATOM   4943  C  C   . GLY E  3 62  ? 43.438  234.919 52.256 1.00 33.53 ?  61  GLY E C   1 
ATOM   4944  O  O   . GLY E  3 62  ? 43.690  235.781 53.104 1.00 35.04 ?  61  GLY E O   1 
ATOM   4945  N  N   . PRO E  3 63  ? 44.118  234.836 51.122 1.00 35.29 ?  62  PRO E N   1 
ATOM   4946  C  CA  . PRO E  3 63  ? 45.281  235.692 50.868 1.00 35.98 ?  62  PRO E CA  1 
ATOM   4947  C  C   . PRO E  3 63  ? 44.842  237.068 50.390 1.00 37.83 ?  62  PRO E C   1 
ATOM   4948  O  O   . PRO E  3 63  ? 43.656  237.382 50.314 1.00 35.57 ?  62  PRO E O   1 
ATOM   4949  C  CB  . PRO E  3 63  ? 46.027  234.938 49.767 1.00 34.53 ?  62  PRO E CB  1 
ATOM   4950  C  CG  . PRO E  3 63  ? 44.920  234.291 48.989 1.00 40.24 ?  62  PRO E CG  1 
ATOM   4951  C  CD  . PRO E  3 63  ? 43.865  233.907 50.005 1.00 34.26 ?  62  PRO E CD  1 
ATOM   4952  N  N   . HIS E  3 64  ? 45.830  237.897 50.068 1.00 36.72 ?  63  HIS E N   1 
ATOM   4953  C  CA  . HIS E  3 64  ? 45.532  239.226 49.564 1.00 37.59 ?  63  HIS E CA  1 
ATOM   4954  C  C   . HIS E  3 64  ? 44.770  239.105 48.258 1.00 33.08 ?  63  HIS E C   1 
ATOM   4955  O  O   . HIS E  3 64  ? 45.022  238.198 47.460 1.00 31.68 ?  63  HIS E O   1 
ATOM   4956  C  CB  . HIS E  3 64  ? 46.820  240.034 49.370 1.00 36.67 ?  63  HIS E CB  1 
ATOM   4957  C  CG  . HIS E  3 64  ? 47.539  240.320 50.647 1.00 39.72 ?  63  HIS E CG  1 
ATOM   4958  N  ND1 . HIS E  3 64  ? 48.763  240.946 50.694 1.00 46.42 ?  63  HIS E ND1 1 
ATOM   4959  C  CD2 . HIS E  3 64  ? 47.212  240.040 51.930 1.00 43.72 ?  63  HIS E CD2 1 
ATOM   4960  C  CE1 . HIS E  3 64  ? 49.151  241.062 51.952 1.00 46.48 ?  63  HIS E CE1 1 
ATOM   4961  N  NE2 . HIS E  3 64  ? 48.228  240.519 52.722 1.00 48.35 ?  63  HIS E NE2 1 
ATOM   4962  N  N   . PHE E  3 65  ? 43.800  239.990 48.073 1.00 32.08 ?  64  PHE E N   1 
ATOM   4963  C  CA  . PHE E  3 65  ? 43.046  240.030 46.829 1.00 36.05 ?  64  PHE E CA  1 
ATOM   4964  C  C   . PHE E  3 65  ? 43.995  240.282 45.660 1.00 35.41 ?  64  PHE E C   1 
ATOM   4965  O  O   . PHE E  3 65  ? 44.697  241.299 45.629 1.00 36.47 ?  64  PHE E O   1 
ATOM   4966  C  CB  . PHE E  3 65  ? 41.987  241.120 46.912 1.00 31.54 ?  64  PHE E CB  1 
ATOM   4967  C  CG  . PHE E  3 65  ? 41.124  241.219 45.691 1.00 31.63 ?  64  PHE E CG  1 
ATOM   4968  C  CD1 . PHE E  3 65  ? 40.725  240.078 45.014 1.00 31.71 ?  64  PHE E CD1 1 
ATOM   4969  C  CD2 . PHE E  3 65  ? 40.708  242.455 45.224 1.00 30.64 ?  64  PHE E CD2 1 
ATOM   4970  C  CE1 . PHE E  3 65  ? 39.922  240.178 43.874 1.00 36.35 ?  64  PHE E CE1 1 
ATOM   4971  C  CE2 . PHE E  3 65  ? 39.902  242.560 44.083 1.00 32.31 ?  64  PHE E CE2 1 
ATOM   4972  C  CZ  . PHE E  3 65  ? 39.513  241.413 43.416 1.00 33.82 ?  64  PHE E CZ  1 
ATOM   4973  N  N   . ASN E  3 66  ? 44.026  239.355 44.697 1.00 35.50 ?  65  ASN E N   1 
ATOM   4974  C  CA  . ASN E  3 66  ? 45.072  239.339 43.669 1.00 42.51 ?  65  ASN E CA  1 
ATOM   4975  C  C   . ASN E  3 66  ? 44.515  238.763 42.371 1.00 41.95 ?  65  ASN E C   1 
ATOM   4976  O  O   . ASN E  3 66  ? 44.924  237.689 41.917 1.00 43.14 ?  65  ASN E O   1 
ATOM   4977  C  CB  . ASN E  3 66  ? 46.277  238.534 44.160 1.00 42.82 ?  65  ASN E CB  1 
ATOM   4978  C  CG  . ASN E  3 66  ? 47.474  238.646 43.241 1.00 51.02 ?  65  ASN E CG  1 
ATOM   4979  O  OD1 . ASN E  3 66  ? 47.606  239.615 42.495 1.00 46.62 ?  65  ASN E OD1 1 
ATOM   4980  N  ND2 . ASN E  3 66  ? 48.364  237.657 43.302 1.00 48.10 ?  65  ASN E ND2 1 
ATOM   4981  N  N   . PRO E  3 67  ? 43.585  239.476 41.727 1.00 45.14 ?  66  PRO E N   1 
ATOM   4982  C  CA  . PRO E  3 67  ? 42.944  238.925 40.523 1.00 43.30 ?  66  PRO E CA  1 
ATOM   4983  C  C   . PRO E  3 67  ? 43.861  238.832 39.312 1.00 48.34 ?  66  PRO E C   1 
ATOM   4984  O  O   . PRO E  3 67  ? 43.497  238.152 38.347 1.00 55.27 ?  66  PRO E O   1 
ATOM   4985  C  CB  . PRO E  3 67  ? 41.795  239.909 40.268 1.00 37.46 ?  66  PRO E CB  1 
ATOM   4986  C  CG  . PRO E  3 67  ? 42.298  241.185 40.801 1.00 40.73 ?  66  PRO E CG  1 
ATOM   4987  C  CD  . PRO E  3 67  ? 43.085  240.826 42.033 1.00 35.96 ?  66  PRO E CD  1 
ATOM   4988  N  N   . LEU E  3 68  ? 45.022  239.489 39.327 1.00 51.07 ?  67  LEU E N   1 
ATOM   4989  C  CA  . LEU E  3 68  ? 45.932  239.520 38.186 1.00 51.31 ?  67  LEU E CA  1 
ATOM   4990  C  C   . LEU E  3 68  ? 47.222  238.740 38.425 1.00 58.73 ?  67  LEU E C   1 
ATOM   4991  O  O   . LEU E  3 68  ? 48.131  238.809 37.592 1.00 59.72 ?  67  LEU E O   1 
ATOM   4992  C  CB  . LEU E  3 68  ? 46.271  240.965 37.824 1.00 53.00 ?  67  LEU E CB  1 
ATOM   4993  C  CG  . LEU E  3 68  ? 45.091  241.873 37.495 1.00 53.07 ?  67  LEU E CG  1 
ATOM   4994  C  CD1 . LEU E  3 68  ? 45.543  243.323 37.501 1.00 51.62 ?  67  LEU E CD1 1 
ATOM   4995  C  CD2 . LEU E  3 68  ? 44.504  241.481 36.154 1.00 52.24 ?  67  LEU E CD2 1 
ATOM   4996  N  N   . SER E  3 69  ? 47.333  238.033 39.552 1.00 57.86 ?  68  SER E N   1 
ATOM   4997  C  CA  . SER E  3 69  ? 48.458  237.140 39.861 1.00 59.37 ?  68  SER E CA  1 
ATOM   4998  C  C   . SER E  3 69  ? 49.810  237.851 39.744 1.00 62.64 ?  68  SER E C   1 
ATOM   4999  O  O   . SER E  3 69  ? 50.681  237.480 38.953 1.00 71.79 ?  68  SER E O   1 
ATOM   5000  C  CB  . SER E  3 69  ? 48.408  235.893 38.976 1.00 57.85 ?  68  SER E CB  1 
ATOM   5001  O  OG  . SER E  3 69  ? 47.065  235.598 38.628 1.00 61.24 ?  68  SER E OG  1 
ATOM   5002  N  N   . ARG E  3 70  ? 49.973  238.886 40.565 1.00 58.23 ?  69  ARG E N   1 
ATOM   5003  C  CA  . ARG E  3 70  ? 51.225  239.612 40.718 1.00 57.91 ?  69  ARG E CA  1 
ATOM   5004  C  C   . ARG E  3 70  ? 51.800  239.361 42.108 1.00 54.92 ?  69  ARG E C   1 
ATOM   5005  O  O   . ARG E  3 70  ? 51.184  238.710 42.956 1.00 59.28 ?  69  ARG E O   1 
ATOM   5006  C  CB  . ARG E  3 70  ? 51.011  241.113 40.483 1.00 57.17 ?  69  ARG E CB  1 
ATOM   5007  C  CG  . ARG E  3 70  ? 50.121  241.413 39.286 1.00 58.77 ?  69  ARG E CG  1 
ATOM   5008  C  CD  . ARG E  3 70  ? 50.741  242.466 38.372 1.00 60.03 ?  69  ARG E CD  1 
ATOM   5009  N  NE  . ARG E  3 70  ? 50.180  242.426 37.025 1.00 69.46 ?  69  ARG E NE  1 
ATOM   5010  C  CZ  . ARG E  3 70  ? 49.653  243.470 36.397 1.00 65.79 ?  69  ARG E CZ  1 
ATOM   5011  N  NH1 . ARG E  3 70  ? 49.610  244.668 36.963 1.00 63.85 ?  69  ARG E NH1 1 
ATOM   5012  N  NH2 . ARG E  3 70  ? 49.156  243.308 35.172 1.00 66.08 ?  69  ARG E NH2 1 
ATOM   5013  N  N   . LYS E  3 71  ? 52.999  239.880 42.339 1.00 59.14 ?  70  LYS E N   1 
ATOM   5014  C  CA  . LYS E  3 71  ? 53.604  239.790 43.656 1.00 55.39 ?  70  LYS E CA  1 
ATOM   5015  C  C   . LYS E  3 71  ? 53.171  240.971 44.526 1.00 59.75 ?  70  LYS E C   1 
ATOM   5016  O  O   . LYS E  3 71  ? 52.624  241.971 44.045 1.00 54.46 ?  70  LYS E O   1 
ATOM   5017  C  CB  . LYS E  3 71  ? 55.128  239.713 43.543 1.00 57.43 ?  70  LYS E CB  1 
ATOM   5018  C  CG  . LYS E  3 71  ? 55.645  238.379 43.004 1.00 55.89 ?  70  LYS E CG  1 
ATOM   5019  C  CD  . LYS E  3 71  ? 57.076  238.486 42.486 1.00 57.81 ?  70  LYS E CD  1 
ATOM   5020  C  CE  . LYS E  3 71  ? 57.946  237.343 43.020 1.00 69.22 ?  70  LYS E CE  1 
ATOM   5021  N  NZ  . LYS E  3 71  ? 59.351  237.384 42.490 1.00 69.70 ?  70  LYS E NZ  1 
ATOM   5022  N  N   . HIS E  3 72  ? 53.415  240.836 45.832 1.00 55.13 ?  71  HIS E N   1 
ATOM   5023  C  CA  . HIS E  3 72  ? 53.022  241.862 46.789 1.00 57.21 ?  71  HIS E CA  1 
ATOM   5024  C  C   . HIS E  3 72  ? 53.920  243.085 46.675 1.00 57.64 ?  71  HIS E C   1 
ATOM   5025  O  O   . HIS E  3 72  ? 55.132  242.973 46.480 1.00 64.34 ?  71  HIS E O   1 
ATOM   5026  C  CB  . HIS E  3 72  ? 53.073  241.309 48.222 1.00 53.57 ?  71  HIS E CB  1 
ATOM   5027  C  CG  . HIS E  3 72  ? 52.889  242.356 49.278 1.00 57.42 ?  71  HIS E CG  1 
ATOM   5028  N  ND1 . HIS E  3 72  ? 51.655  242.882 49.598 1.00 56.50 ?  71  HIS E ND1 1 
ATOM   5029  C  CD2 . HIS E  3 72  ? 53.780  242.975 50.088 1.00 55.95 ?  71  HIS E CD2 1 
ATOM   5030  C  CE1 . HIS E  3 72  ? 51.793  243.779 50.559 1.00 56.12 ?  71  HIS E CE1 1 
ATOM   5031  N  NE2 . HIS E  3 72  ? 53.073  243.851 50.878 1.00 58.17 ?  71  HIS E NE2 1 
ATOM   5032  N  N   . GLY E  3 73  ? 53.315  244.263 46.811 1.00 58.49 ?  72  GLY E N   1 
ATOM   5033  C  CA  . GLY E  3 73  ? 54.053  245.503 46.795 1.00 58.37 ?  72  GLY E CA  1 
ATOM   5034  C  C   . GLY E  3 73  ? 53.322  246.570 47.581 1.00 57.88 ?  72  GLY E C   1 
ATOM   5035  O  O   . GLY E  3 73  ? 52.261  246.334 48.160 1.00 58.61 ?  72  GLY E O   1 
ATOM   5036  N  N   . GLY E  3 74  ? 53.914  247.754 47.615 1.00 54.30 ?  73  GLY E N   1 
ATOM   5037  C  CA  . GLY E  3 74  ? 53.230  248.929 48.131 1.00 51.54 ?  73  GLY E CA  1 
ATOM   5038  C  C   . GLY E  3 74  ? 52.222  249.448 47.140 1.00 55.38 ?  73  GLY E C   1 
ATOM   5039  O  O   . GLY E  3 74  ? 52.188  249.061 45.977 1.00 53.76 ?  73  GLY E O   1 
ATOM   5040  N  N   . PRO E  3 75  ? 51.377  250.356 47.604 1.00 54.46 ?  74  PRO E N   1 
ATOM   5041  C  CA  . PRO E  3 75  ? 50.301  250.878 46.755 1.00 52.10 ?  74  PRO E CA  1 
ATOM   5042  C  C   . PRO E  3 75  ? 50.781  251.583 45.492 1.00 57.87 ?  74  PRO E C   1 
ATOM   5043  O  O   . PRO E  3 75  ? 50.078  251.551 44.464 1.00 56.70 ?  74  PRO E O   1 
ATOM   5044  C  CB  . PRO E  3 75  ? 49.533  251.872 47.653 1.00 52.32 ?  74  PRO E CB  1 
ATOM   5045  C  CG  . PRO E  3 75  ? 50.101  251.698 49.043 1.00 52.41 ?  74  PRO E CG  1 
ATOM   5046  C  CD  . PRO E  3 75  ? 51.157  250.633 49.040 1.00 52.31 ?  74  PRO E CD  1 
ATOM   5047  N  N   . LYS E  3 76  ? 51.960  252.212 45.519 1.00 56.65 ?  75  LYS E N   1 
ATOM   5048  C  CA  . LYS E  3 76  ? 52.459  252.913 44.335 1.00 57.59 ?  75  LYS E CA  1 
ATOM   5049  C  C   . LYS E  3 76  ? 53.303  252.025 43.426 1.00 54.50 ?  75  LYS E C   1 
ATOM   5050  O  O   . LYS E  3 76  ? 53.995  252.540 42.542 1.00 61.74 ?  75  LYS E O   1 
ATOM   5051  C  CB  . LYS E  3 76  ? 53.267  254.142 44.761 1.00 56.96 ?  75  LYS E CB  1 
ATOM   5052  C  CG  . LYS E  3 76  ? 52.392  255.314 45.171 1.00 56.09 ?  75  LYS E CG  1 
ATOM   5053  C  CD  . LYS E  3 76  ? 53.149  256.287 46.057 1.00 46.62 ?  75  LYS E CD  1 
ATOM   5054  C  CE  . LYS E  3 76  ? 52.690  257.716 45.794 1.00 59.29 ?  75  LYS E CE  1 
ATOM   5055  N  NZ  . LYS E  3 76  ? 53.816  258.680 45.969 1.00 66.31 ?  75  LYS E NZ  1 
ATOM   5056  N  N   . ASP E  3 77  ? 53.259  250.709 43.621 1.00 55.04 ?  76  ASP E N   1 
ATOM   5057  C  CA  . ASP E  3 77  ? 53.991  249.767 42.784 1.00 59.23 ?  76  ASP E CA  1 
ATOM   5058  C  C   . ASP E  3 77  ? 53.101  249.304 41.639 1.00 63.31 ?  76  ASP E C   1 
ATOM   5059  O  O   . ASP E  3 77  ? 51.941  248.935 41.857 1.00 63.02 ?  76  ASP E O   1 
ATOM   5060  C  CB  . ASP E  3 77  ? 54.431  248.547 43.597 1.00 59.47 ?  76  ASP E CB  1 
ATOM   5061  C  CG  . ASP E  3 77  ? 55.676  248.803 44.421 1.00 70.69 ?  76  ASP E CG  1 
ATOM   5062  O  OD1 . ASP E  3 77  ? 55.790  249.919 44.983 1.00 72.23 ?  76  ASP E OD1 1 
ATOM   5063  O  OD2 . ASP E  3 77  ? 56.508  247.869 44.545 1.00 72.21 ?  76  ASP E OD2 1 
ATOM   5064  N  N   . ALA E  3 78  ? 53.648  249.304 40.422 1.00 62.40 ?  77  ALA E N   1 
ATOM   5065  C  CA  . ALA E  3 78  ? 52.952  248.633 39.331 1.00 62.94 ?  77  ALA E CA  1 
ATOM   5066  C  C   . ALA E  3 78  ? 52.774  247.152 39.638 1.00 60.94 ?  77  ALA E C   1 
ATOM   5067  O  O   . ALA E  3 78  ? 51.762  246.550 39.258 1.00 62.06 ?  77  ALA E O   1 
ATOM   5068  C  CB  . ALA E  3 78  ? 53.709  248.825 38.013 1.00 58.93 ?  77  ALA E CB  1 
ATOM   5069  N  N   . GLU E  3 79  ? 53.734  246.556 40.345 1.00 59.39 ?  78  GLU E N   1 
ATOM   5070  C  CA  . GLU E  3 79  ? 53.658  245.156 40.760 1.00 61.86 ?  78  GLU E CA  1 
ATOM   5071  C  C   . GLU E  3 79  ? 53.137  245.095 42.191 1.00 62.79 ?  78  GLU E C   1 
ATOM   5072  O  O   . GLU E  3 79  ? 53.897  245.022 43.161 1.00 64.30 ?  78  GLU E O   1 
ATOM   5073  C  CB  . GLU E  3 79  ? 55.019  244.477 40.641 1.00 58.91 ?  78  GLU E CB  1 
ATOM   5074  C  CG  . GLU E  3 79  ? 54.960  242.970 40.781 1.00 54.95 ?  78  GLU E CG  1 
ATOM   5075  C  CD  . GLU E  3 79  ? 54.270  242.285 39.607 1.00 68.13 ?  78  GLU E CD  1 
ATOM   5076  O  OE1 . GLU E  3 79  ? 54.205  241.028 39.612 1.00 69.56 ?  78  GLU E OE1 1 
ATOM   5077  O  OE2 . GLU E  3 79  ? 53.822  242.999 38.672 1.00 73.02 ?  78  GLU E OE2 1 
ATOM   5078  N  N   . ARG E  3 80  ? 51.813  245.123 42.314 1.00 57.61 ?  79  ARG E N   1 
ATOM   5079  C  CA  . ARG E  3 80  ? 51.159  244.941 43.599 1.00 53.21 ?  79  ARG E CA  1 
ATOM   5080  C  C   . ARG E  3 80  ? 49.929  244.070 43.404 1.00 54.72 ?  79  ARG E C   1 
ATOM   5081  O  O   . ARG E  3 80  ? 49.385  243.961 42.298 1.00 49.84 ?  79  ARG E O   1 
ATOM   5082  C  CB  . ARG E  3 80  ? 50.753  246.274 44.221 1.00 49.54 ?  79  ARG E CB  1 
ATOM   5083  C  CG  . ARG E  3 80  ? 49.784  247.054 43.344 1.00 48.07 ?  79  ARG E CG  1 
ATOM   5084  C  CD  . ARG E  3 80  ? 49.273  248.299 44.042 1.00 50.29 ?  79  ARG E CD  1 
ATOM   5085  N  NE  . ARG E  3 80  ? 47.972  248.094 44.677 1.00 48.80 ?  79  ARG E NE  1 
ATOM   5086  C  CZ  . ARG E  3 80  ? 47.135  249.076 44.991 1.00 45.02 ?  79  ARG E CZ  1 
ATOM   5087  N  NH1 . ARG E  3 80  ? 47.450  250.347 44.782 1.00 49.46 ?  79  ARG E NH1 1 
ATOM   5088  N  NH2 . ARG E  3 80  ? 45.954  248.778 45.525 1.00 41.31 ?  79  ARG E NH2 1 
ATOM   5089  N  N   . HIS E  3 81  ? 49.510  243.434 44.492 1.00 46.64 ?  80  HIS E N   1 
ATOM   5090  C  CA  . HIS E  3 81  ? 48.163  242.899 44.559 1.00 48.62 ?  80  HIS E CA  1 
ATOM   5091  C  C   . HIS E  3 81  ? 47.166  244.054 44.560 1.00 42.52 ?  80  HIS E C   1 
ATOM   5092  O  O   . HIS E  3 81  ? 47.439  245.136 45.088 1.00 43.71 ?  80  HIS E O   1 
ATOM   5093  C  CB  . HIS E  3 81  ? 47.983  242.039 45.820 1.00 46.76 ?  80  HIS E CB  1 
ATOM   5094  C  CG  . HIS E  3 81  ? 48.990  240.933 45.961 1.00 51.83 ?  80  HIS E CG  1 
ATOM   5095  N  ND1 . HIS E  3 81  ? 49.548  240.577 47.172 1.00 50.66 ?  80  HIS E ND1 1 
ATOM   5096  C  CD2 . HIS E  3 81  ? 49.524  240.091 45.044 1.00 54.02 ?  80  HIS E CD2 1 
ATOM   5097  C  CE1 . HIS E  3 81  ? 50.378  239.565 46.996 1.00 48.80 ?  80  HIS E CE1 1 
ATOM   5098  N  NE2 . HIS E  3 81  ? 50.381  239.250 45.714 1.00 52.00 ?  80  HIS E NE2 1 
ATOM   5099  N  N   . VAL E  3 82  ? 45.997  243.821 43.960 1.00 38.92 ?  81  VAL E N   1 
ATOM   5100  C  CA  . VAL E  3 82  ? 44.942  244.830 44.028 1.00 37.70 ?  81  VAL E CA  1 
ATOM   5101  C  C   . VAL E  3 82  ? 44.640  245.194 45.483 1.00 34.72 ?  81  VAL E C   1 
ATOM   5102  O  O   . VAL E  3 82  ? 44.474  246.372 45.824 1.00 36.43 ?  81  VAL E O   1 
ATOM   5103  C  CB  . VAL E  3 82  ? 43.686  244.345 43.283 1.00 39.16 ?  81  VAL E CB  1 
ATOM   5104  C  CG1 . VAL E  3 82  ? 42.524  245.274 43.557 1.00 33.08 ?  81  VAL E CG1 1 
ATOM   5105  C  CG2 . VAL E  3 82  ? 43.960  244.275 41.778 1.00 36.25 ?  81  VAL E CG2 1 
ATOM   5106  N  N   . GLY E  3 83  ? 44.616  244.205 46.372 1.00 36.71 ?  82  GLY E N   1 
ATOM   5107  C  CA  . GLY E  3 83  ? 44.280  244.501 47.760 1.00 43.19 ?  82  GLY E CA  1 
ATOM   5108  C  C   . GLY E  3 83  ? 45.340  245.240 48.572 1.00 42.55 ?  82  GLY E C   1 
ATOM   5109  O  O   . GLY E  3 83  ? 45.114  245.474 49.764 1.00 36.47 ?  82  GLY E O   1 
ATOM   5110  N  N   . ASP E  3 84  ? 46.466  245.631 47.971 1.00 40.29 ?  83  ASP E N   1 
ATOM   5111  C  CA  . ASP E  3 84  ? 47.622  246.136 48.722 1.00 41.76 ?  83  ASP E CA  1 
ATOM   5112  C  C   . ASP E  3 84  ? 47.443  247.619 49.015 1.00 43.07 ?  83  ASP E C   1 
ATOM   5113  O  O   . ASP E  3 84  ? 47.791  248.467 48.193 1.00 44.04 ?  83  ASP E O   1 
ATOM   5114  C  CB  . ASP E  3 84  ? 48.912  245.901 47.936 1.00 46.47 ?  83  ASP E CB  1 
ATOM   5115  C  CG  . ASP E  3 84  ? 49.368  244.450 47.972 1.00 50.09 ?  83  ASP E CG  1 
ATOM   5116  O  OD1 . ASP E  3 84  ? 48.767  243.658 48.730 1.00 46.14 ?  83  ASP E OD1 1 
ATOM   5117  O  OD2 . ASP E  3 84  ? 50.315  244.094 47.232 1.00 50.25 ?  83  ASP E OD2 1 
ATOM   5118  N  N   . LEU E  3 85  ? 46.922  247.954 50.197 1.00 33.09 ?  84  LEU E N   1 
ATOM   5119  C  CA  . LEU E  3 85  ? 46.751  249.350 50.579 1.00 38.02 ?  84  LEU E CA  1 
ATOM   5120  C  C   . LEU E  3 85  ? 47.786  249.821 51.595 1.00 40.42 ?  84  LEU E C   1 
ATOM   5121  O  O   . LEU E  3 85  ? 47.529  250.779 52.331 1.00 44.65 ?  84  LEU E O   1 
ATOM   5122  C  CB  . LEU E  3 85  ? 45.338  249.592 51.117 1.00 34.32 ?  84  LEU E CB  1 
ATOM   5123  C  CG  . LEU E  3 85  ? 44.184  249.272 50.162 1.00 37.58 ?  84  LEU E CG  1 
ATOM   5124  C  CD1 . LEU E  3 85  ? 42.847  249.418 50.875 1.00 35.68 ?  84  LEU E CD1 1 
ATOM   5125  C  CD2 . LEU E  3 85  ? 44.236  250.174 48.937 1.00 38.04 ?  84  LEU E CD2 1 
ATOM   5126  N  N   . GLY E  3 86  ? 48.947  249.177 51.651 1.00 44.55 ?  85  GLY E N   1 
ATOM   5127  C  CA  . GLY E  3 86  ? 50.070  249.768 52.366 1.00 40.67 ?  85  GLY E CA  1 
ATOM   5128  C  C   . GLY E  3 86  ? 49.928  249.639 53.868 1.00 41.99 ?  85  GLY E C   1 
ATOM   5129  O  O   . GLY E  3 86  ? 49.511  248.598 54.399 1.00 43.81 ?  85  GLY E O   1 
ATOM   5130  N  N   . ASN E  3 87  ? 50.274  250.708 54.570 1.00 37.73 ?  86  ASN E N   1 
ATOM   5131  C  CA  . ASN E  3 87  ? 50.298  250.741 56.026 1.00 37.79 ?  86  ASN E CA  1 
ATOM   5132  C  C   . ASN E  3 87  ? 49.415  251.865 56.535 1.00 40.86 ?  86  ASN E C   1 
ATOM   5133  O  O   . ASN E  3 87  ? 49.297  252.919 55.905 1.00 43.21 ?  86  ASN E O   1 
ATOM   5134  C  CB  . ASN E  3 87  ? 51.718  250.970 56.567 1.00 43.61 ?  86  ASN E CB  1 
ATOM   5135  C  CG  . ASN E  3 87  ? 52.622  249.773 56.381 1.00 45.22 ?  86  ASN E CG  1 
ATOM   5136  O  OD1 . ASN E  3 87  ? 52.340  248.684 56.890 1.00 45.46 ?  86  ASN E OD1 1 
ATOM   5137  N  ND2 . ASN E  3 87  ? 53.715  249.962 55.652 1.00 43.00 ?  86  ASN E ND2 1 
ATOM   5138  N  N   . VAL E  3 88  ? 48.803  251.639 57.688 1.00 43.18 ?  87  VAL E N   1 
ATOM   5139  C  CA  . VAL E  3 88  ? 48.212  252.723 58.452 1.00 42.00 ?  87  VAL E CA  1 
ATOM   5140  C  C   . VAL E  3 88  ? 49.096  252.948 59.674 1.00 40.89 ?  87  VAL E C   1 
ATOM   5141  O  O   . VAL E  3 88  ? 49.889  252.084 60.066 1.00 41.32 ?  87  VAL E O   1 
ATOM   5142  C  CB  . VAL E  3 88  ? 46.746  252.438 58.852 1.00 41.95 ?  87  VAL E CB  1 
ATOM   5143  C  CG1 . VAL E  3 88  ? 45.902  252.199 57.610 1.00 37.17 ?  87  VAL E CG1 1 
ATOM   5144  C  CG2 . VAL E  3 88  ? 46.664  251.245 59.790 1.00 36.92 ?  87  VAL E CG2 1 
ATOM   5145  N  N   . THR E  3 89  ? 48.971  254.132 60.270 1.00 36.35 ?  88  THR E N   1 
ATOM   5146  C  CA  . THR E  3 89  ? 49.821  254.543 61.389 1.00 42.93 ?  88  THR E CA  1 
ATOM   5147  C  C   . THR E  3 89  ? 48.971  254.756 62.632 1.00 36.34 ?  88  THR E C   1 
ATOM   5148  O  O   . THR E  3 89  ? 48.075  255.607 62.640 1.00 41.73 ?  88  THR E O   1 
ATOM   5149  C  CB  . THR E  3 89  ? 50.599  255.828 61.061 1.00 42.91 ?  88  THR E CB  1 
ATOM   5150  O  OG1 . THR E  3 89  ? 51.324  255.654 59.840 1.00 45.24 ?  88  THR E OG1 1 
ATOM   5151  C  CG2 . THR E  3 89  ? 51.584  256.157 62.181 1.00 46.31 ?  88  THR E CG2 1 
ATOM   5152  N  N   . ALA E  3 90  ? 49.266  254.008 63.687 1.00 36.26 ?  89  ALA E N   1 
ATOM   5153  C  CA  . ALA E  3 90  ? 48.616  254.218 64.970 1.00 38.59 ?  89  ALA E CA  1 
ATOM   5154  C  C   . ALA E  3 90  ? 49.440  255.181 65.821 1.00 37.77 ?  89  ALA E C   1 
ATOM   5155  O  O   . ALA E  3 90  ? 50.659  255.034 65.934 1.00 39.31 ?  89  ALA E O   1 
ATOM   5156  C  CB  . ALA E  3 90  ? 48.441  252.882 65.702 1.00 35.55 ?  89  ALA E CB  1 
ATOM   5157  N  N   . ASP E  3 91  ? 48.766  256.150 66.438 1.00 36.31 ?  90  ASP E N   1 
ATOM   5158  C  CA  . ASP E  3 91  ? 49.443  257.109 67.292 1.00 38.45 ?  90  ASP E CA  1 
ATOM   5159  C  C   . ASP E  3 91  ? 49.724  256.495 68.666 1.00 45.76 ?  90  ASP E C   1 
ATOM   5160  O  O   . ASP E  3 91  ? 49.503  255.301 68.911 1.00 42.93 ?  90  ASP E O   1 
ATOM   5161  C  CB  . ASP E  3 91  ? 48.625  258.403 67.360 1.00 35.24 ?  90  ASP E CB  1 
ATOM   5162  C  CG  . ASP E  3 91  ? 47.330  258.278 68.161 1.00 45.09 ?  90  ASP E CG  1 
ATOM   5163  O  OD1 . ASP E  3 91  ? 46.557  259.260 68.148 1.00 45.54 ?  90  ASP E OD1 1 
ATOM   5164  O  OD2 . ASP E  3 91  ? 47.077  257.250 68.832 1.00 47.00 ?  90  ASP E OD2 1 
ATOM   5165  N  N   . LYS E  3 92  ? 50.233  257.323 69.581 1.00 39.14 ?  91  LYS E N   1 
ATOM   5166  C  CA  . LYS E  3 92  ? 50.618  256.818 70.894 1.00 45.91 ?  91  LYS E CA  1 
ATOM   5167  C  C   . LYS E  3 92  ? 49.412  256.328 71.689 1.00 42.13 ?  91  LYS E C   1 
ATOM   5168  O  O   . LYS E  3 92  ? 49.576  255.536 72.621 1.00 48.16 ?  91  LYS E O   1 
ATOM   5169  C  CB  . LYS E  3 92  ? 51.367  257.909 71.675 1.00 46.37 ?  91  LYS E CB  1 
ATOM   5170  C  CG  . LYS E  3 92  ? 50.479  259.092 72.045 1.00 47.85 ?  91  LYS E CG  1 
ATOM   5171  C  CD  . LYS E  3 92  ? 51.257  260.278 72.600 1.00 61.83 ?  91  LYS E CD  1 
ATOM   5172  C  CE  . LYS E  3 92  ? 50.701  260.714 73.956 1.00 61.06 ?  91  LYS E CE  1 
ATOM   5173  N  NZ  . LYS E  3 92  ? 51.083  259.758 75.042 1.00 67.16 ?  91  LYS E NZ  1 
ATOM   5174  N  N   . ASP E  3 93  ? 48.208  256.776 71.338 1.00 38.62 ?  92  ASP E N   1 
ATOM   5175  C  CA  . ASP E  3 93  ? 46.983  256.324 71.977 1.00 45.53 ?  92  ASP E CA  1 
ATOM   5176  C  C   . ASP E  3 93  ? 46.379  255.095 71.300 1.00 40.43 ?  92  ASP E C   1 
ATOM   5177  O  O   . ASP E  3 93  ? 45.292  254.652 71.689 1.00 40.12 ?  92  ASP E O   1 
ATOM   5178  C  CB  . ASP E  3 93  ? 45.970  257.461 72.003 1.00 42.28 ?  92  ASP E CB  1 
ATOM   5179  C  CG  . ASP E  3 93  ? 46.511  258.694 72.704 1.00 54.37 ?  92  ASP E CG  1 
ATOM   5180  O  OD1 . ASP E  3 93  ? 46.613  259.759 72.053 1.00 57.52 ?  92  ASP E OD1 1 
ATOM   5181  O  OD2 . ASP E  3 93  ? 46.849  258.588 73.906 1.00 52.60 ?  92  ASP E OD2 1 
ATOM   5182  N  N   . GLY E  3 94  ? 47.062  254.530 70.315 1.00 32.40 ?  93  GLY E N   1 
ATOM   5183  C  CA  . GLY E  3 94  ? 46.547  253.355 69.652 1.00 36.82 ?  93  GLY E CA  1 
ATOM   5184  C  C   . GLY E  3 94  ? 45.507  253.625 68.591 1.00 38.17 ?  93  GLY E C   1 
ATOM   5185  O  O   . GLY E  3 94  ? 44.806  252.696 68.183 1.00 37.42 ?  93  GLY E O   1 
ATOM   5186  N  N   . VAL E  3 95  ? 45.397  254.863 68.114 1.00 33.61 ?  94  VAL E N   1 
ATOM   5187  C  CA  . VAL E  3 95  ? 44.377  255.258 67.148 1.00 34.48 ?  94  VAL E CA  1 
ATOM   5188  C  C   . VAL E  3 95  ? 45.047  255.546 65.815 1.00 38.94 ?  94  VAL E C   1 
ATOM   5189  O  O   . VAL E  3 95  ? 45.979  256.357 65.745 1.00 41.09 ?  94  VAL E O   1 
ATOM   5190  C  CB  . VAL E  3 95  ? 43.588  256.487 67.625 1.00 35.36 ?  94  VAL E CB  1 
ATOM   5191  C  CG1 . VAL E  3 95  ? 42.490  256.797 66.640 1.00 38.12 ?  94  VAL E CG1 1 
ATOM   5192  C  CG2 . VAL E  3 95  ? 43.015  256.242 68.990 1.00 38.66 ?  94  VAL E CG2 1 
ATOM   5193  N  N   . ALA E  3 96  ? 44.569  254.889 64.760 1.00 38.36 ?  95  ALA E N   1 
ATOM   5194  C  CA  . ALA E  3 96  ? 45.036  255.119 63.400 1.00 36.18 ?  95  ALA E CA  1 
ATOM   5195  C  C   . ALA E  3 96  ? 43.950  255.871 62.645 1.00 40.62 ?  95  ALA E C   1 
ATOM   5196  O  O   . ALA E  3 96  ? 42.813  255.396 62.549 1.00 41.52 ?  95  ALA E O   1 
ATOM   5197  C  CB  . ALA E  3 96  ? 45.377  253.803 62.704 1.00 38.04 ?  95  ALA E CB  1 
ATOM   5198  N  N   . ASP E  3 97  ? 44.283  257.051 62.138 1.00 39.53 ?  96  ASP E N   1 
ATOM   5199  C  CA  . ASP E  3 97  ? 43.348  257.855 61.363 1.00 41.45 ?  96  ASP E CA  1 
ATOM   5200  C  C   . ASP E  3 97  ? 43.651  257.605 59.889 1.00 42.65 ?  96  ASP E C   1 
ATOM   5201  O  O   . ASP E  3 97  ? 44.684  258.050 59.378 1.00 46.27 ?  96  ASP E O   1 
ATOM   5202  C  CB  . ASP E  3 97  ? 43.454  259.332 61.730 1.00 47.83 ?  96  ASP E CB  1 
ATOM   5203  C  CG  . ASP E  3 97  ? 42.797  259.645 63.075 1.00 63.93 ?  96  ASP E CG  1 
ATOM   5204  O  OD1 . ASP E  3 97  ? 42.028  258.792 63.576 1.00 63.54 ?  96  ASP E OD1 1 
ATOM   5205  O  OD2 . ASP E  3 97  ? 43.039  260.743 63.630 1.00 83.80 ?  96  ASP E OD2 1 
ATOM   5206  N  N   . VAL E  3 98  ? 42.760  256.873 59.221 1.00 36.86 ?  97  VAL E N   1 
ATOM   5207  C  CA  . VAL E  3 98  ? 43.009  256.354 57.877 1.00 37.38 ?  97  VAL E CA  1 
ATOM   5208  C  C   . VAL E  3 98  ? 42.552  257.382 56.852 1.00 36.47 ?  97  VAL E C   1 
ATOM   5209  O  O   . VAL E  3 98  ? 41.433  257.901 56.933 1.00 36.48 ?  97  VAL E O   1 
ATOM   5210  C  CB  . VAL E  3 98  ? 42.298  255.005 57.678 1.00 35.55 ?  97  VAL E CB  1 
ATOM   5211  C  CG1 . VAL E  3 98  ? 42.517  254.470 56.275 1.00 33.00 ?  97  VAL E CG1 1 
ATOM   5212  C  CG2 . VAL E  3 98  ? 42.811  253.996 58.718 1.00 33.60 ?  97  VAL E CG2 1 
ATOM   5213  N  N   . SER E  3 99  ? 43.435  257.703 55.904 1.00 35.68 ?  98  SER E N   1 
ATOM   5214  C  CA  . SER E  3 99  ? 43.097  258.625 54.819 1.00 36.29 ?  98  SER E CA  1 
ATOM   5215  C  C   . SER E  3 99  ? 43.886  258.192 53.597 1.00 42.60 ?  98  SER E C   1 
ATOM   5216  O  O   . SER E  3 99  ? 45.109  258.351 53.537 1.00 45.71 ?  98  SER E O   1 
ATOM   5217  C  CB  . SER E  3 99  ? 43.398  260.068 55.172 1.00 38.29 ?  98  SER E CB  1 
ATOM   5218  O  OG  . SER E  3 99  ? 42.890  260.908 54.154 1.00 45.95 ?  98  SER E OG  1 
ATOM   5219  N  N   . ILE E  3 100 ? 43.177  257.646 52.625 1.00 35.77 ?  99  ILE E N   1 
ATOM   5220  C  CA  . ILE E  3 100 ? 43.774  256.865 51.559 1.00 36.86 ?  99  ILE E CA  1 
ATOM   5221  C  C   . ILE E  3 100 ? 43.039  257.214 50.276 1.00 40.92 ?  99  ILE E C   1 
ATOM   5222  O  O   . ILE E  3 100 ? 41.824  257.442 50.288 1.00 37.50 ?  99  ILE E O   1 
ATOM   5223  C  CB  . ILE E  3 100 ? 43.681  255.362 51.909 1.00 39.69 ?  99  ILE E CB  1 
ATOM   5224  C  CG1 . ILE E  3 100 ? 44.736  254.956 52.939 1.00 43.47 ?  99  ILE E CG1 1 
ATOM   5225  C  CG2 . ILE E  3 100 ? 43.707  254.480 50.696 1.00 41.61 ?  99  ILE E CG2 1 
ATOM   5226  C  CD1 . ILE E  3 100 ? 44.632  253.467 53.341 1.00 37.83 ?  99  ILE E CD1 1 
ATOM   5227  N  N   . GLU E  3 101 ? 43.776  257.322 49.177 1.00 38.94 ?  100 GLU E N   1 
ATOM   5228  C  CA  . GLU E  3 101 ? 43.157  257.439 47.869 1.00 34.25 ?  100 GLU E CA  1 
ATOM   5229  C  C   . GLU E  3 101 ? 43.863  256.469 46.946 1.00 41.91 ?  100 GLU E C   1 
ATOM   5230  O  O   . GLU E  3 101 ? 45.083  256.549 46.777 1.00 44.75 ?  100 GLU E O   1 
ATOM   5231  C  CB  . GLU E  3 101 ? 43.235  258.865 47.331 1.00 42.21 ?  100 GLU E CB  1 
ATOM   5232  C  CG  . GLU E  3 101 ? 42.340  259.064 46.126 1.00 45.65 ?  100 GLU E CG  1 
ATOM   5233  C  CD  . GLU E  3 101 ? 42.424  260.460 45.551 1.00 54.85 ?  100 GLU E CD  1 
ATOM   5234  O  OE1 . GLU E  3 101 ? 41.952  261.405 46.214 1.00 61.00 ?  100 GLU E OE1 1 
ATOM   5235  O  OE2 . GLU E  3 101 ? 42.980  260.606 44.442 1.00 60.92 ?  100 GLU E OE2 1 
ATOM   5236  N  N   . ASP E  3 102 ? 43.116  255.531 46.379 1.00 35.68 ?  101 ASP E N   1 
ATOM   5237  C  CA  . ASP E  3 102 ? 43.717  254.468 45.590 1.00 35.40 ?  101 ASP E CA  1 
ATOM   5238  C  C   . ASP E  3 102 ? 42.954  254.285 44.294 1.00 37.11 ?  101 ASP E C   1 
ATOM   5239  O  O   . ASP E  3 102 ? 41.720  254.281 44.284 1.00 38.32 ?  101 ASP E O   1 
ATOM   5240  C  CB  . ASP E  3 102 ? 43.741  253.136 46.345 1.00 35.67 ?  101 ASP E CB  1 
ATOM   5241  C  CG  . ASP E  3 102 ? 44.646  252.117 45.680 1.00 37.92 ?  101 ASP E CG  1 
ATOM   5242  O  OD1 . ASP E  3 102 ? 45.868  252.148 45.943 1.00 46.39 ?  101 ASP E OD1 1 
ATOM   5243  O  OD2 . ASP E  3 102 ? 44.145  251.295 44.880 1.00 40.70 ?  101 ASP E OD2 1 
ATOM   5244  N  N   . SER E  3 103 ? 43.692  254.112 43.203 1.00 38.54 ?  102 SER E N   1 
ATOM   5245  C  CA  . SER E  3 103 ? 43.087  254.006 41.886 1.00 39.22 ?  102 SER E CA  1 
ATOM   5246  C  C   . SER E  3 103 ? 43.236  252.612 41.302 1.00 37.31 ?  102 SER E C   1 
ATOM   5247  O  O   . SER E  3 103 ? 42.888  252.403 40.133 1.00 39.81 ?  102 SER E O   1 
ATOM   5248  C  CB  . SER E  3 103 ? 43.698  255.045 40.942 1.00 40.57 ?  102 SER E CB  1 
ATOM   5249  O  OG  . SER E  3 103 ? 45.104  255.040 41.080 1.00 47.03 ?  102 SER E OG  1 
ATOM   5250  N  N   . VAL E  3 104 ? 43.760  251.664 42.075 1.00 37.17 ?  103 VAL E N   1 
ATOM   5251  C  CA  . VAL E  3 104 ? 43.780  250.257 41.669 1.00 37.67 ?  103 VAL E CA  1 
ATOM   5252  C  C   . VAL E  3 104 ? 42.532  249.525 42.163 1.00 41.77 ?  103 VAL E C   1 
ATOM   5253  O  O   . VAL E  3 104 ? 41.867  248.820 41.394 1.00 39.13 ?  103 VAL E O   1 
ATOM   5254  C  CB  . VAL E  3 104 ? 45.076  249.575 42.174 1.00 36.82 ?  103 VAL E CB  1 
ATOM   5255  C  CG1 . VAL E  3 104 ? 45.112  248.099 41.780 1.00 32.61 ?  103 VAL E CG1 1 
ATOM   5256  C  CG2 . VAL E  3 104 ? 46.298  250.297 41.634 1.00 43.21 ?  103 VAL E CG2 1 
ATOM   5257  N  N   . ILE E  3 105 ? 42.183  249.679 43.445 1.00 36.58 ?  104 ILE E N   1 
ATOM   5258  C  CA  . ILE E  3 105 ? 40.935  249.102 43.942 1.00 36.02 ?  104 ILE E CA  1 
ATOM   5259  C  C   . ILE E  3 105 ? 39.755  249.803 43.277 1.00 36.51 ?  104 ILE E C   1 
ATOM   5260  O  O   . ILE E  3 105 ? 39.841  250.972 42.882 1.00 34.87 ?  104 ILE E O   1 
ATOM   5261  C  CB  . ILE E  3 105 ? 40.827  249.226 45.472 1.00 32.82 ?  104 ILE E CB  1 
ATOM   5262  C  CG1 . ILE E  3 105 ? 40.878  250.698 45.882 1.00 28.81 ?  104 ILE E CG1 1 
ATOM   5263  C  CG2 . ILE E  3 105 ? 41.895  248.398 46.167 1.00 32.24 ?  104 ILE E CG2 1 
ATOM   5264  C  CD1 . ILE E  3 105 ? 40.432  250.956 47.336 1.00 31.29 ?  104 ILE E CD1 1 
ATOM   5265  N  N   . SER E  3 106 ? 38.633  249.092 43.172 1.00 29.23 ?  105 SER E N   1 
ATOM   5266  C  CA  . SER E  3 106 ? 37.397  249.685 42.686 1.00 29.06 ?  105 SER E CA  1 
ATOM   5267  C  C   . SER E  3 106 ? 36.228  249.191 43.530 1.00 34.25 ?  105 SER E C   1 
ATOM   5268  O  O   . SER E  3 106 ? 36.300  248.146 44.179 1.00 33.13 ?  105 SER E O   1 
ATOM   5269  C  CB  . SER E  3 106 ? 37.152  249.353 41.211 1.00 29.67 ?  105 SER E CB  1 
ATOM   5270  O  OG  . SER E  3 106 ? 36.105  250.148 40.683 1.00 30.96 ?  105 SER E OG  1 
ATOM   5271  N  N   . LEU E  3 107 ? 35.153  249.969 43.541 1.00 32.62 ?  106 LEU E N   1 
ATOM   5272  C  CA  . LEU E  3 107 ? 33.902  249.506 44.120 1.00 30.30 ?  106 LEU E CA  1 
ATOM   5273  C  C   . LEU E  3 107 ? 32.996  248.839 43.085 1.00 30.57 ?  106 LEU E C   1 
ATOM   5274  O  O   . LEU E  3 107 ? 31.883  248.451 43.432 1.00 34.62 ?  106 LEU E O   1 
ATOM   5275  C  CB  . LEU E  3 107 ? 33.173  250.668 44.806 1.00 28.97 ?  106 LEU E CB  1 
ATOM   5276  C  CG  . LEU E  3 107 ? 33.949  251.411 45.894 1.00 29.63 ?  106 LEU E CG  1 
ATOM   5277  C  CD1 . LEU E  3 107 ? 33.063  252.417 46.614 1.00 29.50 ?  106 LEU E CD1 1 
ATOM   5278  C  CD2 . LEU E  3 107 ? 34.554  250.436 46.893 1.00 28.30 ?  106 LEU E CD2 1 
ATOM   5279  N  N   . SER E  3 108 ? 33.456  248.671 41.840 1.00 33.60 ?  107 SER E N   1 
ATOM   5280  C  CA  . SER E  3 108 ? 32.699  247.973 40.803 1.00 31.25 ?  107 SER E CA  1 
ATOM   5281  C  C   . SER E  3 108 ? 33.666  247.298 39.835 1.00 36.03 ?  107 SER E C   1 
ATOM   5282  O  O   . SER E  3 108 ? 34.875  247.548 39.856 1.00 32.52 ?  107 SER E O   1 
ATOM   5283  C  CB  . SER E  3 108 ? 31.757  248.926 40.056 1.00 38.34 ?  107 SER E CB  1 
ATOM   5284  O  OG  . SER E  3 108 ? 32.423  250.116 39.653 1.00 35.38 ?  107 SER E OG  1 
ATOM   5285  N  N   . GLY E  3 109 ? 33.117  246.410 38.991 1.00 35.75 ?  108 GLY E N   1 
ATOM   5286  C  CA  . GLY E  3 109 ? 33.918  245.714 38.000 1.00 33.89 ?  108 GLY E CA  1 
ATOM   5287  C  C   . GLY E  3 109 ? 34.750  244.595 38.605 1.00 46.55 ?  108 GLY E C   1 
ATOM   5288  O  O   . GLY E  3 109 ? 34.382  243.986 39.606 1.00 48.24 ?  108 GLY E O   1 
ATOM   5289  N  N   . ASP E  3 110 ? 35.903  244.335 37.988 1.00 48.79 ?  109 ASP E N   1 
ATOM   5290  C  CA  . ASP E  3 110 ? 36.687  243.151 38.332 1.00 50.67 ?  109 ASP E CA  1 
ATOM   5291  C  C   . ASP E  3 110 ? 37.717  243.394 39.425 1.00 46.61 ?  109 ASP E C   1 
ATOM   5292  O  O   . ASP E  3 110 ? 38.155  242.436 40.058 1.00 44.28 ?  109 ASP E O   1 
ATOM   5293  C  CB  . ASP E  3 110 ? 37.379  242.597 37.081 1.00 59.02 ?  109 ASP E CB  1 
ATOM   5294  C  CG  . ASP E  3 110 ? 36.440  241.730 36.232 1.00 73.16 ?  109 ASP E CG  1 
ATOM   5295  O  OD1 . ASP E  3 110 ? 35.195  241.891 36.350 1.00 69.85 ?  109 ASP E OD1 1 
ATOM   5296  O  OD2 . ASP E  3 110 ? 36.944  240.887 35.453 1.00 76.58 ?  109 ASP E OD2 1 
ATOM   5297  N  N   . HIS E  3 111 ? 38.131  244.641 39.649 1.00 42.99 ?  110 HIS E N   1 
ATOM   5298  C  CA  . HIS E  3 111 ? 38.869  245.001 40.849 1.00 50.89 ?  110 HIS E CA  1 
ATOM   5299  C  C   . HIS E  3 111 ? 37.936  245.352 41.999 1.00 45.22 ?  110 HIS E C   1 
ATOM   5300  O  O   . HIS E  3 111 ? 38.347  246.082 42.914 1.00 39.76 ?  110 HIS E O   1 
ATOM   5301  C  CB  . HIS E  3 111 ? 39.817  246.181 40.579 1.00 42.50 ?  110 HIS E CB  1 
ATOM   5302  C  CG  . HIS E  3 111 ? 41.020  245.819 39.768 1.00 46.28 ?  110 HIS E CG  1 
ATOM   5303  N  ND1 . HIS E  3 111 ? 42.041  246.710 39.510 1.00 49.50 ?  110 HIS E ND1 1 
ATOM   5304  C  CD2 . HIS E  3 111 ? 41.354  244.668 39.137 1.00 47.28 ?  110 HIS E CD2 1 
ATOM   5305  C  CE1 . HIS E  3 111 ? 42.959  246.116 38.766 1.00 52.94 ?  110 HIS E CE1 1 
ATOM   5306  N  NE2 . HIS E  3 111 ? 42.568  244.876 38.530 1.00 49.10 ?  110 HIS E NE2 1 
ATOM   5307  N  N   . CYS E  3 112 ? 36.684  244.893 41.942 1.00 40.19 ?  111 CYS E N   1 
ATOM   5308  C  CA  . CYS E  3 112 ? 35.708  245.286 42.946 1.00 35.24 ?  111 CYS E CA  1 
ATOM   5309  C  C   . CYS E  3 112 ? 36.039  244.599 44.260 1.00 32.41 ?  111 CYS E C   1 
ATOM   5310  O  O   . CYS E  3 112 ? 36.209  243.378 44.308 1.00 32.87 ?  111 CYS E O   1 
ATOM   5311  C  CB  . CYS E  3 112 ? 34.299  244.925 42.492 1.00 35.31 ?  111 CYS E CB  1 
ATOM   5312  S  SG  . CYS E  3 112 ? 33.004  245.310 43.683 1.00 38.26 ?  111 CYS E SG  1 
ATOM   5313  N  N   . ILE E  3 113 ? 36.160  245.395 45.317 1.00 31.15 ?  112 ILE E N   1 
ATOM   5314  C  CA  . ILE E  3 113 ? 36.460  244.881 46.639 1.00 36.90 ?  112 ILE E CA  1 
ATOM   5315  C  C   . ILE E  3 113 ? 35.216  244.726 47.496 1.00 29.77 ?  112 ILE E C   1 
ATOM   5316  O  O   . ILE E  3 113 ? 35.322  244.319 48.651 1.00 27.84 ?  112 ILE E O   1 
ATOM   5317  C  CB  . ILE E  3 113 ? 37.486  245.786 47.341 1.00 29.15 ?  112 ILE E CB  1 
ATOM   5318  C  CG1 . ILE E  3 113 ? 36.884  247.181 47.535 1.00 28.03 ?  112 ILE E CG1 1 
ATOM   5319  C  CG2 . ILE E  3 113 ? 38.785  245.802 46.527 1.00 31.05 ?  112 ILE E CG2 1 
ATOM   5320  C  CD1 . ILE E  3 113 ? 37.735  248.102 48.405 1.00 32.55 ?  112 ILE E CD1 1 
ATOM   5321  N  N   . ILE E  3 114 ? 34.040  245.057 46.972 1.00 31.13 ?  113 ILE E N   1 
ATOM   5322  C  CA  . ILE E  3 114 ? 32.820  244.884 47.739 1.00 32.23 ?  113 ILE E CA  1 
ATOM   5323  C  C   . ILE E  3 114 ? 32.591  243.399 47.953 1.00 31.47 ?  113 ILE E C   1 
ATOM   5324  O  O   . ILE E  3 114 ? 32.771  242.601 47.032 1.00 29.72 ?  113 ILE E O   1 
ATOM   5325  C  CB  . ILE E  3 114 ? 31.647  245.570 47.026 1.00 35.15 ?  113 ILE E CB  1 
ATOM   5326  C  CG1 . ILE E  3 114 ? 31.702  247.063 47.341 1.00 34.28 ?  113 ILE E CG1 1 
ATOM   5327  C  CG2 . ILE E  3 114 ? 30.317  244.973 47.455 1.00 30.11 ?  113 ILE E CG2 1 
ATOM   5328  C  CD1 . ILE E  3 114 ? 30.662  247.860 46.666 1.00 36.99 ?  113 ILE E CD1 1 
ATOM   5329  N  N   . GLY E  3 115 ? 32.280  243.012 49.191 1.00 24.32 ?  114 GLY E N   1 
ATOM   5330  C  CA  . GLY E  3 115 ? 32.093  241.610 49.505 1.00 26.26 ?  114 GLY E CA  1 
ATOM   5331  C  C   . GLY E  3 115 ? 33.371  240.853 49.765 1.00 32.07 ?  114 GLY E C   1 
ATOM   5332  O  O   . GLY E  3 115 ? 33.337  239.624 49.892 1.00 28.95 ?  114 GLY E O   1 
ATOM   5333  N  N   . ARG E  3 116 ? 34.497  241.544 49.829 1.00 32.20 ?  115 ARG E N   1 
ATOM   5334  C  CA  . ARG E  3 116 ? 35.760  240.982 50.266 1.00 30.10 ?  115 ARG E CA  1 
ATOM   5335  C  C   . ARG E  3 116 ? 36.062  241.514 51.664 1.00 30.46 ?  115 ARG E C   1 
ATOM   5336  O  O   . ARG E  3 116 ? 35.305  242.312 52.225 1.00 30.02 ?  115 ARG E O   1 
ATOM   5337  C  CB  . ARG E  3 116 ? 36.843  241.300 49.229 1.00 27.35 ?  115 ARG E CB  1 
ATOM   5338  C  CG  . ARG E  3 116 ? 36.355  240.954 47.810 1.00 32.10 ?  115 ARG E CG  1 
ATOM   5339  C  CD  . ARG E  3 116 ? 37.456  240.950 46.764 1.00 30.42 ?  115 ARG E CD  1 
ATOM   5340  N  NE  . ARG E  3 116 ? 36.932  240.649 45.437 1.00 31.96 ?  115 ARG E NE  1 
ATOM   5341  C  CZ  . ARG E  3 116 ? 36.866  239.422 44.938 1.00 33.80 ?  115 ARG E CZ  1 
ATOM   5342  N  NH1 . ARG E  3 116 ? 37.233  238.369 45.648 1.00 32.88 ?  115 ARG E NH1 1 
ATOM   5343  N  NH2 . ARG E  3 116 ? 36.420  239.245 43.699 1.00 35.45 ?  115 ARG E NH2 1 
ATOM   5344  N  N   . THR E  3 117 ? 37.161  241.051 52.250 1.00 31.42 ?  116 THR E N   1 
ATOM   5345  C  CA  . THR E  3 117 ? 37.496  241.380 53.633 1.00 30.67 ?  116 THR E CA  1 
ATOM   5346  C  C   . THR E  3 117 ? 38.654  242.369 53.680 1.00 31.23 ?  116 THR E C   1 
ATOM   5347  O  O   . THR E  3 117 ? 39.682  242.174 53.017 1.00 31.70 ?  116 THR E O   1 
ATOM   5348  C  CB  . THR E  3 117 ? 37.848  240.122 54.425 1.00 34.63 ?  116 THR E CB  1 
ATOM   5349  O  OG1 . THR E  3 117 ? 36.741  239.210 54.383 1.00 28.59 ?  116 THR E OG1 1 
ATOM   5350  C  CG2 . THR E  3 117 ? 38.133  240.472 55.884 1.00 29.99 ?  116 THR E CG2 1 
ATOM   5351  N  N   . LEU E  3 118 ? 38.464  243.441 54.433 1.00 29.88 ?  117 LEU E N   1 
ATOM   5352  C  CA  . LEU E  3 118 ? 39.536  244.369 54.765 1.00 25.72 ?  117 LEU E CA  1 
ATOM   5353  C  C   . LEU E  3 118 ? 40.158  243.919 56.078 1.00 30.73 ?  117 LEU E C   1 
ATOM   5354  O  O   . LEU E  3 118 ? 39.433  243.637 57.037 1.00 30.73 ?  117 LEU E O   1 
ATOM   5355  C  CB  . LEU E  3 118 ? 38.982  245.789 54.894 1.00 30.25 ?  117 LEU E CB  1 
ATOM   5356  C  CG  . LEU E  3 118 ? 39.951  246.881 55.335 1.00 32.27 ?  117 LEU E CG  1 
ATOM   5357  C  CD1 . LEU E  3 118 ? 40.944  247.132 54.205 1.00 29.62 ?  117 LEU E CD1 1 
ATOM   5358  C  CD2 . LEU E  3 118 ? 39.188  248.150 55.729 1.00 28.14 ?  117 LEU E CD2 1 
ATOM   5359  N  N   . VAL E  3 119 ? 41.488  243.841 56.123 1.00 32.20 ?  118 VAL E N   1 
ATOM   5360  C  CA  . VAL E  3 119 ? 42.205  243.289 57.275 1.00 33.08 ?  118 VAL E CA  1 
ATOM   5361  C  C   . VAL E  3 119 ? 43.280  244.276 57.709 1.00 35.84 ?  118 VAL E C   1 
ATOM   5362  O  O   . VAL E  3 119 ? 44.070  244.738 56.882 1.00 34.41 ?  118 VAL E O   1 
ATOM   5363  C  CB  . VAL E  3 119 ? 42.845  241.923 56.954 1.00 32.44 ?  118 VAL E CB  1 
ATOM   5364  C  CG1 . VAL E  3 119 ? 43.619  241.424 58.147 1.00 35.71 ?  118 VAL E CG1 1 
ATOM   5365  C  CG2 . VAL E  3 119 ? 41.786  240.904 56.563 1.00 30.65 ?  118 VAL E CG2 1 
ATOM   5366  N  N   . VAL E  3 120 ? 43.320  244.596 59.002 1.00 34.39 ?  119 VAL E N   1 
ATOM   5367  C  CA  . VAL E  3 120 ? 44.439  245.343 59.568 1.00 34.42 ?  119 VAL E CA  1 
ATOM   5368  C  C   . VAL E  3 120 ? 45.334  244.368 60.327 1.00 37.61 ?  119 VAL E C   1 
ATOM   5369  O  O   . VAL E  3 120 ? 44.858  243.583 61.162 1.00 40.20 ?  119 VAL E O   1 
ATOM   5370  C  CB  . VAL E  3 120 ? 43.960  246.513 60.450 1.00 33.35 ?  119 VAL E CB  1 
ATOM   5371  C  CG1 . VAL E  3 120 ? 43.122  246.038 61.662 1.00 33.04 ?  119 VAL E CG1 1 
ATOM   5372  C  CG2 . VAL E  3 120 ? 45.159  247.355 60.890 1.00 32.96 ?  119 VAL E CG2 1 
ATOM   5373  N  N   . HIS E  3 121 ? 46.626  244.391 60.008 1.00 31.81 ?  120 HIS E N   1 
ATOM   5374  C  CA  . HIS E  3 121 ? 47.573  243.375 60.439 1.00 33.52 ?  120 HIS E CA  1 
ATOM   5375  C  C   . HIS E  3 121 ? 48.376  243.817 61.665 1.00 39.80 ?  120 HIS E C   1 
ATOM   5376  O  O   . HIS E  3 121 ? 48.359  244.980 62.088 1.00 38.54 ?  120 HIS E O   1 
ATOM   5377  C  CB  . HIS E  3 121 ? 48.515  243.019 59.290 1.00 38.74 ?  120 HIS E CB  1 
ATOM   5378  C  CG  . HIS E  3 121 ? 47.885  242.159 58.242 1.00 43.87 ?  120 HIS E CG  1 
ATOM   5379  N  ND1 . HIS E  3 121 ? 47.988  240.785 58.247 1.00 42.79 ?  120 HIS E ND1 1 
ATOM   5380  C  CD2 . HIS E  3 121 ? 47.132  242.478 57.162 1.00 38.09 ?  120 HIS E CD2 1 
ATOM   5381  C  CE1 . HIS E  3 121 ? 47.333  240.294 57.210 1.00 38.69 ?  120 HIS E CE1 1 
ATOM   5382  N  NE2 . HIS E  3 121 ? 46.806  241.301 56.533 1.00 38.79 ?  120 HIS E NE2 1 
ATOM   5383  N  N   . GLU E  3 122 ? 49.091  242.846 62.235 1.00 42.11 ?  121 GLU E N   1 
ATOM   5384  C  CA  . GLU E  3 122 ? 49.802  243.060 63.494 1.00 43.61 ?  121 GLU E CA  1 
ATOM   5385  C  C   . GLU E  3 122 ? 51.051  243.905 63.288 1.00 43.06 ?  121 GLU E C   1 
ATOM   5386  O  O   . GLU E  3 122 ? 51.297  244.855 64.038 1.00 47.12 ?  121 GLU E O   1 
ATOM   5387  C  CB  . GLU E  3 122 ? 50.149  241.703 64.108 1.00 48.55 ?  121 GLU E CB  1 
ATOM   5388  C  CG  . GLU E  3 122 ? 51.185  241.701 65.221 1.00 48.81 ?  121 GLU E CG  1 
ATOM   5389  C  CD  . GLU E  3 122 ? 51.880  240.342 65.338 1.00 56.69 ?  121 GLU E CD  1 
ATOM   5390  O  OE1 . GLU E  3 122 ? 52.059  239.662 64.294 1.00 51.27 ?  121 GLU E OE1 1 
ATOM   5391  O  OE2 . GLU E  3 122 ? 52.231  239.948 66.474 1.00 61.96 ?  121 GLU E OE2 1 
ATOM   5392  N  N   . LYS E  3 123 ? 51.833  243.593 62.258 1.00 46.32 ?  122 LYS E N   1 
ATOM   5393  C  CA  . LYS E  3 123 ? 53.107  244.242 61.983 1.00 49.68 ?  122 LYS E CA  1 
ATOM   5394  C  C   . LYS E  3 123 ? 53.014  245.123 60.743 1.00 50.68 ?  122 LYS E C   1 
ATOM   5395  O  O   . LYS E  3 123 ? 52.028  245.109 59.997 1.00 45.82 ?  122 LYS E O   1 
ATOM   5396  C  CB  . LYS E  3 123 ? 54.211  243.195 61.794 1.00 47.35 ?  122 LYS E CB  1 
ATOM   5397  C  CG  . LYS E  3 123 ? 54.391  242.269 62.988 1.00 51.42 ?  122 LYS E CG  1 
ATOM   5398  C  CD  . LYS E  3 123 ? 55.743  241.575 62.926 1.00 56.15 ?  122 LYS E CD  1 
ATOM   5399  C  CE  . LYS E  3 123 ? 55.610  240.062 63.003 1.00 61.99 ?  122 LYS E CE  1 
ATOM   5400  N  NZ  . LYS E  3 123 ? 56.741  239.370 62.302 1.00 67.86 ?  122 LYS E NZ  1 
ATOM   5401  N  N   . ALA E  3 124 ? 54.086  245.878 60.517 1.00 48.11 ?  123 ALA E N   1 
ATOM   5402  C  CA  . ALA E  3 124 ? 54.160  246.750 59.359 1.00 46.60 ?  123 ALA E CA  1 
ATOM   5403  C  C   . ALA E  3 124 ? 54.293  245.940 58.078 1.00 44.05 ?  123 ALA E C   1 
ATOM   5404  O  O   . ALA E  3 124 ? 54.899  244.864 58.048 1.00 49.37 ?  123 ALA E O   1 
ATOM   5405  C  CB  . ALA E  3 124 ? 55.338  247.714 59.485 1.00 47.18 ?  123 ALA E CB  1 
ATOM   5406  N  N   . ASP E  3 125 ? 53.692  246.464 57.019 1.00 45.63 ?  124 ASP E N   1 
ATOM   5407  C  CA  . ASP E  3 125 ? 53.858  245.920 55.680 1.00 48.63 ?  124 ASP E CA  1 
ATOM   5408  C  C   . ASP E  3 125 ? 55.168  246.458 55.111 1.00 48.25 ?  124 ASP E C   1 
ATOM   5409  O  O   . ASP E  3 125 ? 55.350  247.678 55.017 1.00 49.69 ?  124 ASP E O   1 
ATOM   5410  C  CB  . ASP E  3 125 ? 52.653  246.318 54.819 1.00 44.33 ?  124 ASP E CB  1 
ATOM   5411  C  CG  . ASP E  3 125 ? 52.705  245.758 53.405 1.00 54.27 ?  124 ASP E CG  1 
ATOM   5412  O  OD1 . ASP E  3 125 ? 53.682  245.063 53.049 1.00 55.61 ?  124 ASP E OD1 1 
ATOM   5413  O  OD2 . ASP E  3 125 ? 51.752  246.031 52.638 1.00 53.37 ?  124 ASP E OD2 1 
ATOM   5414  N  N   . ASP E  3 126 ? 56.083  245.559 54.741 1.00 50.77 ?  125 ASP E N   1 
ATOM   5415  C  CA  . ASP E  3 126 ? 57.342  245.999 54.148 1.00 55.22 ?  125 ASP E CA  1 
ATOM   5416  C  C   . ASP E  3 126 ? 57.250  246.234 52.640 1.00 59.11 ?  125 ASP E C   1 
ATOM   5417  O  O   . ASP E  3 126 ? 58.280  246.516 52.010 1.00 59.44 ?  125 ASP E O   1 
ATOM   5418  C  CB  . ASP E  3 126 ? 58.472  245.006 54.475 1.00 51.70 ?  125 ASP E CB  1 
ATOM   5419  C  CG  . ASP E  3 126 ? 58.290  243.640 53.827 1.00 60.26 ?  125 ASP E CG  1 
ATOM   5420  O  OD1 . ASP E  3 126 ? 57.627  243.535 52.769 1.00 57.73 ?  125 ASP E OD1 1 
ATOM   5421  O  OD2 . ASP E  3 126 ? 58.844  242.656 54.378 1.00 58.80 ?  125 ASP E OD2 1 
ATOM   5422  N  N   . LEU E  3 127 ? 56.059  246.096 52.048 1.00 58.76 ?  126 LEU E N   1 
ATOM   5423  C  CA  . LEU E  3 127 ? 55.796  246.493 50.660 1.00 56.75 ?  126 LEU E CA  1 
ATOM   5424  C  C   . LEU E  3 127 ? 56.605  245.673 49.652 1.00 60.62 ?  126 LEU E C   1 
ATOM   5425  O  O   . LEU E  3 127 ? 56.968  246.171 48.580 1.00 58.30 ?  126 LEU E O   1 
ATOM   5426  C  CB  . LEU E  3 127 ? 56.066  247.988 50.451 1.00 51.31 ?  126 LEU E CB  1 
ATOM   5427  C  CG  . LEU E  3 127 ? 55.509  248.985 51.475 1.00 55.90 ?  126 LEU E CG  1 
ATOM   5428  C  CD1 . LEU E  3 127 ? 55.515  250.372 50.871 1.00 52.37 ?  126 LEU E CD1 1 
ATOM   5429  C  CD2 . LEU E  3 127 ? 54.095  248.611 51.908 1.00 49.41 ?  126 LEU E CD2 1 
ATOM   5430  N  N   . GLY E  3 128 ? 56.907  244.419 49.984 1.00 59.54 ?  127 GLY E N   1 
ATOM   5431  C  CA  . GLY E  3 128 ? 57.683  243.547 49.126 1.00 62.29 ?  127 GLY E CA  1 
ATOM   5432  C  C   . GLY E  3 128 ? 59.186  243.758 49.196 1.00 63.28 ?  127 GLY E C   1 
ATOM   5433  O  O   . GLY E  3 128 ? 59.945  242.822 48.916 1.00 68.68 ?  127 GLY E O   1 
ATOM   5434  N  N   . LYS E  3 129 ? 59.633  244.967 49.578 1.00 65.82 ?  128 LYS E N   1 
ATOM   5435  C  CA  . LYS E  3 129 ? 61.048  245.325 49.679 1.00 64.82 ?  128 LYS E CA  1 
ATOM   5436  C  C   . LYS E  3 129 ? 61.768  244.657 50.879 1.00 69.42 ?  128 LYS E C   1 
ATOM   5437  O  O   . LYS E  3 129 ? 62.823  245.153 51.302 1.00 76.76 ?  128 LYS E O   1 
ATOM   5438  C  CB  . LYS E  3 129 ? 61.204  246.847 49.762 1.00 50.33 ?  128 LYS E CB  1 
ATOM   5439  N  N   . GLY E  3 130 ? 61.231  243.569 51.439 1.00 66.69 ?  129 GLY E N   1 
ATOM   5440  C  CA  . GLY E  3 130 ? 61.782  242.889 52.598 1.00 61.58 ?  129 GLY E CA  1 
ATOM   5441  C  C   . GLY E  3 130 ? 62.801  241.798 52.322 1.00 70.63 ?  129 GLY E C   1 
ATOM   5442  O  O   . GLY E  3 130 ? 63.395  241.262 53.266 1.00 74.97 ?  129 GLY E O   1 
ATOM   5443  N  N   . GLY E  3 131 ? 63.030  241.449 51.059 1.00 69.16 ?  130 GLY E N   1 
ATOM   5444  C  CA  . GLY E  3 131 ? 64.022  240.444 50.728 1.00 65.51 ?  130 GLY E CA  1 
ATOM   5445  C  C   . GLY E  3 131 ? 63.791  239.101 51.399 1.00 68.65 ?  130 GLY E C   1 
ATOM   5446  O  O   . GLY E  3 131 ? 64.519  238.732 52.325 1.00 73.36 ?  130 GLY E O   1 
ATOM   5447  N  N   . ASN E  3 132 ? 62.757  238.386 50.944 1.00 71.49 ?  131 ASN E N   1 
ATOM   5448  C  CA  . ASN E  3 132 ? 62.453  237.004 51.318 1.00 69.49 ?  131 ASN E CA  1 
ATOM   5449  C  C   . ASN E  3 132 ? 61.130  236.603 50.674 1.00 69.22 ?  131 ASN E C   1 
ATOM   5450  O  O   . ASN E  3 132 ? 60.385  237.466 50.193 1.00 70.65 ?  131 ASN E O   1 
ATOM   5451  C  CB  . ASN E  3 132 ? 62.394  236.803 52.842 1.00 65.06 ?  131 ASN E CB  1 
ATOM   5452  C  CG  . ASN E  3 132 ? 61.492  237.810 53.538 1.00 63.82 ?  131 ASN E CG  1 
ATOM   5453  O  OD1 . ASN E  3 132 ? 60.263  237.715 53.475 1.00 66.93 ?  131 ASN E OD1 1 
ATOM   5454  N  ND2 . ASN E  3 132 ? 62.102  238.789 54.203 1.00 68.00 ?  131 ASN E ND2 1 
ATOM   5455  N  N   . GLU E  3 133 ? 60.829  235.300 50.658 1.00 71.57 ?  132 GLU E N   1 
ATOM   5456  C  CA  . GLU E  3 133 ? 59.636  234.819 49.964 1.00 66.54 ?  132 GLU E CA  1 
ATOM   5457  C  C   . GLU E  3 133 ? 58.363  235.352 50.614 1.00 68.74 ?  132 GLU E C   1 
ATOM   5458  O  O   . GLU E  3 133 ? 57.379  235.647 49.922 1.00 69.28 ?  132 GLU E O   1 
ATOM   5459  C  CB  . GLU E  3 133 ? 59.627  233.286 49.934 1.00 62.89 ?  132 GLU E CB  1 
ATOM   5460  C  CG  . GLU E  3 133 ? 58.697  232.646 48.894 1.00 68.30 ?  132 GLU E CG  1 
ATOM   5461  C  CD  . GLU E  3 133 ? 59.297  232.593 47.483 1.00 83.62 ?  132 GLU E CD  1 
ATOM   5462  O  OE1 . GLU E  3 133 ? 58.680  231.954 46.593 1.00 76.62 ?  132 GLU E OE1 1 
ATOM   5463  O  OE2 . GLU E  3 133 ? 60.370  233.202 47.256 1.00 84.88 ?  132 GLU E OE2 1 
ATOM   5464  N  N   . GLU E  3 134 ? 58.365  235.482 51.945 1.00 62.77 ?  133 GLU E N   1 
ATOM   5465  C  CA  . GLU E  3 134 ? 57.195  236.004 52.642 1.00 63.09 ?  133 GLU E CA  1 
ATOM   5466  C  C   . GLU E  3 134 ? 56.891  237.442 52.231 1.00 66.14 ?  133 GLU E C   1 
ATOM   5467  O  O   . GLU E  3 134 ? 55.721  237.847 52.202 1.00 62.63 ?  133 GLU E O   1 
ATOM   5468  C  CB  . GLU E  3 134 ? 57.408  235.917 54.158 1.00 65.16 ?  133 GLU E CB  1 
ATOM   5469  C  CG  . GLU E  3 134 ? 56.138  236.079 54.981 1.00 62.38 ?  133 GLU E CG  1 
ATOM   5470  C  CD  . GLU E  3 134 ? 55.017  235.170 54.495 1.00 70.51 ?  133 GLU E CD  1 
ATOM   5471  O  OE1 . GLU E  3 134 ? 55.194  233.929 54.504 1.00 76.83 ?  133 GLU E OE1 1 
ATOM   5472  O  OE2 . GLU E  3 134 ? 53.962  235.699 54.091 1.00 72.19 ?  133 GLU E OE2 1 
ATOM   5473  N  N   . SER E  3 135 ? 57.928  238.226 51.914 1.00 62.02 ?  134 SER E N   1 
ATOM   5474  C  CA  . SER E  3 135 ? 57.717  239.631 51.581 1.00 62.21 ?  134 SER E CA  1 
ATOM   5475  C  C   . SER E  3 135 ? 56.969  239.797 50.263 1.00 63.95 ?  134 SER E C   1 
ATOM   5476  O  O   . SER E  3 135 ? 56.205  240.759 50.101 1.00 60.45 ?  134 SER E O   1 
ATOM   5477  C  CB  . SER E  3 135 ? 59.056  240.365 51.524 1.00 65.61 ?  134 SER E CB  1 
ATOM   5478  O  OG  . SER E  3 135 ? 58.858  241.770 51.546 1.00 64.59 ?  134 SER E OG  1 
ATOM   5479  N  N   . THR E  3 136 ? 57.183  238.884 49.314 1.00 63.46 ?  135 THR E N   1 
ATOM   5480  C  CA  . THR E  3 136 ? 56.489  238.926 48.032 1.00 63.86 ?  135 THR E CA  1 
ATOM   5481  C  C   . THR E  3 136 ? 55.050  238.441 48.126 1.00 62.72 ?  135 THR E C   1 
ATOM   5482  O  O   . THR E  3 136 ? 54.296  238.610 47.161 1.00 63.77 ?  135 THR E O   1 
ATOM   5483  C  CB  . THR E  3 136 ? 57.231  238.078 46.987 1.00 61.60 ?  135 THR E CB  1 
ATOM   5484  O  OG1 . THR E  3 136 ? 57.014  236.684 47.261 1.00 64.97 ?  135 THR E OG1 1 
ATOM   5485  C  CG2 . THR E  3 136 ? 58.722  238.369 47.003 1.00 55.32 ?  135 THR E CG2 1 
ATOM   5486  N  N   . LYS E  3 137 ? 54.663  237.833 49.249 1.00 57.74 ?  136 LYS E N   1 
ATOM   5487  C  CA  . LYS E  3 137 ? 53.330  237.271 49.426 1.00 59.19 ?  136 LYS E CA  1 
ATOM   5488  C  C   . LYS E  3 137 ? 52.464  238.088 50.375 1.00 62.19 ?  136 LYS E C   1 
ATOM   5489  O  O   . LYS E  3 137 ? 51.310  238.389 50.049 1.00 55.71 ?  136 LYS E O   1 
ATOM   5490  C  CB  . LYS E  3 137 ? 53.436  235.812 49.916 1.00 58.39 ?  136 LYS E CB  1 
ATOM   5491  C  CG  . LYS E  3 137 ? 53.768  234.808 48.792 1.00 62.30 ?  136 LYS E CG  1 
ATOM   5492  C  CD  . LYS E  3 137 ? 53.768  233.336 49.267 1.00 64.12 ?  136 LYS E CD  1 
ATOM   5493  C  CE  . LYS E  3 137 ? 52.356  232.779 49.527 1.00 61.66 ?  136 LYS E CE  1 
ATOM   5494  N  NZ  . LYS E  3 137 ? 51.986  232.797 50.989 1.00 67.35 ?  136 LYS E NZ  1 
ATOM   5495  N  N   . THR E  3 138 ? 52.997  238.477 51.543 1.00 56.02 ?  137 THR E N   1 
ATOM   5496  C  CA  . THR E  3 138 ? 52.210  239.164 52.560 1.00 55.17 ?  137 THR E CA  1 
ATOM   5497  C  C   . THR E  3 138 ? 52.855  240.440 53.085 1.00 57.58 ?  137 THR E C   1 
ATOM   5498  O  O   . THR E  3 138 ? 52.250  241.109 53.934 1.00 52.00 ?  137 THR E O   1 
ATOM   5499  C  CB  . THR E  3 138 ? 51.922  238.232 53.757 1.00 61.79 ?  137 THR E CB  1 
ATOM   5500  O  OG1 . THR E  3 138 ? 53.120  237.993 54.518 1.00 58.32 ?  137 THR E OG1 1 
ATOM   5501  C  CG2 . THR E  3 138 ? 51.317  236.901 53.282 1.00 56.91 ?  137 THR E CG2 1 
ATOM   5502  N  N   . GLY E  3 139 ? 54.052  240.795 52.617 1.00 58.87 ?  138 GLY E N   1 
ATOM   5503  C  CA  . GLY E  3 139 ? 54.755  241.934 53.169 1.00 56.93 ?  138 GLY E CA  1 
ATOM   5504  C  C   . GLY E  3 139 ? 55.218  241.774 54.601 1.00 54.08 ?  138 GLY E C   1 
ATOM   5505  O  O   . GLY E  3 139 ? 55.630  242.762 55.211 1.00 54.71 ?  138 GLY E O   1 
ATOM   5506  N  N   . ASN E  3 140 ? 55.149  240.555 55.152 1.00 52.52 ?  139 ASN E N   1 
ATOM   5507  C  CA  . ASN E  3 140 ? 55.541  240.280 56.539 1.00 54.23 ?  139 ASN E CA  1 
ATOM   5508  C  C   . ASN E  3 140 ? 54.741  241.121 57.538 1.00 56.15 ?  139 ASN E C   1 
ATOM   5509  O  O   . ASN E  3 140 ? 55.256  241.542 58.577 1.00 54.26 ?  139 ASN E O   1 
ATOM   5510  C  CB  . ASN E  3 140 ? 57.047  240.490 56.736 1.00 60.71 ?  139 ASN E CB  1 
ATOM   5511  C  CG  . ASN E  3 140 ? 57.880  239.449 56.013 1.00 60.84 ?  139 ASN E CG  1 
ATOM   5512  O  OD1 . ASN E  3 140 ? 57.858  238.272 56.366 1.00 58.58 ?  139 ASN E OD1 1 
ATOM   5513  N  ND2 . ASN E  3 140 ? 58.603  239.878 54.982 1.00 54.89 ?  139 ASN E ND2 1 
ATOM   5514  N  N   . ALA E  3 141 ? 53.462  241.363 57.232 1.00 55.52 ?  140 ALA E N   1 
ATOM   5515  C  CA  . ALA E  3 141 ? 52.630  242.189 58.107 1.00 51.29 ?  140 ALA E CA  1 
ATOM   5516  C  C   . ALA E  3 141 ? 52.083  241.432 59.323 1.00 50.19 ?  140 ALA E C   1 
ATOM   5517  O  O   . ALA E  3 141 ? 51.328  242.012 60.114 1.00 53.05 ?  140 ALA E O   1 
ATOM   5518  C  CB  . ALA E  3 141 ? 51.480  242.805 57.306 1.00 44.49 ?  140 ALA E CB  1 
ATOM   5519  N  N   . GLY E  3 142 ? 52.441  240.170 59.507 1.00 48.61 ?  141 GLY E N   1 
ATOM   5520  C  CA  . GLY E  3 142 ? 52.073  239.489 60.729 1.00 51.33 ?  141 GLY E CA  1 
ATOM   5521  C  C   . GLY E  3 142 ? 50.622  239.048 60.733 1.00 56.12 ?  141 GLY E C   1 
ATOM   5522  O  O   . GLY E  3 142 ? 49.923  239.051 59.708 1.00 54.82 ?  141 GLY E O   1 
ATOM   5523  N  N   . SER E  3 143 ? 50.164  238.667 61.924 1.00 50.24 ?  142 SER E N   1 
ATOM   5524  C  CA  . SER E  3 143 ? 48.834  238.098 62.074 1.00 51.60 ?  142 SER E CA  1 
ATOM   5525  C  C   . SER E  3 143 ? 47.756  239.158 61.830 1.00 46.92 ?  142 SER E C   1 
ATOM   5526  O  O   . SER E  3 143 ? 48.026  240.351 61.666 1.00 47.79 ?  142 SER E O   1 
ATOM   5527  C  CB  . SER E  3 143 ? 48.673  237.475 63.461 1.00 46.89 ?  142 SER E CB  1 
ATOM   5528  O  OG  . SER E  3 143 ? 48.154  238.423 64.376 1.00 53.45 ?  142 SER E OG  1 
ATOM   5529  N  N   . ARG E  3 144 ? 46.512  238.702 61.807 1.00 45.91 ?  143 ARG E N   1 
ATOM   5530  C  CA  . ARG E  3 144 ? 45.374  239.545 61.471 1.00 39.89 ?  143 ARG E CA  1 
ATOM   5531  C  C   . ARG E  3 144 ? 44.670  239.962 62.754 1.00 40.13 ?  143 ARG E C   1 
ATOM   5532  O  O   . ARG E  3 144 ? 44.157  239.111 63.494 1.00 40.25 ?  143 ARG E O   1 
ATOM   5533  C  CB  . ARG E  3 144 ? 44.439  238.792 60.525 1.00 32.86 ?  143 ARG E CB  1 
ATOM   5534  C  CG  . ARG E  3 144 ? 45.201  238.191 59.385 1.00 36.29 ?  143 ARG E CG  1 
ATOM   5535  C  CD  . ARG E  3 144 ? 44.347  237.313 58.518 1.00 33.62 ?  143 ARG E CD  1 
ATOM   5536  N  NE  . ARG E  3 144 ? 45.169  236.668 57.502 1.00 39.27 ?  143 ARG E NE  1 
ATOM   5537  C  CZ  . ARG E  3 144 ? 44.680  236.017 56.457 1.00 38.30 ?  143 ARG E CZ  1 
ATOM   5538  N  NH1 . ARG E  3 144 ? 43.375  235.909 56.256 1.00 36.54 ?  143 ARG E NH1 1 
ATOM   5539  N  NH2 . ARG E  3 144 ? 45.516  235.448 55.598 1.00 38.32 ?  143 ARG E NH2 1 
ATOM   5540  N  N   . LEU E  3 145 ? 44.656  241.267 63.018 1.00 32.75 ?  144 LEU E N   1 
ATOM   5541  C  CA  . LEU E  3 145 ? 44.146  241.788 64.277 1.00 31.67 ?  144 LEU E CA  1 
ATOM   5542  C  C   . LEU E  3 145 ? 42.649  242.022 64.247 1.00 34.63 ?  144 LEU E C   1 
ATOM   5543  O  O   . LEU E  3 145 ? 41.969  241.851 65.263 1.00 31.83 ?  144 LEU E O   1 
ATOM   5544  C  CB  . LEU E  3 145 ? 44.837  243.110 64.609 1.00 38.63 ?  144 LEU E CB  1 
ATOM   5545  C  CG  . LEU E  3 145 ? 46.338  243.029 64.840 1.00 41.00 ?  144 LEU E CG  1 
ATOM   5546  C  CD1 . LEU E  3 145 ? 46.834  244.361 65.379 1.00 39.29 ?  144 LEU E CD1 1 
ATOM   5547  C  CD2 . LEU E  3 145 ? 46.625  241.912 65.821 1.00 41.19 ?  144 LEU E CD2 1 
ATOM   5548  N  N   . ALA E  3 146 ? 42.127  242.464 63.113 1.00 31.98 ?  145 ALA E N   1 
ATOM   5549  C  CA  . ALA E  3 146 ? 40.710  242.770 63.011 1.00 30.89 ?  145 ALA E CA  1 
ATOM   5550  C  C   . ALA E  3 146 ? 40.369  242.789 61.538 1.00 34.53 ?  145 ALA E C   1 
ATOM   5551  O  O   . ALA E  3 146 ? 41.236  243.060 60.698 1.00 29.16 ?  145 ALA E O   1 
ATOM   5552  C  CB  . ALA E  3 146 ? 40.372  244.116 63.656 1.00 32.51 ?  145 ALA E CB  1 
ATOM   5553  N  N   . CYS E  3 147 ? 39.106  242.504 61.234 1.00 31.14 ?  146 CYS E N   1 
ATOM   5554  C  CA  . CYS E  3 147 ? 38.673  242.516 59.848 1.00 33.08 ?  146 CYS E CA  1 
ATOM   5555  C  C   . CYS E  3 147 ? 37.171  242.720 59.784 1.00 32.26 ?  146 CYS E C   1 
ATOM   5556  O  O   . CYS E  3 147 ? 36.462  242.662 60.791 1.00 33.51 ?  146 CYS E O   1 
ATOM   5557  C  CB  . CYS E  3 147 ? 39.064  241.228 59.127 1.00 30.23 ?  146 CYS E CB  1 
ATOM   5558  S  SG  . CYS E  3 147 ? 38.431  239.740 59.913 1.00 37.12 ?  146 CYS E SG  1 
ATOM   5559  N  N   . GLY E  3 148 ? 36.707  242.953 58.565 1.00 31.62 ?  147 GLY E N   1 
ATOM   5560  C  CA  . GLY E  3 148 ? 35.296  243.131 58.289 1.00 33.46 ?  147 GLY E CA  1 
ATOM   5561  C  C   . GLY E  3 148 ? 35.059  242.893 56.818 1.00 33.55 ?  147 GLY E C   1 
ATOM   5562  O  O   . GLY E  3 148 ? 35.969  243.053 55.997 1.00 30.95 ?  147 GLY E O   1 
ATOM   5563  N  N   . VAL E  3 149 ? 33.841  242.470 56.486 1.00 31.42 ?  148 VAL E N   1 
ATOM   5564  C  CA  . VAL E  3 149 ? 33.441  242.355 55.090 1.00 28.33 ?  148 VAL E CA  1 
ATOM   5565  C  C   . VAL E  3 149 ? 33.049  243.736 54.588 1.00 33.11 ?  148 VAL E C   1 
ATOM   5566  O  O   . VAL E  3 149 ? 32.405  244.516 55.305 1.00 30.86 ?  148 VAL E O   1 
ATOM   5567  C  CB  . VAL E  3 149 ? 32.290  241.338 54.932 1.00 30.26 ?  148 VAL E CB  1 
ATOM   5568  C  CG1 . VAL E  3 149 ? 31.905  241.170 53.456 1.00 26.38 ?  148 VAL E CG1 1 
ATOM   5569  C  CG2 . VAL E  3 149 ? 32.715  240.006 55.487 1.00 30.15 ?  148 VAL E CG2 1 
ATOM   5570  N  N   . ILE E  3 150 ? 33.484  244.068 53.378 1.00 28.50 ?  149 ILE E N   1 
ATOM   5571  C  CA  . ILE E  3 150 ? 33.216  245.386 52.804 1.00 28.71 ?  149 ILE E CA  1 
ATOM   5572  C  C   . ILE E  3 150 ? 31.810  245.379 52.224 1.00 28.92 ?  149 ILE E C   1 
ATOM   5573  O  O   . ILE E  3 150 ? 31.517  244.615 51.294 1.00 27.55 ?  149 ILE E O   1 
ATOM   5574  C  CB  . ILE E  3 150 ? 34.252  245.743 51.725 1.00 28.61 ?  149 ILE E CB  1 
ATOM   5575  C  CG1 . ILE E  3 150 ? 35.651  245.859 52.329 1.00 29.06 ?  149 ILE E CG1 1 
ATOM   5576  C  CG2 . ILE E  3 150 ? 33.897  247.048 51.042 1.00 29.79 ?  149 ILE E CG2 1 
ATOM   5577  C  CD1 . ILE E  3 150 ? 36.767  245.800 51.294 1.00 32.59 ?  149 ILE E CD1 1 
ATOM   5578  N  N   . GLY E  3 151 ? 30.937  246.223 52.770 1.00 25.85 ?  150 GLY E N   1 
ATOM   5579  C  CA  . GLY E  3 151 ? 29.545  246.233 52.353 1.00 30.05 ?  150 GLY E CA  1 
ATOM   5580  C  C   . GLY E  3 151 ? 29.135  247.489 51.599 1.00 32.27 ?  150 GLY E C   1 
ATOM   5581  O  O   . GLY E  3 151 ? 29.796  248.519 51.702 1.00 29.55 ?  150 GLY E O   1 
ATOM   5582  N  N   . ILE E  3 152 ? 28.042  247.420 50.844 1.00 30.02 ?  151 ILE E N   1 
ATOM   5583  C  CA  . ILE E  3 152 ? 27.535  248.599 50.153 1.00 29.95 ?  151 ILE E CA  1 
ATOM   5584  C  C   . ILE E  3 152 ? 26.911  249.534 51.174 1.00 31.25 ?  151 ILE E C   1 
ATOM   5585  O  O   . ILE E  3 152 ? 26.190  249.095 52.078 1.00 30.42 ?  151 ILE E O   1 
ATOM   5586  C  CB  . ILE E  3 152 ? 26.519  248.189 49.074 1.00 33.75 ?  151 ILE E CB  1 
ATOM   5587  C  CG1 . ILE E  3 152 ? 27.199  247.325 48.016 1.00 31.86 ?  151 ILE E CG1 1 
ATOM   5588  C  CG2 . ILE E  3 152 ? 25.908  249.409 48.408 1.00 31.19 ?  151 ILE E CG2 1 
ATOM   5589  C  CD1 . ILE E  3 152 ? 26.231  246.487 47.228 1.00 40.14 ?  151 ILE E CD1 1 
ATOM   5590  N  N   . ALA E  3 153 ? 27.194  250.828 51.050 1.00 29.73 ?  152 ALA E N   1 
ATOM   5591  C  CA  . ALA E  3 153 ? 26.709  251.810 52.004 1.00 32.24 ?  152 ALA E CA  1 
ATOM   5592  C  C   . ALA E  3 153 ? 25.806  252.819 51.311 1.00 33.79 ?  152 ALA E C   1 
ATOM   5593  O  O   . ALA E  3 153 ? 25.873  253.015 50.096 1.00 36.08 ?  152 ALA E O   1 
ATOM   5594  C  CB  . ALA E  3 153 ? 27.866  252.540 52.695 1.00 32.08 ?  152 ALA E CB  1 
ATOM   5595  N  N   . GLN E  3 154 ? 24.941  253.441 52.096 1.00 33.88 ?  153 GLN E N   1 
ATOM   5596  C  CA  . GLN E  3 154 ? 24.083  254.496 51.581 1.00 40.62 ?  153 GLN E CA  1 
ATOM   5597  C  C   . GLN E  3 154 ? 24.894  255.772 51.433 1.00 53.13 ?  153 GLN E C   1 
ATOM   5598  O  O   . GLN E  3 154 ? 25.662  256.147 52.336 1.00 52.27 ?  153 GLN E O   1 
ATOM   5599  C  CB  . GLN E  3 154 ? 22.895  254.738 52.503 1.00 44.01 ?  153 GLN E CB  1 
ATOM   5600  C  CG  . GLN E  3 154 ? 21.856  255.693 51.928 1.00 53.00 ?  153 GLN E CG  1 
ATOM   5601  C  CD  . GLN E  3 154 ? 20.626  255.838 52.821 1.00 54.16 ?  153 GLN E CD  1 
ATOM   5602  O  OE1 . GLN E  3 154 ? 19.490  255.703 52.356 1.00 59.21 ?  153 GLN E OE1 1 
ATOM   5603  N  NE2 . GLN E  3 154 ? 20.850  256.093 54.109 1.00 54.16 ?  153 GLN E NE2 1 
ATOM   5604  O  OXT . GLN E  3 154 ? 24.792  256.444 50.408 1.00 65.91 ?  153 GLN E OXT 1 
ATOM   5605  N  N   . MET F  1 1   ? 30.048  236.820 38.339 1.00 62.78 ?  0   MET F N   1 
ATOM   5606  C  CA  . MET F  1 1   ? 31.067  237.067 39.363 1.00 67.02 ?  0   MET F CA  1 
ATOM   5607  C  C   . MET F  1 1   ? 31.332  235.805 40.185 1.00 69.61 ?  0   MET F C   1 
ATOM   5608  O  O   . MET F  1 1   ? 31.976  234.855 39.714 1.00 69.26 ?  0   MET F O   1 
ATOM   5609  C  CB  . MET F  1 1   ? 30.643  238.219 40.292 1.00 55.13 ?  0   MET F CB  1 
ATOM   5610  N  N   . ALA F  1 2   ? 30.818  235.804 41.414 1.00 67.35 ?  1   ALA F N   1 
ATOM   5611  C  CA  . ALA F  1 2   ? 31.006  234.695 42.336 1.00 51.76 ?  1   ALA F CA  1 
ATOM   5612  C  C   . ALA F  1 2   ? 29.951  233.617 42.120 1.00 45.57 ?  1   ALA F C   1 
ATOM   5613  O  O   . ALA F  1 2   ? 28.847  233.872 41.632 1.00 45.99 ?  1   ALA F O   1 
ATOM   5614  C  CB  . ALA F  1 2   ? 30.959  235.181 43.787 1.00 51.11 ?  1   ALA F CB  1 
ATOM   5615  N  N   . THR F  1 3   ? 30.318  232.391 42.471 1.00 44.24 ?  2   THR F N   1 
ATOM   5616  C  CA  . THR F  1 3   ? 29.372  231.298 42.530 1.00 38.76 ?  2   THR F CA  1 
ATOM   5617  C  C   . THR F  1 3   ? 29.057  230.888 43.955 1.00 34.83 ?  2   THR F C   1 
ATOM   5618  O  O   . THR F  1 3   ? 28.146  230.084 44.160 1.00 34.72 ?  2   THR F O   1 
ATOM   5619  C  CB  . THR F  1 3   ? 29.908  230.085 41.757 1.00 45.15 ?  2   THR F CB  1 
ATOM   5620  O  OG1 . THR F  1 3   ? 31.106  229.620 42.392 1.00 40.38 ?  2   THR F OG1 1 
ATOM   5621  C  CG2 . THR F  1 3   ? 30.198  230.455 40.300 1.00 47.44 ?  2   THR F CG2 1 
ATOM   5622  N  N   . LYS F  1 4   ? 29.801  231.396 44.936 1.00 32.34 ?  3   LYS F N   1 
ATOM   5623  C  CA  . LYS F  1 4   ? 29.556  231.090 46.335 1.00 31.54 ?  3   LYS F CA  1 
ATOM   5624  C  C   . LYS F  1 4   ? 29.707  232.347 47.163 1.00 31.47 ?  3   LYS F C   1 
ATOM   5625  O  O   . LYS F  1 4   ? 30.595  233.167 46.917 1.00 28.99 ?  3   LYS F O   1 
ATOM   5626  C  CB  . LYS F  1 4   ? 30.521  230.031 46.887 1.00 38.00 ?  3   LYS F CB  1 
ATOM   5627  C  CG  . LYS F  1 4   ? 30.374  228.672 46.253 1.00 44.92 ?  3   LYS F CG  1 
ATOM   5628  C  CD  . LYS F  1 4   ? 31.378  227.688 46.836 1.00 42.54 ?  3   LYS F CD  1 
ATOM   5629  C  CE  . LYS F  1 4   ? 30.975  227.236 48.235 1.00 47.90 ?  3   LYS F CE  1 
ATOM   5630  N  NZ  . LYS F  1 4   ? 32.027  226.351 48.824 1.00 48.72 ?  3   LYS F NZ  1 
ATOM   5631  N  N   . ALA F  1 5   ? 28.857  232.467 48.169 1.00 27.87 ?  4   ALA F N   1 
ATOM   5632  C  CA  . ALA F  1 5   ? 28.910  233.573 49.097 1.00 25.96 ?  4   ALA F CA  1 
ATOM   5633  C  C   . ALA F  1 5   ? 28.609  232.991 50.466 1.00 27.44 ?  4   ALA F C   1 
ATOM   5634  O  O   . ALA F  1 5   ? 28.151  231.851 50.582 1.00 28.65 ?  4   ALA F O   1 
ATOM   5635  C  CB  . ALA F  1 5   ? 27.930  234.687 48.695 1.00 24.25 ?  4   ALA F CB  1 
ATOM   5636  N  N   . VAL F  1 6   ? 28.907  233.754 51.510 1.00 23.25 ?  5   VAL F N   1 
ATOM   5637  C  CA  . VAL F  1 6   ? 28.736  233.269 52.870 1.00 27.71 ?  5   VAL F CA  1 
ATOM   5638  C  C   . VAL F  1 6   ? 28.464  234.466 53.763 1.00 29.85 ?  5   VAL F C   1 
ATOM   5639  O  O   . VAL F  1 6   ? 28.857  235.592 53.462 1.00 31.73 ?  5   VAL F O   1 
ATOM   5640  C  CB  . VAL F  1 6   ? 29.966  232.455 53.334 1.00 29.90 ?  5   VAL F CB  1 
ATOM   5641  C  CG1 . VAL F  1 6   ? 31.156  233.383 53.559 1.00 24.43 ?  5   VAL F CG1 1 
ATOM   5642  C  CG2 . VAL F  1 6   ? 29.623  231.673 54.581 1.00 29.45 ?  5   VAL F CG2 1 
ATOM   5643  N  N   . CYS F  1 7   ? 27.763  234.221 54.857 1.00 29.37 ?  6   CYS F N   1 
ATOM   5644  C  CA  . CYS F  1 7   ? 27.347  235.289 55.739 1.00 24.71 ?  6   CYS F CA  1 
ATOM   5645  C  C   . CYS F  1 7   ? 27.378  234.766 57.163 1.00 29.81 ?  6   CYS F C   1 
ATOM   5646  O  O   . CYS F  1 7   ? 26.822  233.701 57.438 1.00 22.70 ?  6   CYS F O   1 
ATOM   5647  C  CB  . CYS F  1 7   ? 25.943  235.747 55.375 1.00 25.26 ?  6   CYS F CB  1 
ATOM   5648  S  SG  . CYS F  1 7   ? 25.347  237.016 56.456 1.00 31.26 ?  6   CYS F SG  1 
ATOM   5649  N  N   . VAL F  1 8   ? 28.025  235.504 58.058 1.00 28.17 ?  7   VAL F N   1 
ATOM   5650  C  CA  . VAL F  1 8   ? 28.054  235.156 59.476 1.00 26.93 ?  7   VAL F CA  1 
ATOM   5651  C  C   . VAL F  1 8   ? 27.047  236.049 60.177 1.00 25.73 ?  7   VAL F C   1 
ATOM   5652  O  O   . VAL F  1 8   ? 27.184  237.276 60.159 1.00 28.60 ?  7   VAL F O   1 
ATOM   5653  C  CB  . VAL F  1 8   ? 29.461  235.320 60.067 1.00 31.44 ?  7   VAL F CB  1 
ATOM   5654  C  CG1 . VAL F  1 8   ? 29.455  235.024 61.560 1.00 33.23 ?  7   VAL F CG1 1 
ATOM   5655  C  CG2 . VAL F  1 8   ? 30.419  234.395 59.344 1.00 31.15 ?  7   VAL F CG2 1 
ATOM   5656  N  N   . LEU F  1 9   ? 26.013  235.447 60.755 1.00 21.99 ?  8   LEU F N   1 
ATOM   5657  C  CA  . LEU F  1 9   ? 24.963  236.213 61.413 1.00 24.33 ?  8   LEU F CA  1 
ATOM   5658  C  C   . LEU F  1 9   ? 25.332  236.421 62.871 1.00 27.00 ?  8   LEU F C   1 
ATOM   5659  O  O   . LEU F  1 9   ? 25.651  235.461 63.571 1.00 30.04 ?  8   LEU F O   1 
ATOM   5660  C  CB  . LEU F  1 9   ? 23.617  235.494 61.309 1.00 27.78 ?  8   LEU F CB  1 
ATOM   5661  C  CG  . LEU F  1 9   ? 23.068  235.348 59.879 1.00 31.44 ?  8   LEU F CG  1 
ATOM   5662  C  CD1 . LEU F  1 9   ? 21.929  234.353 59.862 1.00 27.98 ?  8   LEU F CD1 1 
ATOM   5663  C  CD2 . LEU F  1 9   ? 22.596  236.672 59.366 1.00 29.51 ?  8   LEU F CD2 1 
ATOM   5664  N  N   . LYS F  1 10  ? 25.289  237.669 63.323 1.00 31.30 ?  9   LYS F N   1 
ATOM   5665  C  CA  . LYS F  1 10  ? 25.570  238.013 64.709 1.00 32.19 ?  9   LYS F CA  1 
ATOM   5666  C  C   . LYS F  1 10  ? 24.634  239.122 65.143 1.00 31.37 ?  9   LYS F C   1 
ATOM   5667  O  O   . LYS F  1 10  ? 24.196  239.941 64.328 1.00 28.88 ?  9   LYS F O   1 
ATOM   5668  C  CB  . LYS F  1 10  ? 27.015  238.475 64.919 1.00 33.38 ?  9   LYS F CB  1 
ATOM   5669  C  CG  . LYS F  1 10  ? 28.004  237.332 64.989 1.00 40.78 ?  9   LYS F CG  1 
ATOM   5670  C  CD  . LYS F  1 10  ? 29.386  237.805 65.455 1.00 56.05 ?  9   LYS F CD  1 
ATOM   5671  C  CE  . LYS F  1 10  ? 30.444  236.700 65.306 1.00 59.15 ?  9   LYS F CE  1 
ATOM   5672  N  NZ  . LYS F  1 10  ? 31.165  236.787 63.991 1.00 58.07 ?  9   LYS F NZ  1 
ATOM   5673  N  N   . GLY F  1 11  ? 24.341  239.149 66.438 1.00 35.07 ?  10  GLY F N   1 
ATOM   5674  C  CA  . GLY F  1 11  ? 23.471  240.174 66.975 1.00 37.17 ?  10  GLY F CA  1 
ATOM   5675  C  C   . GLY F  1 11  ? 23.754  240.500 68.427 1.00 37.57 ?  10  GLY F C   1 
ATOM   5676  O  O   . GLY F  1 11  ? 24.744  240.037 69.004 1.00 38.32 ?  10  GLY F O   1 
ATOM   5677  N  N   . ASP F  1 12  ? 22.873  241.298 69.025 1.00 41.77 ?  11  ASP F N   1 
ATOM   5678  C  CA  . ASP F  1 12  ? 23.049  241.651 70.430 1.00 48.80 ?  11  ASP F CA  1 
ATOM   5679  C  C   . ASP F  1 12  ? 22.741  240.478 71.349 1.00 48.26 ?  11  ASP F C   1 
ATOM   5680  O  O   . ASP F  1 12  ? 23.264  240.415 72.463 1.00 55.16 ?  11  ASP F O   1 
ATOM   5681  C  CB  . ASP F  1 12  ? 22.157  242.839 70.776 1.00 50.17 ?  11  ASP F CB  1 
ATOM   5682  C  CG  . ASP F  1 12  ? 22.782  244.159 70.381 1.00 65.05 ?  11  ASP F CG  1 
ATOM   5683  O  OD1 . ASP F  1 12  ? 23.963  244.157 69.961 1.00 66.94 ?  11  ASP F OD1 1 
ATOM   5684  O  OD2 . ASP F  1 12  ? 22.092  245.197 70.483 1.00 77.43 ?  11  ASP F OD2 1 
ATOM   5685  N  N   . GLY F  1 13  ? 21.899  239.548 70.911 1.00 41.76 ?  12  GLY F N   1 
ATOM   5686  C  CA  . GLY F  1 13  ? 21.480  238.461 71.761 1.00 35.44 ?  12  GLY F CA  1 
ATOM   5687  C  C   . GLY F  1 13  ? 22.153  237.161 71.395 1.00 30.43 ?  12  GLY F C   1 
ATOM   5688  O  O   . GLY F  1 13  ? 23.294  237.130 70.922 1.00 37.18 ?  12  GLY F O   1 
ATOM   5689  N  N   . PRO F  1 14  ? 21.450  236.049 71.597 1.00 33.30 ?  13  PRO F N   1 
ATOM   5690  C  CA  . PRO F  1 14  ? 22.039  234.733 71.353 1.00 31.11 ?  13  PRO F CA  1 
ATOM   5691  C  C   . PRO F  1 14  ? 21.926  234.228 69.921 1.00 32.21 ?  13  PRO F C   1 
ATOM   5692  O  O   . PRO F  1 14  ? 22.429  233.140 69.632 1.00 30.01 ?  13  PRO F O   1 
ATOM   5693  C  CB  . PRO F  1 14  ? 21.214  233.843 72.295 1.00 31.75 ?  13  PRO F CB  1 
ATOM   5694  C  CG  . PRO F  1 14  ? 19.868  234.489 72.283 1.00 34.62 ?  13  PRO F CG  1 
ATOM   5695  C  CD  . PRO F  1 14  ? 20.103  235.966 72.190 1.00 30.86 ?  13  PRO F CD  1 
ATOM   5696  N  N   . VAL F  1 15  ? 21.282  234.950 69.015 1.00 30.87 ?  14  VAL F N   1 
ATOM   5697  C  CA  . VAL F  1 15  ? 21.091  234.429 67.664 1.00 27.81 ?  14  VAL F CA  1 
ATOM   5698  C  C   . VAL F  1 15  ? 22.401  234.540 66.898 1.00 26.90 ?  14  VAL F C   1 
ATOM   5699  O  O   . VAL F  1 15  ? 22.967  235.632 66.766 1.00 28.71 ?  14  VAL F O   1 
ATOM   5700  C  CB  . VAL F  1 15  ? 19.962  235.162 66.934 1.00 26.59 ?  14  VAL F CB  1 
ATOM   5701  C  CG1 . VAL F  1 15  ? 19.780  234.557 65.549 1.00 25.68 ?  14  VAL F CG1 1 
ATOM   5702  C  CG2 . VAL F  1 15  ? 18.666  235.028 67.711 1.00 29.07 ?  14  VAL F CG2 1 
ATOM   5703  N  N   . GLN F  1 16  ? 22.887  233.413 66.395 1.00 29.98 ?  15  GLN F N   1 
ATOM   5704  C  CA  . GLN F  1 16  ? 24.080  233.399 65.567 1.00 33.39 ?  15  GLN F CA  1 
ATOM   5705  C  C   . GLN F  1 16  ? 23.984  232.224 64.611 1.00 30.98 ?  15  GLN F C   1 
ATOM   5706  O  O   . GLN F  1 16  ? 23.334  231.220 64.899 1.00 28.88 ?  15  GLN F O   1 
ATOM   5707  C  CB  . GLN F  1 16  ? 25.351  233.293 66.413 1.00 32.12 ?  15  GLN F CB  1 
ATOM   5708  C  CG  . GLN F  1 16  ? 25.395  232.062 67.267 1.00 43.37 ?  15  GLN F CG  1 
ATOM   5709  C  CD  . GLN F  1 16  ? 26.705  231.959 68.009 1.00 54.90 ?  15  GLN F CD  1 
ATOM   5710  O  OE1 . GLN F  1 16  ? 27.643  231.320 67.538 1.00 69.81 ?  15  GLN F OE1 1 
ATOM   5711  N  NE2 . GLN F  1 16  ? 26.794  232.623 69.157 1.00 52.23 ?  15  GLN F NE2 1 
ATOM   5712  N  N   . GLY F  1 17  ? 24.649  232.351 63.472 1.00 31.07 ?  16  GLY F N   1 
ATOM   5713  C  CA  . GLY F  1 17  ? 24.648  231.267 62.513 1.00 30.23 ?  16  GLY F CA  1 
ATOM   5714  C  C   . GLY F  1 17  ? 25.510  231.615 61.321 1.00 27.50 ?  16  GLY F C   1 
ATOM   5715  O  O   . GLY F  1 17  ? 26.102  232.694 61.241 1.00 29.37 ?  16  GLY F O   1 
ATOM   5716  N  N   . ILE F  1 18  ? 25.589  230.662 60.407 1.00 31.74 ?  17  ILE F N   1 
ATOM   5717  C  CA  . ILE F  1 18  ? 26.353  230.785 59.175 1.00 27.27 ?  17  ILE F CA  1 
ATOM   5718  C  C   . ILE F  1 18  ? 25.446  230.363 58.039 1.00 26.98 ?  17  ILE F C   1 
ATOM   5719  O  O   . ILE F  1 18  ? 24.905  229.251 58.059 1.00 21.78 ?  17  ILE F O   1 
ATOM   5720  C  CB  . ILE F  1 18  ? 27.617  229.907 59.184 1.00 28.08 ?  17  ILE F CB  1 
ATOM   5721  C  CG1 . ILE F  1 18  ? 28.658  230.440 60.168 1.00 31.40 ?  17  ILE F CG1 1 
ATOM   5722  C  CG2 . ILE F  1 18  ? 28.175  229.814 57.767 1.00 29.01 ?  17  ILE F CG2 1 
ATOM   5723  C  CD1 . ILE F  1 18  ? 29.751  229.435 60.495 1.00 30.36 ?  17  ILE F CD1 1 
ATOM   5724  N  N   . ILE F  1 19  ? 25.289  231.234 57.043 1.00 26.37 ?  18  ILE F N   1 
ATOM   5725  C  CA  . ILE F  1 19  ? 24.450  230.950 55.892 1.00 20.34 ?  18  ILE F CA  1 
ATOM   5726  C  C   . ILE F  1 19  ? 25.322  230.959 54.646 1.00 29.96 ?  18  ILE F C   1 
ATOM   5727  O  O   . ILE F  1 19  ? 26.089  231.907 54.420 1.00 28.56 ?  18  ILE F O   1 
ATOM   5728  C  CB  . ILE F  1 19  ? 23.297  231.964 55.768 1.00 23.56 ?  18  ILE F CB  1 
ATOM   5729  C  CG1 . ILE F  1 19  ? 22.356  231.879 56.985 1.00 23.50 ?  18  ILE F CG1 1 
ATOM   5730  C  CG2 . ILE F  1 19  ? 22.562  231.755 54.457 1.00 20.34 ?  18  ILE F CG2 1 
ATOM   5731  C  CD1 . ILE F  1 19  ? 21.620  230.511 57.153 1.00 20.53 ?  18  ILE F CD1 1 
ATOM   5732  N  N   . ASN F  1 20  ? 25.195  229.914 53.836 1.00 26.63 ?  19  ASN F N   1 
ATOM   5733  C  CA  . ASN F  1 20  ? 25.933  229.780 52.595 1.00 30.56 ?  19  ASN F CA  1 
ATOM   5734  C  C   . ASN F  1 20  ? 25.016  230.081 51.418 1.00 30.11 ?  19  ASN F C   1 
ATOM   5735  O  O   . ASN F  1 20  ? 23.807  229.824 51.463 1.00 24.50 ?  19  ASN F O   1 
ATOM   5736  C  CB  . ASN F  1 20  ? 26.519  228.369 52.454 1.00 28.33 ?  19  ASN F CB  1 
ATOM   5737  C  CG  . ASN F  1 20  ? 27.312  227.940 53.677 1.00 33.95 ?  19  ASN F CG  1 
ATOM   5738  O  OD1 . ASN F  1 20  ? 26.841  227.137 54.496 1.00 32.78 ?  19  ASN F OD1 1 
ATOM   5739  N  ND2 . ASN F  1 20  ? 28.504  228.492 53.822 1.00 30.60 ?  19  ASN F ND2 1 
ATOM   5740  N  N   . PHE F  1 21  ? 25.602  230.643 50.364 1.00 24.95 ?  20  PHE F N   1 
ATOM   5741  C  CA  . PHE F  1 21  ? 24.879  230.892 49.132 1.00 23.20 ?  20  PHE F CA  1 
ATOM   5742  C  C   . PHE F  1 21  ? 25.664  230.241 48.005 1.00 28.19 ?  20  PHE F C   1 
ATOM   5743  O  O   . PHE F  1 21  ? 26.883  230.395 47.930 1.00 29.47 ?  20  PHE F O   1 
ATOM   5744  C  CB  . PHE F  1 21  ? 24.722  232.374 48.844 1.00 21.79 ?  20  PHE F CB  1 
ATOM   5745  C  CG  . PHE F  1 21  ? 23.989  233.149 49.911 1.00 24.56 ?  20  PHE F CG  1 
ATOM   5746  C  CD1 . PHE F  1 21  ? 24.651  233.598 51.040 1.00 21.94 ?  20  PHE F CD1 1 
ATOM   5747  C  CD2 . PHE F  1 21  ? 22.658  233.494 49.736 1.00 20.53 ?  20  PHE F CD2 1 
ATOM   5748  C  CE1 . PHE F  1 21  ? 23.984  234.356 51.999 1.00 25.99 ?  20  PHE F CE1 1 
ATOM   5749  C  CE2 . PHE F  1 21  ? 21.985  234.233 50.682 1.00 30.35 ?  20  PHE F CE2 1 
ATOM   5750  C  CZ  . PHE F  1 21  ? 22.651  234.674 51.820 1.00 23.93 ?  20  PHE F CZ  1 
ATOM   5751  N  N   . GLU F  1 22  ? 24.978  229.523 47.130 1.00 25.46 ?  21  GLU F N   1 
ATOM   5752  C  CA  . GLU F  1 22  ? 25.649  228.946 45.975 1.00 33.21 ?  21  GLU F CA  1 
ATOM   5753  C  C   . GLU F  1 22  ? 24.828  229.194 44.723 1.00 32.40 ?  21  GLU F C   1 
ATOM   5754  O  O   . GLU F  1 22  ? 23.608  229.001 44.728 1.00 30.01 ?  21  GLU F O   1 
ATOM   5755  C  CB  . GLU F  1 22  ? 25.888  227.451 46.175 1.00 29.73 ?  21  GLU F CB  1 
ATOM   5756  C  CG  . GLU F  1 22  ? 26.907  226.887 45.193 1.00 55.19 ?  21  GLU F CG  1 
ATOM   5757  C  CD  . GLU F  1 22  ? 27.062  225.390 45.334 1.00 67.90 ?  21  GLU F CD  1 
ATOM   5758  O  OE1 . GLU F  1 22  ? 27.125  224.926 46.495 1.00 66.95 ?  21  GLU F OE1 1 
ATOM   5759  O  OE2 . GLU F  1 22  ? 27.111  224.688 44.294 1.00 76.13 ?  21  GLU F OE2 1 
ATOM   5760  N  N   . GLN F  1 23  ? 25.497  229.631 43.655 1.00 32.54 ?  22  GLN F N   1 
ATOM   5761  C  CA  . GLN F  1 23  ? 24.851  229.890 42.373 1.00 31.94 ?  22  GLN F CA  1 
ATOM   5762  C  C   . GLN F  1 23  ? 25.717  229.251 41.286 1.00 39.90 ?  22  GLN F C   1 
ATOM   5763  O  O   . GLN F  1 23  ? 26.765  229.782 40.914 1.00 40.16 ?  22  GLN F O   1 
ATOM   5764  C  CB  . GLN F  1 23  ? 24.657  231.382 42.127 1.00 30.52 ?  22  GLN F CB  1 
ATOM   5765  C  CG  . GLN F  1 23  ? 23.705  231.687 40.969 1.00 36.22 ?  22  GLN F CG  1 
ATOM   5766  C  CD  . GLN F  1 23  ? 23.447  233.170 40.789 1.00 36.64 ?  22  GLN F CD  1 
ATOM   5767  O  OE1 . GLN F  1 23  ? 24.282  234.005 41.151 1.00 36.25 ?  22  GLN F OE1 1 
ATOM   5768  N  NE2 . GLN F  1 23  ? 22.291  233.510 40.221 1.00 34.23 ?  22  GLN F NE2 1 
ATOM   5769  N  N   . LYS F  1 24  ? 25.274  228.098 40.796 1.00 42.62 ?  23  LYS F N   1 
ATOM   5770  C  CA  . LYS F  1 24  ? 26.056  227.324 39.831 1.00 53.61 ?  23  LYS F CA  1 
ATOM   5771  C  C   . LYS F  1 24  ? 26.151  228.043 38.484 1.00 42.27 ?  23  LYS F C   1 
ATOM   5772  O  O   . LYS F  1 24  ? 27.211  228.053 37.854 1.00 49.30 ?  23  LYS F O   1 
ATOM   5773  C  CB  . LYS F  1 24  ? 25.432  225.930 39.709 1.00 51.32 ?  23  LYS F CB  1 
ATOM   5774  C  CG  . LYS F  1 24  ? 25.523  225.215 38.361 1.00 63.75 ?  23  LYS F CG  1 
ATOM   5775  C  CD  . LYS F  1 24  ? 24.351  224.211 38.202 1.00 61.20 ?  23  LYS F CD  1 
ATOM   5776  C  CE  . LYS F  1 24  ? 24.094  223.381 39.477 1.00 64.64 ?  23  LYS F CE  1 
ATOM   5777  N  NZ  . LYS F  1 24  ? 22.735  222.727 39.465 1.00 64.36 ?  23  LYS F NZ  1 
ATOM   5778  N  N   . GLU F  1 25  ? 25.073  228.680 38.044 1.00 46.02 ?  24  GLU F N   1 
ATOM   5779  C  CA  . GLU F  1 25  ? 25.068  229.465 36.819 1.00 50.75 ?  24  GLU F CA  1 
ATOM   5780  C  C   . GLU F  1 25  ? 24.432  230.813 37.108 1.00 45.49 ?  24  GLU F C   1 
ATOM   5781  O  O   . GLU F  1 25  ? 23.534  230.906 37.944 1.00 49.42 ?  24  GLU F O   1 
ATOM   5782  C  CB  . GLU F  1 25  ? 24.282  228.756 35.714 1.00 55.95 ?  24  GLU F CB  1 
ATOM   5783  C  CG  . GLU F  1 25  ? 24.616  227.282 35.537 1.00 59.25 ?  24  GLU F CG  1 
ATOM   5784  C  CD  . GLU F  1 25  ? 25.715  227.075 34.508 1.00 69.50 ?  24  GLU F CD  1 
ATOM   5785  O  OE1 . GLU F  1 25  ? 25.537  227.545 33.359 1.00 79.91 ?  24  GLU F OE1 1 
ATOM   5786  O  OE2 . GLU F  1 25  ? 26.752  226.456 34.849 1.00 70.40 ?  24  GLU F OE2 1 
ATOM   5787  N  N   . SER F  1 26  ? 24.870  231.860 36.405 1.00 45.51 ?  25  SER F N   1 
ATOM   5788  C  CA  . SER F  1 26  ? 24.279  233.174 36.674 1.00 50.59 ?  25  SER F CA  1 
ATOM   5789  C  C   . SER F  1 26  ? 22.809  233.222 36.267 1.00 55.84 ?  25  SER F C   1 
ATOM   5790  O  O   . SER F  1 26  ? 22.012  233.938 36.890 1.00 51.33 ?  25  SER F O   1 
ATOM   5791  C  CB  . SER F  1 26  ? 25.064  234.276 35.970 1.00 56.52 ?  25  SER F CB  1 
ATOM   5792  O  OG  . SER F  1 26  ? 25.142  234.044 34.577 1.00 54.98 ?  25  SER F OG  1 
ATOM   5793  N  N   . ASN F  1 27  ? 22.428  232.457 35.242 1.00 51.08 ?  26  ASN F N   1 
ATOM   5794  C  CA  . ASN F  1 27  ? 21.014  232.294 34.914 1.00 56.15 ?  26  ASN F CA  1 
ATOM   5795  C  C   . ASN F  1 27  ? 20.251  231.485 35.956 1.00 60.48 ?  26  ASN F C   1 
ATOM   5796  O  O   . ASN F  1 27  ? 19.053  231.232 35.772 1.00 63.45 ?  26  ASN F O   1 
ATOM   5797  C  CB  . ASN F  1 27  ? 20.868  231.642 33.530 1.00 52.26 ?  26  ASN F CB  1 
ATOM   5798  C  CG  . ASN F  1 27  ? 21.102  230.110 33.531 1.00 56.60 ?  26  ASN F CG  1 
ATOM   5799  O  OD1 . ASN F  1 27  ? 21.766  229.565 34.406 1.00 60.21 ?  26  ASN F OD1 1 
ATOM   5800  N  ND2 . ASN F  1 27  ? 20.562  229.427 32.516 1.00 52.92 ?  26  ASN F ND2 1 
ATOM   5801  N  N   . GLY F  1 28  ? 20.908  231.076 37.035 1.00 47.80 ?  27  GLY F N   1 
ATOM   5802  C  CA  . GLY F  1 28  ? 20.383  230.025 37.863 1.00 48.07 ?  27  GLY F CA  1 
ATOM   5803  C  C   . GLY F  1 28  ? 19.874  230.507 39.200 1.00 39.86 ?  27  GLY F C   1 
ATOM   5804  O  O   . GLY F  1 28  ? 20.128  231.632 39.646 1.00 36.54 ?  27  GLY F O   1 
ATOM   5805  N  N   . PRO F  1 29  ? 19.109  229.644 39.847 1.00 38.65 ?  28  PRO F N   1 
ATOM   5806  C  CA  . PRO F  1 29  ? 18.685  229.909 41.213 1.00 40.44 ?  28  PRO F CA  1 
ATOM   5807  C  C   . PRO F  1 29  ? 19.869  229.865 42.160 1.00 38.77 ?  28  PRO F C   1 
ATOM   5808  O  O   . PRO F  1 29  ? 20.921  229.292 41.870 1.00 33.03 ?  28  PRO F O   1 
ATOM   5809  C  CB  . PRO F  1 29  ? 17.698  228.773 41.500 1.00 39.70 ?  28  PRO F CB  1 
ATOM   5810  C  CG  . PRO F  1 29  ? 18.078  227.708 40.542 1.00 42.10 ?  28  PRO F CG  1 
ATOM   5811  C  CD  . PRO F  1 29  ? 18.554  228.392 39.321 1.00 43.04 ?  28  PRO F CD  1 
ATOM   5812  N  N   . VAL F  1 30  ? 19.679  230.495 43.314 1.00 29.33 ?  29  VAL F N   1 
ATOM   5813  C  CA  . VAL F  1 30  ? 20.685  230.541 44.358 1.00 26.44 ?  29  VAL F CA  1 
ATOM   5814  C  C   . VAL F  1 30  ? 20.241  229.587 45.446 1.00 29.43 ?  29  VAL F C   1 
ATOM   5815  O  O   . VAL F  1 30  ? 19.106  229.667 45.928 1.00 31.72 ?  29  VAL F O   1 
ATOM   5816  C  CB  . VAL F  1 30  ? 20.855  231.971 44.899 1.00 27.63 ?  29  VAL F CB  1 
ATOM   5817  C  CG1 . VAL F  1 30  ? 21.945  232.021 45.962 1.00 21.98 ?  29  VAL F CG1 1 
ATOM   5818  C  CG2 . VAL F  1 30  ? 21.173  232.925 43.735 1.00 29.12 ?  29  VAL F CG2 1 
ATOM   5819  N  N   . LYS F  1 31  ? 21.107  228.662 45.809 1.00 29.47 ?  30  LYS F N   1 
ATOM   5820  C  CA  . LYS F  1 31  ? 20.845  227.796 46.943 1.00 31.26 ?  30  LYS F CA  1 
ATOM   5821  C  C   . LYS F  1 31  ? 21.326  228.495 48.204 1.00 28.92 ?  30  LYS F C   1 
ATOM   5822  O  O   . LYS F  1 31  ? 22.448  229.011 48.237 1.00 28.42 ?  30  LYS F O   1 
ATOM   5823  C  CB  . LYS F  1 31  ? 21.542  226.453 46.759 1.00 32.58 ?  30  LYS F CB  1 
ATOM   5824  C  CG  . LYS F  1 31  ? 20.655  225.417 46.094 1.00 52.79 ?  30  LYS F CG  1 
ATOM   5825  C  CD  . LYS F  1 31  ? 19.490  225.057 47.025 1.00 58.36 ?  30  LYS F CD  1 
ATOM   5826  C  CE  . LYS F  1 31  ? 19.999  224.634 48.412 1.00 54.94 ?  30  LYS F CE  1 
ATOM   5827  N  NZ  . LYS F  1 31  ? 18.936  224.680 49.459 1.00 43.72 ?  30  LYS F NZ  1 
ATOM   5828  N  N   . VAL F  1 32  ? 20.470  228.525 49.221 1.00 27.53 ?  31  VAL F N   1 
ATOM   5829  C  CA  . VAL F  1 32  ? 20.726  229.210 50.489 1.00 28.84 ?  31  VAL F CA  1 
ATOM   5830  C  C   . VAL F  1 32  ? 20.602  228.164 51.588 1.00 29.16 ?  31  VAL F C   1 
ATOM   5831  O  O   . VAL F  1 32  ? 19.553  227.526 51.717 1.00 28.68 ?  31  VAL F O   1 
ATOM   5832  C  CB  . VAL F  1 32  ? 19.732  230.362 50.721 1.00 27.00 ?  31  VAL F CB  1 
ATOM   5833  C  CG1 . VAL F  1 32  ? 20.056  231.121 52.002 1.00 20.34 ?  31  VAL F CG1 1 
ATOM   5834  C  CG2 . VAL F  1 32  ? 19.706  231.318 49.511 1.00 28.53 ?  31  VAL F CG2 1 
ATOM   5835  N  N   . TRP F  1 33  ? 21.663  227.958 52.356 1.00 24.44 ?  32  TRP F N   1 
ATOM   5836  C  CA  . TRP F  1 33  ? 21.581  226.894 53.347 1.00 25.71 ?  32  TRP F CA  1 
ATOM   5837  C  C   . TRP F  1 33  ? 22.559  227.176 54.471 1.00 30.42 ?  32  TRP F C   1 
ATOM   5838  O  O   . TRP F  1 33  ? 23.572  227.850 54.282 1.00 28.95 ?  32  TRP F O   1 
ATOM   5839  C  CB  . TRP F  1 33  ? 21.853  225.508 52.735 1.00 29.46 ?  32  TRP F CB  1 
ATOM   5840  C  CG  . TRP F  1 33  ? 23.303  225.136 52.660 1.00 32.35 ?  32  TRP F CG  1 
ATOM   5841  C  CD1 . TRP F  1 33  ? 24.045  224.442 53.593 1.00 33.26 ?  32  TRP F CD1 1 
ATOM   5842  C  CD2 . TRP F  1 33  ? 24.194  225.441 51.592 1.00 30.24 ?  32  TRP F CD2 1 
ATOM   5843  N  NE1 . TRP F  1 33  ? 25.346  224.307 53.161 1.00 33.83 ?  32  TRP F NE1 1 
ATOM   5844  C  CE2 . TRP F  1 33  ? 25.460  224.911 51.933 1.00 34.16 ?  32  TRP F CE2 1 
ATOM   5845  C  CE3 . TRP F  1 33  ? 24.050  226.118 50.387 1.00 35.26 ?  32  TRP F CE3 1 
ATOM   5846  C  CZ2 . TRP F  1 33  ? 26.567  225.042 51.103 1.00 44.77 ?  32  TRP F CZ2 1 
ATOM   5847  C  CZ3 . TRP F  1 33  ? 25.153  226.239 49.556 1.00 44.15 ?  32  TRP F CZ3 1 
ATOM   5848  C  CH2 . TRP F  1 33  ? 26.394  225.698 49.915 1.00 44.98 ?  32  TRP F CH2 1 
ATOM   5849  N  N   . GLY F  1 34  ? 22.229  226.665 55.641 1.00 28.70 ?  33  GLY F N   1 
ATOM   5850  C  CA  . GLY F  1 34  ? 23.114  226.791 56.781 1.00 27.78 ?  33  GLY F CA  1 
ATOM   5851  C  C   . GLY F  1 34  ? 22.314  226.621 58.051 1.00 28.09 ?  33  GLY F C   1 
ATOM   5852  O  O   . GLY F  1 34  ? 21.177  226.162 58.040 1.00 31.06 ?  33  GLY F O   1 
ATOM   5853  N  N   . SER F  1 35  ? 22.931  227.007 59.150 1.00 29.77 ?  34  SER F N   1 
ATOM   5854  C  CA  . SER F  1 35  ? 22.327  226.768 60.442 1.00 30.34 ?  34  SER F CA  1 
ATOM   5855  C  C   . SER F  1 35  ? 22.308  228.067 61.225 1.00 28.46 ?  34  SER F C   1 
ATOM   5856  O  O   . SER F  1 35  ? 23.305  228.796 61.232 1.00 31.74 ?  34  SER F O   1 
ATOM   5857  C  CB  . SER F  1 35  ? 23.105  225.690 61.200 1.00 36.84 ?  34  SER F CB  1 
ATOM   5858  O  OG  . SER F  1 35  ? 22.298  225.156 62.218 1.00 44.01 ?  34  SER F OG  1 
ATOM   5859  N  N   . ILE F  1 36  ? 21.169  228.375 61.849 1.00 26.19 ?  35  ILE F N   1 
ATOM   5860  C  CA  . ILE F  1 36  ? 21.043  229.494 62.785 1.00 26.01 ?  35  ILE F CA  1 
ATOM   5861  C  C   . ILE F  1 36  ? 20.566  228.935 64.113 1.00 28.14 ?  35  ILE F C   1 
ATOM   5862  O  O   . ILE F  1 36  ? 19.595  228.176 64.150 1.00 29.37 ?  35  ILE F O   1 
ATOM   5863  C  CB  . ILE F  1 36  ? 20.069  230.577 62.288 1.00 27.51 ?  35  ILE F CB  1 
ATOM   5864  C  CG1 . ILE F  1 36  ? 20.429  231.015 60.865 1.00 29.43 ?  35  ILE F CG1 1 
ATOM   5865  C  CG2 . ILE F  1 36  ? 20.077  231.792 63.227 1.00 23.71 ?  35  ILE F CG2 1 
ATOM   5866  C  CD1 . ILE F  1 36  ? 19.322  231.805 60.170 1.00 29.03 ?  35  ILE F CD1 1 
ATOM   5867  N  N   . LYS F  1 37  ? 21.224  229.314 65.200 1.00 27.14 ?  36  LYS F N   1 
ATOM   5868  C  CA  . LYS F  1 37  ? 20.807  228.817 66.502 1.00 31.05 ?  36  LYS F CA  1 
ATOM   5869  C  C   . LYS F  1 37  ? 20.466  229.977 67.421 1.00 31.34 ?  36  LYS F C   1 
ATOM   5870  O  O   . LYS F  1 37  ? 20.723  231.149 67.110 1.00 29.02 ?  36  LYS F O   1 
ATOM   5871  C  CB  . LYS F  1 37  ? 21.888  227.927 67.119 1.00 31.56 ?  36  LYS F CB  1 
ATOM   5872  C  CG  . LYS F  1 37  ? 23.127  228.678 67.504 1.00 41.96 ?  36  LYS F CG  1 
ATOM   5873  C  CD  . LYS F  1 37  ? 24.180  227.700 67.982 1.00 56.60 ?  36  LYS F CD  1 
ATOM   5874  C  CE  . LYS F  1 37  ? 25.097  228.350 69.019 1.00 56.85 ?  36  LYS F CE  1 
ATOM   5875  N  NZ  . LYS F  1 37  ? 26.123  227.373 69.492 1.00 62.97 ?  36  LYS F NZ  1 
ATOM   5876  N  N   . GLY F  1 38  ? 19.852  229.640 68.554 1.00 28.52 ?  37  GLY F N   1 
ATOM   5877  C  CA  . GLY F  1 38  ? 19.460  230.656 69.518 1.00 27.81 ?  37  GLY F CA  1 
ATOM   5878  C  C   . GLY F  1 38  ? 18.130  231.323 69.239 1.00 28.52 ?  37  GLY F C   1 
ATOM   5879  O  O   . GLY F  1 38  ? 17.805  232.321 69.895 1.00 29.80 ?  37  GLY F O   1 
ATOM   5880  N  N   . LEU F  1 39  ? 17.345  230.808 68.301 1.00 28.25 ?  38  LEU F N   1 
ATOM   5881  C  CA  . LEU F  1 39  ? 16.061  231.405 67.946 1.00 28.31 ?  38  LEU F CA  1 
ATOM   5882  C  C   . LEU F  1 39  ? 14.939  230.829 68.805 1.00 29.25 ?  38  LEU F C   1 
ATOM   5883  O  O   . LEU F  1 39  ? 15.024  229.703 69.270 1.00 28.39 ?  38  LEU F O   1 
ATOM   5884  C  CB  . LEU F  1 39  ? 15.746  231.129 66.477 1.00 25.89 ?  38  LEU F CB  1 
ATOM   5885  C  CG  . LEU F  1 39  ? 16.670  231.752 65.428 1.00 26.33 ?  38  LEU F CG  1 
ATOM   5886  C  CD1 . LEU F  1 39  ? 16.589  230.998 64.081 1.00 26.42 ?  38  LEU F CD1 1 
ATOM   5887  C  CD2 . LEU F  1 39  ? 16.261  233.194 65.279 1.00 21.82 ?  38  LEU F CD2 1 
ATOM   5888  N  N   . THR F  1 40  ? 13.866  231.593 68.980 1.00 30.16 ?  39  THR F N   1 
ATOM   5889  C  CA  . THR F  1 40  ? 12.649  230.978 69.479 1.00 33.23 ?  39  THR F CA  1 
ATOM   5890  C  C   . THR F  1 40  ? 12.059  230.054 68.416 1.00 31.92 ?  39  THR F C   1 
ATOM   5891  O  O   . THR F  1 40  ? 12.154  230.309 67.211 1.00 33.62 ?  39  THR F O   1 
ATOM   5892  C  CB  . THR F  1 40  ? 11.624  232.037 69.875 1.00 29.18 ?  39  THR F CB  1 
ATOM   5893  O  OG1 . THR F  1 40  ? 11.312  232.854 68.734 1.00 33.47 ?  39  THR F OG1 1 
ATOM   5894  C  CG2 . THR F  1 40  ? 12.165  232.917 71.023 1.00 28.73 ?  39  THR F CG2 1 
ATOM   5895  N  N   . GLU F  1 41  ? 11.456  228.965 68.882 1.00 28.92 ?  40  GLU F N   1 
ATOM   5896  C  CA  . GLU F  1 41  ? 10.825  227.988 67.997 1.00 31.44 ?  40  GLU F CA  1 
ATOM   5897  C  C   . GLU F  1 41  ? 9.758   228.634 67.125 1.00 28.68 ?  40  GLU F C   1 
ATOM   5898  O  O   . GLU F  1 41  ? 8.999   229.495 67.573 1.00 30.66 ?  40  GLU F O   1 
ATOM   5899  C  CB  . GLU F  1 41  ? 10.197  226.858 68.820 1.00 30.43 ?  40  GLU F CB  1 
ATOM   5900  C  CG  . GLU F  1 41  ? 9.646   225.701 67.992 1.00 28.65 ?  40  GLU F CG  1 
ATOM   5901  C  CD  . GLU F  1 41  ? 8.971   224.638 68.871 1.00 44.78 ?  40  GLU F CD  1 
ATOM   5902  O  OE1 . GLU F  1 41  ? 8.861   224.858 70.099 1.00 41.18 ?  40  GLU F OE1 1 
ATOM   5903  O  OE2 . GLU F  1 41  ? 8.539   223.595 68.332 1.00 52.05 ?  40  GLU F OE2 1 
ATOM   5904  N  N   . GLY F  1 42  ? 9.697   228.210 65.873 1.00 29.97 ?  41  GLY F N   1 
ATOM   5905  C  CA  . GLY F  1 42  ? 8.733   228.756 64.950 1.00 27.45 ?  41  GLY F CA  1 
ATOM   5906  C  C   . GLY F  1 42  ? 9.372   229.595 63.861 1.00 26.67 ?  41  GLY F C   1 
ATOM   5907  O  O   . GLY F  1 42  ? 10.563  229.489 63.555 1.00 26.46 ?  41  GLY F O   1 
ATOM   5908  N  N   . LEU F  1 43  ? 8.549   230.456 63.265 1.00 25.50 ?  42  LEU F N   1 
ATOM   5909  C  CA  . LEU F  1 43  ? 8.901   231.127 62.017 1.00 29.16 ?  42  LEU F CA  1 
ATOM   5910  C  C   . LEU F  1 43  ? 9.587   232.457 62.274 1.00 27.87 ?  42  LEU F C   1 
ATOM   5911  O  O   . LEU F  1 43  ? 9.180   233.221 63.152 1.00 29.74 ?  42  LEU F O   1 
ATOM   5912  C  CB  . LEU F  1 43  ? 7.661   231.367 61.155 1.00 30.26 ?  42  LEU F CB  1 
ATOM   5913  C  CG  . LEU F  1 43  ? 6.870   230.216 60.532 1.00 32.39 ?  42  LEU F CG  1 
ATOM   5914  C  CD1 . LEU F  1 43  ? 5.487   230.736 60.215 1.00 34.57 ?  42  LEU F CD1 1 
ATOM   5915  C  CD2 . LEU F  1 43  ? 7.533   229.690 59.247 1.00 28.63 ?  42  LEU F CD2 1 
ATOM   5916  N  N   . HIS F  1 44  ? 10.611  232.754 61.473 1.00 26.36 ?  43  HIS F N   1 
ATOM   5917  C  CA  . HIS F  1 44  ? 11.370  233.994 61.580 1.00 24.85 ?  43  HIS F CA  1 
ATOM   5918  C  C   . HIS F  1 44  ? 11.607  234.586 60.201 1.00 25.72 ?  43  HIS F C   1 
ATOM   5919  O  O   . HIS F  1 44  ? 12.136  233.905 59.317 1.00 20.38 ?  43  HIS F O   1 
ATOM   5920  C  CB  . HIS F  1 44  ? 12.711  233.740 62.264 1.00 20.56 ?  43  HIS F CB  1 
ATOM   5921  C  CG  . HIS F  1 44  ? 12.578  233.343 63.701 1.00 29.65 ?  43  HIS F CG  1 
ATOM   5922  N  ND1 . HIS F  1 44  ? 12.559  234.276 64.715 1.00 28.40 ?  43  HIS F ND1 1 
ATOM   5923  C  CD2 . HIS F  1 44  ? 12.438  232.132 64.295 1.00 25.59 ?  43  HIS F CD2 1 
ATOM   5924  C  CE1 . HIS F  1 44  ? 12.422  233.656 65.874 1.00 32.92 ?  43  HIS F CE1 1 
ATOM   5925  N  NE2 . HIS F  1 44  ? 12.344  232.356 65.647 1.00 28.73 ?  43  HIS F NE2 1 
ATOM   5926  N  N   . GLY F  1 45  ? 11.240  235.852 60.030 1.00 23.84 ?  44  GLY F N   1 
ATOM   5927  C  CA  . GLY F  1 45  ? 11.505  236.561 58.793 1.00 25.88 ?  44  GLY F CA  1 
ATOM   5928  C  C   . GLY F  1 45  ? 12.972  236.492 58.448 1.00 27.06 ?  44  GLY F C   1 
ATOM   5929  O  O   . GLY F  1 45  ? 13.832  236.558 59.327 1.00 24.64 ?  44  GLY F O   1 
ATOM   5930  N  N   . PHE F  1 46  ? 13.267  236.338 57.162 1.00 20.34 ?  45  PHE F N   1 
ATOM   5931  C  CA  . PHE F  1 46  ? 14.620  236.045 56.671 1.00 24.10 ?  45  PHE F CA  1 
ATOM   5932  C  C   . PHE F  1 46  ? 14.770  236.851 55.380 1.00 26.00 ?  45  PHE F C   1 
ATOM   5933  O  O   . PHE F  1 46  ? 14.193  236.479 54.350 1.00 25.49 ?  45  PHE F O   1 
ATOM   5934  C  CB  . PHE F  1 46  ? 14.752  234.545 56.443 1.00 21.65 ?  45  PHE F CB  1 
ATOM   5935  C  CG  . PHE F  1 46  ? 16.144  234.053 56.160 1.00 21.98 ?  45  PHE F CG  1 
ATOM   5936  C  CD1 . PHE F  1 46  ? 17.131  234.073 57.135 1.00 20.37 ?  45  PHE F CD1 1 
ATOM   5937  C  CD2 . PHE F  1 46  ? 16.438  233.491 54.916 1.00 27.24 ?  45  PHE F CD2 1 
ATOM   5938  C  CE1 . PHE F  1 46  ? 18.417  233.555 56.870 1.00 23.14 ?  45  PHE F CE1 1 
ATOM   5939  C  CE2 . PHE F  1 46  ? 17.718  232.974 54.644 1.00 28.20 ?  45  PHE F CE2 1 
ATOM   5940  C  CZ  . PHE F  1 46  ? 18.707  233.012 55.642 1.00 25.90 ?  45  PHE F CZ  1 
ATOM   5941  N  N   . HIS F  1 47  ? 15.523  237.952 55.437 1.00 20.45 ?  46  HIS F N   1 
ATOM   5942  C  CA  . HIS F  1 47  ? 15.521  238.940 54.364 1.00 24.88 ?  46  HIS F CA  1 
ATOM   5943  C  C   . HIS F  1 47  ? 16.923  239.435 54.057 1.00 27.79 ?  46  HIS F C   1 
ATOM   5944  O  O   . HIS F  1 47  ? 17.763  239.547 54.956 1.00 25.84 ?  46  HIS F O   1 
ATOM   5945  C  CB  . HIS F  1 47  ? 14.659  240.172 54.724 1.00 24.05 ?  46  HIS F CB  1 
ATOM   5946  C  CG  . HIS F  1 47  ? 13.281  239.819 55.172 1.00 28.54 ?  46  HIS F CG  1 
ATOM   5947  N  ND1 . HIS F  1 47  ? 12.755  240.238 56.373 1.00 28.48 ?  46  HIS F ND1 1 
ATOM   5948  C  CD2 . HIS F  1 47  ? 12.330  239.054 54.589 1.00 27.22 ?  46  HIS F CD2 1 
ATOM   5949  C  CE1 . HIS F  1 47  ? 11.528  239.762 56.503 1.00 27.03 ?  46  HIS F CE1 1 
ATOM   5950  N  NE2 . HIS F  1 47  ? 11.252  239.025 55.443 1.00 25.15 ?  46  HIS F NE2 1 
ATOM   5951  N  N   . VAL F  1 48  ? 17.154  239.774 52.787 1.00 22.48 ?  47  VAL F N   1 
ATOM   5952  C  CA  . VAL F  1 48  ? 18.335  240.533 52.410 1.00 23.40 ?  47  VAL F CA  1 
ATOM   5953  C  C   . VAL F  1 48  ? 17.961  242.004 52.459 1.00 28.13 ?  47  VAL F C   1 
ATOM   5954  O  O   . VAL F  1 48  ? 16.996  242.427 51.816 1.00 23.81 ?  47  VAL F O   1 
ATOM   5955  C  CB  . VAL F  1 48  ? 18.862  240.153 51.020 1.00 20.43 ?  47  VAL F CB  1 
ATOM   5956  C  CG1 . VAL F  1 48  ? 20.066  241.028 50.701 1.00 23.50 ?  47  VAL F CG1 1 
ATOM   5957  C  CG2 . VAL F  1 48  ? 19.256  238.681 50.950 1.00 20.34 ?  47  VAL F CG2 1 
ATOM   5958  N  N   . HIS F  1 49  ? 18.708  242.774 53.235 1.00 21.05 ?  48  HIS F N   1 
ATOM   5959  C  CA  . HIS F  1 49  ? 18.506  244.208 53.318 1.00 26.33 ?  48  HIS F CA  1 
ATOM   5960  C  C   . HIS F  1 49  ? 19.522  244.920 52.433 1.00 23.44 ?  48  HIS F C   1 
ATOM   5961  O  O   . HIS F  1 49  ? 20.555  244.362 52.055 1.00 25.62 ?  48  HIS F O   1 
ATOM   5962  C  CB  . HIS F  1 49  ? 18.612  244.697 54.776 1.00 21.73 ?  48  HIS F CB  1 
ATOM   5963  C  CG  . HIS F  1 49  ? 17.478  244.253 55.651 1.00 25.53 ?  48  HIS F CG  1 
ATOM   5964  N  ND1 . HIS F  1 49  ? 16.656  245.141 56.319 1.00 23.45 ?  48  HIS F ND1 1 
ATOM   5965  C  CD2 . HIS F  1 49  ? 17.034  243.014 55.977 1.00 25.60 ?  48  HIS F CD2 1 
ATOM   5966  C  CE1 . HIS F  1 49  ? 15.754  244.467 57.012 1.00 29.24 ?  48  HIS F CE1 1 
ATOM   5967  N  NE2 . HIS F  1 49  ? 15.956  243.174 56.817 1.00 27.66 ?  48  HIS F NE2 1 
ATOM   5968  N  N   . GLU F  1 50  ? 19.240  246.190 52.161 1.00 28.15 ?  49  GLU F N   1 
ATOM   5969  C  CA  . GLU F  1 50  ? 19.900  246.903 51.072 1.00 27.79 ?  49  GLU F CA  1 
ATOM   5970  C  C   . GLU F  1 50  ? 21.388  247.138 51.325 1.00 26.71 ?  49  GLU F C   1 
ATOM   5971  O  O   . GLU F  1 50  ? 22.202  246.997 50.411 1.00 31.64 ?  49  GLU F O   1 
ATOM   5972  C  CB  . GLU F  1 50  ? 19.201  248.245 50.825 1.00 29.74 ?  49  GLU F CB  1 
ATOM   5973  C  CG  . GLU F  1 50  ? 19.863  249.029 49.695 1.00 32.38 ?  49  GLU F CG  1 
ATOM   5974  C  CD  . GLU F  1 50  ? 19.022  250.196 49.191 1.00 38.48 ?  49  GLU F CD  1 
ATOM   5975  O  OE1 . GLU F  1 50  ? 18.046  250.589 49.878 1.00 36.12 ?  49  GLU F OE1 1 
ATOM   5976  O  OE2 . GLU F  1 50  ? 19.361  250.723 48.106 1.00 41.31 ?  49  GLU F OE2 1 
ATOM   5977  N  N   . PHE F  1 51  ? 21.762  247.579 52.523 1.00 27.61 ?  50  PHE F N   1 
ATOM   5978  C  CA  . PHE F  1 51  ? 23.129  248.029 52.752 1.00 28.23 ?  50  PHE F CA  1 
ATOM   5979  C  C   . PHE F  1 51  ? 23.915  247.041 53.594 1.00 28.80 ?  50  PHE F C   1 
ATOM   5980  O  O   . PHE F  1 51  ? 23.401  246.500 54.573 1.00 30.37 ?  50  PHE F O   1 
ATOM   5981  C  CB  . PHE F  1 51  ? 23.128  249.391 53.431 1.00 25.89 ?  50  PHE F CB  1 
ATOM   5982  C  CG  . PHE F  1 51  ? 22.322  250.402 52.694 1.00 32.31 ?  50  PHE F CG  1 
ATOM   5983  C  CD1 . PHE F  1 51  ? 22.686  250.784 51.422 1.00 32.68 ?  50  PHE F CD1 1 
ATOM   5984  C  CD2 . PHE F  1 51  ? 21.181  250.950 53.256 1.00 34.60 ?  50  PHE F CD2 1 
ATOM   5985  C  CE1 . PHE F  1 51  ? 21.936  251.723 50.731 1.00 37.99 ?  50  PHE F CE1 1 
ATOM   5986  C  CE2 . PHE F  1 51  ? 20.428  251.886 52.565 1.00 34.26 ?  50  PHE F CE2 1 
ATOM   5987  C  CZ  . PHE F  1 51  ? 20.802  252.266 51.309 1.00 33.63 ?  50  PHE F CZ  1 
ATOM   5988  N  N   . GLY F  1 52  ? 25.170  246.826 53.213 1.00 28.33 ?  51  GLY F N   1 
ATOM   5989  C  CA  . GLY F  1 52  ? 26.091  246.029 54.006 1.00 21.82 ?  51  GLY F CA  1 
ATOM   5990  C  C   . GLY F  1 52  ? 26.757  246.876 55.069 1.00 31.41 ?  51  GLY F C   1 
ATOM   5991  O  O   . GLY F  1 52  ? 27.979  246.825 55.268 1.00 29.38 ?  51  GLY F O   1 
ATOM   5992  N  N   . ASP F  1 53  ? 25.948  247.655 55.767 1.00 30.36 ?  52  ASP F N   1 
ATOM   5993  C  CA  . ASP F  1 53  ? 26.424  248.648 56.714 1.00 30.97 ?  52  ASP F CA  1 
ATOM   5994  C  C   . ASP F  1 53  ? 26.048  248.183 58.117 1.00 32.16 ?  52  ASP F C   1 
ATOM   5995  O  O   . ASP F  1 53  ? 24.871  248.207 58.493 1.00 31.78 ?  52  ASP F O   1 
ATOM   5996  C  CB  . ASP F  1 53  ? 25.818  250.005 56.385 1.00 33.18 ?  52  ASP F CB  1 
ATOM   5997  C  CG  . ASP F  1 53  ? 26.306  251.110 57.314 1.00 39.04 ?  52  ASP F CG  1 
ATOM   5998  O  OD1 . ASP F  1 53  ? 26.231  252.287 56.898 1.00 36.26 ?  52  ASP F OD1 1 
ATOM   5999  O  OD2 . ASP F  1 53  ? 26.780  250.800 58.436 1.00 33.74 ?  52  ASP F OD2 1 
ATOM   6000  N  N   . ASN F  1 54  ? 27.043  247.759 58.890 1.00 28.19 ?  53  ASN F N   1 
ATOM   6001  C  CA  . ASN F  1 54  ? 26.826  247.281 60.248 1.00 37.32 ?  53  ASN F CA  1 
ATOM   6002  C  C   . ASN F  1 54  ? 27.298  248.292 61.296 1.00 35.43 ?  53  ASN F C   1 
ATOM   6003  O  O   . ASN F  1 54  ? 27.468  247.936 62.459 1.00 32.75 ?  53  ASN F O   1 
ATOM   6004  C  CB  . ASN F  1 54  ? 27.522  245.929 60.444 1.00 32.39 ?  53  ASN F CB  1 
ATOM   6005  C  CG  . ASN F  1 54  ? 27.104  245.237 61.740 1.00 46.52 ?  53  ASN F CG  1 
ATOM   6006  O  OD1 . ASN F  1 54  ? 25.922  244.974 61.955 1.00 49.25 ?  53  ASN F OD1 1 
ATOM   6007  N  ND2 . ASN F  1 54  ? 28.074  244.952 62.615 1.00 41.57 ?  53  ASN F ND2 1 
ATOM   6008  N  N   . THR F  1 55  ? 27.487  249.557 60.911 1.00 32.49 ?  54  THR F N   1 
ATOM   6009  C  CA  . THR F  1 55  ? 28.075  250.526 61.838 1.00 33.84 ?  54  THR F CA  1 
ATOM   6010  C  C   . THR F  1 55  ? 27.179  250.813 63.036 1.00 34.83 ?  54  THR F C   1 
ATOM   6011  O  O   . THR F  1 55  ? 27.683  251.117 64.120 1.00 37.70 ?  54  THR F O   1 
ATOM   6012  C  CB  . THR F  1 55  ? 28.388  251.826 61.113 1.00 31.81 ?  54  THR F CB  1 
ATOM   6013  O  OG1 . THR F  1 55  ? 27.184  252.343 60.528 1.00 33.92 ?  54  THR F OG1 1 
ATOM   6014  C  CG2 . THR F  1 55  ? 29.431  251.579 60.023 1.00 31.60 ?  54  THR F CG2 1 
ATOM   6015  N  N   . ALA F  1 56  ? 25.866  250.739 62.875 1.00 34.59 ?  55  ALA F N   1 
ATOM   6016  C  CA  . ALA F  1 56  ? 24.957  250.868 64.004 1.00 39.43 ?  55  ALA F CA  1 
ATOM   6017  C  C   . ALA F  1 56  ? 24.228  249.553 64.263 1.00 38.33 ?  55  ALA F C   1 
ATOM   6018  O  O   . ALA F  1 56  ? 23.018  249.531 64.498 1.00 40.24 ?  55  ALA F O   1 
ATOM   6019  C  CB  . ALA F  1 56  ? 23.966  252.007 63.774 1.00 34.19 ?  55  ALA F CB  1 
ATOM   6020  N  N   . GLY F  1 57  ? 24.957  248.436 64.220 1.00 37.04 ?  56  GLY F N   1 
ATOM   6021  C  CA  . GLY F  1 57  ? 24.308  247.135 64.290 1.00 37.00 ?  56  GLY F CA  1 
ATOM   6022  C  C   . GLY F  1 57  ? 23.430  246.889 63.065 1.00 37.36 ?  56  GLY F C   1 
ATOM   6023  O  O   . GLY F  1 57  ? 23.611  247.486 62.000 1.00 32.45 ?  56  GLY F O   1 
ATOM   6024  N  N   . CYS F  1 58  ? 22.451  245.993 63.240 1.00 36.33 ?  57  CYS F N   1 
ATOM   6025  C  CA  . CYS F  1 58  ? 21.581  245.596 62.130 1.00 33.68 ?  57  CYS F CA  1 
ATOM   6026  C  C   . CYS F  1 58  ? 20.688  246.739 61.647 1.00 33.62 ?  57  CYS F C   1 
ATOM   6027  O  O   . CYS F  1 58  ? 20.205  246.697 60.512 1.00 31.78 ?  57  CYS F O   1 
ATOM   6028  C  CB  . CYS F  1 58  ? 20.737  244.389 62.551 1.00 33.18 ?  57  CYS F CB  1 
ATOM   6029  S  SG  . CYS F  1 58  ? 21.762  242.942 63.012 1.00 39.85 ?  57  CYS F SG  1 
ATOM   6030  N  N   . THR F  1 59  ? 20.488  247.765 62.477 1.00 32.31 ?  58  THR F N   1 
ATOM   6031  C  CA  . THR F  1 59  ? 19.644  248.900 62.106 1.00 32.84 ?  58  THR F CA  1 
ATOM   6032  C  C   . THR F  1 59  ? 20.149  249.603 60.859 1.00 32.86 ?  58  THR F C   1 
ATOM   6033  O  O   . THR F  1 59  ? 19.355  250.073 60.030 1.00 31.07 ?  58  THR F O   1 
ATOM   6034  C  CB  . THR F  1 59  ? 19.601  249.905 63.246 1.00 34.69 ?  58  THR F CB  1 
ATOM   6035  O  OG1 . THR F  1 59  ? 19.317  249.217 64.465 1.00 45.35 ?  58  THR F OG1 1 
ATOM   6036  C  CG2 . THR F  1 59  ? 18.561  250.966 62.958 1.00 40.42 ?  58  THR F CG2 1 
ATOM   6037  N  N   . SER F  1 60  ? 21.464  249.724 60.722 1.00 30.09 ?  59  SER F N   1 
ATOM   6038  C  CA  . SER F  1 60  ? 22.007  250.481 59.603 1.00 35.15 ?  59  SER F CA  1 
ATOM   6039  C  C   . SER F  1 60  ? 21.984  249.707 58.301 1.00 32.93 ?  59  SER F C   1 
ATOM   6040  O  O   . SER F  1 60  ? 22.446  250.243 57.287 1.00 31.25 ?  59  SER F O   1 
ATOM   6041  C  CB  . SER F  1 60  ? 23.436  250.938 59.906 1.00 35.17 ?  59  SER F CB  1 
ATOM   6042  O  OG  . SER F  1 60  ? 24.126  250.002 60.702 1.00 36.21 ?  59  SER F OG  1 
ATOM   6043  N  N   . ALA F  1 61  ? 21.476  248.471 58.297 1.00 30.59 ?  60  ALA F N   1 
ATOM   6044  C  CA  . ALA F  1 61  ? 21.334  247.731 57.046 1.00 28.38 ?  60  ALA F CA  1 
ATOM   6045  C  C   . ALA F  1 61  ? 20.235  248.295 56.155 1.00 29.27 ?  60  ALA F C   1 
ATOM   6046  O  O   . ALA F  1 61  ? 20.127  247.882 54.995 1.00 30.29 ?  60  ALA F O   1 
ATOM   6047  C  CB  . ALA F  1 61  ? 21.065  246.249 57.332 1.00 23.90 ?  60  ALA F CB  1 
ATOM   6048  N  N   . GLY F  1 62  ? 19.419  249.222 56.651 1.00 28.85 ?  61  GLY F N   1 
ATOM   6049  C  CA  . GLY F  1 62  ? 18.392  249.821 55.824 1.00 30.87 ?  61  GLY F CA  1 
ATOM   6050  C  C   . GLY F  1 62  ? 17.221  248.882 55.614 1.00 29.87 ?  61  GLY F C   1 
ATOM   6051  O  O   . GLY F  1 62  ? 17.069  247.888 56.326 1.00 30.36 ?  61  GLY F O   1 
ATOM   6052  N  N   . PRO F  1 63  ? 16.381  249.171 54.632 1.00 30.92 ?  62  PRO F N   1 
ATOM   6053  C  CA  . PRO F  1 63  ? 15.189  248.355 54.383 1.00 30.64 ?  62  PRO F CA  1 
ATOM   6054  C  C   . PRO F  1 63  ? 15.541  247.107 53.582 1.00 28.14 ?  62  PRO F C   1 
ATOM   6055  O  O   . PRO F  1 63  ? 16.703  246.851 53.276 1.00 27.88 ?  62  PRO F O   1 
ATOM   6056  C  CB  . PRO F  1 63  ? 14.305  249.297 53.570 1.00 28.58 ?  62  PRO F CB  1 
ATOM   6057  C  CG  . PRO F  1 63  ? 15.297  250.073 52.756 1.00 30.58 ?  62  PRO F CG  1 
ATOM   6058  C  CD  . PRO F  1 63  ? 16.517  250.255 53.648 1.00 30.23 ?  62  PRO F CD  1 
ATOM   6059  N  N   . HIS F  1 64  ? 14.507  246.331 53.239 1.00 28.52 ?  63  HIS F N   1 
ATOM   6060  C  CA  . HIS F  1 64  ? 14.704  245.180 52.373 1.00 28.14 ?  63  HIS F CA  1 
ATOM   6061  C  C   . HIS F  1 64  ? 15.280  245.635 51.038 1.00 28.87 ?  63  HIS F C   1 
ATOM   6062  O  O   . HIS F  1 64  ? 14.925  246.695 50.525 1.00 30.53 ?  63  HIS F O   1 
ATOM   6063  C  CB  . HIS F  1 64  ? 13.379  244.438 52.144 1.00 30.77 ?  63  HIS F CB  1 
ATOM   6064  C  CG  . HIS F  1 64  ? 12.797  243.827 53.384 1.00 29.27 ?  63  HIS F CG  1 
ATOM   6065  N  ND1 . HIS F  1 64  ? 11.605  243.137 53.375 1.00 28.02 ?  63  HIS F ND1 1 
ATOM   6066  C  CD2 . HIS F  1 64  ? 13.242  243.791 54.664 1.00 29.93 ?  63  HIS F CD2 1 
ATOM   6067  C  CE1 . HIS F  1 64  ? 11.326  242.718 54.600 1.00 28.84 ?  63  HIS F CE1 1 
ATOM   6068  N  NE2 . HIS F  1 64  ? 12.311  243.089 55.399 1.00 29.32 ?  63  HIS F NE2 1 
ATOM   6069  N  N   . PHE F  1 65  ? 16.203  244.847 50.505 1.00 28.15 ?  64  PHE F N   1 
ATOM   6070  C  CA  . PHE F  1 65  ? 16.786  245.105 49.195 1.00 28.12 ?  64  PHE F CA  1 
ATOM   6071  C  C   . PHE F  1 65  ? 15.686  245.085 48.146 1.00 29.02 ?  64  PHE F C   1 
ATOM   6072  O  O   . PHE F  1 65  ? 15.033  244.058 47.935 1.00 27.45 ?  64  PHE F O   1 
ATOM   6073  C  CB  . PHE F  1 65  ? 17.850  244.052 48.893 1.00 29.40 ?  64  PHE F CB  1 
ATOM   6074  C  CG  . PHE F  1 65  ? 18.553  244.254 47.578 1.00 30.66 ?  64  PHE F CG  1 
ATOM   6075  C  CD1 . PHE F  1 65  ? 18.845  245.534 47.116 1.00 31.43 ?  64  PHE F CD1 1 
ATOM   6076  C  CD2 . PHE F  1 65  ? 18.921  243.163 46.806 1.00 32.55 ?  64  PHE F CD2 1 
ATOM   6077  C  CE1 . PHE F  1 65  ? 19.495  245.713 45.891 1.00 32.06 ?  64  PHE F CE1 1 
ATOM   6078  C  CE2 . PHE F  1 65  ? 19.570  243.330 45.577 1.00 31.77 ?  64  PHE F CE2 1 
ATOM   6079  C  CZ  . PHE F  1 65  ? 19.859  244.609 45.125 1.00 32.26 ?  64  PHE F CZ  1 
ATOM   6080  N  N   . ASN F  1 66  ? 15.468  246.222 47.511 1.00 30.46 ?  65  ASN F N   1 
ATOM   6081  C  CA  . ASN F  1 66  ? 14.290  246.413 46.682 1.00 27.71 ?  65  ASN F CA  1 
ATOM   6082  C  C   . ASN F  1 66  ? 14.625  247.251 45.451 1.00 32.03 ?  65  ASN F C   1 
ATOM   6083  O  O   . ASN F  1 66  ? 14.055  248.330 45.268 1.00 31.31 ?  65  ASN F O   1 
ATOM   6084  C  CB  . ASN F  1 66  ? 13.197  247.091 47.514 1.00 27.48 ?  65  ASN F CB  1 
ATOM   6085  C  CG  . ASN F  1 66  ? 11.850  247.109 46.808 1.00 33.08 ?  65  ASN F CG  1 
ATOM   6086  O  OD1 . ASN F  1 66  ? 11.605  246.342 45.865 1.00 30.30 ?  65  ASN F OD1 1 
ATOM   6087  N  ND2 . ASN F  1 66  ? 10.979  248.009 47.243 1.00 25.53 ?  65  ASN F ND2 1 
ATOM   6088  N  N   . PRO F  1 67  ? 15.529  246.802 44.580 1.00 32.34 ?  66  PRO F N   1 
ATOM   6089  C  CA  . PRO F  1 67  ? 15.921  247.659 43.450 1.00 32.48 ?  66  PRO F CA  1 
ATOM   6090  C  C   . PRO F  1 67  ? 14.787  247.939 42.487 1.00 39.64 ?  66  PRO F C   1 
ATOM   6091  O  O   . PRO F  1 67  ? 14.867  248.914 41.732 1.00 43.23 ?  66  PRO F O   1 
ATOM   6092  C  CB  . PRO F  1 67  ? 17.032  246.861 42.762 1.00 32.59 ?  66  PRO F CB  1 
ATOM   6093  C  CG  . PRO F  1 67  ? 16.732  245.427 43.108 1.00 30.77 ?  66  PRO F CG  1 
ATOM   6094  C  CD  . PRO F  1 67  ? 16.182  245.481 44.530 1.00 27.97 ?  66  PRO F CD  1 
ATOM   6095  N  N   . LEU F  1 68  ? 13.738  247.120 42.475 1.00 32.28 ?  67  LEU F N   1 
ATOM   6096  C  CA  . LEU F  1 68  ? 12.631  247.302 41.544 1.00 35.37 ?  67  LEU F CA  1 
ATOM   6097  C  C   . LEU F  1 68  ? 11.466  248.076 42.151 1.00 33.96 ?  67  LEU F C   1 
ATOM   6098  O  O   . LEU F  1 68  ? 10.406  248.170 41.524 1.00 36.84 ?  67  LEU F O   1 
ATOM   6099  C  CB  . LEU F  1 68  ? 12.146  245.948 41.033 1.00 35.34 ?  67  LEU F CB  1 
ATOM   6100  C  CG  . LEU F  1 68  ? 13.159  245.158 40.218 1.00 38.56 ?  67  LEU F CG  1 
ATOM   6101  C  CD1 . LEU F  1 68  ? 12.549  243.823 39.774 1.00 43.30 ?  67  LEU F CD1 1 
ATOM   6102  C  CD2 . LEU F  1 68  ? 13.614  245.991 39.012 1.00 38.40 ?  67  LEU F CD2 1 
ATOM   6103  N  N   . SER F  1 69  ? 11.629  248.612 43.357 1.00 31.44 ?  68  SER F N   1 
ATOM   6104  C  CA  . SER F  1 69  ? 10.575  249.364 44.050 1.00 31.67 ?  68  SER F CA  1 
ATOM   6105  C  C   . SER F  1 69  ? 9.222   248.643 44.025 1.00 32.90 ?  68  SER F C   1 
ATOM   6106  O  O   . SER F  1 69  ? 8.190   249.223 43.690 1.00 36.49 ?  68  SER F O   1 
ATOM   6107  C  CB  . SER F  1 69  ? 10.448  250.764 43.456 1.00 38.60 ?  68  SER F CB  1 
ATOM   6108  O  OG  . SER F  1 69  ? 11.711  251.390 43.428 1.00 36.55 ?  68  SER F OG  1 
ATOM   6109  N  N   . ARG F  1 70  ? 9.229   247.360 44.386 1.00 32.68 ?  69  ARG F N   1 
ATOM   6110  C  CA  . ARG F  1 70  ? 7.990   246.613 44.565 1.00 30.03 ?  69  ARG F CA  1 
ATOM   6111  C  C   . ARG F  1 70  ? 7.524   246.679 46.017 1.00 29.54 ?  69  ARG F C   1 
ATOM   6112  O  O   . ARG F  1 70  ? 8.232   247.159 46.906 1.00 32.42 ?  69  ARG F O   1 
ATOM   6113  C  CB  . ARG F  1 70  ? 8.178   245.153 44.157 1.00 32.96 ?  69  ARG F CB  1 
ATOM   6114  C  CG  . ARG F  1 70  ? 8.847   244.948 42.797 1.00 35.04 ?  69  ARG F CG  1 
ATOM   6115  C  CD  . ARG F  1 70  ? 7.871   245.131 41.662 1.00 38.66 ?  69  ARG F CD  1 
ATOM   6116  N  NE  . ARG F  1 70  ? 8.521   244.929 40.373 1.00 45.07 ?  69  ARG F NE  1 
ATOM   6117  C  CZ  . ARG F  1 70  ? 8.606   245.856 39.425 1.00 49.48 ?  69  ARG F CZ  1 
ATOM   6118  N  NH1 . ARG F  1 70  ? 8.037   247.045 39.566 1.00 47.81 ?  69  ARG F NH1 1 
ATOM   6119  N  NH2 . ARG F  1 70  ? 9.283   245.588 38.309 1.00 45.01 ?  69  ARG F NH2 1 
ATOM   6120  N  N   . LYS F  1 71  ? 6.317   246.176 46.257 1.00 31.86 ?  70  LYS F N   1 
ATOM   6121  C  CA  . LYS F  1 71  ? 5.851   245.937 47.620 1.00 31.71 ?  70  LYS F CA  1 
ATOM   6122  C  C   . LYS F  1 71  ? 6.356   244.595 48.155 1.00 34.53 ?  70  LYS F C   1 
ATOM   6123  O  O   . LYS F  1 71  ? 6.646   243.655 47.403 1.00 30.13 ?  70  LYS F O   1 
ATOM   6124  C  CB  . LYS F  1 71  ? 4.321   245.958 47.689 1.00 34.40 ?  70  LYS F CB  1 
ATOM   6125  C  CG  . LYS F  1 71  ? 3.694   247.323 47.363 1.00 42.95 ?  70  LYS F CG  1 
ATOM   6126  C  CD  . LYS F  1 71  ? 2.216   247.208 46.992 1.00 52.96 ?  70  LYS F CD  1 
ATOM   6127  C  CE  . LYS F  1 71  ? 1.971   246.020 46.058 1.00 62.68 ?  70  LYS F CE  1 
ATOM   6128  N  NZ  . LYS F  1 71  ? 1.717   246.432 44.639 1.00 61.81 ?  70  LYS F NZ  1 
ATOM   6129  N  N   . HIS F  1 72  ? 6.447   244.517 49.475 1.00 28.76 ?  71  HIS F N   1 
ATOM   6130  C  CA  . HIS F  1 72  ? 6.910   243.306 50.139 1.00 31.40 ?  71  HIS F CA  1 
ATOM   6131  C  C   . HIS F  1 72  ? 5.991   242.134 49.821 1.00 30.52 ?  71  HIS F C   1 
ATOM   6132  O  O   . HIS F  1 72  ? 4.774   242.287 49.727 1.00 28.63 ?  71  HIS F O   1 
ATOM   6133  C  CB  . HIS F  1 72  ? 6.978   243.526 51.649 1.00 28.90 ?  71  HIS F CB  1 
ATOM   6134  C  CG  . HIS F  1 72  ? 7.337   242.296 52.421 1.00 28.70 ?  71  HIS F CG  1 
ATOM   6135  N  ND1 . HIS F  1 72  ? 8.633   241.847 52.537 1.00 25.95 ?  71  HIS F ND1 1 
ATOM   6136  C  CD2 . HIS F  1 72  ? 6.574   241.432 53.129 1.00 23.24 ?  71  HIS F CD2 1 
ATOM   6137  C  CE1 . HIS F  1 72  ? 8.651   240.744 53.264 1.00 28.90 ?  71  HIS F CE1 1 
ATOM   6138  N  NE2 . HIS F  1 72  ? 7.411   240.464 53.621 1.00 28.56 ?  71  HIS F NE2 1 
ATOM   6139  N  N   . GLY F  1 73  ? 6.584   240.956 49.647 1.00 29.52 ?  72  GLY F N   1 
ATOM   6140  C  CA  . GLY F  1 73  ? 5.825   239.757 49.360 1.00 25.80 ?  72  GLY F CA  1 
ATOM   6141  C  C   . GLY F  1 73  ? 6.596   238.570 49.890 1.00 28.83 ?  72  GLY F C   1 
ATOM   6142  O  O   . GLY F  1 73  ? 7.628   238.720 50.547 1.00 30.79 ?  72  GLY F O   1 
ATOM   6143  N  N   . GLY F  1 74  ? 6.074   237.383 49.623 1.00 26.52 ?  73  GLY F N   1 
ATOM   6144  C  CA  . GLY F  1 74  ? 6.804   236.175 49.922 1.00 26.84 ?  73  GLY F CA  1 
ATOM   6145  C  C   . GLY F  1 74  ? 7.621   235.771 48.708 1.00 29.39 ?  73  GLY F C   1 
ATOM   6146  O  O   . GLY F  1 74  ? 7.423   236.272 47.599 1.00 30.59 ?  73  GLY F O   1 
ATOM   6147  N  N   . PRO F  1 75  ? 8.553   234.846 48.906 1.00 31.19 ?  74  PRO F N   1 
ATOM   6148  C  CA  . PRO F  1 75  ? 9.474   234.487 47.816 1.00 29.03 ?  74  PRO F CA  1 
ATOM   6149  C  C   . PRO F  1 75  ? 8.785   233.882 46.605 1.00 33.28 ?  74  PRO F C   1 
ATOM   6150  O  O   . PRO F  1 75  ? 9.361   233.903 45.516 1.00 31.66 ?  74  PRO F O   1 
ATOM   6151  C  CB  . PRO F  1 75  ? 10.423  233.466 48.474 1.00 26.80 ?  74  PRO F CB  1 
ATOM   6152  C  CG  . PRO F  1 75  ? 9.736   233.029 49.745 1.00 29.65 ?  74  PRO F CG  1 
ATOM   6153  C  CD  . PRO F  1 75  ? 8.902   234.199 50.185 1.00 26.64 ?  74  PRO F CD  1 
ATOM   6154  N  N   . LYS F  1 76  ? 7.595   233.315 46.758 1.00 29.53 ?  75  LYS F N   1 
ATOM   6155  C  CA  . LYS F  1 76  ? 6.886   232.762 45.612 1.00 33.29 ?  75  LYS F CA  1 
ATOM   6156  C  C   . LYS F  1 76  ? 6.098   233.812 44.856 1.00 31.52 ?  75  LYS F C   1 
ATOM   6157  O  O   . LYS F  1 76  ? 5.547   233.500 43.803 1.00 32.77 ?  75  LYS F O   1 
ATOM   6158  C  CB  . LYS F  1 76  ? 5.920   231.653 46.050 1.00 31.08 ?  75  LYS F CB  1 
ATOM   6159  C  CG  . LYS F  1 76  ? 6.562   230.503 46.791 1.00 37.63 ?  75  LYS F CG  1 
ATOM   6160  C  CD  . LYS F  1 76  ? 5.527   229.763 47.635 1.00 38.23 ?  75  LYS F CD  1 
ATOM   6161  C  CE  . LYS F  1 76  ? 4.995   228.519 46.905 1.00 45.67 ?  75  LYS F CE  1 
ATOM   6162  N  NZ  . LYS F  1 76  ? 3.755   227.954 47.539 1.00 40.44 ?  75  LYS F NZ  1 
ATOM   6163  N  N   . ASP F  1 77  ? 5.989   235.029 45.376 1.00 29.66 ?  76  ASP F N   1 
ATOM   6164  C  CA  . ASP F  1 77  ? 5.179   236.035 44.711 1.00 31.47 ?  76  ASP F CA  1 
ATOM   6165  C  C   . ASP F  1 77  ? 5.948   236.698 43.581 1.00 38.57 ?  76  ASP F C   1 
ATOM   6166  O  O   . ASP F  1 77  ? 7.176   236.791 43.606 1.00 33.29 ?  76  ASP F O   1 
ATOM   6167  C  CB  . ASP F  1 77  ? 4.714   237.097 45.698 1.00 32.71 ?  76  ASP F CB  1 
ATOM   6168  C  CG  . ASP F  1 77  ? 3.773   236.534 46.729 1.00 39.93 ?  76  ASP F CG  1 
ATOM   6169  O  OD1 . ASP F  1 77  ? 2.944   235.674 46.353 1.00 39.50 ?  76  ASP F OD1 1 
ATOM   6170  O  OD2 . ASP F  1 77  ? 3.884   236.915 47.907 1.00 38.06 ?  76  ASP F OD2 1 
ATOM   6171  N  N   . GLU F  1 78  ? 5.201   237.170 42.580 1.00 36.54 ?  77  GLU F N   1 
ATOM   6172  C  CA  . GLU F  1 78  ? 5.821   237.988 41.549 1.00 39.67 ?  77  GLU F CA  1 
ATOM   6173  C  C   . GLU F  1 78  ? 6.062   239.395 42.073 1.00 33.66 ?  77  GLU F C   1 
ATOM   6174  O  O   . GLU F  1 78  ? 7.131   239.965 41.844 1.00 38.39 ?  77  GLU F O   1 
ATOM   6175  C  CB  . GLU F  1 78  ? 4.959   238.009 40.282 1.00 42.40 ?  77  GLU F CB  1 
ATOM   6176  C  CG  . GLU F  1 78  ? 4.948   239.359 39.581 1.00 56.55 ?  77  GLU F CG  1 
ATOM   6177  C  CD  . GLU F  1 78  ? 4.528   239.268 38.116 1.00 71.49 ?  77  GLU F CD  1 
ATOM   6178  O  OE1 . GLU F  1 78  ? 3.589   238.497 37.800 1.00 72.61 ?  77  GLU F OE1 1 
ATOM   6179  O  OE2 . GLU F  1 78  ? 5.144   239.977 37.284 1.00 78.27 ?  77  GLU F OE2 1 
ATOM   6180  N  N   . GLU F  1 79  ? 5.105   239.938 42.827 1.00 30.95 ?  78  GLU F N   1 
ATOM   6181  C  CA  . GLU F  1 79  ? 5.279   241.198 43.547 1.00 29.79 ?  78  GLU F CA  1 
ATOM   6182  C  C   . GLU F  1 79  ? 6.030   240.905 44.844 1.00 30.74 ?  78  GLU F C   1 
ATOM   6183  O  O   . GLU F  1 79  ? 5.453   240.420 45.826 1.00 30.96 ?  78  GLU F O   1 
ATOM   6184  C  CB  . GLU F  1 79  ? 3.927   241.841 43.832 1.00 27.83 ?  78  GLU F CB  1 
ATOM   6185  C  CG  . GLU F  1 79  ? 3.988   243.201 44.521 1.00 33.60 ?  78  GLU F CG  1 
ATOM   6186  C  CD  . GLU F  1 79  ? 4.412   244.311 43.558 1.00 43.78 ?  78  GLU F CD  1 
ATOM   6187  O  OE1 . GLU F  1 79  ? 4.522   245.485 43.985 1.00 38.87 ?  78  GLU F OE1 1 
ATOM   6188  O  OE2 . GLU F  1 79  ? 4.634   243.998 42.366 1.00 48.64 ?  78  GLU F OE2 1 
ATOM   6189  N  N   . ARG F  1 80  ? 7.315   241.233 44.870 1.00 31.10 ?  79  ARG F N   1 
ATOM   6190  C  CA  . ARG F  1 80  ? 8.124   241.037 46.062 1.00 31.64 ?  79  ARG F CA  1 
ATOM   6191  C  C   . ARG F  1 80  ? 9.355   241.908 45.937 1.00 28.98 ?  79  ARG F C   1 
ATOM   6192  O  O   . ARG F  1 80  ? 9.758   242.284 44.834 1.00 31.67 ?  79  ARG F O   1 
ATOM   6193  C  CB  . ARG F  1 80  ? 8.534   239.573 46.222 1.00 26.79 ?  79  ARG F CB  1 
ATOM   6194  C  CG  . ARG F  1 80  ? 9.402   239.098 45.057 1.00 27.70 ?  79  ARG F CG  1 
ATOM   6195  C  CD  . ARG F  1 80  ? 9.958   237.720 45.353 1.00 24.60 ?  79  ARG F CD  1 
ATOM   6196  N  NE  . ARG F  1 80  ? 11.324  237.789 45.874 1.00 28.64 ?  79  ARG F NE  1 
ATOM   6197  C  CZ  . ARG F  1 80  ? 12.141  236.747 45.950 1.00 28.59 ?  79  ARG F CZ  1 
ATOM   6198  N  NH1 . ARG F  1 80  ? 11.758  235.536 45.568 1.00 24.57 ?  79  ARG F NH1 1 
ATOM   6199  N  NH2 . ARG F  1 80  ? 13.375  236.925 46.405 1.00 26.66 ?  79  ARG F NH2 1 
ATOM   6200  N  N   . HIS F  1 81  ? 9.954   242.213 47.079 1.00 24.84 ?  80  HIS F N   1 
ATOM   6201  C  CA  . HIS F  1 81  ? 11.303  242.751 47.081 1.00 28.48 ?  80  HIS F CA  1 
ATOM   6202  C  C   . HIS F  1 81  ? 12.269  241.664 46.633 1.00 26.26 ?  80  HIS F C   1 
ATOM   6203  O  O   . HIS F  1 81  ? 12.012  240.473 46.817 1.00 23.34 ?  80  HIS F O   1 
ATOM   6204  C  CB  . HIS F  1 81  ? 11.687  243.217 48.479 1.00 24.00 ?  80  HIS F CB  1 
ATOM   6205  C  CG  . HIS F  1 81  ? 10.752  244.222 49.065 1.00 27.25 ?  80  HIS F CG  1 
ATOM   6206  N  ND1 . HIS F  1 81  ? 10.592  244.380 50.425 1.00 24.24 ?  80  HIS F ND1 1 
ATOM   6207  C  CD2 . HIS F  1 81  ? 9.957   245.151 48.482 1.00 29.90 ?  80  HIS F CD2 1 
ATOM   6208  C  CE1 . HIS F  1 81  ? 9.722   245.349 50.655 1.00 28.43 ?  80  HIS F CE1 1 
ATOM   6209  N  NE2 . HIS F  1 81  ? 9.325   245.835 49.491 1.00 28.36 ?  80  HIS F NE2 1 
ATOM   6210  N  N   . VAL F  1 82  ? 13.395  242.077 46.039 1.00 23.50 ?  81  VAL F N   1 
ATOM   6211  C  CA  . VAL F  1 82  ? 14.434  241.096 45.733 1.00 24.46 ?  81  VAL F CA  1 
ATOM   6212  C  C   . VAL F  1 82  ? 14.885  240.387 47.004 1.00 27.03 ?  81  VAL F C   1 
ATOM   6213  O  O   . VAL F  1 82  ? 15.105  239.173 47.008 1.00 25.13 ?  81  VAL F O   1 
ATOM   6214  C  CB  . VAL F  1 82  ? 15.616  241.760 45.002 1.00 26.56 ?  81  VAL F CB  1 
ATOM   6215  C  CG1 . VAL F  1 82  ? 16.821  240.837 45.022 1.00 24.72 ?  81  VAL F CG1 1 
ATOM   6216  C  CG2 . VAL F  1 82  ? 15.237  242.075 43.524 1.00 22.54 ?  81  VAL F CG2 1 
ATOM   6217  N  N   . GLY F  1 83  ? 14.989  241.114 48.110 1.00 24.03 ?  82  GLY F N   1 
ATOM   6218  C  CA  . GLY F  1 83  ? 15.493  240.489 49.324 1.00 24.65 ?  82  GLY F CA  1 
ATOM   6219  C  C   . GLY F  1 83  ? 14.508  239.642 50.106 1.00 27.56 ?  82  GLY F C   1 
ATOM   6220  O  O   . GLY F  1 83  ? 14.858  239.170 51.192 1.00 27.34 ?  82  GLY F O   1 
ATOM   6221  N  N   . ASP F  1 84  ? 13.301  239.407 49.589 1.00 24.68 ?  83  ASP F N   1 
ATOM   6222  C  CA  . ASP F  1 84  ? 12.239  238.726 50.338 1.00 25.38 ?  83  ASP F CA  1 
ATOM   6223  C  C   . ASP F  1 84  ? 12.441  237.221 50.269 1.00 28.93 ?  83  ASP F C   1 
ATOM   6224  O  O   . ASP F  1 84  ? 11.890  236.545 49.402 1.00 27.35 ?  83  ASP F O   1 
ATOM   6225  C  CB  . ASP F  1 84  ? 10.880  239.095 49.764 1.00 26.25 ?  83  ASP F CB  1 
ATOM   6226  C  CG  . ASP F  1 84  ? 10.453  240.465 50.162 1.00 28.18 ?  83  ASP F CG  1 
ATOM   6227  O  OD1 . ASP F  1 84  ? 11.164  241.060 51.004 1.00 26.37 ?  83  ASP F OD1 1 
ATOM   6228  O  OD2 . ASP F  1 84  ? 9.427   240.953 49.644 1.00 26.95 ?  83  ASP F OD2 1 
ATOM   6229  N  N   . LEU F  1 85  ? 13.223  236.672 51.188 1.00 23.61 ?  84  LEU F N   1 
ATOM   6230  C  CA  . LEU F  1 85  ? 13.409  235.231 51.220 1.00 21.23 ?  84  LEU F CA  1 
ATOM   6231  C  C   . LEU F  1 85  ? 12.395  234.521 52.122 1.00 22.27 ?  84  LEU F C   1 
ATOM   6232  O  O   . LEU F  1 85  ? 12.502  233.308 52.328 1.00 28.78 ?  84  LEU F O   1 
ATOM   6233  C  CB  . LEU F  1 85  ? 14.847  234.899 51.644 1.00 20.34 ?  84  LEU F CB  1 
ATOM   6234  C  CG  . LEU F  1 85  ? 15.908  235.445 50.677 1.00 26.56 ?  84  LEU F CG  1 
ATOM   6235  C  CD1 . LEU F  1 85  ? 17.316  235.092 51.112 1.00 21.62 ?  84  LEU F CD1 1 
ATOM   6236  C  CD2 . LEU F  1 85  ? 15.646  234.966 49.237 1.00 24.17 ?  84  LEU F CD2 1 
ATOM   6237  N  N   . GLY F  1 86  ? 11.408  235.236 52.653 1.00 20.56 ?  85  GLY F N   1 
ATOM   6238  C  CA  . GLY F  1 86  ? 10.328  234.578 53.367 1.00 20.34 ?  85  GLY F CA  1 
ATOM   6239  C  C   . GLY F  1 86  ? 10.698  234.246 54.799 1.00 23.82 ?  85  GLY F C   1 
ATOM   6240  O  O   . GLY F  1 86  ? 11.301  235.079 55.482 1.00 25.61 ?  85  GLY F O   1 
ATOM   6241  N  N   . ASN F  1 87  ? 10.350  233.051 55.263 1.00 20.43 ?  86  ASN F N   1 
ATOM   6242  C  CA  . ASN F  1 87  ? 10.592  232.650 56.643 1.00 24.93 ?  86  ASN F CA  1 
ATOM   6243  C  C   . ASN F  1 87  ? 11.613  231.519 56.698 1.00 22.38 ?  86  ASN F C   1 
ATOM   6244  O  O   . ASN F  1 87  ? 11.740  230.727 55.758 1.00 24.45 ?  86  ASN F O   1 
ATOM   6245  C  CB  . ASN F  1 87  ? 9.286   232.194 57.310 1.00 26.09 ?  86  ASN F CB  1 
ATOM   6246  C  CG  . ASN F  1 87  ? 8.370   233.345 57.650 1.00 30.12 ?  86  ASN F CG  1 
ATOM   6247  O  OD1 . ASN F  1 87  ? 8.753   234.264 58.377 1.00 26.74 ?  86  ASN F OD1 1 
ATOM   6248  N  ND2 . ASN F  1 87  ? 7.153   233.320 57.111 1.00 23.14 ?  86  ASN F ND2 1 
ATOM   6249  N  N   . VAL F  1 88  ? 12.328  231.430 57.811 1.00 26.42 ?  87  VAL F N   1 
ATOM   6250  C  CA  . VAL F  1 88  ? 13.028  230.201 58.165 1.00 22.80 ?  87  VAL F CA  1 
ATOM   6251  C  C   . VAL F  1 88  ? 12.418  229.703 59.469 1.00 27.76 ?  87  VAL F C   1 
ATOM   6252  O  O   . VAL F  1 88  ? 11.868  230.479 60.252 1.00 28.01 ?  87  VAL F O   1 
ATOM   6253  C  CB  . VAL F  1 88  ? 14.546  230.395 58.304 1.00 20.53 ?  87  VAL F CB  1 
ATOM   6254  C  CG1 . VAL F  1 88  ? 15.162  230.803 56.964 1.00 23.80 ?  87  VAL F CG1 1 
ATOM   6255  C  CG2 . VAL F  1 88  ? 14.845  231.401 59.392 1.00 22.61 ?  87  VAL F CG2 1 
ATOM   6256  N  N   . THR F  1 89  ? 12.528  228.402 59.712 1.00 20.34 ?  88  THR F N   1 
ATOM   6257  C  CA  . THR F  1 89  ? 11.849  227.767 60.837 1.00 23.33 ?  88  THR F CA  1 
ATOM   6258  C  C   . THR F  1 89  ? 12.871  227.226 61.823 1.00 26.42 ?  88  THR F C   1 
ATOM   6259  O  O   . THR F  1 89  ? 13.742  226.437 61.440 1.00 27.90 ?  88  THR F O   1 
ATOM   6260  C  CB  . THR F  1 89  ? 10.956  226.612 60.378 1.00 28.23 ?  88  THR F CB  1 
ATOM   6261  O  OG1 . THR F  1 89  ? 9.892   227.125 59.584 1.00 25.17 ?  88  THR F OG1 1 
ATOM   6262  C  CG2 . THR F  1 89  ? 10.334  225.886 61.590 1.00 26.14 ?  88  THR F CG2 1 
ATOM   6263  N  N   . ALA F  1 90  ? 12.753  227.630 63.087 1.00 22.97 ?  89  ALA F N   1 
ATOM   6264  C  CA  . ALA F  1 90  ? 13.598  227.113 64.154 1.00 26.44 ?  89  ALA F CA  1 
ATOM   6265  C  C   . ALA F  1 90  ? 12.880  225.960 64.848 1.00 29.72 ?  89  ALA F C   1 
ATOM   6266  O  O   . ALA F  1 90  ? 11.686  226.055 65.135 1.00 27.78 ?  89  ALA F O   1 
ATOM   6267  C  CB  . ALA F  1 90  ? 13.933  228.205 65.177 1.00 23.54 ?  89  ALA F CB  1 
ATOM   6268  N  N   . ASP F  1 91  ? 13.602  224.868 65.104 1.00 29.10 ?  90  ASP F N   1 
ATOM   6269  C  CA  . ASP F  1 91  ? 13.009  223.723 65.788 1.00 27.82 ?  90  ASP F CA  1 
ATOM   6270  C  C   . ASP F  1 91  ? 12.914  224.014 67.291 1.00 30.06 ?  90  ASP F C   1 
ATOM   6271  O  O   . ASP F  1 91  ? 13.241  225.110 67.764 1.00 28.42 ?  90  ASP F O   1 
ATOM   6272  C  CB  . ASP F  1 91  ? 13.784  222.441 65.469 1.00 23.31 ?  90  ASP F CB  1 
ATOM   6273  C  CG  . ASP F  1 91  ? 15.232  222.452 65.980 1.00 28.80 ?  90  ASP F CG  1 
ATOM   6274  O  OD1 . ASP F  1 91  ? 15.566  223.198 66.933 1.00 30.05 ?  90  ASP F OD1 1 
ATOM   6275  O  OD2 . ASP F  1 91  ? 16.057  221.684 65.421 1.00 34.11 ?  90  ASP F OD2 1 
ATOM   6276  N  N   . LYS F  1 92  ? 12.475  223.017 68.071 1.00 30.92 ?  91  LYS F N   1 
ATOM   6277  C  CA  . LYS F  1 92  ? 12.261  223.245 69.495 1.00 31.36 ?  91  LYS F CA  1 
ATOM   6278  C  C   . LYS F  1 92  ? 13.560  223.509 70.228 1.00 28.18 ?  91  LYS F C   1 
ATOM   6279  O  O   . LYS F  1 92  ? 13.524  224.023 71.349 1.00 33.55 ?  91  LYS F O   1 
ATOM   6280  C  CB  . LYS F  1 92  ? 11.548  222.052 70.133 1.00 38.96 ?  91  LYS F CB  1 
ATOM   6281  C  CG  . LYS F  1 92  ? 12.342  220.767 70.033 1.00 43.17 ?  91  LYS F CG  1 
ATOM   6282  C  CD  . LYS F  1 92  ? 11.655  219.612 70.740 1.00 49.25 ?  91  LYS F CD  1 
ATOM   6283  C  CE  . LYS F  1 92  ? 11.919  218.321 69.989 1.00 49.88 ?  91  LYS F CE  1 
ATOM   6284  N  NZ  . LYS F  1 92  ? 13.232  217.724 70.372 1.00 60.84 ?  91  LYS F NZ  1 
ATOM   6285  N  N   . ASP F  1 93  ? 14.703  223.144 69.640 1.00 34.15 ?  92  ASP F N   1 
ATOM   6286  C  CA  . ASP F  1 93  ? 15.988  223.492 70.243 1.00 32.94 ?  92  ASP F CA  1 
ATOM   6287  C  C   . ASP F  1 93  ? 16.458  224.884 69.850 1.00 32.92 ?  92  ASP F C   1 
ATOM   6288  O  O   . ASP F  1 93  ? 17.559  225.293 70.248 1.00 28.38 ?  92  ASP F O   1 
ATOM   6289  C  CB  . ASP F  1 93  ? 17.058  222.474 69.851 1.00 35.26 ?  92  ASP F CB  1 
ATOM   6290  C  CG  . ASP F  1 93  ? 16.732  221.070 70.325 1.00 45.32 ?  92  ASP F CG  1 
ATOM   6291  O  OD1 . ASP F  1 93  ? 16.325  220.917 71.507 1.00 40.77 ?  92  ASP F OD1 1 
ATOM   6292  O  OD2 . ASP F  1 93  ? 16.941  220.123 69.530 1.00 46.13 ?  92  ASP F OD2 1 
ATOM   6293  N  N   . GLY F  1 94  ? 15.652  225.616 69.079 1.00 33.33 ?  93  GLY F N   1 
ATOM   6294  C  CA  . GLY F  1 94  ? 16.048  226.928 68.604 1.00 32.40 ?  93  GLY F CA  1 
ATOM   6295  C  C   . GLY F  1 94  ? 16.958  226.924 67.390 1.00 31.87 ?  93  GLY F C   1 
ATOM   6296  O  O   . GLY F  1 94  ? 17.633  227.924 67.136 1.00 28.84 ?  93  GLY F O   1 
ATOM   6297  N  N   . VAL F  1 95  ? 16.995  225.837 66.621 1.00 31.30 ?  94  VAL F N   1 
ATOM   6298  C  CA  . VAL F  1 95  ? 17.904  225.708 65.486 1.00 25.53 ?  94  VAL F CA  1 
ATOM   6299  C  C   . VAL F  1 95  ? 17.092  225.792 64.201 1.00 30.84 ?  94  VAL F C   1 
ATOM   6300  O  O   . VAL F  1 95  ? 16.161  225.005 63.995 1.00 28.12 ?  94  VAL F O   1 
ATOM   6301  C  CB  . VAL F  1 95  ? 18.694  224.392 65.545 1.00 31.86 ?  94  VAL F CB  1 
ATOM   6302  C  CG1 . VAL F  1 95  ? 19.593  224.256 64.310 1.00 33.80 ?  94  VAL F CG1 1 
ATOM   6303  C  CG2 . VAL F  1 95  ? 19.515  224.348 66.826 1.00 27.70 ?  94  VAL F CG2 1 
ATOM   6304  N  N   . ALA F  1 96  ? 17.463  226.724 63.332 1.00 25.41 ?  95  ALA F N   1 
ATOM   6305  C  CA  . ALA F  1 96  ? 16.920  226.805 61.981 1.00 27.25 ?  95  ALA F CA  1 
ATOM   6306  C  C   . ALA F  1 96  ? 17.941  226.201 61.024 1.00 31.71 ?  95  ALA F C   1 
ATOM   6307  O  O   . ALA F  1 96  ? 18.993  226.799 60.772 1.00 28.91 ?  95  ALA F O   1 
ATOM   6308  C  CB  . ALA F  1 96  ? 16.598  228.253 61.605 1.00 22.94 ?  95  ALA F CB  1 
ATOM   6309  N  N   . ASP F  1 97  ? 17.648  225.007 60.509 1.00 29.25 ?  96  ASP F N   1 
ATOM   6310  C  CA  . ASP F  1 97  ? 18.475  224.403 59.464 1.00 30.11 ?  96  ASP F CA  1 
ATOM   6311  C  C   . ASP F  1 97  ? 17.958  224.927 58.135 1.00 25.27 ?  96  ASP F C   1 
ATOM   6312  O  O   . ASP F  1 97  ? 17.083  224.339 57.505 1.00 26.61 ?  96  ASP F O   1 
ATOM   6313  C  CB  . ASP F  1 97  ? 18.447  222.878 59.541 1.00 32.99 ?  96  ASP F CB  1 
ATOM   6314  C  CG  . ASP F  1 97  ? 19.190  222.343 60.774 1.00 37.71 ?  96  ASP F CG  1 
ATOM   6315  O  OD1 . ASP F  1 97  ? 18.608  221.562 61.567 1.00 39.58 ?  96  ASP F OD1 1 
ATOM   6316  O  OD2 . ASP F  1 97  ? 20.350  222.758 60.971 1.00 35.92 ?  96  ASP F OD2 1 
ATOM   6317  N  N   . VAL F  1 98  ? 18.502  226.067 57.713 1.00 23.50 ?  97  VAL F N   1 
ATOM   6318  C  CA  . VAL F  1 98  ? 17.964  226.791 56.569 1.00 26.40 ?  97  VAL F CA  1 
ATOM   6319  C  C   . VAL F  1 98  ? 18.225  226.022 55.277 1.00 26.97 ?  97  VAL F C   1 
ATOM   6320  O  O   . VAL F  1 98  ? 19.339  225.545 55.032 1.00 25.59 ?  97  VAL F O   1 
ATOM   6321  C  CB  . VAL F  1 98  ? 18.589  228.193 56.500 1.00 20.34 ?  97  VAL F CB  1 
ATOM   6322  C  CG1 . VAL F  1 98  ? 18.132  228.898 55.256 1.00 20.72 ?  97  VAL F CG1 1 
ATOM   6323  C  CG2 . VAL F  1 98  ? 18.249  229.011 57.759 1.00 21.74 ?  97  VAL F CG2 1 
ATOM   6324  N  N   . SER F  1 99  ? 17.206  225.922 54.427 1.00 24.03 ?  98  SER F N   1 
ATOM   6325  C  CA  . SER F  1 99  ? 17.389  225.334 53.099 1.00 30.04 ?  98  SER F CA  1 
ATOM   6326  C  C   . SER F  1 99  ? 16.395  226.026 52.178 1.00 28.73 ?  98  SER F C   1 
ATOM   6327  O  O   . SER F  1 99  ? 15.200  225.733 52.213 1.00 31.44 ?  98  SER F O   1 
ATOM   6328  C  CB  . SER F  1 99  ? 17.184  223.828 53.104 1.00 30.79 ?  98  SER F CB  1 
ATOM   6329  O  OG  . SER F  1 99  ? 17.347  223.321 51.789 1.00 40.25 ?  98  SER F OG  1 
ATOM   6330  N  N   . ILE F  1 100 ? 16.890  226.958 51.387 1.00 28.73 ?  99  ILE F N   1 
ATOM   6331  C  CA  . ILE F  1 100 ? 16.054  227.780 50.530 1.00 28.94 ?  99  ILE F CA  1 
ATOM   6332  C  C   . ILE F  1 100 ? 16.663  227.776 49.136 1.00 32.89 ?  99  ILE F C   1 
ATOM   6333  O  O   . ILE F  1 100 ? 17.885  227.703 48.969 1.00 28.05 ?  99  ILE F O   1 
ATOM   6334  C  CB  . ILE F  1 100 ? 15.937  229.211 51.095 1.00 28.25 ?  99  ILE F CB  1 
ATOM   6335  C  CG1 . ILE F  1 100 ? 14.955  229.229 52.271 1.00 30.13 ?  99  ILE F CG1 1 
ATOM   6336  C  CG2 . ILE F  1 100 ? 15.533  230.222 50.026 1.00 29.23 ?  99  ILE F CG2 1 
ATOM   6337  C  CD1 . ILE F  1 100 ? 15.031  230.540 53.090 1.00 30.50 ?  99  ILE F CD1 1 
ATOM   6338  N  N   . GLU F  1 101 ? 15.803  227.833 48.132 1.00 29.85 ?  100 GLU F N   1 
ATOM   6339  C  CA  . GLU F  1 101 ? 16.231  227.991 46.753 1.00 28.66 ?  100 GLU F CA  1 
ATOM   6340  C  C   . GLU F  1 101 ? 15.441  229.143 46.162 1.00 27.68 ?  100 GLU F C   1 
ATOM   6341  O  O   . GLU F  1 101 ? 14.211  229.131 46.221 1.00 27.77 ?  100 GLU F O   1 
ATOM   6342  C  CB  . GLU F  1 101 ? 16.003  226.688 45.989 1.00 32.87 ?  100 GLU F CB  1 
ATOM   6343  C  CG  . GLU F  1 101 ? 16.400  226.728 44.564 1.00 48.94 ?  100 GLU F CG  1 
ATOM   6344  C  CD  . GLU F  1 101 ? 16.406  225.338 43.954 1.00 59.83 ?  100 GLU F CD  1 
ATOM   6345  O  OE1 . GLU F  1 101 ? 16.377  225.262 42.713 1.00 65.40 ?  100 GLU F OE1 1 
ATOM   6346  O  OE2 . GLU F  1 101 ? 16.452  224.337 44.717 1.00 57.93 ?  100 GLU F OE2 1 
ATOM   6347  N  N   . ASP F  1 102 ? 16.136  230.157 45.635 1.00 25.90 ?  101 ASP F N   1 
ATOM   6348  C  CA  . ASP F  1 102 ? 15.471  231.367 45.151 1.00 28.91 ?  101 ASP F CA  1 
ATOM   6349  C  C   . ASP F  1 102 ? 16.065  231.799 43.825 1.00 31.90 ?  101 ASP F C   1 
ATOM   6350  O  O   . ASP F  1 102 ? 17.283  231.791 43.666 1.00 32.36 ?  101 ASP F O   1 
ATOM   6351  C  CB  . ASP F  1 102 ? 15.622  232.528 46.134 1.00 28.44 ?  101 ASP F CB  1 
ATOM   6352  C  CG  . ASP F  1 102 ? 14.668  233.675 45.825 1.00 33.21 ?  101 ASP F CG  1 
ATOM   6353  O  OD1 . ASP F  1 102 ? 13.449  233.495 46.060 1.00 34.87 ?  101 ASP F OD1 1 
ATOM   6354  O  OD2 . ASP F  1 102 ? 15.121  234.754 45.344 1.00 27.69 ?  101 ASP F OD2 1 
ATOM   6355  N  N   A SER F  1 103 ? 15.211  232.198 42.883 0.50 30.58 ?  102 SER F N   1 
ATOM   6356  N  N   B SER F  1 103 ? 15.207  232.206 42.893 0.50 30.58 ?  102 SER F N   1 
ATOM   6357  C  CA  A SER F  1 103 ? 15.673  232.588 41.559 0.50 34.57 ?  102 SER F CA  1 
ATOM   6358  C  CA  B SER F  1 103 ? 15.644  232.588 41.559 0.50 34.69 ?  102 SER F CA  1 
ATOM   6359  C  C   A SER F  1 103 ? 15.592  234.090 41.330 0.50 36.94 ?  102 SER F C   1 
ATOM   6360  C  C   B SER F  1 103 ? 15.599  234.090 41.332 0.50 36.94 ?  102 SER F C   1 
ATOM   6361  O  O   A SER F  1 103 ? 15.775  234.542 40.194 0.50 34.76 ?  102 SER F O   1 
ATOM   6362  O  O   B SER F  1 103 ? 15.815  234.540 40.202 0.50 34.80 ?  102 SER F O   1 
ATOM   6363  C  CB  A SER F  1 103 ? 14.879  231.858 40.476 0.50 37.36 ?  102 SER F CB  1 
ATOM   6364  C  CB  B SER F  1 103 ? 14.797  231.882 40.499 0.50 37.28 ?  102 SER F CB  1 
ATOM   6365  O  OG  A SER F  1 103 ? 15.128  230.463 40.509 0.50 36.87 ?  102 SER F OG  1 
ATOM   6366  O  OG  B SER F  1 103 ? 13.436  232.278 40.586 0.50 38.31 ?  102 SER F OG  1 
ATOM   6367  N  N   . VAL F  1 104 ? 15.325  234.874 42.370 1.00 31.61 ?  103 VAL F N   1 
ATOM   6368  C  CA  . VAL F  1 104 ? 15.235  236.319 42.237 1.00 27.06 ?  103 VAL F CA  1 
ATOM   6369  C  C   . VAL F  1 104 ? 16.487  236.999 42.756 1.00 28.19 ?  103 VAL F C   1 
ATOM   6370  O  O   . VAL F  1 104 ? 17.022  237.885 42.096 1.00 28.75 ?  103 VAL F O   1 
ATOM   6371  C  CB  . VAL F  1 104 ? 13.956  236.861 42.913 1.00 30.48 ?  103 VAL F CB  1 
ATOM   6372  C  CG1 . VAL F  1 104 ? 13.964  238.398 42.907 1.00 30.56 ?  103 VAL F CG1 1 
ATOM   6373  C  CG2 . VAL F  1 104 ? 12.723  236.340 42.159 1.00 32.71 ?  103 VAL F CG2 1 
ATOM   6374  N  N   . ILE F  1 105 ? 16.984  236.585 43.927 1.00 23.28 ?  104 ILE F N   1 
ATOM   6375  C  CA  . ILE F  1 105 ? 18.312  237.030 44.361 1.00 26.14 ?  104 ILE F CA  1 
ATOM   6376  C  C   . ILE F  1 105 ? 19.352  236.452 43.408 1.00 22.66 ?  104 ILE F C   1 
ATOM   6377  O  O   . ILE F  1 105 ? 19.119  235.459 42.717 1.00 23.82 ?  104 ILE F O   1 
ATOM   6378  C  CB  . ILE F  1 105 ? 18.627  236.606 45.806 1.00 23.98 ?  104 ILE F CB  1 
ATOM   6379  C  CG1 . ILE F  1 105 ? 18.586  235.068 45.925 1.00 20.34 ?  104 ILE F CG1 1 
ATOM   6380  C  CG2 . ILE F  1 105 ? 17.684  237.301 46.793 1.00 23.03 ?  104 ILE F CG2 1 
ATOM   6381  C  CD1 . ILE F  1 105 ? 19.383  234.491 47.135 1.00 24.32 ?  104 ILE F CD1 1 
ATOM   6382  N  N   . SER F  1 106 ? 20.519  237.076 43.388 1.00 22.37 ?  105 SER F N   1 
ATOM   6383  C  CA  . SER F  1 106 ? 21.611  236.595 42.557 1.00 24.77 ?  105 SER F CA  1 
ATOM   6384  C  C   . SER F  1 106 ? 22.925  236.884 43.256 1.00 25.63 ?  105 SER F C   1 
ATOM   6385  O  O   . SER F  1 106 ? 22.997  237.710 44.169 1.00 28.51 ?  105 SER F O   1 
ATOM   6386  C  CB  . SER F  1 106 ? 21.616  237.259 41.169 1.00 32.03 ?  105 SER F CB  1 
ATOM   6387  O  OG  . SER F  1 106 ? 22.346  236.465 40.252 1.00 32.40 ?  105 SER F OG  1 
ATOM   6388  N  N   . LEU F  1 107 ? 23.969  236.192 42.817 1.00 29.16 ?  106 LEU F N   1 
ATOM   6389  C  CA  . LEU F  1 107 ? 25.324  236.537 43.214 1.00 31.09 ?  106 LEU F CA  1 
ATOM   6390  C  C   . LEU F  1 107 ? 26.036  237.390 42.161 1.00 34.80 ?  106 LEU F C   1 
ATOM   6391  O  O   . LEU F  1 107 ? 27.238  237.623 42.280 1.00 35.80 ?  106 LEU F O   1 
ATOM   6392  C  CB  . LEU F  1 107 ? 26.121  235.268 43.516 1.00 29.72 ?  106 LEU F CB  1 
ATOM   6393  C  CG  . LEU F  1 107 ? 25.485  234.382 44.598 1.00 31.79 ?  106 LEU F CG  1 
ATOM   6394  C  CD1 . LEU F  1 107 ? 26.387  233.215 44.980 1.00 31.66 ?  106 LEU F CD1 1 
ATOM   6395  C  CD2 . LEU F  1 107 ? 25.114  235.195 45.835 1.00 22.10 ?  106 LEU F CD2 1 
ATOM   6396  N  N   . SER F  1 108 ? 25.316  237.877 41.149 1.00 30.96 ?  107 SER F N   1 
ATOM   6397  C  CA  . SER F  1 108 ? 25.874  238.831 40.195 1.00 42.51 ?  107 SER F CA  1 
ATOM   6398  C  C   . SER F  1 108 ? 24.750  239.668 39.603 1.00 36.01 ?  107 SER F C   1 
ATOM   6399  O  O   . SER F  1 108 ? 23.576  239.311 39.696 1.00 33.35 ?  107 SER F O   1 
ATOM   6400  C  CB  . SER F  1 108 ? 26.633  238.127 39.069 1.00 39.97 ?  107 SER F CB  1 
ATOM   6401  O  OG  . SER F  1 108 ? 25.793  237.166 38.469 1.00 36.85 ?  107 SER F OG  1 
ATOM   6402  N  N   . GLY F  1 109 ? 25.125  240.805 39.005 1.00 34.39 ?  108 GLY F N   1 
ATOM   6403  C  CA  . GLY F  1 109 ? 24.178  241.599 38.245 1.00 34.13 ?  108 GLY F CA  1 
ATOM   6404  C  C   . GLY F  1 109 ? 23.346  242.561 39.083 1.00 33.92 ?  108 GLY F C   1 
ATOM   6405  O  O   . GLY F  1 109 ? 23.686  242.924 40.207 1.00 36.59 ?  108 GLY F O   1 
ATOM   6406  N  N   . ASP F  1 110 ? 22.217  242.968 38.487 1.00 36.93 ?  109 ASP F N   1 
ATOM   6407  C  CA  . ASP F  1 110 ? 21.263  243.889 39.115 1.00 40.09 ?  109 ASP F CA  1 
ATOM   6408  C  C   . ASP F  1 110 ? 20.824  243.413 40.494 1.00 39.35 ?  109 ASP F C   1 
ATOM   6409  O  O   . ASP F  1 110 ? 20.649  244.214 41.414 1.00 35.74 ?  109 ASP F O   1 
ATOM   6410  C  CB  . ASP F  1 110 ? 20.030  244.018 38.221 1.00 38.20 ?  109 ASP F CB  1 
ATOM   6411  C  CG  . ASP F  1 110 ? 20.277  244.883 37.019 1.00 49.85 ?  109 ASP F CG  1 
ATOM   6412  O  OD1 . ASP F  1 110 ? 21.476  245.045 36.690 1.00 51.37 ?  109 ASP F OD1 1 
ATOM   6413  O  OD2 . ASP F  1 110 ? 19.300  245.337 36.372 1.00 43.86 ?  109 ASP F OD2 1 
ATOM   6414  N  N   . HIS F  1 111 ? 20.595  242.117 40.638 1.00 32.58 ?  110 HIS F N   1 
ATOM   6415  C  CA  . HIS F  1 111 ? 20.002  241.558 41.840 1.00 36.35 ?  110 HIS F CA  1 
ATOM   6416  C  C   . HIS F  1 111 ? 21.047  240.983 42.776 1.00 34.31 ?  110 HIS F C   1 
ATOM   6417  O  O   . HIS F  1 111 ? 20.700  240.246 43.702 1.00 34.01 ?  110 HIS F O   1 
ATOM   6418  C  CB  . HIS F  1 111 ? 18.971  240.498 41.457 1.00 30.94 ?  110 HIS F CB  1 
ATOM   6419  C  CG  . HIS F  1 111 ? 17.759  241.064 40.781 1.00 38.16 ?  110 HIS F CG  1 
ATOM   6420  N  ND1 . HIS F  1 111 ? 16.684  240.287 40.397 1.00 35.51 ?  110 HIS F ND1 1 
ATOM   6421  C  CD2 . HIS F  1 111 ? 17.453  242.336 40.424 1.00 38.30 ?  110 HIS F CD2 1 
ATOM   6422  C  CE1 . HIS F  1 111 ? 15.767  241.060 39.837 1.00 39.61 ?  110 HIS F CE1 1 
ATOM   6423  N  NE2 . HIS F  1 111 ? 16.210  242.305 39.840 1.00 37.09 ?  110 HIS F NE2 1 
ATOM   6424  N  N   . CYS F  1 112 ? 22.318  241.313 42.549 1.00 28.91 ?  111 CYS F N   1 
ATOM   6425  C  CA  . CYS F  1 112 ? 23.408  240.791 43.358 1.00 31.61 ?  111 CYS F CA  1 
ATOM   6426  C  C   . CYS F  1 112 ? 23.243  241.175 44.825 1.00 29.48 ?  111 CYS F C   1 
ATOM   6427  O  O   . CYS F  1 112 ? 23.018  242.343 45.152 1.00 27.87 ?  111 CYS F O   1 
ATOM   6428  C  CB  . CYS F  1 112 ? 24.733  241.330 42.832 1.00 34.10 ?  111 CYS F CB  1 
ATOM   6429  S  SG  . CYS F  1 112 ? 26.131  240.586 43.636 1.00 37.00 ?  111 CYS F SG  1 
ATOM   6430  N  N   . ILE F  1 113 ? 23.370  240.197 45.712 1.00 26.65 ?  112 ILE F N   1 
ATOM   6431  C  CA  . ILE F  1 113 ? 23.263  240.442 47.146 1.00 28.11 ?  112 ILE F CA  1 
ATOM   6432  C  C   . ILE F  1 113 ? 24.614  240.453 47.832 1.00 29.68 ?  112 ILE F C   1 
ATOM   6433  O  O   . ILE F  1 113 ? 24.666  240.620 49.050 1.00 26.43 ?  112 ILE F O   1 
ATOM   6434  C  CB  . ILE F  1 113 ? 22.331  239.413 47.811 1.00 26.60 ?  112 ILE F CB  1 
ATOM   6435  C  CG1 . ILE F  1 113 ? 22.911  238.012 47.626 1.00 25.21 ?  112 ILE F CG1 1 
ATOM   6436  C  CG2 . ILE F  1 113 ? 20.949  239.498 47.175 1.00 25.16 ?  112 ILE F CG2 1 
ATOM   6437  C  CD1 . ILE F  1 113 ? 22.088  236.893 48.280 1.00 27.59 ?  112 ILE F CD1 1 
ATOM   6438  N  N   . ILE F  1 114 ? 25.707  240.250 47.096 1.00 30.49 ?  113 ILE F N   1 
ATOM   6439  C  CA  . ILE F  1 114 ? 27.040  240.365 47.673 1.00 28.35 ?  113 ILE F CA  1 
ATOM   6440  C  C   . ILE F  1 114 ? 27.237  241.774 48.196 1.00 26.73 ?  113 ILE F C   1 
ATOM   6441  O  O   . ILE F  1 114 ? 26.926  242.750 47.506 1.00 26.68 ?  113 ILE F O   1 
ATOM   6442  C  CB  . ILE F  1 114 ? 28.108  240.026 46.625 1.00 31.25 ?  113 ILE F CB  1 
ATOM   6443  C  CG1 . ILE F  1 114 ? 27.873  238.617 46.048 1.00 32.17 ?  113 ILE F CG1 1 
ATOM   6444  C  CG2 . ILE F  1 114 ? 29.515  240.288 47.180 1.00 26.77 ?  113 ILE F CG2 1 
ATOM   6445  C  CD1 . ILE F  1 114 ? 28.638  237.579 46.689 1.00 35.33 ?  113 ILE F CD1 1 
ATOM   6446  N  N   . GLY F  1 115 ? 27.738  241.890 49.428 1.00 26.48 ?  114 GLY F N   1 
ATOM   6447  C  CA  . GLY F  1 115 ? 27.936  243.200 50.018 1.00 25.60 ?  114 GLY F CA  1 
ATOM   6448  C  C   . GLY F  1 115 ? 26.697  243.805 50.634 1.00 29.77 ?  114 GLY F C   1 
ATOM   6449  O  O   . GLY F  1 115 ? 26.745  244.960 51.094 1.00 28.70 ?  114 GLY F O   1 
ATOM   6450  N  N   . ARG F  1 116 ? 25.589  243.075 50.659 1.00 24.85 ?  115 ARG F N   1 
ATOM   6451  C  CA  . ARG F  1 116 ? 24.400  243.508 51.371 1.00 23.57 ?  115 ARG F CA  1 
ATOM   6452  C  C   . ARG F  1 116 ? 24.280  242.684 52.651 1.00 26.33 ?  115 ARG F C   1 
ATOM   6453  O  O   . ARG F  1 116 ? 25.164  241.899 52.984 1.00 29.01 ?  115 ARG F O   1 
ATOM   6454  C  CB  . ARG F  1 116 ? 23.182  243.388 50.450 1.00 26.55 ?  115 ARG F CB  1 
ATOM   6455  C  CG  . ARG F  1 116 ? 23.432  244.139 49.108 1.00 28.10 ?  115 ARG F CG  1 
ATOM   6456  C  CD  . ARG F  1 116 ? 22.168  244.390 48.319 1.00 32.67 ?  115 ARG F CD  1 
ATOM   6457  N  NE  . ARG F  1 116 ? 22.483  244.891 46.986 1.00 33.02 ?  115 ARG F NE  1 
ATOM   6458  C  CZ  . ARG F  1 116 ? 22.570  246.178 46.675 1.00 32.76 ?  115 ARG F CZ  1 
ATOM   6459  N  NH1 . ARG F  1 116 ? 22.315  247.125 47.569 1.00 29.81 ?  115 ARG F NH1 1 
ATOM   6460  N  NH2 . ARG F  1 116 ? 22.880  246.526 45.426 1.00 29.77 ?  115 ARG F NH2 1 
ATOM   6461  N  N   . THR F  1 117 ? 23.201  242.887 53.395 1.00 24.30 ?  116 THR F N   1 
ATOM   6462  C  CA  . THR F  1 117 ? 23.081  242.320 54.733 1.00 27.21 ?  116 THR F CA  1 
ATOM   6463  C  C   . THR F  1 117 ? 21.945  241.311 54.786 1.00 22.19 ?  116 THR F C   1 
ATOM   6464  O  O   . THR F  1 117 ? 20.807  241.638 54.443 1.00 24.99 ?  116 THR F O   1 
ATOM   6465  C  CB  . THR F  1 117 ? 22.844  243.404 55.788 1.00 28.11 ?  116 THR F CB  1 
ATOM   6466  O  OG1 . THR F  1 117 ? 24.003  244.233 55.892 1.00 28.51 ?  116 THR F OG1 1 
ATOM   6467  C  CG2 . THR F  1 117 ? 22.591  242.743 57.163 1.00 25.15 ?  116 THR F CG2 1 
ATOM   6468  N  N   . LEU F  1 118 ? 22.263  240.093 55.206 1.00 22.28 ?  117 LEU F N   1 
ATOM   6469  C  CA  . LEU F  1 118 ? 21.245  239.110 55.549 1.00 23.12 ?  117 LEU F CA  1 
ATOM   6470  C  C   . LEU F  1 118 ? 20.787  239.346 56.980 1.00 25.00 ?  117 LEU F C   1 
ATOM   6471  O  O   . LEU F  1 118 ? 21.616  239.481 57.875 1.00 26.48 ?  117 LEU F O   1 
ATOM   6472  C  CB  . LEU F  1 118 ? 21.813  237.703 55.417 1.00 20.34 ?  117 LEU F CB  1 
ATOM   6473  C  CG  . LEU F  1 118 ? 20.831  236.568 55.665 1.00 27.14 ?  117 LEU F CG  1 
ATOM   6474  C  CD1 . LEU F  1 118 ? 19.735  236.677 54.650 1.00 20.60 ?  117 LEU F CD1 1 
ATOM   6475  C  CD2 . LEU F  1 118 ? 21.526  235.200 55.527 1.00 20.34 ?  117 LEU F CD2 1 
ATOM   6476  N  N   . VAL F  1 119 ? 19.479  239.370 57.211 1.00 22.95 ?  118 VAL F N   1 
ATOM   6477  C  CA  . VAL F  1 119 ? 18.941  239.613 58.548 1.00 23.27 ?  118 VAL F CA  1 
ATOM   6478  C  C   . VAL F  1 119 ? 17.945  238.516 58.891 1.00 25.48 ?  118 VAL F C   1 
ATOM   6479  O  O   . VAL F  1 119 ? 17.082  238.182 58.070 1.00 23.41 ?  118 VAL F O   1 
ATOM   6480  C  CB  . VAL F  1 119 ? 18.258  240.988 58.641 1.00 24.14 ?  118 VAL F CB  1 
ATOM   6481  C  CG1 . VAL F  1 119 ? 17.602  241.162 60.034 1.00 25.78 ?  118 VAL F CG1 1 
ATOM   6482  C  CG2 . VAL F  1 119 ? 19.247  242.097 58.326 1.00 20.34 ?  118 VAL F CG2 1 
ATOM   6483  N  N   . VAL F  1 120 ? 18.042  237.960 60.099 1.00 20.68 ?  119 VAL F N   1 
ATOM   6484  C  CA  . VAL F  1 120 ? 16.975  237.108 60.605 1.00 22.26 ?  119 VAL F CA  1 
ATOM   6485  C  C   . VAL F  1 120 ? 16.199  237.897 61.657 1.00 27.85 ?  119 VAL F C   1 
ATOM   6486  O  O   . VAL F  1 120 ? 16.790  238.579 62.512 1.00 26.16 ?  119 VAL F O   1 
ATOM   6487  C  CB  . VAL F  1 120 ? 17.515  235.755 61.116 1.00 25.01 ?  119 VAL F CB  1 
ATOM   6488  C  CG1 . VAL F  1 120 ? 18.537  235.920 62.262 1.00 24.70 ?  119 VAL F CG1 1 
ATOM   6489  C  CG2 . VAL F  1 120 ? 16.360  234.812 61.500 1.00 23.61 ?  119 VAL F CG2 1 
ATOM   6490  N  N   . HIS F  1 121 ? 14.874  237.862 61.550 1.00 23.93 ?  120 HIS F N   1 
ATOM   6491  C  CA  . HIS F  1 121 ? 13.997  238.753 62.295 1.00 22.95 ?  120 HIS F CA  1 
ATOM   6492  C  C   . HIS F  1 121 ? 13.332  238.056 63.482 1.00 25.32 ?  120 HIS F C   1 
ATOM   6493  O  O   . HIS F  1 121 ? 13.378  236.835 63.652 1.00 24.88 ?  120 HIS F O   1 
ATOM   6494  C  CB  . HIS F  1 121 ? 12.922  239.343 61.378 1.00 25.12 ?  120 HIS F CB  1 
ATOM   6495  C  CG  . HIS F  1 121 ? 13.425  240.429 60.477 1.00 27.83 ?  120 HIS F CG  1 
ATOM   6496  N  ND1 . HIS F  1 121 ? 13.330  241.770 60.797 1.00 24.67 ?  120 HIS F ND1 1 
ATOM   6497  C  CD2 . HIS F  1 121 ? 14.029  240.372 59.265 1.00 24.15 ?  120 HIS F CD2 1 
ATOM   6498  C  CE1 . HIS F  1 121 ? 13.846  242.492 59.815 1.00 28.05 ?  120 HIS F CE1 1 
ATOM   6499  N  NE2 . HIS F  1 121 ? 14.274  241.666 58.870 1.00 28.66 ?  120 HIS F NE2 1 
ATOM   6500  N  N   . GLU F  1 122 ? 12.654  238.879 64.276 1.00 27.01 ?  121 GLU F N   1 
ATOM   6501  C  CA  . GLU F  1 122 ? 12.114  238.458 65.564 1.00 27.04 ?  121 GLU F CA  1 
ATOM   6502  C  C   . GLU F  1 122 ? 10.875  237.588 65.401 1.00 21.22 ?  121 GLU F C   1 
ATOM   6503  O  O   . GLU F  1 122 ? 10.724  236.585 66.104 1.00 29.62 ?  121 GLU F O   1 
ATOM   6504  C  CB  . GLU F  1 122 ? 11.807  239.718 66.389 1.00 29.92 ?  121 GLU F CB  1 
ATOM   6505  C  CG  . GLU F  1 122 ? 10.777  239.550 67.484 1.00 37.31 ?  121 GLU F CG  1 
ATOM   6506  C  CD  . GLU F  1 122 ? 10.373  240.888 68.117 1.00 47.57 ?  121 GLU F CD  1 
ATOM   6507  O  OE1 . GLU F  1 122 ? 10.271  241.920 67.386 1.00 43.02 ?  121 GLU F OE1 1 
ATOM   6508  O  OE2 . GLU F  1 122 ? 10.140  240.897 69.345 1.00 51.94 ?  121 GLU F OE2 1 
ATOM   6509  N  N   . LYS F  1 123 ? 9.992   237.932 64.469 1.00 30.24 ?  122 LYS F N   1 
ATOM   6510  C  CA  . LYS F  1 123 ? 8.715   237.242 64.280 1.00 32.06 ?  122 LYS F CA  1 
ATOM   6511  C  C   . LYS F  1 123 ? 8.583   236.707 62.851 1.00 29.95 ?  122 LYS F C   1 
ATOM   6512  O  O   . LYS F  1 123 ? 9.418   236.954 61.979 1.00 26.25 ?  122 LYS F O   1 
ATOM   6513  C  CB  . LYS F  1 123 ? 7.531   238.176 64.583 1.00 36.16 ?  122 LYS F CB  1 
ATOM   6514  C  CG  . LYS F  1 123 ? 7.812   239.230 65.635 1.00 40.34 ?  122 LYS F CG  1 
ATOM   6515  C  CD  . LYS F  1 123 ? 6.546   239.961 66.088 1.00 40.04 ?  122 LYS F CD  1 
ATOM   6516  C  CE  . LYS F  1 123 ? 6.003   240.917 65.032 1.00 50.07 ?  122 LYS F CE  1 
ATOM   6517  N  NZ  . LYS F  1 123 ? 4.505   240.976 64.953 1.00 63.78 ?  122 LYS F NZ  1 
ATOM   6518  N  N   . ALA F  1 124 ? 7.480   236.011 62.611 1.00 25.87 ?  123 ALA F N   1 
ATOM   6519  C  CA  . ALA F  1 124 ? 7.185   235.526 61.272 1.00 30.25 ?  123 ALA F CA  1 
ATOM   6520  C  C   . ALA F  1 124 ? 6.973   236.687 60.308 1.00 29.91 ?  123 ALA F C   1 
ATOM   6521  O  O   . ALA F  1 124 ? 6.408   237.727 60.666 1.00 27.42 ?  123 ALA F O   1 
ATOM   6522  C  CB  . ALA F  1 124 ? 5.945   234.637 61.293 1.00 27.34 ?  123 ALA F CB  1 
ATOM   6523  N  N   . ASP F  1 125 ? 7.463   236.508 59.087 1.00 24.42 ?  124 ASP F N   1 
ATOM   6524  C  CA  . ASP F  1 125 ? 7.092   237.358 57.971 1.00 26.26 ?  124 ASP F CA  1 
ATOM   6525  C  C   . ASP F  1 125 ? 5.680   236.986 57.533 1.00 30.58 ?  124 ASP F C   1 
ATOM   6526  O  O   . ASP F  1 125 ? 5.384   235.808 57.324 1.00 23.69 ?  124 ASP F O   1 
ATOM   6527  C  CB  . ASP F  1 125 ? 8.103   237.145 56.842 1.00 23.45 ?  124 ASP F CB  1 
ATOM   6528  C  CG  . ASP F  1 125 ? 7.868   238.031 55.628 1.00 28.09 ?  124 ASP F CG  1 
ATOM   6529  O  OD1 . ASP F  1 125 ? 6.762   238.601 55.451 1.00 21.05 ?  124 ASP F OD1 1 
ATOM   6530  O  OD2 . ASP F  1 125 ? 8.838   238.137 54.840 1.00 28.07 ?  124 ASP F OD2 1 
ATOM   6531  N  N   . ASP F  1 126 ? 4.789   237.973 57.414 1.00 27.86 ?  125 ASP F N   1 
ATOM   6532  C  CA  . ASP F  1 126 ? 3.444   237.614 56.956 1.00 27.59 ?  125 ASP F CA  1 
ATOM   6533  C  C   . ASP F  1 126 ? 3.342   237.556 55.445 1.00 24.53 ?  125 ASP F C   1 
ATOM   6534  O  O   . ASP F  1 126 ? 2.233   237.408 54.916 1.00 24.55 ?  125 ASP F O   1 
ATOM   6535  C  CB  . ASP F  1 126 ? 2.373   238.554 57.558 1.00 30.06 ?  125 ASP F CB  1 
ATOM   6536  C  CG  . ASP F  1 126 ? 2.457   240.004 57.056 1.00 28.00 ?  125 ASP F CG  1 
ATOM   6537  O  OD1 . ASP F  1 126 ? 3.041   240.292 55.990 1.00 31.09 ?  125 ASP F OD1 1 
ATOM   6538  O  OD2 . ASP F  1 126 ? 1.896   240.880 57.746 1.00 29.30 ?  125 ASP F OD2 1 
ATOM   6539  N  N   . LEU F  1 127 ? 4.484   237.634 54.750 1.00 26.92 ?  126 LEU F N   1 
ATOM   6540  C  CA  . LEU F  1 127 ? 4.571   237.495 53.294 1.00 25.77 ?  126 LEU F CA  1 
ATOM   6541  C  C   . LEU F  1 127 ? 3.713   238.536 52.579 1.00 25.38 ?  126 LEU F C   1 
ATOM   6542  O  O   . LEU F  1 127 ? 3.257   238.319 51.456 1.00 27.64 ?  126 LEU F O   1 
ATOM   6543  C  CB  . LEU F  1 127 ? 4.209   236.073 52.850 1.00 25.88 ?  126 LEU F CB  1 
ATOM   6544  C  CG  . LEU F  1 127 ? 4.819   234.974 53.754 1.00 31.34 ?  126 LEU F CG  1 
ATOM   6545  C  CD1 . LEU F  1 127 ? 4.394   233.574 53.304 1.00 23.77 ?  126 LEU F CD1 1 
ATOM   6546  C  CD2 . LEU F  1 127 ? 6.338   235.054 53.824 1.00 20.34 ?  126 LEU F CD2 1 
ATOM   6547  N  N   . GLY F  1 128 ? 3.505   239.680 53.225 1.00 27.04 ?  127 GLY F N   1 
ATOM   6548  C  CA  . GLY F  1 128 ? 2.749   240.773 52.651 1.00 28.32 ?  127 GLY F CA  1 
ATOM   6549  C  C   . GLY F  1 128 ? 1.259   240.568 52.635 1.00 27.02 ?  127 GLY F C   1 
ATOM   6550  O  O   . GLY F  1 128 ? 0.554   241.260 51.890 1.00 29.19 ?  127 GLY F O   1 
ATOM   6551  N  N   . LYS F  1 129 ? 0.747   239.631 53.435 1.00 27.88 ?  128 LYS F N   1 
ATOM   6552  C  CA  . LYS F  1 129 ? -0.673  239.303 53.424 1.00 28.60 ?  128 LYS F CA  1 
ATOM   6553  C  C   . LYS F  1 129 ? -1.389  239.797 54.674 1.00 28.48 ?  128 LYS F C   1 
ATOM   6554  O  O   . LYS F  1 129 ? -2.507  239.354 54.951 1.00 30.43 ?  128 LYS F O   1 
ATOM   6555  C  CB  . LYS F  1 129 ? -0.864  237.794 53.284 1.00 26.22 ?  128 LYS F CB  1 
ATOM   6556  C  CG  . LYS F  1 129 ? -0.344  237.223 51.981 1.00 28.55 ?  128 LYS F CG  1 
ATOM   6557  C  CD  . LYS F  1 129 ? -0.112  235.733 52.080 1.00 40.22 ?  128 LYS F CD  1 
ATOM   6558  C  CE  . LYS F  1 129 ? -1.307  234.951 51.556 1.00 44.22 ?  128 LYS F CE  1 
ATOM   6559  N  NZ  . LYS F  1 129 ? -1.057  233.480 51.561 1.00 48.26 ?  128 LYS F NZ  1 
ATOM   6560  N  N   . GLY F  1 130 ? -0.766  240.698 55.432 1.00 28.92 ?  129 GLY F N   1 
ATOM   6561  C  CA  . GLY F  1 130 ? -1.296  241.138 56.710 1.00 27.95 ?  129 GLY F CA  1 
ATOM   6562  C  C   . GLY F  1 130 ? -2.329  242.247 56.670 1.00 34.41 ?  129 GLY F C   1 
ATOM   6563  O  O   . GLY F  1 130 ? -2.921  242.569 57.709 1.00 30.40 ?  129 GLY F O   1 
ATOM   6564  N  N   . GLY F  1 131 ? -2.534  242.866 55.514 1.00 29.65 ?  130 GLY F N   1 
ATOM   6565  C  CA  . GLY F  1 131 ? -3.567  243.873 55.351 1.00 27.31 ?  130 GLY F CA  1 
ATOM   6566  C  C   . GLY F  1 131 ? -3.259  245.249 55.897 1.00 31.49 ?  130 GLY F C   1 
ATOM   6567  O  O   . GLY F  1 131 ? -4.092  246.150 55.754 1.00 33.33 ?  130 GLY F O   1 
ATOM   6568  N  N   . ASN F  1 132 ? -2.110  245.460 56.521 1.00 30.64 ?  131 ASN F N   1 
ATOM   6569  C  CA  . ASN F  1 132 ? -1.775  246.793 56.993 1.00 29.26 ?  131 ASN F CA  1 
ATOM   6570  C  C   . ASN F  1 132 ? -0.575  247.324 56.233 1.00 32.85 ?  131 ASN F C   1 
ATOM   6571  O  O   . ASN F  1 132 ? 0.017   246.642 55.391 1.00 30.71 ?  131 ASN F O   1 
ATOM   6572  C  CB  . ASN F  1 132 ? -1.538  246.811 58.516 1.00 32.79 ?  131 ASN F CB  1 
ATOM   6573  C  CG  . ASN F  1 132 ? -0.372  245.942 58.967 1.00 34.97 ?  131 ASN F CG  1 
ATOM   6574  O  OD1 . ASN F  1 132 ? 0.292   245.280 58.172 1.00 32.57 ?  131 ASN F OD1 1 
ATOM   6575  N  ND2 . ASN F  1 132 ? -0.128  245.949 60.273 1.00 33.36 ?  131 ASN F ND2 1 
ATOM   6576  N  N   . GLU F  1 133 ? -0.232  248.581 56.508 1.00 33.29 ?  132 GLU F N   1 
ATOM   6577  C  CA  . GLU F  1 133 ? 0.833   249.199 55.726 1.00 35.16 ?  132 GLU F CA  1 
ATOM   6578  C  C   . GLU F  1 133 ? 2.171   248.532 56.004 1.00 35.20 ?  132 GLU F C   1 
ATOM   6579  O  O   . GLU F  1 133 ? 2.990   248.359 55.093 1.00 35.89 ?  132 GLU F O   1 
ATOM   6580  C  CB  . GLU F  1 133 ? 0.911   250.698 56.022 1.00 44.78 ?  132 GLU F CB  1 
ATOM   6581  C  CG  . GLU F  1 133 ? 1.945   251.409 55.140 1.00 54.90 ?  132 GLU F CG  1 
ATOM   6582  C  CD  . GLU F  1 133 ? 1.881   252.932 55.234 1.00 62.11 ?  132 GLU F CD  1 
ATOM   6583  O  OE1 . GLU F  1 133 ? 0.786   253.474 55.510 1.00 70.10 ?  132 GLU F OE1 1 
ATOM   6584  O  OE2 . GLU F  1 133 ? 2.933   253.582 55.031 1.00 59.12 ?  132 GLU F OE2 1 
ATOM   6585  N  N   . GLU F  1 134 ? 2.398   248.131 57.252 1.00 32.02 ?  133 GLU F N   1 
ATOM   6586  C  CA  . GLU F  1 134 ? 3.658   247.494 57.618 1.00 37.12 ?  133 GLU F CA  1 
ATOM   6587  C  C   . GLU F  1 134 ? 3.878   246.192 56.850 1.00 32.80 ?  133 GLU F C   1 
ATOM   6588  O  O   . GLU F  1 134 ? 5.020   245.833 56.543 1.00 32.63 ?  133 GLU F O   1 
ATOM   6589  C  CB  . GLU F  1 134 ? 3.670   247.248 59.125 1.00 35.33 ?  133 GLU F CB  1 
ATOM   6590  C  CG  . GLU F  1 134 ? 5.023   246.930 59.688 1.00 41.49 ?  133 GLU F CG  1 
ATOM   6591  C  CD  . GLU F  1 134 ? 5.986   248.066 59.468 1.00 46.46 ?  133 GLU F CD  1 
ATOM   6592  O  OE1 . GLU F  1 134 ? 5.645   249.209 59.842 1.00 45.94 ?  133 GLU F OE1 1 
ATOM   6593  O  OE2 . GLU F  1 134 ? 7.076   247.814 58.907 1.00 43.27 ?  133 GLU F OE2 1 
ATOM   6594  N  N   . SER F  1 135 ? 2.797   245.488 56.521 1.00 30.03 ?  134 SER F N   1 
ATOM   6595  C  CA  . SER F  1 135 ? 2.908   244.227 55.794 1.00 31.42 ?  134 SER F CA  1 
ATOM   6596  C  C   . SER F  1 135 ? 3.552   244.425 54.428 1.00 34.31 ?  134 SER F C   1 
ATOM   6597  O  O   . SER F  1 135 ? 4.379   243.611 53.996 1.00 30.90 ?  134 SER F O   1 
ATOM   6598  C  CB  . SER F  1 135 ? 1.522   243.607 55.651 1.00 28.98 ?  134 SER F CB  1 
ATOM   6599  O  OG  . SER F  1 135 ? 1.597   242.316 55.087 1.00 30.11 ?  134 SER F OG  1 
ATOM   6600  N  N   . THR F  1 136 ? 3.187   245.504 53.736 1.00 31.54 ?  135 THR F N   1 
ATOM   6601  C  CA  . THR F  1 136 ? 3.723   245.801 52.407 1.00 32.12 ?  135 THR F CA  1 
ATOM   6602  C  C   . THR F  1 136 ? 5.139   246.326 52.460 1.00 27.57 ?  135 THR F C   1 
ATOM   6603  O  O   . THR F  1 136 ? 5.726   246.576 51.402 1.00 32.23 ?  135 THR F O   1 
ATOM   6604  C  CB  . THR F  1 136 ? 2.854   246.843 51.683 1.00 34.83 ?  135 THR F CB  1 
ATOM   6605  O  OG1 . THR F  1 136 ? 3.091   248.143 52.252 1.00 36.43 ?  135 THR F OG1 1 
ATOM   6606  C  CG2 . THR F  1 136 ? 1.389   246.521 51.825 1.00 33.01 ?  135 THR F CG2 1 
ATOM   6607  N  N   . LYS F  1 137 ? 5.694   246.525 53.649 1.00 29.25 ?  136 LYS F N   1 
ATOM   6608  C  CA  . LYS F  1 137 ? 7.060   247.006 53.790 1.00 31.98 ?  136 LYS F CA  1 
ATOM   6609  C  C   . LYS F  1 137 ? 7.997   245.965 54.380 1.00 29.58 ?  136 LYS F C   1 
ATOM   6610  O  O   . LYS F  1 137 ? 9.054   245.684 53.808 1.00 30.67 ?  136 LYS F O   1 
ATOM   6611  C  CB  . LYS F  1 137 ? 7.079   248.269 54.663 1.00 31.64 ?  136 LYS F CB  1 
ATOM   6612  C  CG  . LYS F  1 137 ? 6.820   249.515 53.870 1.00 35.53 ?  136 LYS F CG  1 
ATOM   6613  C  CD  . LYS F  1 137 ? 5.685   250.306 54.474 1.00 52.27 ?  136 LYS F CD  1 
ATOM   6614  C  CE  . LYS F  1 137 ? 6.198   251.591 55.126 1.00 54.97 ?  136 LYS F CE  1 
ATOM   6615  N  NZ  . LYS F  1 137 ? 5.189   252.287 55.998 1.00 54.57 ?  136 LYS F NZ  1 
ATOM   6616  N  N   . THR F  1 138 ? 7.648   245.389 55.524 1.00 31.24 ?  137 THR F N   1 
ATOM   6617  C  CA  . THR F  1 138 ? 8.535   244.475 56.223 1.00 30.28 ?  137 THR F CA  1 
ATOM   6618  C  C   . THR F  1 138 ? 7.921   243.104 56.457 1.00 29.74 ?  137 THR F C   1 
ATOM   6619  O  O   . THR F  1 138 ? 8.579   242.249 57.061 1.00 29.67 ?  137 THR F O   1 
ATOM   6620  C  CB  . THR F  1 138 ? 8.921   245.054 57.585 1.00 33.01 ?  137 THR F CB  1 
ATOM   6621  O  OG1 . THR F  1 138 ? 7.723   245.172 58.371 1.00 32.43 ?  137 THR F OG1 1 
ATOM   6622  C  CG2 . THR F  1 138 ? 9.594   246.430 57.438 1.00 35.60 ?  137 THR F CG2 1 
ATOM   6623  N  N   . GLY F  1 139 ? 6.659   242.901 56.086 1.00 30.37 ?  138 GLY F N   1 
ATOM   6624  C  CA  . GLY F  1 139 ? 5.942   241.706 56.495 1.00 29.48 ?  138 GLY F CA  1 
ATOM   6625  C  C   . GLY F  1 139 ? 5.655   241.595 57.981 1.00 29.98 ?  138 GLY F C   1 
ATOM   6626  O  O   . GLY F  1 139 ? 5.331   240.504 58.442 1.00 27.23 ?  138 GLY F O   1 
ATOM   6627  N  N   . ASN F  1 140 ? 5.755   242.683 58.749 1.00 28.89 ?  139 ASN F N   1 
ATOM   6628  C  CA  . ASN F  1 140 ? 5.548   242.642 60.203 1.00 28.27 ?  139 ASN F CA  1 
ATOM   6629  C  C   . ASN F  1 140 ? 6.484   241.656 60.895 1.00 29.87 ?  139 ASN F C   1 
ATOM   6630  O  O   . ASN F  1 140 ? 6.111   241.035 61.896 1.00 31.40 ?  139 ASN F O   1 
ATOM   6631  C  CB  . ASN F  1 140 ? 4.093   242.289 60.562 1.00 28.83 ?  139 ASN F CB  1 
ATOM   6632  C  CG  . ASN F  1 140 ? 3.127   243.405 60.220 1.00 33.32 ?  139 ASN F CG  1 
ATOM   6633  O  OD1 . ASN F  1 140 ? 3.191   244.491 60.788 1.00 33.65 ?  139 ASN F OD1 1 
ATOM   6634  N  ND2 . ASN F  1 140 ? 2.242   243.144 59.271 1.00 31.02 ?  139 ASN F ND2 1 
ATOM   6635  N  N   . ALA F  1 141 ? 7.698   241.478 60.383 1.00 25.35 ?  140 ALA F N   1 
ATOM   6636  C  CA  . ALA F  1 141 ? 8.609   240.483 60.950 1.00 26.97 ?  140 ALA F CA  1 
ATOM   6637  C  C   . ALA F  1 141 ? 9.350   240.974 62.197 1.00 24.05 ?  140 ALA F C   1 
ATOM   6638  O  O   . ALA F  1 141 ? 10.115  240.204 62.805 1.00 28.35 ?  140 ALA F O   1 
ATOM   6639  C  CB  . ALA F  1 141 ? 9.624   240.030 59.893 1.00 20.34 ?  140 ALA F CB  1 
ATOM   6640  N  N   . GLY F  1 142 ? 9.152   242.215 62.595 1.00 30.65 ?  141 GLY F N   1 
ATOM   6641  C  CA  . GLY F  1 142 ? 9.693   242.647 63.860 1.00 29.38 ?  141 GLY F CA  1 
ATOM   6642  C  C   . GLY F  1 142 ? 11.173  242.949 63.767 1.00 34.11 ?  141 GLY F C   1 
ATOM   6643  O  O   . GLY F  1 142 ? 11.744  243.143 62.690 1.00 29.83 ?  141 GLY F O   1 
ATOM   6644  N  N   . SER F  1 143 ? 11.801  242.985 64.937 1.00 29.61 ?  142 SER F N   1 
ATOM   6645  C  CA  . SER F  1 143 ? 13.133  243.541 65.018 1.00 30.34 ?  142 SER F CA  1 
ATOM   6646  C  C   . SER F  1 143 ? 14.161  242.563 64.448 1.00 29.22 ?  142 SER F C   1 
ATOM   6647  O  O   . SER F  1 143 ? 13.865  241.416 64.091 1.00 27.87 ?  142 SER F O   1 
ATOM   6648  C  CB  . SER F  1 143 ? 13.476  243.894 66.461 1.00 35.80 ?  142 SER F CB  1 
ATOM   6649  O  OG  . SER F  1 143 ? 13.477  242.716 67.228 1.00 35.82 ?  142 SER F OG  1 
ATOM   6650  N  N   . ARG F  1 144 ? 15.386  243.037 64.385 1.00 26.06 ?  143 ARG F N   1 
ATOM   6651  C  CA  . ARG F  1 144 ? 16.481  242.352 63.724 1.00 29.82 ?  143 ARG F CA  1 
ATOM   6652  C  C   . ARG F  1 144 ? 17.282  241.610 64.782 1.00 30.43 ?  143 ARG F C   1 
ATOM   6653  O  O   . ARG F  1 144 ? 17.961  242.231 65.607 1.00 30.80 ?  143 ARG F O   1 
ATOM   6654  C  CB  . ARG F  1 144 ? 17.319  243.376 62.963 1.00 27.46 ?  143 ARG F CB  1 
ATOM   6655  C  CG  . ARG F  1 144 ? 16.423  244.330 62.177 1.00 28.64 ?  143 ARG F CG  1 
ATOM   6656  C  CD  . ARG F  1 144 ? 17.167  245.332 61.316 1.00 23.54 ?  143 ARG F CD  1 
ATOM   6657  N  NE  . ARG F  1 144 ? 16.207  246.134 60.565 1.00 28.29 ?  143 ARG F NE  1 
ATOM   6658  C  CZ  . ARG F  1 144 ? 16.504  246.885 59.516 1.00 30.96 ?  143 ARG F CZ  1 
ATOM   6659  N  NH1 . ARG F  1 144 ? 17.752  247.008 59.083 1.00 29.01 ?  143 ARG F NH1 1 
ATOM   6660  N  NH2 . ARG F  1 144 ? 15.525  247.517 58.874 1.00 24.57 ?  143 ARG F NH2 1 
ATOM   6661  N  N   . LEU F  1 145 ? 17.196  240.282 64.771 1.00 28.60 ?  144 LEU F N   1 
ATOM   6662  C  CA  . LEU F  1 145 ? 17.860  239.526 65.828 1.00 27.64 ?  144 LEU F CA  1 
ATOM   6663  C  C   . LEU F  1 145 ? 19.336  239.345 65.543 1.00 30.86 ?  144 LEU F C   1 
ATOM   6664  O  O   . LEU F  1 145 ? 20.141  239.330 66.476 1.00 27.09 ?  144 LEU F O   1 
ATOM   6665  C  CB  . LEU F  1 145 ? 17.203  238.159 66.030 1.00 20.34 ?  144 LEU F CB  1 
ATOM   6666  C  CG  . LEU F  1 145 ? 15.716  238.188 66.355 1.00 30.62 ?  144 LEU F CG  1 
ATOM   6667  C  CD1 . LEU F  1 145 ? 15.200  236.772 66.589 1.00 30.58 ?  144 LEU F CD1 1 
ATOM   6668  C  CD2 . LEU F  1 145 ? 15.440  239.071 67.577 1.00 32.86 ?  144 LEU F CD2 1 
ATOM   6669  N  N   . ALA F  1 146 ? 19.705  239.192 64.273 1.00 23.72 ?  145 ALA F N   1 
ATOM   6670  C  CA  . ALA F  1 146 ? 21.089  238.957 63.902 1.00 25.06 ?  145 ALA F CA  1 
ATOM   6671  C  C   . ALA F  1 146 ? 21.232  239.269 62.425 1.00 26.99 ?  145 ALA F C   1 
ATOM   6672  O  O   . ALA F  1 146 ? 20.284  239.118 61.654 1.00 28.12 ?  145 ALA F O   1 
ATOM   6673  C  CB  . ALA F  1 146 ? 21.521  237.509 64.173 1.00 21.97 ?  145 ALA F CB  1 
ATOM   6674  N  N   . CYS F  1 147 ? 22.428  239.674 62.032 1.00 28.01 ?  146 CYS F N   1 
ATOM   6675  C  CA  . CYS F  1 147 ? 22.677  240.041 60.650 1.00 27.34 ?  146 CYS F CA  1 
ATOM   6676  C  C   . CYS F  1 147 ? 24.156  239.877 60.369 1.00 31.32 ?  146 CYS F C   1 
ATOM   6677  O  O   . CYS F  1 147 ? 24.956  239.614 61.273 1.00 24.99 ?  146 CYS F O   1 
ATOM   6678  C  CB  . CYS F  1 147 ? 22.218  241.467 60.372 1.00 27.57 ?  146 CYS F CB  1 
ATOM   6679  S  SG  . CYS F  1 147 ? 23.082  242.677 61.383 1.00 32.62 ?  146 CYS F SG  1 
ATOM   6680  N  N   . GLY F  1 148 ? 24.504  240.027 59.093 1.00 28.18 ?  147 GLY F N   1 
ATOM   6681  C  CA  . GLY F  1 148 ? 25.884  239.960 58.661 1.00 23.37 ?  147 GLY F CA  1 
ATOM   6682  C  C   . GLY F  1 148 ? 25.955  240.411 57.221 1.00 27.74 ?  147 GLY F C   1 
ATOM   6683  O  O   . GLY F  1 148 ? 24.951  240.401 56.504 1.00 28.23 ?  147 GLY F O   1 
ATOM   6684  N  N   . VAL F  1 149 ? 27.146  240.833 56.820 1.00 25.55 ?  148 VAL F N   1 
ATOM   6685  C  CA  . VAL F  1 149 ? 27.373  241.234 55.444 1.00 26.07 ?  148 VAL F CA  1 
ATOM   6686  C  C   . VAL F  1 149 ? 27.650  239.988 54.616 1.00 27.91 ?  148 VAL F C   1 
ATOM   6687  O  O   . VAL F  1 149 ? 28.408  239.105 55.034 1.00 29.18 ?  148 VAL F O   1 
ATOM   6688  C  CB  . VAL F  1 149 ? 28.533  242.243 55.350 1.00 29.39 ?  148 VAL F CB  1 
ATOM   6689  C  CG1 . VAL F  1 149 ? 28.631  242.770 53.951 1.00 24.08 ?  148 VAL F CG1 1 
ATOM   6690  C  CG2 . VAL F  1 149 ? 28.322  243.421 56.304 1.00 27.23 ?  148 VAL F CG2 1 
ATOM   6691  N  N   . ILE F  1 150 ? 27.025  239.903 53.443 1.00 27.42 ?  149 ILE F N   1 
ATOM   6692  C  CA  . ILE F  1 150 ? 27.209  238.755 52.556 1.00 28.39 ?  149 ILE F CA  1 
ATOM   6693  C  C   . ILE F  1 150 ? 28.523  238.925 51.808 1.00 26.32 ?  149 ILE F C   1 
ATOM   6694  O  O   . ILE F  1 150 ? 28.708  239.901 51.069 1.00 27.77 ?  149 ILE F O   1 
ATOM   6695  C  CB  . ILE F  1 150 ? 26.027  238.619 51.584 1.00 27.75 ?  149 ILE F CB  1 
ATOM   6696  C  CG1 . ILE F  1 150 ? 24.711  238.462 52.358 1.00 28.81 ?  149 ILE F CG1 1 
ATOM   6697  C  CG2 . ILE F  1 150 ? 26.229  237.444 50.643 1.00 28.48 ?  149 ILE F CG2 1 
ATOM   6698  C  CD1 . ILE F  1 150 ? 23.473  238.675 51.491 1.00 27.48 ?  149 ILE F CD1 1 
ATOM   6699  N  N   . GLY F  1 151 ? 29.435  237.970 51.988 1.00 28.85 ?  150 GLY F N   1 
ATOM   6700  C  CA  . GLY F  1 151 ? 30.759  238.076 51.394 1.00 27.88 ?  150 GLY F CA  1 
ATOM   6701  C  C   . GLY F  1 151 ? 31.063  237.016 50.353 1.00 29.30 ?  150 GLY F C   1 
ATOM   6702  O  O   . GLY F  1 151 ? 30.443  235.951 50.341 1.00 26.79 ?  150 GLY F O   1 
ATOM   6703  N  N   . ILE F  1 152 ? 32.017  237.303 49.467 1.00 27.25 ?  151 ILE F N   1 
ATOM   6704  C  CA  . ILE F  1 152 ? 32.401  236.341 48.443 1.00 30.20 ?  151 ILE F CA  1 
ATOM   6705  C  C   . ILE F  1 152 ? 33.108  235.178 49.112 1.00 32.82 ?  151 ILE F C   1 
ATOM   6706  O  O   . ILE F  1 152 ? 34.004  235.378 49.945 1.00 30.69 ?  151 ILE F O   1 
ATOM   6707  C  CB  . ILE F  1 152 ? 33.310  236.996 47.393 1.00 33.53 ?  151 ILE F CB  1 
ATOM   6708  C  CG1 . ILE F  1 152 ? 32.508  237.956 46.525 1.00 33.39 ?  151 ILE F CG1 1 
ATOM   6709  C  CG2 . ILE F  1 152 ? 33.974  235.931 46.541 1.00 33.60 ?  151 ILE F CG2 1 
ATOM   6710  C  CD1 . ILE F  1 152 ? 33.313  239.136 46.036 1.00 39.69 ?  151 ILE F CD1 1 
ATOM   6711  N  N   . ALA F  1 153 ? 32.700  233.957 48.770 1.00 28.80 ?  152 ALA F N   1 
ATOM   6712  C  CA  . ALA F  1 153 ? 33.269  232.781 49.406 1.00 32.22 ?  152 ALA F CA  1 
ATOM   6713  C  C   . ALA F  1 153 ? 34.064  231.989 48.386 1.00 34.30 ?  152 ALA F C   1 
ATOM   6714  O  O   . ALA F  1 153 ? 33.869  232.126 47.177 1.00 33.70 ?  152 ALA F O   1 
ATOM   6715  C  CB  . ALA F  1 153 ? 32.189  231.892 50.033 1.00 33.62 ?  152 ALA F CB  1 
ATOM   6716  N  N   . GLN F  1 154 ? 34.968  231.170 48.903 1.00 39.89 ?  153 GLN F N   1 
ATOM   6717  C  CA  . GLN F  1 154 ? 35.846  230.327 48.096 1.00 47.17 ?  153 GLN F CA  1 
ATOM   6718  C  C   . GLN F  1 154 ? 35.127  229.093 47.585 1.00 54.43 ?  153 GLN F C   1 
ATOM   6719  O  O   . GLN F  1 154 ? 34.895  228.133 48.339 1.00 60.12 ?  153 GLN F O   1 
ATOM   6720  C  CB  . GLN F  1 154 ? 37.081  229.909 48.909 1.00 47.40 ?  153 GLN F CB  1 
ATOM   6721  C  CG  . GLN F  1 154 ? 38.162  229.239 48.085 1.00 50.96 ?  153 GLN F CG  1 
ATOM   6722  C  CD  . GLN F  1 154 ? 39.459  229.125 48.852 1.00 58.07 ?  153 GLN F CD  1 
ATOM   6723  O  OE1 . GLN F  1 154 ? 40.506  228.755 48.284 1.00 56.81 ?  153 GLN F OE1 1 
ATOM   6724  N  NE2 . GLN F  1 154 ? 39.415  229.466 50.151 1.00 46.63 ?  153 GLN F NE2 1 
ATOM   6725  O  OXT . GLN F  1 154 ? 34.777  229.040 46.401 1.00 63.86 ?  153 GLN F OXT 1 
ATOM   6726  N  N   . ALA G  3 2   ? -5.349  148.932 28.614 1.00 67.80 ?  1   ALA G N   1 
ATOM   6727  C  CA  . ALA G  3 2   ? -5.285  148.530 27.211 1.00 63.82 ?  1   ALA G CA  1 
ATOM   6728  C  C   . ALA G  3 2   ? -4.190  147.493 26.973 1.00 59.81 ?  1   ALA G C   1 
ATOM   6729  O  O   . ALA G  3 2   ? -3.110  147.564 27.556 1.00 63.67 ?  1   ALA G O   1 
ATOM   6730  C  CB  . ALA G  3 2   ? -5.059  149.740 26.321 1.00 57.95 ?  1   ALA G CB  1 
ATOM   6731  N  N   . THR G  3 3   ? -4.478  146.535 26.096 1.00 58.73 ?  2   THR G N   1 
ATOM   6732  C  CA  . THR G  3 3   ? -3.543  145.465 25.790 1.00 56.07 ?  2   THR G CA  1 
ATOM   6733  C  C   . THR G  3 3   ? -3.023  145.506 24.356 1.00 59.28 ?  2   THR G C   1 
ATOM   6734  O  O   . THR G  3 3   ? -2.048  144.808 24.051 1.00 52.93 ?  2   THR G O   1 
ATOM   6735  C  CB  . THR G  3 3   ? -4.204  144.105 26.078 1.00 59.99 ?  2   THR G CB  1 
ATOM   6736  O  OG1 . THR G  3 3   ? -3.226  143.056 26.000 1.00 69.15 ?  2   THR G OG1 1 
ATOM   6737  C  CG2 . THR G  3 3   ? -5.356  143.839 25.101 1.00 57.81 ?  2   THR G CG2 1 
ATOM   6738  N  N   . LYS G  3 4   ? -3.623  146.320 23.478 1.00 57.28 ?  3   LYS G N   1 
ATOM   6739  C  CA  . LYS G  3 4   ? -3.155  146.496 22.107 1.00 46.70 ?  3   LYS G CA  1 
ATOM   6740  C  C   . LYS G  3 4   ? -3.053  147.979 21.771 1.00 51.40 ?  3   LYS G C   1 
ATOM   6741  O  O   . LYS G  3 4   ? -3.908  148.781 22.161 1.00 49.54 ?  3   LYS G O   1 
ATOM   6742  C  CB  . LYS G  3 4   ? -4.081  145.806 21.100 1.00 50.71 ?  3   LYS G CB  1 
ATOM   6743  C  CG  . LYS G  3 4   ? -3.892  144.299 21.014 1.00 59.90 ?  3   LYS G CG  1 
ATOM   6744  C  CD  . LYS G  3 4   ? -4.945  143.660 20.110 1.00 67.03 ?  3   LYS G CD  1 
ATOM   6745  C  CE  . LYS G  3 4   ? -5.511  142.386 20.737 1.00 69.80 ?  3   LYS G CE  1 
ATOM   6746  N  NZ  . LYS G  3 4   ? -5.819  142.556 22.204 1.00 71.71 ?  3   LYS G NZ  1 
ATOM   6747  N  N   . ALA G  3 5   ? -1.998  148.341 21.049 1.00 47.70 ?  4   ALA G N   1 
ATOM   6748  C  CA  . ALA G  3 5   ? -1.821  149.707 20.589 1.00 48.26 ?  4   ALA G CA  1 
ATOM   6749  C  C   . ALA G  3 5   ? -1.335  149.687 19.147 1.00 46.58 ?  4   ALA G C   1 
ATOM   6750  O  O   . ALA G  3 5   ? -0.885  148.661 18.626 1.00 43.59 ?  4   ALA G O   1 
ATOM   6751  C  CB  . ALA G  3 5   ? -0.840  150.490 21.473 1.00 45.30 ?  4   ALA G CB  1 
ATOM   6752  N  N   . VAL G  3 6   ? -1.437  150.842 18.500 1.00 41.41 ?  5   VAL G N   1 
ATOM   6753  C  CA  . VAL G  3 6   ? -1.061  150.960 17.100 1.00 39.95 ?  5   VAL G CA  1 
ATOM   6754  C  C   . VAL G  3 6   ? -0.570  152.374 16.853 1.00 41.17 ?  5   VAL G C   1 
ATOM   6755  O  O   . VAL G  3 6   ? -0.993  153.328 17.517 1.00 41.03 ?  5   VAL G O   1 
ATOM   6756  C  CB  . VAL G  3 6   ? -2.238  150.604 16.164 1.00 39.00 ?  5   VAL G CB  1 
ATOM   6757  C  CG1 . VAL G  3 6   ? -3.301  151.686 16.225 1.00 37.30 ?  5   VAL G CG1 1 
ATOM   6758  C  CG2 . VAL G  3 6   ? -1.739  150.393 14.744 1.00 44.65 ?  5   VAL G CG2 1 
ATOM   6759  N  N   . CYS G  3 7   ? 0.340   152.502 15.894 1.00 35.34 ?  6   CYS G N   1 
ATOM   6760  C  CA  . CYS G  3 7   ? 0.891   153.790 15.507 1.00 39.81 ?  6   CYS G CA  1 
ATOM   6761  C  C   . CYS G  3 7   ? 1.030   153.837 13.992 1.00 38.71 ?  6   CYS G C   1 
ATOM   6762  O  O   . CYS G  3 7   ? 1.611   152.922 13.399 1.00 40.65 ?  6   CYS G O   1 
ATOM   6763  C  CB  . CYS G  3 7   ? 2.250   154.003 16.166 1.00 33.71 ?  6   CYS G CB  1 
ATOM   6764  S  SG  . CYS G  3 7   ? 2.953   155.594 15.832 1.00 41.07 ?  6   CYS G SG  1 
ATOM   6765  N  N   . VAL G  3 8   ? 0.487   154.884 13.371 1.00 40.02 ?  7   VAL G N   1 
ATOM   6766  C  CA  . VAL G  3 8   ? 0.701   155.167 11.952 1.00 34.39 ?  7   VAL G CA  1 
ATOM   6767  C  C   . VAL G  3 8   ? 1.744   156.272 11.847 1.00 41.02 ?  7   VAL G C   1 
ATOM   6768  O  O   . VAL G  3 8   ? 1.508   157.399 12.303 1.00 36.67 ?  7   VAL G O   1 
ATOM   6769  C  CB  . VAL G  3 8   ? -0.603  155.583 11.254 1.00 37.63 ?  7   VAL G CB  1 
ATOM   6770  C  CG1 . VAL G  3 8   ? -0.304  156.073 9.870  1.00 40.38 ?  7   VAL G CG1 1 
ATOM   6771  C  CG2 . VAL G  3 8   ? -1.559  154.433 11.177 1.00 40.40 ?  7   VAL G CG2 1 
ATOM   6772  N  N   . LEU G  3 9   ? 2.892   155.956 11.244 1.00 37.60 ?  8   LEU G N   1 
ATOM   6773  C  CA  . LEU G  3 9   ? 3.990   156.907 11.085 1.00 37.91 ?  8   LEU G CA  1 
ATOM   6774  C  C   . LEU G  3 9   ? 3.876   157.628 9.752  1.00 36.46 ?  8   LEU G C   1 
ATOM   6775  O  O   . LEU G  3 9   ? 3.756   156.987 8.703  1.00 35.04 ?  8   LEU G O   1 
ATOM   6776  C  CB  . LEU G  3 9   ? 5.339   156.196 11.146 1.00 38.74 ?  8   LEU G CB  1 
ATOM   6777  C  CG  . LEU G  3 9   ? 5.570   155.337 12.385 1.00 39.82 ?  8   LEU G CG  1 
ATOM   6778  C  CD1 . LEU G  3 9   ? 6.648   154.330 12.080 1.00 39.22 ?  8   LEU G CD1 1 
ATOM   6779  C  CD2 . LEU G  3 9   ? 6.009   156.232 13.472 1.00 40.17 ?  8   LEU G CD2 1 
ATOM   6780  N  N   . LYS G  3 10  ? 3.930   158.957 9.800  1.00 34.23 ?  9   LYS G N   1 
ATOM   6781  C  CA  . LYS G  3 10  ? 3.956   159.797 8.612  1.00 43.30 ?  9   LYS G CA  1 
ATOM   6782  C  C   . LYS G  3 10  ? 4.950   160.922 8.849  1.00 43.41 ?  9   LYS G C   1 
ATOM   6783  O  O   . LYS G  3 10  ? 5.239   161.282 9.992  1.00 36.82 ?  9   LYS G O   1 
ATOM   6784  C  CB  . LYS G  3 10  ? 2.582   160.404 8.284  1.00 38.69 ?  9   LYS G CB  1 
ATOM   6785  C  CG  . LYS G  3 10  ? 1.427   159.419 8.211  1.00 46.18 ?  9   LYS G CG  1 
ATOM   6786  C  CD  . LYS G  3 10  ? 1.286   158.858 6.797  1.00 58.90 ?  9   LYS G CD  1 
ATOM   6787  C  CE  . LYS G  3 10  ? 0.562   157.511 6.790  1.00 53.82 ?  9   LYS G CE  1 
ATOM   6788  N  NZ  . LYS G  3 10  ? 1.482   156.342 6.576  1.00 52.58 ?  9   LYS G NZ  1 
ATOM   6789  N  N   . GLY G  3 11  ? 5.457   161.496 7.757  1.00 38.32 ?  10  GLY G N   1 
ATOM   6790  C  CA  . GLY G  3 11  ? 6.349   162.637 7.854  1.00 37.84 ?  10  GLY G CA  1 
ATOM   6791  C  C   . GLY G  3 11  ? 6.339   163.536 6.632  1.00 40.15 ?  10  GLY G C   1 
ATOM   6792  O  O   . GLY G  3 11  ? 5.492   163.398 5.749  1.00 42.40 ?  10  GLY G O   1 
ATOM   6793  N  N   . ASP G  3 12  ? 7.291   164.460 6.569  1.00 43.92 ?  11  ASP G N   1 
ATOM   6794  C  CA  . ASP G  3 12  ? 7.316   165.411 5.463  1.00 45.86 ?  11  ASP G CA  1 
ATOM   6795  C  C   . ASP G  3 12  ? 7.743   164.740 4.164  1.00 55.57 ?  11  ASP G C   1 
ATOM   6796  O  O   . ASP G  3 12  ? 7.406   165.229 3.079  1.00 51.34 ?  11  ASP G O   1 
ATOM   6797  C  CB  . ASP G  3 12  ? 8.245   166.577 5.797  1.00 39.08 ?  11  ASP G CB  1 
ATOM   6798  C  CG  . ASP G  3 12  ? 7.848   167.296 7.089  1.00 61.25 ?  11  ASP G CG  1 
ATOM   6799  O  OD1 . ASP G  3 12  ? 6.639   167.551 7.298  1.00 59.98 ?  11  ASP G OD1 1 
ATOM   6800  O  OD2 . ASP G  3 12  ? 8.746   167.593 7.910  1.00 80.14 -1 11  ASP G OD2 1 
ATOM   6801  N  N   . GLY G  3 13  ? 8.459   163.618 4.253  1.00 47.50 ?  12  GLY G N   1 
ATOM   6802  C  CA  . GLY G  3 13  ? 8.923   162.910 3.085  1.00 37.10 ?  12  GLY G CA  1 
ATOM   6803  C  C   . GLY G  3 13  ? 8.136   161.641 2.839  1.00 37.28 ?  12  GLY G C   1 
ATOM   6804  O  O   . GLY G  3 13  ? 6.938   161.552 3.133  1.00 43.67 ?  12  GLY G O   1 
ATOM   6805  N  N   . PRO G  3 14  ? 8.805   160.630 2.291  1.00 37.78 ?  13  PRO G N   1 
ATOM   6806  C  CA  . PRO G  3 14  ? 8.136   159.374 1.924  1.00 38.09 ?  13  PRO G CA  1 
ATOM   6807  C  C   . PRO G  3 14  ? 8.076   158.307 3.008  1.00 38.63 ?  13  PRO G C   1 
ATOM   6808  O  O   . PRO G  3 14  ? 7.435   157.273 2.788  1.00 35.59 ?  13  PRO G O   1 
ATOM   6809  C  CB  . PRO G  3 14  ? 8.991   158.884 0.750  1.00 37.74 ?  13  PRO G CB  1 
ATOM   6810  C  CG  . PRO G  3 14  ? 10.358  159.472 0.998  1.00 34.67 ?  13  PRO G CG  1 
ATOM   6811  C  CD  . PRO G  3 14  ? 10.222  160.659 1.894  1.00 37.23 ?  13  PRO G CD  1 
ATOM   6812  N  N   . VAL G  3 15  ? 8.712   158.500 4.159  1.00 36.39 ?  14  VAL G N   1 
ATOM   6813  C  CA  . VAL G  3 15  ? 8.700   157.453 5.179  1.00 36.78 ?  14  VAL G CA  1 
ATOM   6814  C  C   . VAL G  3 15  ? 7.289   157.285 5.733  1.00 36.13 ?  14  VAL G C   1 
ATOM   6815  O  O   . VAL G  3 15  ? 6.662   158.247 6.198  1.00 39.06 ?  14  VAL G O   1 
ATOM   6816  C  CB  . VAL G  3 15  ? 9.701   157.771 6.289  1.00 37.37 ?  14  VAL G CB  1 
ATOM   6817  C  CG1 . VAL G  3 15  ? 9.666   156.659 7.350  1.00 34.26 ?  14  VAL G CG1 1 
ATOM   6818  C  CG2 . VAL G  3 15  ? 11.111  157.953 5.695  1.00 35.23 ?  14  VAL G CG2 1 
ATOM   6819  N  N   . GLN G  3 16  ? 6.797   156.050 5.692  1.00 38.08 ?  15  GLN G N   1 
ATOM   6820  C  CA  . GLN G  3 16  ? 5.433   155.667 6.028  1.00 36.96 ?  15  GLN G CA  1 
ATOM   6821  C  C   . GLN G  3 16  ? 5.485   154.302 6.694  1.00 44.94 ?  15  GLN G C   1 
ATOM   6822  O  O   . GLN G  3 16  ? 6.293   153.453 6.303  1.00 36.69 ?  15  GLN G O   1 
ATOM   6823  C  CB  . GLN G  3 16  ? 4.553   155.540 4.777  1.00 41.43 ?  15  GLN G CB  1 
ATOM   6824  C  CG  . GLN G  3 16  ? 3.822   156.782 4.328  1.00 57.79 ?  15  GLN G CG  1 
ATOM   6825  C  CD  . GLN G  3 16  ? 2.685   156.442 3.365  1.00 63.42 ?  15  GLN G CD  1 
ATOM   6826  O  OE1 . GLN G  3 16  ? 2.823   155.561 2.515  1.00 63.15 ?  15  GLN G OE1 1 
ATOM   6827  N  NE2 . GLN G  3 16  ? 1.554   157.136 3.505  1.00 68.60 ?  15  GLN G NE2 1 
ATOM   6828  N  N   . GLY G  3 17  ? 4.609   154.063 7.661  1.00 41.75 ?  16  GLY G N   1 
ATOM   6829  C  CA  . GLY G  3 17  ? 4.586   152.751 8.274  1.00 43.89 ?  16  GLY G CA  1 
ATOM   6830  C  C   . GLY G  3 17  ? 3.506   152.620 9.323  1.00 42.47 ?  16  GLY G C   1 
ATOM   6831  O  O   . GLY G  3 17  ? 2.979   153.611 9.844  1.00 42.60 ?  16  GLY G O   1 
ATOM   6832  N  N   . ILE G  3 18  ? 3.195   151.365 9.627  1.00 38.59 ?  17  ILE G N   1 
ATOM   6833  C  CA  . ILE G  3 18  ? 2.267   150.997 10.683 1.00 41.80 ?  17  ILE G CA  1 
ATOM   6834  C  C   . ILE G  3 18  ? 3.010   150.077 11.649 1.00 46.58 ?  17  ILE G C   1 
ATOM   6835  O  O   . ILE G  3 18  ? 3.578   149.062 11.227 1.00 41.19 ?  17  ILE G O   1 
ATOM   6836  C  CB  . ILE G  3 18  ? 1.012   150.317 10.118 1.00 41.16 ?  17  ILE G CB  1 
ATOM   6837  C  CG1 . ILE G  3 18  ? 0.113   151.363 9.456  1.00 43.35 ?  17  ILE G CG1 1 
ATOM   6838  C  CG2 . ILE G  3 18  ? 0.258   149.580 11.224 1.00 41.13 ?  17  ILE G CG2 1 
ATOM   6839  C  CD1 . ILE G  3 18  ? -0.675  150.824 8.291  1.00 45.34 ?  17  ILE G CD1 1 
ATOM   6840  N  N   . ILE G  3 19  ? 3.035   150.450 12.933 1.00 38.98 ?  18  ILE G N   1 
ATOM   6841  C  CA  . ILE G  3 19  ? 3.693   149.679 13.980 1.00 39.25 ?  18  ILE G CA  1 
ATOM   6842  C  C   . ILE G  3 19  ? 2.645   149.263 15.011 1.00 46.14 ?  18  ILE G C   1 
ATOM   6843  O  O   . ILE G  3 19  ? 1.897   150.106 15.519 1.00 44.39 ?  18  ILE G O   1 
ATOM   6844  C  CB  . ILE G  3 19  ? 4.825   150.478 14.653 1.00 43.63 ?  18  ILE G CB  1 
ATOM   6845  C  CG1 . ILE G  3 19  ? 5.915   150.854 13.642 1.00 42.05 ?  18  ILE G CG1 1 
ATOM   6846  C  CG2 . ILE G  3 19  ? 5.429   149.677 15.775 1.00 41.88 ?  18  ILE G CG2 1 
ATOM   6847  C  CD1 . ILE G  3 19  ? 6.737   149.676 13.125 1.00 43.85 ?  18  ILE G CD1 1 
ATOM   6848  N  N   . ASN G  3 20  ? 2.595   147.968 15.318 1.00 45.66 ?  19  ASN G N   1 
ATOM   6849  C  CA  . ASN G  3 20  ? 1.635   147.419 16.265 1.00 44.90 ?  19  ASN G CA  1 
ATOM   6850  C  C   . ASN G  3 20  ? 2.308   147.106 17.595 1.00 45.87 ?  19  ASN G C   1 
ATOM   6851  O  O   . ASN G  3 20  ? 3.503   146.798 17.653 1.00 45.86 ?  19  ASN G O   1 
ATOM   6852  C  CB  . ASN G  3 20  ? 0.986   146.152 15.719 1.00 41.71 ?  19  ASN G CB  1 
ATOM   6853  C  CG  . ASN G  3 20  ? 0.349   146.369 14.383 1.00 44.96 ?  19  ASN G CG  1 
ATOM   6854  O  OD1 . ASN G  3 20  ? -0.791  146.836 14.287 1.00 46.18 ?  19  ASN G OD1 1 
ATOM   6855  N  ND2 . ASN G  3 20  ? 1.081   146.033 13.327 1.00 46.89 ?  19  ASN G ND2 1 
ATOM   6856  N  N   . PHE G  3 21  ? 1.520   147.194 18.667 1.00 48.39 ?  20  PHE G N   1 
ATOM   6857  C  CA  . PHE G  3 21  ? 1.984   146.893 20.014 1.00 45.79 ?  20  PHE G CA  1 
ATOM   6858  C  C   . PHE G  3 21  ? 1.010   145.923 20.662 1.00 46.69 ?  20  PHE G C   1 
ATOM   6859  O  O   . PHE G  3 21  ? -0.209  146.072 20.522 1.00 45.71 ?  20  PHE G O   1 
ATOM   6860  C  CB  . PHE G  3 21  ? 2.087   148.141 20.883 1.00 38.43 ?  20  PHE G CB  1 
ATOM   6861  C  CG  . PHE G  3 21  ? 3.037   149.182 20.366 1.00 46.29 ?  20  PHE G CG  1 
ATOM   6862  C  CD1 . PHE G  3 21  ? 2.646   150.072 19.370 1.00 48.07 ?  20  PHE G CD1 1 
ATOM   6863  C  CD2 . PHE G  3 21  ? 4.315   149.286 20.888 1.00 41.55 ?  20  PHE G CD2 1 
ATOM   6864  C  CE1 . PHE G  3 21  ? 3.523   151.055 18.905 1.00 42.65 ?  20  PHE G CE1 1 
ATOM   6865  C  CE2 . PHE G  3 21  ? 5.192   150.257 20.436 1.00 44.92 ?  20  PHE G CE2 1 
ATOM   6866  C  CZ  . PHE G  3 21  ? 4.797   151.147 19.445 1.00 43.04 ?  20  PHE G CZ  1 
ATOM   6867  N  N   . GLU G  3 22  ? 1.546   144.932 21.371 1.00 50.79 ?  21  GLU G N   1 
ATOM   6868  C  CA  . GLU G  3 22  ? 0.716   143.997 22.126 1.00 51.76 ?  21  GLU G CA  1 
ATOM   6869  C  C   . GLU G  3 22  ? 1.402   143.681 23.444 1.00 53.52 ?  21  GLU G C   1 
ATOM   6870  O  O   . GLU G  3 22  ? 2.562   143.250 23.461 1.00 48.79 ?  21  GLU G O   1 
ATOM   6871  C  CB  . GLU G  3 22  ? 0.447   142.712 21.338 1.00 56.82 ?  21  GLU G CB  1 
ATOM   6872  C  CG  . GLU G  3 22  ? -0.598  141.810 21.988 1.00 58.85 ?  21  GLU G CG  1 
ATOM   6873  C  CD  . GLU G  3 22  ? -1.256  140.858 20.996 1.00 73.58 ?  21  GLU G CD  1 
ATOM   6874  O  OE1 . GLU G  3 22  ? -0.537  140.267 20.151 1.00 69.57 ?  21  GLU G OE1 1 
ATOM   6875  O  OE2 . GLU G  3 22  ? -2.498  140.701 21.064 1.00 80.16 -1 21  GLU G OE2 1 
ATOM   6876  N  N   . GLN G  3 23  ? 0.690   143.922 24.541 1.00 57.60 ?  22  GLN G N   1 
ATOM   6877  C  CA  . GLN G  3 23  ? 1.141   143.587 25.887 1.00 57.70 ?  22  GLN G CA  1 
ATOM   6878  C  C   . GLN G  3 23  ? 0.113   142.621 26.470 1.00 64.60 ?  22  GLN G C   1 
ATOM   6879  O  O   . GLN G  3 23  ? -0.863  143.051 27.092 1.00 65.26 ?  22  GLN G O   1 
ATOM   6880  C  CB  . GLN G  3 23  ? 1.299   144.827 26.749 1.00 53.82 ?  22  GLN G CB  1 
ATOM   6881  C  CG  . GLN G  3 23  ? 1.896   144.533 28.112 1.00 58.39 ?  22  GLN G CG  1 
ATOM   6882  C  CD  . GLN G  3 23  ? 2.251   145.794 28.870 1.00 59.38 ?  22  GLN G CD  1 
ATOM   6883  O  OE1 . GLN G  3 23  ? 1.490   146.766 28.870 1.00 60.63 ?  22  GLN G OE1 1 
ATOM   6884  N  NE2 . GLN G  3 23  ? 3.418   145.790 29.517 1.00 57.47 ?  22  GLN G NE2 1 
ATOM   6885  N  N   . LYS G  3 24  ? 0.343   141.315 26.266 1.00 65.09 ?  23  LYS G N   1 
ATOM   6886  C  CA  . LYS G  3 24  ? -0.627  140.303 26.690 1.00 64.69 ?  23  LYS G CA  1 
ATOM   6887  C  C   . LYS G  3 24  ? -0.794  140.277 28.208 1.00 70.49 ?  23  LYS G C   1 
ATOM   6888  O  O   . LYS G  3 24  ? -1.907  140.085 28.715 1.00 66.32 ?  23  LYS G O   1 
ATOM   6889  C  CB  . LYS G  3 24  ? -0.205  138.923 26.177 1.00 57.53 ?  23  LYS G CB  1 
ATOM   6890  N  N   . GLU G  3 25  ? 0.291   140.477 28.953 1.00 67.97 ?  24  GLU G N   1 
ATOM   6891  C  CA  . GLU G  3 25  ? 0.258   140.384 30.407 1.00 72.16 ?  24  GLU G CA  1 
ATOM   6892  C  C   . GLU G  3 25  ? 0.465   141.757 31.032 1.00 65.02 ?  24  GLU G C   1 
ATOM   6893  O  O   . GLU G  3 25  ? 1.393   142.479 30.653 1.00 61.37 ?  24  GLU G O   1 
ATOM   6894  C  CB  . GLU G  3 25  ? 1.315   139.399 30.917 1.00 75.97 ?  24  GLU G CB  1 
ATOM   6895  C  CG  . GLU G  3 25  ? 0.810   138.475 32.033 1.00 73.98 ?  24  GLU G CG  1 
ATOM   6896  C  CD  . GLU G  3 25  ? -0.439  137.688 31.634 1.00 81.80 ?  24  GLU G CD  1 
ATOM   6897  O  OE1 . GLU G  3 25  ? -0.458  137.109 30.520 1.00 76.97 ?  24  GLU G OE1 1 
ATOM   6898  O  OE2 . GLU G  3 25  ? -1.404  137.654 32.434 1.00 86.96 -1 24  GLU G OE2 1 
ATOM   6899  N  N   . SER G  3 26  ? -0.382  142.077 32.022 1.00 68.53 ?  25  SER G N   1 
ATOM   6900  C  CA  . SER G  3 26  ? -0.487  143.355 32.734 1.00 67.62 ?  25  SER G CA  1 
ATOM   6901  C  C   . SER G  3 26  ? 0.827   144.099 32.948 1.00 63.91 ?  25  SER G C   1 
ATOM   6902  O  O   . SER G  3 26  ? 0.834   145.330 33.065 1.00 73.92 ?  25  SER G O   1 
ATOM   6903  C  CB  . SER G  3 26  ? -1.156  143.133 34.100 1.00 71.09 ?  25  SER G CB  1 
ATOM   6904  O  OG  . SER G  3 26  ? -1.692  144.342 34.628 1.00 75.51 ?  25  SER G OG  1 
ATOM   6905  N  N   . ASN G  3 27  ? 1.943   143.379 33.029 1.00 65.87 ?  26  ASN G N   1 
ATOM   6906  C  CA  . ASN G  3 27  ? 3.225   144.073 33.049 1.00 67.84 ?  26  ASN G CA  1 
ATOM   6907  C  C   . ASN G  3 27  ? 4.309   143.260 32.353 1.00 69.76 ?  26  ASN G C   1 
ATOM   6908  O  O   . ASN G  3 27  ? 5.479   143.311 32.752 1.00 68.65 ?  26  ASN G O   1 
ATOM   6909  C  CB  . ASN G  3 27  ? 3.642   144.409 34.479 1.00 71.70 ?  26  ASN G CB  1 
ATOM   6910  C  CG  . ASN G  3 27  ? 4.575   145.600 34.540 1.00 75.40 ?  26  ASN G CG  1 
ATOM   6911  O  OD1 . ASN G  3 27  ? 5.264   145.920 33.563 1.00 75.95 ?  26  ASN G OD1 1 
ATOM   6912  N  ND2 . ASN G  3 27  ? 4.594   146.276 35.686 1.00 71.53 ?  26  ASN G ND2 1 
ATOM   6913  N  N   . GLY G  3 28  ? 3.946   142.520 31.308 1.00 67.72 ?  27  GLY G N   1 
ATOM   6914  C  CA  . GLY G  3 28  ? 4.921   141.761 30.567 1.00 66.73 ?  27  GLY G CA  1 
ATOM   6915  C  C   . GLY G  3 28  ? 5.668   142.616 29.563 1.00 68.61 ?  27  GLY G C   1 
ATOM   6916  O  O   . GLY G  3 28  ? 5.506   143.846 29.476 1.00 64.93 ?  27  GLY G O   1 
ATOM   6917  N  N   . PRO G  3 29  ? 6.520   141.962 28.782 1.00 68.32 ?  28  PRO G N   1 
ATOM   6918  C  CA  . PRO G  3 29  ? 7.163   142.661 27.667 1.00 64.65 ?  28  PRO G CA  1 
ATOM   6919  C  C   . PRO G  3 29  ? 6.122   143.046 26.626 1.00 61.85 ?  28  PRO G C   1 
ATOM   6920  O  O   . PRO G  3 29  ? 5.050   142.444 26.525 1.00 51.23 ?  28  PRO G O   1 
ATOM   6921  C  CB  . PRO G  3 29  ? 8.163   141.632 27.115 1.00 63.18 ?  28  PRO G CB  1 
ATOM   6922  C  CG  . PRO G  3 29  ? 8.164   140.475 28.114 1.00 62.44 ?  28  PRO G CG  1 
ATOM   6923  C  CD  . PRO G  3 29  ? 6.837   140.527 28.806 1.00 60.81 ?  28  PRO G CD  1 
ATOM   6924  N  N   . VAL G  3 30  ? 6.440   144.079 25.853 1.00 62.10 ?  29  VAL G N   1 
ATOM   6925  C  CA  . VAL G  3 30  ? 5.579   144.519 24.763 1.00 53.60 ?  29  VAL G CA  1 
ATOM   6926  C  C   . VAL G  3 30  ? 6.097   143.938 23.457 1.00 47.76 ?  29  VAL G C   1 
ATOM   6927  O  O   . VAL G  3 30  ? 7.288   144.042 23.140 1.00 50.39 ?  29  VAL G O   1 
ATOM   6928  C  CB  . VAL G  3 30  ? 5.495   146.050 24.698 1.00 54.97 ?  29  VAL G CB  1 
ATOM   6929  C  CG1 . VAL G  3 30  ? 4.321   146.460 23.813 1.00 51.76 ?  29  VAL G CG1 1 
ATOM   6930  C  CG2 . VAL G  3 30  ? 5.342   146.611 26.114 1.00 51.89 ?  29  VAL G CG2 1 
ATOM   6931  N  N   . LYS G  3 31  ? 5.208   143.295 22.721 1.00 44.38 ?  30  LYS G N   1 
ATOM   6932  C  CA  . LYS G  3 31  ? 5.500   142.853 21.373 1.00 53.72 ?  30  LYS G CA  1 
ATOM   6933  C  C   . LYS G  3 31  ? 5.277   144.036 20.432 1.00 54.49 ?  30  LYS G C   1 
ATOM   6934  O  O   . LYS G  3 31  ? 4.181   144.608 20.400 1.00 54.16 ?  30  LYS G O   1 
ATOM   6935  C  CB  . LYS G  3 31  ? 4.605   141.665 21.019 1.00 54.32 ?  30  LYS G CB  1 
ATOM   6936  C  CG  . LYS G  3 31  ? 5.155   140.720 19.965 1.00 61.03 ?  30  LYS G CG  1 
ATOM   6937  C  CD  . LYS G  3 31  ? 4.036   140.223 19.052 1.00 67.75 ?  30  LYS G CD  1 
ATOM   6938  C  CE  . LYS G  3 31  ? 4.543   139.241 17.989 1.00 63.94 ?  30  LYS G CE  1 
ATOM   6939  N  NZ  . LYS G  3 31  ? 3.633   139.224 16.793 1.00 61.55 ?  30  LYS G NZ  1 
ATOM   6940  N  N   . VAL G  3 32  ? 6.324   144.426 19.703 1.00 50.14 ?  31  VAL G N   1 
ATOM   6941  C  CA  . VAL G  3 32  ? 6.286   145.552 18.770 1.00 50.72 ?  31  VAL G CA  1 
ATOM   6942  C  C   . VAL G  3 32  ? 6.582   145.033 17.371 1.00 47.56 ?  31  VAL G C   1 
ATOM   6943  O  O   . VAL G  3 32  ? 7.650   144.457 17.135 1.00 53.24 ?  31  VAL G O   1 
ATOM   6944  C  CB  . VAL G  3 32  ? 7.296   146.638 19.158 1.00 46.63 ?  31  VAL G CB  1 
ATOM   6945  C  CG1 . VAL G  3 32  ? 7.096   147.879 18.281 1.00 45.26 ?  31  VAL G CG1 1 
ATOM   6946  C  CG2 . VAL G  3 32  ? 7.178   146.961 20.643 1.00 40.97 ?  31  VAL G CG2 1 
ATOM   6947  N  N   . TRP G  3 33  ? 5.660   145.250 16.439 1.00 50.07 ?  32  TRP G N   1 
ATOM   6948  C  CA  . TRP G  3 33  ? 5.894   144.738 15.094 1.00 47.08 ?  32  TRP G CA  1 
ATOM   6949  C  C   . TRP G  3 33  ? 5.134   145.551 14.054 1.00 45.57 ?  32  TRP G C   1 
ATOM   6950  O  O   . TRP G  3 33  ? 4.140   146.219 14.346 1.00 47.84 ?  32  TRP G O   1 
ATOM   6951  C  CB  . TRP G  3 33  ? 5.510   143.260 14.983 1.00 47.46 ?  32  TRP G CB  1 
ATOM   6952  C  CG  . TRP G  3 33  ? 4.043   143.034 14.809 1.00 44.48 ?  32  TRP G CG  1 
ATOM   6953  C  CD1 . TRP G  3 33  ? 3.378   142.808 13.639 1.00 43.80 ?  32  TRP G CD1 1 
ATOM   6954  C  CD2 . TRP G  3 33  ? 3.057   143.014 15.844 1.00 44.81 ?  32  TRP G CD2 1 
ATOM   6955  N  NE1 . TRP G  3 33  ? 2.033   142.650 13.884 1.00 45.77 ?  32  TRP G NE1 1 
ATOM   6956  C  CE2 . TRP G  3 33  ? 1.811   142.768 15.231 1.00 41.61 ?  32  TRP G CE2 1 
ATOM   6957  C  CE3 . TRP G  3 33  ? 3.108   143.175 17.234 1.00 48.53 ?  32  TRP G CE3 1 
ATOM   6958  C  CZ2 . TRP G  3 33  ? 0.625   142.684 15.955 1.00 46.17 ?  32  TRP G CZ2 1 
ATOM   6959  C  CZ3 . TRP G  3 33  ? 1.926   143.094 17.955 1.00 49.11 ?  32  TRP G CZ3 1 
ATOM   6960  C  CH2 . TRP G  3 33  ? 0.702   142.847 17.315 1.00 44.94 ?  32  TRP G CH2 1 
ATOM   6961  N  N   . GLY G  3 34  ? 5.607   145.456 12.834 1.00 47.67 ?  33  GLY G N   1 
ATOM   6962  C  CA  . GLY G  3 34  ? 5.009   146.137 11.713 1.00 45.36 ?  33  GLY G CA  1 
ATOM   6963  C  C   . GLY G  3 34  ? 6.063   146.372 10.652 1.00 48.10 ?  33  GLY G C   1 
ATOM   6964  O  O   . GLY G  3 34  ? 7.053   145.645 10.581 1.00 44.66 ?  33  GLY G O   1 
ATOM   6965  N  N   . SER G  3 35  ? 5.852   147.418 9.862  1.00 42.34 ?  34  SER G N   1 
ATOM   6966  C  CA  . SER G  3 35  ? 6.752   147.662 8.754  1.00 40.70 ?  34  SER G CA  1 
ATOM   6967  C  C   . SER G  3 35  ? 6.828   149.153 8.476  1.00 43.86 ?  34  SER G C   1 
ATOM   6968  O  O   . SER G  3 35  ? 5.867   149.892 8.692  1.00 45.36 ?  34  SER G O   1 
ATOM   6969  C  CB  . SER G  3 35  ? 6.297   146.908 7.506  1.00 46.10 ?  34  SER G CB  1 
ATOM   6970  O  OG  . SER G  3 35  ? 7.207   147.157 6.459  1.00 55.67 ?  34  SER G OG  1 
ATOM   6971  N  N   . ILE G  3 36  ? 7.990   149.590 8.015  1.00 40.64 ?  35  ILE G N   1 
ATOM   6972  C  CA  . ILE G  3 36  ? 8.204   150.972 7.613  1.00 45.40 ?  35  ILE G CA  1 
ATOM   6973  C  C   . ILE G  3 36  ? 8.793   150.954 6.214  1.00 47.98 ?  35  ILE G C   1 
ATOM   6974  O  O   . ILE G  3 36  ? 9.670   150.135 5.916  1.00 44.30 ?  35  ILE G O   1 
ATOM   6975  C  CB  . ILE G  3 36  ? 9.134   151.707 8.592  1.00 38.80 ?  35  ILE G CB  1 
ATOM   6976  C  CG1 . ILE G  3 36  ? 8.662   151.491 10.022 1.00 39.60 ?  35  ILE G CG1 1 
ATOM   6977  C  CG2 . ILE G  3 36  ? 9.184   153.190 8.275  1.00 40.87 ?  35  ILE G CG2 1 
ATOM   6978  C  CD1 . ILE G  3 36  ? 9.544   152.165 11.057 1.00 39.33 ?  35  ILE G CD1 1 
ATOM   6979  N  N   . LYS G  3 37  ? 8.292   151.825 5.342  1.00 43.11 ?  36  LYS G N   1 
ATOM   6980  C  CA  . LYS G  3 37  ? 8.824   151.916 3.993  1.00 37.88 ?  36  LYS G CA  1 
ATOM   6981  C  C   . LYS G  3 37  ? 9.255   153.350 3.713  1.00 43.17 ?  36  LYS G C   1 
ATOM   6982  O  O   . LYS G  3 37  ? 8.952   154.281 4.474  1.00 35.75 ?  36  LYS G O   1 
ATOM   6983  C  CB  . LYS G  3 37  ? 7.811   151.430 2.951  1.00 43.93 ?  36  LYS G CB  1 
ATOM   6984  C  CG  . LYS G  3 37  ? 6.646   152.369 2.687  1.00 43.43 ?  36  LYS G CG  1 
ATOM   6985  C  CD  . LYS G  3 37  ? 5.536   151.617 1.947  1.00 44.36 ?  36  LYS G CD  1 
ATOM   6986  C  CE  . LYS G  3 37  ? 4.252   152.433 1.899  1.00 51.34 ?  36  LYS G CE  1 
ATOM   6987  N  NZ  . LYS G  3 37  ? 3.112   151.643 1.343  1.00 56.63 ?  36  LYS G NZ  1 
ATOM   6988  N  N   . GLY G  3 38  ? 9.987   153.518 2.613  1.00 35.37 ?  37  GLY G N   1 
ATOM   6989  C  CA  . GLY G  3 38  ? 10.478  154.827 2.244  1.00 40.36 ?  37  GLY G CA  1 
ATOM   6990  C  C   . GLY G  3 38  ? 11.779  155.243 2.888  1.00 37.94 ?  37  GLY G C   1 
ATOM   6991  O  O   . GLY G  3 38  ? 12.145  156.422 2.797  1.00 36.77 ?  37  GLY G O   1 
ATOM   6992  N  N   . LEU G  3 39  ? 12.496  154.324 3.526  1.00 40.07 ?  38  LEU G N   1 
ATOM   6993  C  CA  . LEU G  3 39  ? 13.746  154.644 4.203  1.00 40.20 ?  38  LEU G CA  1 
ATOM   6994  C  C   . LEU G  3 39  ? 14.930  154.359 3.283  1.00 38.95 ?  38  LEU G C   1 
ATOM   6995  O  O   . LEU G  3 39  ? 14.814  153.633 2.296  1.00 39.77 ?  38  LEU G O   1 
ATOM   6996  C  CB  . LEU G  3 39  ? 13.882  153.829 5.496  1.00 43.08 ?  38  LEU G CB  1 
ATOM   6997  C  CG  . LEU G  3 39  ? 12.874  154.036 6.644  1.00 38.05 ?  38  LEU G CG  1 
ATOM   6998  C  CD1 . LEU G  3 39  ? 12.733  152.767 7.483  1.00 39.65 ?  38  LEU G CD1 1 
ATOM   6999  C  CD2 . LEU G  3 39  ? 13.284  155.199 7.527  1.00 43.49 ?  38  LEU G CD2 1 
ATOM   7000  N  N   . THR G  3 40  ? 16.081  154.943 3.612  1.00 38.52 ?  39  THR G N   1 
ATOM   7001  C  CA  . THR G  3 40  ? 17.306  154.516 2.950  1.00 42.01 ?  39  THR G CA  1 
ATOM   7002  C  C   . THR G  3 40  ? 17.806  153.224 3.590  1.00 48.82 ?  39  THR G C   1 
ATOM   7003  O  O   . THR G  3 40  ? 17.601  152.980 4.785  1.00 45.22 ?  39  THR G O   1 
ATOM   7004  C  CB  . THR G  3 40  ? 18.385  155.594 3.024  1.00 43.56 ?  39  THR G CB  1 
ATOM   7005  O  OG1 . THR G  3 40  ? 18.623  155.953 4.395  1.00 46.56 ?  39  THR G OG1 1 
ATOM   7006  C  CG2 . THR G  3 40  ? 17.950  156.827 2.245  1.00 37.56 ?  39  THR G CG2 1 
ATOM   7007  N  N   . GLU G  3 41  ? 18.427  152.376 2.771  1.00 44.38 ?  40  GLU G N   1 
ATOM   7008  C  CA  . GLU G  3 41  ? 18.998  151.128 3.264  1.00 47.12 ?  40  GLU G CA  1 
ATOM   7009  C  C   . GLU G  3 41  ? 19.915  151.387 4.450  1.00 45.74 ?  40  GLU G C   1 
ATOM   7010  O  O   . GLU G  3 41  ? 20.688  152.352 4.458  1.00 49.64 ?  40  GLU G O   1 
ATOM   7011  C  CB  . GLU G  3 41  ? 19.781  150.434 2.149  1.00 50.70 ?  40  GLU G CB  1 
ATOM   7012  C  CG  . GLU G  3 41  ? 20.005  148.949 2.373  1.00 51.48 ?  40  GLU G CG  1 
ATOM   7013  C  CD  . GLU G  3 41  ? 20.906  148.336 1.314  1.00 58.15 ?  40  GLU G CD  1 
ATOM   7014  O  OE1 . GLU G  3 41  ? 20.996  148.914 0.204  1.00 56.75 ?  40  GLU G OE1 1 
ATOM   7015  O  OE2 . GLU G  3 41  ? 21.515  147.274 1.588  1.00 60.78 -1 40  GLU G OE2 1 
ATOM   7016  N  N   . GLY G  3 42  ? 19.824  150.519 5.457  1.00 49.35 ?  41  GLY G N   1 
ATOM   7017  C  CA  . GLY G  3 42  ? 20.663  150.680 6.626  1.00 42.32 ?  41  GLY G CA  1 
ATOM   7018  C  C   . GLY G  3 42  ? 19.883  150.914 7.905  1.00 46.13 ?  41  GLY G C   1 
ATOM   7019  O  O   . GLY G  3 42  ? 18.664  150.719 7.942  1.00 42.71 ?  41  GLY G O   1 
ATOM   7020  N  N   . LEU G  3 43  ? 20.581  151.351 8.950  1.00 43.89 ?  42  LEU G N   1 
ATOM   7021  C  CA  . LEU G  3 43  ? 20.013  151.504 10.281 1.00 50.22 ?  42  LEU G CA  1 
ATOM   7022  C  C   . LEU G  3 43  ? 19.370  152.872 10.460 1.00 45.39 ?  42  LEU G C   1 
ATOM   7023  O  O   . LEU G  3 43  ? 19.826  153.873 9.900  1.00 48.10 ?  42  LEU G O   1 
ATOM   7024  C  CB  . LEU G  3 43  ? 21.092  151.316 11.348 1.00 48.85 ?  42  LEU G CB  1 
ATOM   7025  C  CG  . LEU G  3 43  ? 21.648  149.907 11.479 1.00 48.00 ?  42  LEU G CG  1 
ATOM   7026  C  CD1 . LEU G  3 43  ? 22.744  149.911 12.518 1.00 54.79 ?  42  LEU G CD1 1 
ATOM   7027  C  CD2 . LEU G  3 43  ? 20.552  148.946 11.860 1.00 52.24 ?  42  LEU G CD2 1 
ATOM   7028  N  N   . HIS G  3 44  ? 18.313  152.908 11.267 1.00 44.74 ?  43  HIS G N   1 
ATOM   7029  C  CA  . HIS G  3 44  ? 17.635  154.155 11.590 1.00 44.38 ?  43  HIS G CA  1 
ATOM   7030  C  C   . HIS G  3 44  ? 17.174  154.121 13.038 1.00 47.54 ?  43  HIS G C   1 
ATOM   7031  O  O   . HIS G  3 44  ? 16.597  153.128 13.485 1.00 47.63 ?  43  HIS G O   1 
ATOM   7032  C  CB  . HIS G  3 44  ? 16.435  154.392 10.661 1.00 41.11 ?  43  HIS G CB  1 
ATOM   7033  C  CG  . HIS G  3 44  ? 16.813  154.573 9.221  1.00 43.77 ?  43  HIS G CG  1 
ATOM   7034  N  ND1 . HIS G  3 44  ? 17.233  155.783 8.706  1.00 49.81 ?  43  HIS G ND1 1 
ATOM   7035  C  CD2 . HIS G  3 44  ? 16.831  153.696 8.187  1.00 42.54 ?  43  HIS G CD2 1 
ATOM   7036  C  CE1 . HIS G  3 44  ? 17.491  155.642 7.415  1.00 43.73 ?  43  HIS G CE1 1 
ATOM   7037  N  NE2 . HIS G  3 44  ? 17.255  154.386 7.075  1.00 42.45 ?  43  HIS G NE2 1 
ATOM   7038  N  N   . GLY G  3 45  ? 17.414  155.219 13.752 1.00 49.66 ?  44  GLY G N   1 
ATOM   7039  C  CA  . GLY G  3 45  ? 16.934  155.327 15.119 1.00 48.84 ?  44  GLY G CA  1 
ATOM   7040  C  C   . GLY G  3 45  ? 15.428  155.174 15.210 1.00 50.28 ?  44  GLY G C   1 
ATOM   7041  O  O   . GLY G  3 45  ? 14.678  155.539 14.302 1.00 49.05 ?  44  GLY G O   1 
ATOM   7042  N  N   . PHE G  3 46  ? 14.983  154.637 16.343 1.00 47.52 ?  45  PHE G N   1 
ATOM   7043  C  CA  . PHE G  3 46  ? 13.595  154.222 16.519 1.00 36.81 ?  45  PHE G CA  1 
ATOM   7044  C  C   . PHE G  3 46  ? 13.282  154.442 17.997 1.00 51.88 ?  45  PHE G C   1 
ATOM   7045  O  O   . PHE G  3 46  ? 13.666  153.625 18.839 1.00 52.41 ?  45  PHE G O   1 
ATOM   7046  C  CB  . PHE G  3 46  ? 13.434  152.766 16.095 1.00 41.31 ?  45  PHE G CB  1 
ATOM   7047  C  CG  . PHE G  3 46  ? 12.007  152.310 15.919 1.00 46.99 ?  45  PHE G CG  1 
ATOM   7048  C  CD1 . PHE G  3 46  ? 11.089  153.081 15.239 1.00 42.45 ?  45  PHE G CD1 1 
ATOM   7049  C  CD2 . PHE G  3 46  ? 11.598  151.076 16.408 1.00 45.14 ?  45  PHE G CD2 1 
ATOM   7050  C  CE1 . PHE G  3 46  ? 9.784   152.644 15.069 1.00 41.78 ?  45  PHE G CE1 1 
ATOM   7051  C  CE2 . PHE G  3 46  ? 10.294  150.636 16.237 1.00 40.91 ?  45  PHE G CE2 1 
ATOM   7052  C  CZ  . PHE G  3 46  ? 9.388   151.429 15.564 1.00 39.04 ?  45  PHE G CZ  1 
ATOM   7053  N  N   . HIS G  3 47  ? 12.613  155.553 18.309 1.00 51.87 ?  46  HIS G N   1 
ATOM   7054  C  CA  . HIS G  3 47  ? 12.466  155.984 19.691 1.00 45.68 ?  46  HIS G CA  1 
ATOM   7055  C  C   . HIS G  3 47  ? 11.042  156.421 19.987 1.00 48.18 ?  46  HIS G C   1 
ATOM   7056  O  O   . HIS G  3 47  ? 10.382  157.033 19.143 1.00 45.81 ?  46  HIS G O   1 
ATOM   7057  C  CB  . HIS G  3 47  ? 13.396  157.153 20.012 1.00 49.44 ?  46  HIS G CB  1 
ATOM   7058  C  CG  . HIS G  3 47  ? 14.844  156.859 19.787 1.00 55.64 ?  46  HIS G CG  1 
ATOM   7059  N  ND1 . HIS G  3 47  ? 15.656  156.331 20.768 1.00 59.11 ?  46  HIS G ND1 1 
ATOM   7060  C  CD2 . HIS G  3 47  ? 15.636  157.051 18.704 1.00 55.48 ?  46  HIS G CD2 1 
ATOM   7061  C  CE1 . HIS G  3 47  ? 16.883  156.196 20.295 1.00 65.00 ?  46  HIS G CE1 1 
ATOM   7062  N  NE2 . HIS G  3 47  ? 16.898  156.625 19.044 1.00 63.83 ?  46  HIS G NE2 1 
ATOM   7063  N  N   . VAL G  3 48  ? 10.589  156.129 21.201 1.00 45.06 ?  47  VAL G N   1 
ATOM   7064  C  CA  . VAL G  3 48  ? 9.398   156.769 21.752 1.00 47.00 ?  47  VAL G CA  1 
ATOM   7065  C  C   . VAL G  3 48  ? 9.796   158.126 22.305 1.00 46.61 ?  47  VAL G C   1 
ATOM   7066  O  O   . VAL G  3 48  ? 10.735  158.230 23.104 1.00 49.91 ?  47  VAL G O   1 
ATOM   7067  C  CB  . VAL G  3 48  ? 8.761   155.903 22.848 1.00 41.94 ?  47  VAL G CB  1 
ATOM   7068  C  CG1 . VAL G  3 48  ? 7.699   156.698 23.571 1.00 47.48 ?  47  VAL G CG1 1 
ATOM   7069  C  CG2 . VAL G  3 48  ? 8.169   154.655 22.261 1.00 39.68 ?  47  VAL G CG2 1 
ATOM   7070  N  N   . HIS G  3 49  ? 9.096   159.176 21.881 1.00 44.62 ?  48  HIS G N   1 
ATOM   7071  C  CA  . HIS G  3 49  ? 9.347   160.517 22.383 1.00 36.78 ?  48  HIS G CA  1 
ATOM   7072  C  C   . HIS G  3 49  ? 8.204   160.925 23.289 1.00 42.36 ?  48  HIS G C   1 
ATOM   7073  O  O   . HIS G  3 49  ? 7.142   160.295 23.301 1.00 47.61 ?  48  HIS G O   1 
ATOM   7074  C  CB  . HIS G  3 49  ? 9.533   161.522 21.238 1.00 39.00 ?  48  HIS G CB  1 
ATOM   7075  C  CG  . HIS G  3 49  ? 10.821  161.349 20.498 1.00 40.84 ?  48  HIS G CG  1 
ATOM   7076  N  ND1 . HIS G  3 49  ? 11.760  162.350 20.397 1.00 44.37 ?  48  HIS G ND1 1 
ATOM   7077  C  CD2 . HIS G  3 49  ? 11.328  160.289 19.822 1.00 43.99 ?  48  HIS G CD2 1 
ATOM   7078  C  CE1 . HIS G  3 49  ? 12.788  161.919 19.686 1.00 40.80 ?  48  HIS G CE1 1 
ATOM   7079  N  NE2 . HIS G  3 49  ? 12.550  160.671 19.324 1.00 44.48 ?  48  HIS G NE2 1 
ATOM   7080  N  N   . GLU G  3 50  ? 8.426   162.001 24.049 1.00 43.83 ?  49  GLU G N   1 
ATOM   7081  C  CA  . GLU G  3 50  ? 7.607   162.207 25.241 1.00 52.09 ?  49  GLU G CA  1 
ATOM   7082  C  C   . GLU G  3 50  ? 6.177   162.625 24.913 1.00 51.11 ?  49  GLU G C   1 
ATOM   7083  O  O   . GLU G  3 50  ? 5.232   162.193 25.588 1.00 48.32 ?  49  GLU G O   1 
ATOM   7084  C  CB  . GLU G  3 50  ? 8.238   163.240 26.167 1.00 46.88 ?  49  GLU G CB  1 
ATOM   7085  C  CG  . GLU G  3 50  ? 7.294   163.512 27.326 1.00 54.97 ?  49  GLU G CG  1 
ATOM   7086  C  CD  . GLU G  3 50  ? 7.919   164.231 28.490 1.00 61.59 ?  49  GLU G CD  1 
ATOM   7087  O  OE1 . GLU G  3 50  ? 7.180   164.473 29.474 1.00 61.24 ?  49  GLU G OE1 1 
ATOM   7088  O  OE2 . GLU G  3 50  ? 9.130   164.551 28.413 1.00 60.25 -1 49  GLU G OE2 1 
ATOM   7089  N  N   . PHE G  3 51  ? 5.990   163.484 23.919 1.00 45.71 ?  50  PHE G N   1 
ATOM   7090  C  CA  . PHE G  3 51  ? 4.681   164.071 23.661 1.00 46.38 ?  50  PHE G CA  1 
ATOM   7091  C  C   . PHE G  3 51  ? 4.070   163.531 22.375 1.00 45.54 ?  50  PHE G C   1 
ATOM   7092  O  O   . PHE G  3 51  ? 4.757   163.397 21.357 1.00 47.40 ?  50  PHE G O   1 
ATOM   7093  C  CB  . PHE G  3 51  ? 4.782   165.591 23.578 1.00 42.75 ?  50  PHE G CB  1 
ATOM   7094  C  CG  . PHE G  3 51  ? 5.508   166.206 24.743 1.00 48.92 ?  50  PHE G CG  1 
ATOM   7095  C  CD1 . PHE G  3 51  ? 4.916   166.254 25.990 1.00 49.70 ?  50  PHE G CD1 1 
ATOM   7096  C  CD2 . PHE G  3 51  ? 6.779   166.731 24.590 1.00 49.23 ?  50  PHE G CD2 1 
ATOM   7097  C  CE1 . PHE G  3 51  ? 5.581   166.818 27.068 1.00 56.13 ?  50  PHE G CE1 1 
ATOM   7098  C  CE2 . PHE G  3 51  ? 7.450   167.299 25.662 1.00 52.29 ?  50  PHE G CE2 1 
ATOM   7099  C  CZ  . PHE G  3 51  ? 6.851   167.342 26.901 1.00 50.09 ?  50  PHE G CZ  1 
ATOM   7100  N  N   . GLY G  3 52  ? 2.771   163.235 22.433 1.00 36.51 ?  51  GLY G N   1 
ATOM   7101  C  CA  . GLY G  3 52  ? 1.971   162.957 21.257 1.00 40.89 ?  51  GLY G CA  1 
ATOM   7102  C  C   . GLY G  3 52  ? 1.456   164.248 20.644 1.00 40.70 ?  51  GLY G C   1 
ATOM   7103  O  O   . GLY G  3 52  ? 0.260   164.409 20.384 1.00 41.34 ?  51  GLY G O   1 
ATOM   7104  N  N   . ASP G  3 53  ? 2.368   165.180 20.433 1.00 38.50 ?  52  ASP G N   1 
ATOM   7105  C  CA  . ASP G  3 53  ? 2.066   166.505 19.914 1.00 42.63 ?  52  ASP G CA  1 
ATOM   7106  C  C   . ASP G  3 53  ? 2.656   166.580 18.515 1.00 42.93 ?  52  ASP G C   1 
ATOM   7107  O  O   . ASP G  3 53  ? 3.881   166.609 18.353 1.00 42.06 ?  52  ASP G O   1 
ATOM   7108  C  CB  . ASP G  3 53  ? 2.650   167.575 20.830 1.00 41.64 ?  52  ASP G CB  1 
ATOM   7109  C  CG  . ASP G  3 53  ? 2.335   168.994 20.378 1.00 44.79 ?  52  ASP G CG  1 
ATOM   7110  O  OD1 . ASP G  3 53  ? 2.028   169.223 19.183 1.00 41.39 ?  52  ASP G OD1 1 
ATOM   7111  O  OD2 . ASP G  3 53  ? 2.427   169.897 21.241 1.00 46.61 -1 52  ASP G OD2 1 
ATOM   7112  N  N   . ASN G  3 54  ? 1.782   166.609 17.510 1.00 40.87 ?  53  ASN G N   1 
ATOM   7113  C  CA  . ASN G  3 54  ? 2.187   166.619 16.112 1.00 40.25 ?  53  ASN G CA  1 
ATOM   7114  C  C   . ASN G  3 54  ? 1.914   167.974 15.454 1.00 42.52 ?  53  ASN G C   1 
ATOM   7115  O  O   . ASN G  3 54  ? 1.907   168.077 14.224 1.00 40.68 ?  53  ASN G O   1 
ATOM   7116  C  CB  . ASN G  3 54  ? 1.474   165.473 15.389 1.00 39.43 ?  53  ASN G CB  1 
ATOM   7117  C  CG  . ASN G  3 54  ? 1.970   165.261 13.973 1.00 54.76 ?  53  ASN G CG  1 
ATOM   7118  O  OD1 . ASN G  3 54  ? 3.134   164.913 13.746 1.00 56.50 ?  53  ASN G OD1 1 
ATOM   7119  N  ND2 . ASN G  3 54  ? 1.080   165.472 13.001 1.00 50.06 ?  53  ASN G ND2 1 
ATOM   7120  N  N   . THR G  3 55  ? 1.715   169.028 16.256 1.00 38.45 ?  54  THR G N   1 
ATOM   7121  C  CA  . THR G  3 55  ? 1.331   170.319 15.696 1.00 39.33 ?  54  THR G CA  1 
ATOM   7122  C  C   . THR G  3 55  ? 2.457   170.957 14.896 1.00 44.66 ?  54  THR G C   1 
ATOM   7123  O  O   . THR G  3 55  ? 2.189   171.753 13.992 1.00 42.37 ?  54  THR G O   1 
ATOM   7124  C  CB  . THR G  3 55  ? 0.880   171.275 16.797 1.00 31.78 ?  54  THR G CB  1 
ATOM   7125  O  OG1 . THR G  3 55  ? 1.865   171.334 17.831 1.00 38.35 ?  54  THR G OG1 1 
ATOM   7126  C  CG2 . THR G  3 55  ? -0.426  170.810 17.375 1.00 34.36 ?  54  THR G CG2 1 
ATOM   7127  N  N   . ALA G  3 56  ? 3.710   170.629 15.210 1.00 38.72 ?  55  ALA G N   1 
ATOM   7128  C  CA  . ALA G  3 56  ? 4.857   171.109 14.447 1.00 39.60 ?  55  ALA G CA  1 
ATOM   7129  C  C   . ALA G  3 56  ? 5.559   169.917 13.822 1.00 43.20 ?  55  ALA G C   1 
ATOM   7130  O  O   . ALA G  3 56  ? 6.788   169.804 13.881 1.00 43.66 ?  55  ALA G O   1 
ATOM   7131  C  CB  . ALA G  3 56  ? 5.816   171.897 15.338 1.00 39.21 ?  55  ALA G CB  1 
ATOM   7132  N  N   . GLY G  3 57  ? 4.779   169.014 13.240 1.00 44.28 ?  56  GLY G N   1 
ATOM   7133  C  CA  . GLY G  3 57  ? 5.387   167.802 12.759 1.00 43.39 ?  56  GLY G CA  1 
ATOM   7134  C  C   . GLY G  3 57  ? 5.998   167.029 13.911 1.00 38.77 ?  56  GLY G C   1 
ATOM   7135  O  O   . GLY G  3 57  ? 5.509   167.046 15.045 1.00 41.78 ?  56  GLY G O   1 
ATOM   7136  N  N   . CYS G  3 58  ? 7.108   166.359 13.619 1.00 35.40 ?  57  CYS G N   1 
ATOM   7137  C  CA  . CYS G  3 58  ? 7.736   165.470 14.581 1.00 43.64 ?  57  CYS G CA  1 
ATOM   7138  C  C   . CYS G  3 58  ? 8.612   166.219 15.573 1.00 41.60 ?  57  CYS G C   1 
ATOM   7139  O  O   . CYS G  3 58  ? 9.046   165.625 16.567 1.00 40.36 ?  57  CYS G O   1 
ATOM   7140  C  CB  . CYS G  3 58  ? 8.548   164.405 13.834 1.00 42.37 ?  57  CYS G CB  1 
ATOM   7141  S  SG  . CYS G  3 58  ? 7.558   163.344 12.703 1.00 57.91 ?  57  CYS G SG  1 
ATOM   7142  N  N   . THR G  3 59  ? 8.877   167.505 15.323 1.00 38.50 ?  58  THR G N   1 
ATOM   7143  C  CA  . THR G  3 59  ? 9.634   168.316 16.271 1.00 40.29 ?  58  THR G CA  1 
ATOM   7144  C  C   . THR G  3 59  ? 8.890   168.464 17.593 1.00 45.96 ?  58  THR G C   1 
ATOM   7145  O  O   . THR G  3 59  ? 9.488   168.349 18.670 1.00 46.15 ?  58  THR G O   1 
ATOM   7146  C  CB  . THR G  3 59  ? 9.925   169.686 15.654 1.00 37.85 ?  58  THR G CB  1 
ATOM   7147  O  OG1 . THR G  3 59  ? 10.782  169.507 14.522 1.00 41.05 ?  58  THR G OG1 1 
ATOM   7148  C  CG2 . THR G  3 59  ? 10.594  170.611 16.656 1.00 42.71 ?  58  THR G CG2 1 
ATOM   7149  N  N   . SER G  3 60  ? 7.580   168.706 17.534 1.00 43.59 ?  59  SER G N   1 
ATOM   7150  C  CA  . SER G  3 60  ? 6.832   168.966 18.758 1.00 43.25 ?  59  SER G CA  1 
ATOM   7151  C  C   . SER G  3 60  ? 6.621   167.712 19.586 1.00 38.71 ?  59  SER G C   1 
ATOM   7152  O  O   . SER G  3 60  ? 6.012   167.796 20.656 1.00 46.21 ?  59  SER G O   1 
ATOM   7153  C  CB  . SER G  3 60  ? 5.488   169.614 18.427 1.00 43.98 ?  59  SER G CB  1 
ATOM   7154  O  OG  . SER G  3 60  ? 4.911   168.994 17.292 1.00 44.52 ?  59  SER G OG  1 
ATOM   7155  N  N   . ALA G  3 61  ? 7.092   166.555 19.111 1.00 39.37 ?  60  ALA G N   1 
ATOM   7156  C  CA  . ALA G  3 61  ? 7.113   165.365 19.953 1.00 43.92 ?  60  ALA G CA  1 
ATOM   7157  C  C   . ALA G  3 61  ? 8.050   165.521 21.147 1.00 44.81 ?  60  ALA G C   1 
ATOM   7158  O  O   . ALA G  3 61  ? 7.943   164.747 22.106 1.00 48.95 ?  60  ALA G O   1 
ATOM   7159  C  CB  . ALA G  3 61  ? 7.526   164.140 19.133 1.00 42.05 ?  60  ALA G CB  1 
ATOM   7160  N  N   . GLY G  3 62  ? 8.974   166.483 21.097 1.00 46.47 ?  61  GLY G N   1 
ATOM   7161  C  CA  . GLY G  3 62  ? 9.903   166.727 22.176 1.00 46.37 ?  61  GLY G CA  1 
ATOM   7162  C  C   . GLY G  3 62  ? 11.032  165.711 22.249 1.00 53.47 ?  61  GLY G C   1 
ATOM   7163  O  O   . GLY G  3 62  ? 11.431  165.102 21.244 1.00 45.63 ?  61  GLY G O   1 
ATOM   7164  N  N   . PRO G  3 63  ? 11.560  165.509 23.462 1.00 51.48 ?  62  PRO G N   1 
ATOM   7165  C  CA  . PRO G  3 63  ? 12.711  164.617 23.658 1.00 44.78 ?  62  PRO G CA  1 
ATOM   7166  C  C   . PRO G  3 63  ? 12.323  163.144 23.774 1.00 47.04 ?  62  PRO G C   1 
ATOM   7167  O  O   . PRO G  3 63  ? 11.146  162.779 23.860 1.00 47.54 ?  62  PRO G O   1 
ATOM   7168  C  CB  . PRO G  3 63  ? 13.307  165.118 24.979 1.00 44.98 ?  62  PRO G CB  1 
ATOM   7169  C  CG  . PRO G  3 63  ? 12.122  165.653 25.723 1.00 43.55 ?  62  PRO G CG  1 
ATOM   7170  C  CD  . PRO G  3 63  ? 11.283  166.320 24.665 1.00 46.40 ?  62  PRO G CD  1 
ATOM   7171  N  N   . HIS G  3 64  ? 13.360  162.295 23.789 1.00 48.00 ?  63  HIS G N   1 
ATOM   7172  C  CA  . HIS G  3 64  ? 13.192  160.884 24.133 1.00 49.43 ?  63  HIS G CA  1 
ATOM   7173  C  C   . HIS G  3 64  ? 12.351  160.751 25.393 1.00 46.29 ?  63  HIS G C   1 
ATOM   7174  O  O   . HIS G  3 64  ? 12.432  161.575 26.306 1.00 51.66 ?  63  HIS G O   1 
ATOM   7175  C  CB  . HIS G  3 64  ? 14.545  160.207 24.370 1.00 50.21 ?  63  HIS G CB  1 
ATOM   7176  C  CG  . HIS G  3 64  ? 15.310  159.902 23.120 1.00 53.08 ?  63  HIS G CG  1 
ATOM   7177  N  ND1 . HIS G  3 64  ? 14.927  160.360 21.876 1.00 54.28 ?  63  HIS G ND1 1 
ATOM   7178  C  CD2 . HIS G  3 64  ? 16.435  159.175 22.921 1.00 56.15 ?  63  HIS G CD2 1 
ATOM   7179  C  CE1 . HIS G  3 64  ? 15.788  159.939 20.966 1.00 50.48 ?  63  HIS G CE1 1 
ATOM   7180  N  NE2 . HIS G  3 64  ? 16.710  159.213 21.573 1.00 56.25 ?  63  HIS G NE2 1 
ATOM   7181  N  N   . PHE G  3 65  ? 11.539  159.704 25.448 1.00 47.80 ?  64  PHE G N   1 
ATOM   7182  C  CA  . PHE G  3 65  ? 10.636  159.525 26.573 1.00 52.98 ?  64  PHE G CA  1 
ATOM   7183  C  C   . PHE G  3 65  ? 11.358  158.960 27.795 1.00 60.55 ?  64  PHE G C   1 
ATOM   7184  O  O   . PHE G  3 65  ? 11.990  157.899 27.718 1.00 59.23 ?  64  PHE G O   1 
ATOM   7185  C  CB  . PHE G  3 65  ? 9.491   158.593 26.195 1.00 49.79 ?  64  PHE G CB  1 
ATOM   7186  C  CG  . PHE G  3 65  ? 8.591   158.251 27.346 1.00 52.16 ?  64  PHE G CG  1 
ATOM   7187  C  CD1 . PHE G  3 65  ? 8.179   159.237 28.240 1.00 49.42 ?  64  PHE G CD1 1 
ATOM   7188  C  CD2 . PHE G  3 65  ? 8.151   156.949 27.536 1.00 48.64 ?  64  PHE G CD2 1 
ATOM   7189  C  CE1 . PHE G  3 65  ? 7.347   158.922 29.300 1.00 56.41 ?  64  PHE G CE1 1 
ATOM   7190  C  CE2 . PHE G  3 65  ? 7.316   156.628 28.588 1.00 53.49 ?  64  PHE G CE2 1 
ATOM   7191  C  CZ  . PHE G  3 65  ? 6.915   157.613 29.475 1.00 56.94 ?  64  PHE G CZ  1 
ATOM   7192  N  N   . ASN G  3 66  ? 11.233  159.674 28.933 1.00 58.09 ?  65  ASN G N   1 
ATOM   7193  C  CA  . ASN G  3 66  ? 11.473  159.184 30.294 1.00 65.81 ?  65  ASN G CA  1 
ATOM   7194  C  C   . ASN G  3 66  ? 12.863  158.592 30.470 1.00 66.16 ?  65  ASN G C   1 
ATOM   7195  O  O   . ASN G  3 66  ? 12.989  157.371 30.644 1.00 69.64 ?  65  ASN G O   1 
ATOM   7196  C  CB  . ASN G  3 66  ? 10.430  158.128 30.670 1.00 61.79 ?  65  ASN G CB  1 
ATOM   7197  C  CG  . ASN G  3 66  ? 10.256  157.980 32.177 1.00 71.90 ?  65  ASN G CG  1 
ATOM   7198  O  OD1 . ASN G  3 66  ? 10.878  158.704 32.965 1.00 69.26 ?  65  ASN G OD1 1 
ATOM   7199  N  ND2 . ASN G  3 66  ? 9.399   157.034 32.584 1.00 65.07 ?  65  ASN G ND2 1 
ATOM   7200  N  N   . PRO G  3 67  ? 13.915  159.411 30.457 1.00 65.14 ?  66  PRO G N   1 
ATOM   7201  C  CA  . PRO G  3 67  ? 15.278  158.864 30.504 1.00 66.40 ?  66  PRO G CA  1 
ATOM   7202  C  C   . PRO G  3 67  ? 15.532  158.061 31.777 1.00 77.71 ?  66  PRO G C   1 
ATOM   7203  O  O   . PRO G  3 67  ? 14.809  158.172 32.777 1.00 76.94 ?  66  PRO G O   1 
ATOM   7204  C  CB  . PRO G  3 67  ? 16.171  160.113 30.434 1.00 53.87 ?  66  PRO G CB  1 
ATOM   7205  C  CG  . PRO G  3 67  ? 15.277  161.183 29.852 1.00 61.10 ?  66  PRO G CG  1 
ATOM   7206  C  CD  . PRO G  3 67  ? 13.908  160.878 30.392 1.00 62.41 ?  66  PRO G CD  1 
ATOM   7207  N  N   . LEU G  3 68  ? 16.587  157.236 31.714 1.00 81.07 ?  67  LEU G N   1 
ATOM   7208  C  CA  . LEU G  3 68  ? 16.935  156.239 32.738 1.00 71.00 ?  67  LEU G CA  1 
ATOM   7209  C  C   . LEU G  3 68  ? 15.832  155.178 32.845 1.00 65.46 ?  67  LEU G C   1 
ATOM   7210  O  O   . LEU G  3 68  ? 15.621  154.389 31.909 1.00 62.85 ?  67  LEU G O   1 
ATOM   7211  C  CB  . LEU G  3 68  ? 17.197  156.906 34.108 1.00 61.93 ?  67  LEU G CB  1 
ATOM   7212  N  N   . ARG G  3 80  ? 19.887  155.012 27.253 1.00 65.79 ?  79  ARG G N   1 
ATOM   7213  C  CA  . ARG G  3 80  ? 18.743  154.153 27.556 1.00 68.79 ?  79  ARG G CA  1 
ATOM   7214  C  C   . ARG G  3 80  ? 17.627  154.911 28.260 1.00 70.62 ?  79  ARG G C   1 
ATOM   7215  O  O   . ARG G  3 80  ? 17.790  155.379 29.387 1.00 74.71 ?  79  ARG G O   1 
ATOM   7216  C  CB  . ARG G  3 80  ? 19.155  152.966 28.432 1.00 65.46 ?  79  ARG G CB  1 
ATOM   7217  C  CG  . ARG G  3 80  ? 17.969  152.118 28.921 1.00 60.98 ?  79  ARG G CG  1 
ATOM   7218  C  CD  . ARG G  3 80  ? 17.544  151.063 27.895 1.00 62.53 ?  79  ARG G CD  1 
ATOM   7219  N  NE  . ARG G  3 80  ? 16.093  151.024 27.727 1.00 70.85 ?  79  ARG G NE  1 
ATOM   7220  C  CZ  . ARG G  3 80  ? 15.451  150.293 26.823 1.00 69.71 ?  79  ARG G CZ  1 
ATOM   7221  N  NH1 . ARG G  3 80  ? 16.101  149.496 25.990 1.00 74.44 ?  79  ARG G NH1 1 
ATOM   7222  N  NH2 . ARG G  3 80  ? 14.124  150.367 26.748 1.00 68.26 ?  79  ARG G NH2 1 
ATOM   7223  N  N   . HIS G  3 81  ? 16.483  155.003 27.593 1.00 70.34 ?  80  HIS G N   1 
ATOM   7224  C  CA  . HIS G  3 81  ? 15.271  155.575 28.160 1.00 65.86 ?  80  HIS G CA  1 
ATOM   7225  C  C   . HIS G  3 81  ? 14.150  154.565 27.964 1.00 61.08 ?  80  HIS G C   1 
ATOM   7226  O  O   . HIS G  3 81  ? 14.364  153.488 27.398 1.00 63.90 ?  80  HIS G O   1 
ATOM   7227  C  CB  . HIS G  3 81  ? 14.958  156.923 27.506 1.00 67.22 ?  80  HIS G CB  1 
ATOM   7228  C  CG  . HIS G  3 81  ? 14.450  156.806 26.102 1.00 70.46 ?  80  HIS G CG  1 
ATOM   7229  N  ND1 . HIS G  3 81  ? 13.115  156.623 25.804 1.00 66.35 ?  80  HIS G ND1 1 
ATOM   7230  C  CD2 . HIS G  3 81  ? 15.106  156.808 24.914 1.00 69.07 ?  80  HIS G CD2 1 
ATOM   7231  C  CE1 . HIS G  3 81  ? 12.966  156.565 24.491 1.00 65.08 ?  80  HIS G CE1 1 
ATOM   7232  N  NE2 . HIS G  3 81  ? 14.159  156.655 23.928 1.00 65.22 ?  80  HIS G NE2 1 
ATOM   7233  N  N   . VAL G  3 82  ? 12.942  154.909 28.417 1.00 55.15 ?  81  VAL G N   1 
ATOM   7234  C  CA  . VAL G  3 82  ? 11.862  153.923 28.404 1.00 57.84 ?  81  VAL G CA  1 
ATOM   7235  C  C   . VAL G  3 82  ? 11.616  153.417 26.985 1.00 67.93 ?  81  VAL G C   1 
ATOM   7236  O  O   . VAL G  3 82  ? 11.659  152.207 26.724 1.00 71.32 ?  81  VAL G O   1 
ATOM   7237  C  CB  . VAL G  3 82  ? 10.584  154.501 29.035 1.00 61.88 ?  81  VAL G CB  1 
ATOM   7238  C  CG1 . VAL G  3 82  ? 9.361   153.645 28.657 1.00 56.60 ?  81  VAL G CG1 1 
ATOM   7239  C  CG2 . VAL G  3 82  ? 10.747  154.597 30.560 1.00 59.53 ?  81  VAL G CG2 1 
ATOM   7240  N  N   . GLY G  3 83  ? 11.401  154.330 26.040 1.00 66.27 ?  82  GLY G N   1 
ATOM   7241  C  CA  . GLY G  3 83  ? 11.089  153.905 24.684 1.00 66.96 ?  82  GLY G CA  1 
ATOM   7242  C  C   . GLY G  3 83  ? 12.277  153.830 23.744 1.00 65.38 ?  82  GLY G C   1 
ATOM   7243  O  O   . GLY G  3 83  ? 12.163  154.181 22.564 1.00 59.47 ?  82  GLY G O   1 
ATOM   7244  N  N   . ASP G  3 84  ? 13.437  153.419 24.256 1.00 67.33 ?  83  ASP G N   1 
ATOM   7245  C  CA  . ASP G  3 84  ? 14.623  153.263 23.415 1.00 64.11 ?  83  ASP G CA  1 
ATOM   7246  C  C   . ASP G  3 84  ? 14.561  151.884 22.781 1.00 63.49 ?  83  ASP G C   1 
ATOM   7247  O  O   . ASP G  3 84  ? 15.032  150.894 23.340 1.00 66.33 ?  83  ASP G O   1 
ATOM   7248  C  CB  . ASP G  3 84  ? 15.901  153.446 24.218 1.00 69.09 ?  83  ASP G CB  1 
ATOM   7249  C  CG  . ASP G  3 84  ? 17.104  153.701 23.329 1.00 83.08 ?  83  ASP G CG  1 
ATOM   7250  O  OD1 . ASP G  3 84  ? 17.240  152.998 22.293 1.00 81.30 ?  83  ASP G OD1 1 
ATOM   7251  O  OD2 . ASP G  3 84  ? 17.898  154.618 23.656 1.00 92.75 -1 83  ASP G OD2 1 
ATOM   7252  N  N   . LEU G  3 85  ? 13.983  151.820 21.586 1.00 57.46 ?  84  LEU G N   1 
ATOM   7253  C  CA  . LEU G  3 85  ? 13.743  150.548 20.922 1.00 52.76 ?  84  LEU G CA  1 
ATOM   7254  C  C   . LEU G  3 85  ? 14.852  150.190 19.939 1.00 52.55 ?  84  LEU G C   1 
ATOM   7255  O  O   . LEU G  3 85  ? 14.659  149.316 19.088 1.00 59.75 ?  84  LEU G O   1 
ATOM   7256  C  CB  . LEU G  3 85  ? 12.387  150.573 20.223 1.00 51.68 ?  84  LEU G CB  1 
ATOM   7257  C  CG  . LEU G  3 85  ? 11.207  151.194 20.974 1.00 49.91 ?  84  LEU G CG  1 
ATOM   7258  C  CD1 . LEU G  3 85  ? 9.881   150.808 20.319 1.00 44.08 ?  84  LEU G CD1 1 
ATOM   7259  C  CD2 . LEU G  3 85  ? 11.202  150.780 22.451 1.00 57.05 ?  84  LEU G CD2 1 
ATOM   7260  N  N   . GLY G  3 86  ? 16.002  150.859 20.035 1.00 53.11 ?  85  GLY G N   1 
ATOM   7261  C  CA  . GLY G  3 86  ? 17.166  150.504 19.248 1.00 52.94 ?  85  GLY G CA  1 
ATOM   7262  C  C   . GLY G  3 86  ? 17.201  151.108 17.861 1.00 56.54 ?  85  GLY G C   1 
ATOM   7263  O  O   . GLY G  3 86  ? 16.907  152.293 17.669 1.00 58.75 ?  85  GLY G O   1 
ATOM   7264  N  N   . ASN G  3 87  ? 17.588  150.301 16.886 1.00 47.22 ?  86  ASN G N   1 
ATOM   7265  C  CA  . ASN G  3 87  ? 17.622  150.716 15.498 1.00 46.01 ?  86  ASN G CA  1 
ATOM   7266  C  C   . ASN G  3 87  ? 16.761  149.756 14.698 1.00 52.01 ?  86  ASN G C   1 
ATOM   7267  O  O   . ASN G  3 87  ? 16.724  148.555 14.981 1.00 48.95 ?  86  ASN G O   1 
ATOM   7268  C  CB  . ASN G  3 87  ? 19.050  150.711 14.928 1.00 53.81 ?  86  ASN G CB  1 
ATOM   7269  C  CG  . ASN G  3 87  ? 19.954  151.768 15.559 1.00 60.47 ?  86  ASN G CG  1 
ATOM   7270  O  OD1 . ASN G  3 87  ? 19.627  152.959 15.594 1.00 63.64 ?  86  ASN G OD1 1 
ATOM   7271  N  ND2 . ASN G  3 87  ? 21.117  151.330 16.039 1.00 58.15 ?  86  ASN G ND2 1 
ATOM   7272  N  N   . VAL G  3 88  ? 16.076  150.277 13.697 1.00 49.78 ?  87  VAL G N   1 
ATOM   7273  C  CA  . VAL G  3 88  ? 15.440  149.429 12.713 1.00 43.97 ?  87  VAL G CA  1 
ATOM   7274  C  C   . VAL G  3 88  ? 16.356  149.355 11.502 1.00 44.29 ?  87  VAL G C   1 
ATOM   7275  O  O   . VAL G  3 88  ? 17.209  150.221 11.277 1.00 46.49 ?  87  VAL G O   1 
ATOM   7276  C  CB  . VAL G  3 88  ? 14.027  149.930 12.338 1.00 49.24 ?  87  VAL G CB  1 
ATOM   7277  C  CG1 . VAL G  3 88  ? 13.133  149.863 13.558 1.00 39.53 ?  87  VAL G CG1 1 
ATOM   7278  C  CG2 . VAL G  3 88  ? 14.076  151.358 11.772 1.00 41.78 ?  87  VAL G CG2 1 
ATOM   7279  N  N   . THR G  3 89  ? 16.180  148.299 10.710 1.00 43.88 ?  88  THR G N   1 
ATOM   7280  C  CA  . THR G  3 89  ? 17.029  148.016 9.559  1.00 44.61 ?  88  THR G CA  1 
ATOM   7281  C  C   . THR G  3 89  ? 16.179  148.015 8.301  1.00 43.88 ?  88  THR G C   1 
ATOM   7282  O  O   . THR G  3 89  ? 15.277  147.181 8.154  1.00 42.57 ?  88  THR G O   1 
ATOM   7283  C  CB  . THR G  3 89  ? 17.734  146.664 9.709  1.00 44.43 ?  88  THR G CB  1 
ATOM   7284  O  OG1 . THR G  3 89  ? 18.697  146.741 10.760 1.00 54.01 ?  88  THR G OG1 1 
ATOM   7285  C  CG2 . THR G  3 89  ? 18.434  146.258 8.395  1.00 47.24 ?  88  THR G CG2 1 
ATOM   7286  N  N   . ALA G  3 90  ? 16.468  148.932 7.391  1.00 43.26 ?  89  ALA G N   1 
ATOM   7287  C  CA  . ALA G  3 90  ? 15.810  148.926 6.097  1.00 41.28 ?  89  ALA G CA  1 
ATOM   7288  C  C   . ALA G  3 90  ? 16.657  148.121 5.118  1.00 41.38 ?  89  ALA G C   1 
ATOM   7289  O  O   . ALA G  3 90  ? 17.877  148.312 5.039  1.00 39.76 ?  89  ALA G O   1 
ATOM   7290  C  CB  . ALA G  3 90  ? 15.594  150.357 5.589  1.00 38.51 ?  89  ALA G CB  1 
ATOM   7291  N  N   . ASP G  3 91  ? 16.006  147.225 4.386  1.00 37.33 ?  90  ASP G N   1 
ATOM   7292  C  CA  . ASP G  3 91  ? 16.663  146.435 3.356  1.00 44.40 ?  90  ASP G CA  1 
ATOM   7293  C  C   . ASP G  3 91  ? 16.954  147.313 2.132  1.00 46.79 ?  90  ASP G C   1 
ATOM   7294  O  O   . ASP G  3 91  ? 16.724  148.526 2.130  1.00 43.79 ?  90  ASP G O   1 
ATOM   7295  C  CB  . ASP G  3 91  ? 15.802  145.222 3.014  1.00 39.56 ?  90  ASP G CB  1 
ATOM   7296  C  CG  . ASP G  3 91  ? 14.429  145.604 2.442  1.00 52.10 ?  90  ASP G CG  1 
ATOM   7297  O  OD1 . ASP G  3 91  ? 14.272  146.723 1.889  1.00 49.12 ?  90  ASP G OD1 1 
ATOM   7298  O  OD2 . ASP G  3 91  ? 13.497  144.772 2.542  1.00 46.86 -1 90  ASP G OD2 1 
ATOM   7299  N  N   . LYS G  3 92  ? 17.433  146.682 1.053  1.00 43.86 ?  91  LYS G N   1 
ATOM   7300  C  CA  . LYS G  3 92  ? 17.771  147.406 -0.171 1.00 47.48 ?  91  LYS G CA  1 
ATOM   7301  C  C   . LYS G  3 92  ? 16.557  148.037 -0.842 1.00 46.66 ?  91  LYS G C   1 
ATOM   7302  O  O   . LYS G  3 92  ? 16.728  148.902 -1.707 1.00 45.61 ?  91  LYS G O   1 
ATOM   7303  C  CB  . LYS G  3 92  ? 18.476  146.476 -1.163 1.00 45.08 ?  91  LYS G CB  1 
ATOM   7304  C  CG  . LYS G  3 92  ? 17.799  145.117 -1.343 1.00 50.68 ?  91  LYS G CG  1 
ATOM   7305  C  CD  . LYS G  3 92  ? 17.144  144.980 -2.715 1.00 60.39 ?  91  LYS G CD  1 
ATOM   7306  C  CE  . LYS G  3 92  ? 16.121  143.836 -2.737 1.00 68.18 ?  91  LYS G CE  1 
ATOM   7307  N  NZ  . LYS G  3 92  ? 15.296  143.794 -3.995 1.00 66.83 ?  91  LYS G NZ  1 
ATOM   7308  N  N   . ASP G  3 93  ? 15.342  147.628 -0.480 1.00 46.04 ?  92  ASP G N   1 
ATOM   7309  C  CA  . ASP G  3 93  ? 14.133  148.239 -1.014 1.00 45.27 ?  92  ASP G CA  1 
ATOM   7310  C  C   . ASP G  3 93  ? 13.582  149.339 -0.120 1.00 46.40 ?  92  ASP G C   1 
ATOM   7311  O  O   . ASP G  3 93  ? 12.461  149.807 -0.353 1.00 44.17 ?  92  ASP G O   1 
ATOM   7312  C  CB  . ASP G  3 93  ? 13.066  147.182 -1.242 1.00 45.94 ?  92  ASP G CB  1 
ATOM   7313  C  CG  . ASP G  3 93  ? 13.414  146.269 -2.366 1.00 61.45 ?  92  ASP G CG  1 
ATOM   7314  O  OD1 . ASP G  3 93  ? 13.280  145.038 -2.187 1.00 68.71 ?  92  ASP G OD1 1 
ATOM   7315  O  OD2 . ASP G  3 93  ? 13.840  146.785 -3.425 1.00 71.19 -1 92  ASP G OD2 1 
ATOM   7316  N  N   . GLY G  3 94  ? 14.340  149.766 0.887  1.00 39.95 ?  93  GLY G N   1 
ATOM   7317  C  CA  . GLY G  3 94  ? 13.866  150.815 1.766  1.00 41.11 ?  93  GLY G CA  1 
ATOM   7318  C  C   . GLY G  3 94  ? 12.825  150.382 2.771  1.00 43.72 ?  93  GLY G C   1 
ATOM   7319  O  O   . GLY G  3 94  ? 12.192  151.242 3.396  1.00 41.36 ?  93  GLY G O   1 
ATOM   7320  N  N   . VAL G  3 95  ? 12.630  149.079 2.958  1.00 39.73 ?  94  VAL G N   1 
ATOM   7321  C  CA  . VAL G  3 95  ? 11.600  148.560 3.848  1.00 47.06 ?  94  VAL G CA  1 
ATOM   7322  C  C   . VAL G  3 95  ? 12.270  148.024 5.108  1.00 48.49 ?  94  VAL G C   1 
ATOM   7323  O  O   . VAL G  3 95  ? 13.166  147.173 5.037  1.00 45.54 ?  94  VAL G O   1 
ATOM   7324  C  CB  . VAL G  3 95  ? 10.756  147.479 3.161  1.00 43.65 ?  94  VAL G CB  1 
ATOM   7325  C  CG1 . VAL G  3 95  ? 9.625   147.031 4.069  1.00 42.29 ?  94  VAL G CG1 1 
ATOM   7326  C  CG2 . VAL G  3 95  ? 10.207  148.021 1.856  1.00 41.54 ?  94  VAL G CG2 1 
ATOM   7327  N  N   . ALA G  3 96  ? 11.843  148.529 6.261  1.00 44.46 ?  95  ALA G N   1 
ATOM   7328  C  CA  . ALA G  3 96  ? 12.288  148.023 7.550  1.00 39.63 ?  95  ALA G CA  1 
ATOM   7329  C  C   . ALA G  3 96  ? 11.153  147.199 8.144  1.00 45.36 ?  95  ALA G C   1 
ATOM   7330  O  O   . ALA G  3 96  ? 10.087  147.733 8.461  1.00 46.75 ?  95  ALA G O   1 
ATOM   7331  C  CB  . ALA G  3 96  ? 12.687  149.159 8.480  1.00 38.23 ?  95  ALA G CB  1 
ATOM   7332  N  N   . ASP G  3 97  ? 11.381  145.899 8.283  1.00 46.63 ?  96  ASP G N   1 
ATOM   7333  C  CA  . ASP G  3 97  ? 10.423  145.007 8.913  1.00 48.78 ?  96  ASP G CA  1 
ATOM   7334  C  C   . ASP G  3 97  ? 10.775  144.881 10.392 1.00 50.02 ?  96  ASP G C   1 
ATOM   7335  O  O   . ASP G  3 97  ? 11.898  144.510 10.742 1.00 52.63 ?  96  ASP G O   1 
ATOM   7336  C  CB  . ASP G  3 97  ? 10.427  143.664 8.194  1.00 48.09 ?  96  ASP G CB  1 
ATOM   7337  C  CG  . ASP G  3 97  ? 9.713   143.737 6.847  1.00 64.92 ?  96  ASP G CG  1 
ATOM   7338  O  OD1 . ASP G  3 97  ? 10.303  143.294 5.829  1.00 64.44 ?  96  ASP G OD1 1 
ATOM   7339  O  OD2 . ASP G  3 97  ? 8.562   144.232 6.805  1.00 66.52 -1 96  ASP G OD2 1 
ATOM   7340  N  N   . VAL G  3 98  ? 9.831   145.240 11.255 1.00 47.14 ?  97  VAL G N   1 
ATOM   7341  C  CA  . VAL G  3 98  ? 10.086  145.391 12.679 1.00 44.22 ?  97  VAL G CA  1 
ATOM   7342  C  C   . VAL G  3 98  ? 9.451   144.222 13.411 1.00 48.95 ?  97  VAL G C   1 
ATOM   7343  O  O   . VAL G  3 98  ? 8.269   143.916 13.207 1.00 43.30 ?  97  VAL G O   1 
ATOM   7344  C  CB  . VAL G  3 98  ? 9.548   146.727 13.217 1.00 47.46 ?  97  VAL G CB  1 
ATOM   7345  C  CG1 . VAL G  3 98  ? 9.789   146.831 14.716 1.00 44.59 ?  97  VAL G CG1 1 
ATOM   7346  C  CG2 . VAL G  3 98  ? 10.184  147.891 12.479 1.00 42.88 ?  97  VAL G CG2 1 
ATOM   7347  N  N   . SER G  3 99  ? 10.254  143.567 14.257 1.00 48.77 ?  98  SER G N   1 
ATOM   7348  C  CA  . SER G  3 99  ? 9.801   142.509 15.163 1.00 51.81 ?  98  SER G CA  1 
ATOM   7349  C  C   . SER G  3 99  ? 10.660  142.647 16.416 1.00 51.32 ?  98  SER G C   1 
ATOM   7350  O  O   . SER G  3 99  ? 11.834  142.275 16.415 1.00 60.00 ?  98  SER G O   1 
ATOM   7351  C  CB  . SER G  3 99  ? 9.936   141.130 14.534 1.00 51.48 ?  98  SER G CB  1 
ATOM   7352  O  OG  . SER G  3 99  ? 8.915   140.259 14.994 1.00 65.54 ?  98  SER G OG  1 
ATOM   7353  N  N   . ILE G  3 100 ? 10.078  143.204 17.472 1.00 55.00 ?  99  ILE G N   1 
ATOM   7354  C  CA  . ILE G  3 100 ? 10.820  143.574 18.667 1.00 52.74 ?  99  ILE G CA  1 
ATOM   7355  C  C   . ILE G  3 100 ? 10.022  143.128 19.884 1.00 55.34 ?  99  ILE G C   1 
ATOM   7356  O  O   . ILE G  3 100 ? 8.786   143.126 19.873 1.00 57.09 ?  99  ILE G O   1 
ATOM   7357  C  CB  . ILE G  3 100 ? 11.093  145.102 18.686 1.00 55.27 ?  99  ILE G CB  1 
ATOM   7358  C  CG1 . ILE G  3 100 ? 12.147  145.462 17.636 1.00 56.26 ?  99  ILE G CG1 1 
ATOM   7359  C  CG2 . ILE G  3 100 ? 11.477  145.608 20.074 1.00 54.97 ?  99  ILE G CG2 1 
ATOM   7360  C  CD1 . ILE G  3 100 ? 13.588  145.276 18.096 1.00 56.69 ?  99  ILE G CD1 1 
ATOM   7361  N  N   . GLU G  3 101 ? 10.732  142.717 20.931 1.00 58.22 ?  100 GLU G N   1 
ATOM   7362  C  CA  . GLU G  3 101 ? 10.133  142.558 22.251 1.00 56.40 ?  100 GLU G CA  1 
ATOM   7363  C  C   . GLU G  3 101 ? 10.884  143.452 23.224 1.00 54.39 ?  100 GLU G C   1 
ATOM   7364  O  O   . GLU G  3 101 ? 12.109  143.354 23.354 1.00 56.36 ?  100 GLU G O   1 
ATOM   7365  C  CB  . GLU G  3 101 ? 10.142  141.102 22.720 1.00 59.77 ?  100 GLU G CB  1 
ATOM   7366  C  CG  . GLU G  3 101 ? 8.759   140.646 23.183 1.00 64.27 ?  100 GLU G CG  1 
ATOM   7367  C  CD  . GLU G  3 101 ? 8.706   139.190 23.619 1.00 77.55 ?  100 GLU G CD  1 
ATOM   7368  O  OE1 . GLU G  3 101 ? 7.614   138.741 24.043 1.00 75.98 ?  100 GLU G OE1 1 
ATOM   7369  O  OE2 . GLU G  3 101 ? 9.748   138.498 23.535 1.00 84.33 -1 100 GLU G OE2 1 
ATOM   7370  N  N   . ASP G  3 102 ? 10.156  144.350 23.868 1.00 54.12 ?  101 ASP G N   1 
ATOM   7371  C  CA  . ASP G  3 102 ? 10.737  145.254 24.841 1.00 53.99 ?  101 ASP G CA  1 
ATOM   7372  C  C   . ASP G  3 102 ? 9.959   145.105 26.133 1.00 58.02 ?  101 ASP G C   1 
ATOM   7373  O  O   . ASP G  3 102 ? 8.722   145.097 26.114 1.00 60.11 ?  101 ASP G O   1 
ATOM   7374  C  CB  . ASP G  3 102 ? 10.700  146.701 24.359 1.00 54.56 ?  101 ASP G CB  1 
ATOM   7375  C  CG  . ASP G  3 102 ? 11.693  147.578 25.092 1.00 62.18 ?  101 ASP G CG  1 
ATOM   7376  O  OD1 . ASP G  3 102 ? 11.251  148.570 25.711 1.00 64.96 -1 101 ASP G OD1 1 
ATOM   7377  O  OD2 . ASP G  3 102 ? 12.911  147.279 25.047 1.00 67.21 ?  101 ASP G OD2 1 
ATOM   7378  N  N   . SER G  3 103 ? 10.681  144.961 27.243 1.00 63.62 ?  102 SER G N   1 
ATOM   7379  C  CA  . SER G  3 103 ? 10.073  144.861 28.564 1.00 64.82 ?  102 SER G CA  1 
ATOM   7380  C  C   . SER G  3 103 ? 10.117  146.176 29.327 1.00 56.86 ?  102 SER G C   1 
ATOM   7381  O  O   . SER G  3 103 ? 9.599   146.247 30.444 1.00 64.13 ?  102 SER G O   1 
ATOM   7382  C  CB  . SER G  3 103 ? 10.754  143.758 29.390 1.00 61.09 ?  102 SER G CB  1 
ATOM   7383  O  OG  . SER G  3 103 ? 11.978  143.357 28.799 1.00 63.56 ?  102 SER G OG  1 
ATOM   7384  N  N   . VAL G  3 104 ? 10.706  147.216 28.744 1.00 55.51 ?  103 VAL G N   1 
ATOM   7385  C  CA  . VAL G  3 104 ? 10.814  148.510 29.412 1.00 60.15 ?  103 VAL G CA  1 
ATOM   7386  C  C   . VAL G  3 104 ? 9.605   149.398 29.138 1.00 63.56 ?  103 VAL G C   1 
ATOM   7387  O  O   . VAL G  3 104 ? 9.134   150.107 30.036 1.00 63.45 ?  103 VAL G O   1 
ATOM   7388  C  CB  . VAL G  3 104 ? 12.122  149.196 28.990 1.00 53.72 ?  103 VAL G CB  1 
ATOM   7389  C  CG1 . VAL G  3 104 ? 12.397  150.408 29.873 1.00 57.74 ?  103 VAL G CG1 1 
ATOM   7390  C  CG2 . VAL G  3 104 ? 13.264  148.191 29.060 1.00 57.31 ?  103 VAL G CG2 1 
ATOM   7391  N  N   . ILE G  3 105 ? 9.104   149.417 27.899 1.00 59.20 ?  104 ILE G N   1 
ATOM   7392  C  CA  . ILE G  3 105 ? 7.877   150.144 27.586 1.00 56.08 ?  104 ILE G CA  1 
ATOM   7393  C  C   . ILE G  3 105 ? 6.719   149.315 28.121 1.00 53.98 ?  104 ILE G C   1 
ATOM   7394  O  O   . ILE G  3 105 ? 6.888   148.134 28.437 1.00 61.71 ?  104 ILE G O   1 
ATOM   7395  C  CB  . ILE G  3 105 ? 7.715   150.408 26.072 1.00 51.14 ?  104 ILE G CB  1 
ATOM   7396  C  CG1 . ILE G  3 105 ? 7.690   149.087 25.297 1.00 54.01 ?  104 ILE G CG1 1 
ATOM   7397  C  CG2 . ILE G  3 105 ? 8.796   151.346 25.551 1.00 50.75 ?  104 ILE G CG2 1 
ATOM   7398  C  CD1 . ILE G  3 105 ? 7.659   149.252 23.793 1.00 52.22 ?  104 ILE G CD1 1 
ATOM   7399  N  N   . SER G  3 106 ? 5.540   149.924 28.230 1.00 53.41 ?  105 SER G N   1 
ATOM   7400  C  CA  . SER G  3 106 ? 4.324   149.202 28.569 1.00 51.48 ?  105 SER G CA  1 
ATOM   7401  C  C   . SER G  3 106 ? 3.132   149.970 28.012 1.00 52.71 ?  105 SER G C   1 
ATOM   7402  O  O   . SER G  3 106 ? 3.245   151.138 27.631 1.00 51.53 ?  105 SER G O   1 
ATOM   7403  C  CB  . SER G  3 106 ? 4.172   149.001 30.092 1.00 55.40 ?  105 SER G CB  1 
ATOM   7404  O  OG  . SER G  3 106 ? 2.943   148.352 30.414 1.00 47.84 ?  105 SER G OG  1 
ATOM   7405  N  N   . LEU G  3 107 ? 1.981   149.297 27.968 1.00 48.60 ?  106 LEU G N   1 
ATOM   7406  C  CA  . LEU G  3 107 ? 0.736   149.895 27.503 1.00 47.29 ?  106 LEU G CA  1 
ATOM   7407  C  C   . LEU G  3 107 ? -0.169  150.301 28.664 1.00 54.26 ?  106 LEU G C   1 
ATOM   7408  O  O   . LEU G  3 107 ? -1.398  150.382 28.515 1.00 53.67 ?  106 LEU G O   1 
ATOM   7409  C  CB  . LEU G  3 107 ? 0.030   148.931 26.554 1.00 49.43 ?  106 LEU G CB  1 
ATOM   7410  C  CG  . LEU G  3 107 ? 0.924   148.505 25.379 1.00 51.25 ?  106 LEU G CG  1 
ATOM   7411  C  CD1 . LEU G  3 107 ? 0.126   147.762 24.293 1.00 46.03 ?  106 LEU G CD1 1 
ATOM   7412  C  CD2 . LEU G  3 107 ? 1.684   149.699 24.787 1.00 42.38 ?  106 LEU G CD2 1 
ATOM   7413  N  N   . SER G  3 108 ? 0.438   150.548 29.822 1.00 59.23 ?  107 SER G N   1 
ATOM   7414  C  CA  . SER G  3 108 ? -0.215  150.898 31.078 1.00 60.09 ?  107 SER G CA  1 
ATOM   7415  C  C   . SER G  3 108 ? 0.902   151.209 32.060 1.00 56.31 ?  107 SER G C   1 
ATOM   7416  O  O   . SER G  3 108 ? 2.087   151.032 31.756 1.00 61.07 ?  107 SER G O   1 
ATOM   7417  C  CB  . SER G  3 108 ? -1.107  149.775 31.613 1.00 56.16 ?  107 SER G CB  1 
ATOM   7418  O  OG  . SER G  3 108 ? -0.318  148.678 32.043 1.00 62.39 ?  107 SER G OG  1 
ATOM   7419  N  N   . GLY G  3 109 ? 0.520   151.687 33.233 1.00 59.68 ?  108 GLY G N   1 
ATOM   7420  C  CA  . GLY G  3 109 ? 1.500   151.951 34.265 1.00 52.38 ?  108 GLY G CA  1 
ATOM   7421  C  C   . GLY G  3 109 ? 2.298   153.208 33.989 1.00 64.58 ?  108 GLY G C   1 
ATOM   7422  O  O   . GLY G  3 109 ? 1.865   154.124 33.275 1.00 64.56 ?  108 GLY G O   1 
ATOM   7423  N  N   . ASP G  3 110 ? 3.491   153.251 34.577 1.00 63.49 ?  109 ASP G N   1 
ATOM   7424  C  CA  . ASP G  3 110 ? 4.293   154.467 34.559 1.00 68.07 ?  109 ASP G CA  1 
ATOM   7425  C  C   . ASP G  3 110 ? 5.178   154.565 33.330 1.00 65.28 ?  109 ASP G C   1 
ATOM   7426  O  O   . ASP G  3 110 ? 5.585   155.675 32.955 1.00 62.52 ?  109 ASP G O   1 
ATOM   7427  C  CB  . ASP G  3 110 ? 5.144   154.550 35.830 1.00 73.43 ?  109 ASP G CB  1 
ATOM   7428  C  CG  . ASP G  3 110 ? 4.399   154.029 37.053 1.00 76.40 ?  109 ASP G CG  1 
ATOM   7429  O  OD1 . ASP G  3 110 ? 3.533   154.764 37.584 1.00 76.21 ?  109 ASP G OD1 1 
ATOM   7430  O  OD2 . ASP G  3 110 ? 4.644   152.866 37.451 1.00 80.29 -1 109 ASP G OD2 1 
ATOM   7431  N  N   . HIS G  3 111 ? 5.480   153.432 32.706 1.00 61.22 ?  110 HIS G N   1 
ATOM   7432  C  CA  . HIS G  3 111 ? 6.187   153.393 31.438 1.00 62.39 ?  110 HIS G CA  1 
ATOM   7433  C  C   . HIS G  3 111 ? 5.232   153.352 30.247 1.00 59.48 ?  110 HIS G C   1 
ATOM   7434  O  O   . HIS G  3 111 ? 5.618   152.895 29.163 1.00 61.61 ?  110 HIS G O   1 
ATOM   7435  C  CB  . HIS G  3 111 ? 7.138   152.194 31.426 1.00 62.04 ?  110 HIS G CB  1 
ATOM   7436  C  CG  . HIS G  3 111 ? 8.246   152.308 32.422 1.00 61.52 ?  110 HIS G CG  1 
ATOM   7437  N  ND1 . HIS G  3 111 ? 9.315   151.439 32.451 1.00 58.54 ?  110 HIS G ND1 1 
ATOM   7438  C  CD2 . HIS G  3 111 ? 8.462   153.206 33.414 1.00 61.46 ?  110 HIS G CD2 1 
ATOM   7439  C  CE1 . HIS G  3 111 ? 10.140  151.795 33.421 1.00 67.04 ?  110 HIS G CE1 1 
ATOM   7440  N  NE2 . HIS G  3 111 ? 9.647   152.866 34.018 1.00 61.22 ?  110 HIS G NE2 1 
ATOM   7441  N  N   . CYS G  3 112 ? 3.994   153.808 30.436 1.00 54.60 ?  111 CYS G N   1 
ATOM   7442  C  CA  . CYS G  3 112 ? 3.010   153.801 29.364 1.00 55.69 ?  111 CYS G CA  1 
ATOM   7443  C  C   . CYS G  3 112 ? 3.437   154.727 28.229 1.00 52.48 ?  111 CYS G C   1 
ATOM   7444  O  O   . CYS G  3 112 ? 3.892   155.851 28.460 1.00 47.32 ?  111 CYS G O   1 
ATOM   7445  C  CB  . CYS G  3 112 ? 1.651   154.225 29.906 1.00 48.76 ?  111 CYS G CB  1 
ATOM   7446  S  SG  . CYS G  3 112 ? 0.295   154.052 28.737 1.00 58.23 ?  111 CYS G SG  1 
ATOM   7447  N  N   . ILE G  3 113 ? 3.292   154.238 26.999 1.00 56.59 ?  112 ILE G N   1 
ATOM   7448  C  CA  . ILE G  3 113 ? 3.632   154.993 25.796 1.00 44.82 ?  112 ILE G CA  1 
ATOM   7449  C  C   . ILE G  3 113 ? 2.403   155.422 25.012 1.00 46.16 ?  112 ILE G C   1 
ATOM   7450  O  O   . ILE G  3 113 ? 2.548   156.150 24.015 1.00 46.11 ?  112 ILE G O   1 
ATOM   7451  C  CB  . ILE G  3 113 ? 4.579   154.185 24.890 1.00 44.98 ?  112 ILE G CB  1 
ATOM   7452  C  CG1 . ILE G  3 113 ? 3.917   152.855 24.531 1.00 41.91 ?  112 ILE G CG1 1 
ATOM   7453  C  CG2 . ILE G  3 113 ? 5.894   153.936 25.596 1.00 45.31 ?  112 ILE G CG2 1 
ATOM   7454  C  CD1 . ILE G  3 113 ? 4.725   152.015 23.563 1.00 45.09 ?  112 ILE G CD1 1 
ATOM   7455  N  N   . ILE G  3 114 ? 1.205   154.984 25.413 1.00 44.58 ?  113 ILE G N   1 
ATOM   7456  C  CA  . ILE G  3 114 ? -0.031  155.437 24.788 1.00 44.08 ?  113 ILE G CA  1 
ATOM   7457  C  C   . ILE G  3 114 ? -0.131  156.952 24.880 1.00 47.01 ?  113 ILE G C   1 
ATOM   7458  O  O   . ILE G  3 114 ? 0.096   157.543 25.944 1.00 40.06 ?  113 ILE G O   1 
ATOM   7459  C  CB  . ILE G  3 114 ? -1.228  154.758 25.465 1.00 43.40 ?  113 ILE G CB  1 
ATOM   7460  C  CG1 . ILE G  3 114 ? -1.027  153.242 25.495 1.00 48.70 ?  113 ILE G CG1 1 
ATOM   7461  C  CG2 . ILE G  3 114 ? -2.524  155.143 24.777 1.00 42.49 ?  113 ILE G CG2 1 
ATOM   7462  C  CD1 . ILE G  3 114 ? -1.666  152.500 24.350 1.00 49.56 ?  113 ILE G CD1 1 
ATOM   7463  N  N   . GLY G  3 115 ? -0.475  157.597 23.762 1.00 43.11 ?  114 GLY G N   1 
ATOM   7464  C  CA  . GLY G  3 115 ? -0.518  159.048 23.749 1.00 36.28 ?  114 GLY G CA  1 
ATOM   7465  C  C   . GLY G  3 115 ? 0.836   159.704 23.605 1.00 39.65 ?  114 GLY G C   1 
ATOM   7466  O  O   . GLY G  3 115 ? 0.924   160.942 23.648 1.00 42.29 ?  114 GLY G O   1 
ATOM   7467  N  N   . ARG G  3 116 ? 1.890   158.927 23.428 1.00 37.06 ?  115 ARG G N   1 
ATOM   7468  C  CA  . ARG G  3 116 ? 3.197   159.474 23.122 1.00 44.48 ?  115 ARG G CA  1 
ATOM   7469  C  C   . ARG G  3 116 ? 3.483   159.250 21.639 1.00 37.78 ?  115 ARG G C   1 
ATOM   7470  O  O   . ARG G  3 116 ? 2.650   158.713 20.909 1.00 44.21 ?  115 ARG G O   1 
ATOM   7471  C  CB  . ARG G  3 116 ? 4.251   158.866 24.048 1.00 45.61 ?  115 ARG G CB  1 
ATOM   7472  C  CG  . ARG G  3 116 ? 4.075   159.388 25.478 1.00 46.21 ?  115 ARG G CG  1 
ATOM   7473  C  CD  . ARG G  3 116 ? 4.779   158.571 26.553 1.00 54.37 ?  115 ARG G CD  1 
ATOM   7474  N  NE  . ARG G  3 116 ? 4.198   158.827 27.873 1.00 53.51 ?  115 ARG G NE  1 
ATOM   7475  C  CZ  . ARG G  3 116 ? 4.256   159.990 28.513 1.00 49.52 ?  115 ARG G CZ  1 
ATOM   7476  N  NH1 . ARG G  3 116 ? 4.879   161.037 27.995 1.00 46.61 ?  115 ARG G NH1 1 
ATOM   7477  N  NH2 . ARG G  3 116 ? 3.678   160.103 29.704 1.00 52.33 ?  115 ARG G NH2 1 
ATOM   7478  N  N   . THR G  3 117 ? 4.656   159.687 21.188 1.00 41.18 ?  116 THR G N   1 
ATOM   7479  C  CA  . THR G  3 117 ? 4.996   159.687 19.769 1.00 39.62 ?  116 THR G CA  1 
ATOM   7480  C  C   . THR G  3 117 ? 6.105   158.686 19.487 1.00 39.12 ?  116 THR G C   1 
ATOM   7481  O  O   . THR G  3 117 ? 7.160   158.725 20.125 1.00 44.77 ?  116 THR G O   1 
ATOM   7482  C  CB  . THR G  3 117 ? 5.437   161.075 19.288 1.00 41.85 ?  116 THR G CB  1 
ATOM   7483  O  OG1 . THR G  3 117 ? 4.359   162.015 19.419 1.00 40.48 ?  116 THR G OG1 1 
ATOM   7484  C  CG2 . THR G  3 117 ? 5.847   161.006 17.826 1.00 41.17 ?  116 THR G CG2 1 
ATOM   7485  N  N   . LEU G  3 118 ? 5.860   157.796 18.529 1.00 38.08 ?  117 LEU G N   1 
ATOM   7486  C  CA  . LEU G  3 118 ? 6.897   156.945 17.960 1.00 35.50 ?  117 LEU G CA  1 
ATOM   7487  C  C   . LEU G  3 118 ? 7.560   157.701 16.817 1.00 39.92 ?  117 LEU G C   1 
ATOM   7488  O  O   . LEU G  3 118 ? 6.871   158.202 15.925 1.00 42.88 ?  117 LEU G O   1 
ATOM   7489  C  CB  . LEU G  3 118 ? 6.288   155.642 17.461 1.00 32.86 ?  117 LEU G CB  1 
ATOM   7490  C  CG  . LEU G  3 118 ? 7.272   154.569 17.016 1.00 41.13 ?  117 LEU G CG  1 
ATOM   7491  C  CD1 . LEU G  3 118 ? 8.157   154.149 18.182 1.00 43.44 ?  117 LEU G CD1 1 
ATOM   7492  C  CD2 . LEU G  3 118 ? 6.534   153.383 16.421 1.00 41.36 ?  117 LEU G CD2 1 
ATOM   7493  N  N   . VAL G  3 119 ? 8.885   157.822 16.861 1.00 40.20 ?  118 VAL G N   1 
ATOM   7494  C  CA  . VAL G  3 119 ? 9.652   158.547 15.849 1.00 39.25 ?  118 VAL G CA  1 
ATOM   7495  C  C   . VAL G  3 119 ? 10.673  157.602 15.234 1.00 44.65 ?  118 VAL G C   1 
ATOM   7496  O  O   . VAL G  3 119 ? 11.355  156.862 15.952 1.00 39.23 ?  118 VAL G O   1 
ATOM   7497  C  CB  . VAL G  3 119 ? 10.382  159.773 16.437 1.00 40.86 ?  118 VAL G CB  1 
ATOM   7498  C  CG1 . VAL G  3 119 ? 11.234  160.442 15.367 1.00 40.41 ?  118 VAL G CG1 1 
ATOM   7499  C  CG2 . VAL G  3 119 ? 9.414   160.759 17.068 1.00 38.24 ?  118 VAL G CG2 1 
ATOM   7500  N  N   . VAL G  3 120 ? 10.800  157.636 13.909 1.00 41.23 ?  119 VAL G N   1 
ATOM   7501  C  CA  . VAL G  3 120 ? 11.918  156.996 13.235 1.00 34.92 ?  119 VAL G CA  1 
ATOM   7502  C  C   . VAL G  3 120 ? 12.858  158.091 12.761 1.00 46.78 ?  119 VAL G C   1 
ATOM   7503  O  O   . VAL G  3 120 ? 12.415  159.096 12.187 1.00 44.39 ?  119 VAL G O   1 
ATOM   7504  C  CB  . VAL G  3 120 ? 11.473  156.069 12.087 1.00 42.34 ?  119 VAL G CB  1 
ATOM   7505  C  CG1 . VAL G  3 120 ? 10.610  156.799 11.066 1.00 42.45 ?  119 VAL G CG1 1 
ATOM   7506  C  CG2 . VAL G  3 120 ? 12.701  155.459 11.422 1.00 42.41 ?  119 VAL G CG2 1 
ATOM   7507  N  N   . HIS G  3 121 ? 14.149  157.917 13.045 1.00 47.58 ?  120 HIS G N   1 
ATOM   7508  C  CA  . HIS G  3 121 ? 15.154  158.948 12.835 1.00 48.82 ?  120 HIS G CA  1 
ATOM   7509  C  C   . HIS G  3 121 ? 15.982  158.659 11.593 1.00 45.17 ?  120 HIS G C   1 
ATOM   7510  O  O   . HIS G  3 121 ? 16.125  157.512 11.168 1.00 50.03 ?  120 HIS G O   1 
ATOM   7511  C  CB  . HIS G  3 121 ? 16.073  159.065 14.049 1.00 43.06 ?  120 HIS G CB  1 
ATOM   7512  C  CG  . HIS G  3 121 ? 15.404  159.658 15.243 1.00 46.26 ?  120 HIS G CG  1 
ATOM   7513  N  ND1 . HIS G  3 121 ? 15.578  160.973 15.613 1.00 51.00 ?  120 HIS G ND1 1 
ATOM   7514  C  CD2 . HIS G  3 121 ? 14.545  159.121 16.142 1.00 41.14 ?  120 HIS G CD2 1 
ATOM   7515  C  CE1 . HIS G  3 121 ? 14.858  161.222 16.695 1.00 50.33 ?  120 HIS G CE1 1 
ATOM   7516  N  NE2 . HIS G  3 121 ? 14.221  160.113 17.035 1.00 47.59 ?  120 HIS G NE2 1 
ATOM   7517  N  N   . GLU G  3 122 ? 16.512  159.731 11.004 1.00 49.81 ?  121 GLU G N   1 
ATOM   7518  C  CA  . GLU G  3 122 ? 17.373  159.587 9.837  1.00 51.52 ?  121 GLU G CA  1 
ATOM   7519  C  C   . GLU G  3 122 ? 18.607  158.757 10.162 1.00 56.21 ?  121 GLU G C   1 
ATOM   7520  O  O   . GLU G  3 122 ? 19.014  157.892 9.375  1.00 54.86 ?  121 GLU G O   1 
ATOM   7521  C  CB  . GLU G  3 122 ? 17.785  160.968 9.329  1.00 52.78 ?  121 GLU G CB  1 
ATOM   7522  C  CG  . GLU G  3 122 ? 18.897  160.947 8.283  1.00 61.39 ?  121 GLU G CG  1 
ATOM   7523  C  CD  . GLU G  3 122 ? 19.205  162.342 7.741  1.00 76.81 ?  121 GLU G CD  1 
ATOM   7524  O  OE1 . GLU G  3 122 ? 19.487  162.465 6.522  1.00 76.55 ?  121 GLU G OE1 1 
ATOM   7525  O  OE2 . GLU G  3 122 ? 19.157  163.313 8.537  1.00 77.07 -1 121 GLU G OE2 1 
ATOM   7526  N  N   . LYS G  3 123 ? 19.205  159.003 11.323 1.00 52.66 ?  122 LYS G N   1 
ATOM   7527  C  CA  . LYS G  3 123 ? 20.483  158.429 11.703 1.00 57.65 ?  122 LYS G CA  1 
ATOM   7528  C  C   . LYS G  3 123 ? 20.285  157.365 12.771 1.00 54.86 ?  122 LYS G C   1 
ATOM   7529  O  O   . LYS G  3 123 ? 19.486  157.544 13.700 1.00 58.47 ?  122 LYS G O   1 
ATOM   7530  C  CB  . LYS G  3 123 ? 21.419  159.523 12.217 1.00 55.45 ?  122 LYS G CB  1 
ATOM   7531  C  CG  . LYS G  3 123 ? 22.029  160.326 11.081 1.00 61.08 ?  122 LYS G CG  1 
ATOM   7532  C  CD  . LYS G  3 123 ? 23.062  161.340 11.558 1.00 65.20 ?  122 LYS G CD  1 
ATOM   7533  C  CE  . LYS G  3 123 ? 24.043  161.660 10.434 1.00 66.47 ?  122 LYS G CE  1 
ATOM   7534  N  NZ  . LYS G  3 123 ? 23.431  161.433 9.076  1.00 71.41 ?  122 LYS G NZ  1 
ATOM   7535  N  N   . ALA G  3 124 ? 21.015  156.262 12.626 1.00 58.85 ?  123 ALA G N   1 
ATOM   7536  C  CA  . ALA G  3 124 ? 21.059  155.240 13.661 1.00 57.19 ?  123 ALA G CA  1 
ATOM   7537  C  C   . ALA G  3 124 ? 21.528  155.842 14.988 1.00 55.71 ?  123 ALA G C   1 
ATOM   7538  O  O   . ALA G  3 124 ? 22.213  156.866 15.026 1.00 58.60 ?  123 ALA G O   1 
ATOM   7539  C  CB  . ALA G  3 124 ? 21.986  154.106 13.233 1.00 53.21 ?  123 ALA G CB  1 
ATOM   7540  N  N   . ASP G  3 125 ? 21.135  155.205 16.092 1.00 54.72 ?  124 ASP G N   1 
ATOM   7541  C  CA  . ASP G  3 125 ? 21.581  155.675 17.391 1.00 57.66 ?  124 ASP G CA  1 
ATOM   7542  C  C   . ASP G  3 125 ? 22.551  154.648 17.992 1.00 70.84 ?  124 ASP G C   1 
ATOM   7543  O  O   . ASP G  3 125 ? 23.119  153.817 17.255 1.00 67.66 ?  124 ASP G O   1 
ATOM   7544  C  CB  . ASP G  3 125 ? 20.360  155.997 18.279 1.00 63.33 ?  124 ASP G CB  1 
ATOM   7545  C  CG  . ASP G  3 125 ? 19.804  154.779 19.004 1.00 73.43 ?  124 ASP G CG  1 
ATOM   7546  O  OD1 . ASP G  3 125 ? 19.584  153.738 18.349 1.00 75.24 ?  124 ASP G OD1 1 
ATOM   7547  O  OD2 . ASP G  3 125 ? 19.585  154.857 20.237 1.00 76.97 -1 124 ASP G OD2 1 
ATOM   7548  N  N   . ASP G  3 126 ? 22.738  154.718 19.324 1.00 69.84 ?  125 ASP G N   1 
ATOM   7549  C  CA  . ASP G  3 126 ? 23.731  154.016 20.154 1.00 67.96 ?  125 ASP G CA  1 
ATOM   7550  C  C   . ASP G  3 126 ? 24.539  152.911 19.476 1.00 63.29 ?  125 ASP G C   1 
ATOM   7551  O  O   . ASP G  3 126 ? 24.158  151.735 19.534 1.00 63.55 ?  125 ASP G O   1 
ATOM   7552  C  CB  . ASP G  3 126 ? 23.045  153.428 21.392 1.00 64.54 ?  125 ASP G CB  1 
ATOM   7553  N  N   . LEU G  3 127 ? 25.677  153.284 18.864 1.00 67.99 ?  126 LEU G N   1 
ATOM   7554  C  CA  . LEU G  3 127 ? 26.595  152.329 18.252 1.00 69.08 ?  126 LEU G CA  1 
ATOM   7555  C  C   . LEU G  3 127 ? 27.858  152.273 19.097 1.00 69.13 ?  126 LEU G C   1 
ATOM   7556  O  O   . LEU G  3 127 ? 27.872  151.596 20.141 1.00 70.54 ?  126 LEU G O   1 
ATOM   7557  C  CB  . LEU G  3 127 ? 26.837  152.696 16.781 1.00 58.04 ?  126 LEU G CB  1 
ATOM   7558  N  N   . GLY G  3 128 ? 28.938  152.963 18.725 1.00 74.60 ?  127 GLY G N   1 
ATOM   7559  C  CA  . GLY G  3 128 ? 30.151  152.922 19.520 1.00 54.08 ?  127 GLY G CA  1 
ATOM   7560  C  C   . GLY G  3 128 ? 31.107  154.045 19.187 1.00 64.90 ?  127 GLY G C   1 
ATOM   7561  O  O   . GLY G  3 128 ? 31.192  154.497 18.037 1.00 63.90 ?  127 GLY G O   1 
ATOM   7562  N  N   . LYS G  3 129 ? 31.775  154.579 20.250 1.00 63.79 ?  128 LYS G N   1 
ATOM   7563  C  CA  . LYS G  3 129 ? 33.110  155.168 20.166 1.00 56.85 ?  128 LYS G CA  1 
ATOM   7564  C  C   . LYS G  3 129 ? 33.924  154.879 21.445 1.00 63.93 ?  128 LYS G C   1 
ATOM   7565  O  O   . LYS G  3 129 ? 34.759  155.700 21.855 1.00 57.06 ?  128 LYS G O   1 
ATOM   7566  C  CB  . LYS G  3 129 ? 33.042  156.674 19.900 1.00 63.40 ?  128 LYS G CB  1 
ATOM   7567  N  N   . GLY G  3 130 ? 33.674  153.720 22.072 1.00 60.74 ?  129 GLY G N   1 
ATOM   7568  C  CA  . GLY G  3 130 ? 34.161  153.296 23.388 1.00 60.40 ?  129 GLY G CA  1 
ATOM   7569  C  C   . GLY G  3 130 ? 33.770  154.212 24.545 1.00 58.18 ?  129 GLY G C   1 
ATOM   7570  O  O   . GLY G  3 130 ? 33.102  155.234 24.350 1.00 59.65 ?  129 GLY G O   1 
ATOM   7571  N  N   . GLY G  3 131 ? 34.201  153.832 25.763 1.00 61.62 ?  130 GLY G N   1 
ATOM   7572  C  CA  . GLY G  3 131 ? 33.834  154.471 27.029 1.00 59.17 ?  130 GLY G CA  1 
ATOM   7573  C  C   . GLY G  3 131 ? 34.144  155.975 27.071 1.00 50.01 ?  130 GLY G C   1 
ATOM   7574  O  O   . GLY G  3 131 ? 34.952  156.414 27.897 1.00 66.03 ?  130 GLY G O   1 
ATOM   7575  N  N   . ASN G  3 132 ? 33.529  156.762 26.175 1.00 68.10 ?  131 ASN G N   1 
ATOM   7576  C  CA  . ASN G  3 132 ? 33.458  158.241 26.257 1.00 65.28 ?  131 ASN G CA  1 
ATOM   7577  C  C   . ASN G  3 132 ? 32.569  158.808 25.128 1.00 69.10 ?  131 ASN G C   1 
ATOM   7578  O  O   . ASN G  3 132 ? 31.561  159.494 25.385 1.00 61.09 ?  131 ASN G O   1 
ATOM   7579  C  CB  . ASN G  3 132 ? 34.846  158.871 26.213 1.00 53.80 ?  131 ASN G CB  1 
ATOM   7580  N  N   . GLY G  3 142 ? 19.286  162.096 13.541 1.00 62.20 ?  141 GLY G N   1 
ATOM   7581  C  CA  . GLY G  3 142 ? 19.640  163.497 13.339 1.00 65.23 ?  141 GLY G CA  1 
ATOM   7582  C  C   . GLY G  3 142 ? 18.430  164.380 13.070 1.00 69.02 ?  141 GLY G C   1 
ATOM   7583  O  O   . GLY G  3 142 ? 18.191  165.378 13.763 1.00 72.66 ?  141 GLY G O   1 
ATOM   7584  N  N   . SER G  3 143 ? 17.667  164.010 12.046 1.00 61.62 ?  142 SER G N   1 
ATOM   7585  C  CA  . SER G  3 143 ? 16.349  164.567 11.804 1.00 55.14 ?  142 SER G CA  1 
ATOM   7586  C  C   . SER G  3 143 ? 15.306  163.470 11.965 1.00 51.01 ?  142 SER G C   1 
ATOM   7587  O  O   . SER G  3 143 ? 15.602  162.274 11.869 1.00 47.17 ?  142 SER G O   1 
ATOM   7588  C  CB  . SER G  3 143 ? 16.251  165.182 10.406 1.00 47.63 ?  142 SER G CB  1 
ATOM   7589  O  OG  . SER G  3 143 ? 16.278  164.163 9.431  1.00 57.00 ?  142 SER G OG  1 
ATOM   7590  N  N   . ARG G  3 144 ? 14.074  163.887 12.224 1.00 42.65 ?  143 ARG G N   1 
ATOM   7591  C  CA  . ARG G  3 144 ? 12.984  162.952 12.438 1.00 39.98 ?  143 ARG G CA  1 
ATOM   7592  C  C   . ARG G  3 144 ? 12.233  162.775 11.126 1.00 45.64 ?  143 ARG G C   1 
ATOM   7593  O  O   . ARG G  3 144 ? 11.691  163.741 10.587 1.00 44.83 ?  143 ARG G O   1 
ATOM   7594  C  CB  . ARG G  3 144 ? 12.087  163.459 13.562 1.00 39.81 ?  143 ARG G CB  1 
ATOM   7595  C  CG  . ARG G  3 144 ? 12.933  163.982 14.731 1.00 40.69 ?  143 ARG G CG  1 
ATOM   7596  C  CD  . ARG G  3 144 ? 12.116  164.527 15.898 1.00 39.45 ?  143 ARG G CD  1 
ATOM   7597  N  NE  . ARG G  3 144 ? 12.976  164.742 17.057 1.00 42.66 ?  143 ARG G NE  1 
ATOM   7598  C  CZ  . ARG G  3 144 ? 12.562  165.149 18.251 1.00 44.74 ?  143 ARG G CZ  1 
ATOM   7599  N  NH1 . ARG G  3 144 ? 11.294  165.435 18.484 1.00 46.20 ?  143 ARG G NH1 1 
ATOM   7600  N  NH2 . ARG G  3 144 ? 13.443  165.271 19.238 1.00 48.22 ?  143 ARG G NH2 1 
ATOM   7601  N  N   . LEU G  3 145 ? 12.219  161.549 10.607 1.00 39.61 ?  144 LEU G N   1 
ATOM   7602  C  CA  . LEU G  3 145 ? 11.674  161.304 9.280  1.00 38.14 ?  144 LEU G CA  1 
ATOM   7603  C  C   . LEU G  3 145 ? 10.180  161.047 9.277  1.00 40.25 ?  144 LEU G C   1 
ATOM   7604  O  O   . LEU G  3 145 ? 9.509   161.345 8.286  1.00 38.42 ?  144 LEU G O   1 
ATOM   7605  C  CB  . LEU G  3 145 ? 12.364  160.105 8.623  1.00 35.69 ?  144 LEU G CB  1 
ATOM   7606  C  CG  . LEU G  3 145 ? 13.880  160.178 8.491  1.00 46.51 ?  144 LEU G CG  1 
ATOM   7607  C  CD1 . LEU G  3 145 ? 14.375  158.861 7.978  1.00 45.88 ?  144 LEU G CD1 1 
ATOM   7608  C  CD2 . LEU G  3 145 ? 14.272  161.286 7.547  1.00 44.16 ?  144 LEU G CD2 1 
ATOM   7609  N  N   . ALA G  3 146 ? 9.654   160.434 10.326 1.00 39.76 ?  145 ALA G N   1 
ATOM   7610  C  CA  . ALA G  3 146 ? 8.242   160.105 10.375 1.00 35.71 ?  145 ALA G CA  1 
ATOM   7611  C  C   . ALA G  3 146 ? 7.887   159.864 11.826 1.00 40.47 ?  145 ALA G C   1 
ATOM   7612  O  O   . ALA G  3 146 ? 8.753   159.533 12.639 1.00 38.37 ?  145 ALA G O   1 
ATOM   7613  C  CB  . ALA G  3 146 ? 7.908   158.870 9.532  1.00 33.99 ?  145 ALA G CB  1 
ATOM   7614  N  N   . CYS G  3 147 ? 6.611   160.037 12.141 1.00 40.16 ?  146 CYS G N   1 
ATOM   7615  C  CA  . CYS G  3 147 ? 6.156   159.879 13.511 1.00 37.70 ?  146 CYS G CA  1 
ATOM   7616  C  C   . CYS G  3 147 ? 4.649   159.760 13.517 1.00 40.75 ?  146 CYS G C   1 
ATOM   7617  O  O   . CYS G  3 147 ? 3.972   160.095 12.538 1.00 35.04 ?  146 CYS G O   1 
ATOM   7618  C  CB  . CYS G  3 147 ? 6.576   161.048 14.401 1.00 39.31 ?  146 CYS G CB  1 
ATOM   7619  S  SG  . CYS G  3 147 ? 5.956   162.640 13.848 1.00 43.67 ?  146 CYS G SG  1 
ATOM   7620  N  N   . GLY G  3 148 ? 4.144   159.254 14.634 1.00 36.06 ?  147 GLY G N   1 
ATOM   7621  C  CA  . GLY G  3 148 ? 2.721   159.190 14.877 1.00 35.16 ?  147 GLY G CA  1 
ATOM   7622  C  C   . GLY G  3 148 ? 2.482   159.087 16.364 1.00 40.93 ?  147 GLY G C   1 
ATOM   7623  O  O   . GLY G  3 148 ? 3.367   158.703 17.133 1.00 38.67 ?  147 GLY G O   1 
ATOM   7624  N  N   . VAL G  3 149 ? 1.276   159.438 16.757 1.00 38.24 ?  148 VAL G N   1 
ATOM   7625  C  CA  . VAL G  3 149 ? 0.829   159.252 18.128 1.00 41.38 ?  148 VAL G CA  1 
ATOM   7626  C  C   . VAL G  3 149 ? 0.424   157.800 18.335 1.00 40.95 ?  148 VAL G C   1 
ATOM   7627  O  O   . VAL G  3 149 ? -0.268  157.201 17.502 1.00 41.80 ?  148 VAL G O   1 
ATOM   7628  C  CB  . VAL G  3 149 ? -0.323  160.218 18.434 1.00 37.15 ?  148 VAL G CB  1 
ATOM   7629  C  CG1 . VAL G  3 149 ? -0.705  160.146 19.901 1.00 40.62 ?  148 VAL G CG1 1 
ATOM   7630  C  CG2 . VAL G  3 149 ? 0.105   161.625 18.062 1.00 37.14 ?  148 VAL G CG2 1 
ATOM   7631  N  N   . ILE G  3 150 ? 0.871   157.228 19.446 1.00 42.25 ?  149 ILE G N   1 
ATOM   7632  C  CA  . ILE G  3 150 ? 0.578   155.843 19.793 1.00 41.26 ?  149 ILE G CA  1 
ATOM   7633  C  C   . ILE G  3 150 ? -0.834  155.790 20.354 1.00 41.44 ?  149 ILE G C   1 
ATOM   7634  O  O   . ILE G  3 150 ? -1.139  156.442 21.360 1.00 40.07 ?  149 ILE G O   1 
ATOM   7635  C  CB  . ILE G  3 150 ? 1.602   155.310 20.801 1.00 41.87 ?  149 ILE G CB  1 
ATOM   7636  C  CG1 . ILE G  3 150 ? 3.004   155.430 20.199 1.00 40.82 ?  149 ILE G CG1 1 
ATOM   7637  C  CG2 . ILE G  3 150 ? 1.277   153.876 21.191 1.00 40.89 ?  149 ILE G CG2 1 
ATOM   7638  C  CD1 . ILE G  3 150 ? 4.105   154.823 21.024 1.00 41.63 ?  149 ILE G CD1 1 
ATOM   7639  N  N   . GLY G  3 151 ? -1.707  155.037 19.689 1.00 36.12 ?  150 GLY G N   1 
ATOM   7640  C  CA  . GLY G  3 151 ? -3.130  155.045 19.986 1.00 39.02 ?  150 GLY G CA  1 
ATOM   7641  C  C   . GLY G  3 151 ? -3.572  153.704 20.534 1.00 42.65 ?  150 GLY G C   1 
ATOM   7642  O  O   . GLY G  3 151 ? -2.948  152.678 20.260 1.00 39.50 ?  150 GLY G O   1 
ATOM   7643  N  N   . ILE G  3 152 ? -4.642  153.715 21.329 1.00 43.79 ?  151 ILE G N   1 
ATOM   7644  C  CA  . ILE G  3 152 ? -5.223  152.471 21.827 1.00 41.43 ?  151 ILE G CA  1 
ATOM   7645  C  C   . ILE G  3 152 ? -5.877  151.732 20.665 1.00 47.56 ?  151 ILE G C   1 
ATOM   7646  O  O   . ILE G  3 152 ? -6.747  152.276 19.974 1.00 46.76 ?  151 ILE G O   1 
ATOM   7647  C  CB  . ILE G  3 152 ? -6.242  152.731 22.943 1.00 40.43 ?  151 ILE G CB  1 
ATOM   7648  C  CG1 . ILE G  3 152 ? -5.567  153.336 24.168 1.00 45.53 ?  151 ILE G CG1 1 
ATOM   7649  C  CG2 . ILE G  3 152 ? -6.923  151.446 23.334 1.00 39.81 ?  151 ILE G CG2 1 
ATOM   7650  C  CD1 . ILE G  3 152 ? -6.502  154.154 25.046 1.00 49.59 ?  151 ILE G CD1 1 
ATOM   7651  N  N   . ALA G  3 153 ? -5.477  150.480 20.462 1.00 44.76 ?  152 ALA G N   1 
ATOM   7652  C  CA  . ALA G  3 153 ? -6.023  149.663 19.393 1.00 43.27 ?  152 ALA G CA  1 
ATOM   7653  C  C   . ALA G  3 153 ? -6.963  148.608 19.955 1.00 51.10 ?  152 ALA G C   1 
ATOM   7654  O  O   . ALA G  3 153 ? -6.893  148.238 21.129 1.00 50.94 ?  152 ALA G O   1 
ATOM   7655  C  CB  . ALA G  3 153 ? -4.909  148.985 18.592 1.00 46.40 ?  152 ALA G CB  1 
ATOM   7656  N  N   . GLN G  3 154 ? -7.835  148.115 19.089 1.00 47.52 ?  153 GLN G N   1 
ATOM   7657  C  CA  . GLN G  3 154 ? -8.732  147.029 19.449 1.00 56.04 ?  153 GLN G CA  1 
ATOM   7658  C  C   . GLN G  3 154 ? -8.003  145.683 19.432 1.00 69.22 ?  153 GLN G C   1 
ATOM   7659  O  O   . GLN G  3 154 ? -7.379  145.290 18.435 1.00 68.42 ?  153 GLN G O   1 
ATOM   7660  C  CB  . GLN G  3 154 ? -9.918  146.997 18.496 1.00 56.77 ?  153 GLN G CB  1 
ATOM   7661  C  CG  . GLN G  3 154 ? -10.879 145.858 18.727 1.00 56.19 ?  153 GLN G CG  1 
ATOM   7662  C  CD  . GLN G  3 154 ? -12.047 145.937 17.782 1.00 62.23 ?  153 GLN G CD  1 
ATOM   7663  O  OE1 . GLN G  3 154 ? -11.868 145.983 16.558 1.00 69.95 ?  153 GLN G OE1 1 
ATOM   7664  N  NE2 . GLN G  3 154 ? -13.256 145.987 18.337 1.00 64.55 ?  153 GLN G NE2 1 
ATOM   7665  O  OXT . GLN G  3 154 ? -8.024  144.952 20.425 1.00 78.69 -1 153 GLN G OXT 1 
ATOM   7666  N  N   . ALA H  4 1   ? -0.263  164.552 31.917 1.00 72.14 ?  1   ALA H N   1 
ATOM   7667  C  CA  . ALA H  4 1   ? -1.650  164.264 31.564 1.00 58.54 ?  1   ALA H CA  1 
ATOM   7668  C  C   . ALA H  4 1   ? -2.601  165.370 32.049 1.00 52.24 ?  1   ALA H C   1 
ATOM   7669  O  O   . ALA H  4 1   ? -3.722  165.084 32.474 1.00 55.13 ?  1   ALA H O   1 
ATOM   7670  C  CB  . ALA H  4 1   ? -2.074  162.905 32.133 1.00 53.47 ?  1   ALA H CB  1 
ATOM   7671  N  N   . THR H  4 2   ? -2.144  166.629 31.990 1.00 48.18 ?  2   THR H N   1 
ATOM   7672  C  CA  . THR H  4 2   ? -3.010  167.786 32.200 1.00 49.32 ?  2   THR H CA  1 
ATOM   7673  C  C   . THR H  4 2   ? -3.197  168.632 30.939 1.00 49.69 ?  2   THR H C   1 
ATOM   7674  O  O   . THR H  4 2   ? -4.030  169.547 30.940 1.00 46.26 ?  2   THR H O   1 
ATOM   7675  C  CB  . THR H  4 2   ? -2.473  168.676 33.345 1.00 50.73 ?  2   THR H CB  1 
ATOM   7676  O  OG1 . THR H  4 2   ? -1.547  169.642 32.836 1.00 58.77 ?  2   THR H OG1 1 
ATOM   7677  C  CG2 . THR H  4 2   ? -1.765  167.829 34.420 1.00 55.82 ?  2   THR H CG2 1 
ATOM   7678  N  N   . LYS H  4 3   ? -2.458  168.359 29.867 1.00 49.25 ?  3   LYS H N   1 
ATOM   7679  C  CA  . LYS H  4 3   ? -2.730  168.988 28.582 1.00 43.31 ?  3   LYS H CA  1 
ATOM   7680  C  C   . LYS H  4 3   ? -2.653  167.932 27.493 1.00 47.54 ?  3   LYS H C   1 
ATOM   7681  O  O   . LYS H  4 3   ? -1.799  167.039 27.540 1.00 42.18 ?  3   LYS H O   1 
ATOM   7682  C  CB  . LYS H  4 3   ? -1.751  170.118 28.280 1.00 47.38 ?  3   LYS H CB  1 
ATOM   7683  C  CG  . LYS H  4 3   ? -2.152  171.459 28.866 1.00 56.13 ?  3   LYS H CG  1 
ATOM   7684  C  CD  . LYS H  4 3   ? -1.273  172.596 28.336 1.00 51.52 ?  3   LYS H CD  1 
ATOM   7685  C  CE  . LYS H  4 3   ? -1.672  173.942 28.950 1.00 60.04 ?  3   LYS H CE  1 
ATOM   7686  N  NZ  . LYS H  4 3   ? -0.512  174.745 29.445 1.00 57.60 ?  3   LYS H NZ  1 
ATOM   7687  N  N   . ALA H  4 4   ? -3.554  168.026 26.521 1.00 38.45 ?  4   ALA H N   1 
ATOM   7688  C  CA  . ALA H  4 4   ? -3.544  167.107 25.395 1.00 39.24 ?  4   ALA H CA  1 
ATOM   7689  C  C   . ALA H  4 4   ? -3.790  167.889 24.110 1.00 39.31 ?  4   ALA H C   1 
ATOM   7690  O  O   . ALA H  4 4   ? -4.270  169.030 24.126 1.00 32.32 ?  4   ALA H O   1 
ATOM   7691  C  CB  . ALA H  4 4   ? -4.578  165.996 25.558 1.00 32.86 ?  4   ALA H CB  1 
ATOM   7692  N  N   . VAL H  4 5   ? -3.429  167.266 22.988 1.00 35.62 ?  5   VAL H N   1 
ATOM   7693  C  CA  . VAL H  4 5   ? -3.571  167.927 21.698 1.00 34.64 ?  5   VAL H CA  1 
ATOM   7694  C  C   . VAL H  4 5   ? -3.900  166.885 20.636 1.00 37.16 ?  5   VAL H C   1 
ATOM   7695  O  O   . VAL H  4 5   ? -3.545  165.709 20.753 1.00 36.12 ?  5   VAL H O   1 
ATOM   7696  C  CB  . VAL H  4 5   ? -2.305  168.739 21.346 1.00 36.39 ?  5   VAL H CB  1 
ATOM   7697  C  CG1 . VAL H  4 5   ? -1.134  167.810 21.065 1.00 40.12 ?  5   VAL H CG1 1 
ATOM   7698  C  CG2 . VAL H  4 5   ? -2.584  169.655 20.172 1.00 37.25 ?  5   VAL H CG2 1 
ATOM   7699  N  N   . CYS H  4 6   ? -4.607  167.326 19.601 1.00 34.13 ?  6   CYS H N   1 
ATOM   7700  C  CA  . CYS H  4 6   ? -5.037  166.460 18.518 1.00 31.56 ?  6   CYS H CA  1 
ATOM   7701  C  C   . CYS H  4 6   ? -4.894  167.208 17.198 1.00 32.89 ?  6   CYS H C   1 
ATOM   7702  O  O   . CYS H  4 6   ? -5.409  168.320 17.067 1.00 33.68 ?  6   CYS H O   1 
ATOM   7703  C  CB  . CYS H  4 6   ? -6.494  166.044 18.712 1.00 29.72 ?  6   CYS H CB  1 
ATOM   7704  S  SG  . CYS H  4 6   ? -7.055  164.888 17.450 1.00 38.45 ?  6   CYS H SG  1 
ATOM   7705  N  N   . VAL H  4 7   ? -4.220  166.597 16.225 1.00 32.68 ?  7   VAL H N   1 
ATOM   7706  C  CA  . VAL H  4 7   ? -4.163  167.124 14.864 1.00 31.86 ?  7   VAL H CA  1 
ATOM   7707  C  C   . VAL H  4 7   ? -5.162  166.348 14.019 1.00 28.95 ?  7   VAL H C   1 
ATOM   7708  O  O   . VAL H  4 7   ? -4.995  165.148 13.790 1.00 33.84 ?  7   VAL H O   1 
ATOM   7709  C  CB  . VAL H  4 7   ? -2.755  167.031 14.256 1.00 33.06 ?  7   VAL H CB  1 
ATOM   7710  C  CG1 . VAL H  4 7   ? -2.780  167.586 12.825 1.00 32.98 ?  7   VAL H CG1 1 
ATOM   7711  C  CG2 . VAL H  4 7   ? -1.744  167.797 15.111 1.00 30.35 ?  7   VAL H CG2 1 
ATOM   7712  N  N   . LEU H  4 8   ? -6.188  167.044 13.551 1.00 30.36 ?  8   LEU H N   1 
ATOM   7713  C  CA  . LEU H  4 8   ? -7.245  166.464 12.737 1.00 34.85 ?  8   LEU H CA  1 
ATOM   7714  C  C   . LEU H  4 8   ? -6.876  166.547 11.260 1.00 32.40 ?  8   LEU H C   1 
ATOM   7715  O  O   . LEU H  4 8   ? -6.667  167.648 10.733 1.00 34.05 ?  8   LEU H O   1 
ATOM   7716  C  CB  . LEU H  4 8   ? -8.540  167.216 12.990 1.00 29.46 ?  8   LEU H CB  1 
ATOM   7717  C  CG  . LEU H  4 8   ? -9.068  167.088 14.412 1.00 37.14 ?  8   LEU H CG  1 
ATOM   7718  C  CD1 . LEU H  4 8   ? -10.209 168.057 14.581 1.00 32.02 ?  8   LEU H CD1 1 
ATOM   7719  C  CD2 . LEU H  4 8   ? -9.550  165.691 14.611 1.00 31.48 ?  8   LEU H CD2 1 
ATOM   7720  N  N   . LYS H  4 9   ? -6.803  165.392 10.602 1.00 34.93 ?  9   LYS H N   1 
ATOM   7721  C  CA  . LYS H  4 9   ? -6.614  165.289 9.159  1.00 37.13 ?  9   LYS H CA  1 
ATOM   7722  C  C   . LYS H  4 9   ? -7.640  164.311 8.602  1.00 39.98 ?  9   LYS H C   1 
ATOM   7723  O  O   . LYS H  4 9   ? -8.101  163.407 9.303  1.00 35.05 ?  9   LYS H O   1 
ATOM   7724  C  CB  . LYS H  4 9   ? -5.210  164.793 8.776  1.00 35.82 ?  9   LYS H CB  1 
ATOM   7725  C  CG  . LYS H  4 9   ? -4.032  165.617 9.290  1.00 41.79 ?  9   LYS H CG  1 
ATOM   7726  C  CD  . LYS H  4 9   ? -4.192  167.110 8.994  1.00 45.74 ?  9   LYS H CD  1 
ATOM   7727  C  CE  . LYS H  4 9   ? -2.839  167.825 8.871  1.00 51.60 ?  9   LYS H CE  1 
ATOM   7728  N  NZ  . LYS H  4 9   ? -1.711  167.014 9.452  1.00 58.56 ?  9   LYS H NZ  1 
ATOM   7729  N  N   . GLY H  4 10  ? -7.970  164.473 7.329  1.00 34.15 ?  10  GLY H N   1 
ATOM   7730  C  CA  . GLY H  4 10  ? -8.833  163.516 6.655  1.00 40.17 ?  10  GLY H CA  1 
ATOM   7731  C  C   . GLY H  4 10  ? -8.571  163.416 5.165  1.00 44.07 ?  10  GLY H C   1 
ATOM   7732  O  O   . GLY H  4 10  ? -7.550  163.912 4.682  1.00 43.32 ?  10  GLY H O   1 
ATOM   7733  N  N   . ASP H  4 11  ? -9.489  162.782 4.426  1.00 48.78 ?  11  ASP H N   1 
ATOM   7734  C  CA  . ASP H  4 11  ? -9.334  162.658 2.978  1.00 49.02 ?  11  ASP H CA  1 
ATOM   7735  C  C   . ASP H  4 11  ? -9.563  163.969 2.248  1.00 48.23 ?  11  ASP H C   1 
ATOM   7736  O  O   . ASP H  4 11  ? -9.090  164.123 1.120  1.00 59.47 ?  11  ASP H O   1 
ATOM   7737  C  CB  . ASP H  4 11  ? -10.315 161.628 2.414  1.00 51.92 ?  11  ASP H CB  1 
ATOM   7738  C  CG  . ASP H  4 11  ? -9.978  160.223 2.827  1.00 66.17 ?  11  ASP H CG  1 
ATOM   7739  O  OD1 . ASP H  4 11  ? -10.926 159.420 3.003  1.00 79.30 -1 11  ASP H OD1 1 
ATOM   7740  O  OD2 . ASP H  4 11  ? -8.768  159.925 2.981  1.00 72.70 ?  11  ASP H OD2 1 
ATOM   7741  N  N   . GLY H  4 12  ? -10.306 164.896 2.838  1.00 40.15 ?  12  GLY H N   1 
ATOM   7742  C  CA  . GLY H  4 12  ? -10.718 166.074 2.135  1.00 36.50 ?  12  GLY H CA  1 
ATOM   7743  C  C   . GLY H  4 12  ? -10.029 167.294 2.680  1.00 37.48 ?  12  GLY H C   1 
ATOM   7744  O  O   . GLY H  4 12  ? -8.930  167.223 3.235  1.00 41.59 ?  12  GLY H O   1 
ATOM   7745  N  N   . PRO H  4 13  ? -10.675 168.450 2.546  1.00 33.16 ?  13  PRO H N   1 
ATOM   7746  C  CA  . PRO H  4 13  ? -10.054 169.697 2.986  1.00 28.42 ?  13  PRO H CA  1 
ATOM   7747  C  C   . PRO H  4 13  ? -10.120 169.933 4.492  1.00 36.59 ?  13  PRO H C   1 
ATOM   7748  O  O   . PRO H  4 13  ? -9.541  170.917 4.964  1.00 30.11 ?  13  PRO H O   1 
ATOM   7749  C  CB  . PRO H  4 13  ? -10.872 170.751 2.231  1.00 30.59 ?  13  PRO H CB  1 
ATOM   7750  C  CG  . PRO H  4 13  ? -12.246 170.165 2.222  1.00 34.01 ?  13  PRO H CG  1 
ATOM   7751  C  CD  . PRO H  4 13  ? -12.036 168.664 2.023  1.00 34.72 ?  13  PRO H CD  1 
ATOM   7752  N  N   . VAL H  4 14  ? -10.795 169.090 5.272  1.00 29.87 ?  14  VAL H N   1 
ATOM   7753  C  CA  . VAL H  4 14  ? -11.008 169.420 6.679  1.00 32.81 ?  14  VAL H CA  1 
ATOM   7754  C  C   . VAL H  4 14  ? -9.742  169.107 7.462  1.00 28.08 ?  14  VAL H C   1 
ATOM   7755  O  O   . VAL H  4 14  ? -9.193  168.001 7.373  1.00 34.47 ?  14  VAL H O   1 
ATOM   7756  C  CB  . VAL H  4 14  ? -12.221 168.677 7.247  1.00 30.75 ?  14  VAL H CB  1 
ATOM   7757  C  CG1 . VAL H  4 14  ? -12.377 169.014 8.747  1.00 29.59 ?  14  VAL H CG1 1 
ATOM   7758  C  CG2 . VAL H  4 14  ? -13.459 169.104 6.480  1.00 30.27 ?  14  VAL H CG2 1 
ATOM   7759  N  N   . GLN H  4 15  ? -9.248  170.101 8.195  1.00 32.32 ?  15  GLN H N   1 
ATOM   7760  C  CA  . GLN H  4 15  ? -8.102  169.891 9.065  1.00 34.81 ?  15  GLN H CA  1 
ATOM   7761  C  C   . GLN H  4 15  ? -8.148  170.907 10.191 1.00 32.07 ?  15  GLN H C   1 
ATOM   7762  O  O   . GLN H  4 15  ? -8.822  171.938 10.109 1.00 33.20 ?  15  GLN H O   1 
ATOM   7763  C  CB  . GLN H  4 15  ? -6.769  170.005 8.313  1.00 35.04 ?  15  GLN H CB  1 
ATOM   7764  C  CG  . GLN H  4 15  ? -6.594  171.306 7.550  1.00 42.87 ?  15  GLN H CG  1 
ATOM   7765  C  CD  . GLN H  4 15  ? -5.246  171.380 6.815  1.00 50.66 ?  15  GLN H CD  1 
ATOM   7766  O  OE1 . GLN H  4 15  ? -4.227  170.882 7.302  1.00 62.22 ?  15  GLN H OE1 1 
ATOM   7767  N  NE2 . GLN H  4 15  ? -5.247  171.991 5.635  1.00 55.60 ?  15  GLN H NE2 1 
ATOM   7768  N  N   . GLY H  4 16  ? -7.413  170.611 11.248 1.00 30.45 ?  16  GLY H N   1 
ATOM   7769  C  CA  . GLY H  4 16  ? -7.455  171.493 12.393 1.00 32.66 ?  16  GLY H CA  1 
ATOM   7770  C  C   . GLY H  4 16  ? -6.559  170.979 13.493 1.00 26.54 ?  16  GLY H C   1 
ATOM   7771  O  O   . GLY H  4 16  ? -5.918  169.926 13.373 1.00 30.07 ?  16  GLY H O   1 
ATOM   7772  N  N   . ILE H  4 17  ? -6.509  171.767 14.564 1.00 31.26 ?  17  ILE H N   1 
ATOM   7773  C  CA  . ILE H  4 17  ? -5.752  171.452 15.764 1.00 32.92 ?  17  ILE H CA  1 
ATOM   7774  C  C   . ILE H  4 17  ? -6.663  171.705 16.952 1.00 32.15 ?  17  ILE H C   1 
ATOM   7775  O  O   . ILE H  4 17  ? -7.230  172.797 17.079 1.00 30.69 ?  17  ILE H O   1 
ATOM   7776  C  CB  . ILE H  4 17  ? -4.481  172.307 15.890 1.00 33.68 ?  17  ILE H CB  1 
ATOM   7777  C  CG1 . ILE H  4 17  ? -3.458  171.894 14.846 1.00 32.79 ?  17  ILE H CG1 1 
ATOM   7778  C  CG2 . ILE H  4 17  ? -3.893  172.184 17.301 1.00 31.60 ?  17  ILE H CG2 1 
ATOM   7779  C  CD1 . ILE H  4 17  ? -2.324  172.890 14.726 1.00 38.22 ?  17  ILE H CD1 1 
ATOM   7780  N  N   . ILE H  4 18  ? -6.815  170.699 17.807 1.00 30.16 ?  18  ILE H N   1 
ATOM   7781  C  CA  . ILE H  4 18  ? -7.696  170.789 18.962 1.00 30.98 ?  18  ILE H CA  1 
ATOM   7782  C  C   . ILE H  4 18  ? -6.878  170.553 20.226 1.00 32.82 ?  18  ILE H C   1 
ATOM   7783  O  O   . ILE H  4 18  ? -6.179  169.538 20.340 1.00 32.29 ?  18  ILE H O   1 
ATOM   7784  C  CB  . ILE H  4 18  ? -8.857  169.787 18.873 1.00 30.49 ?  18  ILE H CB  1 
ATOM   7785  C  CG1 . ILE H  4 18  ? -9.751  170.120 17.680 1.00 29.34 ?  18  ILE H CG1 1 
ATOM   7786  C  CG2 . ILE H  4 18  ? -9.661  169.834 20.186 1.00 32.80 ?  18  ILE H CG2 1 
ATOM   7787  C  CD1 . ILE H  4 18  ? -10.495 171.417 17.825 1.00 26.99 ?  18  ILE H CD1 1 
ATOM   7788  N  N   . ASN H  4 19  ? -6.996  171.477 21.178 1.00 31.74 ?  19  ASN H N   1 
ATOM   7789  C  CA  . ASN H  4 19  ? -6.272  171.441 22.443 1.00 34.63 ?  19  ASN H CA  1 
ATOM   7790  C  C   . ASN H  4 19  ? -7.213  171.043 23.571 1.00 34.24 ?  19  ASN H C   1 
ATOM   7791  O  O   . ASN H  4 19  ? -8.383  171.447 23.584 1.00 34.64 ?  19  ASN H O   1 
ATOM   7792  C  CB  . ASN H  4 19  ? -5.667  172.810 22.770 1.00 32.83 ?  19  ASN H CB  1 
ATOM   7793  C  CG  . ASN H  4 19  ? -4.776  173.333 21.672 1.00 30.36 ?  19  ASN H CG  1 
ATOM   7794  O  OD1 . ASN H  4 19  ? -5.164  174.227 20.928 1.00 35.49 ?  19  ASN H OD1 1 
ATOM   7795  N  ND2 . ASN H  4 19  ? -3.575  172.799 21.580 1.00 32.10 ?  19  ASN H ND2 1 
ATOM   7796  N  N   . PHE H  4 20  ? -6.683  170.276 24.526 1.00 34.69 ?  20  PHE H N   1 
ATOM   7797  C  CA  . PHE H  4 20  ? -7.395  169.859 25.732 1.00 33.07 ?  20  PHE H CA  1 
ATOM   7798  C  C   . PHE H  4 20  ? -6.595  170.279 26.962 1.00 40.07 ?  20  PHE H C   1 
ATOM   7799  O  O   . PHE H  4 20  ? -5.373  170.103 27.009 1.00 38.81 ?  20  PHE H O   1 
ATOM   7800  C  CB  . PHE H  4 20  ? -7.597  168.334 25.795 1.00 37.03 ?  20  PHE H CB  1 
ATOM   7801  C  CG  . PHE H  4 20  ? -8.365  167.753 24.630 1.00 36.39 ?  20  PHE H CG  1 
ATOM   7802  C  CD1 . PHE H  4 20  ? -7.713  167.401 23.455 1.00 37.40 ?  20  PHE H CD1 1 
ATOM   7803  C  CD2 . PHE H  4 20  ? -9.729  167.531 24.726 1.00 35.47 ?  20  PHE H CD2 1 
ATOM   7804  C  CE1 . PHE H  4 20  ? -8.423  166.849 22.376 1.00 34.37 ?  20  PHE H CE1 1 
ATOM   7805  C  CE2 . PHE H  4 20  ? -10.444 166.989 23.664 1.00 37.23 ?  20  PHE H CE2 1 
ATOM   7806  C  CZ  . PHE H  4 20  ? -9.787  166.650 22.488 1.00 35.87 ?  20  PHE H CZ  1 
ATOM   7807  N  N   . GLU H  4 21  ? -7.288  170.793 27.974 1.00 43.28 ?  21  GLU H N   1 
ATOM   7808  C  CA  . GLU H  4 21  ? -6.635  171.276 29.184 1.00 46.07 ?  21  GLU H CA  1 
ATOM   7809  C  C   . GLU H  4 21  ? -7.484  170.881 30.383 1.00 41.83 ?  21  GLU H C   1 
ATOM   7810  O  O   . GLU H  4 21  ? -8.691  171.146 30.398 1.00 40.89 ?  21  GLU H O   1 
ATOM   7811  C  CB  . GLU H  4 21  ? -6.451  172.793 29.123 1.00 44.14 ?  21  GLU H CB  1 
ATOM   7812  C  CG  . GLU H  4 21  ? -5.114  173.271 29.637 1.00 58.59 ?  21  GLU H CG  1 
ATOM   7813  C  CD  . GLU H  4 21  ? -5.189  174.648 30.262 1.00 69.36 ?  21  GLU H CD  1 
ATOM   7814  O  OE1 . GLU H  4 21  ? -4.533  174.850 31.309 1.00 74.23 ?  21  GLU H OE1 1 
ATOM   7815  O  OE2 . GLU H  4 21  ? -5.897  175.521 29.708 1.00 75.10 -1 21  GLU H OE2 1 
ATOM   7816  N  N   . GLN H  4 22  ? -6.867  170.216 31.361 1.00 42.62 ?  22  GLN H N   1 
ATOM   7817  C  CA  . GLN H  4 22  ? -7.563  169.748 32.561 1.00 47.33 ?  22  GLN H CA  1 
ATOM   7818  C  C   . GLN H  4 22  ? -6.740  170.121 33.786 1.00 46.29 ?  22  GLN H C   1 
ATOM   7819  O  O   . GLN H  4 22  ? -5.650  169.578 33.990 1.00 48.21 ?  22  GLN H O   1 
ATOM   7820  C  CB  . GLN H  4 22  ? -7.796  168.241 32.525 1.00 39.63 ?  22  GLN H CB  1 
ATOM   7821  C  CG  . GLN H  4 22  ? -8.666  167.742 33.666 1.00 43.46 ?  22  GLN H CG  1 
ATOM   7822  C  CD  . GLN H  4 22  ? -9.013  166.283 33.528 1.00 44.08 ?  22  GLN H CD  1 
ATOM   7823  O  OE1 . GLN H  4 22  ? -8.217  165.492 33.026 1.00 40.60 ?  22  GLN H OE1 1 
ATOM   7824  N  NE2 . GLN H  4 22  ? -10.214 165.912 33.975 1.00 51.08 ?  22  GLN H NE2 1 
ATOM   7825  N  N   . LYS H  4 23  ? -7.266  171.031 34.605 1.00 54.69 ?  23  LYS H N   1 
ATOM   7826  C  CA  . LYS H  4 23  ? -6.548  171.452 35.807 1.00 53.24 ?  23  LYS H CA  1 
ATOM   7827  C  C   . LYS H  4 23  ? -6.689  170.444 36.955 1.00 49.45 ?  23  LYS H C   1 
ATOM   7828  O  O   . LYS H  4 23  ? -5.685  170.024 37.541 1.00 62.13 ?  23  LYS H O   1 
ATOM   7829  C  CB  . LYS H  4 23  ? -7.026  172.843 36.220 1.00 49.09 ?  23  LYS H CB  1 
ATOM   7830  C  CG  . LYS H  4 23  ? -6.068  173.958 35.786 1.00 55.98 ?  23  LYS H CG  1 
ATOM   7831  C  CD  . LYS H  4 23  ? -6.318  174.421 34.361 1.00 60.69 ?  23  LYS H CD  1 
ATOM   7832  C  CE  . LYS H  4 23  ? -7.810  174.641 34.086 1.00 68.25 ?  23  LYS H CE  1 
ATOM   7833  N  NZ  . LYS H  4 23  ? -8.086  174.777 32.611 1.00 70.67 ?  23  LYS H NZ  1 
ATOM   7834  N  N   . GLU H  4 24  ? -7.910  170.028 37.284 1.00 47.58 ?  24  GLU H N   1 
ATOM   7835  C  CA  . GLU H  4 24  ? -8.150  169.114 38.393 1.00 53.05 ?  24  GLU H CA  1 
ATOM   7836  C  C   . GLU H  4 24  ? -8.488  167.720 37.878 1.00 59.07 ?  24  GLU H C   1 
ATOM   7837  O  O   . GLU H  4 24  ? -9.200  167.577 36.879 1.00 55.04 ?  24  GLU H O   1 
ATOM   7838  C  CB  . GLU H  4 24  ? -9.287  169.616 39.280 1.00 56.07 ?  24  GLU H CB  1 
ATOM   7839  C  CG  . GLU H  4 24  ? -9.196  171.098 39.625 1.00 47.94 ?  24  GLU H CG  1 
ATOM   7840  C  CD  . GLU H  4 24  ? -10.524 171.653 40.106 1.00 52.96 ?  24  GLU H CD  1 
ATOM   7841  O  OE1 . GLU H  4 24  ? -11.102 171.093 41.070 1.00 54.11 ?  24  GLU H OE1 1 
ATOM   7842  O  OE2 . GLU H  4 24  ? -10.997 172.644 39.511 1.00 56.46 -1 24  GLU H OE2 1 
ATOM   7843  N  N   . SER H  4 25  ? -8.022  166.703 38.616 1.00 53.30 ?  25  SER H N   1 
ATOM   7844  C  CA  . SER H  4 25  ? -8.012  165.320 38.139 1.00 54.14 ?  25  SER H CA  1 
ATOM   7845  C  C   . SER H  4 25  ? -9.374  164.854 37.651 1.00 58.80 ?  25  SER H C   1 
ATOM   7846  O  O   . SER H  4 25  ? -9.470  164.163 36.628 1.00 60.97 ?  25  SER H O   1 
ATOM   7847  C  CB  . SER H  4 25  ? -7.519  164.389 39.246 1.00 57.50 ?  25  SER H CB  1 
ATOM   7848  O  OG  . SER H  4 25  ? -6.480  165.001 39.987 1.00 68.07 ?  25  SER H OG  1 
ATOM   7849  N  N   . ASN H  4 26  ? -10.436 165.185 38.378 1.00 58.10 ?  26  ASN H N   1 
ATOM   7850  C  CA  . ASN H  4 26  ? -11.787 164.854 37.940 1.00 65.16 ?  26  ASN H CA  1 
ATOM   7851  C  C   . ASN H  4 26  ? -12.568 166.089 37.507 1.00 65.48 ?  26  ASN H C   1 
ATOM   7852  O  O   . ASN H  4 26  ? -13.797 166.018 37.352 1.00 67.36 ?  26  ASN H O   1 
ATOM   7853  C  CB  . ASN H  4 26  ? -12.538 164.103 39.046 1.00 71.95 ?  26  ASN H CB  1 
ATOM   7854  C  CG  . ASN H  4 26  ? -13.000 165.024 40.179 1.00 83.82 ?  26  ASN H CG  1 
ATOM   7855  O  OD1 . ASN H  4 26  ? -12.356 165.097 41.237 1.00 82.13 ?  26  ASN H OD1 1 
ATOM   7856  N  ND2 . ASN H  4 26  ? -14.131 165.716 39.971 1.00 77.96 ?  26  ASN H ND2 1 
ATOM   7857  N  N   . GLY H  4 27  ? -11.881 167.220 37.302 1.00 57.62 ?  27  GLY H N   1 
ATOM   7858  C  CA  . GLY H  4 27  ? -12.538 168.449 36.924 1.00 58.57 ?  27  GLY H CA  1 
ATOM   7859  C  C   . GLY H  4 27  ? -12.847 168.514 35.443 1.00 53.07 ?  27  GLY H C   1 
ATOM   7860  O  O   . GLY H  4 27  ? -12.600 167.576 34.665 1.00 50.47 ?  27  GLY H O   1 
ATOM   7861  N  N   . PRO H  4 28  ? -13.404 169.649 35.032 1.00 48.09 ?  28  PRO H N   1 
ATOM   7862  C  CA  . PRO H  4 28  ? -13.767 169.828 33.623 1.00 48.54 ?  28  PRO H CA  1 
ATOM   7863  C  C   . PRO H  4 28  ? -12.541 169.914 32.722 1.00 48.03 ?  28  PRO H C   1 
ATOM   7864  O  O   . PRO H  4 28  ? -11.459 170.336 33.137 1.00 44.07 ?  28  PRO H O   1 
ATOM   7865  C  CB  . PRO H  4 28  ? -14.546 171.147 33.633 1.00 42.82 ?  28  PRO H CB  1 
ATOM   7866  C  CG  . PRO H  4 28  ? -13.994 171.880 34.799 1.00 45.72 ?  28  PRO H CG  1 
ATOM   7867  C  CD  . PRO H  4 28  ? -13.761 170.828 35.836 1.00 40.00 ?  28  PRO H CD  1 
ATOM   7868  N  N   . VAL H  4 29  ? -12.725 169.500 31.467 1.00 49.42 ?  29  VAL H N   1 
ATOM   7869  C  CA  . VAL H  4 29  ? -11.695 169.592 30.433 1.00 40.55 ?  29  VAL H CA  1 
ATOM   7870  C  C   . VAL H  4 29  ? -12.082 170.708 29.477 1.00 42.22 ?  29  VAL H C   1 
ATOM   7871  O  O   . VAL H  4 29  ? -13.197 170.710 28.941 1.00 41.04 ?  29  VAL H O   1 
ATOM   7872  C  CB  . VAL H  4 29  ? -11.529 168.263 29.676 1.00 42.08 ?  29  VAL H CB  1 
ATOM   7873  C  CG1 . VAL H  4 29  ? -10.481 168.398 28.540 1.00 36.01 ?  29  VAL H CG1 1 
ATOM   7874  C  CG2 . VAL H  4 29  ? -11.148 167.164 30.630 1.00 40.14 ?  29  VAL H CG2 1 
ATOM   7875  N  N   . LYS H  4 30  ? -11.167 171.655 29.275 1.00 39.32 ?  30  LYS H N   1 
ATOM   7876  C  CA  . LYS H  4 30  ? -11.348 172.715 28.292 1.00 42.95 ?  30  LYS H CA  1 
ATOM   7877  C  C   . LYS H  4 30  ? -10.919 172.202 26.926 1.00 38.85 ?  30  LYS H C   1 
ATOM   7878  O  O   . LYS H  4 30  ? -9.841  171.619 26.792 1.00 41.57 ?  30  LYS H O   1 
ATOM   7879  C  CB  . LYS H  4 30  ? -10.511 173.941 28.661 1.00 40.36 ?  30  LYS H CB  1 
ATOM   7880  C  CG  . LYS H  4 30  ? -11.172 174.907 29.624 1.00 53.69 ?  30  LYS H CG  1 
ATOM   7881  C  CD  . LYS H  4 30  ? -10.381 176.227 29.740 1.00 59.87 ?  30  LYS H CD  1 
ATOM   7882  C  CE  . LYS H  4 30  ? -9.768  176.659 28.395 1.00 58.00 ?  30  LYS H CE  1 
ATOM   7883  N  NZ  . LYS H  4 30  ? -8.743  177.771 28.502 1.00 55.63 ?  30  LYS H NZ  1 
ATOM   7884  N  N   . VAL H  4 31  ? -11.760 172.410 25.916 1.00 40.13 ?  31  VAL H N   1 
ATOM   7885  C  CA  . VAL H  4 31  ? -11.465 171.997 24.544 1.00 36.39 ?  31  VAL H CA  1 
ATOM   7886  C  C   . VAL H  4 31  ? -11.537 173.237 23.670 1.00 40.02 ?  31  VAL H C   1 
ATOM   7887  O  O   . VAL H  4 31  ? -12.575 173.906 23.627 1.00 37.93 ?  31  VAL H O   1 
ATOM   7888  C  CB  . VAL H  4 31  ? -12.436 170.928 24.036 1.00 30.11 ?  31  VAL H CB  1 
ATOM   7889  C  CG1 . VAL H  4 31  ? -11.989 170.429 22.668 1.00 26.09 ?  31  VAL H CG1 1 
ATOM   7890  C  CG2 . VAL H  4 31  ? -12.525 169.760 25.032 1.00 35.37 ?  31  VAL H CG2 1 
ATOM   7891  N  N   . TRP H  4 32  ? -10.441 173.536 22.973 1.00 35.00 ?  32  TRP H N   1 
ATOM   7892  C  CA  . TRP H  4 32  ? -10.392 174.733 22.150 1.00 33.51 ?  32  TRP H CA  1 
ATOM   7893  C  C   . TRP H  4 32  ? -9.431  174.516 20.989 1.00 34.69 ?  32  TRP H C   1 
ATOM   7894  O  O   . TRP H  4 32  ? -8.460  173.759 21.097 1.00 32.38 ?  32  TRP H O   1 
ATOM   7895  C  CB  . TRP H  4 32  ? -9.972  175.980 22.955 1.00 35.27 ?  32  TRP H CB  1 
ATOM   7896  C  CG  . TRP H  4 32  ? -8.519  175.978 23.403 1.00 37.39 ?  32  TRP H CG  1 
ATOM   7897  C  CD1 . TRP H  4 32  ? -8.012  175.416 24.539 1.00 38.07 ?  32  TRP H CD1 1 
ATOM   7898  C  CD2 . TRP H  4 32  ? -7.399  176.570 22.714 1.00 38.35 ?  32  TRP H CD2 1 
ATOM   7899  N  NE1 . TRP H  4 32  ? -6.647  175.620 24.602 1.00 36.84 ?  32  TRP H NE1 1 
ATOM   7900  C  CE2 . TRP H  4 32  ? -6.249  176.320 23.488 1.00 36.66 ?  32  TRP H CE2 1 
ATOM   7901  C  CE3 . TRP H  4 32  ? -7.262  177.282 21.513 1.00 46.19 ?  32  TRP H CE3 1 
ATOM   7902  C  CZ2 . TRP H  4 32  ? -4.971  176.765 23.107 1.00 39.01 ?  32  TRP H CZ2 1 
ATOM   7903  C  CZ3 . TRP H  4 32  ? -5.980  177.721 21.124 1.00 42.60 ?  32  TRP H CZ3 1 
ATOM   7904  C  CH2 . TRP H  4 32  ? -4.859  177.467 21.926 1.00 39.51 ?  32  TRP H CH2 1 
ATOM   7905  N  N   . GLY H  4 33  ? -9.731  175.182 19.874 1.00 30.99 ?  33  GLY H N   1 
ATOM   7906  C  CA  . GLY H  4 33  ? -8.866  175.170 18.711 1.00 32.77 ?  33  GLY H CA  1 
ATOM   7907  C  C   . GLY H  4 33  ? -9.657  175.475 17.445 1.00 31.38 ?  33  GLY H C   1 
ATOM   7908  O  O   . GLY H  4 33  ? -10.817 175.867 17.490 1.00 35.33 ?  33  GLY H O   1 
ATOM   7909  N  N   . SER H  4 34  ? -9.009  175.274 16.300 1.00 35.13 ?  34  SER H N   1 
ATOM   7910  C  CA  . SER H  4 34  ? -9.584  175.696 15.028 1.00 31.66 ?  34  SER H CA  1 
ATOM   7911  C  C   . SER H  4 34  ? -9.650  174.514 14.075 1.00 30.28 ?  34  SER H C   1 
ATOM   7912  O  O   . SER H  4 34  ? -8.680  173.768 13.940 1.00 33.21 ?  34  SER H O   1 
ATOM   7913  C  CB  . SER H  4 34  ? -8.762  176.832 14.416 1.00 43.51 ?  34  SER H CB  1 
ATOM   7914  O  OG  . SER H  4 34  ? -9.532  177.598 13.516 1.00 46.33 ?  34  SER H OG  1 
ATOM   7915  N  N   . ILE H  4 35  ? -10.804 174.340 13.443 1.00 31.39 ?  35  ILE H N   1 
ATOM   7916  C  CA  . ILE H  4 35  ? -10.983 173.386 12.353 1.00 31.91 ?  35  ILE H CA  1 
ATOM   7917  C  C   . ILE H  4 35  ? -11.461 174.169 11.146 1.00 30.33 ?  35  ILE H C   1 
ATOM   7918  O  O   . ILE H  4 35  ? -12.429 174.938 11.232 1.00 30.14 ?  35  ILE H O   1 
ATOM   7919  C  CB  . ILE H  4 35  ? -11.987 172.274 12.701 1.00 29.63 ?  35  ILE H CB  1 
ATOM   7920  C  CG1 . ILE H  4 35  ? -11.593 171.570 13.993 1.00 32.70 ?  35  ILE H CG1 1 
ATOM   7921  C  CG2 . ILE H  4 35  ? -12.055 171.261 11.570 1.00 24.19 ?  35  ILE H CG2 1 
ATOM   7922  C  CD1 . ILE H  4 35  ? -12.701 170.738 14.524 1.00 34.24 ?  35  ILE H CD1 1 
ATOM   7923  N  N   . LYS H  4 36  ? -10.760 174.015 10.037 1.00 30.88 ?  36  LYS H N   1 
ATOM   7924  C  CA  . LYS H  4 36  ? -11.119 174.735 8.823  1.00 33.00 ?  36  LYS H CA  1 
ATOM   7925  C  C   . LYS H  4 36  ? -11.504 173.735 7.740  1.00 31.78 ?  36  LYS H C   1 
ATOM   7926  O  O   . LYS H  4 36  ? -11.312 172.519 7.880  1.00 29.00 ?  36  LYS H O   1 
ATOM   7927  C  CB  . LYS H  4 36  ? -9.966  175.638 8.361  1.00 32.44 ?  36  LYS H CB  1 
ATOM   7928  C  CG  . LYS H  4 36  ? -8.714  174.860 8.041  1.00 36.56 ?  36  LYS H CG  1 
ATOM   7929  C  CD  . LYS H  4 36  ? -7.529  175.769 7.734  1.00 44.55 ?  36  LYS H CD  1 
ATOM   7930  C  CE  . LYS H  4 36  ? -6.693  175.179 6.600  1.00 48.74 ?  36  LYS H CE  1 
ATOM   7931  N  NZ  . LYS H  4 36  ? -5.238  175.296 6.883  1.00 56.96 ?  36  LYS H NZ  1 
ATOM   7932  N  N   . GLY H  4 37  ? -12.075 174.266 6.661  1.00 34.29 ?  37  GLY H N   1 
ATOM   7933  C  CA  . GLY H  4 37  ? -12.496 173.447 5.547  1.00 30.20 ?  37  GLY H CA  1 
ATOM   7934  C  C   . GLY H  4 37  ? -13.844 172.784 5.705  1.00 32.64 ?  37  GLY H C   1 
ATOM   7935  O  O   . GLY H  4 37  ? -14.155 171.859 4.949  1.00 30.23 ?  37  GLY H O   1 
ATOM   7936  N  N   . LEU H  4 38  ? -14.665 173.236 6.650  1.00 31.67 ?  38  LEU H N   1 
ATOM   7937  C  CA  . LEU H  4 38  ? -15.960 172.629 6.930  1.00 33.48 ?  38  LEU H CA  1 
ATOM   7938  C  C   . LEU H  4 38  ? -17.068 173.384 6.224  1.00 35.85 ?  38  LEU H C   1 
ATOM   7939  O  O   . LEU H  4 38  ? -16.971 174.588 5.993  1.00 32.56 ?  38  LEU H O   1 
ATOM   7940  C  CB  . LEU H  4 38  ? -16.274 172.623 8.434  1.00 30.61 ?  38  LEU H CB  1 
ATOM   7941  C  CG  . LEU H  4 38  ? -15.407 171.733 9.303  1.00 28.36 ?  38  LEU H CG  1 
ATOM   7942  C  CD1 . LEU H  4 38  ? -15.433 172.250 10.755 1.00 30.71 ?  38  LEU H CD1 1 
ATOM   7943  C  CD2 . LEU H  4 38  ? -15.904 170.301 9.215  1.00 31.76 ?  38  LEU H CD2 1 
ATOM   7944  N  N   . THR H  4 39  ? -18.153 172.686 5.924  1.00 33.66 ?  39  THR H N   1 
ATOM   7945  C  CA  . THR H  4 39  ? -19.335 173.406 5.476  1.00 32.24 ?  39  THR H CA  1 
ATOM   7946  C  C   . THR H  4 39  ? -19.915 174.196 6.643  1.00 32.76 ?  39  THR H C   1 
ATOM   7947  O  O   . THR H  4 39  ? -19.901 173.739 7.789  1.00 31.84 ?  39  THR H O   1 
ATOM   7948  C  CB  . THR H  4 39  ? -20.384 172.442 4.940  1.00 35.76 ?  39  THR H CB  1 
ATOM   7949  O  OG1 . THR H  4 39  ? -20.710 171.521 5.974  1.00 33.42 ?  39  THR H OG1 1 
ATOM   7950  C  CG2 . THR H  4 39  ? -19.866 171.675 3.735  1.00 35.67 ?  39  THR H CG2 1 
ATOM   7951  N  N   . GLU H  4 40  ? -20.446 175.373 6.339  1.00 31.29 ?  40  GLU H N   1 
ATOM   7952  C  CA  . GLU H  4 40  ? -21.038 176.234 7.351  1.00 34.42 ?  40  GLU H CA  1 
ATOM   7953  C  C   . GLU H  4 40  ? -22.118 175.484 8.126  1.00 34.98 ?  40  GLU H C   1 
ATOM   7954  O  O   . GLU H  4 40  ? -22.908 174.739 7.545  1.00 33.57 ?  40  GLU H O   1 
ATOM   7955  C  CB  . GLU H  4 40  ? -21.635 177.467 6.680  1.00 30.48 ?  40  GLU H CB  1 
ATOM   7956  C  CG  . GLU H  4 40  ? -22.370 178.380 7.653  1.00 34.54 ?  40  GLU H CG  1 
ATOM   7957  C  CD  . GLU H  4 40  ? -22.822 179.679 7.011  1.00 44.13 ?  40  GLU H CD  1 
ATOM   7958  O  OE1 . GLU H  4 40  ? -22.547 179.869 5.808  1.00 49.91 ?  40  GLU H OE1 1 
ATOM   7959  O  OE2 . GLU H  4 40  ? -23.449 180.515 7.706  1.00 55.22 -1 40  GLU H OE2 1 
ATOM   7960  N  N   . GLY H  4 41  ? -22.136 175.650 9.447  1.00 35.09 ?  41  GLY H N   1 
ATOM   7961  C  CA  . GLY H  4 41  ? -23.159 174.991 10.242 1.00 33.57 ?  41  GLY H CA  1 
ATOM   7962  C  C   . GLY H  4 41  ? -22.656 173.968 11.241 1.00 33.34 ?  41  GLY H C   1 
ATOM   7963  O  O   . GLY H  4 41  ? -21.459 173.922 11.533 1.00 31.31 ?  41  GLY H O   1 
ATOM   7964  N  N   . LEU H  4 42  ? -23.571 173.145 11.762 1.00 33.81 ?  42  LEU H N   1 
ATOM   7965  C  CA  . LEU H  4 42  ? -23.262 172.241 12.866 1.00 34.34 ?  42  LEU H CA  1 
ATOM   7966  C  C   . LEU H  4 42  ? -22.549 170.995 12.369 1.00 34.45 ?  42  LEU H C   1 
ATOM   7967  O  O   . LEU H  4 42  ? -22.913 170.424 11.336 1.00 36.33 ?  42  LEU H O   1 
ATOM   7968  C  CB  . LEU H  4 42  ? -24.546 171.832 13.590 1.00 33.70 ?  42  LEU H CB  1 
ATOM   7969  C  CG  . LEU H  4 42  ? -25.302 172.953 14.289 1.00 38.90 ?  42  LEU H CG  1 
ATOM   7970  C  CD1 . LEU H  4 42  ? -26.755 172.581 14.518 1.00 35.05 ?  42  LEU H CD1 1 
ATOM   7971  C  CD2 . LEU H  4 42  ? -24.616 173.258 15.618 1.00 39.56 ?  42  LEU H CD2 1 
ATOM   7972  N  N   . HIS H  4 43  ? -21.535 170.567 13.110 1.00 30.38 ?  43  HIS H N   1 
ATOM   7973  C  CA  . HIS H  4 43  ? -20.831 169.324 12.810 1.00 30.70 ?  43  HIS H CA  1 
ATOM   7974  C  C   . HIS H  4 43  ? -20.664 168.512 14.084 1.00 33.75 ?  43  HIS H C   1 
ATOM   7975  O  O   . HIS H  4 43  ? -20.264 169.057 15.117 1.00 30.40 ?  43  HIS H O   1 
ATOM   7976  C  CB  . HIS H  4 43  ? -19.474 169.598 12.174 1.00 24.48 ?  43  HIS H CB  1 
ATOM   7977  C  CG  . HIS H  4 43  ? -19.576 170.134 10.784 1.00 28.96 ?  43  HIS H CG  1 
ATOM   7978  N  ND1 . HIS H  4 43  ? -19.517 169.321 9.670  1.00 32.90 ?  43  HIS H ND1 1 
ATOM   7979  C  CD2 . HIS H  4 43  ? -19.791 171.393 10.329 1.00 30.78 ?  43  HIS H CD2 1 
ATOM   7980  C  CE1 . HIS H  4 43  ? -19.668 170.062 8.585  1.00 32.98 ?  43  HIS H CE1 1 
ATOM   7981  N  NE2 . HIS H  4 43  ? -19.835 171.320 8.956  1.00 34.41 ?  43  HIS H NE2 1 
ATOM   7982  N  N   . GLY H  4 44  ? -20.968 167.218 14.007 1.00 29.85 ?  44  GLY H N   1 
ATOM   7983  C  CA  . GLY H  4 44  ? -20.770 166.358 15.159 1.00 32.45 ?  44  GLY H CA  1 
ATOM   7984  C  C   . GLY H  4 44  ? -19.301 166.262 15.528 1.00 31.89 ?  44  GLY H C   1 
ATOM   7985  O  O   . GLY H  4 44  ? -18.425 166.226 14.668 1.00 29.38 ?  44  GLY H O   1 
ATOM   7986  N  N   . PHE H  4 45  ? -19.040 166.169 16.830 1.00 29.35 ?  45  PHE H N   1 
ATOM   7987  C  CA  . PHE H  4 45  ? -17.697 166.319 17.393 1.00 29.08 ?  45  PHE H CA  1 
ATOM   7988  C  C   . PHE H  4 45  ? -17.569 165.293 18.514 1.00 30.80 ?  45  PHE H C   1 
ATOM   7989  O  O   . PHE H  4 45  ? -18.114 165.504 19.601 1.00 31.19 ?  45  PHE H O   1 
ATOM   7990  C  CB  . PHE H  4 45  ? -17.530 167.735 17.912 1.00 24.77 ?  45  PHE H CB  1 
ATOM   7991  C  CG  . PHE H  4 45  ? -16.114 168.122 18.241 1.00 33.89 ?  45  PHE H CG  1 
ATOM   7992  C  CD1 . PHE H  4 45  ? -15.142 168.181 17.253 1.00 32.10 ?  45  PHE H CD1 1 
ATOM   7993  C  CD2 . PHE H  4 45  ? -15.770 168.484 19.537 1.00 31.43 ?  45  PHE H CD2 1 
ATOM   7994  C  CE1 . PHE H  4 45  ? -13.848 168.580 17.550 1.00 32.36 ?  45  PHE H CE1 1 
ATOM   7995  C  CE2 . PHE H  4 45  ? -14.477 168.880 19.840 1.00 31.99 ?  45  PHE H CE2 1 
ATOM   7996  C  CZ  . PHE H  4 45  ? -13.513 168.928 18.835 1.00 33.16 ?  45  PHE H CZ  1 
ATOM   7997  N  N   . HIS H  4 46  ? -16.868 164.185 18.258 1.00 30.74 ?  46  HIS H N   1 
ATOM   7998  C  CA  . HIS H  4 46  ? -16.916 163.040 19.159 1.00 30.48 ?  46  HIS H CA  1 
ATOM   7999  C  C   . HIS H  4 46  ? -15.546 162.421 19.346 1.00 33.97 ?  46  HIS H C   1 
ATOM   8000  O  O   . HIS H  4 46  ? -14.745 162.366 18.407 1.00 33.41 ?  46  HIS H O   1 
ATOM   8001  C  CB  . HIS H  4 46  ? -17.851 161.954 18.636 1.00 29.41 ?  46  HIS H CB  1 
ATOM   8002  C  CG  . HIS H  4 46  ? -19.201 162.457 18.261 1.00 29.58 ?  46  HIS H CG  1 
ATOM   8003  N  ND1 . HIS H  4 46  ? -19.770 162.206 17.032 1.00 31.16 ?  46  HIS H ND1 1 
ATOM   8004  C  CD2 . HIS H  4 46  ? -20.097 163.204 18.949 1.00 29.08 ?  46  HIS H CD2 1 
ATOM   8005  C  CE1 . HIS H  4 46  ? -20.967 162.762 16.983 1.00 32.35 ?  46  HIS H CE1 1 
ATOM   8006  N  NE2 . HIS H  4 46  ? -21.189 163.380 18.132 1.00 32.04 ?  46  HIS H NE2 1 
ATOM   8007  N  N   . VAL H  4 47  ? -15.298 161.939 20.562 1.00 34.93 ?  47  VAL H N   1 
ATOM   8008  C  CA  . VAL H  4 47  ? -14.164 161.064 20.838 1.00 33.96 ?  47  VAL H CA  1 
ATOM   8009  C  C   . VAL H  4 47  ? -14.605 159.628 20.585 1.00 36.69 ?  47  VAL H C   1 
ATOM   8010  O  O   . VAL H  4 47  ? -15.573 159.151 21.187 1.00 39.98 ?  47  VAL H O   1 
ATOM   8011  C  CB  . VAL H  4 47  ? -13.656 161.226 22.278 1.00 33.97 ?  47  VAL H CB  1 
ATOM   8012  C  CG1 . VAL H  4 47  ? -12.460 160.319 22.484 1.00 31.77 ?  47  VAL H CG1 1 
ATOM   8013  C  CG2 . VAL H  4 47  ? -13.286 162.672 22.567 1.00 34.10 ?  47  VAL H CG2 1 
ATOM   8014  N  N   . HIS H  4 48  ? -13.898 158.946 19.697 1.00 34.26 ?  48  HIS H N   1 
ATOM   8015  C  CA  . HIS H  4 48  ? -14.138 157.548 19.379 1.00 36.79 ?  48  HIS H CA  1 
ATOM   8016  C  C   . HIS H  4 48  ? -13.132 156.672 20.110 1.00 38.88 ?  48  HIS H C   1 
ATOM   8017  O  O   . HIS H  4 48  ? -12.102 157.138 20.606 1.00 38.62 ?  48  HIS H O   1 
ATOM   8018  C  CB  . HIS H  4 48  ? -14.056 157.300 17.870 1.00 31.26 ?  48  HIS H CB  1 
ATOM   8019  C  CG  . HIS H  4 48  ? -15.153 157.956 17.088 1.00 35.18 ?  48  HIS H CG  1 
ATOM   8020  N  ND1 . HIS H  4 48  ? -15.999 157.252 16.259 1.00 34.42 ?  48  HIS H ND1 1 
ATOM   8021  C  CD2 . HIS H  4 48  ? -15.537 159.252 17.002 1.00 34.59 ?  48  HIS H CD2 1 
ATOM   8022  C  CE1 . HIS H  4 48  ? -16.861 158.084 15.699 1.00 32.44 ?  48  HIS H CE1 1 
ATOM   8023  N  NE2 . HIS H  4 48  ? -16.600 159.305 16.129 1.00 34.54 ?  48  HIS H NE2 1 
ATOM   8024  N  N   . GLU H  4 49  ? -13.430 155.375 20.144 1.00 39.92 ?  49  GLU H N   1 
ATOM   8025  C  CA  . GLU H  4 49  ? -12.792 154.513 21.133 1.00 36.41 ?  49  GLU H CA  1 
ATOM   8026  C  C   . GLU H  4 49  ? -11.320 154.254 20.814 1.00 39.46 ?  49  GLU H C   1 
ATOM   8027  O  O   . GLU H  4 49  ? -10.477 154.257 21.716 1.00 39.85 ?  49  GLU H O   1 
ATOM   8028  C  CB  . GLU H  4 49  ? -13.566 153.198 21.238 1.00 43.45 ?  49  GLU H CB  1 
ATOM   8029  C  CG  . GLU H  4 49  ? -12.817 152.129 22.012 1.00 49.33 ?  49  GLU H CG  1 
ATOM   8030  C  CD  . GLU H  4 49  ? -13.699 150.967 22.450 1.00 51.48 ?  49  GLU H CD  1 
ATOM   8031  O  OE1 . GLU H  4 49  ? -13.312 150.271 23.417 1.00 52.73 ?  49  GLU H OE1 1 
ATOM   8032  O  OE2 . GLU H  4 49  ? -14.756 150.745 21.817 1.00 50.39 -1 49  GLU H OE2 1 
ATOM   8033  N  N   . PHE H  4 50  ? -10.976 154.033 19.550 1.00 41.22 ?  50  PHE H N   1 
ATOM   8034  C  CA  . PHE H  4 50  ? -9.636  153.569 19.210 1.00 40.06 ?  50  PHE H CA  1 
ATOM   8035  C  C   . PHE H  4 50  ? -8.816  154.687 18.578 1.00 38.90 ?  50  PHE H C   1 
ATOM   8036  O  O   . PHE H  4 50  ? -9.295  155.373 17.671 1.00 40.08 ?  50  PHE H O   1 
ATOM   8037  C  CB  . PHE H  4 50  ? -9.721  152.363 18.274 1.00 40.46 ?  50  PHE H CB  1 
ATOM   8038  C  CG  . PHE H  4 50  ? -10.577 151.258 18.819 1.00 43.04 ?  50  PHE H CG  1 
ATOM   8039  C  CD1 . PHE H  4 50  ? -10.282 150.684 20.049 1.00 42.67 ?  50  PHE H CD1 1 
ATOM   8040  C  CD2 . PHE H  4 50  ? -11.692 150.819 18.129 1.00 45.29 ?  50  PHE H CD2 1 
ATOM   8041  C  CE1 . PHE H  4 50  ? -11.069 149.673 20.559 1.00 44.79 ?  50  PHE H CE1 1 
ATOM   8042  C  CE2 . PHE H  4 50  ? -12.483 149.802 18.637 1.00 46.55 ?  50  PHE H CE2 1 
ATOM   8043  C  CZ  . PHE H  4 50  ? -12.175 149.237 19.856 1.00 43.56 ?  50  PHE H CZ  1 
ATOM   8044  N  N   . GLY H  4 51  ? -7.589  154.866 19.064 1.00 39.54 ?  51  GLY H N   1 
ATOM   8045  C  CA  . GLY H  4 51  ? -6.596  155.682 18.386 1.00 36.10 ?  51  GLY H CA  1 
ATOM   8046  C  C   . GLY H  4 51  ? -5.939  154.924 17.250 1.00 40.30 ?  51  GLY H C   1 
ATOM   8047  O  O   . GLY H  4 51  ? -4.713  154.946 17.086 1.00 42.02 ?  51  GLY H O   1 
ATOM   8048  N  N   . ASP H  4 52  ? -6.759  154.226 16.468 1.00 40.94 ?  52  ASP H N   1 
ATOM   8049  C  CA  . ASP H  4 52  ? -6.320  153.419 15.336 1.00 39.29 ?  52  ASP H CA  1 
ATOM   8050  C  C   . ASP H  4 52  ? -6.667  154.165 14.056 1.00 41.56 ?  52  ASP H C   1 
ATOM   8051  O  O   . ASP H  4 52  ? -7.847  154.323 13.727 1.00 40.84 ?  52  ASP H O   1 
ATOM   8052  C  CB  . ASP H  4 52  ? -6.978  152.040 15.371 1.00 40.69 ?  52  ASP H CB  1 
ATOM   8053  C  CG  . ASP H  4 52  ? -6.434  151.098 14.306 1.00 45.72 ?  52  ASP H CG  1 
ATOM   8054  O  OD1 . ASP H  4 52  ? -5.795  151.566 13.335 1.00 43.75 ?  52  ASP H OD1 1 
ATOM   8055  O  OD2 . ASP H  4 52  ? -6.648  149.873 14.438 1.00 56.03 -1 52  ASP H OD2 1 
ATOM   8056  N  N   . ASN H  4 53  ? -5.641  154.613 13.331 1.00 38.73 ?  53  ASN H N   1 
ATOM   8057  C  CA  . ASN H  4 53  ? -5.848  155.334 12.079 1.00 38.41 ?  53  ASN H CA  1 
ATOM   8058  C  C   . ASN H  4 53  ? -5.324  154.555 10.874 1.00 41.29 ?  53  ASN H C   1 
ATOM   8059  O  O   . ASN H  4 53  ? -5.101  155.136 9.809  1.00 44.12 ?  53  ASN H O   1 
ATOM   8060  C  CB  . ASN H  4 53  ? -5.195  156.715 12.167 1.00 40.13 ?  53  ASN H CB  1 
ATOM   8061  C  CG  . ASN H  4 53  ? -5.601  157.638 11.024 1.00 52.39 ?  53  ASN H CG  1 
ATOM   8062  O  OD1 . ASN H  4 53  ? -4.785  157.972 10.158 1.00 54.96 ?  53  ASN H OD1 1 
ATOM   8063  N  ND2 . ASN H  4 53  ? -6.863  158.052 11.016 1.00 56.64 ?  53  ASN H ND2 1 
ATOM   8064  N  N   . THR H  4 54  ? -5.125  153.243 11.018 1.00 38.29 ?  54  THR H N   1 
ATOM   8065  C  CA  . THR H  4 54  ? -4.511  152.459 9.954  1.00 42.21 ?  54  THR H CA  1 
ATOM   8066  C  C   . THR H  4 54  ? -5.371  152.405 8.705  1.00 46.39 ?  54  THR H C   1 
ATOM   8067  O  O   . THR H  4 54  ? -4.847  152.136 7.621  1.00 53.30 ?  54  THR H O   1 
ATOM   8068  C  CB  . THR H  4 54  ? -4.225  151.038 10.427 1.00 43.31 ?  54  THR H CB  1 
ATOM   8069  O  OG1 . THR H  4 54  ? -5.422  150.463 10.963 1.00 45.98 ?  54  THR H OG1 1 
ATOM   8070  C  CG2 . THR H  4 54  ? -3.154  151.049 11.501 1.00 45.33 ?  54  THR H CG2 1 
ATOM   8071  N  N   . ALA H  4 55  ? -6.670  152.650 8.832  1.00 41.96 ?  55  ALA H N   1 
ATOM   8072  C  CA  . ALA H  4 55  ? -7.589  152.724 7.707  1.00 42.76 ?  55  ALA H CA  1 
ATOM   8073  C  C   . ALA H  4 55  ? -8.297  154.071 7.691  1.00 43.10 ?  55  ALA H C   1 
ATOM   8074  O  O   . ALA H  4 55  ? -9.504  154.159 7.456  1.00 50.71 ?  55  ALA H O   1 
ATOM   8075  C  CB  . ALA H  4 55  ? -8.602  151.581 7.753  1.00 42.58 ?  55  ALA H CB  1 
ATOM   8076  N  N   . GLY H  4 56  ? -7.553  155.142 7.942  1.00 41.42 ?  56  GLY H N   1 
ATOM   8077  C  CA  . GLY H  4 56  ? -8.235  156.413 8.060  1.00 46.57 ?  56  GLY H CA  1 
ATOM   8078  C  C   . GLY H  4 56  ? -9.103  156.442 9.312  1.00 45.16 ?  56  GLY H C   1 
ATOM   8079  O  O   . GLY H  4 56  ? -8.894  155.696 10.275 1.00 39.14 ?  56  GLY H O   1 
ATOM   8080  N  N   . CYS H  4 57  ? -10.111 157.311 9.272  1.00 36.29 ?  57  CYS H N   1 
ATOM   8081  C  CA  . CYS H  4 57  ? -10.951 157.541 10.440 1.00 40.52 ?  57  CYS H CA  1 
ATOM   8082  C  C   . CYS H  4 57  ? -11.908 156.381 10.704 1.00 44.66 ?  57  CYS H C   1 
ATOM   8083  O  O   . CYS H  4 57  ? -12.405 156.242 11.830 1.00 39.58 ?  57  CYS H O   1 
ATOM   8084  C  CB  . CYS H  4 57  ? -11.726 158.848 10.263 1.00 36.45 ?  57  CYS H CB  1 
ATOM   8085  S  SG  . CYS H  4 57  ? -10.643 160.310 10.143 1.00 52.19 ?  57  CYS H SG  1 
ATOM   8086  N  N   . THR H  4 58  ? -12.151 155.540 9.697  1.00 40.34 ?  58  THR H N   1 
ATOM   8087  C  CA  . THR H  4 58  ? -13.010 154.372 9.864  1.00 41.47 ?  58  THR H CA  1 
ATOM   8088  C  C   . THR H  4 58  ? -12.516 153.464 10.986 1.00 42.12 ?  58  THR H C   1 
ATOM   8089  O  O   . THR H  4 58  ? -13.321 152.893 11.728 1.00 45.89 ?  58  THR H O   1 
ATOM   8090  C  CB  . THR H  4 58  ? -13.085 153.593 8.551  1.00 42.57 ?  58  THR H CB  1 
ATOM   8091  O  OG1 . THR H  4 58  ? -13.738 154.391 7.555  1.00 51.96 ?  58  THR H OG1 1 
ATOM   8092  C  CG2 . THR H  4 58  ? -13.855 152.300 8.740  1.00 54.54 ?  58  THR H CG2 1 
ATOM   8093  N  N   . SER H  4 59  ? -11.200 153.316 11.137 1.00 39.14 ?  59  SER H N   1 
ATOM   8094  C  CA  . SER H  4 59  ? -10.697 152.365 12.126 1.00 41.99 ?  59  SER H CA  1 
ATOM   8095  C  C   . SER H  4 59  ? -10.695 152.906 13.547 1.00 40.28 ?  59  SER H C   1 
ATOM   8096  O  O   . SER H  4 59  ? -10.211 152.211 14.443 1.00 42.83 ?  59  SER H O   1 
ATOM   8097  C  CB  . SER H  4 59  ? -9.287  151.894 11.765 1.00 38.14 ?  59  SER H CB  1 
ATOM   8098  O  OG  . SER H  4 59  ? -8.626  152.848 10.972 1.00 46.47 ?  59  SER H OG  1 
ATOM   8099  N  N   . ALA H  4 60  ? -11.213 154.108 13.785 1.00 36.63 ?  60  ALA H N   1 
ATOM   8100  C  CA  . ALA H  4 60  ? -11.292 154.616 15.151 1.00 40.06 ?  60  ALA H CA  1 
ATOM   8101  C  C   . ALA H  4 60  ? -12.436 153.983 15.944 1.00 41.39 ?  60  ALA H C   1 
ATOM   8102  O  O   . ALA H  4 60  ? -12.512 154.169 17.166 1.00 41.42 ?  60  ALA H O   1 
ATOM   8103  C  CB  . ALA H  4 60  ? -11.438 156.142 15.130 1.00 33.62 ?  60  ALA H CB  1 
ATOM   8104  N  N   . GLY H  4 61  ? -13.313 153.233 15.284 1.00 44.15 ?  61  GLY H N   1 
ATOM   8105  C  CA  . GLY H  4 61  ? -14.382 152.540 15.956 1.00 40.69 ?  61  GLY H CA  1 
ATOM   8106  C  C   . GLY H  4 61  ? -15.557 153.438 16.288 1.00 46.16 ?  61  GLY H C   1 
ATOM   8107  O  O   . GLY H  4 61  ? -15.770 154.500 15.690 1.00 39.98 ?  61  GLY H O   1 
ATOM   8108  N  N   . PRO H  4 62  ? -16.347 153.006 17.256 1.00 42.46 ?  62  PRO H N   1 
ATOM   8109  C  CA  . PRO H  4 62  ? -17.547 153.745 17.646 1.00 38.17 ?  62  PRO H CA  1 
ATOM   8110  C  C   . PRO H  4 62  ? -17.211 154.853 18.640 1.00 34.74 ?  62  PRO H C   1 
ATOM   8111  O  O   . PRO H  4 62  ? -16.068 154.990 19.082 1.00 39.30 ?  62  PRO H O   1 
ATOM   8112  C  CB  . PRO H  4 62  ? -18.404 152.660 18.308 1.00 43.50 ?  62  PRO H CB  1 
ATOM   8113  C  CG  . PRO H  4 62  ? -17.361 151.808 19.004 1.00 41.10 ?  62  PRO H CG  1 
ATOM   8114  C  CD  . PRO H  4 62  ? -16.175 151.766 18.033 1.00 38.61 ?  62  PRO H CD  1 
ATOM   8115  N  N   . HIS H  4 63  ? -18.225 155.613 19.018 1.00 31.10 ?  63  HIS H N   1 
ATOM   8116  C  CA  . HIS H  4 63  ? -18.025 156.625 20.050 1.00 38.07 ?  63  HIS H CA  1 
ATOM   8117  C  C   . HIS H  4 63  ? -17.498 155.970 21.312 1.00 38.13 ?  63  HIS H C   1 
ATOM   8118  O  O   . HIS H  4 63  ? -17.906 154.864 21.668 1.00 41.59 ?  63  HIS H O   1 
ATOM   8119  C  CB  . HIS H  4 63  ? -19.324 157.365 20.337 1.00 36.70 ?  63  HIS H CB  1 
ATOM   8120  C  CG  . HIS H  4 63  ? -19.817 158.176 19.188 1.00 40.04 ?  63  HIS H CG  1 
ATOM   8121  N  ND1 . HIS H  4 63  ? -20.961 158.937 19.257 1.00 36.99 ?  63  HIS H ND1 1 
ATOM   8122  C  CD2 . HIS H  4 63  ? -19.332 158.337 17.933 1.00 37.57 ?  63  HIS H CD2 1 
ATOM   8123  C  CE1 . HIS H  4 63  ? -21.153 159.549 18.100 1.00 38.42 ?  63  HIS H CE1 1 
ATOM   8124  N  NE2 . HIS H  4 63  ? -20.178 159.200 17.278 1.00 38.75 ?  63  HIS H NE2 1 
ATOM   8125  N  N   . PHE H  4 64  ? -16.553 156.641 21.970 1.00 39.93 ?  64  PHE H N   1 
ATOM   8126  C  CA  . PHE H  4 64  ? -15.983 156.122 23.206 1.00 44.43 ?  64  PHE H CA  1 
ATOM   8127  C  C   . PHE H  4 64  ? -17.073 155.991 24.262 1.00 46.40 ?  64  PHE H C   1 
ATOM   8128  O  O   . PHE H  4 64  ? -17.657 156.993 24.692 1.00 43.97 ?  64  PHE H O   1 
ATOM   8129  C  CB  . PHE H  4 64  ? -14.872 157.046 23.693 1.00 40.70 ?  64  PHE H CB  1 
ATOM   8130  C  CG  . PHE H  4 64  ? -14.223 156.596 24.964 1.00 44.06 ?  64  PHE H CG  1 
ATOM   8131  C  CD1 . PHE H  4 64  ? -13.928 155.262 25.175 1.00 43.50 ?  64  PHE H CD1 1 
ATOM   8132  C  CD2 . PHE H  4 64  ? -13.908 157.514 25.949 1.00 38.54 ?  64  PHE H CD2 1 
ATOM   8133  C  CE1 . PHE H  4 64  ? -13.324 154.859 26.348 1.00 45.07 ?  64  PHE H CE1 1 
ATOM   8134  C  CE2 . PHE H  4 64  ? -13.302 157.116 27.126 1.00 45.64 ?  64  PHE H CE2 1 
ATOM   8135  C  CZ  . PHE H  4 64  ? -13.012 155.792 27.325 1.00 43.21 ?  64  PHE H CZ  1 
ATOM   8136  N  N   . ASN H  4 65  ? -17.338 154.746 24.687 1.00 45.00 ?  65  ASN H N   1 
ATOM   8137  C  CA  . ASN H  4 65  ? -18.541 154.433 25.449 1.00 45.16 ?  65  ASN H CA  1 
ATOM   8138  C  C   . ASN H  4 65  ? -18.264 153.389 26.526 1.00 46.31 ?  65  ASN H C   1 
ATOM   8139  O  O   . ASN H  4 65  ? -18.853 152.304 26.494 1.00 42.93 ?  65  ASN H O   1 
ATOM   8140  C  CB  . ASN H  4 65  ? -19.630 153.944 24.483 1.00 43.36 ?  65  ASN H CB  1 
ATOM   8141  C  CG  . ASN H  4 65  ? -20.974 153.696 25.166 1.00 48.57 ?  65  ASN H CG  1 
ATOM   8142  O  OD1 . ASN H  4 65  ? -21.282 154.275 26.211 1.00 47.65 ?  65  ASN H OD1 1 
ATOM   8143  N  ND2 . ASN H  4 65  ? -21.803 152.872 24.533 1.00 45.21 ?  65  ASN H ND2 1 
ATOM   8144  N  N   . PRO H  4 66  ? -17.397 153.672 27.499 1.00 45.04 ?  66  PRO H N   1 
ATOM   8145  C  CA  . PRO H  4 66  ? -17.038 152.625 28.467 1.00 45.69 ?  66  PRO H CA  1 
ATOM   8146  C  C   . PRO H  4 66  ? -18.190 152.221 29.375 1.00 50.83 ?  66  PRO H C   1 
ATOM   8147  O  O   . PRO H  4 66  ? -18.211 151.080 29.848 1.00 50.38 ?  66  PRO H O   1 
ATOM   8148  C  CB  . PRO H  4 66  ? -15.887 153.254 29.268 1.00 44.84 ?  66  PRO H CB  1 
ATOM   8149  C  CG  . PRO H  4 66  ? -16.112 154.725 29.166 1.00 46.85 ?  66  PRO H CG  1 
ATOM   8150  C  CD  . PRO H  4 66  ? -16.783 154.972 27.824 1.00 44.53 ?  66  PRO H CD  1 
ATOM   8151  N  N   . LEU H  4 67  ? -19.154 153.107 29.609 1.00 48.66 ?  67  LEU H N   1 
ATOM   8152  C  CA  . LEU H  4 67  ? -20.298 152.840 30.467 1.00 45.61 ?  67  LEU H CA  1 
ATOM   8153  C  C   . LEU H  4 67  ? -21.474 152.247 29.710 1.00 51.47 ?  67  LEU H C   1 
ATOM   8154  O  O   . LEU H  4 67  ? -22.557 152.107 30.288 1.00 55.64 ?  67  LEU H O   1 
ATOM   8155  C  CB  . LEU H  4 67  ? -20.739 154.126 31.166 1.00 42.52 ?  67  LEU H CB  1 
ATOM   8156  C  CG  . LEU H  4 67  ? -19.675 154.908 31.943 1.00 48.84 ?  67  LEU H CG  1 
ATOM   8157  C  CD1 . LEU H  4 67  ? -20.290 156.119 32.618 1.00 46.09 ?  67  LEU H CD1 1 
ATOM   8158  C  CD2 . LEU H  4 67  ? -18.988 154.024 32.967 1.00 48.49 ?  67  LEU H CD2 1 
ATOM   8159  N  N   . SER H  4 68  ? -21.301 151.932 28.432 1.00 48.71 ?  68  SER H N   1 
ATOM   8160  C  CA  . SER H  4 68  ? -22.320 151.268 27.624 1.00 47.80 ?  68  SER H CA  1 
ATOM   8161  C  C   . SER H  4 68  ? -23.684 151.956 27.721 1.00 49.11 ?  68  SER H C   1 
ATOM   8162  O  O   . SER H  4 68  ? -24.693 151.343 28.071 1.00 51.24 ?  68  SER H O   1 
ATOM   8163  C  CB  . SER H  4 68  ? -22.428 149.795 28.021 1.00 51.34 ?  68  SER H CB  1 
ATOM   8164  O  OG  . SER H  4 68  ? -21.300 149.080 27.561 1.00 56.06 ?  68  SER H OG  1 
ATOM   8165  N  N   . ARG H  4 69  ? -23.709 153.243 27.382 1.00 46.64 ?  69  ARG H N   1 
ATOM   8166  C  CA  . ARG H  4 69  ? -24.949 154.004 27.333 1.00 43.22 ?  69  ARG H CA  1 
ATOM   8167  C  C   . ARG H  4 69  ? -25.365 154.287 25.895 1.00 48.15 ?  69  ARG H C   1 
ATOM   8168  O  O   . ARG H  4 69  ? -24.662 153.962 24.936 1.00 51.19 ?  69  ARG H O   1 
ATOM   8169  C  CB  . ARG H  4 69  ? -24.808 155.313 28.094 1.00 44.14 ?  69  ARG H CB  1 
ATOM   8170  C  CG  . ARG H  4 69  ? -24.071 155.179 29.380 1.00 47.37 ?  69  ARG H CG  1 
ATOM   8171  C  CD  . ARG H  4 69  ? -25.027 155.372 30.519 1.00 48.84 ?  69  ARG H CD  1 
ATOM   8172  N  NE  . ARG H  4 69  ? -24.302 155.485 31.775 1.00 53.28 ?  69  ARG H NE  1 
ATOM   8173  C  CZ  . ARG H  4 69  ? -24.211 156.598 32.487 1.00 58.56 ?  69  ARG H CZ  1 
ATOM   8174  N  NH1 . ARG H  4 69  ? -24.805 157.714 32.099 1.00 58.07 ?  69  ARG H NH1 1 
ATOM   8175  N  NH2 . ARG H  4 69  ? -23.516 156.590 33.620 1.00 64.30 ?  69  ARG H NH2 1 
ATOM   8176  N  N   . LYS H  4 70  ? -26.533 154.904 25.758 1.00 42.17 ?  70  LYS H N   1 
ATOM   8177  C  CA  . LYS H  4 70  ? -26.966 155.417 24.474 1.00 46.68 ?  70  LYS H CA  1 
ATOM   8178  C  C   . LYS H  4 70  ? -26.298 156.766 24.196 1.00 43.77 ?  70  LYS H C   1 
ATOM   8179  O  O   . LYS H  4 70  ? -25.775 157.433 25.093 1.00 39.67 ?  70  LYS H O   1 
ATOM   8180  C  CB  . LYS H  4 70  ? -28.490 155.565 24.427 1.00 45.91 ?  70  LYS H CB  1 
ATOM   8181  C  CG  . LYS H  4 70  ? -29.267 154.388 24.992 1.00 47.39 ?  70  LYS H CG  1 
ATOM   8182  C  CD  . LYS H  4 70  ? -29.714 153.470 23.884 1.00 55.91 ?  70  LYS H CD  1 
ATOM   8183  C  CE  . LYS H  4 70  ? -31.177 153.058 24.031 1.00 60.31 ?  70  LYS H CE  1 
ATOM   8184  N  NZ  . LYS H  4 70  ? -31.510 151.927 23.094 1.00 60.49 ?  70  LYS H NZ  1 
ATOM   8185  N  N   . HIS H  4 71  ? -26.322 157.161 22.932 1.00 42.35 ?  71  HIS H N   1 
ATOM   8186  C  CA  . HIS H  4 71  ? -25.701 158.417 22.537 1.00 39.52 ?  71  HIS H CA  1 
ATOM   8187  C  C   . HIS H  4 71  ? -26.541 159.595 23.018 1.00 43.21 ?  71  HIS H C   1 
ATOM   8188  O  O   . HIS H  4 71  ? -27.773 159.567 22.952 1.00 43.49 ?  71  HIS H O   1 
ATOM   8189  C  CB  . HIS H  4 71  ? -25.542 158.468 21.019 1.00 40.46 ?  71  HIS H CB  1 
ATOM   8190  C  CG  . HIS H  4 71  ? -25.155 159.819 20.505 1.00 38.49 ?  71  HIS H CG  1 
ATOM   8191  N  ND1 . HIS H  4 71  ? -23.842 160.227 20.410 1.00 37.21 ?  71  HIS H ND1 1 
ATOM   8192  C  CD2 . HIS H  4 71  ? -25.909 160.862 20.087 1.00 38.79 ?  71  HIS H CD2 1 
ATOM   8193  C  CE1 . HIS H  4 71  ? -23.803 161.464 19.945 1.00 38.66 ?  71  HIS H CE1 1 
ATOM   8194  N  NE2 . HIS H  4 71  ? -25.044 161.870 19.738 1.00 40.27 ?  71  HIS H NE2 1 
ATOM   8195  N  N   . GLY H  4 72  ? -25.873 160.646 23.496 1.00 39.13 ?  72  GLY H N   1 
ATOM   8196  C  CA  . GLY H  4 72  ? -26.571 161.835 23.945 1.00 39.67 ?  72  GLY H CA  1 
ATOM   8197  C  C   . GLY H  4 72  ? -25.817 163.105 23.602 1.00 41.58 ?  72  GLY H C   1 
ATOM   8198  O  O   . GLY H  4 72  ? -24.781 163.082 22.933 1.00 43.37 ?  72  GLY H O   1 
ATOM   8199  N  N   . GLY H  4 73  ? -26.374 164.226 24.052 1.00 36.18 ?  73  GLY H N   1 
ATOM   8200  C  CA  . GLY H  4 73  ? -25.656 165.474 24.065 1.00 39.41 ?  73  GLY H CA  1 
ATOM   8201  C  C   . GLY H  4 73  ? -24.747 165.554 25.264 1.00 40.67 ?  73  GLY H C   1 
ATOM   8202  O  O   . GLY H  4 73  ? -24.852 164.778 26.224 1.00 42.05 ?  73  GLY H O   1 
ATOM   8203  N  N   . PRO H  4 74  ? -23.808 166.504 25.225 1.00 45.24 ?  74  PRO H N   1 
ATOM   8204  C  CA  . PRO H  4 74  ? -22.859 166.614 26.341 1.00 36.33 ?  74  PRO H CA  1 
ATOM   8205  C  C   . PRO H  4 74  ? -23.530 166.937 27.662 1.00 42.36 ?  74  PRO H C   1 
ATOM   8206  O  O   . PRO H  4 74  ? -23.058 166.463 28.701 1.00 44.00 ?  74  PRO H O   1 
ATOM   8207  C  CB  . PRO H  4 74  ? -21.900 167.727 25.890 1.00 37.54 ?  74  PRO H CB  1 
ATOM   8208  C  CG  . PRO H  4 74  ? -22.593 168.430 24.806 1.00 35.53 ?  74  PRO H CG  1 
ATOM   8209  C  CD  . PRO H  4 74  ? -23.518 167.470 24.156 1.00 37.19 ?  74  PRO H CD  1 
ATOM   8210  N  N   . LYS H  4 75  ? -24.636 167.688 27.648 1.00 44.67 ?  75  LYS H N   1 
ATOM   8211  C  CA  . LYS H  4 75  ? -25.353 168.050 28.868 1.00 50.69 ?  75  LYS H CA  1 
ATOM   8212  C  C   . LYS H  4 75  ? -26.269 166.952 29.392 1.00 50.01 ?  75  LYS H C   1 
ATOM   8213  O  O   . LYS H  4 75  ? -26.860 167.138 30.459 1.00 53.04 ?  75  LYS H O   1 
ATOM   8214  C  CB  . LYS H  4 75  ? -26.203 169.304 28.644 1.00 43.41 ?  75  LYS H CB  1 
ATOM   8215  C  CG  . LYS H  4 75  ? -25.512 170.426 27.901 1.00 52.55 ?  75  LYS H CG  1 
ATOM   8216  C  CD  . LYS H  4 75  ? -26.122 171.769 28.277 1.00 57.70 ?  75  LYS H CD  1 
ATOM   8217  C  CE  . LYS H  4 75  ? -27.401 172.066 27.489 1.00 53.79 ?  75  LYS H CE  1 
ATOM   8218  N  NZ  . LYS H  4 75  ? -27.667 173.541 27.461 1.00 55.14 ?  75  LYS H NZ  1 
ATOM   8219  N  N   . ASP H  4 76  ? -26.434 165.845 28.667 1.00 45.55 ?  76  ASP H N   1 
ATOM   8220  C  CA  . ASP H  4 76  ? -27.298 164.760 29.125 1.00 47.53 ?  76  ASP H CA  1 
ATOM   8221  C  C   . ASP H  4 76  ? -26.570 163.854 30.108 1.00 49.70 ?  76  ASP H C   1 
ATOM   8222  O  O   . ASP H  4 76  ? -25.341 163.726 30.081 1.00 47.75 ?  76  ASP H O   1 
ATOM   8223  C  CB  . ASP H  4 76  ? -27.782 163.908 27.956 1.00 47.24 ?  76  ASP H CB  1 
ATOM   8224  C  CG  . ASP H  4 76  ? -28.643 164.679 26.991 1.00 52.63 ?  76  ASP H CG  1 
ATOM   8225  O  OD1 . ASP H  4 76  ? -29.319 165.631 27.440 1.00 55.82 ?  76  ASP H OD1 1 
ATOM   8226  O  OD2 . ASP H  4 76  ? -28.663 164.323 25.786 1.00 55.64 -1 76  ASP H OD2 1 
ATOM   8227  N  N   . GLU H  4 77  ? -27.348 163.205 30.978 1.00 51.01 ?  77  GLU H N   1 
ATOM   8228  C  CA  . GLU H  4 77  ? -26.770 162.156 31.805 1.00 47.34 ?  77  GLU H CA  1 
ATOM   8229  C  C   . GLU H  4 77  ? -26.559 160.886 30.997 1.00 49.19 ?  77  GLU H C   1 
ATOM   8230  O  O   . GLU H  4 77  ? -25.530 160.211 31.141 1.00 52.29 ?  77  GLU H O   1 
ATOM   8231  C  CB  . GLU H  4 77  ? -27.665 161.877 33.012 1.00 59.67 ?  77  GLU H CB  1 
ATOM   8232  C  CG  . GLU H  4 77  ? -26.904 161.367 34.231 1.00 68.30 ?  77  GLU H CG  1 
ATOM   8233  C  CD  . GLU H  4 77  ? -26.656 162.461 35.272 1.00 89.05 ?  77  GLU H CD  1 
ATOM   8234  O  OE1 . GLU H  4 77  ? -25.479 162.865 35.454 1.00 87.89 ?  77  GLU H OE1 1 
ATOM   8235  O  OE2 . GLU H  4 77  ? -27.640 162.916 35.905 1.00 90.28 -1 77  GLU H OE2 1 
ATOM   8236  N  N   . GLU H  4 78  ? -27.519 160.551 30.141 1.00 42.02 ?  78  GLU H N   1 
ATOM   8237  C  CA  . GLU H  4 78  ? -27.400 159.399 29.252 1.00 47.09 ?  78  GLU H CA  1 
ATOM   8238  C  C   . GLU H  4 78  ? -26.622 159.826 28.007 1.00 46.69 ?  78  GLU H C   1 
ATOM   8239  O  O   . GLU H  4 78  ? -27.171 160.462 27.103 1.00 40.00 ?  78  GLU H O   1 
ATOM   8240  C  CB  . GLU H  4 78  ? -28.777 158.864 28.885 1.00 39.50 ?  78  GLU H CB  1 
ATOM   8241  C  CG  . GLU H  4 78  ? -28.727 157.645 27.976 1.00 45.88 ?  78  GLU H CG  1 
ATOM   8242  C  CD  . GLU H  4 78  ? -28.330 156.357 28.713 1.00 55.84 ?  78  GLU H CD  1 
ATOM   8243  O  OE1 . GLU H  4 78  ? -28.135 156.384 29.959 1.00 58.52 ?  78  GLU H OE1 1 
ATOM   8244  O  OE2 . GLU H  4 78  ? -28.218 155.312 28.035 1.00 52.35 -1 78  GLU H OE2 1 
ATOM   8245  N  N   . ARG H  4 79  ? -25.346 159.457 27.952 1.00 43.88 ?  79  ARG H N   1 
ATOM   8246  C  CA  . ARG H  4 79  ? -24.490 159.854 26.848 1.00 43.71 ?  79  ARG H CA  1 
ATOM   8247  C  C   . ARG H  4 79  ? -23.240 159.004 26.897 1.00 48.10 ?  79  ARG H C   1 
ATOM   8248  O  O   . ARG H  4 79  ? -22.850 158.497 27.957 1.00 46.08 ?  79  ARG H O   1 
ATOM   8249  C  CB  . ARG H  4 79  ? -24.108 161.336 26.927 1.00 40.90 ?  79  ARG H CB  1 
ATOM   8250  C  CG  . ARG H  4 79  ? -23.309 161.652 28.181 1.00 42.24 ?  79  ARG H CG  1 
ATOM   8251  C  CD  . ARG H  4 79  ? -22.657 163.029 28.129 1.00 43.27 ?  79  ARG H CD  1 
ATOM   8252  N  NE  . ARG H  4 79  ? -21.272 162.975 27.669 1.00 42.83 ?  79  ARG H NE  1 
ATOM   8253  C  CZ  . ARG H  4 79  ? -20.417 163.988 27.759 1.00 38.75 ?  79  ARG H CZ  1 
ATOM   8254  N  NH1 . ARG H  4 79  ? -20.770 165.147 28.294 1.00 36.83 ?  79  ARG H NH1 1 
ATOM   8255  N  NH2 . ARG H  4 79  ? -19.174 163.830 27.313 1.00 40.12 ?  79  ARG H NH2 1 
ATOM   8256  N  N   . HIS H  4 80  ? -22.618 158.854 25.733 1.00 40.60 ?  80  HIS H N   1 
ATOM   8257  C  CA  . HIS H  4 80  ? -21.296 158.257 25.684 1.00 39.43 ?  80  HIS H CA  1 
ATOM   8258  C  C   . HIS H  4 80  ? -20.302 159.216 26.308 1.00 37.21 ?  80  HIS H C   1 
ATOM   8259  O  O   . HIS H  4 80  ? -20.507 160.432 26.316 1.00 41.50 ?  80  HIS H O   1 
ATOM   8260  C  CB  . HIS H  4 80  ? -20.885 157.962 24.247 1.00 39.68 ?  80  HIS H CB  1 
ATOM   8261  C  CG  . HIS H  4 80  ? -21.841 157.089 23.507 1.00 44.13 ?  80  HIS H CG  1 
ATOM   8262  N  ND1 . HIS H  4 80  ? -22.056 157.209 22.152 1.00 41.57 ?  80  HIS H ND1 1 
ATOM   8263  C  CD2 . HIS H  4 80  ? -22.618 156.062 23.924 1.00 44.89 ?  80  HIS H CD2 1 
ATOM   8264  C  CE1 . HIS H  4 80  ? -22.943 156.308 21.766 1.00 43.28 ?  80  HIS H CE1 1 
ATOM   8265  N  NE2 . HIS H  4 80  ? -23.293 155.593 22.822 1.00 50.16 ?  80  HIS H NE2 1 
ATOM   8266  N  N   . VAL H  4 81  ? -19.206 158.668 26.827 1.00 38.48 ?  81  VAL H N   1 
ATOM   8267  C  CA  . VAL H  4 81  ? -18.170 159.549 27.352 1.00 37.09 ?  81  VAL H CA  1 
ATOM   8268  C  C   . VAL H  4 81  ? -17.689 160.505 26.257 1.00 40.99 ?  81  VAL H C   1 
ATOM   8269  O  O   . VAL H  4 81  ? -17.479 161.697 26.507 1.00 38.70 ?  81  VAL H O   1 
ATOM   8270  C  CB  . VAL H  4 81  ? -17.015 158.729 27.949 1.00 41.67 ?  81  VAL H CB  1 
ATOM   8271  C  CG1 . VAL H  4 81  ? -15.786 159.598 28.139 1.00 39.06 ?  81  VAL H CG1 1 
ATOM   8272  C  CG2 . VAL H  4 81  ? -17.454 158.110 29.275 1.00 42.22 ?  81  VAL H CG2 1 
ATOM   8273  N  N   . GLY H  4 82  ? -17.554 160.008 25.019 1.00 34.04 ?  82  GLY H N   1 
ATOM   8274  C  CA  . GLY H  4 82  ? -17.070 160.817 23.913 1.00 40.04 ?  82  GLY H CA  1 
ATOM   8275  C  C   . GLY H  4 82  ? -18.061 161.763 23.266 1.00 36.28 ?  82  GLY H C   1 
ATOM   8276  O  O   . GLY H  4 82  ? -17.722 162.408 22.267 1.00 35.15 ?  82  GLY H O   1 
ATOM   8277  N  N   . ASP H  4 83  ? -19.275 161.892 23.803 1.00 37.88 ?  83  ASP H N   1 
ATOM   8278  C  CA  . ASP H  4 83  ? -20.308 162.748 23.210 1.00 36.98 ?  83  ASP H CA  1 
ATOM   8279  C  C   . ASP H  4 83  ? -20.053 164.219 23.558 1.00 42.89 ?  83  ASP H C   1 
ATOM   8280  O  O   . ASP H  4 83  ? -20.617 164.766 24.511 1.00 40.19 ?  83  ASP H O   1 
ATOM   8281  C  CB  . ASP H  4 83  ? -21.690 162.317 23.686 1.00 42.44 ?  83  ASP H CB  1 
ATOM   8282  C  CG  . ASP H  4 83  ? -22.130 160.979 23.109 1.00 44.12 ?  83  ASP H CG  1 
ATOM   8283  O  OD1 . ASP H  4 83  ? -21.438 160.471 22.198 1.00 39.76 ?  83  ASP H OD1 1 
ATOM   8284  O  OD2 . ASP H  4 83  ? -23.174 160.448 23.562 1.00 41.48 -1 83  ASP H OD2 1 
ATOM   8285  N  N   . LEU H  4 84  ? -19.237 164.897 22.749 1.00 38.79 ?  84  LEU H N   1 
ATOM   8286  C  CA  . LEU H  4 84  ? -18.980 166.320 22.964 1.00 36.83 ?  84  LEU H CA  1 
ATOM   8287  C  C   . LEU H  4 84  ? -19.947 167.217 22.207 1.00 34.27 ?  84  LEU H C   1 
ATOM   8288  O  O   . LEU H  4 84  ? -19.789 168.440 22.243 1.00 36.00 ?  84  LEU H O   1 
ATOM   8289  C  CB  . LEU H  4 84  ? -17.535 166.672 22.580 1.00 33.35 ?  84  LEU H CB  1 
ATOM   8290  C  CG  . LEU H  4 84  ? -16.455 165.967 23.405 1.00 38.87 ?  84  LEU H CG  1 
ATOM   8291  C  CD1 . LEU H  4 84  ? -15.082 166.321 22.880 1.00 34.52 ?  84  LEU H CD1 1 
ATOM   8292  C  CD2 . LEU H  4 84  ? -16.568 166.316 24.893 1.00 41.29 ?  84  LEU H CD2 1 
ATOM   8293  N  N   . GLY H  4 85  ? -20.937 166.654 21.520 1.00 30.60 ?  85  GLY H N   1 
ATOM   8294  C  CA  . GLY H  4 85  ? -21.970 167.481 20.928 1.00 30.29 ?  85  GLY H CA  1 
ATOM   8295  C  C   . GLY H  4 85  ? -21.581 167.965 19.546 1.00 31.27 ?  85  GLY H C   1 
ATOM   8296  O  O   . GLY H  4 85  ? -20.966 167.223 18.778 1.00 31.36 ?  85  GLY H O   1 
ATOM   8297  N  N   . ASN H  4 86  ? -21.932 169.196 19.216 1.00 29.75 ?  86  ASN H N   1 
ATOM   8298  C  CA  . ASN H  4 86  ? -21.616 169.779 17.919 1.00 31.95 ?  86  ASN H CA  1 
ATOM   8299  C  C   . ASN H  4 86  ? -20.563 170.867 18.054 1.00 30.15 ?  86  ASN H C   1 
ATOM   8300  O  O   . ASN H  4 86  ? -20.433 171.498 19.102 1.00 26.15 ?  86  ASN H O   1 
ATOM   8301  C  CB  . ASN H  4 86  ? -22.857 170.401 17.281 1.00 33.33 ?  86  ASN H CB  1 
ATOM   8302  C  CG  . ASN H  4 86  ? -23.808 169.372 16.754 1.00 33.07 ?  86  ASN H CG  1 
ATOM   8303  O  OD1 . ASN H  4 86  ? -23.414 168.469 16.022 1.00 30.23 ?  86  ASN H OD1 1 
ATOM   8304  N  ND2 . ASN H  4 86  ? -25.070 169.486 17.142 1.00 33.36 ?  86  ASN H ND2 1 
ATOM   8305  N  N   . VAL H  4 87  ? -19.845 171.116 16.958 1.00 29.05 ?  87  VAL H N   1 
ATOM   8306  C  CA  . VAL H  4 87  ? -19.127 172.372 16.767 1.00 29.94 ?  87  VAL H CA  1 
ATOM   8307  C  C   . VAL H  4 87  ? -19.729 173.089 15.560 1.00 33.00 ?  87  VAL H C   1 
ATOM   8308  O  O   . VAL H  4 87  ? -20.305 172.465 14.666 1.00 35.80 ?  87  VAL H O   1 
ATOM   8309  C  CB  . VAL H  4 87  ? -17.607 172.166 16.578 1.00 29.61 ?  87  VAL H CB  1 
ATOM   8310  C  CG1 . VAL H  4 87  ? -17.010 171.469 17.793 1.00 29.30 ?  87  VAL H CG1 1 
ATOM   8311  C  CG2 . VAL H  4 87  ? -17.321 171.385 15.322 1.00 29.98 ?  87  VAL H CG2 1 
ATOM   8312  N  N   . THR H  4 88  ? -19.605 174.410 15.540 1.00 28.46 ?  88  THR H N   1 
ATOM   8313  C  CA  . THR H  4 88  ? -20.244 175.226 14.523 1.00 31.94 ?  88  THR H CA  1 
ATOM   8314  C  C   . THR H  4 88  ? -19.198 175.901 13.648 1.00 36.51 ?  88  THR H C   1 
ATOM   8315  O  O   . THR H  4 88  ? -18.325 176.632 14.143 1.00 32.34 ?  88  THR H O   1 
ATOM   8316  C  CB  . THR H  4 88  ? -21.161 176.271 15.151 1.00 31.98 ?  88  THR H CB  1 
ATOM   8317  O  OG1 . THR H  4 88  ? -22.251 175.603 15.804 1.00 32.17 ?  88  THR H OG1 1 
ATOM   8318  C  CG2 . THR H  4 88  ? -21.716 177.233 14.070 1.00 30.41 ?  88  THR H CG2 1 
ATOM   8319  N  N   . ALA H  4 89  ? -19.310 175.670 12.348 1.00 32.82 ?  89  ALA H N   1 
ATOM   8320  C  CA  . ALA H  4 89  ? -18.444 176.285 11.360 1.00 27.94 ?  89  ALA H CA  1 
ATOM   8321  C  C   . ALA H  4 89  ? -19.131 177.542 10.855 1.00 31.70 ?  89  ALA H C   1 
ATOM   8322  O  O   . ALA H  4 89  ? -20.342 177.541 10.625 1.00 32.20 ?  89  ALA H O   1 
ATOM   8323  C  CB  . ALA H  4 89  ? -18.162 175.315 10.212 1.00 29.38 ?  89  ALA H CB  1 
ATOM   8324  N  N   . ASP H  4 90  ? -18.362 178.627 10.730 1.00 31.65 ?  90  ASP H N   1 
ATOM   8325  C  CA  . ASP H  4 90  ? -18.900 179.893 10.248 1.00 33.91 ?  90  ASP H CA  1 
ATOM   8326  C  C   . ASP H  4 90  ? -18.955 179.874 8.725  1.00 35.65 ?  90  ASP H C   1 
ATOM   8327  O  O   . ASP H  4 90  ? -18.631 178.873 8.075  1.00 32.78 ?  90  ASP H O   1 
ATOM   8328  C  CB  . ASP H  4 90  ? -18.072 181.073 10.770 1.00 34.77 ?  90  ASP H CB  1 
ATOM   8329  C  CG  . ASP H  4 90  ? -16.621 181.089 10.235 1.00 36.95 ?  90  ASP H CG  1 
ATOM   8330  O  OD1 . ASP H  4 90  ? -16.305 180.444 9.207  1.00 36.37 ?  90  ASP H OD1 1 
ATOM   8331  O  OD2 . ASP H  4 90  ? -15.775 181.766 10.862 1.00 43.32 -1 90  ASP H OD2 1 
ATOM   8332  N  N   . LYS H  4 91  ? -19.309 181.021 8.137  1.00 37.44 ?  91  LYS H N   1 
ATOM   8333  C  CA  . LYS H  4 91  ? -19.486 181.095 6.693  1.00 36.51 ?  91  LYS H CA  1 
ATOM   8334  C  C   . LYS H  4 91  ? -18.193 180.833 5.924  1.00 36.78 ?  91  LYS H C   1 
ATOM   8335  O  O   . LYS H  4 91  ? -18.246 180.442 4.747  1.00 37.88 ?  91  LYS H O   1 
ATOM   8336  C  CB  . LYS H  4 91  ? -20.093 182.451 6.342  1.00 37.34 ?  91  LYS H CB  1 
ATOM   8337  C  CG  . LYS H  4 91  ? -19.169 183.634 6.511  1.00 45.89 ?  91  LYS H CG  1 
ATOM   8338  C  CD  . LYS H  4 91  ? -19.523 184.744 5.514  1.00 53.59 ?  91  LYS H CD  1 
ATOM   8339  C  CE  . LYS H  4 91  ? -20.537 185.731 6.088  1.00 59.48 ?  91  LYS H CE  1 
ATOM   8340  N  NZ  . LYS H  4 91  ? -20.940 186.778 5.084  1.00 65.64 ?  91  LYS H NZ  1 
ATOM   8341  N  N   . ASP H  4 92  ? -17.035 180.991 6.559  1.00 37.16 ?  92  ASP H N   1 
ATOM   8342  C  CA  . ASP H  4 92  ? -15.757 180.715 5.908  1.00 36.58 ?  92  ASP H CA  1 
ATOM   8343  C  C   . ASP H  4 92  ? -15.313 179.276 6.094  1.00 32.58 ?  92  ASP H C   1 
ATOM   8344  O  O   . ASP H  4 92  ? -14.189 178.930 5.721  1.00 33.24 ?  92  ASP H O   1 
ATOM   8345  C  CB  . ASP H  4 92  ? -14.675 181.658 6.433  1.00 40.73 ?  92  ASP H CB  1 
ATOM   8346  C  CG  . ASP H  4 92  ? -14.909 183.101 6.015  1.00 50.36 ?  92  ASP H CG  1 
ATOM   8347  O  OD1 . ASP H  4 92  ? -15.363 183.324 4.870  1.00 49.04 ?  92  ASP H OD1 1 
ATOM   8348  O  OD2 . ASP H  4 92  ? -14.647 184.007 6.838  1.00 58.79 -1 92  ASP H OD2 1 
ATOM   8349  N  N   . GLY H  4 93  ? -16.166 178.436 6.664  1.00 30.72 ?  93  GLY H N   1 
ATOM   8350  C  CA  . GLY H  4 93  ? -15.791 177.063 6.920  1.00 33.91 ?  93  GLY H CA  1 
ATOM   8351  C  C   . GLY H  4 93  ? -14.949 176.830 8.158  1.00 31.30 ?  93  GLY H C   1 
ATOM   8352  O  O   . GLY H  4 93  ? -14.380 175.742 8.300  1.00 30.51 ?  93  GLY H O   1 
ATOM   8353  N  N   . VAL H  4 94  ? -14.848 177.802 9.060  1.00 29.79 ?  94  VAL H N   1 
ATOM   8354  C  CA  . VAL H  4 94  ? -13.969 177.695 10.217 1.00 29.58 ?  94  VAL H CA  1 
ATOM   8355  C  C   . VAL H  4 94  ? -14.806 177.484 11.468 1.00 28.04 ?  94  VAL H C   1 
ATOM   8356  O  O   . VAL H  4 94  ? -15.709 178.277 11.764 1.00 31.82 ?  94  VAL H O   1 
ATOM   8357  C  CB  . VAL H  4 94  ? -13.075 178.934 10.383 1.00 35.22 ?  94  VAL H CB  1 
ATOM   8358  C  CG1 . VAL H  4 94  ? -12.232 178.798 11.631 1.00 36.11 ?  94  VAL H CG1 1 
ATOM   8359  C  CG2 . VAL H  4 94  ? -12.191 179.134 9.137  1.00 33.85 ?  94  VAL H CG2 1 
ATOM   8360  N  N   . ALA H  4 95  ? -14.484 176.428 12.211 1.00 28.96 ?  95  ALA H N   1 
ATOM   8361  C  CA  . ALA H  4 95  ? -15.053 176.176 13.528 1.00 30.03 ?  95  ALA H CA  1 
ATOM   8362  C  C   . ALA H  4 95  ? -13.993 176.558 14.563 1.00 31.30 ?  95  ALA H C   1 
ATOM   8363  O  O   . ALA H  4 95  ? -12.972 175.878 14.692 1.00 34.73 ?  95  ALA H O   1 
ATOM   8364  C  CB  . ALA H  4 95  ? -15.472 174.714 13.673 1.00 28.69 ?  95  ALA H CB  1 
ATOM   8365  N  N   . ASP H  4 96  ? -14.213 177.674 15.260 1.00 30.66 ?  96  ASP H N   1 
ATOM   8366  C  CA  . ASP H  4 96  ? -13.355 178.051 16.385 1.00 34.59 ?  96  ASP H CA  1 
ATOM   8367  C  C   . ASP H  4 96  ? -13.935 177.378 17.617 1.00 31.45 ?  96  ASP H C   1 
ATOM   8368  O  O   . ASP H  4 96  ? -14.849 177.887 18.264 1.00 34.50 ?  96  ASP H O   1 
ATOM   8369  C  CB  . ASP H  4 96  ? -13.267 179.564 16.535 1.00 36.22 ?  96  ASP H CB  1 
ATOM   8370  C  CG  . ASP H  4 96  ? -12.524 180.220 15.373 1.00 40.69 ?  96  ASP H CG  1 
ATOM   8371  O  OD1 . ASP H  4 96  ? -11.366 179.818 15.101 1.00 34.51 ?  96  ASP H OD1 1 
ATOM   8372  O  OD2 . ASP H  4 96  ? -13.104 181.125 14.731 1.00 47.41 -1 96  ASP H OD2 1 
ATOM   8373  N  N   . VAL H  4 97  ? -13.410 176.196 17.926 1.00 33.21 ?  97  VAL H N   1 
ATOM   8374  C  CA  . VAL H  4 97  ? -14.017 175.345 18.942 1.00 34.69 ?  97  VAL H CA  1 
ATOM   8375  C  C   . VAL H  4 97  ? -13.742 175.916 20.327 1.00 38.66 ?  97  VAL H C   1 
ATOM   8376  O  O   . VAL H  4 97  ? -12.602 176.269 20.660 1.00 32.87 ?  97  VAL H O   1 
ATOM   8377  C  CB  . VAL H  4 97  ? -13.493 173.910 18.817 1.00 32.51 ?  97  VAL H CB  1 
ATOM   8378  C  CG1 . VAL H  4 97  ? -14.048 173.059 19.943 1.00 32.49 ?  97  VAL H CG1 1 
ATOM   8379  C  CG2 . VAL H  4 97  ? -13.864 173.311 17.433 1.00 30.46 ?  97  VAL H CG2 1 
ATOM   8380  N  N   . SER H  4 98  ? -14.797 176.029 21.131 1.00 33.14 ?  98  SER H N   1 
ATOM   8381  C  CA  . SER H  4 98  ? -14.673 176.394 22.539 1.00 38.66 ?  98  SER H CA  1 
ATOM   8382  C  C   . SER H  4 98  ? -15.713 175.600 23.307 1.00 34.91 ?  98  SER H C   1 
ATOM   8383  O  O   . SER H  4 98  ? -16.909 175.897 23.231 1.00 40.94 ?  98  SER H O   1 
ATOM   8384  C  CB  . SER H  4 98  ? -14.871 177.885 22.759 1.00 37.62 ?  98  SER H CB  1 
ATOM   8385  O  OG  . SER H  4 98  ? -14.828 178.175 24.145 1.00 47.58 ?  98  SER H OG  1 
ATOM   8386  N  N   . ILE H  4 99  ? -15.259 174.590 24.035 1.00 35.00 ?  99  ILE H N   1 
ATOM   8387  C  CA  . ILE H  4 99  ? -16.140 173.655 24.725 1.00 39.38 ?  99  ILE H CA  1 
ATOM   8388  C  C   . ILE H  4 99  ? -15.552 173.383 26.106 1.00 37.72 ?  99  ILE H C   1 
ATOM   8389  O  O   . ILE H  4 99  ? -14.333 173.429 26.299 1.00 32.68 ?  99  ILE H O   1 
ATOM   8390  C  CB  . ILE H  4 99  ? -16.302 172.354 23.904 1.00 35.32 ?  99  ILE H CB  1 
ATOM   8391  C  CG1 . ILE H  4 99  ? -17.261 172.570 22.735 1.00 40.28 ?  99  ILE H CG1 1 
ATOM   8392  C  CG2 . ILE H  4 99  ? -16.791 171.178 24.744 1.00 39.76 ?  99  ILE H CG2 1 
ATOM   8393  C  CD1 . ILE H  4 99  ? -17.511 171.294 21.937 1.00 35.07 ?  99  ILE H CD1 1 
ATOM   8394  N  N   . GLU H  4 100 ? -16.427 173.125 27.075 1.00 36.66 ?  100 GLU H N   1 
ATOM   8395  C  CA  . GLU H  4 100 ? -16.006 172.661 28.388 1.00 41.09 ?  100 GLU H CA  1 
ATOM   8396  C  C   . GLU H  4 100 ? -16.835 171.440 28.755 1.00 37.30 ?  100 GLU H C   1 
ATOM   8397  O  O   . GLU H  4 100 ? -18.063 171.464 28.630 1.00 41.31 ?  100 GLU H O   1 
ATOM   8398  C  CB  . GLU H  4 100 ? -16.162 173.766 29.435 1.00 42.34 ?  100 GLU H CB  1 
ATOM   8399  C  CG  . GLU H  4 100 ? -15.869 173.284 30.856 1.00 55.76 ?  100 GLU H CG  1 
ATOM   8400  C  CD  . GLU H  4 100 ? -15.890 174.412 31.881 1.00 62.15 ?  100 GLU H CD  1 
ATOM   8401  O  OE1 . GLU H  4 100 ? -15.919 175.599 31.470 1.00 65.62 ?  100 GLU H OE1 1 
ATOM   8402  O  OE2 . GLU H  4 100 ? -15.886 174.102 33.094 1.00 66.05 -1 100 GLU H OE2 1 
ATOM   8403  N  N   . ASP H  4 101 ? -16.169 170.364 29.174 1.00 39.61 ?  101 ASP H N   1 
ATOM   8404  C  CA  . ASP H  4 101 ? -16.863 169.108 29.434 1.00 39.69 ?  101 ASP H CA  1 
ATOM   8405  C  C   . ASP H  4 101 ? -16.274 168.399 30.643 1.00 44.87 ?  101 ASP H C   1 
ATOM   8406  O  O   . ASP H  4 101 ? -15.049 168.307 30.784 1.00 46.59 ?  101 ASP H O   1 
ATOM   8407  C  CB  . ASP H  4 101 ? -16.789 168.177 28.227 1.00 42.76 ?  101 ASP H CB  1 
ATOM   8408  C  CG  . ASP H  4 101 ? -17.760 167.028 28.329 1.00 45.08 ?  101 ASP H CG  1 
ATOM   8409  O  OD1 . ASP H  4 101 ? -18.982 167.281 28.223 1.00 47.30 ?  101 ASP H OD1 1 
ATOM   8410  O  OD2 . ASP H  4 101 ? -17.302 165.882 28.543 1.00 43.83 -1 101 ASP H OD2 1 
ATOM   8411  N  N   . SER H  4 102 ? -17.149 167.865 31.498 1.00 41.79 ?  102 SER H N   1 
ATOM   8412  C  CA  . SER H  4 102 ? -16.714 167.256 32.752 1.00 49.80 ?  102 SER H CA  1 
ATOM   8413  C  C   . SER H  4 102 ? -16.870 165.740 32.764 1.00 51.89 ?  102 SER H C   1 
ATOM   8414  O  O   . SER H  4 102 ? -16.687 165.120 33.816 1.00 54.27 ?  102 SER H O   1 
ATOM   8415  C  CB  . SER H  4 102 ? -17.468 167.872 33.937 1.00 50.98 ?  102 SER H CB  1 
ATOM   8416  O  OG  . SER H  4 102 ? -18.841 168.035 33.622 1.00 68.64 ?  102 SER H OG  1 
ATOM   8417  N  N   . VAL H  4 103 ? -17.189 165.129 31.627 1.00 43.92 ?  103 VAL H N   1 
ATOM   8418  C  CA  . VAL H  4 103 ? -17.302 163.682 31.524 1.00 39.27 ?  103 VAL H CA  1 
ATOM   8419  C  C   . VAL H  4 103 ? -16.050 163.065 30.912 1.00 49.11 ?  103 VAL H C   1 
ATOM   8420  O  O   . VAL H  4 103 ? -15.603 162.004 31.345 1.00 48.62 ?  103 VAL H O   1 
ATOM   8421  C  CB  . VAL H  4 103 ? -18.561 163.314 30.716 1.00 38.21 ?  103 VAL H CB  1 
ATOM   8422  C  CG1 . VAL H  4 103 ? -18.650 161.797 30.508 1.00 46.48 ?  103 VAL H CG1 1 
ATOM   8423  C  CG2 . VAL H  4 103 ? -19.796 163.854 31.401 1.00 38.48 ?  103 VAL H CG2 1 
ATOM   8424  N  N   . ILE H  4 104 ? -15.479 163.703 29.883 1.00 48.88 ?  104 ILE H N   1 
ATOM   8425  C  CA  . ILE H  4 104 ? -14.176 163.262 29.398 1.00 42.89 ?  104 ILE H CA  1 
ATOM   8426  C  C   . ILE H  4 104 ? -13.114 163.613 30.428 1.00 41.20 ?  104 ILE H C   1 
ATOM   8427  O  O   . ILE H  4 104 ? -13.292 164.499 31.271 1.00 41.58 ?  104 ILE H O   1 
ATOM   8428  C  CB  . ILE H  4 104 ? -13.840 163.882 28.030 1.00 40.26 ?  104 ILE H CB  1 
ATOM   8429  C  CG1 . ILE H  4 104 ? -13.822 165.409 28.121 1.00 37.58 ?  104 ILE H CG1 1 
ATOM   8430  C  CG2 . ILE H  4 104 ? -14.828 163.424 26.981 1.00 39.16 ?  104 ILE H CG2 1 
ATOM   8431  C  CD1 . ILE H  4 104 ? -12.930 166.108 27.042 1.00 43.09 ?  104 ILE H CD1 1 
ATOM   8432  N  N   . SER H  4 105 ? -11.983 162.924 30.340 1.00 40.18 ?  105 SER H N   1 
ATOM   8433  C  CA  . SER H  4 105 ? -10.874 163.223 31.224 1.00 39.10 ?  105 SER H CA  1 
ATOM   8434  C  C   . SER H  4 105 ? -9.562  162.963 30.513 1.00 39.07 ?  105 SER H C   1 
ATOM   8435  O  O   . SER H  4 105 ? -9.485  162.146 29.593 1.00 44.01 ?  105 SER H O   1 
ATOM   8436  C  CB  . SER H  4 105 ? -10.925 162.379 32.510 1.00 42.30 ?  105 SER H CB  1 
ATOM   8437  O  OG  . SER H  4 105 ? -9.970  162.859 33.439 1.00 45.60 ?  105 SER H OG  1 
ATOM   8438  N  N   . LEU H  4 106 ? -8.520  163.642 30.977 1.00 37.44 ?  106 LEU H N   1 
ATOM   8439  C  CA  . LEU H  4 106 ? -7.163  163.331 30.573 1.00 37.17 ?  106 LEU H CA  1 
ATOM   8440  C  C   . LEU H  4 106 ? -6.494  162.328 31.511 1.00 51.75 ?  106 LEU H C   1 
ATOM   8441  O  O   . LEU H  4 106 ? -5.276  162.117 31.411 1.00 51.70 ?  106 LEU H O   1 
ATOM   8442  C  CB  . LEU H  4 106 ? -6.354  164.627 30.479 1.00 38.74 ?  106 LEU H CB  1 
ATOM   8443  C  CG  . LEU H  4 106 ? -7.011  165.663 29.550 1.00 42.08 ?  106 LEU H CG  1 
ATOM   8444  C  CD1 . LEU H  4 106 ? -6.178  166.937 29.404 1.00 35.47 ?  106 LEU H CD1 1 
ATOM   8445  C  CD2 . LEU H  4 106 ? -7.303  165.050 28.175 1.00 33.83 ?  106 LEU H CD2 1 
ATOM   8446  N  N   . SER H  4 107 ? -7.264  161.699 32.407 1.00 51.77 ?  107 SER H N   1 
ATOM   8447  C  CA  . SER H  4 107 ? -6.748  160.684 33.325 1.00 53.72 ?  107 SER H CA  1 
ATOM   8448  C  C   . SER H  4 107 ? -7.857  159.701 33.674 1.00 52.78 ?  107 SER H C   1 
ATOM   8449  O  O   . SER H  4 107 ? -9.043  159.963 33.453 1.00 51.94 ?  107 SER H O   1 
ATOM   8450  C  CB  . SER H  4 107 ? -6.199  161.310 34.614 1.00 42.64 ?  107 SER H CB  1 
ATOM   8451  O  OG  . SER H  4 107 ? -7.034  162.385 35.014 1.00 58.79 ?  107 SER H OG  1 
ATOM   8452  N  N   . GLY H  4 108 ? -7.453  158.552 34.222 1.00 55.09 ?  108 GLY H N   1 
ATOM   8453  C  CA  . GLY H  4 108 ? -8.406  157.625 34.801 1.00 47.87 ?  108 GLY H CA  1 
ATOM   8454  C  C   . GLY H  4 108 ? -9.149  156.772 33.790 1.00 57.38 ?  108 GLY H C   1 
ATOM   8455  O  O   . GLY H  4 108 ? -8.735  156.593 32.640 1.00 57.36 ?  108 GLY H O   1 
ATOM   8456  N  N   . ASP H  4 109 ? -10.287 156.233 34.247 1.00 59.79 ?  109 ASP H N   1 
ATOM   8457  C  CA  . ASP H  4 109 ? -11.048 155.298 33.418 1.00 62.35 ?  109 ASP H CA  1 
ATOM   8458  C  C   . ASP H  4 109 ? -11.649 155.985 32.193 1.00 57.27 ?  109 ASP H C   1 
ATOM   8459  O  O   . ASP H  4 109 ? -11.762 155.374 31.120 1.00 53.87 ?  109 ASP H O   1 
ATOM   8460  C  CB  . ASP H  4 109 ? -12.148 154.632 34.251 1.00 64.09 ?  109 ASP H CB  1 
ATOM   8461  C  CG  . ASP H  4 109 ? -11.639 153.439 35.062 1.00 73.19 ?  109 ASP H CG  1 
ATOM   8462  O  OD1 . ASP H  4 109 ? -10.463 153.048 34.886 1.00 72.87 ?  109 ASP H OD1 1 
ATOM   8463  O  OD2 . ASP H  4 109 ? -12.424 152.884 35.865 1.00 79.33 -1 109 ASP H OD2 1 
ATOM   8464  N  N   . HIS H  4 110 ? -12.063 157.243 32.343 1.00 51.56 ?  110 HIS H N   1 
ATOM   8465  C  CA  . HIS H  4 110 ? -12.660 158.045 31.280 1.00 53.52 ?  110 HIS H CA  1 
ATOM   8466  C  C   . HIS H  4 110 ? -11.611 158.720 30.385 1.00 50.07 ?  110 HIS H C   1 
ATOM   8467  O  O   . HIS H  4 110 ? -11.947 159.671 29.662 1.00 47.59 ?  110 HIS H O   1 
ATOM   8468  C  CB  . HIS H  4 110 ? -13.573 159.110 31.893 1.00 51.24 ?  110 HIS H CB  1 
ATOM   8469  C  CG  . HIS H  4 110 ? -14.906 158.588 32.334 1.00 59.67 ?  110 HIS H CG  1 
ATOM   8470  N  ND1 . HIS H  4 110 ? -15.937 159.418 32.732 1.00 54.55 ?  110 HIS H ND1 1 
ATOM   8471  C  CD2 . HIS H  4 110 ? -15.381 157.321 32.429 1.00 52.24 ?  110 HIS H CD2 1 
ATOM   8472  C  CE1 . HIS H  4 110 ? -16.991 158.684 33.046 1.00 54.92 ?  110 HIS H CE1 1 
ATOM   8473  N  NE2 . HIS H  4 110 ? -16.680 157.410 32.873 1.00 52.71 ?  110 HIS H NE2 1 
ATOM   8474  N  N   . CYS H  4 111 ? -10.358 158.267 30.443 1.00 43.44 ?  111 CYS H N   1 
ATOM   8475  C  CA  . CYS H  4 111 ? -9.277  158.938 29.736 1.00 47.25 ?  111 CYS H CA  1 
ATOM   8476  C  C   . CYS H  4 111 ? -9.457  158.840 28.225 1.00 39.47 ?  111 CYS H C   1 
ATOM   8477  O  O   . CYS H  4 111 ? -9.741  157.768 27.681 1.00 41.51 ?  111 CYS H O   1 
ATOM   8478  C  CB  . CYS H  4 111 ? -7.937  158.341 30.146 1.00 46.18 ?  111 CYS H CB  1 
ATOM   8479  S  SG  . CYS H  4 111 ? -6.527  159.334 29.672 1.00 50.12 ?  111 CYS H SG  1 
ATOM   8480  N  N   . ILE H  4 112 ? -9.289  159.972 27.545 1.00 40.06 ?  112 ILE H N   1 
ATOM   8481  C  CA  . ILE H  4 112 ? -9.418  160.005 26.099 1.00 40.25 ?  112 ILE H CA  1 
ATOM   8482  C  C   . ILE H  4 112 ? -8.072  160.092 25.416 1.00 43.59 ?  112 ILE H C   1 
ATOM   8483  O  O   . ILE H  4 112 ? -8.015  160.162 24.179 1.00 40.56 ?  112 ILE H O   1 
ATOM   8484  C  CB  . ILE H  4 112 ? -10.316 161.176 25.663 1.00 41.28 ?  112 ILE H CB  1 
ATOM   8485  C  CG1 . ILE H  4 112 ? -9.706  162.482 26.149 1.00 37.67 ?  112 ILE H CG1 1 
ATOM   8486  C  CG2 . ILE H  4 112 ? -11.722 161.011 26.235 1.00 35.95 ?  112 ILE H CG2 1 
ATOM   8487  C  CD1 . ILE H  4 112 ? -10.264 163.702 25.474 1.00 39.79 ?  112 ILE H CD1 1 
ATOM   8488  N  N   . ILE H  4 113 ? -6.977  160.080 26.178 1.00 38.34 ?  113 ILE H N   1 
ATOM   8489  C  CA  . ILE H  4 113 ? -5.658  160.106 25.558 1.00 41.74 ?  113 ILE H CA  1 
ATOM   8490  C  C   . ILE H  4 113 ? -5.401  158.777 24.855 1.00 44.63 ?  113 ILE H C   1 
ATOM   8491  O  O   . ILE H  4 113 ? -5.728  157.700 25.371 1.00 36.87 ?  113 ILE H O   1 
ATOM   8492  C  CB  . ILE H  4 113 ? -4.585  160.434 26.610 1.00 42.11 ?  113 ILE H CB  1 
ATOM   8493  C  CG1 . ILE H  4 113 ? -4.663  161.922 26.952 1.00 40.49 ?  113 ILE H CG1 1 
ATOM   8494  C  CG2 . ILE H  4 113 ? -3.189  160.068 26.116 1.00 39.46 ?  113 ILE H CG2 1 
ATOM   8495  C  CD1 . ILE H  4 113 ? -3.752  162.345 28.059 1.00 45.48 ?  113 ILE H CD1 1 
ATOM   8496  N  N   . GLY H  4 114 ? -4.851  158.846 23.650 1.00 38.81 ?  114 GLY H N   1 
ATOM   8497  C  CA  . GLY H  4 114 ? -4.685  157.646 22.861 1.00 35.85 ?  114 GLY H CA  1 
ATOM   8498  C  C   . GLY H  4 114 ? -5.943  157.180 22.173 1.00 32.10 ?  114 GLY H C   1 
ATOM   8499  O  O   . GLY H  4 114 ? -5.925  156.112 21.545 1.00 36.75 ?  114 GLY H O   1 
ATOM   8500  N  N   . ARG H  4 115 ? -7.033  157.939 22.272 1.00 33.81 ?  115 ARG H N   1 
ATOM   8501  C  CA  . ARG H  4 115 ? -8.235  157.702 21.485 1.00 32.59 ?  115 ARG H CA  1 
ATOM   8502  C  C   . ARG H  4 115 ? -8.294  158.726 20.348 1.00 33.97 ?  115 ARG H C   1 
ATOM   8503  O  O   . ARG H  4 115 ? -7.363  159.507 20.155 1.00 35.60 ?  115 ARG H O   1 
ATOM   8504  C  CB  . ARG H  4 115 ? -9.460  157.741 22.395 1.00 35.59 ?  115 ARG H CB  1 
ATOM   8505  C  CG  . ARG H  4 115 ? -9.244  156.882 23.627 1.00 38.58 ?  115 ARG H CG  1 
ATOM   8506  C  CD  . ARG H  4 115 ? -10.532 156.453 24.302 1.00 42.75 ?  115 ARG H CD  1 
ATOM   8507  N  NE  . ARG H  4 115 ? -10.215 155.678 25.498 1.00 45.46 ?  115 ARG H NE  1 
ATOM   8508  C  CZ  . ARG H  4 115 ? -10.232 154.353 25.559 1.00 44.54 ?  115 ARG H CZ  1 
ATOM   8509  N  NH1 . ARG H  4 115 ? -10.613 153.615 24.528 1.00 41.79 ?  115 ARG H NH1 1 
ATOM   8510  N  NH2 . ARG H  4 115 ? -9.870  153.752 26.685 1.00 53.65 ?  115 ARG H NH2 1 
ATOM   8511  N  N   . THR H  4 116 ? -9.381  158.711 19.571 1.00 31.92 ?  116 THR H N   1 
ATOM   8512  C  CA  . THR H  4 116 ? -9.476  159.521 18.353 1.00 33.79 ?  116 THR H CA  1 
ATOM   8513  C  C   . THR H  4 116 ? -10.605 160.539 18.461 1.00 34.83 ?  116 THR H C   1 
ATOM   8514  O  O   . THR H  4 116 ? -11.751 160.183 18.755 1.00 34.41 ?  116 THR H O   1 
ATOM   8515  C  CB  . THR H  4 116 ? -9.688  158.650 17.113 1.00 34.06 ?  116 THR H CB  1 
ATOM   8516  O  OG1 . THR H  4 116 ? -8.536  157.826 16.899 1.00 41.09 ?  116 THR H OG1 1 
ATOM   8517  C  CG2 . THR H  4 116 ? -9.900  159.521 15.889 1.00 32.52 ?  116 THR H CG2 1 
ATOM   8518  N  N   . LEU H  4 117 ? -10.273 161.804 18.229 1.00 30.38 ?  117 LEU H N   1 
ATOM   8519  C  CA  . LEU H  4 117 ? -11.255 162.859 18.053 1.00 30.62 ?  117 LEU H CA  1 
ATOM   8520  C  C   . LEU H  4 117 ? -11.655 162.899 16.578 1.00 29.10 ?  117 LEU H C   1 
ATOM   8521  O  O   . LEU H  4 117 ? -10.787 162.885 15.706 1.00 31.87 ?  117 LEU H O   1 
ATOM   8522  C  CB  . LEU H  4 117 ? -10.650 164.193 18.501 1.00 28.34 ?  117 LEU H CB  1 
ATOM   8523  C  CG  . LEU H  4 117 ? -11.559 165.410 18.441 1.00 32.07 ?  117 LEU H CG  1 
ATOM   8524  C  CD1 . LEU H  4 117 ? -12.594 165.318 19.539 1.00 29.62 ?  117 LEU H CD1 1 
ATOM   8525  C  CD2 . LEU H  4 117 ? -10.731 166.678 18.596 1.00 29.32 ?  117 LEU H CD2 1 
ATOM   8526  N  N   . VAL H  4 118 ? -12.957 162.937 16.298 1.00 28.98 ?  118 VAL H N   1 
ATOM   8527  C  CA  . VAL H  4 118 ? -13.470 162.914 14.933 1.00 30.49 ?  118 VAL H CA  1 
ATOM   8528  C  C   . VAL H  4 118 ? -14.452 164.053 14.771 1.00 32.97 ?  118 VAL H C   1 
ATOM   8529  O  O   . VAL H  4 118 ? -15.368 164.203 15.586 1.00 30.04 ?  118 VAL H O   1 
ATOM   8530  C  CB  . VAL H  4 118 ? -14.170 161.584 14.596 1.00 31.98 ?  118 VAL H CB  1 
ATOM   8531  C  CG1 . VAL H  4 118 ? -14.801 161.663 13.214 1.00 30.14 ?  118 VAL H CG1 1 
ATOM   8532  C  CG2 . VAL H  4 118 ? -13.202 160.423 14.708 1.00 30.33 ?  118 VAL H CG2 1 
ATOM   8533  N  N   . VAL H  4 119 ? -14.284 164.848 13.717 1.00 26.25 ?  119 VAL H N   1 
ATOM   8534  C  CA  . VAL H  4 119 ? -15.293 165.835 13.368 1.00 25.09 ?  119 VAL H CA  1 
ATOM   8535  C  C   . VAL H  4 119 ? -16.082 165.262 12.206 1.00 31.08 ?  119 VAL H C   1 
ATOM   8536  O  O   . VAL H  4 119 ? -15.504 164.682 11.269 1.00 30.73 ?  119 VAL H O   1 
ATOM   8537  C  CB  . VAL H  4 119 ? -14.690 167.216 13.034 1.00 27.19 ?  119 VAL H CB  1 
ATOM   8538  C  CG1 . VAL H  4 119 ? -13.733 167.142 11.849 1.00 26.36 ?  119 VAL H CG1 1 
ATOM   8539  C  CG2 . VAL H  4 119 ? -15.806 168.217 12.749 1.00 25.52 ?  119 VAL H CG2 1 
ATOM   8540  N  N   . HIS H  4 120 ? -17.401 165.416 12.266 1.00 31.12 ?  120 HIS H N   1 
ATOM   8541  C  CA  . HIS H  4 120 ? -18.315 164.653 11.428 1.00 31.66 ?  120 HIS H CA  1 
ATOM   8542  C  C   . HIS H  4 120 ? -18.977 165.499 10.347 1.00 31.25 ?  120 HIS H C   1 
ATOM   8543  O  O   . HIS H  4 120 ? -19.028 166.736 10.406 1.00 30.05 ?  120 HIS H O   1 
ATOM   8544  C  CB  . HIS H  4 120 ? -19.390 163.988 12.288 1.00 30.76 ?  120 HIS H CB  1 
ATOM   8545  C  CG  . HIS H  4 120 ? -18.921 162.738 12.952 1.00 33.07 ?  120 HIS H CG  1 
ATOM   8546  N  ND1 . HIS H  4 120 ? -19.066 161.494 12.379 1.00 33.55 ?  120 HIS H ND1 1 
ATOM   8547  C  CD2 . HIS H  4 120 ? -18.256 162.544 14.114 1.00 30.24 ?  120 HIS H CD2 1 
ATOM   8548  C  CE1 . HIS H  4 120 ? -18.540 160.581 13.178 1.00 33.20 ?  120 HIS H CE1 1 
ATOM   8549  N  NE2 . HIS H  4 120 ? -18.040 161.192 14.237 1.00 33.08 ?  120 HIS H NE2 1 
ATOM   8550  N  N   . GLU H  4 121 ? -19.560 164.779 9.392  1.00 33.26 ?  121 GLU H N   1 
ATOM   8551  C  CA  . GLU H  4 121 ? -20.089 165.390 8.180  1.00 32.24 ?  121 GLU H CA  1 
ATOM   8552  C  C   . GLU H  4 121 ? -21.271 166.306 8.462  1.00 30.85 ?  121 GLU H C   1 
ATOM   8553  O  O   . GLU H  4 121 ? -21.378 167.381 7.864  1.00 31.30 ?  121 GLU H O   1 
ATOM   8554  C  CB  . GLU H  4 121 ? -20.481 164.285 7.194  1.00 33.17 ?  121 GLU H CB  1 
ATOM   8555  C  CG  . GLU H  4 121 ? -21.568 164.675 6.216  1.00 40.23 ?  121 GLU H CG  1 
ATOM   8556  C  CD  . GLU H  4 121 ? -22.009 163.497 5.351  1.00 51.13 ?  121 GLU H CD  1 
ATOM   8557  O  OE1 . GLU H  4 121 ? -22.379 162.429 5.911  1.00 41.97 ?  121 GLU H OE1 1 
ATOM   8558  O  OE2 . GLU H  4 121 ? -21.988 163.659 4.108  1.00 65.08 -1 121 GLU H OE2 1 
ATOM   8559  N  N   . LYS H  4 122 ? -22.183 165.905 9.343  1.00 33.77 ?  122 LYS H N   1 
ATOM   8560  C  CA  . LYS H  4 122 ? -23.345 166.749 9.594  1.00 34.40 ?  122 LYS H CA  1 
ATOM   8561  C  C   . LYS H  4 122 ? -23.585 166.858 11.095 1.00 33.88 ?  122 LYS H C   1 
ATOM   8562  O  O   . LYS H  4 122 ? -22.772 166.418 11.914 1.00 29.46 ?  122 LYS H O   1 
ATOM   8563  C  CB  . LYS H  4 122 ? -24.594 166.238 8.863  1.00 44.08 ?  122 LYS H CB  1 
ATOM   8564  C  CG  . LYS H  4 122 ? -24.714 164.745 8.723  1.00 47.09 ?  122 LYS H CG  1 
ATOM   8565  C  CD  . LYS H  4 122 ? -25.570 164.422 7.502  1.00 43.26 ?  122 LYS H CD  1 
ATOM   8566  C  CE  . LYS H  4 122 ? -25.615 162.926 7.232  1.00 51.14 ?  122 LYS H CE  1 
ATOM   8567  N  NZ  . LYS H  4 122 ? -25.716 162.570 5.773  1.00 60.94 ?  122 LYS H NZ  1 
ATOM   8568  N  N   . ALA H  4 123 ? -24.720 167.467 11.434 1.00 34.64 ?  123 ALA H N   1 
ATOM   8569  C  CA  . ALA H  4 123 ? -25.032 167.806 12.811 1.00 33.86 ?  123 ALA H CA  1 
ATOM   8570  C  C   . ALA H  4 123 ? -25.300 166.558 13.632 1.00 40.35 ?  123 ALA H C   1 
ATOM   8571  O  O   . ALA H  4 123 ? -25.902 165.590 13.159 1.00 35.14 ?  123 ALA H O   1 
ATOM   8572  C  CB  . ALA H  4 123 ? -26.250 168.716 12.868 1.00 34.86 ?  123 ALA H CB  1 
ATOM   8573  N  N   . ASP H  4 124 ? -24.824 166.580 14.863 1.00 33.94 ?  124 ASP H N   1 
ATOM   8574  C  CA  . ASP H  4 124 ? -25.255 165.605 15.845 1.00 35.60 ?  124 ASP H CA  1 
ATOM   8575  C  C   . ASP H  4 124 ? -26.666 165.957 16.302 1.00 37.67 ?  124 ASP H C   1 
ATOM   8576  O  O   . ASP H  4 124 ? -26.921 167.088 16.738 1.00 36.22 ?  124 ASP H O   1 
ATOM   8577  C  CB  . ASP H  4 124 ? -24.285 165.615 17.018 1.00 31.88 ?  124 ASP H CB  1 
ATOM   8578  C  CG  . ASP H  4 124 ? -24.533 164.488 17.988 1.00 39.00 ?  124 ASP H CG  1 
ATOM   8579  O  OD1 . ASP H  4 124 ? -25.649 163.926 17.997 1.00 39.28 ?  124 ASP H OD1 1 
ATOM   8580  O  OD2 . ASP H  4 124 ? -23.595 164.166 18.738 1.00 35.02 -1 124 ASP H OD2 1 
ATOM   8581  N  N   . ASP H  4 125 ? -27.598 165.007 16.184 1.00 36.31 ?  125 ASP H N   1 
ATOM   8582  C  CA  . ASP H  4 125 ? -28.945 165.272 16.694 1.00 33.92 ?  125 ASP H CA  1 
ATOM   8583  C  C   . ASP H  4 125 ? -29.040 165.048 18.199 1.00 35.72 ?  125 ASP H C   1 
ATOM   8584  O  O   . ASP H  4 125 ? -30.129 165.168 18.769 1.00 37.78 ?  125 ASP H O   1 
ATOM   8585  C  CB  . ASP H  4 125 ? -30.008 164.449 15.930 1.00 35.35 ?  125 ASP H CB  1 
ATOM   8586  C  CG  . ASP H  4 125 ? -29.942 162.933 16.191 1.00 38.77 ?  125 ASP H CG  1 
ATOM   8587  O  OD1 . ASP H  4 125 ? -29.320 162.470 17.172 1.00 38.80 ?  125 ASP H OD1 1 
ATOM   8588  O  OD2 . ASP H  4 125 ? -30.541 162.195 15.372 1.00 38.60 -1 125 ASP H OD2 1 
ATOM   8589  N  N   . LEU H  4 126 ? -27.918 164.738 18.840 1.00 36.08 ?  126 LEU H N   1 
ATOM   8590  C  CA  . LEU H  4 126 ? -27.804 164.714 20.290 1.00 38.76 ?  126 LEU H CA  1 
ATOM   8591  C  C   . LEU H  4 126 ? -28.662 163.607 20.889 1.00 41.29 ?  126 LEU H C   1 
ATOM   8592  O  O   . LEU H  4 126 ? -29.108 163.700 22.033 1.00 34.07 ?  126 LEU H O   1 
ATOM   8593  C  CB  . LEU H  4 126 ? -28.145 166.084 20.900 1.00 37.89 ?  126 LEU H CB  1 
ATOM   8594  C  CG  . LEU H  4 126 ? -27.380 167.309 20.352 1.00 43.07 ?  126 LEU H CG  1 
ATOM   8595  C  CD1 . LEU H  4 126 ? -27.858 168.603 21.007 1.00 36.47 ?  126 LEU H CD1 1 
ATOM   8596  C  CD2 . LEU H  4 126 ? -25.883 167.172 20.556 1.00 32.51 ?  126 LEU H CD2 1 
ATOM   8597  N  N   . GLY H  4 127 ? -28.884 162.549 20.110 1.00 38.02 ?  127 GLY H N   1 
ATOM   8598  C  CA  . GLY H  4 127 ? -29.640 161.410 20.578 1.00 38.16 ?  127 GLY H CA  1 
ATOM   8599  C  C   . GLY H  4 127 ? -31.133 161.613 20.590 1.00 37.60 ?  127 GLY H C   1 
ATOM   8600  O  O   . GLY H  4 127 ? -31.850 160.781 21.149 1.00 36.91 ?  127 GLY H O   1 
ATOM   8601  N  N   . LYS H  4 128 ? -31.633 162.678 19.972 1.00 33.84 ?  128 LYS H N   1 
ATOM   8602  C  CA  . LYS H  4 128 ? -33.055 162.986 19.995 1.00 36.13 ?  128 LYS H CA  1 
ATOM   8603  C  C   . LYS H  4 128 ? -33.743 162.695 18.671 1.00 33.16 ?  128 LYS H C   1 
ATOM   8604  O  O   . LYS H  4 128 ? -34.829 163.230 18.417 1.00 35.02 ?  128 LYS H O   1 
ATOM   8605  C  CB  . LYS H  4 128 ? -33.259 164.439 20.396 1.00 38.65 ?  128 LYS H CB  1 
ATOM   8606  C  CG  . LYS H  4 128 ? -32.254 164.858 21.450 1.00 41.07 ?  128 LYS H CG  1 
ATOM   8607  C  CD  . LYS H  4 128 ? -32.863 165.698 22.540 1.00 45.34 ?  128 LYS H CD  1 
ATOM   8608  C  CE  . LYS H  4 128 ? -33.001 167.126 22.081 1.00 51.83 ?  128 LYS H CE  1 
ATOM   8609  N  NZ  . LYS H  4 128 ? -32.789 168.042 23.225 1.00 56.06 ?  128 LYS H NZ  1 
ATOM   8610  N  N   . GLY H  4 129 ? -33.143 161.862 17.820 1.00 33.26 ?  129 GLY H N   1 
ATOM   8611  C  CA  . GLY H  4 129 ? -33.697 161.629 16.501 1.00 34.37 ?  129 GLY H CA  1 
ATOM   8612  C  C   . GLY H  4 129 ? -34.769 160.560 16.417 1.00 39.19 ?  129 GLY H C   1 
ATOM   8613  O  O   . GLY H  4 129 ? -35.408 160.407 15.372 1.00 35.88 ?  129 GLY H O   1 
ATOM   8614  N  N   . GLY H  4 130 ? -34.985 159.799 17.489 1.00 40.35 ?  130 GLY H N   1 
ATOM   8615  C  CA  . GLY H  4 130 ? -36.014 158.778 17.505 1.00 34.34 ?  130 GLY H CA  1 
ATOM   8616  C  C   . GLY H  4 130 ? -35.743 157.545 16.671 1.00 38.81 ?  130 GLY H C   1 
ATOM   8617  O  O   . GLY H  4 130 ? -36.620 156.677 16.578 1.00 40.73 ?  130 GLY H O   1 
ATOM   8618  N  N   . ASN H  4 131 ? -34.582 157.422 16.045 1.00 37.60 ?  131 ASN H N   1 
ATOM   8619  C  CA  . ASN H  4 131 ? -34.283 156.195 15.326 1.00 41.10 ?  131 ASN H CA  1 
ATOM   8620  C  C   . ASN H  4 131 ? -33.057 155.546 15.942 1.00 39.09 ?  131 ASN H C   1 
ATOM   8621  O  O   . ASN H  4 131 ? -32.431 156.087 16.860 1.00 43.21 ?  131 ASN H O   1 
ATOM   8622  C  CB  . ASN H  4 131 ? -34.113 156.435 13.808 1.00 43.68 ?  131 ASN H CB  1 
ATOM   8623  C  CG  . ASN H  4 131 ? -32.925 157.344 13.453 1.00 47.34 ?  131 ASN H CG  1 
ATOM   8624  O  OD1 . ASN H  4 131 ? -32.315 157.998 14.308 1.00 41.71 ?  131 ASN H OD1 1 
ATOM   8625  N  ND2 . ASN H  4 131 ? -32.593 157.370 12.170 1.00 45.61 ?  131 ASN H ND2 1 
ATOM   8626  N  N   . GLU H  4 132 ? -32.747 154.334 15.475 1.00 44.20 ?  132 GLU H N   1 
ATOM   8627  C  CA  . GLU H  4 132 ? -31.673 153.588 16.124 1.00 47.63 ?  132 GLU H CA  1 
ATOM   8628  C  C   . GLU H  4 132 ? -30.331 154.257 15.876 1.00 43.11 ?  132 GLU H C   1 
ATOM   8629  O  O   . GLU H  4 132 ? -29.451 154.249 16.748 1.00 42.10 ?  132 GLU H O   1 
ATOM   8630  C  CB  . GLU H  4 132 ? -31.650 152.139 15.636 1.00 46.70 ?  132 GLU H CB  1 
ATOM   8631  C  CG  . GLU H  4 132 ? -32.973 151.653 15.072 1.00 50.89 ?  132 GLU H CG  1 
ATOM   8632  C  CD  . GLU H  4 132 ? -32.905 150.217 14.564 1.00 65.81 ?  132 GLU H CD  1 
ATOM   8633  O  OE1 . GLU H  4 132 ? -31.825 149.781 14.090 1.00 65.45 ?  132 GLU H OE1 1 
ATOM   8634  O  OE2 . GLU H  4 132 ? -33.942 149.519 14.651 1.00 69.35 -1 132 GLU H OE2 1 
ATOM   8635  N  N   . GLU H  4 133 ? -30.167 154.848 14.691 1.00 47.98 ?  133 GLU H N   1 
ATOM   8636  C  CA  . GLU H  4 133 ? -28.943 155.580 14.393 1.00 47.94 ?  133 GLU H CA  1 
ATOM   8637  C  C   . GLU H  4 133 ? -28.711 156.702 15.404 1.00 41.48 ?  133 GLU H C   1 
ATOM   8638  O  O   . GLU H  4 133 ? -27.586 156.886 15.882 1.00 43.57 ?  133 GLU H O   1 
ATOM   8639  C  CB  . GLU H  4 133 ? -29.007 156.128 12.968 1.00 44.85 ?  133 GLU H CB  1 
ATOM   8640  C  CG  . GLU H  4 133 ? -27.642 156.400 12.358 1.00 47.94 ?  133 GLU H CG  1 
ATOM   8641  C  CD  . GLU H  4 133 ? -26.691 155.234 12.533 1.00 51.10 ?  133 GLU H CD  1 
ATOM   8642  O  OE1 . GLU H  4 133 ? -26.848 154.240 11.793 1.00 60.35 ?  133 GLU H OE1 1 
ATOM   8643  O  OE2 . GLU H  4 133 ? -25.788 155.309 13.398 1.00 51.90 -1 133 GLU H OE2 1 
ATOM   8644  N  N   . SER H  4 134 ? -29.766 157.447 15.756 1.00 38.20 ?  134 SER H N   1 
ATOM   8645  C  CA  . SER H  4 134 ? -29.613 158.540 16.717 1.00 36.40 ?  134 SER H CA  1 
ATOM   8646  C  C   . SER H  4 134 ? -29.015 158.049 18.023 1.00 42.06 ?  134 SER H C   1 
ATOM   8647  O  O   . SER H  4 134 ? -28.200 158.743 18.646 1.00 44.33 ?  134 SER H O   1 
ATOM   8648  C  CB  . SER H  4 134 ? -30.963 159.222 16.964 1.00 38.70 ?  134 SER H CB  1 
ATOM   8649  O  OG  . SER H  4 134 ? -30.884 160.259 17.942 1.00 35.58 ?  134 SER H OG  1 
ATOM   8650  N  N   . THR H  4 135 ? -29.387 156.845 18.446 1.00 41.80 ?  135 THR H N   1 
ATOM   8651  C  CA  . THR H  4 135 ? -28.911 156.303 19.711 1.00 41.35 ?  135 THR H CA  1 
ATOM   8652  C  C   . THR H  4 135 ? -27.464 155.845 19.662 1.00 39.25 ?  135 THR H C   1 
ATOM   8653  O  O   . THR H  4 135 ? -26.879 155.598 20.727 1.00 40.78 ?  135 THR H O   1 
ATOM   8654  C  CB  . THR H  4 135 ? -29.791 155.126 20.131 1.00 43.56 ?  135 THR H CB  1 
ATOM   8655  O  OG1 . THR H  4 135 ? -29.554 154.030 19.235 1.00 46.84 ?  135 THR H OG1 1 
ATOM   8656  C  CG2 . THR H  4 135 ? -31.249 155.514 20.039 1.00 43.20 ?  135 THR H CG2 1 
ATOM   8657  N  N   . LYS H  4 136 ? -26.888 155.691 18.467 1.00 37.16 ?  136 LYS H N   1 
ATOM   8658  C  CA  . LYS H  4 136 ? -25.505 155.255 18.297 1.00 39.45 ?  136 LYS H CA  1 
ATOM   8659  C  C   . LYS H  4 136 ? -24.567 156.403 17.929 1.00 41.86 ?  136 LYS H C   1 
ATOM   8660  O  O   . LYS H  4 136 ? -23.533 156.598 18.574 1.00 38.77 ?  136 LYS H O   1 
ATOM   8661  C  CB  . LYS H  4 136 ? -25.416 154.176 17.211 1.00 46.43 ?  136 LYS H CB  1 
ATOM   8662  C  CG  . LYS H  4 136 ? -26.264 152.930 17.432 1.00 46.79 ?  136 LYS H CG  1 
ATOM   8663  C  CD  . LYS H  4 136 ? -26.689 152.326 16.081 1.00 52.42 ?  136 LYS H CD  1 
ATOM   8664  C  CE  . LYS H  4 136 ? -26.550 150.799 16.032 1.00 57.41 ?  136 LYS H CE  1 
ATOM   8665  N  NZ  . LYS H  4 136 ? -25.195 150.330 15.589 1.00 67.59 ?  136 LYS H NZ  1 
ATOM   8666  N  N   . THR H  4 137 ? -24.893 157.154 16.880 1.00 41.94 ?  137 THR H N   1 
ATOM   8667  C  CA  . THR H  4 137 ? -23.990 158.163 16.339 1.00 40.01 ?  137 THR H CA  1 
ATOM   8668  C  C   . THR H  4 137 ? -24.613 159.545 16.275 1.00 42.53 ?  137 THR H C   1 
ATOM   8669  O  O   . THR H  4 137 ? -23.944 160.496 15.845 1.00 43.84 ?  137 THR H O   1 
ATOM   8670  C  CB  . THR H  4 137 ? -23.528 157.761 14.938 1.00 36.42 ?  137 THR H CB  1 
ATOM   8671  O  OG1 . THR H  4 137 ? -24.630 157.885 14.023 1.00 46.26 ?  137 THR H OG1 1 
ATOM   8672  C  CG2 . THR H  4 137 ? -23.020 156.317 14.932 1.00 43.51 ?  137 THR H CG2 1 
ATOM   8673  N  N   . GLY H  4 138 ? -25.865 159.691 16.691 1.00 39.05 ?  138 GLY H N   1 
ATOM   8674  C  CA  . GLY H  4 138 ? -26.530 160.966 16.570 1.00 37.64 ?  138 GLY H CA  1 
ATOM   8675  C  C   . GLY H  4 138 ? -26.832 161.375 15.150 1.00 37.74 ?  138 GLY H C   1 
ATOM   8676  O  O   . GLY H  4 138 ? -27.187 162.536 14.924 1.00 37.61 ?  138 GLY H O   1 
ATOM   8677  N  N   . ASN H  4 139 ? -26.707 160.459 14.184 1.00 37.93 ?  139 ASN H N   1 
ATOM   8678  C  CA  . ASN H  4 139 ? -26.935 160.760 12.764 1.00 36.74 ?  139 ASN H CA  1 
ATOM   8679  C  C   . ASN H  4 139 ? -25.941 161.794 12.237 1.00 39.74 ?  139 ASN H C   1 
ATOM   8680  O  O   . ASN H  4 139 ? -26.268 162.586 11.346 1.00 39.73 ?  139 ASN H O   1 
ATOM   8681  C  CB  . ASN H  4 139 ? -28.372 161.230 12.506 1.00 37.74 ?  139 ASN H CB  1 
ATOM   8682  C  CG  . ASN H  4 139 ? -29.397 160.105 12.678 1.00 48.15 ?  139 ASN H CG  1 
ATOM   8683  O  OD1 . ASN H  4 139 ? -29.329 159.086 11.994 1.00 51.31 ?  139 ASN H OD1 1 
ATOM   8684  N  ND2 . ASN H  4 139 ? -30.340 160.288 13.595 1.00 38.51 ?  139 ASN H ND2 1 
ATOM   8685  N  N   . ALA H  4 140 ? -24.726 161.809 12.791 1.00 35.14 ?  140 ALA H N   1 
ATOM   8686  C  CA  . ALA H  4 140 ? -23.742 162.818 12.407 1.00 40.16 ?  140 ALA H CA  1 
ATOM   8687  C  C   . ALA H  4 140 ? -23.091 162.536 11.053 1.00 34.89 ?  140 ALA H C   1 
ATOM   8688  O  O   . ALA H  4 140 ? -22.394 163.408 10.516 1.00 35.02 ?  140 ALA H O   1 
ATOM   8689  C  CB  . ALA H  4 140 ? -22.666 162.932 13.488 1.00 37.12 ?  140 ALA H CB  1 
ATOM   8690  N  N   . GLY H  4 141 ? -23.306 161.359 10.478 1.00 37.86 ?  141 GLY H N   1 
ATOM   8691  C  CA  . GLY H  4 141 ? -22.783 161.109 9.153  1.00 34.57 ?  141 GLY H CA  1 
ATOM   8692  C  C   . GLY H  4 141 ? -21.317 160.724 9.186  1.00 35.27 ?  141 GLY H C   1 
ATOM   8693  O  O   . GLY H  4 141 ? -20.781 160.224 10.191 1.00 35.83 ?  141 GLY H O   1 
ATOM   8694  N  N   . SER H  4 142 ? -20.652 160.968 8.059  1.00 33.18 ?  142 SER H N   1 
ATOM   8695  C  CA  . SER H  4 142 ? -19.344 160.367 7.851  1.00 33.77 ?  142 SER H CA  1 
ATOM   8696  C  C   . SER H  4 142 ? -18.257 161.123 8.621  1.00 32.91 ?  142 SER H C   1 
ATOM   8697  O  O   . SER H  4 142 ? -18.491 162.169 9.228  1.00 32.91 ?  142 SER H O   1 
ATOM   8698  C  CB  . SER H  4 142 ? -19.022 160.324 6.361  1.00 34.06 ?  142 SER H CB  1 
ATOM   8699  O  OG  . SER H  4 142 ? -19.167 161.616 5.821  1.00 43.79 ?  142 SER H OG  1 
ATOM   8700  N  N   . ARG H  4 143 ? -17.049 160.576 8.578  1.00 34.01 ?  143 ARG H N   1 
ATOM   8701  C  CA  . ARG H  4 143 ? -15.925 161.083 9.351  1.00 35.35 ?  143 ARG H CA  1 
ATOM   8702  C  C   . ARG H  4 143 ? -15.042 161.936 8.445  1.00 39.19 ?  143 ARG H C   1 
ATOM   8703  O  O   . ARG H  4 143 ? -14.288 161.404 7.625  1.00 40.02 ?  143 ARG H O   1 
ATOM   8704  C  CB  . ARG H  4 143 ? -15.155 159.915 9.970  1.00 33.41 ?  143 ARG H CB  1 
ATOM   8705  C  CG  . ARG H  4 143 ? -16.086 158.954 10.706 1.00 32.80 ?  143 ARG H CG  1 
ATOM   8706  C  CD  . ARG H  4 143 ? -15.394 157.733 11.289 1.00 32.92 ?  143 ARG H CD  1 
ATOM   8707  N  NE  . ARG H  4 143 ? -16.380 156.865 11.932 1.00 36.24 ?  143 ARG H NE  1 
ATOM   8708  C  CZ  . ARG H  4 143 ? -16.106 155.960 12.864 1.00 39.31 ?  143 ARG H CZ  1 
ATOM   8709  N  NH1 . ARG H  4 143 ? -14.864 155.721 13.258 1.00 33.15 ?  143 ARG H NH1 1 
ATOM   8710  N  NH2 . ARG H  4 143 ? -17.109 155.283 13.426 1.00 39.68 ?  143 ARG H NH2 1 
ATOM   8711  N  N   . LEU H  4 144 ? -15.142 163.262 8.597  1.00 33.78 ?  144 LEU H N   1 
ATOM   8712  C  CA  . LEU H  4 144 ? -14.409 164.197 7.745  1.00 32.88 ?  144 LEU H CA  1 
ATOM   8713  C  C   . LEU H  4 144 ? -12.935 164.271 8.102  1.00 34.84 ?  144 LEU H C   1 
ATOM   8714  O  O   . LEU H  4 144 ? -12.082 164.351 7.215  1.00 32.54 ?  144 LEU H O   1 
ATOM   8715  C  CB  . LEU H  4 144 ? -15.015 165.589 7.857  1.00 30.16 ?  144 LEU H CB  1 
ATOM   8716  C  CG  . LEU H  4 144 ? -16.464 165.648 7.404  1.00 38.12 ?  144 LEU H CG  1 
ATOM   8717  C  CD1 . LEU H  4 144 ? -16.909 167.093 7.303  1.00 34.63 ?  144 LEU H CD1 1 
ATOM   8718  C  CD2 . LEU H  4 144 ? -16.623 164.902 6.071  1.00 34.94 ?  144 LEU H CD2 1 
ATOM   8719  N  N   . ALA H  4 145 ? -12.605 164.283 9.386  1.00 27.37 ?  145 ALA H N   1 
ATOM   8720  C  CA  . ALA H  4 145 ? -11.209 164.375 9.778  1.00 28.54 ?  145 ALA H CA  1 
ATOM   8721  C  C   . ALA H  4 145 ? -11.087 163.842 11.194 1.00 31.01 ?  145 ALA H C   1 
ATOM   8722  O  O   . ALA H  4 145 ? -12.041 163.903 11.979 1.00 31.10 ?  145 ALA H O   1 
ATOM   8723  C  CB  . ALA H  4 145 ? -10.712 165.826 9.684  1.00 22.31 ?  145 ALA H CB  1 
ATOM   8724  N  N   . CYS H  4 146 ? -9.913  163.314 11.515 1.00 29.92 ?  146 CYS H N   1 
ATOM   8725  C  CA  . CYS H  4 146 ? -9.696  162.752 12.836 1.00 33.50 ?  146 CYS H CA  1 
ATOM   8726  C  C   . CYS H  4 146 ? -8.212  162.779 13.135 1.00 35.63 ?  146 CYS H C   1 
ATOM   8727  O  O   . CYS H  4 146 ? -7.377  162.982 12.243 1.00 30.11 ?  146 CYS H O   1 
ATOM   8728  C  CB  . CYS H  4 146 ? -10.224 161.323 12.934 1.00 32.74 ?  146 CYS H CB  1 
ATOM   8729  S  SG  . CYS H  4 146 ? -9.392  160.220 11.797 1.00 40.27 ?  146 CYS H SG  1 
ATOM   8730  N  N   . GLY H  4 147 ? -7.898  162.565 14.409 1.00 31.82 ?  147 GLY H N   1 
ATOM   8731  C  CA  . GLY H  4 147 ? -6.527  162.384 14.842 1.00 31.03 ?  147 GLY H CA  1 
ATOM   8732  C  C   . GLY H  4 147 ? -6.497  161.732 16.207 1.00 35.34 ?  147 GLY H C   1 
ATOM   8733  O  O   . GLY H  4 147 ? -7.487  161.746 16.947 1.00 31.18 ?  147 GLY H O   1 
ATOM   8734  N  N   . VAL H  4 148 ? -5.344  161.157 16.534 1.00 30.68 ?  148 VAL H N   1 
ATOM   8735  C  CA  . VAL H  4 148 ? -5.147  160.535 17.841 1.00 37.39 ?  148 VAL H CA  1 
ATOM   8736  C  C   . VAL H  4 148 ? -4.838  161.620 18.862 1.00 34.97 ?  148 VAL H C   1 
ATOM   8737  O  O   . VAL H  4 148 ? -3.995  162.491 18.624 1.00 35.78 ?  148 VAL H O   1 
ATOM   8738  C  CB  . VAL H  4 148 ? -4.020  159.491 17.790 1.00 33.58 ?  148 VAL H CB  1 
ATOM   8739  C  CG1 . VAL H  4 148 ? -3.975  158.682 19.085 1.00 37.30 ?  148 VAL H CG1 1 
ATOM   8740  C  CG2 . VAL H  4 148 ? -4.173  158.571 16.573 1.00 41.31 ?  148 VAL H CG2 1 
ATOM   8741  N  N   . ILE H  4 149 ? -5.533  161.581 19.994 1.00 35.00 ?  149 ILE H N   1 
ATOM   8742  C  CA  . ILE H  4 149 ? -5.342  162.558 21.062 1.00 33.28 ?  149 ILE H CA  1 
ATOM   8743  C  C   . ILE H  4 149 ? -4.067  162.210 21.818 1.00 35.28 ?  149 ILE H C   1 
ATOM   8744  O  O   . ILE H  4 149 ? -3.945  161.118 22.380 1.00 41.13 ?  149 ILE H O   1 
ATOM   8745  C  CB  . ILE H  4 149 ? -6.553  162.588 22.002 1.00 40.15 ?  149 ILE H CB  1 
ATOM   8746  C  CG1 . ILE H  4 149 ? -7.801  162.988 21.229 1.00 32.60 ?  149 ILE H CG1 1 
ATOM   8747  C  CG2 . ILE H  4 149 ? -6.315  163.551 23.155 1.00 36.95 ?  149 ILE H CG2 1 
ATOM   8748  C  CD1 . ILE H  4 149 ? -9.081  162.651 21.945 1.00 35.52 ?  149 ILE H CD1 1 
ATOM   8749  N  N   . GLY H  4 150 ? -3.112  163.127 21.827 1.00 36.00 ?  150 GLY H N   1 
ATOM   8750  C  CA  . GLY H  4 150 ? -1.809  162.841 22.391 1.00 37.49 ?  150 GLY H CA  1 
ATOM   8751  C  C   . GLY H  4 150 ? -1.459  163.759 23.542 1.00 41.57 ?  150 GLY H C   1 
ATOM   8752  O  O   . GLY H  4 150 ? -2.040  164.836 23.679 1.00 37.31 ?  150 GLY H O   1 
ATOM   8753  N  N   . ILE H  4 151 ? -0.501  163.339 24.366 1.00 37.09 ?  151 ILE H N   1 
ATOM   8754  C  CA  . ILE H  4 151 ? -0.102  164.119 25.526 1.00 39.27 ?  151 ILE H CA  1 
ATOM   8755  C  C   . ILE H  4 151 ? 0.738   165.305 25.080 1.00 40.80 ?  151 ILE H C   1 
ATOM   8756  O  O   . ILE H  4 151 ? 1.680   165.156 24.293 1.00 44.16 ?  151 ILE H O   1 
ATOM   8757  C  CB  . ILE H  4 151 ? 0.667   163.234 26.522 1.00 44.84 ?  151 ILE H CB  1 
ATOM   8758  C  CG1 . ILE H  4 151 ? -0.214  162.068 26.962 1.00 48.60 ?  151 ILE H CG1 1 
ATOM   8759  C  CG2 . ILE H  4 151 ? 1.114   164.038 27.740 1.00 45.15 ?  151 ILE H CG2 1 
ATOM   8760  C  CD1 . ILE H  4 151 ? 0.557   160.870 27.463 1.00 50.21 ?  151 ILE H CD1 1 
ATOM   8761  N  N   . ALA H  4 152 ? 0.402   166.485 25.588 1.00 39.20 ?  152 ALA H N   1 
ATOM   8762  C  CA  . ALA H  4 152 ? 1.105   167.736 25.349 1.00 45.20 ?  152 ALA H CA  1 
ATOM   8763  C  C   . ALA H  4 152 ? 1.685   168.231 26.673 1.00 49.59 ?  152 ALA H C   1 
ATOM   8764  O  O   . ALA H  4 152 ? 1.448   167.643 27.728 1.00 55.53 ?  152 ALA H O   1 
ATOM   8765  C  CB  . ALA H  4 152 ? 0.160   168.778 24.742 1.00 35.50 ?  152 ALA H CB  1 
ATOM   8766  N  N   . ALA H  4 153 ? 2.432   169.330 26.633 1.00 55.25 ?  153 ALA H N   1 
ATOM   8767  C  CA  . ALA H  4 153 ? 2.924   169.913 27.895 1.00 63.52 ?  153 ALA H CA  1 
ATOM   8768  C  C   . ALA H  4 153 ? 1.998   171.003 28.454 1.00 62.54 ?  153 ALA H C   1 
ATOM   8769  O  O   . ALA H  4 153 ? 2.054   171.327 29.649 1.00 73.32 ?  153 ALA H O   1 
ATOM   8770  C  CB  . ALA H  4 153 ? 4.322   170.466 27.716 1.00 60.65 ?  153 ALA H CB  1 
ATOM   8771  N  N   . MET I  1 1   ? 28.827  202.360 34.428 1.00 59.85 ?  0   MET I N   1 
ATOM   8772  C  CA  . MET I  1 1   ? 27.803  203.191 35.066 1.00 75.15 ?  0   MET I CA  1 
ATOM   8773  C  C   . MET I  1 1   ? 28.232  203.647 36.474 1.00 76.46 ?  0   MET I C   1 
ATOM   8774  O  O   . MET I  1 1   ? 28.059  202.915 37.460 1.00 75.18 ?  0   MET I O   1 
ATOM   8775  C  CB  . MET I  1 1   ? 26.465  202.434 35.139 1.00 65.11 ?  0   MET I CB  1 
ATOM   8776  N  N   . ALA I  1 2   ? 28.784  204.865 36.567 1.00 67.90 ?  1   ALA I N   1 
ATOM   8777  C  CA  . ALA I  1 2   ? 29.300  205.402 37.835 1.00 66.50 ?  1   ALA I CA  1 
ATOM   8778  C  C   . ALA I  1 2   ? 28.917  206.882 37.941 1.00 56.91 ?  1   ALA I C   1 
ATOM   8779  O  O   . ALA I  1 2   ? 29.643  207.756 37.461 1.00 62.98 ?  1   ALA I O   1 
ATOM   8780  C  CB  . ALA I  1 2   ? 30.808  205.197 37.931 1.00 54.35 ?  1   ALA I CB  1 
ATOM   8781  N  N   . THR I  1 3   ? 27.781  207.162 38.588 1.00 55.62 ?  2   THR I N   1 
ATOM   8782  C  CA  . THR I  1 3   ? 27.301  208.528 38.745 1.00 47.01 ?  2   THR I CA  1 
ATOM   8783  C  C   . THR I  1 3   ? 27.385  209.066 40.172 1.00 51.01 ?  2   THR I C   1 
ATOM   8784  O  O   . THR I  1 3   ? 27.277  210.287 40.355 1.00 48.36 ?  2   THR I O   1 
ATOM   8785  C  CB  . THR I  1 3   ? 25.847  208.654 38.251 1.00 50.90 ?  2   THR I CB  1 
ATOM   8786  O  OG1 . THR I  1 3   ? 24.964  207.951 39.133 1.00 58.30 ?  2   THR I OG1 1 
ATOM   8787  C  CG2 . THR I  1 3   ? 25.694  208.124 36.830 1.00 50.64 ?  2   THR I CG2 1 
ATOM   8788  N  N   . LYS I  1 4   ? 27.574  208.212 41.183 1.00 42.32 ?  3   LYS I N   1 
ATOM   8789  C  CA  . LYS I  1 4   ? 27.720  208.673 42.560 1.00 42.69 ?  3   LYS I CA  1 
ATOM   8790  C  C   . LYS I  1 4   ? 28.868  207.941 43.239 1.00 43.18 ?  3   LYS I C   1 
ATOM   8791  O  O   . LYS I  1 4   ? 29.043  206.730 43.071 1.00 44.69 ?  3   LYS I O   1 
ATOM   8792  C  CB  . LYS I  1 4   ? 26.430  208.473 43.389 1.00 44.98 ?  3   LYS I CB  1 
ATOM   8793  C  CG  . LYS I  1 4   ? 25.183  209.164 42.841 1.00 49.54 ?  3   LYS I CG  1 
ATOM   8794  C  CD  . LYS I  1 4   ? 23.935  208.292 43.038 1.00 60.89 ?  3   LYS I CD  1 
ATOM   8795  C  CE  . LYS I  1 4   ? 22.953  208.389 41.842 1.00 67.79 ?  3   LYS I CE  1 
ATOM   8796  N  NZ  . LYS I  1 4   ? 22.285  207.071 41.506 1.00 66.08 ?  3   LYS I NZ  1 
ATOM   8797  N  N   . ALA I  1 5   ? 29.638  208.683 44.019 1.00 34.36 ?  4   ALA I N   1 
ATOM   8798  C  CA  . ALA I  1 5   ? 30.750  208.128 44.763 1.00 36.90 ?  4   ALA I CA  1 
ATOM   8799  C  C   . ALA I  1 5   ? 30.759  208.777 46.134 1.00 37.15 ?  4   ALA I C   1 
ATOM   8800  O  O   . ALA I  1 5   ? 30.088  209.785 46.366 1.00 39.52 ?  4   ALA I O   1 
ATOM   8801  C  CB  . ALA I  1 5   ? 32.088  208.358 44.047 1.00 38.39 ?  4   ALA I CB  1 
ATOM   8802  N  N   . VAL I  1 6   ? 31.529  208.200 47.051 1.00 34.03 ?  5   VAL I N   1 
ATOM   8803  C  CA  . VAL I  1 6   ? 31.543  208.687 48.423 1.00 37.23 ?  5   VAL I CA  1 
ATOM   8804  C  C   . VAL I  1 6   ? 32.886  208.350 49.044 1.00 36.46 ?  5   VAL I C   1 
ATOM   8805  O  O   . VAL I  1 6   ? 33.572  207.413 48.625 1.00 41.59 ?  5   VAL I O   1 
ATOM   8806  C  CB  . VAL I  1 6   ? 30.372  208.087 49.237 1.00 40.77 ?  5   VAL I CB  1 
ATOM   8807  C  CG1 . VAL I  1 6   ? 30.582  206.599 49.473 1.00 39.21 ?  5   VAL I CG1 1 
ATOM   8808  C  CG2 . VAL I  1 6   ? 30.160  208.841 50.548 1.00 36.92 ?  5   VAL I CG2 1 
ATOM   8809  N  N   . CYS I  1 7   ? 33.255  209.114 50.065 1.00 33.27 ?  6   CYS I N   1 
ATOM   8810  C  CA  . CYS I  1 7   ? 34.540  208.905 50.701 1.00 37.82 ?  6   CYS I CA  1 
ATOM   8811  C  C   . CYS I  1 7   ? 34.428  209.304 52.168 1.00 40.71 ?  6   CYS I C   1 
ATOM   8812  O  O   . CYS I  1 7   ? 33.980  210.413 52.481 1.00 37.75 ?  6   CYS I O   1 
ATOM   8813  C  CB  . CYS I  1 7   ? 35.638  209.703 49.981 1.00 36.83 ?  6   CYS I CB  1 
ATOM   8814  S  SG  . CYS I  1 7   ? 37.154  209.942 50.942 1.00 44.63 ?  6   CYS I SG  1 
ATOM   8815  N  N   . VAL I  1 8   ? 34.807  208.385 53.055 1.00 32.50 ?  7   VAL I N   1 
ATOM   8816  C  CA  . VAL I  1 8   ? 34.867  208.647 54.491 1.00 37.12 ?  7   VAL I CA  1 
ATOM   8817  C  C   . VAL I  1 8   ? 36.296  209.035 54.838 1.00 43.24 ?  7   VAL I C   1 
ATOM   8818  O  O   . VAL I  1 8   ? 37.223  208.244 54.644 1.00 45.95 ?  7   VAL I O   1 
ATOM   8819  C  CB  . VAL I  1 8   ? 34.426  207.420 55.300 1.00 38.18 ?  7   VAL I CB  1 
ATOM   8820  C  CG1 . VAL I  1 8   ? 34.498  207.715 56.785 1.00 33.27 ?  7   VAL I CG1 1 
ATOM   8821  C  CG2 . VAL I  1 8   ? 33.023  207.014 54.912 1.00 36.52 ?  7   VAL I CG2 1 
ATOM   8822  N  N   . LEU I  1 9   ? 36.480  210.253 55.341 1.00 37.14 ?  8   LEU I N   1 
ATOM   8823  C  CA  . LEU I  1 9   ? 37.804  210.750 55.682 1.00 34.43 ?  8   LEU I CA  1 
ATOM   8824  C  C   . LEU I  1 9   ? 38.086  210.458 57.147 1.00 39.47 ?  8   LEU I C   1 
ATOM   8825  O  O   . LEU I  1 9   ? 37.293  210.818 58.026 1.00 35.34 ?  8   LEU I O   1 
ATOM   8826  C  CB  . LEU I  1 9   ? 37.909  212.255 55.414 1.00 35.93 ?  8   LEU I CB  1 
ATOM   8827  C  CG  . LEU I  1 9   ? 37.756  212.719 53.964 1.00 41.31 ?  8   LEU I CG  1 
ATOM   8828  C  CD1 . LEU I  1 9   ? 37.829  214.234 53.884 1.00 45.09 ?  8   LEU I CD1 1 
ATOM   8829  C  CD2 . LEU I  1 9   ? 38.830  212.132 53.110 1.00 45.43 ?  8   LEU I CD2 1 
ATOM   8830  N  N   . LYS I  1 10  ? 39.211  209.796 57.407 1.00 39.56 ?  9   LYS I N   1 
ATOM   8831  C  CA  . LYS I  1 10  ? 39.666  209.536 58.765 1.00 41.74 ?  9   LYS I CA  1 
ATOM   8832  C  C   . LYS I  1 10  ? 41.170  209.759 58.812 1.00 38.94 ?  9   LYS I C   1 
ATOM   8833  O  O   . LYS I  1 10  ? 41.856  209.711 57.785 1.00 42.76 ?  9   LYS I O   1 
ATOM   8834  C  CB  . LYS I  1 10  ? 39.336  208.101 59.226 1.00 43.81 ?  9   LYS I CB  1 
ATOM   8835  C  CG  . LYS I  1 10  ? 37.858  207.719 59.189 1.00 45.45 ?  9   LYS I CG  1 
ATOM   8836  C  CD  . LYS I  1 10  ? 37.103  208.209 60.410 0.00 39.16 ?  9   LYS I CD  1 
ATOM   8837  C  CE  . LYS I  1 10  ? 35.796  207.447 60.587 0.00 37.84 ?  9   LYS I CE  1 
ATOM   8838  N  NZ  . LYS I  1 10  ? 35.824  206.118 59.912 0.00 37.75 ?  9   LYS I NZ  1 
ATOM   8839  N  N   . GLY I  1 11  ? 41.683  209.980 60.019 1.00 45.85 ?  10  GLY I N   1 
ATOM   8840  C  CA  . GLY I  1 11  ? 43.118  210.101 60.197 1.00 47.65 ?  10  GLY I CA  1 
ATOM   8841  C  C   . GLY I  1 11  ? 43.527  209.759 61.616 1.00 54.62 ?  10  GLY I C   1 
ATOM   8842  O  O   . GLY I  1 11  ? 42.718  209.318 62.436 1.00 49.12 ?  10  GLY I O   1 
ATOM   8843  N  N   . ASP I  1 12  ? 44.812  209.972 61.900 1.00 50.16 ?  11  ASP I N   1 
ATOM   8844  C  CA  . ASP I  1 12  ? 45.322  209.673 63.230 1.00 53.95 ?  11  ASP I CA  1 
ATOM   8845  C  C   . ASP I  1 12  ? 44.822  210.661 64.272 1.00 55.35 ?  11  ASP I C   1 
ATOM   8846  O  O   . ASP I  1 12  ? 44.745  210.308 65.452 1.00 61.46 ?  11  ASP I O   1 
ATOM   8847  C  CB  . ASP I  1 12  ? 46.851  209.638 63.209 1.00 56.62 ?  11  ASP I CB  1 
ATOM   8848  C  CG  . ASP I  1 12  ? 47.392  208.245 62.933 1.00 69.14 ?  11  ASP I CG  1 
ATOM   8849  O  OD1 . ASP I  1 12  ? 47.597  207.899 61.745 1.00 78.68 ?  11  ASP I OD1 1 
ATOM   8850  O  OD2 . ASP I  1 12  ? 47.600  207.490 63.913 1.00 76.93 ?  11  ASP I OD2 1 
ATOM   8851  N  N   . GLY I  1 13  ? 44.448  211.867 63.863 1.00 51.09 ?  12  GLY I N   1 
ATOM   8852  C  CA  . GLY I  1 13  ? 43.928  212.848 64.781 1.00 44.44 ?  12  GLY I CA  1 
ATOM   8853  C  C   . GLY I  1 13  ? 42.413  212.868 64.795 1.00 44.56 ?  12  GLY I C   1 
ATOM   8854  O  O   . GLY I  1 13  ? 41.748  211.861 64.524 1.00 52.34 ?  12  GLY I O   1 
ATOM   8855  N  N   . PRO I  1 14  ? 41.838  214.025 65.118 1.00 48.04 ?  13  PRO I N   1 
ATOM   8856  C  CA  . PRO I  1 14  ? 40.379  214.147 65.239 1.00 45.66 ?  13  PRO I CA  1 
ATOM   8857  C  C   . PRO I  1 14  ? 39.648  214.584 63.978 1.00 44.17 ?  13  PRO I C   1 
ATOM   8858  O  O   . PRO I  1 14  ? 38.420  214.736 64.027 1.00 42.63 ?  13  PRO I O   1 
ATOM   8859  C  CB  . PRO I  1 14  ? 40.238  215.214 66.330 1.00 43.37 ?  13  PRO I CB  1 
ATOM   8860  C  CG  . PRO I  1 14  ? 41.434  216.114 66.128 1.00 40.00 ?  13  PRO I CG  1 
ATOM   8861  C  CD  . PRO I  1 14  ? 42.532  215.273 65.486 1.00 47.44 ?  13  PRO I CD  1 
ATOM   8862  N  N   . VAL I  1 15  ? 40.357  214.784 62.865 1.00 43.41 ?  14  VAL I N   1 
ATOM   8863  C  CA  . VAL I  1 15  ? 39.705  215.179 61.620 1.00 43.10 ?  14  VAL I CA  1 
ATOM   8864  C  C   . VAL I  1 15  ? 38.944  213.994 61.044 1.00 43.72 ?  14  VAL I C   1 
ATOM   8865  O  O   . VAL I  1 15  ? 39.491  212.893 60.895 1.00 45.06 ?  14  VAL I O   1 
ATOM   8866  C  CB  . VAL I  1 15  ? 40.734  215.705 60.614 1.00 39.69 ?  14  VAL I CB  1 
ATOM   8867  C  CG1 . VAL I  1 15  ? 40.038  216.055 59.308 1.00 36.58 ?  14  VAL I CG1 1 
ATOM   8868  C  CG2 . VAL I  1 15  ? 41.470  216.906 61.191 1.00 38.08 ?  14  VAL I CG2 1 
ATOM   8869  N  N   . GLN I  1 16  ? 37.676  214.211 60.708 1.00 37.76 ?  15  GLN I N   1 
ATOM   8870  C  CA  . GLN I  1 16  ? 36.919  213.184 60.003 1.00 37.71 ?  15  GLN I CA  1 
ATOM   8871  C  C   . GLN I  1 16  ? 35.793  213.845 59.229 1.00 36.45 ?  15  GLN I C   1 
ATOM   8872  O  O   . GLN I  1 16  ? 35.352  214.947 59.569 1.00 35.17 ?  15  GLN I O   1 
ATOM   8873  C  CB  . GLN I  1 16  ? 36.355  212.160 60.972 1.00 37.86 ?  15  GLN I CB  1 
ATOM   8874  C  CG  . GLN I  1 16  ? 35.748  212.820 62.150 1.00 40.91 ?  15  GLN I CG  1 
ATOM   8875  C  CD  . GLN I  1 16  ? 35.185  211.823 63.119 1.00 53.27 ?  15  GLN I CD  1 
ATOM   8876  O  OE1 . GLN I  1 16  ? 35.791  211.528 64.151 1.00 51.92 ?  15  GLN I OE1 1 
ATOM   8877  N  NE2 . GLN I  1 16  ? 34.016  211.282 62.791 1.00 56.31 ?  15  GLN I NE2 1 
ATOM   8878  N  N   . GLY I  1 17  ? 35.313  213.145 58.208 1.00 36.77 ?  16  GLY I N   1 
ATOM   8879  C  CA  . GLY I  1 17  ? 34.187  213.649 57.448 1.00 36.27 ?  16  GLY I CA  1 
ATOM   8880  C  C   . GLY I  1 17  ? 33.744  212.658 56.394 1.00 40.50 ?  16  GLY I C   1 
ATOM   8881  O  O   . GLY I  1 17  ? 34.339  211.591 56.204 1.00 36.54 ?  16  GLY I O   1 
ATOM   8882  N  N   . ILE I  1 18  ? 32.674  213.042 55.706 1.00 32.03 ?  17  ILE I N   1 
ATOM   8883  C  CA  . ILE I  1 18  ? 32.099  212.291 54.605 1.00 31.79 ?  17  ILE I CA  1 
ATOM   8884  C  C   . ILE I  1 18  ? 31.951  213.249 53.440 1.00 38.36 ?  17  ILE I C   1 
ATOM   8885  O  O   . ILE I  1 18  ? 31.391  214.341 53.599 1.00 38.29 ?  17  ILE I O   1 
ATOM   8886  C  CB  . ILE I  1 18  ? 30.733  211.688 54.980 1.00 30.61 ?  17  ILE I CB  1 
ATOM   8887  C  CG1 . ILE I  1 18  ? 30.927  210.588 56.017 1.00 34.00 ?  17  ILE I CG1 1 
ATOM   8888  C  CG2 . ILE I  1 18  ? 30.020  211.183 53.737 1.00 31.36 ?  17  ILE I CG2 1 
ATOM   8889  C  CD1 . ILE I  1 18  ? 29.692  210.243 56.785 1.00 36.14 ?  17  ILE I CD1 1 
ATOM   8890  N  N   . ILE I  1 19  ? 32.461  212.856 52.282 1.00 33.10 ?  18  ILE I N   1 
ATOM   8891  C  CA  . ILE I  1 19  ? 32.366  213.659 51.075 1.00 34.56 ?  18  ILE I CA  1 
ATOM   8892  C  C   . ILE I  1 19  ? 31.677  212.827 50.008 1.00 39.89 ?  18  ILE I C   1 
ATOM   8893  O  O   . ILE I  1 19  ? 32.079  211.685 49.750 1.00 37.14 ?  18  ILE I O   1 
ATOM   8894  C  CB  . ILE I  1 19  ? 33.750  214.131 50.590 1.00 32.27 ?  18  ILE I CB  1 
ATOM   8895  C  CG1 . ILE I  1 19  ? 34.446  214.948 51.671 1.00 33.30 ?  18  ILE I CG1 1 
ATOM   8896  C  CG2 . ILE I  1 19  ? 33.599  214.905 49.299 1.00 34.40 ?  18  ILE I CG2 1 
ATOM   8897  C  CD1 . ILE I  1 19  ? 33.812  216.316 51.918 1.00 34.22 ?  18  ILE I CD1 1 
ATOM   8898  N  N   . ASN I  1 20  ? 30.643  213.398 49.399 1.00 32.72 ?  19  ASN I N   1 
ATOM   8899  C  CA  . ASN I  1 20  ? 29.889  212.786 48.315 1.00 36.58 ?  19  ASN I CA  1 
ATOM   8900  C  C   . ASN I  1 20  ? 30.291  213.377 46.973 1.00 38.35 ?  19  ASN I C   1 
ATOM   8901  O  O   . ASN I  1 20  ? 30.689  214.545 46.885 1.00 36.02 ?  19  ASN I O   1 
ATOM   8902  C  CB  . ASN I  1 20  ? 28.393  212.989 48.528 1.00 32.40 ?  19  ASN I CB  1 
ATOM   8903  C  CG  . ASN I  1 20  ? 27.960  212.544 49.881 1.00 40.79 ?  19  ASN I CG  1 
ATOM   8904  O  OD1 . ASN I  1 20  ? 27.714  211.358 50.089 1.00 41.22 ?  19  ASN I OD1 1 
ATOM   8905  N  ND2 . ASN I  1 20  ? 27.881  213.483 50.828 1.00 38.00 ?  19  ASN I ND2 1 
ATOM   8906  N  N   . PHE I  1 21  ? 30.193  212.552 45.929 1.00 35.20 ?  20  PHE I N   1 
ATOM   8907  C  CA  . PHE I  1 21  ? 30.463  212.961 44.551 1.00 40.26 ?  20  PHE I CA  1 
ATOM   8908  C  C   . PHE I  1 21  ? 29.269  212.562 43.703 1.00 41.89 ?  20  PHE I C   1 
ATOM   8909  O  O   . PHE I  1 21  ? 28.656  211.517 43.938 1.00 40.59 ?  20  PHE I O   1 
ATOM   8910  C  CB  . PHE I  1 21  ? 31.731  212.307 43.955 1.00 34.23 ?  20  PHE I CB  1 
ATOM   8911  C  CG  . PHE I  1 21  ? 32.978  212.533 44.756 1.00 36.36 ?  20  PHE I CG  1 
ATOM   8912  C  CD1 . PHE I  1 21  ? 33.175  211.884 45.964 1.00 38.87 ?  20  PHE I CD1 1 
ATOM   8913  C  CD2 . PHE I  1 21  ? 33.962  213.388 44.290 1.00 34.70 ?  20  PHE I CD2 1 
ATOM   8914  C  CE1 . PHE I  1 21  ? 34.322  212.100 46.703 1.00 39.35 ?  20  PHE I CE1 1 
ATOM   8915  C  CE2 . PHE I  1 21  ? 35.108  213.605 45.018 1.00 37.77 ?  20  PHE I CE2 1 
ATOM   8916  C  CZ  . PHE I  1 21  ? 35.292  212.961 46.229 1.00 35.38 ?  20  PHE I CZ  1 
ATOM   8917  N  N   . GLU I  1 22  ? 28.931  213.388 42.724 1.00 39.20 ?  21  GLU I N   1 
ATOM   8918  C  CA  . GLU I  1 22  ? 27.828  213.031 41.848 1.00 41.46 ?  21  GLU I CA  1 
ATOM   8919  C  C   . GLU I  1 22  ? 28.118  213.573 40.456 1.00 50.17 ?  21  GLU I C   1 
ATOM   8920  O  O   . GLU I  1 22  ? 28.561  214.718 40.308 1.00 45.60 ?  21  GLU I O   1 
ATOM   8921  C  CB  . GLU I  1 22  ? 26.504  213.573 42.387 1.00 47.44 ?  21  GLU I CB  1 
ATOM   8922  C  CG  . GLU I  1 22  ? 25.362  213.518 41.391 1.00 56.06 ?  21  GLU I CG  1 
ATOM   8923  C  CD  . GLU I  1 22  ? 24.025  213.207 42.047 1.00 61.60 ?  21  GLU I CD  1 
ATOM   8924  O  OE1 . GLU I  1 22  ? 24.000  212.571 43.127 1.00 68.70 ?  21  GLU I OE1 1 
ATOM   8925  O  OE2 . GLU I  1 22  ? 22.996  213.645 41.489 1.00 69.21 ?  21  GLU I OE2 1 
ATOM   8926  N  N   . GLN I  1 23  ? 27.893  212.741 39.443 1.00 41.81 ?  22  GLN I N   1 
ATOM   8927  C  CA  . GLN I  1 23  ? 28.172  213.120 38.062 1.00 51.92 ?  22  GLN I CA  1 
ATOM   8928  C  C   . GLN I  1 23  ? 27.057  212.557 37.192 1.00 53.15 ?  22  GLN I C   1 
ATOM   8929  O  O   . GLN I  1 23  ? 26.956  211.343 36.996 1.00 53.87 ?  22  GLN I O   1 
ATOM   8930  C  CB  . GLN I  1 23  ? 29.540  212.624 37.605 1.00 49.43 ?  22  GLN I CB  1 
ATOM   8931  C  CG  . GLN I  1 23  ? 29.855  213.011 36.172 1.00 50.82 ?  22  GLN I CG  1 
ATOM   8932  C  CD  . GLN I  1 23  ? 31.248  212.602 35.765 1.00 54.57 ?  22  GLN I CD  1 
ATOM   8933  O  OE1 . GLN I  1 23  ? 31.734  211.543 36.177 1.00 55.16 ?  22  GLN I OE1 1 
ATOM   8934  N  NE2 . GLN I  1 23  ? 31.892  213.415 34.933 1.00 48.61 ?  22  GLN I NE2 1 
ATOM   8935  N  N   . LYS I  1 24  ? 26.218  213.449 36.687 1.00 55.02 ?  23  LYS I N   1 
ATOM   8936  C  CA  . LYS I  1 24  ? 25.000  213.063 35.993 1.00 54.17 ?  23  LYS I CA  1 
ATOM   8937  C  C   . LYS I  1 24  ? 25.308  212.722 34.542 1.00 59.74 ?  23  LYS I C   1 
ATOM   8938  O  O   . LYS I  1 24  ? 24.884  211.679 34.033 1.00 64.41 ?  23  LYS I O   1 
ATOM   8939  C  CB  . LYS I  1 24  ? 23.957  214.195 36.083 1.00 55.80 ?  23  LYS I CB  1 
ATOM   8940  C  CG  . LYS I  1 24  ? 23.609  214.798 37.491 1.00 61.30 ?  23  LYS I CG  1 
ATOM   8941  C  CD  . LYS I  1 24  ? 24.826  215.300 38.323 1.00 62.38 ?  23  LYS I CD  1 
ATOM   8942  C  CE  . LYS I  1 24  ? 25.589  216.439 37.634 1.00 62.96 ?  23  LYS I CE  1 
ATOM   8943  N  NZ  . LYS I  1 24  ? 26.677  217.049 38.471 1.00 58.71 ?  23  LYS I NZ  1 
ATOM   8944  N  N   . GLU I  1 25  ? 26.054  213.589 33.867 1.00 66.83 ?  24  GLU I N   1 
ATOM   8945  C  CA  . GLU I  1 25  ? 26.457  213.344 32.494 1.00 63.24 ?  24  GLU I CA  1 
ATOM   8946  C  C   . GLU I  1 25  ? 27.819  212.676 32.482 1.00 59.17 ?  24  GLU I C   1 
ATOM   8947  O  O   . GLU I  1 25  ? 28.680  212.991 33.304 1.00 58.12 ?  24  GLU I O   1 
ATOM   8948  C  CB  . GLU I  1 25  ? 26.502  214.643 31.684 1.00 65.89 ?  24  GLU I CB  1 
ATOM   8949  C  CG  . GLU I  1 25  ? 25.143  215.329 31.486 1.00 75.06 ?  24  GLU I CG  1 
ATOM   8950  C  CD  . GLU I  1 25  ? 23.948  214.371 31.480 1.00 82.99 ?  24  GLU I CD  1 
ATOM   8951  O  OE1 . GLU I  1 25  ? 22.924  214.720 32.118 1.00 89.69 ?  24  GLU I OE1 1 
ATOM   8952  O  OE2 . GLU I  1 25  ? 24.004  213.312 30.804 1.00 75.15 ?  24  GLU I OE2 1 
ATOM   8953  N  N   . SER I  1 26  ? 28.002  211.762 31.525 1.00 64.12 ?  25  SER I N   1 
ATOM   8954  C  CA  . SER I  1 26  ? 29.194  210.923 31.471 1.00 60.34 ?  25  SER I CA  1 
ATOM   8955  C  C   . SER I  1 26  ? 30.479  211.739 31.577 1.00 62.84 ?  25  SER I C   1 
ATOM   8956  O  O   . SER I  1 26  ? 31.440  211.320 32.234 1.00 68.83 ?  25  SER I O   1 
ATOM   8957  C  CB  . SER I  1 26  ? 29.181  210.110 30.176 1.00 69.22 ?  25  SER I CB  1 
ATOM   8958  O  OG  . SER I  1 26  ? 29.807  208.850 30.354 1.00 82.02 ?  25  SER I OG  1 
ATOM   8959  N  N   . ASN I  1 27  ? 30.520  212.905 30.939 1.00 56.73 ?  26  ASN I N   1 
ATOM   8960  C  CA  . ASN I  1 27  ? 31.709  213.743 30.968 1.00 62.70 ?  26  ASN I CA  1 
ATOM   8961  C  C   . ASN I  1 27  ? 31.427  215.131 31.529 1.00 69.18 ?  26  ASN I C   1 
ATOM   8962  O  O   . ASN I  1 27  ? 32.278  216.026 31.403 1.00 74.59 ?  26  ASN I O   1 
ATOM   8963  C  CB  . ASN I  1 27  ? 32.312  213.847 29.563 1.00 67.76 ?  26  ASN I CB  1 
ATOM   8964  C  CG  . ASN I  1 27  ? 33.240  212.688 29.241 1.00 73.83 ?  26  ASN I CG  1 
ATOM   8965  O  OD1 . ASN I  1 27  ? 33.048  211.980 28.250 1.00 75.32 ?  26  ASN I OD1 1 
ATOM   8966  N  ND2 . ASN I  1 27  ? 34.255  212.487 30.082 1.00 74.60 ?  26  ASN I ND2 1 
ATOM   8967  N  N   . GLY I  1 28  ? 30.263  215.334 32.150 1.00 65.27 ?  27  GLY I N   1 
ATOM   8968  C  CA  . GLY I  1 28  ? 29.918  216.608 32.739 1.00 56.35 ?  27  GLY I CA  1 
ATOM   8969  C  C   . GLY I  1 28  ? 30.647  216.871 34.045 1.00 54.13 ?  27  GLY I C   1 
ATOM   8970  O  O   . GLY I  1 28  ? 31.535  216.116 34.458 1.00 56.29 ?  27  GLY I O   1 
ATOM   8971  N  N   . PRO I  1 29  ? 30.285  217.955 34.720 1.00 53.24 ?  28  PRO I N   1 
ATOM   8972  C  CA  . PRO I  1 29  ? 30.968  218.313 35.963 1.00 50.77 ?  28  PRO I CA  1 
ATOM   8973  C  C   . PRO I  1 29  ? 30.551  217.400 37.106 1.00 48.91 ?  28  PRO I C   1 
ATOM   8974  O  O   . PRO I  1 29  ? 29.475  216.795 37.101 1.00 45.23 ?  28  PRO I O   1 
ATOM   8975  C  CB  . PRO I  1 29  ? 30.492  219.745 36.217 1.00 48.36 ?  28  PRO I CB  1 
ATOM   8976  C  CG  . PRO I  1 29  ? 29.099  219.743 35.678 1.00 49.99 ?  28  PRO I CG  1 
ATOM   8977  C  CD  . PRO I  1 29  ? 29.143  218.847 34.450 1.00 50.97 ?  28  PRO I CD  1 
ATOM   8978  N  N   . VAL I  1 30  ? 31.422  217.334 38.109 1.00 46.78 ?  29  VAL I N   1 
ATOM   8979  C  CA  . VAL I  1 30  ? 31.203  216.510 39.293 1.00 47.27 ?  29  VAL I CA  1 
ATOM   8980  C  C   . VAL I  1 30  ? 30.901  217.431 40.469 1.00 42.44 ?  29  VAL I C   1 
ATOM   8981  O  O   . VAL I  1 30  ? 31.704  218.310 40.804 1.00 43.67 ?  29  VAL I O   1 
ATOM   8982  C  CB  . VAL I  1 30  ? 32.414  215.610 39.587 1.00 46.09 ?  29  VAL I CB  1 
ATOM   8983  C  CG1 . VAL I  1 30  ? 32.194  214.827 40.884 1.00 48.01 ?  29  VAL I CG1 1 
ATOM   8984  C  CG2 . VAL I  1 30  ? 32.665  214.667 38.423 1.00 45.26 ?  29  VAL I CG2 1 
ATOM   8985  N  N   . LYS I  1 31  ? 29.736  217.239 41.083 1.00 42.77 ?  30  LYS I N   1 
ATOM   8986  C  CA  . LYS I  1 31  ? 29.387  217.936 42.313 1.00 44.89 ?  30  LYS I CA  1 
ATOM   8987  C  C   . LYS I  1 31  ? 30.060  217.226 43.489 1.00 40.16 ?  30  LYS I C   1 
ATOM   8988  O  O   . LYS I  1 31  ? 29.983  216.000 43.608 1.00 39.85 ?  30  LYS I O   1 
ATOM   8989  C  CB  . LYS I  1 31  ? 27.859  217.973 42.479 1.00 45.16 ?  30  LYS I CB  1 
ATOM   8990  C  CG  . LYS I  1 31  ? 27.310  218.623 43.778 1.00 55.26 ?  30  LYS I CG  1 
ATOM   8991  C  CD  . LYS I  1 31  ? 27.657  220.137 43.898 1.00 57.86 ?  30  LYS I CD  1 
ATOM   8992  C  CE  . LYS I  1 31  ? 26.673  220.949 44.789 1.00 61.28 ?  30  LYS I CE  1 
ATOM   8993  N  NZ  . LYS I  1 31  ? 26.096  220.195 45.970 1.00 61.23 ?  30  LYS I NZ  1 
ATOM   8994  N  N   . VAL I  1 32  ? 30.753  217.994 44.330 1.00 40.67 ?  31  VAL I N   1 
ATOM   8995  C  CA  . VAL I  1 32  ? 31.482  217.480 45.492 1.00 38.62 ?  31  VAL I CA  1 
ATOM   8996  C  C   . VAL I  1 32  ? 30.944  218.222 46.702 1.00 42.03 ?  31  VAL I C   1 
ATOM   8997  O  O   . VAL I  1 32  ? 31.090  219.446 46.802 1.00 42.02 ?  31  VAL I O   1 
ATOM   8998  C  CB  . VAL I  1 32  ? 32.998  217.681 45.362 1.00 38.72 ?  31  VAL I CB  1 
ATOM   8999  C  CG1 . VAL I  1 32  ? 33.724  216.986 46.477 1.00 37.21 ?  31  VAL I CG1 1 
ATOM   9000  C  CG2 . VAL I  1 32  ? 33.483  217.181 44.022 1.00 35.23 ?  31  VAL I CG2 1 
ATOM   9001  N  N   . TRP I  1 33  ? 30.309  217.498 47.615 1.00 34.07 ?  32  TRP I N   1 
ATOM   9002  C  CA  . TRP I  1 33  ? 29.759  218.161 48.784 1.00 37.74 ?  32  TRP I CA  1 
ATOM   9003  C  C   . TRP I  1 33  ? 29.801  217.225 49.980 1.00 39.85 ?  32  TRP I C   1 
ATOM   9004  O  O   . TRP I  1 33  ? 29.721  216.000 49.847 1.00 38.15 ?  32  TRP I O   1 
ATOM   9005  C  CB  . TRP I  1 33  ? 28.319  218.634 48.552 1.00 35.98 ?  32  TRP I CB  1 
ATOM   9006  C  CG  . TRP I  1 33  ? 27.313  217.534 48.687 1.00 33.15 ?  32  TRP I CG  1 
ATOM   9007  C  CD1 . TRP I  1 33  ? 26.529  217.277 49.764 1.00 37.81 ?  32  TRP I CD1 1 
ATOM   9008  C  CD2 . TRP I  1 33  ? 26.987  216.548 47.707 1.00 34.57 ?  32  TRP I CD2 1 
ATOM   9009  N  NE1 . TRP I  1 33  ? 25.732  216.193 49.521 1.00 36.79 ?  32  TRP I NE1 1 
ATOM   9010  C  CE2 . TRP I  1 33  ? 25.995  215.727 48.260 1.00 34.37 ?  32  TRP I CE2 1 
ATOM   9011  C  CE3 . TRP I  1 33  ? 27.444  216.279 46.414 1.00 39.97 ?  32  TRP I CE3 1 
ATOM   9012  C  CZ2 . TRP I  1 33  ? 25.442  214.658 47.568 1.00 43.23 ?  32  TRP I CZ2 1 
ATOM   9013  C  CZ3 . TRP I  1 33  ? 26.896  215.209 45.722 1.00 45.23 ?  32  TRP I CZ3 1 
ATOM   9014  C  CH2 . TRP I  1 33  ? 25.905  214.414 46.299 1.00 43.62 ?  32  TRP I CH2 1 
ATOM   9015  N  N   . GLY I  1 34  ? 29.920  217.833 51.149 1.00 37.95 ?  33  GLY I N   1 
ATOM   9016  C  CA  . GLY I  1 34  ? 29.908  217.087 52.388 1.00 34.53 ?  33  GLY I CA  1 
ATOM   9017  C  C   . GLY I  1 34  ? 30.407  217.975 53.499 1.00 38.54 ?  33  GLY I C   1 
ATOM   9018  O  O   . GLY I  1 34  ? 30.402  219.200 53.381 1.00 37.75 ?  33  GLY I O   1 
ATOM   9019  N  N   . SER I  1 35  ? 30.863  217.336 54.569 1.00 34.70 ?  34  SER I N   1 
ATOM   9020  C  CA  . SER I  1 35  ? 31.323  218.062 55.740 1.00 35.16 ?  34  SER I CA  1 
ATOM   9021  C  C   . SER I  1 35  ? 32.541  217.365 56.332 1.00 37.44 ?  34  SER I C   1 
ATOM   9022  O  O   . SER I  1 35  ? 32.691  216.144 56.220 1.00 34.91 ?  34  SER I O   1 
ATOM   9023  C  CB  . SER I  1 35  ? 30.206  218.176 56.776 1.00 41.32 ?  34  SER I CB  1 
ATOM   9024  O  OG  . SER I  1 35  ? 30.548  219.104 57.782 1.00 46.20 ?  34  SER I OG  1 
ATOM   9025  N  N   . ILE I  1 36  ? 33.424  218.163 56.935 1.00 35.90 ?  35  ILE I N   1 
ATOM   9026  C  CA  . ILE I  1 36  ? 34.625  217.686 57.619 1.00 38.06 ?  35  ILE I CA  1 
ATOM   9027  C  C   . ILE I  1 36  ? 34.739  218.435 58.936 1.00 37.56 ?  35  ILE I C   1 
ATOM   9028  O  O   . ILE I  1 36  ? 34.684  219.669 58.957 1.00 38.96 ?  35  ILE I O   1 
ATOM   9029  C  CB  . ILE I  1 36  ? 35.909  217.906 56.788 1.00 36.65 ?  35  ILE I CB  1 
ATOM   9030  C  CG1 . ILE I  1 36  ? 35.790  217.287 55.402 1.00 30.26 ?  35  ILE I CG1 1 
ATOM   9031  C  CG2 . ILE I  1 36  ? 37.111  217.302 57.491 1.00 34.37 ?  35  ILE I CG2 1 
ATOM   9032  C  CD1 . ILE I  1 36  ? 36.954  217.643 54.504 1.00 33.69 ?  35  ILE I CD1 1 
ATOM   9033  N  N   . LYS I  1 37  ? 34.910  217.708 60.031 1.00 34.99 ?  36  LYS I N   1 
ATOM   9034  C  CA  . LYS I  1 37  ? 34.986  218.343 61.334 1.00 34.08 ?  36  LYS I CA  1 
ATOM   9035  C  C   . LYS I  1 37  ? 36.319  218.018 61.994 1.00 35.71 ?  36  LYS I C   1 
ATOM   9036  O  O   . LYS I  1 37  ? 37.111  217.218 61.492 1.00 42.68 ?  36  LYS I O   1 
ATOM   9037  C  CB  . LYS I  1 37  ? 33.813  217.913 62.218 1.00 41.32 ?  36  LYS I CB  1 
ATOM   9038  C  CG  . LYS I  1 37  ? 33.797  216.431 62.541 1.00 42.37 ?  36  LYS I CG  1 
ATOM   9039  C  CD  . LYS I  1 37  ? 32.414  216.007 63.017 1.00 52.08 ?  36  LYS I CD  1 
ATOM   9040  C  CE  . LYS I  1 37  ? 32.489  214.797 63.944 1.00 54.32 ?  36  LYS I CE  1 
ATOM   9041  N  NZ  . LYS I  1 37  ? 32.338  215.229 65.368 1.00 66.97 ?  36  LYS I NZ  1 
ATOM   9042  N  N   . GLY I  1 38  ? 36.571  218.672 63.123 1.00 35.35 ?  37  GLY I N   1 
ATOM   9043  C  CA  . GLY I  1 38  ? 37.827  218.513 63.827 1.00 41.75 ?  37  GLY I CA  1 
ATOM   9044  C  C   . GLY I  1 38  ? 39.013  219.253 63.240 1.00 40.35 ?  37  GLY I C   1 
ATOM   9045  O  O   . GLY I  1 38  ? 40.148  218.994 63.659 1.00 39.09 ?  37  GLY I O   1 
ATOM   9046  N  N   . LEU I  1 39  ? 38.792  220.166 62.301 1.00 33.46 ?  38  LEU I N   1 
ATOM   9047  C  CA  . LEU I  1 39  ? 39.871  220.942 61.705 1.00 37.44 ?  38  LEU I CA  1 
ATOM   9048  C  C   . LEU I  1 39  ? 40.189  222.168 62.548 1.00 40.04 ?  38  LEU I C   1 
ATOM   9049  O  O   . LEU I  1 39  ? 39.381  222.634 63.351 1.00 39.31 ?  38  LEU I O   1 
ATOM   9050  C  CB  . LEU I  1 39  ? 39.502  221.380 60.283 1.00 34.91 ?  38  LEU I CB  1 
ATOM   9051  C  CG  . LEU I  1 39  ? 39.343  220.228 59.292 1.00 40.00 ?  38  LEU I CG  1 
ATOM   9052  C  CD1 . LEU I  1 39  ? 38.504  220.633 58.083 1.00 37.69 ?  38  LEU I CD1 1 
ATOM   9053  C  CD2 . LEU I  1 39  ? 40.720  219.740 58.853 1.00 36.16 ?  38  LEU I CD2 1 
ATOM   9054  N  N   . THR I  1 40  ? 41.393  222.693 62.358 1.00 41.36 ?  39  THR I N   1 
ATOM   9055  C  CA  . THR I  1 40  ? 41.684  224.040 62.816 1.00 40.68 ?  39  THR I CA  1 
ATOM   9056  C  C   . THR I  1 40  ? 41.009  225.056 61.889 1.00 40.93 ?  39  THR I C   1 
ATOM   9057  O  O   . THR I  1 40  ? 40.844  224.815 60.686 1.00 39.16 ?  39  THR I O   1 
ATOM   9058  C  CB  . THR I  1 40  ? 43.199  224.285 62.861 1.00 41.28 ?  39  THR I CB  1 
ATOM   9059  O  OG1 . THR I  1 40  ? 43.771  224.031 61.571 1.00 43.82 ?  39  THR I OG1 1 
ATOM   9060  C  CG2 . THR I  1 40  ? 43.867  223.355 63.885 1.00 45.32 ?  39  THR I CG2 1 
ATOM   9061  N  N   . GLU I  1 41  ? 40.603  226.190 62.474 1.00 40.30 ?  40  GLU I N   1 
ATOM   9062  C  CA  . GLU I  1 41  ? 40.079  227.344 61.743 1.00 37.42 ?  40  GLU I CA  1 
ATOM   9063  C  C   . GLU I  1 41  ? 40.851  227.620 60.462 1.00 40.60 ?  40  GLU I C   1 
ATOM   9064  O  O   . GLU I  1 41  ? 42.082  227.579 60.444 1.00 42.92 ?  40  GLU I O   1 
ATOM   9065  C  CB  . GLU I  1 41  ? 40.177  228.587 62.622 1.00 36.95 ?  40  GLU I CB  1 
ATOM   9066  C  CG  . GLU I  1 41  ? 39.072  228.802 63.578 1.00 48.00 ?  40  GLU I CG  1 
ATOM   9067  C  CD  . GLU I  1 41  ? 39.333  230.028 64.441 1.00 49.62 ?  40  GLU I CD  1 
ATOM   9068  O  OE1 . GLU I  1 41  ? 38.629  230.208 65.452 1.00 61.75 ?  40  GLU I OE1 1 
ATOM   9069  O  OE2 . GLU I  1 41  ? 40.267  230.799 64.115 1.00 53.13 ?  40  GLU I OE2 1 
ATOM   9070  N  N   . GLY I  1 42  ? 40.127  227.941 59.397 1.00 37.85 ?  41  GLY I N   1 
ATOM   9071  C  CA  . GLY I  1 42  ? 40.736  228.488 58.204 1.00 39.34 ?  41  GLY I CA  1 
ATOM   9072  C  C   . GLY I  1 42  ? 40.819  227.496 57.061 1.00 37.93 ?  41  GLY I C   1 
ATOM   9073  O  O   . GLY I  1 42  ? 40.097  226.491 57.001 1.00 33.78 ?  41  GLY I O   1 
ATOM   9074  N  N   . LEU I  1 43  ? 41.739  227.781 56.144 1.00 31.49 ?  42  LEU I N   1 
ATOM   9075  C  CA  . LEU I  1 43  ? 41.788  227.082 54.864 1.00 38.50 ?  42  LEU I CA  1 
ATOM   9076  C  C   . LEU I  1 43  ? 42.616  225.809 54.967 1.00 39.33 ?  42  LEU I C   1 
ATOM   9077  O  O   . LEU I  1 43  ? 43.633  225.769 55.663 1.00 40.21 ?  42  LEU I O   1 
ATOM   9078  C  CB  . LEU I  1 43  ? 42.370  227.990 53.782 1.00 34.71 ?  42  LEU I CB  1 
ATOM   9079  C  CG  . LEU I  1 43  ? 41.469  229.082 53.192 1.00 37.02 ?  42  LEU I CG  1 
ATOM   9080  C  CD1 . LEU I  1 43  ? 41.008  230.084 54.228 1.00 36.95 ?  42  LEU I CD1 1 
ATOM   9081  C  CD2 . LEU I  1 43  ? 42.203  229.798 52.071 1.00 38.60 ?  42  LEU I CD2 1 
ATOM   9082  N  N   . HIS I  1 44  ? 42.176  224.768 54.270 1.00 32.74 ?  43  HIS I N   1 
ATOM   9083  C  CA  . HIS I  1 44  ? 42.909  223.507 54.247 1.00 35.59 ?  43  HIS I CA  1 
ATOM   9084  C  C   . HIS I  1 44  ? 42.937  222.981 52.820 1.00 39.57 ?  43  HIS I C   1 
ATOM   9085  O  O   . HIS I  1 44  ? 41.902  222.953 52.150 1.00 36.25 ?  43  HIS I O   1 
ATOM   9086  C  CB  . HIS I  1 44  ? 42.272  222.480 55.192 1.00 30.95 ?  43  HIS I CB  1 
ATOM   9087  C  CG  . HIS I  1 44  ? 42.336  222.864 56.641 1.00 30.94 ?  43  HIS I CG  1 
ATOM   9088  N  ND1 . HIS I  1 44  ? 43.241  222.308 57.522 1.00 36.93 ?  43  HIS I ND1 1 
ATOM   9089  C  CD2 . HIS I  1 44  ? 41.621  223.766 57.359 1.00 36.07 ?  43  HIS I CD2 1 
ATOM   9090  C  CE1 . HIS I  1 44  ? 43.080  222.847 58.721 1.00 39.81 ?  43  HIS I CE1 1 
ATOM   9091  N  NE2 . HIS I  1 44  ? 42.103  223.737 58.649 1.00 37.65 ?  43  HIS I NE2 1 
ATOM   9092  N  N   . GLY I  1 45  ? 44.120  222.583 52.351 1.00 39.28 ?  44  GLY I N   1 
ATOM   9093  C  CA  . GLY I  1 45  ? 44.214  221.952 51.044 1.00 41.36 ?  44  GLY I CA  1 
ATOM   9094  C  C   . GLY I  1 45  ? 43.338  220.716 50.942 1.00 37.26 ?  44  GLY I C   1 
ATOM   9095  O  O   . GLY I  1 45  ? 43.148  219.975 51.907 1.00 38.60 ?  44  GLY I O   1 
ATOM   9096  N  N   . PHE I  1 46  ? 42.792  220.505 49.746 1.00 37.05 ?  45  PHE I N   1 
ATOM   9097  C  CA  . PHE I  1 46  ? 41.758  219.502 49.497 1.00 41.50 ?  45  PHE I CA  1 
ATOM   9098  C  C   . PHE I  1 46  ? 42.071  218.908 48.128 1.00 40.75 ?  45  PHE I C   1 
ATOM   9099  O  O   . PHE I  1 46  ? 41.808  219.553 47.109 1.00 42.74 ?  45  PHE I O   1 
ATOM   9100  C  CB  . PHE I  1 46  ? 40.377  220.155 49.533 1.00 39.98 ?  45  PHE I CB  1 
ATOM   9101  C  CG  . PHE I  1 46  ? 39.220  219.192 49.602 1.00 35.20 ?  45  PHE I CG  1 
ATOM   9102  C  CD1 . PHE I  1 46  ? 39.080  218.333 50.677 1.00 36.26 ?  45  PHE I CD1 1 
ATOM   9103  C  CD2 . PHE I  1 46  ? 38.246  219.189 48.620 1.00 37.26 ?  45  PHE I CD2 1 
ATOM   9104  C  CE1 . PHE I  1 46  ? 37.996  217.467 50.768 1.00 37.30 ?  45  PHE I CE1 1 
ATOM   9105  C  CE2 . PHE I  1 46  ? 37.156  218.322 48.699 1.00 39.97 ?  45  PHE I CE2 1 
ATOM   9106  C  CZ  . PHE I  1 46  ? 37.036  217.459 49.784 1.00 29.00 ?  45  PHE I CZ  1 
ATOM   9107  N  N   . HIS I  1 47  ? 42.641  217.692 48.098 1.00 39.59 ?  46  HIS I N   1 
ATOM   9108  C  CA  . HIS I  1 47  ? 43.158  217.137 46.844 1.00 43.52 ?  46  HIS I CA  1 
ATOM   9109  C  C   . HIS I  1 47  ? 42.850  215.653 46.705 1.00 40.23 ?  46  HIS I C   1 
ATOM   9110  O  O   . HIS I  1 47  ? 42.828  214.908 47.689 1.00 41.15 ?  46  HIS I O   1 
ATOM   9111  C  CB  . HIS I  1 47  ? 44.684  217.307 46.723 1.00 40.86 ?  46  HIS I CB  1 
ATOM   9112  C  CG  . HIS I  1 47  ? 45.186  218.631 47.197 1.00 41.78 ?  46  HIS I CG  1 
ATOM   9113  N  ND1 . HIS I  1 47  ? 45.908  218.782 48.363 1.00 44.04 ?  46  HIS I ND1 1 
ATOM   9114  C  CD2 . HIS I  1 47  ? 45.062  219.871 46.666 1.00 44.80 ?  46  HIS I CD2 1 
ATOM   9115  C  CE1 . HIS I  1 47  ? 46.216  220.057 48.525 1.00 43.19 ?  46  HIS I CE1 1 
ATOM   9116  N  NE2 . HIS I  1 47  ? 45.710  220.741 47.512 1.00 44.39 ?  46  HIS I NE2 1 
ATOM   9117  N  N   . VAL I  1 48  ? 42.647  215.215 45.468 1.00 42.37 ?  47  VAL I N   1 
ATOM   9118  C  CA  . VAL I  1 48  ? 42.633  213.786 45.170 1.00 42.66 ?  47  VAL I CA  1 
ATOM   9119  C  C   . VAL I  1 48  ? 44.071  213.363 44.892 1.00 47.66 ?  47  VAL I C   1 
ATOM   9120  O  O   . VAL I  1 48  ? 44.709  213.871 43.961 1.00 47.29 ?  47  VAL I O   1 
ATOM   9121  C  CB  . VAL I  1 48  ? 41.728  213.457 43.976 1.00 43.89 ?  47  VAL I CB  1 
ATOM   9122  C  CG1 . VAL I  1 48  ? 41.845  211.960 43.638 1.00 39.72 ?  47  VAL I CG1 1 
ATOM   9123  C  CG2 . VAL I  1 48  ? 40.295  213.840 44.248 1.00 38.94 ?  47  VAL I CG2 1 
ATOM   9124  N  N   . HIS I  1 49  ? 44.589  212.457 45.712 1.00 45.68 ?  48  HIS I N   1 
ATOM   9125  C  CA  . HIS I  1 49  ? 45.904  211.879 45.484 1.00 44.27 ?  48  HIS I CA  1 
ATOM   9126  C  C   . HIS I  1 49  ? 45.791  210.616 44.631 1.00 46.58 ?  48  HIS I C   1 
ATOM   9127  O  O   . HIS I  1 49  ? 44.704  210.076 44.412 1.00 45.45 ?  48  HIS I O   1 
ATOM   9128  C  CB  . HIS I  1 49  ? 46.596  211.595 46.809 1.00 42.36 ?  48  HIS I CB  1 
ATOM   9129  C  CG  . HIS I  1 49  ? 46.952  212.831 47.564 1.00 42.95 ?  48  HIS I CG  1 
ATOM   9130  N  ND1 . HIS I  1 49  ? 48.180  213.016 48.160 1.00 50.56 ?  48  HIS I ND1 1 
ATOM   9131  C  CD2 . HIS I  1 49  ? 46.240  213.956 47.812 1.00 43.04 ?  48  HIS I CD2 1 
ATOM   9132  C  CE1 . HIS I  1 49  ? 48.207  214.199 48.752 1.00 50.61 ?  48  HIS I CE1 1 
ATOM   9133  N  NE2 . HIS I  1 49  ? 47.041  214.789 48.557 1.00 46.93 ?  48  HIS I NE2 1 
ATOM   9134  N  N   . GLU I  1 50  ? 46.939  210.143 44.136 1.00 47.79 ?  49  GLU I N   1 
ATOM   9135  C  CA  . GLU I  1 50  ? 46.903  209.218 43.006 1.00 49.19 ?  49  GLU I CA  1 
ATOM   9136  C  C   . GLU I  1 50  ? 46.398  207.828 43.404 1.00 47.86 ?  49  GLU I C   1 
ATOM   9137  O  O   . GLU I  1 50  ? 45.601  207.225 42.672 1.00 47.83 ?  49  GLU I O   1 
ATOM   9138  C  CB  . GLU I  1 50  ? 48.278  209.117 42.348 1.00 47.66 ?  49  GLU I CB  1 
ATOM   9139  C  CG  . GLU I  1 50  ? 48.299  208.063 41.244 1.00 54.78 ?  49  GLU I CG  1 
ATOM   9140  C  CD  . GLU I  1 50  ? 49.473  208.193 40.292 1.00 59.32 ?  49  GLU I CD  1 
ATOM   9141  O  OE1 . GLU I  1 50  ? 49.265  207.986 39.071 1.00 52.55 ?  49  GLU I OE1 1 
ATOM   9142  O  OE2 . GLU I  1 50  ? 50.590  208.493 40.775 1.00 55.70 ?  49  GLU I OE2 1 
ATOM   9143  N  N   . PHE I  1 51  ? 46.838  207.302 44.545 1.00 43.65 ?  50  PHE I N   1 
ATOM   9144  C  CA  . PHE I  1 51  ? 46.546  205.917 44.898 1.00 52.33 ?  50  PHE I CA  1 
ATOM   9145  C  C   . PHE I  1 51  ? 45.487  205.815 45.987 1.00 46.70 ?  50  PHE I C   1 
ATOM   9146  O  O   . PHE I  1 51  ? 45.425  206.639 46.902 1.00 47.41 ?  50  PHE I O   1 
ATOM   9147  C  CB  . PHE I  1 51  ? 47.814  205.188 45.355 1.00 50.71 ?  50  PHE I CB  1 
ATOM   9148  C  CG  . PHE I  1 51  ? 48.950  205.348 44.406 1.00 52.89 ?  50  PHE I CG  1 
ATOM   9149  C  CD1 . PHE I  1 51  ? 48.875  204.807 43.134 1.00 49.55 ?  50  PHE I CD1 1 
ATOM   9150  C  CD2 . PHE I  1 51  ? 50.079  206.069 44.767 1.00 51.18 ?  50  PHE I CD2 1 
ATOM   9151  C  CE1 . PHE I  1 51  ? 49.910  204.968 42.241 1.00 50.94 ?  50  PHE I CE1 1 
ATOM   9152  C  CE2 . PHE I  1 51  ? 51.119  206.231 43.878 1.00 49.69 ?  50  PHE I CE2 1 
ATOM   9153  C  CZ  . PHE I  1 51  ? 51.033  205.682 42.612 1.00 50.75 ?  50  PHE I CZ  1 
ATOM   9154  N  N   . GLY I  1 52  ? 44.662  204.775 45.873 1.00 50.23 ?  51  GLY I N   1 
ATOM   9155  C  CA  . GLY I  1 52  ? 43.738  204.401 46.922 1.00 42.29 ?  51  GLY I CA  1 
ATOM   9156  C  C   . GLY I  1 52  ? 44.404  203.461 47.899 1.00 48.61 ?  51  GLY I C   1 
ATOM   9157  O  O   . GLY I  1 52  ? 43.894  202.371 48.174 1.00 47.32 ?  51  GLY I O   1 
ATOM   9158  N  N   . ASP I  1 53  ? 45.544  203.885 48.440 1.00 47.74 ?  52  ASP I N   1 
ATOM   9159  C  CA  . ASP I  1 53  ? 46.385  203.058 49.302 1.00 43.58 ?  52  ASP I CA  1 
ATOM   9160  C  C   . ASP I  1 53  ? 46.495  203.740 50.663 1.00 46.03 ?  52  ASP I C   1 
ATOM   9161  O  O   . ASP I  1 53  ? 47.129  204.793 50.783 1.00 53.64 ?  52  ASP I O   1 
ATOM   9162  C  CB  . ASP I  1 53  ? 47.762  202.862 48.655 1.00 48.83 ?  52  ASP I CB  1 
ATOM   9163  C  CG  . ASP I  1 53  ? 48.646  201.865 49.401 1.00 47.62 ?  52  ASP I CG  1 
ATOM   9164  O  OD1 . ASP I  1 53  ? 48.550  201.746 50.643 1.00 44.23 ?  52  ASP I OD1 1 
ATOM   9165  O  OD2 . ASP I  1 53  ? 49.471  201.213 48.722 1.00 56.03 ?  52  ASP I OD2 1 
ATOM   9166  N  N   A ASN I  1 54  ? 45.880  203.148 51.683 0.50 42.21 ?  53  ASN I N   1 
ATOM   9167  N  N   B ASN I  1 54  ? 45.887  203.129 51.686 0.50 42.18 ?  53  ASN I N   1 
ATOM   9168  C  CA  A ASN I  1 54  ? 45.934  203.696 53.031 0.50 42.52 ?  53  ASN I CA  1 
ATOM   9169  C  CA  B ASN I  1 54  ? 45.882  203.642 53.053 0.50 42.59 ?  53  ASN I CA  1 
ATOM   9170  C  C   A ASN I  1 54  ? 46.671  202.756 53.987 0.50 44.97 ?  53  ASN I C   1 
ATOM   9171  C  C   B ASN I  1 54  ? 46.712  202.777 53.998 0.50 44.95 ?  53  ASN I C   1 
ATOM   9172  O  O   A ASN I  1 54  ? 46.444  202.804 55.204 0.50 46.89 ?  53  ASN I O   1 
ATOM   9173  O  O   B ASN I  1 54  ? 46.592  202.905 55.225 0.50 46.24 ?  53  ASN I O   1 
ATOM   9174  C  CB  A ASN I  1 54  ? 44.519  204.005 53.536 0.50 43.47 ?  53  ASN I CB  1 
ATOM   9175  C  CB  B ASN I  1 54  ? 44.439  203.751 53.566 0.50 42.83 ?  53  ASN I CB  1 
ATOM   9176  C  CG  A ASN I  1 54  ? 43.856  205.201 52.805 0.50 42.44 ?  53  ASN I CG  1 
ATOM   9177  C  CG  B ASN I  1 54  ? 44.344  204.443 54.921 0.50 42.31 ?  53  ASN I CG  1 
ATOM   9178  O  OD1 A ASN I  1 54  ? 44.388  205.738 51.826 0.50 41.08 ?  53  ASN I OD1 1 
ATOM   9179  O  OD1 B ASN I  1 54  ? 44.753  205.589 55.066 0.50 46.00 ?  53  ASN I OD1 1 
ATOM   9180  N  ND2 A ASN I  1 54  ? 42.684  205.612 53.299 0.50 38.55 ?  53  ASN I ND2 1 
ATOM   9181  N  ND2 B ASN I  1 54  ? 43.836  203.730 55.924 0.50 44.42 ?  53  ASN I ND2 1 
ATOM   9182  N  N   . THR I  1 55  ? 47.563  201.907 53.457 1.00 46.57 ?  54  THR I N   1 
ATOM   9183  C  CA  . THR I  1 55  ? 48.256  200.922 54.292 1.00 50.56 ?  54  THR I CA  1 
ATOM   9184  C  C   . THR I  1 55  ? 49.172  201.589 55.312 1.00 50.49 ?  54  THR I C   1 
ATOM   9185  O  O   . THR I  1 55  ? 49.183  201.213 56.489 1.00 51.25 ?  54  THR I O   1 
ATOM   9186  C  CB  . THR I  1 55  ? 49.043  199.952 53.413 1.00 47.54 ?  54  THR I CB  1 
ATOM   9187  O  OG1 . THR I  1 55  ? 49.829  200.697 52.476 1.00 51.20 ?  54  THR I OG1 1 
ATOM   9188  C  CG2 . THR I  1 55  ? 48.082  199.071 52.642 1.00 48.03 ?  54  THR I CG2 1 
ATOM   9189  N  N   . ALA I  1 56  ? 49.942  202.583 54.886 1.00 53.24 ?  55  ALA I N   1 
ATOM   9190  C  CA  . ALA I  1 56  ? 50.725  203.398 55.819 1.00 52.98 ?  55  ALA I CA  1 
ATOM   9191  C  C   . ALA I  1 56  ? 50.048  204.744 56.069 1.00 61.41 ?  55  ALA I C   1 
ATOM   9192  O  O   . ALA I  1 56  ? 50.658  205.809 55.918 1.00 54.60 ?  55  ALA I O   1 
ATOM   9193  C  CB  . ALA I  1 56  ? 52.144  203.587 55.292 1.00 47.62 ?  55  ALA I CB  1 
ATOM   9194  N  N   . GLY I  1 57  ? 48.769  204.713 56.449 1.00 55.48 ?  56  GLY I N   1 
ATOM   9195  C  CA  . GLY I  1 57  ? 48.031  205.953 56.607 1.00 47.47 ?  56  GLY I CA  1 
ATOM   9196  C  C   . GLY I  1 57  ? 47.904  206.697 55.288 1.00 50.53 ?  56  GLY I C   1 
ATOM   9197  O  O   . GLY I  1 57  ? 47.919  206.109 54.202 1.00 51.77 ?  56  GLY I O   1 
ATOM   9198  N  N   . CYS I  1 58  ? 47.801  208.026 55.380 1.00 49.70 ?  57  CYS I N   1 
ATOM   9199  C  CA  . CYS I  1 58  ? 47.587  208.838 54.187 1.00 49.06 ?  57  CYS I CA  1 
ATOM   9200  C  C   . CYS I  1 58  ? 48.841  209.001 53.339 1.00 45.52 ?  57  CYS I C   1 
ATOM   9201  O  O   . CYS I  1 58  ? 48.733  209.426 52.183 1.00 46.83 ?  57  CYS I O   1 
ATOM   9202  C  CB  . CYS I  1 58  ? 47.039  210.215 54.588 1.00 54.38 ?  57  CYS I CB  1 
ATOM   9203  S  SG  . CYS I  1 58  ? 45.477  210.147 55.558 1.00 61.86 ?  57  CYS I SG  1 
ATOM   9204  N  N   . THR I  1 59  ? 50.022  208.673 53.876 1.00 52.21 ?  58  THR I N   1 
ATOM   9205  C  CA  . THR I  1 59  ? 51.255  208.773 53.094 1.00 49.63 ?  58  THR I CA  1 
ATOM   9206  C  C   . THR I  1 59  ? 51.233  207.862 51.877 1.00 47.93 ?  58  THR I C   1 
ATOM   9207  O  O   . THR I  1 59  ? 51.788  208.210 50.830 1.00 49.66 ?  58  THR I O   1 
ATOM   9208  C  CB  . THR I  1 59  ? 52.466  208.417 53.950 1.00 51.66 ?  58  THR I CB  1 
ATOM   9209  O  OG1 . THR I  1 59  ? 52.288  208.925 55.276 1.00 54.32 ?  58  THR I OG1 1 
ATOM   9210  C  CG2 . THR I  1 59  ? 53.711  209.034 53.350 1.00 50.26 ?  58  THR I CG2 1 
ATOM   9211  N  N   . SER I  1 60  ? 50.607  206.692 51.989 1.00 48.13 ?  59  SER I N   1 
ATOM   9212  C  CA  . SER I  1 60  ? 50.659  205.740 50.890 1.00 47.23 ?  59  SER I CA  1 
ATOM   9213  C  C   . SER I  1 60  ? 49.820  206.172 49.699 1.00 48.31 ?  59  SER I C   1 
ATOM   9214  O  O   . SER I  1 60  ? 49.877  205.520 48.650 1.00 45.71 ?  59  SER I O   1 
ATOM   9215  C  CB  . SER I  1 60  ? 50.216  204.363 51.382 1.00 46.25 ?  59  SER I CB  1 
ATOM   9216  O  OG  . SER I  1 60  ? 50.106  204.351 52.798 1.00 51.92 ?  59  SER I OG  1 
ATOM   9217  N  N   . ALA I  1 61  ? 49.050  207.254 49.825 1.00 49.98 ?  60  ALA I N   1 
ATOM   9218  C  CA  . ALA I  1 61  ? 48.232  207.706 48.707 1.00 46.29 ?  60  ALA I CA  1 
ATOM   9219  C  C   . ALA I  1 61  ? 49.069  208.287 47.582 1.00 48.15 ?  60  ALA I C   1 
ATOM   9220  O  O   . ALA I  1 61  ? 48.564  208.428 46.459 1.00 45.50 ?  60  ALA I O   1 
ATOM   9221  C  CB  . ALA I  1 61  ? 47.210  208.737 49.191 1.00 49.82 ?  60  ALA I CB  1 
ATOM   9222  N  N   . GLY I  1 62  ? 50.331  208.609 47.851 1.00 48.68 ?  61  GLY I N   1 
ATOM   9223  C  CA  . GLY I  1 62  ? 51.193  209.185 46.850 1.00 47.54 ?  61  GLY I CA  1 
ATOM   9224  C  C   . GLY I  1 62  ? 50.954  210.672 46.715 1.00 54.43 ?  61  GLY I C   1 
ATOM   9225  O  O   . GLY I  1 62  ? 50.545  211.351 47.668 1.00 47.59 ?  61  GLY I O   1 
ATOM   9226  N  N   . PRO I  1 63  ? 51.205  211.208 45.508 1.00 54.53 ?  62  PRO I N   1 
ATOM   9227  C  CA  . PRO I  1 63  ? 51.030  212.645 45.271 1.00 51.45 ?  62  PRO I CA  1 
ATOM   9228  C  C   . PRO I  1 63  ? 49.686  212.978 44.650 1.00 44.82 ?  62  PRO I C   1 
ATOM   9229  O  O   . PRO I  1 63  ? 48.895  212.080 44.349 1.00 49.07 ?  62  PRO I O   1 
ATOM   9230  C  CB  . PRO I  1 63  ? 52.166  212.956 44.295 1.00 52.90 ?  62  PRO I CB  1 
ATOM   9231  C  CG  . PRO I  1 63  ? 52.171  211.710 43.418 1.00 49.02 ?  62  PRO I CG  1 
ATOM   9232  C  CD  . PRO I  1 63  ? 51.809  210.543 44.340 1.00 48.52 ?  62  PRO I CD  1 
ATOM   9233  N  N   . HIS I  1 64  ? 49.436  214.264 44.424 1.00 43.03 ?  63  HIS I N   1 
ATOM   9234  C  CA  . HIS I  1 64  ? 48.198  214.686 43.784 1.00 47.23 ?  63  HIS I CA  1 
ATOM   9235  C  C   . HIS I  1 64  ? 48.009  213.933 42.474 1.00 48.29 ?  63  HIS I C   1 
ATOM   9236  O  O   . HIS I  1 64  ? 48.955  213.759 41.705 1.00 51.04 ?  63  HIS I O   1 
ATOM   9237  C  CB  . HIS I  1 64  ? 48.210  216.207 43.541 1.00 42.28 ?  63  HIS I CB  1 
ATOM   9238  C  CG  . HIS I  1 64  ? 48.439  217.020 44.784 1.00 50.24 ?  63  HIS I CG  1 
ATOM   9239  N  ND1 . HIS I  1 64  ? 48.645  218.386 44.760 1.00 49.61 ?  63  HIS I ND1 1 
ATOM   9240  C  CD2 . HIS I  1 64  ? 48.500  216.655 46.089 1.00 48.82 ?  63  HIS I CD2 1 
ATOM   9241  C  CE1 . HIS I  1 64  ? 48.818  218.825 45.997 1.00 52.55 ?  63  HIS I CE1 1 
ATOM   9242  N  NE2 . HIS I  1 64  ? 48.739  217.795 46.822 1.00 45.39 ?  63  HIS I NE2 1 
ATOM   9243  N  N   . PHE I  1 65  ? 46.792  213.442 42.253 1.00 46.91 ?  64  PHE I N   1 
ATOM   9244  C  CA  . PHE I  1 65  ? 46.455  212.773 41.003 1.00 43.65 ?  64  PHE I CA  1 
ATOM   9245  C  C   . PHE I  1 65  ? 46.739  213.696 39.820 1.00 53.72 ?  64  PHE I C   1 
ATOM   9246  O  O   . PHE I  1 65  ? 46.150  214.780 39.704 1.00 50.44 ?  64  PHE I O   1 
ATOM   9247  C  CB  . PHE I  1 65  ? 44.984  212.365 41.029 1.00 46.94 ?  64  PHE I CB  1 
ATOM   9248  C  CG  . PHE I  1 65  ? 44.534  211.590 39.826 1.00 42.26 ?  64  PHE I CG  1 
ATOM   9249  C  CD1 . PHE I  1 65  ? 45.325  210.590 39.280 1.00 46.94 ?  64  PHE I CD1 1 
ATOM   9250  C  CD2 . PHE I  1 65  ? 43.291  211.838 39.261 1.00 42.54 ?  64  PHE I CD2 1 
ATOM   9251  C  CE1 . PHE I  1 65  ? 44.889  209.862 38.180 1.00 43.08 ?  64  PHE I CE1 1 
ATOM   9252  C  CE2 . PHE I  1 65  ? 42.849  211.119 38.162 1.00 42.33 ?  64  PHE I CE2 1 
ATOM   9253  C  CZ  . PHE I  1 65  ? 43.649  210.128 37.619 1.00 44.20 ?  64  PHE I CZ  1 
ATOM   9254  N  N   . ASN I  1 66  ? 47.617  213.248 38.923 1.00 52.80 ?  65  ASN I N   1 
ATOM   9255  C  CA  . ASN I  1 66  ? 48.184  214.108 37.894 1.00 50.88 ?  65  ASN I CA  1 
ATOM   9256  C  C   . ASN I  1 66  ? 48.413  213.334 36.599 1.00 52.36 ?  65  ASN I C   1 
ATOM   9257  O  O   . ASN I  1 66  ? 49.550  213.261 36.122 1.00 54.15 ?  65  ASN I O   1 
ATOM   9258  C  CB  . ASN I  1 66  ? 49.506  214.704 38.403 1.00 52.20 ?  65  ASN I CB  1 
ATOM   9259  C  CG  . ASN I  1 66  ? 50.079  215.766 37.475 1.00 52.93 ?  65  ASN I CG  1 
ATOM   9260  O  OD1 . ASN I  1 66  ? 49.432  216.200 36.521 1.00 51.97 ?  65  ASN I OD1 1 
ATOM   9261  N  ND2 . ASN I  1 66  ? 51.316  216.173 37.746 1.00 49.29 ?  65  ASN I ND2 1 
ATOM   9262  N  N   . PRO I  1 67  ? 47.375  212.760 35.986 1.00 55.59 ?  66  PRO I N   1 
ATOM   9263  C  CA  . PRO I  1 67  ? 47.609  211.939 34.786 1.00 56.75 ?  66  PRO I CA  1 
ATOM   9264  C  C   . PRO I  1 67  ? 48.188  212.714 33.605 1.00 60.49 ?  66  PRO I C   1 
ATOM   9265  O  O   . PRO I  1 67  ? 48.817  212.099 32.734 1.00 63.83 ?  66  PRO I O   1 
ATOM   9266  C  CB  . PRO I  1 67  ? 46.212  211.389 34.456 1.00 51.73 ?  66  PRO I CB  1 
ATOM   9267  C  CG  . PRO I  1 67  ? 45.273  212.409 35.013 1.00 54.10 ?  66  PRO I CG  1 
ATOM   9268  C  CD  . PRO I  1 67  ? 45.936  212.915 36.274 1.00 50.79 ?  66  PRO I CD  1 
ATOM   9269  N  N   . LEU I  1 68  ? 47.993  214.031 33.543 1.00 58.51 ?  67  LEU I N   1 
ATOM   9270  C  CA  . LEU I  1 68  ? 48.441  214.841 32.416 1.00 52.99 ?  67  LEU I CA  1 
ATOM   9271  C  C   . LEU I  1 68  ? 49.770  215.539 32.674 1.00 59.45 ?  67  LEU I C   1 
ATOM   9272  O  O   . LEU I  1 68  ? 50.138  216.446 31.918 1.00 63.71 ?  67  LEU I O   1 
ATOM   9273  C  CB  . LEU I  1 68  ? 47.369  215.863 32.055 1.00 56.96 ?  67  LEU I CB  1 
ATOM   9274  C  CG  . LEU I  1 68  ? 46.116  215.145 31.563 1.00 60.23 ?  67  LEU I CG  1 
ATOM   9275  C  CD1 . LEU I  1 68  ? 45.085  216.137 31.056 1.00 56.47 ?  67  LEU I CD1 1 
ATOM   9276  C  CD2 . LEU I  1 68  ? 46.502  214.143 30.476 1.00 54.10 ?  67  LEU I CD2 1 
ATOM   9277  N  N   . SER I  1 69  ? 50.483  215.153 33.735 1.00 57.09 ?  68  SER I N   1 
ATOM   9278  C  CA  . SER I  1 69  ? 51.858  215.601 33.976 1.00 58.90 ?  68  SER I CA  1 
ATOM   9279  C  C   . SER I  1 69  ? 51.996  217.127 33.962 1.00 65.18 ?  68  SER I C   1 
ATOM   9280  O  O   . SER I  1 69  ? 52.957  217.680 33.421 1.00 64.28 ?  68  SER I O   1 
ATOM   9281  C  CB  . SER I  1 69  ? 52.810  214.962 32.966 1.00 56.76 ?  68  SER I CB  1 
ATOM   9282  O  OG  . SER I  1 69  ? 53.403  213.800 33.520 1.00 61.60 ?  68  SER I OG  1 
ATOM   9283  N  N   . ARG I  1 70  ? 51.048  217.815 34.597 1.00 61.92 ?  69  ARG I N   1 
ATOM   9284  C  CA  . ARG I  1 70  ? 51.081  219.263 34.721 1.00 55.69 ?  69  ARG I CA  1 
ATOM   9285  C  C   . ARG I  1 70  ? 51.580  219.642 36.115 1.00 49.88 ?  69  ARG I C   1 
ATOM   9286  O  O   . ARG I  1 70  ? 51.864  218.781 36.950 1.00 56.46 ?  69  ARG I O   1 
ATOM   9287  C  CB  . ARG I  1 70  ? 49.699  219.841 34.422 1.00 51.83 ?  69  ARG I CB  1 
ATOM   9288  C  CG  . ARG I  1 70  ? 49.302  219.660 32.968 1.00 54.46 ?  69  ARG I CG  1 
ATOM   9289  C  CD  . ARG I  1 70  ? 48.003  220.364 32.626 1.00 58.74 ?  69  ARG I CD  1 
ATOM   9290  N  NE  . ARG I  1 70  ? 47.518  219.954 31.313 1.00 63.70 ?  69  ARG I NE  1 
ATOM   9291  C  CZ  . ARG I  1 70  ? 46.271  220.110 30.884 1.00 72.21 ?  69  ARG I CZ  1 
ATOM   9292  N  NH1 . ARG I  1 70  ? 45.358  220.725 31.622 1.00 69.22 ?  69  ARG I NH1 1 
ATOM   9293  N  NH2 . ARG I  1 70  ? 45.931  219.641 29.684 1.00 67.01 ?  69  ARG I NH2 1 
ATOM   9294  N  N   . LYS I  1 71  ? 51.718  220.941 36.371 1.00 54.14 ?  70  LYS I N   1 
ATOM   9295  C  CA  . LYS I  1 71  ? 52.108  221.381 37.705 1.00 60.93 ?  70  LYS I CA  1 
ATOM   9296  C  C   . LYS I  1 71  ? 50.896  221.893 38.484 1.00 59.22 ?  70  LYS I C   1 
ATOM   9297  O  O   . LYS I  1 71  ? 49.790  222.055 37.954 1.00 51.00 ?  70  LYS I O   1 
ATOM   9298  C  CB  . LYS I  1 71  ? 53.215  222.441 37.656 1.00 59.67 ?  70  LYS I CB  1 
ATOM   9299  C  CG  . LYS I  1 71  ? 53.067  223.488 36.571 1.00 68.51 ?  70  LYS I CG  1 
ATOM   9300  C  CD  . LYS I  1 71  ? 54.435  223.869 35.988 1.00 72.87 ?  70  LYS I CD  1 
ATOM   9301  C  CE  . LYS I  1 71  ? 55.352  224.531 37.035 1.00 69.53 ?  70  LYS I CE  1 
ATOM   9302  N  NZ  . LYS I  1 71  ? 54.774  225.780 37.640 1.00 66.34 ?  70  LYS I NZ  1 
ATOM   9303  N  N   . HIS I  1 72  ? 51.125  222.127 39.773 1.00 57.85 ?  71  HIS I N   1 
ATOM   9304  C  CA  . HIS I  1 72  ? 50.030  222.338 40.708 1.00 57.63 ?  71  HIS I CA  1 
ATOM   9305  C  C   . HIS I  1 72  ? 49.398  223.714 40.516 1.00 60.18 ?  71  HIS I C   1 
ATOM   9306  O  O   . HIS I  1 72  ? 50.088  224.708 40.268 1.00 60.22 ?  71  HIS I O   1 
ATOM   9307  C  CB  . HIS I  1 72  ? 50.538  222.171 42.141 1.00 58.15 ?  71  HIS I CB  1 
ATOM   9308  C  CG  . HIS I  1 72  ? 49.533  222.533 43.183 1.00 59.88 ?  71  HIS I CG  1 
ATOM   9309  N  ND1 . HIS I  1 72  ? 48.582  221.645 43.636 1.00 61.88 ?  71  HIS I ND1 1 
ATOM   9310  C  CD2 . HIS I  1 72  ? 49.332  223.685 43.865 1.00 57.05 ?  71  HIS I CD2 1 
ATOM   9311  C  CE1 . HIS I  1 72  ? 47.834  222.235 44.551 1.00 56.76 ?  71  HIS I CE1 1 
ATOM   9312  N  NE2 . HIS I  1 72  ? 48.265  223.475 44.706 1.00 59.54 ?  71  HIS I NE2 1 
ATOM   9313  N  N   . GLY I  1 73  ? 48.070  223.758 40.611 1.00 59.59 ?  72  GLY I N   1 
ATOM   9314  C  CA  . GLY I  1 73  ? 47.325  225.001 40.529 1.00 56.75 ?  72  GLY I CA  1 
ATOM   9315  C  C   . GLY I  1 73  ? 46.088  224.967 41.405 1.00 58.79 ?  72  GLY I C   1 
ATOM   9316  O  O   . GLY I  1 73  ? 45.928  224.050 42.219 1.00 59.66 ?  72  GLY I O   1 
ATOM   9317  N  N   . GLY I  1 74  ? 45.220  225.967 41.274 1.00 52.72 ?  73  GLY I N   1 
ATOM   9318  C  CA  . GLY I  1 74  ? 43.917  225.921 41.893 1.00 47.04 ?  73  GLY I CA  1 
ATOM   9319  C  C   . GLY I  1 74  ? 42.916  225.346 40.911 1.00 50.52 ?  73  GLY I C   1 
ATOM   9320  O  O   . GLY I  1 74  ? 43.173  225.277 39.704 1.00 51.51 ?  73  GLY I O   1 
ATOM   9321  N  N   . PRO I  1 75  ? 41.755  224.917 41.405 1.00 45.28 ?  74  PRO I N   1 
ATOM   9322  C  CA  . PRO I  1 75  ? 40.764  224.300 40.509 1.00 49.22 ?  74  PRO I CA  1 
ATOM   9323  C  C   . PRO I  1 75  ? 40.406  225.171 39.315 1.00 46.05 ?  74  PRO I C   1 
ATOM   9324  O  O   . PRO I  1 75  ? 40.105  224.640 38.239 1.00 50.96 ?  74  PRO I O   1 
ATOM   9325  C  CB  . PRO I  1 75  ? 39.553  224.063 41.427 1.00 46.16 ?  74  PRO I CB  1 
ATOM   9326  C  CG  . PRO I  1 75  ? 39.824  224.860 42.673 1.00 46.62 ?  74  PRO I CG  1 
ATOM   9327  C  CD  . PRO I  1 75  ? 41.302  224.948 42.804 1.00 50.66 ?  74  PRO I CD  1 
ATOM   9328  N  N   . LYS I  1 76  ? 40.461  226.499 39.468 1.00 50.69 ?  75  LYS I N   1 
ATOM   9329  C  CA  . LYS I  1 76  ? 40.128  227.424 38.385 1.00 48.55 ?  75  LYS I CA  1 
ATOM   9330  C  C   . LYS I  1 76  ? 41.248  227.574 37.358 1.00 47.81 ?  75  LYS I C   1 
ATOM   9331  O  O   . LYS I  1 76  ? 40.984  228.026 36.237 1.00 52.94 ?  75  LYS I O   1 
ATOM   9332  C  CB  . LYS I  1 76  ? 39.783  228.801 38.965 1.00 48.43 ?  75  LYS I CB  1 
ATOM   9333  C  CG  . LYS I  1 76  ? 38.442  228.855 39.692 1.00 57.25 ?  75  LYS I CG  1 
ATOM   9334  C  CD  . LYS I  1 76  ? 38.026  230.295 40.035 1.00 56.60 ?  75  LYS I CD  1 
ATOM   9335  C  CE  . LYS I  1 76  ? 38.554  230.734 41.408 1.00 59.89 ?  75  LYS I CE  1 
ATOM   9336  N  NZ  . LYS I  1 76  ? 38.961  232.181 41.439 1.00 66.41 ?  75  LYS I NZ  1 
ATOM   9337  N  N   . ASP I  1 77  ? 42.479  227.212 37.716 1.00 50.33 ?  76  ASP I N   1 
ATOM   9338  C  CA  . ASP I  1 77  ? 43.616  227.327 36.812 1.00 48.45 ?  76  ASP I CA  1 
ATOM   9339  C  C   . ASP I  1 77  ? 43.528  226.314 35.674 1.00 53.61 ?  76  ASP I C   1 
ATOM   9340  O  O   . ASP I  1 77  ? 43.053  225.188 35.851 1.00 57.45 ?  76  ASP I O   1 
ATOM   9341  C  CB  . ASP I  1 77  ? 44.913  227.119 37.595 1.00 47.71 ?  76  ASP I CB  1 
ATOM   9342  C  CG  . ASP I  1 77  ? 45.200  228.261 38.549 1.00 59.69 ?  76  ASP I CG  1 
ATOM   9343  O  OD1 . ASP I  1 77  ? 44.641  229.358 38.320 1.00 61.48 ?  76  ASP I OD1 1 
ATOM   9344  O  OD2 . ASP I  1 77  ? 45.976  228.074 39.520 1.00 59.28 ?  76  ASP I OD2 1 
ATOM   9345  N  N   . GLU I  1 78  ? 43.993  226.723 34.491 1.00 56.69 ?  77  GLU I N   1 
ATOM   9346  C  CA  . GLU I  1 78  ? 44.113  225.783 33.380 1.00 53.86 ?  77  GLU I CA  1 
ATOM   9347  C  C   . GLU I  1 78  ? 45.256  224.804 33.620 1.00 55.15 ?  77  GLU I C   1 
ATOM   9348  O  O   . GLU I  1 78  ? 45.124  223.604 33.353 1.00 62.27 ?  77  GLU I O   1 
ATOM   9349  C  CB  . GLU I  1 78  ? 44.319  226.543 32.067 1.00 65.25 ?  77  GLU I CB  1 
ATOM   9350  C  CG  . GLU I  1 78  ? 43.144  226.474 31.081 1.00 69.63 ?  77  GLU I CG  1 
ATOM   9351  C  CD  . GLU I  1 78  ? 42.830  225.049 30.629 1.00 86.95 ?  77  GLU I CD  1 
ATOM   9352  O  OE1 . GLU I  1 78  ? 43.786  224.249 30.460 1.00 81.61 ?  77  GLU I OE1 1 
ATOM   9353  O  OE2 . GLU I  1 78  ? 41.628  224.731 30.445 1.00 92.17 ?  77  GLU I OE2 1 
ATOM   9354  N  N   . GLU I  1 79  ? 46.377  225.294 34.136 1.00 55.15 ?  78  GLU I N   1 
ATOM   9355  C  CA  . GLU I  1 79  ? 47.499  224.440 34.502 1.00 52.96 ?  78  GLU I CA  1 
ATOM   9356  C  C   . GLU I  1 79  ? 47.312  223.964 35.943 1.00 62.59 ?  78  GLU I C   1 
ATOM   9357  O  O   . GLU I  1 79  ? 47.542  224.724 36.894 1.00 57.64 ?  78  GLU I O   1 
ATOM   9358  C  CB  . GLU I  1 79  ? 48.817  225.184 34.331 1.00 47.10 ?  78  GLU I CB  1 
ATOM   9359  C  CG  . GLU I  1 79  ? 50.029  224.392 34.806 1.00 63.31 ?  78  GLU I CG  1 
ATOM   9360  C  CD  . GLU I  1 79  ? 50.603  223.483 33.716 1.00 67.96 ?  78  GLU I CD  1 
ATOM   9361  O  OE1 . GLU I  1 79  ? 51.656  222.846 33.957 1.00 64.43 ?  78  GLU I OE1 1 
ATOM   9362  O  OE2 . GLU I  1 79  ? 49.993  223.399 32.623 1.00 68.90 ?  78  GLU I OE2 1 
ATOM   9363  N  N   . ARG I  1 80  ? 46.911  222.703 36.102 1.00 58.19 ?  79  ARG I N   1 
ATOM   9364  C  CA  . ARG I  1 80  ? 46.700  222.110 37.417 1.00 55.64 ?  79  ARG I CA  1 
ATOM   9365  C  C   . ARG I  1 80  ? 46.780  220.594 37.290 1.00 54.89 ?  79  ARG I C   1 
ATOM   9366  O  O   . ARG I  1 80  ? 46.635  220.036 36.199 1.00 55.21 ?  79  ARG I O   1 
ATOM   9367  C  CB  . ARG I  1 80  ? 45.338  222.503 37.989 1.00 49.36 ?  79  ARG I CB  1 
ATOM   9368  C  CG  . ARG I  1 80  ? 44.214  222.154 37.016 1.00 47.10 ?  79  ARG I CG  1 
ATOM   9369  C  CD  . ARG I  1 80  ? 42.848  222.284 37.646 1.00 53.02 ?  79  ARG I CD  1 
ATOM   9370  N  NE  . ARG I  1 80  ? 42.371  221.042 38.244 1.00 51.36 ?  79  ARG I NE  1 
ATOM   9371  C  CZ  . ARG I  1 80  ? 41.116  220.842 38.622 1.00 50.53 ?  79  ARG I CZ  1 
ATOM   9372  N  NH1 . ARG I  1 80  ? 40.200  221.792 38.500 1.00 47.42 ?  79  ARG I NH1 1 
ATOM   9373  N  NH2 . ARG I  1 80  ? 40.767  219.662 39.130 1.00 50.65 ?  79  ARG I NH2 1 
ATOM   9374  N  N   . HIS I  1 81  ? 46.994  219.936 38.426 1.00 53.71 ?  80  HIS I N   1 
ATOM   9375  C  CA  . HIS I  1 81  ? 46.751  218.503 38.508 1.00 48.65 ?  80  HIS I CA  1 
ATOM   9376  C  C   . HIS I  1 81  ? 45.259  218.221 38.420 1.00 49.25 ?  80  HIS I C   1 
ATOM   9377  O  O   . HIS I  1 81  ? 44.423  219.058 38.781 1.00 50.20 ?  80  HIS I O   1 
ATOM   9378  C  CB  . HIS I  1 81  ? 47.303  217.948 39.816 1.00 48.03 ?  80  HIS I CB  1 
ATOM   9379  C  CG  . HIS I  1 81  ? 48.721  218.333 40.070 1.00 50.52 ?  80  HIS I CG  1 
ATOM   9380  N  ND1 . HIS I  1 81  ? 49.237  218.491 41.337 1.00 51.80 ?  80  HIS I ND1 1 
ATOM   9381  C  CD2 . HIS I  1 81  ? 49.743  218.572 39.215 1.00 53.49 ?  80  HIS I CD2 1 
ATOM   9382  C  CE1 . HIS I  1 81  ? 50.514  218.821 41.253 1.00 52.56 ?  80  HIS I CE1 1 
ATOM   9383  N  NE2 . HIS I  1 81  ? 50.847  218.875 39.975 1.00 54.92 ?  80  HIS I NE2 1 
ATOM   9384  N  N   . VAL I  1 82  ? 44.919  217.026 37.931 1.00 46.33 ?  81  VAL I N   1 
ATOM   9385  C  CA  . VAL I  1 82  ? 43.510  216.646 37.901 1.00 54.15 ?  81  VAL I CA  1 
ATOM   9386  C  C   . VAL I  1 82  ? 42.925  216.641 39.311 1.00 48.48 ?  81  VAL I C   1 
ATOM   9387  O  O   . VAL I  1 82  ? 41.753  216.982 39.505 1.00 45.42 ?  81  VAL I O   1 
ATOM   9388  C  CB  . VAL I  1 82  ? 43.323  215.288 37.190 1.00 49.30 ?  81  VAL I CB  1 
ATOM   9389  C  CG1 . VAL I  1 82  ? 41.950  214.705 37.494 1.00 47.83 ?  81  VAL I CG1 1 
ATOM   9390  C  CG2 . VAL I  1 82  ? 43.484  215.461 35.675 1.00 53.72 ?  81  VAL I CG2 1 
ATOM   9391  N  N   . GLY I  1 83  ? 43.729  216.318 40.316 1.00 45.24 ?  82  GLY I N   1 
ATOM   9392  C  CA  . GLY I  1 83  ? 43.206  216.238 41.664 1.00 46.38 ?  82  GLY I CA  1 
ATOM   9393  C  C   . GLY I  1 83  ? 43.211  217.527 42.459 1.00 50.99 ?  82  GLY I C   1 
ATOM   9394  O  O   . GLY I  1 83  ? 42.963  217.486 43.669 1.00 46.55 ?  82  GLY I O   1 
ATOM   9395  N  N   . ASP I  1 84  ? 43.477  218.671 41.826 1.00 48.14 ?  83  ASP I N   1 
ATOM   9396  C  CA  . ASP I  1 84  ? 43.657  219.944 42.530 1.00 49.42 ?  83  ASP I CA  1 
ATOM   9397  C  C   . ASP I  1 84  ? 42.290  220.573 42.777 1.00 47.32 ?  83  ASP I C   1 
ATOM   9398  O  O   . ASP I  1 84  ? 41.725  221.236 41.906 1.00 44.53 ?  83  ASP I O   1 
ATOM   9399  C  CB  . ASP I  1 84  ? 44.558  220.878 41.724 1.00 49.31 ?  83  ASP I CB  1 
ATOM   9400  C  CG  . ASP I  1 84  ? 46.033  220.478 41.773 1.00 53.51 ?  83  ASP I CG  1 
ATOM   9401  O  OD1 . ASP I  1 84  ? 46.356  219.445 42.390 1.00 54.51 ?  83  ASP I OD1 1 
ATOM   9402  O  OD2 . ASP I  1 84  ? 46.874  221.184 41.170 1.00 55.57 ?  83  ASP I OD2 1 
ATOM   9403  N  N   . LEU I  1 85  ? 41.745  220.371 43.975 1.00 43.72 ?  84  LEU I N   1 
ATOM   9404  C  CA  . LEU I  1 85  ? 40.433  220.903 44.321 1.00 44.72 ?  84  LEU I CA  1 
ATOM   9405  C  C   . LEU I  1 85  ? 40.525  222.100 45.260 1.00 41.38 ?  84  LEU I C   1 
ATOM   9406  O  O   . LEU I  1 85  ? 39.528  222.472 45.883 1.00 41.89 ?  84  LEU I O   1 
ATOM   9407  C  CB  . LEU I  1 85  ? 39.554  219.807 44.926 1.00 39.68 ?  84  LEU I CB  1 
ATOM   9408  C  CG  . LEU I  1 85  ? 39.265  218.620 44.003 1.00 41.87 ?  84  LEU I CG  1 
ATOM   9409  C  CD1 . LEU I  1 85  ? 38.509  217.538 44.743 1.00 39.48 ?  84  LEU I CD1 1 
ATOM   9410  C  CD2 . LEU I  1 85  ? 38.490  219.039 42.763 1.00 37.12 ?  84  LEU I CD2 1 
ATOM   9411  N  N   . GLY I  1 86  ? 41.708  222.689 45.399 1.00 42.36 ?  85  GLY I N   1 
ATOM   9412  C  CA  . GLY I  1 86  ? 41.789  223.952 46.114 1.00 38.71 ?  85  GLY I CA  1 
ATOM   9413  C  C   . GLY I  1 86  ? 41.734  223.792 47.618 1.00 40.86 ?  85  GLY I C   1 
ATOM   9414  O  O   . GLY I  1 86  ? 42.314  222.858 48.201 1.00 41.53 ?  85  GLY I O   1 
ATOM   9415  N  N   . ASN I  1 87  ? 41.026  224.718 48.259 1.00 36.74 ?  86  ASN I N   1 
ATOM   9416  C  CA  . ASN I  1 87  ? 40.913  224.789 49.710 1.00 38.00 ?  86  ASN I CA  1 
ATOM   9417  C  C   . ASN I  1 87  ? 39.469  224.586 50.143 1.00 37.22 ?  86  ASN I C   1 
ATOM   9418  O  O   . ASN I  1 87  ? 38.533  224.995 49.454 1.00 38.46 ?  86  ASN I O   1 
ATOM   9419  C  CB  . ASN I  1 87  ? 41.382  226.149 50.241 1.00 39.38 ?  86  ASN I CB  1 
ATOM   9420  C  CG  . ASN I  1 87  ? 42.867  226.345 50.097 1.00 44.18 ?  86  ASN I CG  1 
ATOM   9421  O  OD1 . ASN I  1 87  ? 43.658  225.746 50.837 1.00 43.83 ?  86  ASN I OD1 1 
ATOM   9422  N  ND2 . ASN I  1 87  ? 43.264  227.196 49.152 1.00 41.13 ?  86  ASN I ND2 1 
ATOM   9423  N  N   . VAL I  1 88  ? 39.303  223.960 51.296 1.00 35.92 ?  87  VAL I N   1 
ATOM   9424  C  CA  . VAL I  1 88  ? 38.042  224.005 52.012 1.00 35.53 ?  87  VAL I CA  1 
ATOM   9425  C  C   . VAL I  1 88  ? 38.299  224.843 53.246 1.00 36.80 ?  87  VAL I C   1 
ATOM   9426  O  O   . VAL I  1 88  ? 39.431  224.925 53.730 1.00 37.16 ?  87  VAL I O   1 
ATOM   9427  C  CB  . VAL I  1 88  ? 37.505  222.607 52.381 1.00 35.14 ?  87  VAL I CB  1 
ATOM   9428  C  CG1 . VAL I  1 88  ? 37.323  221.768 51.123 1.00 36.83 ?  87  VAL I CG1 1 
ATOM   9429  C  CG2 . VAL I  1 88  ? 38.445  221.922 53.339 1.00 32.40 ?  87  VAL I CG2 1 
ATOM   9430  N  N   . THR I  1 89  ? 37.253  225.487 53.742 1.00 31.82 ?  88  THR I N   1 
ATOM   9431  C  CA  . THR I  1 89  ? 37.372  226.479 54.802 1.00 34.93 ?  88  THR I CA  1 
ATOM   9432  C  C   . THR I  1 89  ? 36.627  225.982 56.029 1.00 32.76 ?  88  THR I C   1 
ATOM   9433  O  O   . THR I  1 89  ? 35.410  225.779 55.980 1.00 33.44 ?  88  THR I O   1 
ATOM   9434  C  CB  . THR I  1 89  ? 36.807  227.825 54.354 1.00 34.03 ?  88  THR I CB  1 
ATOM   9435  O  OG1 . THR I  1 89  ? 37.552  228.317 53.241 1.00 34.08 ?  88  THR I OG1 1 
ATOM   9436  C  CG2 . THR I  1 89  ? 36.880  228.838 55.489 1.00 35.02 ?  88  THR I CG2 1 
ATOM   9437  N  N   . ALA I  1 90  ? 37.350  225.811 57.129 1.00 31.35 ?  89  ALA I N   1 
ATOM   9438  C  CA  . ALA I  1 90  ? 36.753  225.374 58.381 1.00 34.47 ?  89  ALA I CA  1 
ATOM   9439  C  C   . ALA I  1 90  ? 36.395  226.582 59.233 1.00 37.02 ?  89  ALA I C   1 
ATOM   9440  O  O   . ALA I  1 90  ? 37.199  227.507 59.382 1.00 31.51 ?  89  ALA I O   1 
ATOM   9441  C  CB  . ALA I  1 90  ? 37.711  224.464 59.148 1.00 35.14 ?  89  ALA I CB  1 
ATOM   9442  N  N   . ASP I  1 91  ? 35.205  226.545 59.833 1.00 34.05 ?  90  ASP I N   1 
ATOM   9443  C  CA  . ASP I  1 91  ? 34.736  227.680 60.612 1.00 38.10 ?  90  ASP I CA  1 
ATOM   9444  C  C   . ASP I  1 91  ? 35.356  227.639 62.008 1.00 38.89 ?  90  ASP I C   1 
ATOM   9445  O  O   . ASP I  1 91  ? 36.181  226.783 62.321 1.00 33.41 ?  90  ASP I O   1 
ATOM   9446  C  CB  . ASP I  1 91  ? 33.203  227.703 60.676 1.00 34.25 ?  90  ASP I CB  1 
ATOM   9447  C  CG  . ASP I  1 91  ? 32.602  226.487 61.385 1.00 43.61 ?  90  ASP I CG  1 
ATOM   9448  O  OD1 . ASP I  1 91  ? 33.292  225.827 62.203 1.00 37.62 ?  90  ASP I OD1 1 
ATOM   9449  O  OD2 . ASP I  1 91  ? 31.411  226.199 61.118 1.00 43.31 ?  90  ASP I OD2 1 
ATOM   9450  N  N   . LYS I  1 92  ? 34.924  228.562 62.869 1.00 35.55 ?  91  LYS I N   1 
ATOM   9451  C  CA  . LYS I  1 92  ? 35.488  228.672 64.213 1.00 43.31 ?  91  LYS I CA  1 
ATOM   9452  C  C   . LYS I  1 92  ? 35.276  227.414 65.042 1.00 43.04 ?  91  LYS I C   1 
ATOM   9453  O  O   . LYS I  1 92  ? 35.929  227.250 66.077 1.00 42.32 ?  91  LYS I O   1 
ATOM   9454  C  CB  . LYS I  1 92  ? 34.873  229.868 64.942 1.00 39.46 ?  91  LYS I CB  1 
ATOM   9455  C  CG  . LYS I  1 92  ? 35.455  231.209 64.517 1.00 53.24 ?  91  LYS I CG  1 
ATOM   9456  C  CD  . LYS I  1 92  ? 35.122  232.331 65.512 1.00 56.43 ?  91  LYS I CD  1 
ATOM   9457  C  CE  . LYS I  1 92  ? 35.353  233.710 64.880 1.00 46.28 ?  91  LYS I CE  1 
ATOM   9458  N  NZ  . LYS I  1 92  ? 34.810  234.820 65.715 1.00 59.19 ?  91  LYS I NZ  1 
ATOM   9459  N  N   . ASP I  1 93  ? 34.369  226.538 64.631 1.00 39.27 ?  92  ASP I N   1 
ATOM   9460  C  CA  . ASP I  1 93  ? 34.096  225.314 65.369 1.00 44.46 ?  92  ASP I CA  1 
ATOM   9461  C  C   . ASP I  1 93  ? 34.835  224.120 64.793 1.00 37.24 ?  92  ASP I C   1 
ATOM   9462  O  O   . ASP I  1 93  ? 34.640  223.000 65.267 1.00 43.52 ?  92  ASP I O   1 
ATOM   9463  C  CB  . ASP I  1 93  ? 32.591  225.036 65.386 1.00 44.24 ?  92  ASP I CB  1 
ATOM   9464  C  CG  . ASP I  1 93  ? 31.830  226.031 66.241 1.00 46.57 ?  92  ASP I CG  1 
ATOM   9465  O  OD1 . ASP I  1 93  ? 32.416  226.540 67.223 1.00 49.40 ?  92  ASP I OD1 1 
ATOM   9466  O  OD2 . ASP I  1 93  ? 30.655  226.321 65.912 1.00 51.54 ?  92  ASP I OD2 1 
ATOM   9467  N  N   . GLY I  1 94  ? 35.673  224.336 63.784 1.00 40.35 ?  93  GLY I N   1 
ATOM   9468  C  CA  . GLY I  1 94  ? 36.425  223.277 63.158 1.00 34.63 ?  93  GLY I CA  1 
ATOM   9469  C  C   . GLY I  1 94  ? 35.683  222.533 62.085 1.00 36.76 ?  93  GLY I C   1 
ATOM   9470  O  O   . GLY I  1 94  ? 36.138  221.455 61.678 1.00 37.39 ?  93  GLY I O   1 
ATOM   9471  N  N   . VAL I  1 95  ? 34.563  223.073 61.606 1.00 34.24 ?  94  VAL I N   1 
ATOM   9472  C  CA  . VAL I  1 95  ? 33.713  222.410 60.628 1.00 32.56 ?  94  VAL I CA  1 
ATOM   9473  C  C   . VAL I  1 95  ? 33.879  223.106 59.284 1.00 34.43 ?  94  VAL I C   1 
ATOM   9474  O  O   . VAL I  1 95  ? 33.686  224.324 59.174 1.00 33.28 ?  94  VAL I O   1 
ATOM   9475  C  CB  . VAL I  1 95  ? 32.247  222.411 61.081 1.00 34.81 ?  94  VAL I CB  1 
ATOM   9476  C  CG1 . VAL I  1 95  ? 31.366  221.735 60.031 1.00 32.79 ?  94  VAL I CG1 1 
ATOM   9477  C  CG2 . VAL I  1 95  ? 32.135  221.706 62.428 1.00 35.89 ?  94  VAL I CG2 1 
ATOM   9478  N  N   . ALA I  1 96  ? 34.241  222.342 58.270 1.00 31.66 ?  95  ALA I N   1 
ATOM   9479  C  CA  . ALA I  1 96  ? 34.294  222.820 56.896 1.00 36.42 ?  95  ALA I CA  1 
ATOM   9480  C  C   . ALA I  1 96  ? 33.164  222.137 56.138 1.00 39.10 ?  95  ALA I C   1 
ATOM   9481  O  O   . ALA I  1 96  ? 33.195  220.916 55.930 1.00 41.00 ?  95  ALA I O   1 
ATOM   9482  C  CB  . ALA I  1 96  ? 35.648  222.524 56.249 1.00 37.62 ?  95  ALA I CB  1 
ATOM   9483  N  N   . ASP I  1 97  ? 32.163  222.918 55.745 1.00 34.61 ?  96  ASP I N   1 
ATOM   9484  C  CA  . ASP I  1 97  ? 31.122  222.440 54.848 1.00 37.56 ?  96  ASP I CA  1 
ATOM   9485  C  C   . ASP I  1 97  ? 31.636  222.577 53.424 1.00 41.77 ?  96  ASP I C   1 
ATOM   9486  O  O   . ASP I  1 97  ? 32.030  223.668 53.002 1.00 35.95 ?  96  ASP I O   1 
ATOM   9487  C  CB  . ASP I  1 97  ? 29.831  223.227 55.040 1.00 37.74 ?  96  ASP I CB  1 
ATOM   9488  C  CG  . ASP I  1 97  ? 29.176  222.946 56.365 1.00 51.55 ?  96  ASP I CG  1 
ATOM   9489  O  OD1 . ASP I  1 97  ? 28.673  223.900 57.000 1.00 56.28 ?  96  ASP I OD1 1 
ATOM   9490  O  OD2 . ASP I  1 97  ? 29.153  221.761 56.772 1.00 55.18 ?  96  ASP I OD2 1 
ATOM   9491  N  N   . VAL I  1 98  ? 31.659  221.477 52.693 1.00 34.39 ?  97  VAL I N   1 
ATOM   9492  C  CA  . VAL I  1 98  ? 32.260  221.461 51.374 1.00 34.25 ?  97  VAL I CA  1 
ATOM   9493  C  C   . VAL I  1 98  ? 31.155  221.519 50.338 1.00 34.40 ?  97  VAL I C   1 
ATOM   9494  O  O   . VAL I  1 98  ? 30.159  220.790 50.434 1.00 30.47 ?  97  VAL I O   1 
ATOM   9495  C  CB  . VAL I  1 98  ? 33.148  220.227 51.187 1.00 39.09 ?  97  VAL I CB  1 
ATOM   9496  C  CG1 . VAL I  1 98  ? 33.811  220.270 49.820 1.00 34.88 ?  97  VAL I CG1 1 
ATOM   9497  C  CG2 . VAL I  1 98  ? 34.189  220.173 52.310 1.00 35.04 ?  97  VAL I CG2 1 
ATOM   9498  N  N   . SER I  1 99  ? 31.314  222.411 49.364 1.00 33.77 ?  98  SER I N   1 
ATOM   9499  C  CA  . SER I  1 99  ? 30.374  222.506 48.249 1.00 38.63 ?  98  SER I CA  1 
ATOM   9500  C  C   . SER I  1 99  ? 31.178  223.005 47.055 1.00 39.70 ?  98  SER I C   1 
ATOM   9501  O  O   . SER I  1 99  ? 31.540  224.189 46.987 1.00 41.40 ?  98  SER I O   1 
ATOM   9502  C  CB  . SER I  1 99  ? 29.206  223.426 48.571 1.00 41.26 ?  98  SER I CB  1 
ATOM   9503  O  OG  . SER I  1 99  ? 28.136  223.145 47.693 1.00 49.70 ?  98  SER I OG  1 
ATOM   9504  N  N   . ILE I  1 100 ? 31.463  222.087 46.136 1.00 42.24 ?  99  ILE I N   1 
ATOM   9505  C  CA  . ILE I  1 100 ? 32.402  222.288 45.040 1.00 38.81 ?  99  ILE I CA  1 
ATOM   9506  C  C   . ILE I  1 100 ? 31.780  221.704 43.787 1.00 41.20 ?  99  ILE I C   1 
ATOM   9507  O  O   . ILE I  1 100 ? 31.080  220.688 43.847 1.00 44.55 ?  99  ILE I O   1 
ATOM   9508  C  CB  . ILE I  1 100 ? 33.755  221.607 45.336 1.00 40.05 ?  99  ILE I CB  1 
ATOM   9509  C  CG1 . ILE I  1 100 ? 34.510  222.342 46.446 1.00 47.11 ?  99  ILE I CG1 1 
ATOM   9510  C  CG2 . ILE I  1 100 ? 34.612  221.492 44.099 1.00 41.81 ?  99  ILE I CG2 1 
ATOM   9511  C  CD1 . ILE I  1 100 ? 35.745  221.563 46.928 1.00 39.40 ?  99  ILE I CD1 1 
ATOM   9512  N  N   . GLU I  1 101 ? 32.016  222.352 42.654 1.00 42.21 ?  100 GLU I N   1 
ATOM   9513  C  CA  . GLU I  1 101 ? 31.711  221.779 41.352 1.00 42.83 ?  100 GLU I CA  1 
ATOM   9514  C  C   . GLU I  1 101 ? 32.989  221.825 40.531 1.00 45.45 ?  100 GLU I C   1 
ATOM   9515  O  O   . GLU I  1 101 ? 33.679  222.851 40.516 1.00 41.06 ?  100 GLU I O   1 
ATOM   9516  C  CB  . GLU I  1 101 ? 30.579  222.538 40.669 1.00 45.70 ?  100 GLU I CB  1 
ATOM   9517  C  CG  . GLU I  1 101 ? 29.881  221.752 39.578 1.00 56.93 ?  100 GLU I CG  1 
ATOM   9518  C  CD  . GLU I  1 101 ? 28.364  221.770 39.721 1.00 67.72 ?  100 GLU I CD  1 
ATOM   9519  O  OE1 . GLU I  1 101 ? 27.665  221.722 38.681 1.00 69.36 ?  100 GLU I OE1 1 
ATOM   9520  O  OE2 . GLU I  1 101 ? 27.873  221.812 40.877 1.00 71.08 ?  100 GLU I OE2 1 
ATOM   9521  N  N   . ASP I  1 102 ? 33.334  220.702 39.902 1.00 46.72 ?  101 ASP I N   1 
ATOM   9522  C  CA  . ASP I  1 102 ? 34.575  220.589 39.144 1.00 46.01 ?  101 ASP I CA  1 
ATOM   9523  C  C   . ASP I  1 102 ? 34.320  219.796 37.872 1.00 49.14 ?  101 ASP I C   1 
ATOM   9524  O  O   . ASP I  1 102 ? 33.577  218.807 37.886 1.00 47.61 ?  101 ASP I O   1 
ATOM   9525  C  CB  . ASP I  1 102 ? 35.688  219.914 39.962 1.00 46.49 ?  101 ASP I CB  1 
ATOM   9526  C  CG  . ASP I  1 102 ? 37.076  220.089 39.332 1.00 51.22 ?  101 ASP I CG  1 
ATOM   9527  O  OD1 . ASP I  1 102 ? 37.693  221.160 39.508 1.00 46.44 ?  101 ASP I OD1 1 
ATOM   9528  O  OD2 . ASP I  1 102 ? 37.552  219.148 38.655 1.00 47.84 ?  101 ASP I OD2 1 
ATOM   9529  N  N   . SER I  1 103 ? 34.941  220.231 36.774 1.00 44.30 ?  102 SER I N   1 
ATOM   9530  C  CA  . SER I  1 103 ? 34.772  219.557 35.495 1.00 52.66 ?  102 SER I CA  1 
ATOM   9531  C  C   . SER I  1 103 ? 36.059  218.918 34.991 1.00 49.01 ?  102 SER I C   1 
ATOM   9532  O  O   . SER I  1 103 ? 36.062  218.344 33.892 1.00 52.03 ?  102 SER I O   1 
ATOM   9533  C  CB  . SER I  1 103 ? 34.216  220.534 34.445 1.00 51.90 ?  102 SER I CB  1 
ATOM   9534  O  OG  . SER I  1 103 ? 35.036  221.686 34.340 1.00 62.14 ?  102 SER I OG  1 
ATOM   9535  N  N   . VAL I  1 104 ? 37.141  218.984 35.763 1.00 47.09 ?  103 VAL I N   1 
ATOM   9536  C  CA  . VAL I  1 104 ? 38.373  218.275 35.423 1.00 47.20 ?  103 VAL I CA  1 
ATOM   9537  C  C   . VAL I  1 104 ? 38.386  216.866 36.019 1.00 48.21 ?  103 VAL I C   1 
ATOM   9538  O  O   . VAL I  1 104 ? 38.709  215.895 35.335 1.00 49.31 ?  103 VAL I O   1 
ATOM   9539  C  CB  . VAL I  1 104 ? 39.589  219.100 35.889 1.00 45.10 ?  103 VAL I CB  1 
ATOM   9540  C  CG1 . VAL I  1 104 ? 40.860  218.259 35.850 1.00 50.02 ?  103 VAL I CG1 1 
ATOM   9541  C  CG2 . VAL I  1 104 ? 39.726  220.345 35.045 1.00 46.71 ?  103 VAL I CG2 1 
ATOM   9542  N  N   . ILE I  1 105 ? 38.047  216.722 37.306 1.00 48.40 ?  104 ILE I N   1 
ATOM   9543  C  CA  . ILE I  1 105 ? 37.839  215.383 37.872 1.00 48.07 ?  104 ILE I CA  1 
ATOM   9544  C  C   . ILE I  1 105 ? 36.634  214.722 37.214 1.00 47.30 ?  104 ILE I C   1 
ATOM   9545  O  O   . ILE I  1 105 ? 35.760  215.378 36.627 1.00 48.67 ?  104 ILE I O   1 
ATOM   9546  C  CB  . ILE I  1 105 ? 37.678  215.434 39.402 1.00 44.93 ?  104 ILE I CB  1 
ATOM   9547  C  CG1 . ILE I  1 105 ? 36.393  216.180 39.809 1.00 40.36 ?  104 ILE I CG1 1 
ATOM   9548  C  CG2 . ILE I  1 105 ? 38.905  216.001 40.068 1.00 45.69 ?  104 ILE I CG2 1 
ATOM   9549  C  CD1 . ILE I  1 105 ? 35.837  215.745 41.151 1.00 42.48 ?  104 ILE I CD1 1 
ATOM   9550  N  N   . SER I  1 106 ? 36.600  213.394 37.289 1.00 46.28 ?  105 SER I N   1 
ATOM   9551  C  CA  . SER I  1 106 ? 35.491  212.656 36.705 1.00 45.38 ?  105 SER I CA  1 
ATOM   9552  C  C   . SER I  1 106 ? 35.273  211.380 37.498 1.00 45.03 ?  105 SER I C   1 
ATOM   9553  O  O   . SER I  1 106 ? 36.175  210.889 38.181 1.00 45.24 ?  105 SER I O   1 
ATOM   9554  C  CB  . SER I  1 106 ? 35.739  212.333 35.228 1.00 42.94 ?  105 SER I CB  1 
ATOM   9555  O  OG  . SER I  1 106 ? 34.602  211.691 34.684 1.00 50.76 ?  105 SER I OG  1 
ATOM   9556  N  N   . LEU I  1 107 ? 34.057  210.846 37.401 1.00 43.95 ?  106 LEU I N   1 
ATOM   9557  C  CA  . LEU I  1 107 ? 33.738  209.546 37.972 1.00 44.04 ?  106 LEU I CA  1 
ATOM   9558  C  C   . LEU I  1 107 ? 33.770  208.437 36.923 1.00 52.26 ?  106 LEU I C   1 
ATOM   9559  O  O   . LEU I  1 107 ? 33.174  207.372 37.133 1.00 52.36 ?  106 LEU I O   1 
ATOM   9560  C  CB  . LEU I  1 107 ? 32.377  209.594 38.670 1.00 45.96 ?  106 LEU I CB  1 
ATOM   9561  C  CG  . LEU I  1 107 ? 32.333  210.585 39.835 1.00 42.45 ?  106 LEU I CG  1 
ATOM   9562  C  CD1 . LEU I  1 107 ? 31.065  210.408 40.659 1.00 42.69 ?  106 LEU I CD1 1 
ATOM   9563  C  CD2 . LEU I  1 107 ? 33.567  210.417 40.694 1.00 38.08 ?  106 LEU I CD2 1 
ATOM   9564  N  N   . SER I  1 108 ? 34.451  208.668 35.801 1.00 48.84 ?  107 SER I N   1 
ATOM   9565  C  CA  . SER I  1 108 ? 34.661  207.641 34.790 1.00 50.52 ?  107 SER I CA  1 
ATOM   9566  C  C   . SER I  1 108 ? 35.672  208.159 33.779 1.00 51.68 ?  107 SER I C   1 
ATOM   9567  O  O   . SER I  1 108 ? 35.816  209.370 33.600 1.00 57.93 ?  107 SER I O   1 
ATOM   9568  C  CB  . SER I  1 108 ? 33.355  207.267 34.090 1.00 47.34 ?  107 SER I CB  1 
ATOM   9569  O  OG  . SER I  1 108 ? 33.260  207.946 32.860 1.00 55.85 ?  107 SER I OG  1 
ATOM   9570  N  N   . GLY I  1 109 ? 36.377  207.237 33.136 1.00 55.74 ?  108 GLY I N   1 
ATOM   9571  C  CA  . GLY I  1 109 ? 37.293  207.593 32.071 1.00 43.74 ?  108 GLY I CA  1 
ATOM   9572  C  C   . GLY I  1 109 ? 38.720  207.788 32.541 1.00 53.93 ?  108 GLY I C   1 
ATOM   9573  O  O   . GLY I  1 109 ? 39.152  207.304 33.591 1.00 56.12 ?  108 GLY I O   1 
ATOM   9574  N  N   . ASP I  1 110 ? 39.465  208.540 31.729 1.00 56.14 ?  109 ASP I N   1 
ATOM   9575  C  CA  . ASP I  1 110 ? 40.891  208.732 31.969 1.00 58.24 ?  109 ASP I CA  1 
ATOM   9576  C  C   . ASP I  1 110 ? 41.172  209.608 33.182 1.00 62.54 ?  109 ASP I C   1 
ATOM   9577  O  O   . ASP I  1 110 ? 42.272  209.530 33.743 1.00 64.03 ?  109 ASP I O   1 
ATOM   9578  C  CB  . ASP I  1 110 ? 41.548  209.339 30.722 1.00 67.53 ?  109 ASP I CB  1 
ATOM   9579  C  CG  . ASP I  1 110 ? 41.853  208.291 29.649 1.00 74.39 ?  109 ASP I CG  1 
ATOM   9580  O  OD1 . ASP I  1 110 ? 41.045  207.347 29.495 1.00 71.25 ?  109 ASP I OD1 1 
ATOM   9581  O  OD2 . ASP I  1 110 ? 42.893  208.413 28.960 1.00 80.39 ?  109 ASP I OD2 1 
ATOM   9582  N  N   . HIS I  1 111 ? 40.220  210.446 33.589 1.00 53.83 ?  110 HIS I N   1 
ATOM   9583  C  CA  . HIS I  1 111 ? 40.385  211.279 34.772 1.00 56.97 ?  110 HIS I CA  1 
ATOM   9584  C  C   . HIS I  1 111 ? 39.640  210.727 35.985 1.00 56.13 ?  110 HIS I C   1 
ATOM   9585  O  O   . HIS I  1 111 ? 39.518  211.429 36.998 1.00 53.33 ?  110 HIS I O   1 
ATOM   9586  C  CB  . HIS I  1 111 ? 39.925  212.714 34.476 1.00 55.93 ?  110 HIS I CB  1 
ATOM   9587  C  CG  . HIS I  1 111 ? 40.783  213.436 33.479 1.00 65.90 ?  110 HIS I CG  1 
ATOM   9588  N  ND1 . HIS I  1 111 ? 40.639  214.781 33.208 1.00 64.59 ?  110 HIS I ND1 1 
ATOM   9589  C  CD2 . HIS I  1 111 ? 41.794  212.999 32.688 1.00 63.83 ?  110 HIS I CD2 1 
ATOM   9590  C  CE1 . HIS I  1 111 ? 41.526  215.143 32.297 1.00 65.08 ?  110 HIS I CE1 1 
ATOM   9591  N  NE2 . HIS I  1 111 ? 42.239  214.081 31.965 1.00 67.59 ?  110 HIS I NE2 1 
ATOM   9592  N  N   . CYS I  1 112 ? 39.159  209.483 35.911 1.00 53.63 ?  111 CYS I N   1 
ATOM   9593  C  CA  . CYS I  1 112 ? 38.324  208.932 36.972 1.00 48.94 ?  111 CYS I CA  1 
ATOM   9594  C  C   . CYS I  1 112 ? 39.068  208.922 38.305 1.00 44.78 ?  111 CYS I C   1 
ATOM   9595  O  O   . CYS I  1 112 ? 40.249  208.567 38.378 1.00 43.11 ?  111 CYS I O   1 
ATOM   9596  C  CB  . CYS I  1 112 ? 37.868  207.515 36.608 1.00 48.86 ?  111 CYS I CB  1 
ATOM   9597  S  SG  . CYS I  1 112 ? 36.794  206.759 37.830 1.00 60.34 ?  111 CYS I SG  1 
ATOM   9598  N  N   . ILE I  1 113 ? 38.375  209.335 39.363 1.00 42.76 ?  112 ILE I N   1 
ATOM   9599  C  CA  . ILE I  1 113 ? 38.947  209.376 40.704 1.00 41.28 ?  112 ILE I CA  1 
ATOM   9600  C  C   . ILE I  1 113 ? 38.436  208.255 41.593 1.00 41.25 ?  112 ILE I C   1 
ATOM   9601  O  O   . ILE I  1 113 ? 38.848  208.167 42.767 1.00 38.95 ?  112 ILE I O   1 
ATOM   9602  C  CB  . ILE I  1 113 ? 38.693  210.740 41.370 1.00 40.69 ?  112 ILE I CB  1 
ATOM   9603  C  CG1 . ILE I  1 113 ? 37.189  210.960 41.543 1.00 39.48 ?  112 ILE I CG1 1 
ATOM   9604  C  CG2 . ILE I  1 113 ? 39.351  211.854 40.555 1.00 43.41 ?  112 ILE I CG2 1 
ATOM   9605  C  CD1 . ILE I  1 113 ? 36.847  212.155 42.429 1.00 36.77 ?  112 ILE I CD1 1 
ATOM   9606  N  N   . ILE I  1 114 ? 37.531  207.410 41.093 1.00 43.01 ?  113 ILE I N   1 
ATOM   9607  C  CA  . ILE I  1 114 ? 37.128  206.232 41.851 1.00 39.29 ?  113 ILE I CA  1 
ATOM   9608  C  C   . ILE I  1 114 ? 38.358  205.393 42.141 1.00 43.15 ?  113 ILE I C   1 
ATOM   9609  O  O   . ILE I  1 114 ? 39.207  205.179 41.270 1.00 45.12 ?  113 ILE I O   1 
ATOM   9610  C  CB  . ILE I  1 114 ? 36.090  205.396 41.087 1.00 43.30 ?  113 ILE I CB  1 
ATOM   9611  C  CG1 . ILE I  1 114 ? 34.901  206.258 40.676 1.00 43.50 ?  113 ILE I CG1 1 
ATOM   9612  C  CG2 . ILE I  1 114 ? 35.662  204.188 41.931 1.00 38.59 ?  113 ILE I CG2 1 
ATOM   9613  C  CD1 . ILE I  1 114 ? 34.027  206.613 41.800 1.00 43.34 ?  113 ILE I CD1 1 
ATOM   9614  N  N   . GLY I  1 115 ? 38.468  204.915 43.369 1.00 45.33 ?  114 GLY I N   1 
ATOM   9615  C  CA  . GLY I  1 115 ? 39.595  204.088 43.720 1.00 44.57 ?  114 GLY I CA  1 
ATOM   9616  C  C   . GLY I  1 115 ? 40.811  204.853 44.167 1.00 42.62 ?  114 GLY I C   1 
ATOM   9617  O  O   . GLY I  1 115 ? 41.815  204.231 44.527 1.00 44.13 ?  114 GLY I O   1 
ATOM   9618  N  N   . ARG I  1 116 ? 40.760  206.173 44.165 1.00 40.46 ?  115 ARG I N   1 
ATOM   9619  C  CA  . ARG I  1 116 ? 41.882  206.981 44.610 1.00 43.13 ?  115 ARG I CA  1 
ATOM   9620  C  C   . ARG I  1 116 ? 41.548  207.563 45.974 1.00 43.53 ?  115 ARG I C   1 
ATOM   9621  O  O   . ARG I  1 116 ? 40.496  207.270 46.548 1.00 42.75 ?  115 ARG I O   1 
ATOM   9622  C  CB  . ARG I  1 116 ? 42.209  208.047 43.564 1.00 41.91 ?  115 ARG I CB  1 
ATOM   9623  C  CG  . ARG I  1 116 ? 42.316  207.429 42.164 1.00 41.27 ?  115 ARG I CG  1 
ATOM   9624  C  CD  . ARG I  1 116 ? 42.879  208.379 41.115 1.00 45.97 ?  115 ARG I CD  1 
ATOM   9625  N  NE  . ARG I  1 116 ? 42.868  207.769 39.787 1.00 44.20 ?  115 ARG I NE  1 
ATOM   9626  C  CZ  . ARG I  1 116 ? 43.835  206.991 39.316 1.00 44.67 ?  115 ARG I CZ  1 
ATOM   9627  N  NH1 . ARG I  1 116 ? 44.914  206.718 40.039 1.00 45.07 ?  115 ARG I NH1 1 
ATOM   9628  N  NH2 . ARG I  1 116 ? 43.717  206.475 38.094 1.00 42.90 ?  115 ARG I NH2 1 
ATOM   9629  N  N   . THR I  1 117 ? 42.454  208.378 46.507 1.00 36.06 ?  116 THR I N   1 
ATOM   9630  C  CA  . THR I  1 117 ? 42.321  208.881 47.865 1.00 44.00 ?  116 THR I CA  1 
ATOM   9631  C  C   . THR I  1 117 ? 42.011  210.374 47.856 1.00 46.80 ?  116 THR I C   1 
ATOM   9632  O  O   . THR I  1 117 ? 42.670  211.146 47.154 1.00 42.78 ?  116 THR I O   1 
ATOM   9633  C  CB  . THR I  1 117 ? 43.590  208.612 48.672 1.00 46.35 ?  116 THR I CB  1 
ATOM   9634  O  OG1 . THR I  1 117 ? 43.809  207.194 48.758 1.00 47.80 ?  116 THR I OG1 1 
ATOM   9635  C  CG2 . THR I  1 117 ? 43.438  209.172 50.071 1.00 40.76 ?  116 THR I CG2 1 
ATOM   9636  N  N   . LEU I  1 118 ? 41.004  210.769 48.630 1.00 42.61 ?  117 LEU I N   1 
ATOM   9637  C  CA  . LEU I  1 118 ? 40.758  212.172 48.922 1.00 39.20 ?  117 LEU I CA  1 
ATOM   9638  C  C   . LEU I  1 118 ? 41.484  212.511 50.216 1.00 39.29 ?  117 LEU I C   1 
ATOM   9639  O  O   . LEU I  1 118 ? 41.415  211.749 51.182 1.00 40.64 ?  117 LEU I O   1 
ATOM   9640  C  CB  . LEU I  1 118 ? 39.254  212.436 49.039 1.00 37.63 ?  117 LEU I CB  1 
ATOM   9641  C  CG  . LEU I  1 118 ? 38.795  213.873 49.304 1.00 40.41 ?  117 LEU I CG  1 
ATOM   9642  C  CD1 . LEU I  1 118 ? 39.122  214.786 48.114 1.00 39.69 ?  117 LEU I CD1 1 
ATOM   9643  C  CD2 . LEU I  1 118 ? 37.300  213.880 49.593 1.00 35.86 ?  117 LEU I CD2 1 
ATOM   9644  N  N   . VAL I  1 119 ? 42.204  213.632 50.226 1.00 39.84 ?  118 VAL I N   1 
ATOM   9645  C  CA  . VAL I  1 119 ? 43.003  214.043 51.378 1.00 34.90 ?  118 VAL I CA  1 
ATOM   9646  C  C   . VAL I  1 119 ? 42.695  215.494 51.713 1.00 36.65 ?  118 VAL I C   1 
ATOM   9647  O  O   . VAL I  1 119 ? 42.682  216.351 50.824 1.00 38.54 ?  118 VAL I O   1 
ATOM   9648  C  CB  . VAL I  1 119 ? 44.516  213.902 51.113 1.00 43.30 ?  118 VAL I CB  1 
ATOM   9649  C  CG1 . VAL I  1 119 ? 45.295  214.195 52.390 1.00 43.14 ?  118 VAL I CG1 1 
ATOM   9650  C  CG2 . VAL I  1 119 ? 44.859  212.526 50.549 1.00 42.77 ?  118 VAL I CG2 1 
ATOM   9651  N  N   . VAL I  1 120 ? 42.489  215.773 52.997 1.00 34.45 ?  119 VAL I N   1 
ATOM   9652  C  CA  . VAL I  1 120 ? 42.395  217.135 53.513 1.00 38.84 ?  119 VAL I CA  1 
ATOM   9653  C  C   . VAL I  1 120 ? 43.677  217.423 54.292 1.00 41.99 ?  119 VAL I C   1 
ATOM   9654  O  O   . VAL I  1 120 ? 44.089  216.619 55.142 1.00 44.52 ?  119 VAL I O   1 
ATOM   9655  C  CB  . VAL I  1 120 ? 41.139  217.330 54.384 1.00 35.52 ?  119 VAL I CB  1 
ATOM   9656  C  CG1 . VAL I  1 120 ? 41.019  216.238 55.456 1.00 41.84 ?  119 VAL I CG1 1 
ATOM   9657  C  CG2 . VAL I  1 120 ? 41.143  218.721 55.026 1.00 36.51 ?  119 VAL I CG2 1 
ATOM   9658  N  N   . HIS I  1 121 ? 44.315  218.558 53.993 1.00 38.21 ?  120 HIS I N   1 
ATOM   9659  C  CA  . HIS I  1 121 ? 45.670  218.835 54.452 1.00 43.96 ?  120 HIS I CA  1 
ATOM   9660  C  C   . HIS I  1 121 ? 45.711  219.801 55.637 1.00 42.82 ?  120 HIS I C   1 
ATOM   9661  O  O   . HIS I  1 121 ? 44.723  220.440 56.008 1.00 41.50 ?  120 HIS I O   1 
ATOM   9662  C  CB  . HIS I  1 121 ? 46.513  219.379 53.296 1.00 41.59 ?  120 HIS I CB  1 
ATOM   9663  C  CG  . HIS I  1 121 ? 46.862  218.339 52.280 1.00 45.09 ?  120 HIS I CG  1 
ATOM   9664  N  ND1 . HIS I  1 121 ? 48.050  217.637 52.309 1.00 44.97 ?  120 HIS I ND1 1 
ATOM   9665  C  CD2 . HIS I  1 121 ? 46.169  217.865 51.218 1.00 43.38 ?  120 HIS I CD2 1 
ATOM   9666  C  CE1 . HIS I  1 121 ? 48.078  216.784 51.300 1.00 48.10 ?  120 HIS I CE1 1 
ATOM   9667  N  NE2 . HIS I  1 121 ? 46.952  216.908 50.616 1.00 50.58 ?  120 HIS I NE2 1 
ATOM   9668  N  N   . GLU I  1 122 ? 46.909  219.916 56.213 1.00 42.55 ?  121 GLU I N   1 
ATOM   9669  C  CA  . GLU I  1 122 ? 47.106  220.666 57.448 1.00 44.42 ?  121 GLU I CA  1 
ATOM   9670  C  C   . GLU I  1 122 ? 47.023  222.179 57.238 1.00 42.07 ?  121 GLU I C   1 
ATOM   9671  O  O   . GLU I  1 122 ? 46.607  222.904 58.148 1.00 45.65 ?  121 GLU I O   1 
ATOM   9672  C  CB  . GLU I  1 122 ? 48.452  220.260 58.052 1.00 49.58 ?  121 GLU I CB  1 
ATOM   9673  C  CG  . GLU I  1 122 ? 49.131  221.286 58.946 1.00 55.51 ?  121 GLU I CG  1 
ATOM   9674  C  CD  . GLU I  1 122 ? 50.654  221.106 59.006 1.00 63.08 ?  121 GLU I CD  1 
ATOM   9675  O  OE1 . GLU I  1 122 ? 51.280  221.669 59.936 1.00 64.29 ?  121 GLU I OE1 1 
ATOM   9676  O  OE2 . GLU I  1 122 ? 51.220  220.410 58.127 1.00 64.06 ?  121 GLU I OE2 1 
ATOM   9677  N  N   . LYS I  1 123 ? 47.398  222.678 56.064 1.00 45.39 ?  122 LYS I N   1 
ATOM   9678  C  CA  . LYS I  1 123 ? 47.493  224.118 55.847 1.00 47.13 ?  122 LYS I CA  1 
ATOM   9679  C  C   . LYS I  1 123 ? 46.827  224.505 54.535 1.00 45.68 ?  122 LYS I C   1 
ATOM   9680  O  O   . LYS I  1 123 ? 46.349  223.661 53.765 1.00 47.08 ?  122 LYS I O   1 
ATOM   9681  C  CB  . LYS I  1 123 ? 48.952  224.598 55.839 1.00 47.88 ?  122 LYS I CB  1 
ATOM   9682  C  CG  . LYS I  1 123 ? 49.640  224.610 57.201 1.00 54.58 ?  122 LYS I CG  1 
ATOM   9683  C  CD  . LYS I  1 123 ? 51.097  224.207 57.060 1.00 54.81 ?  122 LYS I CD  1 
ATOM   9684  C  CE  . LYS I  1 123 ? 51.669  224.767 55.759 1.00 62.56 ?  122 LYS I CE  1 
ATOM   9685  N  NZ  . LYS I  1 123 ? 53.155  224.768 55.752 1.00 72.44 ?  122 LYS I NZ  1 
ATOM   9686  N  N   . ALA I  1 124 ? 46.826  225.803 54.265 1.00 45.18 ?  123 ALA I N   1 
ATOM   9687  C  CA  . ALA I  1 124 ? 46.207  226.294 53.047 1.00 40.99 ?  123 ALA I CA  1 
ATOM   9688  C  C   . ALA I  1 124 ? 47.032  225.890 51.831 1.00 41.53 ?  123 ALA I C   1 
ATOM   9689  O  O   . ALA I  1 124 ? 48.264  225.881 51.864 1.00 47.80 ?  123 ALA I O   1 
ATOM   9690  C  CB  . ALA I  1 124 ? 46.041  227.818 53.107 1.00 40.80 ?  123 ALA I CB  1 
ATOM   9691  N  N   . ASP I  1 125 ? 46.334  225.524 50.768 1.00 38.80 ?  124 ASP I N   1 
ATOM   9692  C  CA  . ASP I  1 125 ? 46.933  225.345 49.454 1.00 44.90 ?  124 ASP I CA  1 
ATOM   9693  C  C   . ASP I  1 125 ? 47.158  226.722 48.833 1.00 48.31 ?  124 ASP I C   1 
ATOM   9694  O  O   . ASP I  1 125 ? 46.204  227.489 48.667 1.00 48.07 ?  124 ASP I O   1 
ATOM   9695  C  CB  . ASP I  1 125 ? 45.991  224.487 48.608 1.00 44.83 ?  124 ASP I CB  1 
ATOM   9696  C  CG  . ASP I  1 125 ? 46.510  224.211 47.211 1.00 52.02 ?  124 ASP I CG  1 
ATOM   9697  O  OD1 . ASP I  1 125 ? 47.556  224.774 46.813 1.00 55.87 ?  124 ASP I OD1 1 
ATOM   9698  O  OD2 . ASP I  1 125 ? 45.846  223.416 46.500 1.00 48.93 ?  124 ASP I OD2 1 
ATOM   9699  N  N   . ASP I  1 126 ? 48.411  227.051 48.494 1.00 48.27 ?  125 ASP I N   1 
ATOM   9700  C  CA  . ASP I  1 126 ? 48.657  228.354 47.873 1.00 46.71 ?  125 ASP I CA  1 
ATOM   9701  C  C   . ASP I  1 126 ? 48.290  228.379 46.396 1.00 49.98 ?  125 ASP I C   1 
ATOM   9702  O  O   . ASP I  1 126 ? 48.488  229.410 45.739 1.00 51.47 ?  125 ASP I O   1 
ATOM   9703  C  CB  . ASP I  1 126 ? 50.119  228.800 48.065 1.00 49.77 ?  125 ASP I CB  1 
ATOM   9704  C  CG  . ASP I  1 126 ? 51.140  227.847 47.436 1.00 53.23 ?  125 ASP I CG  1 
ATOM   9705  O  OD1 . ASP I  1 126 ? 50.851  227.226 46.385 1.00 51.86 ?  125 ASP I OD1 1 
ATOM   9706  O  OD2 . ASP I  1 126 ? 52.256  227.735 48.006 1.00 56.61 ?  125 ASP I OD2 1 
ATOM   9707  N  N   . LEU I  1 127 ? 47.767  227.275 45.868 1.00 46.96 ?  126 LEU I N   1 
ATOM   9708  C  CA  . LEU I  1 127 ? 47.206  227.192 44.524 1.00 49.22 ?  126 LEU I CA  1 
ATOM   9709  C  C   . LEU I  1 127 ? 48.260  227.358 43.433 1.00 54.70 ?  126 LEU I C   1 
ATOM   9710  O  O   . LEU I  1 127 ? 47.921  227.673 42.283 1.00 54.88 ?  126 LEU I O   1 
ATOM   9711  C  CB  . LEU I  1 127 ? 46.076  228.213 44.332 1.00 45.46 ?  126 LEU I CB  1 
ATOM   9712  C  CG  . LEU I  1 127 ? 45.025  228.265 45.445 1.00 49.26 ?  126 LEU I CG  1 
ATOM   9713  C  CD1 . LEU I  1 127 ? 43.906  229.248 45.117 1.00 42.86 ?  126 LEU I CD1 1 
ATOM   9714  C  CD2 . LEU I  1 127 ? 44.480  226.874 45.663 1.00 42.15 ?  126 LEU I CD2 1 
ATOM   9715  N  N   . GLY I  1 128 ? 49.532  227.131 43.764 1.00 54.83 ?  127 GLY I N   1 
ATOM   9716  C  CA  . GLY I  1 128 ? 50.619  227.275 42.821 1.00 60.55 ?  127 GLY I CA  1 
ATOM   9717  C  C   . GLY I  1 128 ? 51.307  228.626 42.845 1.00 63.84 ?  127 GLY I C   1 
ATOM   9718  O  O   . GLY I  1 128 ? 52.468  228.721 42.436 1.00 64.19 ?  127 GLY I O   1 
ATOM   9719  N  N   . LYS I  1 129 ? 50.629  229.664 43.338 1.00 61.14 ?  128 LYS I N   1 
ATOM   9720  C  CA  . LYS I  1 129 ? 51.148  231.025 43.355 1.00 56.78 ?  128 LYS I CA  1 
ATOM   9721  C  C   . LYS I  1 129 ? 52.024  231.267 44.574 1.00 58.32 ?  128 LYS I C   1 
ATOM   9722  O  O   . LYS I  1 129 ? 52.068  232.383 45.107 1.00 62.90 ?  128 LYS I O   1 
ATOM   9723  C  CB  . LYS I  1 129 ? 49.997  232.033 43.341 1.00 56.31 ?  128 LYS I CB  1 
ATOM   9724  C  CG  . LYS I  1 129 ? 48.739  231.532 42.647 1.00 56.10 ?  128 LYS I CG  1 
ATOM   9725  C  CD  . LYS I  1 129 ? 48.258  232.530 41.595 1.00 60.72 ?  128 LYS I CD  1 
ATOM   9726  C  CE  . LYS I  1 129 ? 47.257  231.876 40.647 1.00 67.79 ?  128 LYS I CE  1 
ATOM   9727  N  NZ  . LYS I  1 129 ? 47.886  230.800 39.817 1.00 69.44 ?  128 LYS I NZ  1 
ATOM   9728  N  N   . GLY I  1 130 ? 52.713  230.226 45.043 1.00 56.27 ?  129 GLY I N   1 
ATOM   9729  C  CA  . GLY I  1 130 ? 53.579  230.396 46.195 1.00 56.44 ?  129 GLY I CA  1 
ATOM   9730  C  C   . GLY I  1 130 ? 54.946  230.927 45.818 1.00 64.97 ?  129 GLY I C   1 
ATOM   9731  O  O   . GLY I  1 130 ? 55.627  231.537 46.652 1.00 65.38 ?  129 GLY I O   1 
ATOM   9732  N  N   . GLY I  1 131 ? 55.368  230.703 44.571 1.00 61.81 ?  130 GLY I N   1 
ATOM   9733  C  CA  . GLY I  1 131 ? 56.623  231.220 44.074 1.00 66.67 ?  130 GLY I CA  1 
ATOM   9734  C  C   . GLY I  1 131 ? 57.817  230.291 44.185 1.00 71.13 ?  130 GLY I C   1 
ATOM   9735  O  O   . GLY I  1 131 ? 58.861  230.594 43.593 1.00 76.76 ?  130 GLY I O   1 
ATOM   9736  N  N   . ASN I  1 132 ? 57.710  229.175 44.914 1.00 68.19 ?  131 ASN I N   1 
ATOM   9737  C  CA  . ASN I  1 132 ? 58.830  228.256 45.110 1.00 61.82 ?  131 ASN I CA  1 
ATOM   9738  C  C   . ASN I  1 132 ? 58.566  226.922 44.412 1.00 65.97 ?  131 ASN I C   1 
ATOM   9739  O  O   . ASN I  1 132 ? 57.563  226.736 43.715 1.00 69.77 ?  131 ASN I O   1 
ATOM   9740  C  CB  . ASN I  1 132 ? 59.122  228.063 46.603 1.00 61.83 ?  131 ASN I CB  1 
ATOM   9741  C  CG  . ASN I  1 132 ? 57.894  227.632 47.409 1.00 68.79 ?  131 ASN I CG  1 
ATOM   9742  O  OD1 . ASN I  1 132 ? 57.166  226.701 47.038 1.00 67.56 ?  131 ASN I OD1 1 
ATOM   9743  N  ND2 . ASN I  1 132 ? 57.668  228.310 48.530 1.00 66.40 ?  131 ASN I ND2 1 
ATOM   9744  N  N   . GLU I  1 133 ? 59.501  225.981 44.593 1.00 67.86 ?  132 GLU I N   1 
ATOM   9745  C  CA  . GLU I  1 133 ? 59.376  224.690 43.919 1.00 62.87 ?  132 GLU I CA  1 
ATOM   9746  C  C   . GLU I  1 133 ? 58.292  223.835 44.564 1.00 60.79 ?  132 GLU I C   1 
ATOM   9747  O  O   . GLU I  1 133 ? 57.536  223.150 43.863 1.00 61.76 ?  132 GLU I O   1 
ATOM   9748  C  CB  . GLU I  1 133 ? 60.719  223.959 43.923 1.00 60.20 ?  132 GLU I CB  1 
ATOM   9749  N  N   . GLU I  1 134 ? 58.203  223.859 45.897 1.00 62.39 ?  133 GLU I N   1 
ATOM   9750  C  CA  . GLU I  1 134 ? 57.143  223.128 46.586 1.00 63.73 ?  133 GLU I CA  1 
ATOM   9751  C  C   . GLU I  1 134 ? 55.770  223.529 46.062 1.00 61.92 ?  133 GLU I C   1 
ATOM   9752  O  O   . GLU I  1 134 ? 54.945  222.672 45.719 1.00 59.22 ?  133 GLU I O   1 
ATOM   9753  C  CB  . GLU I  1 134 ? 57.226  223.375 48.092 1.00 61.26 ?  133 GLU I CB  1 
ATOM   9754  C  CG  . GLU I  1 134 ? 56.612  222.263 48.939 1.00 63.65 ?  133 GLU I CG  1 
ATOM   9755  C  CD  . GLU I  1 134 ? 57.309  220.930 48.754 1.00 71.51 ?  133 GLU I CD  1 
ATOM   9756  O  OE1 . GLU I  1 134 ? 56.875  220.142 47.875 1.00 72.11 ?  133 GLU I OE1 1 
ATOM   9757  O  OE2 . GLU I  1 134 ? 58.291  220.678 49.493 1.00 72.41 ?  133 GLU I OE2 1 
ATOM   9758  N  N   . SER I  1 135 ? 55.528  224.839 45.958 1.00 57.94 ?  134 SER I N   1 
ATOM   9759  C  CA  . SER I  1 135 ? 54.210  225.336 45.583 1.00 57.60 ?  134 SER I CA  1 
ATOM   9760  C  C   . SER I  1 135 ? 53.784  224.830 44.212 1.00 57.60 ?  134 SER I C   1 
ATOM   9761  O  O   . SER I  1 135 ? 52.586  224.643 43.963 1.00 58.35 ?  134 SER I O   1 
ATOM   9762  C  CB  . SER I  1 135 ? 54.203  226.868 45.626 1.00 60.08 ?  134 SER I CB  1 
ATOM   9763  O  OG  . SER I  1 135 ? 53.217  227.405 44.756 1.00 59.09 ?  134 SER I OG  1 
ATOM   9764  N  N   . THR I  1 136 ? 54.742  224.597 43.313 1.00 58.27 ?  135 THR I N   1 
ATOM   9765  C  CA  . THR I  1 136 ? 54.421  223.991 42.025 1.00 59.10 ?  135 THR I CA  1 
ATOM   9766  C  C   . THR I  1 136 ? 54.035  222.523 42.156 1.00 58.23 ?  135 THR I C   1 
ATOM   9767  O  O   . THR I  1 136 ? 53.501  221.945 41.199 1.00 60.28 ?  135 THR I O   1 
ATOM   9768  C  CB  . THR I  1 136 ? 55.612  224.111 41.076 1.00 62.16 ?  135 THR I CB  1 
ATOM   9769  O  OG1 . THR I  1 136 ? 56.654  223.228 41.520 1.00 63.97 ?  135 THR I OG1 1 
ATOM   9770  C  CG2 . THR I  1 136 ? 56.132  225.541 41.055 1.00 57.07 ?  135 THR I CG2 1 
ATOM   9771  N  N   . LYS I  1 137 ? 54.299  221.908 43.308 1.00 53.90 ?  136 LYS I N   1 
ATOM   9772  C  CA  . LYS I  1 137 ? 54.080  220.483 43.494 1.00 57.32 ?  136 LYS I CA  1 
ATOM   9773  C  C   . LYS I  1 137 ? 52.915  220.201 44.436 1.00 60.34 ?  136 LYS I C   1 
ATOM   9774  O  O   . LYS I  1 137 ? 51.965  219.507 44.055 1.00 59.68 ?  136 LYS I O   1 
ATOM   9775  C  CB  . LYS I  1 137 ? 55.370  219.831 44.011 1.00 55.06 ?  136 LYS I CB  1 
ATOM   9776  C  CG  . LYS I  1 137 ? 56.291  219.306 42.892 1.00 59.16 ?  136 LYS I CG  1 
ATOM   9777  C  CD  . LYS I  1 137 ? 57.749  219.163 43.349 1.00 58.56 ?  136 LYS I CD  1 
ATOM   9778  C  CE  . LYS I  1 137 ? 57.845  219.142 44.875 1.00 68.50 ?  136 LYS I CE  1 
ATOM   9779  N  NZ  . LYS I  1 137 ? 59.239  219.134 45.417 1.00 73.73 ?  136 LYS I NZ  1 
ATOM   9780  N  N   . THR I  1 138 ? 52.962  220.734 45.660 1.00 53.65 ?  137 THR I N   1 
ATOM   9781  C  CA  . THR I  1 138 ? 51.975  220.449 46.690 1.00 54.60 ?  137 THR I CA  1 
ATOM   9782  C  C   . THR I  1 138 ? 51.153  221.661 47.107 1.00 59.98 ?  137 THR I C   1 
ATOM   9783  O  O   . THR I  1 138 ? 50.252  221.519 47.949 1.00 54.28 ?  137 THR I O   1 
ATOM   9784  C  CB  . THR I  1 138 ? 52.666  219.883 47.936 1.00 53.06 ?  137 THR I CB  1 
ATOM   9785  O  OG1 . THR I  1 138 ? 53.230  220.967 48.687 1.00 52.09 ?  137 THR I OG1 1 
ATOM   9786  C  CG2 . THR I  1 138 ? 53.763  218.909 47.536 1.00 57.31 ?  137 THR I CG2 1 
ATOM   9787  N  N   . GLY I  1 139 ? 51.450  222.844 46.573 1.00 52.98 ?  138 GLY I N   1 
ATOM   9788  C  CA  . GLY I  1 139 ? 50.821  224.064 47.037 1.00 53.94 ?  138 GLY I CA  1 
ATOM   9789  C  C   . GLY I  1 139 ? 51.163  224.418 48.473 1.00 49.26 ?  138 GLY I C   1 
ATOM   9790  O  O   . GLY I  1 139 ? 50.533  225.303 49.056 1.00 49.59 ?  138 GLY I O   1 
ATOM   9791  N  N   . ASN I  1 140 ? 52.151  223.725 49.048 1.00 50.71 ?  139 ASN I N   1 
ATOM   9792  C  CA  . ASN I  1 140 ? 52.591  223.933 50.429 1.00 45.10 ?  139 ASN I CA  1 
ATOM   9793  C  C   . ASN I  1 140 ? 51.484  223.637 51.442 1.00 52.57 ?  139 ASN I C   1 
ATOM   9794  O  O   . ASN I  1 140 ? 51.479  224.185 52.551 1.00 56.98 ?  139 ASN I O   1 
ATOM   9795  C  CB  . ASN I  1 140 ? 53.141  225.352 50.637 1.00 53.78 ?  139 ASN I CB  1 
ATOM   9796  C  CG  . ASN I  1 140 ? 54.483  225.571 49.937 1.00 58.63 ?  139 ASN I CG  1 
ATOM   9797  O  OD1 . ASN I  1 140 ? 55.518  225.060 50.378 1.00 56.87 ?  139 ASN I OD1 1 
ATOM   9798  N  ND2 . ASN I  1 140 ? 54.463  226.327 48.833 1.00 54.23 ?  139 ASN I ND2 1 
ATOM   9799  N  N   . ALA I  1 141 ? 50.556  222.742 51.091 1.00 53.49 ?  140 ALA I N   1 
ATOM   9800  C  CA  . ALA I  1 141 ? 49.435  222.418 51.975 1.00 45.41 ?  140 ALA I CA  1 
ATOM   9801  C  C   . ALA I  1 141 ? 49.848  221.632 53.216 1.00 51.87 ?  140 ALA I C   1 
ATOM   9802  O  O   . ALA I  1 141 ? 49.036  221.492 54.143 1.00 49.78 ?  140 ALA I O   1 
ATOM   9803  C  CB  . ALA I  1 141 ? 48.366  221.646 51.205 1.00 47.74 ?  140 ALA I CB  1 
ATOM   9804  N  N   . GLY I  1 142 ? 51.079  221.129 53.274 1.00 51.75 ?  141 GLY I N   1 
ATOM   9805  C  CA  . GLY I  1 142 ? 51.541  220.504 54.498 1.00 46.57 ?  141 GLY I CA  1 
ATOM   9806  C  C   . GLY I  1 142 ? 51.087  219.059 54.638 1.00 45.58 ?  141 GLY I C   1 
ATOM   9807  O  O   . GLY I  1 142 ? 50.750  218.366 53.669 1.00 54.86 ?  141 GLY I O   1 
ATOM   9808  N  N   . SER I  1 143 ? 51.057  218.614 55.885 1.00 49.01 ?  142 SER I N   1 
ATOM   9809  C  CA  . SER I  1 143 ? 50.820  217.215 56.175 1.00 51.74 ?  142 SER I CA  1 
ATOM   9810  C  C   . SER I  1 143 ? 49.371  216.825 55.873 1.00 55.56 ?  142 SER I C   1 
ATOM   9811  O  O   . SER I  1 143 ? 48.482  217.666 55.678 1.00 50.81 ?  142 SER I O   1 
ATOM   9812  C  CB  . SER I  1 143 ? 51.165  216.923 57.628 1.00 45.49 ?  142 SER I CB  1 
ATOM   9813  O  OG  . SER I  1 143 ? 50.083  217.274 58.466 1.00 57.91 ?  142 SER I OG  1 
ATOM   9814  N  N   . ARG I  1 144 ? 49.144  215.514 55.833 1.00 48.24 ?  143 ARG I N   1 
ATOM   9815  C  CA  . ARG I  1 144 ? 47.835  214.954 55.539 1.00 44.15 ?  143 ARG I CA  1 
ATOM   9816  C  C   . ARG I  1 144 ? 47.131  214.659 56.857 1.00 45.32 ?  143 ARG I C   1 
ATOM   9817  O  O   . ARG I  1 144 ? 47.656  213.910 57.684 1.00 51.54 ?  143 ARG I O   1 
ATOM   9818  C  CB  . ARG I  1 144 ? 47.996  213.702 54.687 1.00 44.82 ?  143 ARG I CB  1 
ATOM   9819  C  CG  . ARG I  1 144 ? 48.734  213.997 53.385 1.00 45.92 ?  143 ARG I CG  1 
ATOM   9820  C  CD  . ARG I  1 144 ? 49.363  212.771 52.748 1.00 45.64 ?  143 ARG I CD  1 
ATOM   9821  N  NE  . ARG I  1 144 ? 50.256  213.177 51.667 1.00 51.65 ?  143 ARG I NE  1 
ATOM   9822  C  CZ  . ARG I  1 144 ? 50.437  212.503 50.540 1.00 50.14 ?  143 ARG I CZ  1 
ATOM   9823  N  NH1 . ARG I  1 144 ? 49.811  211.357 50.307 1.00 48.90 ?  143 ARG I NH1 1 
ATOM   9824  N  NH2 . ARG I  1 144 ? 51.257  212.997 49.617 1.00 48.00 ?  143 ARG I NH2 1 
ATOM   9825  N  N   . LEU I  1 145 ? 45.964  215.276 57.067 1.00 44.52 ?  144 LEU I N   1 
ATOM   9826  C  CA  . LEU I  1 145 ? 45.256  215.149 58.341 1.00 42.79 ?  144 LEU I CA  1 
ATOM   9827  C  C   . LEU I  1 145 ? 44.278  213.984 58.343 1.00 38.99 ?  144 LEU I C   1 
ATOM   9828  O  O   . LEU I  1 145 ? 44.055  213.350 59.385 1.00 43.68 ?  144 LEU I O   1 
ATOM   9829  C  CB  . LEU I  1 145 ? 44.489  216.436 58.658 1.00 39.89 ?  144 LEU I CB  1 
ATOM   9830  C  CG  . LEU I  1 145 ? 45.262  217.742 58.807 1.00 43.20 ?  144 LEU I CG  1 
ATOM   9831  C  CD1 . LEU I  1 145 ? 44.278  218.878 59.031 1.00 44.26 ?  144 LEU I CD1 1 
ATOM   9832  C  CD2 . LEU I  1 145 ? 46.220  217.650 59.965 1.00 41.49 ?  144 LEU I CD2 1 
ATOM   9833  N  N   . ALA I  1 146 ? 43.664  213.719 57.200 1.00 41.79 ?  145 ALA I N   1 
ATOM   9834  C  CA  . ALA I  1 146 ? 42.668  212.669 57.079 1.00 43.23 ?  145 ALA I CA  1 
ATOM   9835  C  C   . ALA I  1 146 ? 42.542  212.343 55.609 1.00 39.51 ?  145 ALA I C   1 
ATOM   9836  O  O   . ALA I  1 146 ? 42.810  213.185 54.747 1.00 41.56 ?  145 ALA I O   1 
ATOM   9837  C  CB  . ALA I  1 146 ? 41.309  213.088 57.659 1.00 38.92 ?  145 ALA I CB  1 
ATOM   9838  N  N   . CYS I  1 147 ? 42.117  211.115 55.330 1.00 36.04 ?  146 CYS I N   1 
ATOM   9839  C  CA  . CYS I  1 147 ? 41.994  210.684 53.946 1.00 34.79 ?  146 CYS I CA  1 
ATOM   9840  C  C   . CYS I  1 147 ? 41.022  209.517 53.894 1.00 35.27 ?  146 CYS I C   1 
ATOM   9841  O  O   . CYS I  1 147 ? 40.655  208.944 54.920 1.00 36.45 ?  146 CYS I O   1 
ATOM   9842  C  CB  . CYS I  1 147 ? 43.349  210.281 53.369 1.00 42.31 ?  146 CYS I CB  1 
ATOM   9843  S  SG  . CYS I  1 147 ? 44.182  209.031 54.367 1.00 49.15 ?  146 CYS I SG  1 
ATOM   9844  N  N   . GLY I  1 148 ? 40.627  209.156 52.682 1.00 43.51 ?  147 GLY I N   1 
ATOM   9845  C  CA  . GLY I  1 148 ? 39.785  207.991 52.513 1.00 38.12 ?  147 GLY I CA  1 
ATOM   9846  C  C   . GLY I  1 148 ? 39.775  207.574 51.068 1.00 38.52 ?  147 GLY I C   1 
ATOM   9847  O  O   . GLY I  1 148 ? 40.033  208.402 50.195 1.00 41.00 ?  147 GLY I O   1 
ATOM   9848  N  N   . VAL I  1 149 ? 39.505  206.313 50.796 1.00 34.50 ?  148 VAL I N   1 
ATOM   9849  C  CA  . VAL I  1 149 ? 39.407  205.863 49.415 1.00 37.94 ?  148 VAL I CA  1 
ATOM   9850  C  C   . VAL I  1 149 ? 38.029  206.225 48.883 1.00 39.91 ?  148 VAL I C   1 
ATOM   9851  O  O   . VAL I  1 149 ? 37.013  206.076 49.574 1.00 41.72 ?  148 VAL I O   1 
ATOM   9852  C  CB  . VAL I  1 149 ? 39.691  204.351 49.305 1.00 37.56 ?  148 VAL I CB  1 
ATOM   9853  C  CG1 . VAL I  1 149 ? 39.781  203.935 47.847 1.00 36.86 ?  148 VAL I CG1 1 
ATOM   9854  C  CG2 . VAL I  1 149 ? 40.999  204.008 50.017 1.00 39.39 ?  148 VAL I CG2 1 
ATOM   9855  N  N   . ILE I  1 150 ? 37.997  206.706 47.646 1.00 37.88 ?  149 ILE I N   1 
ATOM   9856  C  CA  . ILE I  1 150 ? 36.770  207.141 46.991 1.00 40.61 ?  149 ILE I CA  1 
ATOM   9857  C  C   . ILE I  1 150 ? 36.077  205.919 46.403 1.00 40.17 ?  149 ILE I C   1 
ATOM   9858  O  O   . ILE I  1 150 ? 36.595  205.297 45.475 1.00 39.31 ?  149 ILE I O   1 
ATOM   9859  C  CB  . ILE I  1 150 ? 37.076  208.172 45.901 1.00 38.32 ?  149 ILE I CB  1 
ATOM   9860  C  CG1 . ILE I  1 150 ? 37.864  209.335 46.518 1.00 38.86 ?  149 ILE I CG1 1 
ATOM   9861  C  CG2 . ILE I  1 150 ? 35.795  208.615 45.194 1.00 35.80 ?  149 ILE I CG2 1 
ATOM   9862  C  CD1 . ILE I  1 150 ? 37.898  210.556 45.653 1.00 44.05 ?  149 ILE I CD1 1 
ATOM   9863  N  N   . GLY I  1 151 ? 34.893  205.595 46.922 1.00 39.83 ?  150 GLY I N   1 
ATOM   9864  C  CA  . GLY I  1 151 ? 34.188  204.377 46.558 1.00 37.74 ?  150 GLY I CA  1 
ATOM   9865  C  C   . GLY I  1 151 ? 32.924  204.650 45.763 1.00 41.27 ?  150 GLY I C   1 
ATOM   9866  O  O   . GLY I  1 151 ? 32.292  205.694 45.915 1.00 37.37 ?  150 GLY I O   1 
ATOM   9867  N  N   . ILE I  1 152 ? 32.559  203.698 44.901 1.00 36.87 ?  151 ILE I N   1 
ATOM   9868  C  CA  . ILE I  1 152 ? 31.275  203.763 44.212 1.00 39.79 ?  151 ILE I CA  1 
ATOM   9869  C  C   . ILE I  1 152 ? 30.146  203.760 45.230 1.00 42.29 ?  151 ILE I C   1 
ATOM   9870  O  O   . ILE I  1 152 ? 30.159  202.978 46.190 1.00 38.01 ?  151 ILE I O   1 
ATOM   9871  C  CB  . ILE I  1 152 ? 31.144  202.584 43.246 1.00 38.56 ?  151 ILE I CB  1 
ATOM   9872  C  CG1 . ILE I  1 152 ? 32.263  202.635 42.204 1.00 42.44 ?  151 ILE I CG1 1 
ATOM   9873  C  CG2 . ILE I  1 152 ? 29.774  202.594 42.585 1.00 36.74 ?  151 ILE I CG2 1 
ATOM   9874  C  CD1 . ILE I  1 152 ? 32.301  201.408 41.297 1.00 46.11 ?  151 ILE I CD1 1 
ATOM   9875  N  N   . ALA I  1 153 ? 29.158  204.635 45.027 1.00 39.95 ?  152 ALA I N   1 
ATOM   9876  C  CA  . ALA I  1 153 ? 28.038  204.782 45.946 1.00 39.63 ?  152 ALA I CA  1 
ATOM   9877  C  C   . ALA I  1 153 ? 26.737  204.424 45.239 1.00 40.12 ?  152 ALA I C   1 
ATOM   9878  O  O   . ALA I  1 153 ? 26.642  204.454 44.011 1.00 43.53 ?  152 ALA I O   1 
ATOM   9879  C  CB  . ALA I  1 153 ? 27.959  206.206 46.514 1.00 38.75 ?  152 ALA I CB  1 
ATOM   9880  N  N   . GLN I  1 154 ? 25.732  204.060 46.027 1.00 38.42 ?  153 GLN I N   1 
ATOM   9881  C  CA  . GLN I  1 154 ? 24.451  203.693 45.440 1.00 49.31 ?  153 GLN I CA  1 
ATOM   9882  C  C   . GLN I  1 154 ? 23.717  204.943 44.981 1.00 61.27 ?  153 GLN I C   1 
ATOM   9883  O  O   . GLN I  1 154 ? 23.274  205.734 45.818 1.00 60.60 ?  153 GLN I O   1 
ATOM   9884  C  CB  . GLN I  1 154 ? 23.594  202.915 46.433 1.00 52.19 ?  153 GLN I CB  1 
ATOM   9885  C  CG  . GLN I  1 154 ? 22.283  202.425 45.851 1.00 52.43 ?  153 GLN I CG  1 
ATOM   9886  C  CD  . GLN I  1 154 ? 21.328  201.950 46.932 1.00 57.61 ?  153 GLN I CD  1 
ATOM   9887  O  OE1 . GLN I  1 154 ? 21.060  202.667 47.902 1.00 67.79 ?  153 GLN I OE1 1 
ATOM   9888  N  NE2 . GLN I  1 154 ? 20.807  200.738 46.770 1.00 59.55 ?  153 GLN I NE2 1 
ATOM   9889  O  OXT . GLN I  1 154 ? 23.558  205.184 43.777 1.00 67.27 ?  153 GLN I OXT 1 
ATOM   9890  N  N   . MET J  1 1   ? 42.919  199.429 33.180 1.00 61.13 ?  0   MET J N   1 
ATOM   9891  C  CA  . MET J  1 1   ? 43.290  200.483 34.130 1.00 75.23 ?  0   MET J CA  1 
ATOM   9892  C  C   . MET J  1 1   ? 44.388  199.995 35.078 1.00 75.14 ?  0   MET J C   1 
ATOM   9893  O  O   . MET J  1 1   ? 45.505  199.675 34.648 1.00 76.80 ?  0   MET J O   1 
ATOM   9894  C  CB  . MET J  1 1   ? 42.070  200.955 34.938 1.00 60.88 ?  0   MET J CB  1 
ATOM   9895  N  N   . ALA J  1 2   ? 44.062  199.930 36.368 1.00 68.11 ?  1   ALA J N   1 
ATOM   9896  C  CA  . ALA J  1 2   ? 45.029  199.474 37.355 1.00 66.63 ?  1   ALA J CA  1 
ATOM   9897  C  C   . ALA J  1 2   ? 45.325  197.987 37.183 1.00 61.91 ?  1   ALA J C   1 
ATOM   9898  O  O   . ALA J  1 2   ? 44.477  197.197 36.758 1.00 61.93 ?  1   ALA J O   1 
ATOM   9899  C  CB  . ALA J  1 2   ? 44.523  199.746 38.774 1.00 61.04 ?  1   ALA J CB  1 
ATOM   9900  N  N   . THR J  1 3   ? 46.557  197.614 37.502 1.00 57.53 ?  2   THR J N   1 
ATOM   9901  C  CA  . THR J  1 3   ? 46.923  196.213 37.572 1.00 55.81 ?  2   THR J CA  1 
ATOM   9902  C  C   . THR J  1 3   ? 47.247  195.775 38.992 1.00 55.38 ?  2   THR J C   1 
ATOM   9903  O  O   . THR J  1 3   ? 47.362  194.568 39.242 1.00 54.87 ?  2   THR J O   1 
ATOM   9904  C  CB  . THR J  1 3   ? 48.109  195.913 36.637 1.00 56.74 ?  2   THR J CB  1 
ATOM   9905  O  OG1 . THR J  1 3   ? 49.288  196.575 37.114 1.00 58.18 ?  2   THR J OG1 1 
ATOM   9906  C  CG2 . THR J  1 3   ? 47.797  196.371 35.207 1.00 53.88 ?  2   THR J CG2 1 
ATOM   9907  N  N   . LYS J  1 4   ? 47.395  196.716 39.923 1.00 48.00 ?  3   LYS J N   1 
ATOM   9908  C  CA  . LYS J  1 4   ? 47.501  196.410 41.341 1.00 51.49 ?  3   LYS J CA  1 
ATOM   9909  C  C   . LYS J  1 4   ? 46.427  197.176 42.100 1.00 53.70 ?  3   LYS J C   1 
ATOM   9910  O  O   . LYS J  1 4   ? 46.086  198.311 41.745 1.00 51.06 ?  3   LYS J O   1 
ATOM   9911  C  CB  . LYS J  1 4   ? 48.886  196.754 41.906 1.00 52.95 ?  3   LYS J CB  1 
ATOM   9912  C  CG  . LYS J  1 4   ? 49.957  195.715 41.607 1.00 62.26 ?  3   LYS J CG  1 
ATOM   9913  C  CD  . LYS J  1 4   ? 51.298  196.365 41.304 1.00 65.18 ?  3   LYS J CD  1 
ATOM   9914  C  CE  . LYS J  1 4   ? 52.223  196.348 42.516 1.00 62.45 ?  3   LYS J CE  1 
ATOM   9915  N  NZ  . LYS J  1 4   ? 53.282  197.411 42.413 1.00 65.59 ?  3   LYS J NZ  1 
ATOM   9916  N  N   . ALA J  1 5   ? 45.900  196.550 43.147 1.00 47.23 ?  4   ALA J N   1 
ATOM   9917  C  CA  . ALA J  1 5   ? 44.953  197.198 44.032 1.00 44.33 ?  4   ALA J CA  1 
ATOM   9918  C  C   . ALA J  1 5   ? 45.277  196.792 45.459 1.00 50.49 ?  4   ALA J C   1 
ATOM   9919  O  O   . ALA J  1 5   ? 46.075  195.877 45.703 1.00 45.78 ?  4   ALA J O   1 
ATOM   9920  C  CB  . ALA J  1 5   ? 43.512  196.850 43.656 1.00 43.74 ?  4   ALA J CB  1 
ATOM   9921  N  N   . VAL J  1 6   ? 44.668  197.501 46.415 1.00 39.73 ?  5   VAL J N   1 
ATOM   9922  C  CA  . VAL J  1 6   ? 44.913  197.247 47.828 1.00 36.95 ?  5   VAL J CA  1 
ATOM   9923  C  C   . VAL J  1 6   ? 43.699  197.708 48.620 1.00 43.72 ?  5   VAL J C   1 
ATOM   9924  O  O   . VAL J  1 6   ? 42.931  198.565 48.180 1.00 43.45 ?  5   VAL J O   1 
ATOM   9925  C  CB  . VAL J  1 6   ? 46.198  197.942 48.338 1.00 43.55 ?  5   VAL J CB  1 
ATOM   9926  C  CG1 . VAL J  1 6   ? 45.992  199.452 48.476 1.00 45.44 ?  5   VAL J CG1 1 
ATOM   9927  C  CG2 . VAL J  1 6   ? 46.631  197.340 49.656 1.00 40.86 ?  5   VAL J CG2 1 
ATOM   9928  N  N   . CYS J  1 7   ? 43.539  197.136 49.807 1.00 41.19 ?  6   CYS J N   1 
ATOM   9929  C  CA  . CYS J  1 7   ? 42.367  197.385 50.628 1.00 39.46 ?  6   CYS J CA  1 
ATOM   9930  C  C   . CYS J  1 7   ? 42.735  197.176 52.091 1.00 41.28 ?  6   CYS J C   1 
ATOM   9931  O  O   . CYS J  1 7   ? 43.307  196.142 52.454 1.00 41.79 ?  6   CYS J O   1 
ATOM   9932  C  CB  . CYS J  1 7   ? 41.220  196.458 50.207 1.00 41.18 ?  6   CYS J CB  1 
ATOM   9933  S  SG  . CYS J  1 7   ? 39.823  196.454 51.340 1.00 44.67 ?  6   CYS J SG  1 
ATOM   9934  N  N   . VAL J  1 8   ? 42.402  198.152 52.926 1.00 37.88 ?  7   VAL J N   1 
ATOM   9935  C  CA  . VAL J  1 8   ? 42.682  198.105 54.358 1.00 40.32 ?  7   VAL J CA  1 
ATOM   9936  C  C   . VAL J  1 8   ? 41.386  197.747 55.067 1.00 40.93 ?  7   VAL J C   1 
ATOM   9937  O  O   . VAL J  1 8   ? 40.403  198.498 55.005 1.00 42.39 ?  7   VAL J O   1 
ATOM   9938  C  CB  . VAL J  1 8   ? 43.240  199.447 54.862 1.00 42.38 ?  7   VAL J CB  1 
ATOM   9939  C  CG1 . VAL J  1 8   ? 43.531  199.364 56.338 1.00 36.23 ?  7   VAL J CG1 1 
ATOM   9940  C  CG2 . VAL J  1 8   ? 44.487  199.838 54.052 1.00 35.83 ?  7   VAL J CG2 1 
ATOM   9941  N  N   . LEU J  1 9   ? 41.363  196.591 55.708 1.00 42.20 ?  8   LEU J N   1 
ATOM   9942  C  CA  . LEU J  1 9   ? 40.156  196.117 56.366 1.00 43.10 ?  8   LEU J CA  1 
ATOM   9943  C  C   . LEU J  1 9   ? 40.147  196.627 57.795 1.00 38.92 ?  8   LEU J C   1 
ATOM   9944  O  O   . LEU J  1 9   ? 41.127  196.438 58.518 1.00 43.31 ?  8   LEU J O   1 
ATOM   9945  C  CB  . LEU J  1 9   ? 40.099  194.587 56.358 1.00 42.66 ?  8   LEU J CB  1 
ATOM   9946  C  CG  . LEU J  1 9   ? 39.397  193.904 55.183 1.00 39.65 ?  8   LEU J CG  1 
ATOM   9947  C  CD1 . LEU J  1 9   ? 40.054  194.299 53.918 1.00 44.73 ?  8   LEU J CD1 1 
ATOM   9948  C  CD2 . LEU J  1 9   ? 39.491  192.418 55.347 1.00 47.86 ?  8   LEU J CD2 1 
ATOM   9949  N  N   . LYS J  1 10  ? 39.055  197.291 58.193 1.00 43.09 ?  9   LYS J N   1 
ATOM   9950  C  CA  . LYS J  1 10  ? 38.853  197.723 59.580 1.00 40.89 ?  9   LYS J CA  1 
ATOM   9951  C  C   . LYS J  1 10  ? 37.383  197.551 59.940 1.00 39.09 ?  9   LYS J C   1 
ATOM   9952  O  O   . LYS J  1 10  ? 36.510  197.495 59.067 1.00 38.22 ?  9   LYS J O   1 
ATOM   9953  C  CB  . LYS J  1 10  ? 39.272  199.190 59.831 1.00 44.13 ?  9   LYS J CB  1 
ATOM   9954  C  CG  . LYS J  1 10  ? 40.606  199.613 59.185 1.00 49.70 ?  9   LYS J CG  1 
ATOM   9955  C  CD  . LYS J  1 10  ? 41.194  200.877 59.822 1.00 54.57 ?  9   LYS J CD  1 
ATOM   9956  C  CE  . LYS J  1 10  ? 42.686  201.071 59.470 1.00 57.79 ?  9   LYS J CE  1 
ATOM   9957  N  NZ  . LYS J  1 10  ? 42.950  202.398 58.784 1.00 57.32 ?  9   LYS J NZ  1 
ATOM   9958  N  N   . GLY J  1 11  ? 37.119  197.456 61.241 1.00 41.28 ?  10  GLY J N   1 
ATOM   9959  C  CA  . GLY J  1 11  ? 35.761  197.297 61.730 1.00 43.75 ?  10  GLY J CA  1 
ATOM   9960  C  C   . GLY J  1 11  ? 35.563  197.864 63.122 1.00 46.23 ?  10  GLY J C   1 
ATOM   9961  O  O   . GLY J  1 11  ? 36.462  198.523 63.655 1.00 46.08 ?  10  GLY J O   1 
ATOM   9962  N  N   . ASP J  1 12  ? 34.390  197.615 63.721 1.00 46.44 ?  11  ASP J N   1 
ATOM   9963  C  CA  . ASP J  1 12  ? 34.139  198.038 65.097 1.00 50.36 ?  11  ASP J CA  1 
ATOM   9964  C  C   . ASP J  1 12  ? 34.928  197.226 66.109 1.00 51.44 ?  11  ASP J C   1 
ATOM   9965  O  O   . ASP J  1 12  ? 35.177  197.713 67.214 1.00 57.12 ?  11  ASP J O   1 
ATOM   9966  C  CB  . ASP J  1 12  ? 32.656  197.919 65.450 1.00 54.57 ?  11  ASP J CB  1 
ATOM   9967  C  CG  . ASP J  1 12  ? 31.777  198.803 64.598 1.00 68.09 ?  11  ASP J CG  1 
ATOM   9968  O  OD1 . ASP J  1 12  ? 32.262  199.865 64.145 1.00 69.57 ?  11  ASP J OD1 1 
ATOM   9969  O  OD2 . ASP J  1 12  ? 30.596  198.436 64.391 1.00 72.20 ?  11  ASP J OD2 1 
ATOM   9970  N  N   . GLY J  1 13  ? 35.303  195.995 65.768 1.00 50.50 ?  12  GLY J N   1 
ATOM   9971  C  CA  . GLY J  1 13  ? 35.962  195.117 66.700 1.00 38.88 ?  12  GLY J CA  1 
ATOM   9972  C  C   . GLY J  1 13  ? 37.446  195.009 66.437 1.00 44.72 ?  12  GLY J C   1 
ATOM   9973  O  O   . GLY J  1 13  ? 38.076  195.910 65.872 1.00 46.08 ?  12  GLY J O   1 
ATOM   9974  N  N   . PRO J  1 14  ? 38.030  193.878 66.847 1.00 44.87 ?  13  PRO J N   1 
ATOM   9975  C  CA  . PRO J  1 14  ? 39.484  193.693 66.734 1.00 45.56 ?  13  PRO J CA  1 
ATOM   9976  C  C   . PRO J  1 14  ? 39.967  193.292 65.354 1.00 47.39 ?  13  PRO J C   1 
ATOM   9977  O  O   . PRO J  1 14  ? 41.186  193.294 65.127 1.00 50.29 ?  13  PRO J O   1 
ATOM   9978  C  CB  . PRO J  1 14  ? 39.760  192.565 67.739 1.00 46.64 ?  13  PRO J CB  1 
ATOM   9979  C  CG  . PRO J  1 14  ? 38.499  191.758 67.726 1.00 42.71 ?  13  PRO J CG  1 
ATOM   9980  C  CD  . PRO J  1 14  ? 37.384  192.772 67.576 1.00 41.93 ?  13  PRO J CD  1 
ATOM   9981  N  N   . VAL J  1 15  ? 39.068  192.940 64.434 1.00 43.08 ?  14  VAL J N   1 
ATOM   9982  C  CA  . VAL J  1 15  ? 39.486  192.421 63.136 1.00 39.22 ?  14  VAL J CA  1 
ATOM   9983  C  C   . VAL J  1 15  ? 40.066  193.547 62.295 1.00 44.87 ?  14  VAL J C   1 
ATOM   9984  O  O   . VAL J  1 15  ? 39.475  194.630 62.185 1.00 45.42 ?  14  VAL J O   1 
ATOM   9985  C  CB  . VAL J  1 15  ? 38.296  191.750 62.433 1.00 40.77 ?  14  VAL J CB  1 
ATOM   9986  C  CG1 . VAL J  1 15  ? 38.687  191.268 61.042 1.00 35.71 ?  14  VAL J CG1 1 
ATOM   9987  C  CG2 . VAL J  1 15  ? 37.760  190.599 63.289 1.00 40.08 ?  14  VAL J CG2 1 
ATOM   9988  N  N   . GLN J  1 16  ? 41.227  193.297 61.690 1.00 43.04 ?  15  GLN J N   1 
ATOM   9989  C  CA  . GLN J  1 16  ? 41.828  194.264 60.785 1.00 40.10 ?  15  GLN J CA  1 
ATOM   9990  C  C   . GLN J  1 16  ? 42.870  193.565 59.920 1.00 41.11 ?  15  GLN J C   1 
ATOM   9991  O  O   . GLN J  1 16  ? 43.430  192.538 60.311 1.00 41.88 ?  15  GLN J O   1 
ATOM   9992  C  CB  . GLN J  1 16  ? 42.458  195.423 61.556 1.00 42.99 ?  15  GLN J CB  1 
ATOM   9993  C  CG  . GLN J  1 16  ? 43.528  194.983 62.503 1.00 49.98 ?  15  GLN J CG  1 
ATOM   9994  C  CD  . GLN J  1 16  ? 44.036  196.115 63.371 1.00 63.17 ?  15  GLN J CD  1 
ATOM   9995  O  OE1 . GLN J  1 16  ? 43.551  196.330 64.491 1.00 62.52 ?  15  GLN J OE1 1 
ATOM   9996  N  NE2 . GLN J  1 16  ? 45.015  196.858 62.854 1.00 62.14 ?  15  GLN J NE2 1 
ATOM   9997  N  N   . GLY J  1 17  ? 43.110  194.119 58.738 1.00 43.26 ?  16  GLY J N   1 
ATOM   9998  C  CA  . GLY J  1 17  ? 44.072  193.508 57.840 1.00 43.20 ?  16  GLY J CA  1 
ATOM   9999  C  C   . GLY J  1 17  ? 44.261  194.309 56.572 1.00 44.91 ?  16  GLY J C   1 
ATOM   10000 O  O   . GLY J  1 17  ? 43.582  195.313 56.326 1.00 44.67 ?  16  GLY J O   1 
ATOM   10001 N  N   . ILE J  1 18  ? 45.205  193.832 55.760 1.00 39.70 ?  17  ILE J N   1 
ATOM   10002 C  CA  . ILE J  1 18  ? 45.559  194.437 54.482 1.00 40.79 ?  17  ILE J CA  1 
ATOM   10003 C  C   . ILE J  1 18  ? 45.508  193.349 53.418 1.00 43.93 ?  17  ILE J C   1 
ATOM   10004 O  O   . ILE J  1 18  ? 46.089  192.274 53.604 1.00 49.44 ?  17  ILE J O   1 
ATOM   10005 C  CB  . ILE J  1 18  ? 46.955  195.090 54.537 1.00 40.10 ?  17  ILE J CB  1 
ATOM   10006 C  CG1 . ILE J  1 18  ? 46.944  196.275 55.499 1.00 48.36 ?  17  ILE J CG1 1 
ATOM   10007 C  CG2 . ILE J  1 18  ? 47.376  195.560 53.171 1.00 40.86 ?  17  ILE J CG2 1 
ATOM   10008 C  CD1 . ILE J  1 18  ? 48.324  196.671 55.983 1.00 50.10 ?  17  ILE J CD1 1 
ATOM   10009 N  N   . ILE J  1 19  ? 44.805  193.615 52.315 1.00 39.89 ?  18  ILE J N   1 
ATOM   10010 C  CA  . ILE J  1 19  ? 44.631  192.652 51.230 1.00 39.96 ?  18  ILE J CA  1 
ATOM   10011 C  C   . ILE J  1 19  ? 45.101  193.297 49.933 1.00 47.08 ?  18  ILE J C   1 
ATOM   10012 O  O   . ILE J  1 19  ? 44.674  194.411 49.603 1.00 40.82 ?  18  ILE J O   1 
ATOM   10013 C  CB  . ILE J  1 19  ? 43.167  192.194 51.091 1.00 38.26 ?  18  ILE J CB  1 
ATOM   10014 C  CG1 . ILE J  1 19  ? 42.730  191.352 52.292 1.00 36.39 ?  18  ILE J CG1 1 
ATOM   10015 C  CG2 . ILE J  1 19  ? 42.972  191.411 49.778 1.00 40.01 ?  18  ILE J CG2 1 
ATOM   10016 C  CD1 . ILE J  1 19  ? 43.388  189.988 52.375 1.00 36.77 ?  18  ILE J CD1 1 
ATOM   10017 N  N   . ASN J  1 20  ? 45.953  192.588 49.186 1.00 41.81 ?  19  ASN J N   1 
ATOM   10018 C  CA  . ASN J  1 20  ? 46.479  193.081 47.921 1.00 40.77 ?  19  ASN J CA  1 
ATOM   10019 C  C   . ASN J  1 20  ? 45.815  192.377 46.751 1.00 39.57 ?  19  ASN J C   1 
ATOM   10020 O  O   . ASN J  1 20  ? 45.343  191.240 46.867 1.00 44.08 ?  19  ASN J O   1 
ATOM   10021 C  CB  . ASN J  1 20  ? 47.994  192.896 47.840 1.00 40.07 ?  19  ASN J CB  1 
ATOM   10022 C  CG  . ASN J  1 20  ? 48.707  193.526 49.003 1.00 43.79 ?  19  ASN J CG  1 
ATOM   10023 O  OD1 . ASN J  1 20  ? 48.966  194.732 48.997 1.00 51.39 ?  19  ASN J OD1 1 
ATOM   10024 N  ND2 . ASN J  1 20  ? 49.011  192.725 50.027 1.00 38.24 ?  19  ASN J ND2 1 
ATOM   10025 N  N   . PHE J  1 21  ? 45.770  193.075 45.625 1.00 40.53 ?  20  PHE J N   1 
ATOM   10026 C  CA  . PHE J  1 21  ? 45.229  192.542 44.389 1.00 40.39 ?  20  PHE J CA  1 
ATOM   10027 C  C   . PHE J  1 21  ? 46.230  192.814 43.275 1.00 46.11 ?  20  PHE J C   1 
ATOM   10028 O  O   . PHE J  1 21  ? 46.909  193.843 43.275 1.00 44.42 ?  20  PHE J O   1 
ATOM   10029 C  CB  . PHE J  1 21  ? 43.871  193.171 44.014 1.00 42.97 ?  20  PHE J CB  1 
ATOM   10030 C  CG  . PHE J  1 21  ? 42.777  192.980 45.045 1.00 43.49 ?  20  PHE J CG  1 
ATOM   10031 C  CD1 . PHE J  1 21  ? 42.746  193.748 46.208 1.00 42.02 ?  20  PHE J CD1 1 
ATOM   10032 C  CD2 . PHE J  1 21  ? 41.745  192.074 44.817 1.00 41.55 ?  20  PHE J CD2 1 
ATOM   10033 C  CE1 . PHE J  1 21  ? 41.717  193.589 47.149 1.00 41.31 ?  20  PHE J CE1 1 
ATOM   10034 C  CE2 . PHE J  1 21  ? 40.717  191.903 45.749 1.00 39.95 ?  20  PHE J CE2 1 
ATOM   10035 C  CZ  . PHE J  1 21  ? 40.700  192.672 46.916 1.00 36.18 ?  20  PHE J CZ  1 
ATOM   10036 N  N   . GLU J  1 22  ? 46.319  191.884 42.326 1.00 46.59 ?  21  GLU J N   1 
ATOM   10037 C  CA  . GLU J  1 22  ? 47.260  192.016 41.220 1.00 50.22 ?  21  GLU J CA  1 
ATOM   10038 C  C   . GLU J  1 22  ? 46.706  191.273 40.019 1.00 50.04 ?  21  GLU J C   1 
ATOM   10039 O  O   . GLU J  1 22  ? 46.249  190.133 40.153 1.00 54.22 ?  21  GLU J O   1 
ATOM   10040 C  CB  . GLU J  1 22  ? 48.639  191.470 41.592 1.00 52.47 ?  21  GLU J CB  1 
ATOM   10041 C  CG  . GLU J  1 22  ? 49.734  191.840 40.595 1.00 59.91 ?  21  GLU J CG  1 
ATOM   10042 C  CD  . GLU J  1 22  ? 51.109  191.343 41.026 1.00 70.92 ?  21  GLU J CD  1 
ATOM   10043 O  OE1 . GLU J  1 22  ? 51.770  192.038 41.833 1.00 75.52 ?  21  GLU J OE1 1 
ATOM   10044 O  OE2 . GLU J  1 22  ? 51.524  190.255 40.562 1.00 76.90 ?  21  GLU J OE2 1 
ATOM   10045 N  N   . GLN J  1 23  ? 46.730  191.924 38.858 1.00 44.20 ?  22  GLN J N   1 
ATOM   10046 C  CA  . GLN J  1 23  ? 46.152  191.365 37.634 1.00 45.84 ?  22  GLN J CA  1 
ATOM   10047 C  C   . GLN J  1 23  ? 47.073  191.752 36.478 1.00 57.64 ?  22  GLN J C   1 
ATOM   10048 O  O   . GLN J  1 23  ? 47.048  192.898 36.021 1.00 59.26 ?  22  GLN J O   1 
ATOM   10049 C  CB  . GLN J  1 23  ? 44.734  191.875 37.411 1.00 42.69 ?  22  GLN J CB  1 
ATOM   10050 C  CG  . GLN J  1 23  ? 43.967  191.104 36.358 1.00 51.14 ?  22  GLN J CG  1 
ATOM   10051 C  CD  . GLN J  1 23  ? 42.649  191.759 35.999 1.00 52.38 ?  22  GLN J CD  1 
ATOM   10052 O  OE1 . GLN J  1 23  ? 42.461  192.954 36.213 1.00 53.46 ?  22  GLN J OE1 1 
ATOM   10053 N  NE2 . GLN J  1 23  ? 41.724  190.974 35.455 1.00 52.30 ?  22  GLN J NE2 1 
ATOM   10054 N  N   . LYS J  1 24  ? 47.881  190.797 36.004 1.00 60.86 ?  23  LYS J N   1 
ATOM   10055 C  CA  . LYS J  1 24  ? 48.873  191.111 34.976 1.00 57.62 ?  23  LYS J CA  1 
ATOM   10056 C  C   . LYS J  1 24  ? 48.215  191.347 33.621 1.00 60.60 ?  23  LYS J C   1 
ATOM   10057 O  O   . LYS J  1 24  ? 48.413  192.394 32.995 1.00 65.04 ?  23  LYS J O   1 
ATOM   10058 C  CB  . LYS J  1 24  ? 49.913  189.992 34.889 1.00 61.09 ?  23  LYS J CB  1 
ATOM   10059 C  CG  . LYS J  1 24  ? 50.976  190.042 35.989 1.00 63.41 ?  23  LYS J CG  1 
ATOM   10060 C  CD  . LYS J  1 24  ? 51.902  188.820 35.920 1.00 69.44 ?  23  LYS J CD  1 
ATOM   10061 C  CE  . LYS J  1 24  ? 53.230  189.144 35.221 1.00 69.11 ?  23  LYS J CE  1 
ATOM   10062 N  NZ  . LYS J  1 24  ? 54.412  188.624 35.988 1.00 68.94 ?  23  LYS J NZ  1 
ATOM   10063 N  N   . GLU J  1 25  ? 47.432  190.382 33.148 1.00 59.81 ?  24  GLU J N   1 
ATOM   10064 C  CA  . GLU J  1 25  ? 46.748  190.496 31.866 1.00 63.65 ?  24  GLU J CA  1 
ATOM   10065 C  C   . GLU J  1 25  ? 45.307  190.952 32.074 1.00 63.06 ?  24  GLU J C   1 
ATOM   10066 O  O   . GLU J  1 25  ? 44.646  190.541 33.032 1.00 64.66 ?  24  GLU J O   1 
ATOM   10067 C  CB  . GLU J  1 25  ? 46.773  189.163 31.105 1.00 64.59 ?  24  GLU J CB  1 
ATOM   10068 C  CG  . GLU J  1 25  ? 48.172  188.686 30.706 1.00 70.84 ?  24  GLU J CG  1 
ATOM   10069 C  CD  . GLU J  1 25  ? 48.633  187.452 31.477 1.00 82.98 ?  24  GLU J CD  1 
ATOM   10070 O  OE1 . GLU J  1 25  ? 49.729  187.510 32.087 1.00 84.41 ?  24  GLU J OE1 1 
ATOM   10071 O  OE2 . GLU J  1 25  ? 47.913  186.421 31.446 1.00 76.86 ?  24  GLU J OE2 1 
ATOM   10072 N  N   . SER J  1 26  ? 44.821  191.783 31.148 1.00 65.16 ?  25  SER J N   1 
ATOM   10073 C  CA  . SER J  1 26  ? 43.547  192.487 31.282 1.00 66.43 ?  25  SER J CA  1 
ATOM   10074 C  C   . SER J  1 26  ? 42.373  191.555 31.575 1.00 69.05 ?  25  SER J C   1 
ATOM   10075 O  O   . SER J  1 26  ? 41.797  191.611 32.668 1.00 72.42 ?  25  SER J O   1 
ATOM   10076 C  CB  . SER J  1 26  ? 43.264  193.303 30.017 1.00 68.66 ?  25  SER J CB  1 
ATOM   10077 O  OG  . SER J  1 26  ? 44.459  193.536 29.281 1.00 75.12 ?  25  SER J OG  1 
ATOM   10078 N  N   . ASN J  1 27  ? 41.992  190.710 30.616 1.00 69.49 ?  26  ASN J N   1 
ATOM   10079 C  CA  . ASN J  1 27  ? 40.916  189.764 30.955 1.00 68.84 ?  26  ASN J CA  1 
ATOM   10080 C  C   . ASN J  1 27  ? 41.404  188.616 31.883 1.00 70.12 ?  26  ASN J C   1 
ATOM   10081 O  O   . ASN J  1 27  ? 40.619  187.675 32.105 1.00 71.30 ?  26  ASN J O   1 
ATOM   10082 C  CB  . ASN J  1 27  ? 40.294  189.167 29.684 1.00 74.08 ?  26  ASN J CB  1 
ATOM   10083 C  CG  . ASN J  1 27  ? 39.403  190.160 28.920 1.00 80.10 ?  26  ASN J CG  1 
ATOM   10084 O  OD1 . ASN J  1 27  ? 39.862  191.219 28.471 1.00 78.66 ?  26  ASN J OD1 1 
ATOM   10085 N  ND2 . ASN J  1 27  ? 38.123  189.807 28.760 1.00 70.63 ?  26  ASN J ND2 1 
ATOM   10086 N  N   . GLY J  1 28  ? 42.634  188.688 32.407 1.00 66.50 ?  27  GLY J N   1 
ATOM   10087 C  CA  . GLY J  1 28  ? 43.244  187.590 33.125 1.00 56.86 ?  27  GLY J CA  1 
ATOM   10088 C  C   . GLY J  1 28  ? 42.789  187.442 34.564 1.00 61.02 ?  27  GLY J C   1 
ATOM   10089 O  O   . GLY J  1 28  ? 41.907  188.165 35.040 1.00 65.81 ?  27  GLY J O   1 
ATOM   10090 N  N   . PRO J  1 29  ? 43.384  186.495 35.285 1.00 58.08 ?  28  PRO J N   1 
ATOM   10091 C  CA  . PRO J  1 29  ? 42.986  186.260 36.673 1.00 55.94 ?  28  PRO J CA  1 
ATOM   10092 C  C   . PRO J  1 29  ? 43.677  187.219 37.629 1.00 51.34 ?  28  PRO J C   1 
ATOM   10093 O  O   . PRO J  1 29  ? 44.715  187.817 37.333 1.00 50.24 ?  28  PRO J O   1 
ATOM   10094 C  CB  . PRO J  1 29  ? 43.437  184.821 36.927 1.00 54.73 ?  28  PRO J CB  1 
ATOM   10095 C  CG  . PRO J  1 29  ? 44.687  184.703 36.105 1.00 57.57 ?  28  PRO J CG  1 
ATOM   10096 C  CD  . PRO J  1 29  ? 44.479  185.594 34.879 1.00 57.92 ?  28  PRO J CD  1 
ATOM   10097 N  N   . VAL J  1 30  ? 43.087  187.332 38.813 1.00 52.27 ?  29  VAL J N   1 
ATOM   10098 C  CA  . VAL J  1 30  ? 43.521  188.273 39.833 1.00 40.32 ?  29  VAL J CA  1 
ATOM   10099 C  C   . VAL J  1 30  ? 44.055  187.478 41.006 1.00 42.79 ?  29  VAL J C   1 
ATOM   10100 O  O   . VAL J  1 30  ? 43.358  186.610 41.544 1.00 44.90 ?  29  VAL J O   1 
ATOM   10101 C  CB  . VAL J  1 30  ? 42.368  189.186 40.277 1.00 44.67 ?  29  VAL J CB  1 
ATOM   10102 C  CG1 . VAL J  1 30  ? 42.883  190.276 41.192 1.00 45.20 ?  29  VAL J CG1 1 
ATOM   10103 C  CG2 . VAL J  1 30  ? 41.656  189.753 39.070 1.00 40.90 ?  29  VAL J CG2 1 
ATOM   10104 N  N   . LYS J  1 31  ? 45.286  187.768 41.402 1.00 42.14 ?  30  LYS J N   1 
ATOM   10105 C  CA  . LYS J  1 31  ? 45.854  187.192 42.608 1.00 42.58 ?  30  LYS J CA  1 
ATOM   10106 C  C   . LYS J  1 31  ? 45.433  188.081 43.769 1.00 47.54 ?  30  LYS J C   1 
ATOM   10107 O  O   . LYS J  1 31  ? 45.509  189.311 43.668 1.00 45.62 ?  30  LYS J O   1 
ATOM   10108 C  CB  . LYS J  1 31  ? 47.378  187.091 42.506 1.00 42.27 ?  30  LYS J CB  1 
ATOM   10109 C  CG  . LYS J  1 31  ? 48.091  186.746 43.825 1.00 51.74 ?  30  LYS J CG  1 
ATOM   10110 C  CD  . LYS J  1 31  ? 47.621  185.405 44.444 1.00 56.40 ?  30  LYS J CD  1 
ATOM   10111 C  CE  . LYS J  1 31  ? 48.594  184.866 45.521 1.00 55.26 ?  30  LYS J CE  1 
ATOM   10112 N  NZ  . LYS J  1 31  ? 49.977  185.484 45.505 1.00 61.35 ?  30  LYS J NZ  1 
ATOM   10113 N  N   . VAL J  1 32  ? 44.950  187.458 44.843 1.00 42.89 ?  31  VAL J N   1 
ATOM   10114 C  CA  . VAL J  1 32  ? 44.490  188.139 46.049 1.00 41.81 ?  31  VAL J CA  1 
ATOM   10115 C  C   . VAL J  1 32  ? 45.258  187.559 47.224 1.00 43.42 ?  31  VAL J C   1 
ATOM   10116 O  O   . VAL J  1 32  ? 45.108  186.372 47.539 1.00 47.52 ?  31  VAL J O   1 
ATOM   10117 C  CB  . VAL J  1 32  ? 42.977  187.961 46.271 1.00 38.59 ?  31  VAL J CB  1 
ATOM   10118 C  CG1 . VAL J  1 32  ? 42.542  188.712 47.530 1.00 35.77 ?  31  VAL J CG1 1 
ATOM   10119 C  CG2 . VAL J  1 32  ? 42.184  188.432 45.072 1.00 41.26 ?  31  VAL J CG2 1 
ATOM   10120 N  N   . TRP J  1 33  ? 46.047  188.392 47.897 1.00 42.60 ?  32  TRP J N   1 
ATOM   10121 C  CA  . TRP J  1 33  ? 46.815  187.901 49.031 1.00 43.48 ?  32  TRP J CA  1 
ATOM   10122 C  C   . TRP J  1 33  ? 46.938  188.983 50.088 1.00 43.93 ?  32  TRP J C   1 
ATOM   10123 O  O   . TRP J  1 33  ? 46.922  190.179 49.786 1.00 45.34 ?  32  TRP J O   1 
ATOM   10124 C  CB  . TRP J  1 33  ? 48.211  187.429 48.605 1.00 47.81 ?  32  TRP J CB  1 
ATOM   10125 C  CG  . TRP J  1 33  ? 49.199  188.539 48.336 1.00 40.87 ?  32  TRP J CG  1 
ATOM   10126 C  CD1 . TRP J  1 33  ? 50.178  189.001 49.184 1.00 40.88 ?  32  TRP J CD1 1 
ATOM   10127 C  CD2 . TRP J  1 33  ? 49.297  189.324 47.144 1.00 35.75 ?  32  TRP J CD2 1 
ATOM   10128 N  NE1 . TRP J  1 33  ? 50.878  190.025 48.580 1.00 39.23 ?  32  TRP J NE1 1 
ATOM   10129 C  CE2 . TRP J  1 33  ? 50.357  190.238 47.329 1.00 32.99 ?  32  TRP J CE2 1 
ATOM   10130 C  CE3 . TRP J  1 33  ? 48.583  189.352 45.942 1.00 44.52 ?  32  TRP J CE3 1 
ATOM   10131 C  CZ2 . TRP J  1 33  ? 50.725  191.164 46.351 1.00 36.95 ?  32  TRP J CZ2 1 
ATOM   10132 C  CZ3 . TRP J  1 33  ? 48.947  190.276 44.967 1.00 44.89 ?  32  TRP J CZ3 1 
ATOM   10133 C  CH2 . TRP J  1 33  ? 50.008  191.169 45.179 1.00 45.09 ?  32  TRP J CH2 1 
ATOM   10134 N  N   . GLY J  1 34  ? 47.082  188.545 51.334 1.00 41.94 ?  33  GLY J N   1 
ATOM   10135 C  CA  . GLY J  1 34  ? 47.305  189.473 52.418 1.00 39.98 ?  33  GLY J CA  1 
ATOM   10136 C  C   . GLY J  1 34  ? 47.165  188.762 53.749 1.00 46.08 ?  33  GLY J C   1 
ATOM   10137 O  O   . GLY J  1 34  ? 47.175  187.534 53.825 1.00 45.81 ?  33  GLY J O   1 
ATOM   10138 N  N   . SER J  1 35  ? 47.036  189.563 54.794 1.00 39.40 ?  34  SER J N   1 
ATOM   10139 C  CA  . SER J  1 35  ? 46.917  189.053 56.147 1.00 43.46 ?  34  SER J CA  1 
ATOM   10140 C  C   . SER J  1 35  ? 45.774  189.769 56.855 1.00 46.01 ?  34  SER J C   1 
ATOM   10141 O  O   . SER J  1 35  ? 45.597  190.978 56.695 1.00 48.00 ?  34  SER J O   1 
ATOM   10142 C  CB  . SER J  1 35  ? 48.230  189.250 56.903 1.00 44.91 ?  34  SER J CB  1 
ATOM   10143 O  OG  . SER J  1 35  ? 48.114  188.785 58.228 1.00 58.22 ?  34  SER J OG  1 
ATOM   10144 N  N   . ILE J  1 36  ? 44.987  189.017 57.616 1.00 45.13 ?  35  ILE J N   1 
ATOM   10145 C  CA  . ILE J  1 36  ? 43.908  189.562 58.430 1.00 44.37 ?  35  ILE J CA  1 
ATOM   10146 C  C   . ILE J  1 36  ? 44.081  189.002 59.828 1.00 44.76 ?  35  ILE J C   1 
ATOM   10147 O  O   . ILE J  1 36  ? 44.140  187.779 59.995 1.00 47.75 ?  35  ILE J O   1 
ATOM   10148 C  CB  . ILE J  1 36  ? 42.519  189.189 57.878 1.00 42.09 ?  35  ILE J CB  1 
ATOM   10149 C  CG1 . ILE J  1 36  ? 42.354  189.631 56.430 1.00 36.72 ?  35  ILE J CG1 1 
ATOM   10150 C  CG2 . ILE J  1 36  ? 41.409  189.757 58.754 1.00 41.03 ?  35  ILE J CG2 1 
ATOM   10151 C  CD1 . ILE J  1 36  ? 41.068  189.122 55.819 1.00 34.81 ?  35  ILE J CD1 1 
ATOM   10152 N  N   . LYS J  1 37  ? 44.167  189.874 60.829 1.00 43.74 ?  36  LYS J N   1 
ATOM   10153 C  CA  . LYS J  1 37  ? 44.294  189.430 62.212 1.00 39.42 ?  36  LYS J CA  1 
ATOM   10154 C  C   . LYS J  1 37  ? 43.021  189.744 62.985 1.00 47.15 ?  36  LYS J C   1 
ATOM   10155 O  O   . LYS J  1 37  ? 42.158  190.499 62.525 1.00 49.24 ?  36  LYS J O   1 
ATOM   10156 C  CB  . LYS J  1 37  ? 45.510  190.075 62.894 1.00 51.17 ?  36  LYS J CB  1 
ATOM   10157 C  CG  . LYS J  1 37  ? 45.546  191.606 62.830 1.00 52.34 ?  36  LYS J CG  1 
ATOM   10158 C  CD  . LYS J  1 37  ? 46.578  192.193 63.795 1.00 52.77 ?  36  LYS J CD  1 
ATOM   10159 C  CE  . LYS J  1 37  ? 47.065  193.570 63.333 1.00 59.91 ?  36  LYS J CE  1 
ATOM   10160 N  NZ  . LYS J  1 37  ? 48.548  193.740 63.481 1.00 64.64 ?  36  LYS J NZ  1 
ATOM   10161 N  N   . GLY J  1 38  ? 42.907  189.133 64.167 1.00 41.61 ?  37  GLY J N   1 
ATOM   10162 C  CA  . GLY J  1 38  ? 41.801  189.374 65.078 1.00 40.14 ?  37  GLY J CA  1 
ATOM   10163 C  C   . GLY J  1 38  ? 40.583  188.500 64.883 1.00 44.39 ?  37  GLY J C   1 
ATOM   10164 O  O   . GLY J  1 38  ? 39.547  188.750 65.521 1.00 43.30 ?  37  GLY J O   1 
ATOM   10165 N  N   . LEU J  1 39  ? 40.668  187.480 64.040 1.00 43.55 ?  38  LEU J N   1 
ATOM   10166 C  CA  . LEU J  1 39  ? 39.531  186.620 63.744 1.00 44.70 ?  38  LEU J CA  1 
ATOM   10167 C  C   . LEU J  1 39  ? 39.460  185.437 64.708 1.00 47.88 ?  38  LEU J C   1 
ATOM   10168 O  O   . LEU J  1 39  ? 40.457  185.023 65.300 1.00 49.34 ?  38  LEU J O   1 
ATOM   10169 C  CB  . LEU J  1 39  ? 39.626  186.092 62.316 1.00 41.17 ?  38  LEU J CB  1 
ATOM   10170 C  CG  . LEU J  1 39  ? 39.645  187.151 61.222 1.00 42.81 ?  38  LEU J CG  1 
ATOM   10171 C  CD1 . LEU J  1 39  ? 40.306  186.580 59.980 1.00 36.59 ?  38  LEU J CD1 1 
ATOM   10172 C  CD2 . LEU J  1 39  ? 38.228  187.591 60.932 1.00 35.48 ?  38  LEU J CD2 1 
ATOM   10173 N  N   . THR J  1 40  ? 38.257  184.888 64.850 1.00 42.80 ?  39  THR J N   1 
ATOM   10174 C  CA  . THR J  1 40  ? 38.115  183.580 65.468 1.00 46.54 ?  39  THR J CA  1 
ATOM   10175 C  C   . THR J  1 40  ? 38.674  182.508 64.534 1.00 47.15 ?  39  THR J C   1 
ATOM   10176 O  O   . THR J  1 40  ? 38.579  182.610 63.308 1.00 44.76 ?  39  THR J O   1 
ATOM   10177 C  CB  . THR J  1 40  ? 36.650  183.293 65.783 1.00 44.47 ?  39  THR J CB  1 
ATOM   10178 O  OG1 . THR J  1 40  ? 35.912  183.220 64.555 1.00 50.62 ?  39  THR J OG1 1 
ATOM   10179 C  CG2 . THR J  1 40  ? 36.072  184.415 66.619 1.00 45.27 ?  39  THR J CG2 1 
ATOM   10180 N  N   . GLU J  1 41  ? 39.287  181.485 65.128 1.00 45.95 ?  40  GLU J N   1 
ATOM   10181 C  CA  . GLU J  1 41  ? 39.891  180.406 64.352 1.00 40.12 ?  40  GLU J CA  1 
ATOM   10182 C  C   . GLU J  1 41  ? 38.852  179.736 63.464 1.00 38.79 ?  40  GLU J C   1 
ATOM   10183 O  O   . GLU J  1 41  ? 37.741  179.438 63.907 1.00 43.03 ?  40  GLU J O   1 
ATOM   10184 C  CB  . GLU J  1 41  ? 40.511  179.385 65.305 1.00 48.06 ?  40  GLU J CB  1 
ATOM   10185 C  CG  . GLU J  1 41  ? 40.940  178.086 64.663 1.00 51.50 ?  40  GLU J CG  1 
ATOM   10186 C  CD  . GLU J  1 41  ? 41.494  177.093 65.682 1.00 61.80 ?  40  GLU J CD  1 
ATOM   10187 O  OE1 . GLU J  1 41  ? 41.008  177.084 66.836 1.00 55.67 ?  40  GLU J OE1 1 
ATOM   10188 O  OE2 . GLU J  1 41  ? 42.424  176.334 65.325 1.00 62.91 ?  40  GLU J OE2 1 
ATOM   10189 N  N   . GLY J  1 42  ? 39.208  179.507 62.203 1.00 44.42 ?  41  GLY J N   1 
ATOM   10190 C  CA  . GLY J  1 42  ? 38.286  178.854 61.296 1.00 40.31 ?  41  GLY J CA  1 
ATOM   10191 C  C   . GLY J  1 42  ? 37.909  179.668 60.074 1.00 40.06 ?  41  GLY J C   1 
ATOM   10192 O  O   . GLY J  1 42  ? 38.562  180.666 59.745 1.00 39.69 ?  41  GLY J O   1 
ATOM   10193 N  N   . LEU J  1 43  ? 36.849  179.235 59.396 1.00 39.57 ?  42  LEU J N   1 
ATOM   10194 C  CA  . LEU J  1 43  ? 36.456  179.793 58.106 1.00 34.23 ?  42  LEU J CA  1 
ATOM   10195 C  C   . LEU J  1 43  ? 35.619  181.057 58.271 1.00 39.50 ?  42  LEU J C   1 
ATOM   10196 O  O   . LEU J  1 43  ? 34.712  181.110 59.106 1.00 35.54 ?  42  LEU J O   1 
ATOM   10197 C  CB  . LEU J  1 43  ? 35.650  178.761 57.318 1.00 37.33 ?  42  LEU J CB  1 
ATOM   10198 C  CG  . LEU J  1 43  ? 36.392  177.508 56.854 1.00 39.91 ?  42  LEU J CG  1 
ATOM   10199 C  CD1 . LEU J  1 43  ? 35.433  176.574 56.126 1.00 37.61 ?  42  LEU J CD1 1 
ATOM   10200 C  CD2 . LEU J  1 43  ? 37.529  177.904 55.958 1.00 38.08 ?  42  LEU J CD2 1 
ATOM   10201 N  N   . HIS J  1 44  ? 35.896  182.059 57.434 1.00 40.13 ?  43  HIS J N   1 
ATOM   10202 C  CA  . HIS J  1 44  ? 35.152  183.316 57.409 1.00 36.16 ?  43  HIS J CA  1 
ATOM   10203 C  C   . HIS J  1 44  ? 34.852  183.703 55.971 1.00 37.45 ?  43  HIS J C   1 
ATOM   10204 O  O   . HIS J  1 44  ? 35.760  183.750 55.138 1.00 34.65 ?  43  HIS J O   1 
ATOM   10205 C  CB  . HIS J  1 44  ? 35.951  184.440 58.066 1.00 36.34 ?  43  HIS J CB  1 
ATOM   10206 C  CG  . HIS J  1 44  ? 36.163  184.243 59.527 1.00 38.81 ?  43  HIS J CG  1 
ATOM   10207 N  ND1 . HIS J  1 44  ? 35.211  184.584 60.461 1.00 39.98 ?  43  HIS J ND1 1 
ATOM   10208 C  CD2 . HIS J  1 44  ? 37.203  183.714 60.216 1.00 37.81 ?  43  HIS J CD2 1 
ATOM   10209 C  CE1 . HIS J  1 44  ? 35.660  184.284 61.667 1.00 45.55 ?  43  HIS J CE1 1 
ATOM   10210 N  NE2 . HIS J  1 44  ? 36.865  183.753 61.545 1.00 43.79 ?  43  HIS J NE2 1 
ATOM   10211 N  N   . GLY J  1 45  ? 33.585  183.992 55.687 1.00 34.66 ?  44  GLY J N   1 
ATOM   10212 C  CA  . GLY J  1 45  ? 33.228  184.448 54.356 1.00 31.12 ?  44  GLY J CA  1 
ATOM   10213 C  C   . GLY J  1 45  ? 34.025  185.681 53.968 1.00 35.75 ?  44  GLY J C   1 
ATOM   10214 O  O   . GLY J  1 45  ? 34.351  186.530 54.803 1.00 33.33 ?  44  GLY J O   1 
ATOM   10215 N  N   . PHE J  1 46  ? 34.354  185.765 52.680 1.00 32.16 ?  45  PHE J N   1 
ATOM   10216 C  CA  . PHE J  1 46  ? 35.286  186.759 52.143 1.00 34.19 ?  45  PHE J CA  1 
ATOM   10217 C  C   . PHE J  1 46  ? 34.716  187.184 50.796 1.00 37.20 ?  45  PHE J C   1 
ATOM   10218 O  O   . PHE J  1 46  ? 34.737  186.394 49.850 1.00 38.34 ?  45  PHE J O   1 
ATOM   10219 C  CB  . PHE J  1 46  ? 36.676  186.135 52.000 1.00 35.26 ?  45  PHE J CB  1 
ATOM   10220 C  CG  . PHE J  1 46  ? 37.799  187.107 51.726 1.00 36.05 ?  45  PHE J CG  1 
ATOM   10221 C  CD1 . PHE J  1 46  ? 38.128  188.092 52.634 1.00 34.10 ?  45  PHE J CD1 1 
ATOM   10222 C  CD2 . PHE J  1 46  ? 38.582  186.969 50.583 1.00 34.71 ?  45  PHE J CD2 1 
ATOM   10223 C  CE1 . PHE J  1 46  ? 39.192  188.946 52.393 1.00 34.65 ?  45  PHE J CE1 1 
ATOM   10224 C  CE2 . PHE J  1 46  ? 39.640  187.830 50.336 1.00 33.03 ?  45  PHE J CE2 1 
ATOM   10225 C  CZ  . PHE J  1 46  ? 39.943  188.817 51.238 1.00 35.89 ?  45  PHE J CZ  1 
ATOM   10226 N  N   . HIS J  1 47  ? 34.190  188.409 50.701 1.00 36.32 ?  46  HIS J N   1 
ATOM   10227 C  CA  . HIS J  1 47  ? 33.404  188.798 49.536 1.00 30.69 ?  46  HIS J CA  1 
ATOM   10228 C  C   . HIS J  1 47  ? 33.699  190.231 49.117 1.00 38.27 ?  46  HIS J C   1 
ATOM   10229 O  O   . HIS J  1 47  ? 34.108  191.067 49.926 1.00 35.06 ?  46  HIS J O   1 
ATOM   10230 C  CB  . HIS J  1 47  ? 31.897  188.671 49.801 1.00 35.95 ?  46  HIS J CB  1 
ATOM   10231 C  CG  . HIS J  1 47  ? 31.495  187.372 50.420 1.00 39.50 ?  46  HIS J CG  1 
ATOM   10232 N  ND1 . HIS J  1 47  ? 30.885  187.293 51.651 1.00 37.51 ?  46  HIS J ND1 1 
ATOM   10233 C  CD2 . HIS J  1 47  ? 31.621  186.098 49.977 1.00 39.95 ?  46  HIS J CD2 1 
ATOM   10234 C  CE1 . HIS J  1 47  ? 30.638  186.026 51.938 1.00 38.69 ?  46  HIS J CE1 1 
ATOM   10235 N  NE2 . HIS J  1 47  ? 31.086  185.279 50.945 1.00 41.41 ?  46  HIS J NE2 1 
ATOM   10236 N  N   . VAL J  1 48  ? 33.478  190.505 47.836 1.00 36.52 ?  47  VAL J N   1 
ATOM   10237 C  CA  . VAL J  1 48  ? 33.447  191.876 47.347 1.00 42.01 ?  47  VAL J CA  1 
ATOM   10238 C  C   . VAL J  1 48  ? 31.990  192.309 47.320 1.00 36.54 ?  47  VAL J C   1 
ATOM   10239 O  O   . VAL J  1 48  ? 31.163  191.697 46.635 1.00 34.82 ?  47  VAL J O   1 
ATOM   10240 C  CB  . VAL J  1 48  ? 34.099  192.005 45.962 1.00 35.94 ?  47  VAL J CB  1 
ATOM   10241 C  CG1 . VAL J  1 48  ? 34.024  193.461 45.486 1.00 36.97 ?  47  VAL J CG1 1 
ATOM   10242 C  CG2 . VAL J  1 48  ? 35.541  191.570 46.027 1.00 35.19 ?  47  VAL J CG2 1 
ATOM   10243 N  N   . HIS J  1 49  ? 31.664  193.336 48.099 1.00 33.29 ?  48  HIS J N   1 
ATOM   10244 C  CA  . HIS J  1 49  ? 30.310  193.859 48.082 1.00 36.42 ?  48  HIS J CA  1 
ATOM   10245 C  C   . HIS J  1 49  ? 30.221  195.045 47.116 1.00 36.85 ?  48  HIS J C   1 
ATOM   10246 O  O   . HIS J  1 49  ? 31.233  195.617 46.701 1.00 37.06 ?  48  HIS J O   1 
ATOM   10247 C  CB  . HIS J  1 49  ? 29.876  194.254 49.492 1.00 33.65 ?  48  HIS J CB  1 
ATOM   10248 C  CG  . HIS J  1 49  ? 29.650  193.085 50.407 1.00 32.39 ?  48  HIS J CG  1 
ATOM   10249 N  ND1 . HIS J  1 49  ? 28.447  192.861 51.044 1.00 33.48 ?  48  HIS J ND1 1 
ATOM   10250 C  CD2 . HIS J  1 49  ? 30.478  192.093 50.815 1.00 33.00 ?  48  HIS J CD2 1 
ATOM   10251 C  CE1 . HIS J  1 49  ? 28.541  191.782 51.803 1.00 31.78 ?  48  HIS J CE1 1 
ATOM   10252 N  NE2 . HIS J  1 49  ? 29.764  191.297 51.683 1.00 34.45 ?  48  HIS J NE2 1 
ATOM   10253 N  N   . GLU J  1 50  ? 28.985  195.420 46.777 1.00 35.28 ?  49  GLU J N   1 
ATOM   10254 C  CA  . GLU J  1 50  ? 28.748  196.217 45.570 1.00 37.52 ?  49  GLU J CA  1 
ATOM   10255 C  C   . GLU J  1 50  ? 29.296  197.642 45.679 1.00 35.70 ?  49  GLU J C   1 
ATOM   10256 O  O   . GLU J  1 50  ? 29.842  198.173 44.706 1.00 38.98 ?  49  GLU J O   1 
ATOM   10257 C  CB  . GLU J  1 50  ? 27.257  196.247 45.255 1.00 38.88 ?  49  GLU J CB  1 
ATOM   10258 C  CG  . GLU J  1 50  ? 26.943  196.878 43.901 1.00 48.11 ?  49  GLU J CG  1 
ATOM   10259 C  CD  . GLU J  1 50  ? 25.456  196.992 43.629 1.00 47.09 ?  49  GLU J CD  1 
ATOM   10260 O  OE1 . GLU J  1 50  ? 24.649  196.394 44.385 1.00 49.15 ?  49  GLU J OE1 1 
ATOM   10261 O  OE2 . GLU J  1 50  ? 25.096  197.669 42.642 1.00 51.90 ?  49  GLU J OE2 1 
ATOM   10262 N  N   . PHE J  1 51  ? 29.159  198.276 46.838 1.00 34.00 ?  50  PHE J N   1 
ATOM   10263 C  CA  . PHE J  1 51  ? 29.402  199.704 46.982 1.00 35.92 ?  50  PHE J CA  1 
ATOM   10264 C  C   . PHE J  1 51  ? 30.611  199.970 47.864 1.00 36.70 ?  50  PHE J C   1 
ATOM   10265 O  O   . PHE J  1 51  ? 30.769  199.349 48.915 1.00 36.37 ?  50  PHE J O   1 
ATOM   10266 C  CB  . PHE J  1 51  ? 28.174  200.385 47.580 1.00 33.48 ?  50  PHE J CB  1 
ATOM   10267 C  CG  . PHE J  1 51  ? 26.931  200.171 46.782 1.00 38.98 ?  50  PHE J CG  1 
ATOM   10268 C  CD1 . PHE J  1 51  ? 26.848  200.640 45.483 1.00 39.69 ?  50  PHE J CD1 1 
ATOM   10269 C  CD2 . PHE J  1 51  ? 25.851  199.497 47.319 1.00 43.63 ?  50  PHE J CD2 1 
ATOM   10270 C  CE1 . PHE J  1 51  ? 25.716  200.442 44.731 1.00 39.63 ?  50  PHE J CE1 1 
ATOM   10271 C  CE2 . PHE J  1 51  ? 24.699  199.299 46.565 1.00 43.83 ?  50  PHE J CE2 1 
ATOM   10272 C  CZ  . PHE J  1 51  ? 24.641  199.769 45.268 1.00 43.05 ?  50  PHE J CZ  1 
ATOM   10273 N  N   . GLY J  1 52  ? 31.449  200.919 47.445 1.00 36.97 ?  51  GLY J N   1 
ATOM   10274 C  CA  . GLY J  1 52  ? 32.526  201.385 48.305 1.00 37.30 ?  51  GLY J CA  1 
ATOM   10275 C  C   . GLY J  1 52  ? 32.094  202.465 49.279 1.00 41.39 ?  51  GLY J C   1 
ATOM   10276 O  O   . GLY J  1 52  ? 32.754  203.505 49.426 1.00 41.42 ?  51  GLY J O   1 
ATOM   10277 N  N   . ASP J  1 53  ? 30.988  202.221 49.961 1.00 42.19 ?  52  ASP J N   1 
ATOM   10278 C  CA  . ASP J  1 53  ? 30.362  203.192 50.850 1.00 36.11 ?  52  ASP J CA  1 
ATOM   10279 C  C   . ASP J  1 53  ? 30.493  202.685 52.281 1.00 37.76 ?  52  ASP J C   1 
ATOM   10280 O  O   . ASP J  1 53  ? 29.816  201.733 52.675 1.00 36.79 ?  52  ASP J O   1 
ATOM   10281 C  CB  . ASP J  1 53  ? 28.900  203.383 50.447 1.00 40.95 ?  52  ASP J CB  1 
ATOM   10282 C  CG  . ASP J  1 53  ? 28.163  204.379 51.318 1.00 39.33 ?  52  ASP J CG  1 
ATOM   10283 O  OD1 . ASP J  1 53  ? 28.626  204.688 52.442 1.00 38.26 ?  52  ASP J OD1 1 
ATOM   10284 O  OD2 . ASP J  1 53  ? 27.097  204.843 50.862 1.00 40.87 ?  52  ASP J OD2 1 
ATOM   10285 N  N   . ASN J  1 54  ? 31.344  203.324 53.071 1.00 36.99 ?  53  ASN J N   1 
ATOM   10286 C  CA  . ASN J  1 54  ? 31.504  202.927 54.460 1.00 38.26 ?  53  ASN J CA  1 
ATOM   10287 C  C   . ASN J  1 54  ? 30.935  203.975 55.418 1.00 35.86 ?  53  ASN J C   1 
ATOM   10288 O  O   . ASN J  1 54  ? 31.358  204.064 56.573 1.00 35.36 ?  53  ASN J O   1 
ATOM   10289 C  CB  . ASN J  1 54  ? 32.975  202.629 54.771 1.00 40.23 ?  53  ASN J CB  1 
ATOM   10290 C  CG  . ASN J  1 54  ? 33.525  201.409 53.984 1.00 60.89 ?  53  ASN J CG  1 
ATOM   10291 O  OD1 . ASN J  1 54  ? 32.765  200.571 53.461 1.00 56.49 ?  53  ASN J OD1 1 
ATOM   10292 N  ND2 . ASN J  1 54  ? 34.861  201.298 53.930 1.00 54.73 ?  53  ASN J ND2 1 
ATOM   10293 N  N   . THR J  1 55  ? 29.939  204.742 54.964 1.00 32.89 ?  54  THR J N   1 
ATOM   10294 C  CA  . THR J  1 55  ? 29.409  205.827 55.793 1.00 41.84 ?  54  THR J CA  1 
ATOM   10295 C  C   . THR J  1 55  ? 28.679  205.308 57.020 1.00 41.87 ?  54  THR J C   1 
ATOM   10296 O  O   . THR J  1 55  ? 28.718  205.953 58.071 1.00 43.22 ?  54  THR J O   1 
ATOM   10297 C  CB  . THR J  1 55  ? 28.480  206.724 54.982 1.00 36.86 ?  54  THR J CB  1 
ATOM   10298 O  OG1 . THR J  1 55  ? 27.473  205.920 54.350 1.00 39.16 ?  54  THR J OG1 1 
ATOM   10299 C  CG2 . THR J  1 55  ? 29.275  207.482 53.928 1.00 30.91 ?  54  THR J CG2 1 
ATOM   10300 N  N   . ALA J  1 56  ? 28.007  204.165 56.909 1.00 40.51 ?  55  ALA J N   1 
ATOM   10301 C  CA  . ALA J  1 56  ? 27.430  203.463 58.047 1.00 41.96 ?  55  ALA J CA  1 
ATOM   10302 C  C   . ALA J  1 56  ? 28.242  202.212 58.373 1.00 46.17 ?  55  ALA J C   1 
ATOM   10303 O  O   . ALA J  1 56  ? 27.688  201.138 58.620 1.00 47.98 ?  55  ALA J O   1 
ATOM   10304 C  CB  . ALA J  1 56  ? 25.975  203.093 57.773 1.00 41.84 ?  55  ALA J CB  1 
ATOM   10305 N  N   . GLY J  1 57  ? 29.570  202.336 58.356 1.00 44.82 ?  56  GLY J N   1 
ATOM   10306 C  CA  . GLY J  1 57  ? 30.391  201.153 58.505 1.00 40.08 ?  56  GLY J CA  1 
ATOM   10307 C  C   . GLY J  1 57  ? 30.190  200.178 57.354 1.00 44.49 ?  56  GLY J C   1 
ATOM   10308 O  O   . GLY J  1 57  ? 29.855  200.550 56.223 1.00 40.18 ?  56  GLY J O   1 
ATOM   10309 N  N   . CYS J  1 58  ? 30.381  198.896 57.659 1.00 40.46 ?  57  CYS J N   1 
ATOM   10310 C  CA  . CYS J  1 58  ? 30.351  197.863 56.628 1.00 42.13 ?  57  CYS J CA  1 
ATOM   10311 C  C   . CYS J  1 58  ? 28.952  197.647 56.069 1.00 36.93 ?  57  CYS J C   1 
ATOM   10312 O  O   . CYS J  1 58  ? 28.804  197.144 54.949 1.00 38.61 ?  57  CYS J O   1 
ATOM   10313 C  CB  . CYS J  1 58  ? 30.920  196.560 57.210 1.00 37.23 ?  57  CYS J CB  1 
ATOM   10314 S  SG  . CYS J  1 58  ? 32.698  196.669 57.616 1.00 48.03 ?  57  CYS J SG  1 
ATOM   10315 N  N   . THR J  1 59  ? 27.926  198.059 56.808 1.00 34.57 ?  58  THR J N   1 
ATOM   10316 C  CA  . THR J  1 59  ? 26.550  197.837 56.385 1.00 39.43 ?  58  THR J CA  1 
ATOM   10317 C  C   . THR J  1 59  ? 26.230  198.559 55.079 1.00 38.92 ?  58  THR J C   1 
ATOM   10318 O  O   . THR J  1 59  ? 25.499  198.031 54.230 1.00 38.77 ?  58  THR J O   1 
ATOM   10319 C  CB  . THR J  1 59  ? 25.614  198.293 57.498 1.00 40.14 ?  58  THR J CB  1 
ATOM   10320 O  OG1 . THR J  1 59  ? 25.718  197.361 58.581 1.00 50.02 ?  58  THR J OG1 1 
ATOM   10321 C  CG2 . THR J  1 59  ? 24.182  198.325 57.003 1.00 42.35 ?  58  THR J CG2 1 
ATOM   10322 N  N   . SER J  1 60  ? 26.775  199.755 54.884 1.00 35.78 ?  59  SER J N   1 
ATOM   10323 C  CA  . SER J  1 60  ? 26.454  200.499 53.668 1.00 32.77 ?  59  SER J CA  1 
ATOM   10324 C  C   . SER J  1 60  ? 27.176  199.978 52.427 1.00 41.33 ?  59  SER J C   1 
ATOM   10325 O  O   . SER J  1 60  ? 27.033  200.578 51.350 1.00 37.91 ?  59  SER J O   1 
ATOM   10326 C  CB  . SER J  1 60  ? 26.743  201.991 53.863 1.00 36.44 ?  59  SER J CB  1 
ATOM   10327 O  OG  . SER J  1 60  ? 27.868  202.216 54.690 1.00 39.70 ?  59  SER J OG  1 
ATOM   10328 N  N   . ALA J  1 61  ? 27.918  198.871 52.532 1.00 35.58 ?  60  ALA J N   1 
ATOM   10329 C  CA  . ALA J  1 61  ? 28.553  198.290 51.347 1.00 33.78 ?  60  ALA J CA  1 
ATOM   10330 C  C   . ALA J  1 61  ? 27.561  197.617 50.410 1.00 34.53 ?  60  ALA J C   1 
ATOM   10331 O  O   . ALA J  1 61  ? 27.932  197.295 49.275 1.00 35.73 ?  60  ALA J O   1 
ATOM   10332 C  CB  . ALA J  1 61  ? 29.623  197.279 51.766 1.00 37.53 ?  60  ALA J CB  1 
ATOM   10333 N  N   . GLY J  1 62  ? 26.313  197.399 50.836 1.00 36.08 ?  61  GLY J N   1 
ATOM   10334 C  CA  . GLY J  1 62  ? 25.350  196.699 50.014 1.00 35.64 ?  61  GLY J CA  1 
ATOM   10335 C  C   . GLY J  1 62  ? 25.598  195.196 49.973 1.00 41.63 ?  61  GLY J C   1 
ATOM   10336 O  O   . GLY J  1 62  ? 26.354  194.645 50.782 1.00 34.08 ?  61  GLY J O   1 
ATOM   10337 N  N   . PRO J  1 63  ? 24.965  194.510 49.022 1.00 35.77 ?  62  PRO J N   1 
ATOM   10338 C  CA  . PRO J  1 63  ? 25.090  193.052 48.916 1.00 38.71 ?  62  PRO J CA  1 
ATOM   10339 C  C   . PRO J  1 63  ? 26.374  192.676 48.183 1.00 40.20 ?  62  PRO J C   1 
ATOM   10340 O  O   . PRO J  1 63  ? 27.154  193.527 47.759 1.00 38.01 ?  62  PRO J O   1 
ATOM   10341 C  CB  . PRO J  1 63  ? 23.866  192.664 48.085 1.00 37.14 ?  62  PRO J CB  1 
ATOM   10342 C  CG  . PRO J  1 63  ? 23.758  193.818 47.103 1.00 35.73 ?  62  PRO J CG  1 
ATOM   10343 C  CD  . PRO J  1 63  ? 24.151  195.067 47.927 1.00 33.14 ?  62  PRO J CD  1 
ATOM   10344 N  N   . HIS J  1 64  ? 26.575  191.371 48.024 1.00 36.06 ?  63  HIS J N   1 
ATOM   10345 C  CA  . HIS J  1 64  ? 27.693  190.903 47.224 1.00 36.49 ?  63  HIS J CA  1 
ATOM   10346 C  C   . HIS J  1 64  ? 27.612  191.505 45.825 1.00 36.89 ?  63  HIS J C   1 
ATOM   10347 O  O   . HIS J  1 64  ? 26.533  191.607 45.237 1.00 39.22 ?  63  HIS J O   1 
ATOM   10348 C  CB  . HIS J  1 64  ? 27.695  189.373 47.150 1.00 37.78 ?  63  HIS J CB  1 
ATOM   10349 C  CG  . HIS J  1 64  ? 27.827  188.702 48.484 1.00 33.72 ?  63  HIS J CG  1 
ATOM   10350 N  ND1 . HIS J  1 64  ? 27.550  187.367 48.671 1.00 35.01 ?  63  HIS J ND1 1 
ATOM   10351 C  CD2 . HIS J  1 64  ? 28.195  189.183 49.698 1.00 39.66 ?  63  HIS J CD2 1 
ATOM   10352 C  CE1 . HIS J  1 64  ? 27.749  187.046 49.939 1.00 41.17 ?  63  HIS J CE1 1 
ATOM   10353 N  NE2 . HIS J  1 64  ? 28.145  188.130 50.585 1.00 40.30 ?  63  HIS J NE2 1 
ATOM   10354 N  N   . PHE J  1 65  ? 28.757  191.941 45.313 1.00 39.06 ?  64  PHE J N   1 
ATOM   10355 C  CA  . PHE J  1 65  ? 28.827  192.459 43.952 1.00 38.05 ?  64  PHE J CA  1 
ATOM   10356 C  C   . PHE J  1 65  ? 28.330  191.398 42.972 1.00 43.26 ?  64  PHE J C   1 
ATOM   10357 O  O   . PHE J  1 65  ? 28.925  190.321 42.848 1.00 41.47 ?  64  PHE J O   1 
ATOM   10358 C  CB  . PHE J  1 65  ? 30.264  192.864 43.633 1.00 37.31 ?  64  PHE J CB  1 
ATOM   10359 C  CG  . PHE J  1 65  ? 30.436  193.463 42.264 1.00 43.37 ?  64  PHE J CG  1 
ATOM   10360 C  CD1 . PHE J  1 65  ? 29.522  194.391 41.780 1.00 44.39 ?  64  PHE J CD1 1 
ATOM   10361 C  CD2 . PHE J  1 65  ? 31.521  193.112 41.468 1.00 40.20 ?  64  PHE J CD2 1 
ATOM   10362 C  CE1 . PHE J  1 65  ? 29.679  194.955 40.523 1.00 40.50 ?  64  PHE J CE1 1 
ATOM   10363 C  CE2 . PHE J  1 65  ? 31.683  193.666 40.211 1.00 43.69 ?  64  PHE J CE2 1 
ATOM   10364 C  CZ  . PHE J  1 65  ? 30.759  194.593 39.737 1.00 42.90 ?  64  PHE J CZ  1 
ATOM   10365 N  N   . ASN J  1 66  ? 27.229  191.698 42.282 1.00 43.13 ?  65  ASN J N   1 
ATOM   10366 C  CA  . ASN J  1 66  ? 26.499  190.701 41.497 1.00 40.51 ?  65  ASN J CA  1 
ATOM   10367 C  C   . ASN J  1 66  ? 25.981  191.300 40.190 1.00 41.60 ?  65  ASN J C   1 
ATOM   10368 O  O   . ASN J  1 66  ? 24.776  191.323 39.941 1.00 43.14 ?  65  ASN J O   1 
ATOM   10369 C  CB  . ASN J  1 66  ? 25.342  190.145 42.326 1.00 37.86 ?  65  ASN J CB  1 
ATOM   10370 C  CG  . ASN J  1 66  ? 24.627  188.998 41.632 1.00 42.32 ?  65  ASN J CG  1 
ATOM   10371 O  OD1 . ASN J  1 66  ? 25.179  188.376 40.726 1.00 42.55 ?  65  ASN J OD1 1 
ATOM   10372 N  ND2 . ASN J  1 66  ? 23.404  188.699 42.071 1.00 39.56 ?  65  ASN J ND2 1 
ATOM   10373 N  N   . PRO J  1 67  ? 26.871  191.781 39.316 1.00 44.92 ?  66  PRO J N   1 
ATOM   10374 C  CA  . PRO J  1 67  ? 26.380  192.420 38.081 1.00 45.33 ?  66  PRO J CA  1 
ATOM   10375 C  C   . PRO J  1 67  ? 25.573  191.489 37.185 1.00 54.50 ?  66  PRO J C   1 
ATOM   10376 O  O   . PRO J  1 67  ? 24.612  191.939 36.546 1.00 52.31 ?  66  PRO J O   1 
ATOM   10377 C  CB  . PRO J  1 67  ? 27.663  192.898 37.387 1.00 47.47 ?  66  PRO J CB  1 
ATOM   10378 C  CG  . PRO J  1 67  ? 28.761  192.120 38.000 1.00 47.58 ?  66  PRO J CG  1 
ATOM   10379 C  CD  . PRO J  1 67  ? 28.340  191.838 39.417 1.00 42.75 ?  66  PRO J CD  1 
ATOM   10380 N  N   . LEU J  1 68  ? 25.910  190.201 37.126 1.00 50.98 ?  67  LEU J N   1 
ATOM   10381 C  CA  . LEU J  1 68  ? 25.144  189.278 36.292 1.00 49.01 ?  67  LEU J CA  1 
ATOM   10382 C  C   . LEU J  1 68  ? 23.865  188.804 36.965 1.00 47.22 ?  67  LEU J C   1 
ATOM   10383 O  O   . LEU J  1 68  ? 23.142  187.991 36.381 1.00 46.90 ?  67  LEU J O   1 
ATOM   10384 C  CB  . LEU J  1 68  ? 26.006  188.076 35.900 1.00 48.98 ?  67  LEU J CB  1 
ATOM   10385 C  CG  . LEU J  1 68  ? 27.446  188.421 35.493 1.00 51.57 ?  67  LEU J CG  1 
ATOM   10386 C  CD1 . LEU J  1 68  ? 28.188  187.192 35.001 1.00 54.43 ?  67  LEU J CD1 1 
ATOM   10387 C  CD2 . LEU J  1 68  ? 27.470  189.522 34.423 1.00 47.36 ?  67  LEU J CD2 1 
ATOM   10388 N  N   . SER J  1 69  ? 23.575  189.293 38.165 1.00 48.97 ?  68  SER J N   1 
ATOM   10389 C  CA  . SER J  1 69  ? 22.410  188.880 38.947 1.00 49.63 ?  68  SER J CA  1 
ATOM   10390 C  C   . SER J  1 69  ? 22.229  187.353 38.927 1.00 51.72 ?  68  SER J C   1 
ATOM   10391 O  O   . SER J  1 69  ? 21.224  186.811 38.468 1.00 50.99 ?  68  SER J O   1 
ATOM   10392 C  CB  . SER J  1 69  ? 21.159  189.609 38.463 1.00 53.52 ?  68  SER J CB  1 
ATOM   10393 O  OG  . SER J  1 69  ? 20.509  188.872 37.452 1.00 59.44 ?  68  SER J OG  1 
ATOM   10394 N  N   . ARG J  1 70  ? 23.242  186.662 39.441 1.00 47.65 ?  69  ARG J N   1 
ATOM   10395 C  CA  . ARG J  1 70  ? 23.188  185.226 39.654 1.00 43.88 ?  69  ARG J CA  1 
ATOM   10396 C  C   . ARG J  1 70  ? 22.869  184.934 41.115 1.00 47.77 ?  69  ARG J C   1 
ATOM   10397 O  O   . ARG J  1 70  ? 22.666  185.842 41.924 1.00 47.51 ?  69  ARG J O   1 
ATOM   10398 C  CB  . ARG J  1 70  ? 24.518  184.587 39.268 1.00 44.14 ?  69  ARG J CB  1 
ATOM   10399 C  CG  . ARG J  1 70  ? 25.011  185.044 37.939 1.00 50.93 ?  69  ARG J CG  1 
ATOM   10400 C  CD  . ARG J  1 70  ? 24.446  184.199 36.833 1.00 52.45 ?  69  ARG J CD  1 
ATOM   10401 N  NE  . ARG J  1 70  ? 25.510  183.819 35.915 1.00 56.47 ?  69  ARG J NE  1 
ATOM   10402 C  CZ  . ARG J  1 70  ? 25.631  184.294 34.684 1.00 68.44 ?  69  ARG J CZ  1 
ATOM   10403 N  NH1 . ARG J  1 70  ? 24.747  185.151 34.183 1.00 61.59 ?  69  ARG J NH1 1 
ATOM   10404 N  NH2 . ARG J  1 70  ? 26.658  183.899 33.936 1.00 68.15 ?  69  ARG J NH2 1 
ATOM   10405 N  N   . LYS J  1 71  ? 22.858  183.647 41.464 1.00 44.18 ?  70  LYS J N   1 
ATOM   10406 C  CA  . LYS J  1 71  ? 22.758  183.249 42.859 1.00 40.90 ?  70  LYS J CA  1 
ATOM   10407 C  C   . LYS J  1 71  ? 24.146  183.131 43.481 1.00 40.66 ?  70  LYS J C   1 
ATOM   10408 O  O   . LYS J  1 71  ? 25.168  183.046 42.788 1.00 39.59 ?  70  LYS J O   1 
ATOM   10409 C  CB  . LYS J  1 71  ? 22.011  181.929 43.006 1.00 47.76 ?  70  LYS J CB  1 
ATOM   10410 C  CG  . LYS J  1 71  ? 20.549  181.987 42.587 1.00 48.67 ?  70  LYS J CG  1 
ATOM   10411 C  CD  . LYS J  1 71  ? 20.009  180.585 42.274 1.00 53.25 ?  70  LYS J CD  1 
ATOM   10412 C  CE  . LYS J  1 71  ? 20.856  179.481 42.942 1.00 58.46 ?  70  LYS J CE  1 
ATOM   10413 N  NZ  . LYS J  1 71  ? 20.987  178.228 42.108 1.00 62.89 ?  70  LYS J NZ  1 
ATOM   10414 N  N   . HIS J  1 72  ? 24.168  183.144 44.809 1.00 40.54 ?  71  HIS J N   1 
ATOM   10415 C  CA  . HIS J  1 72  ? 25.417  183.014 45.546 1.00 38.84 ?  71  HIS J CA  1 
ATOM   10416 C  C   . HIS J  1 72  ? 25.987  181.600 45.399 1.00 39.46 ?  71  HIS J C   1 
ATOM   10417 O  O   . HIS J  1 72  ? 25.245  180.618 45.353 1.00 39.74 ?  71  HIS J O   1 
ATOM   10418 C  CB  . HIS J  1 72  ? 25.171  183.339 47.018 1.00 37.39 ?  71  HIS J CB  1 
ATOM   10419 C  CG  . HIS J  1 72  ? 26.378  183.171 47.879 1.00 37.84 ?  71  HIS J CG  1 
ATOM   10420 N  ND1 . HIS J  1 72  ? 27.422  184.067 47.876 1.00 39.72 ?  71  HIS J ND1 1 
ATOM   10421 C  CD2 . HIS J  1 72  ? 26.726  182.188 48.742 1.00 36.01 ?  71  HIS J CD2 1 
ATOM   10422 C  CE1 . HIS J  1 72  ? 28.352  183.661 48.720 1.00 35.37 ?  71  HIS J CE1 1 
ATOM   10423 N  NE2 . HIS J  1 72  ? 27.953  182.522 49.261 1.00 40.51 ?  71  HIS J NE2 1 
ATOM   10424 N  N   . GLY J  1 73  ? 27.310  181.504 45.315 1.00 38.38 ?  72  GLY J N   1 
ATOM   10425 C  CA  . GLY J  1 73  ? 27.990  180.228 45.346 1.00 39.20 ?  72  GLY J CA  1 
ATOM   10426 C  C   . GLY J  1 73  ? 29.441  180.415 45.725 1.00 41.77 ?  72  GLY J C   1 
ATOM   10427 O  O   . GLY J  1 73  ? 29.869  181.509 46.096 1.00 41.86 ?  72  GLY J O   1 
ATOM   10428 N  N   . GLY J  1 74  ? 30.208  179.331 45.640 1.00 39.38 ?  73  GLY J N   1 
ATOM   10429 C  CA  . GLY J  1 74  ? 31.625  179.413 45.916 1.00 34.97 ?  73  GLY J CA  1 
ATOM   10430 C  C   . GLY J  1 74  ? 32.403  179.914 44.718 1.00 35.85 ?  73  GLY J C   1 
ATOM   10431 O  O   . GLY J  1 74  ? 31.909  179.979 43.591 1.00 36.47 ?  73  GLY J O   1 
ATOM   10432 N  N   . PRO J  1 75  ? 33.664  180.274 44.954 1.00 35.01 ?  74  PRO J N   1 
ATOM   10433 C  CA  . PRO J  1 75  ? 34.479  180.837 43.865 1.00 34.29 ?  74  PRO J CA  1 
ATOM   10434 C  C   . PRO J  1 75  ? 34.675  179.884 42.693 1.00 46.21 ?  74  PRO J C   1 
ATOM   10435 O  O   . PRO J  1 75  ? 34.921  180.351 41.571 1.00 43.28 ?  74  PRO J O   1 
ATOM   10436 C  CB  . PRO J  1 75  ? 35.813  181.168 44.544 1.00 35.26 ?  74  PRO J CB  1 
ATOM   10437 C  CG  . PRO J  1 75  ? 35.796  180.401 45.831 1.00 38.92 ?  74  PRO J CG  1 
ATOM   10438 C  CD  . PRO J  1 75  ? 34.388  180.184 46.226 1.00 36.21 ?  74  PRO J CD  1 
ATOM   10439 N  N   . LYS J  1 76  ? 34.547  178.571 42.906 1.00 42.22 ?  75  LYS J N   1 
ATOM   10440 C  CA  . LYS J  1 76  ? 34.763  177.590 41.848 1.00 43.85 ?  75  LYS J CA  1 
ATOM   10441 C  C   . LYS J  1 76  ? 33.477  177.213 41.121 1.00 44.92 ?  75  LYS J C   1 
ATOM   10442 O  O   . LYS J  1 76  ? 33.533  176.467 40.140 1.00 48.40 ?  75  LYS J O   1 
ATOM   10443 C  CB  . LYS J  1 76  ? 35.433  176.325 42.428 1.00 41.44 ?  75  LYS J CB  1 
ATOM   10444 C  CG  . LYS J  1 76  ? 36.440  176.615 43.538 1.00 55.55 ?  75  LYS J CG  1 
ATOM   10445 C  CD  . LYS J  1 76  ? 37.832  176.983 43.035 1.00 63.62 ?  75  LYS J CD  1 
ATOM   10446 C  CE  . LYS J  1 76  ? 38.834  177.154 44.229 1.00 65.10 ?  75  LYS J CE  1 
ATOM   10447 N  NZ  . LYS J  1 76  ? 39.775  175.992 44.492 1.00 52.77 ?  75  LYS J NZ  1 
ATOM   10448 N  N   . ASP J  1 77  ? 32.325  177.701 41.571 1.00 45.31 ?  76  ASP J N   1 
ATOM   10449 C  CA  . ASP J  1 77  ? 31.067  177.426 40.899 1.00 43.05 ?  76  ASP J CA  1 
ATOM   10450 C  C   . ASP J  1 77  ? 30.915  178.314 39.667 1.00 47.99 ?  76  ASP J C   1 
ATOM   10451 O  O   . ASP J  1 77  ? 31.510  179.387 39.561 1.00 47.77 ?  76  ASP J O   1 
ATOM   10452 C  CB  . ASP J  1 77  ? 29.881  177.661 41.841 1.00 44.66 ?  76  ASP J CB  1 
ATOM   10453 C  CG  . ASP J  1 77  ? 29.902  176.740 43.056 1.00 50.17 ?  76  ASP J CG  1 
ATOM   10454 O  OD1 . ASP J  1 77  ? 29.299  177.097 44.094 1.00 44.87 ?  76  ASP J OD1 1 
ATOM   10455 O  OD2 . ASP J  1 77  ? 30.516  175.652 42.966 1.00 55.24 ?  76  ASP J OD2 1 
ATOM   10456 N  N   . GLU J  1 78  ? 30.114  177.845 38.714 1.00 51.40 ?  77  GLU J N   1 
ATOM   10457 C  CA  . GLU J  1 78  ? 29.746  178.726 37.615 1.00 50.08 ?  77  GLU J CA  1 
ATOM   10458 C  C   . GLU J  1 78  ? 28.617  179.651 38.033 1.00 50.55 ?  77  GLU J C   1 
ATOM   10459 O  O   . GLU J  1 78  ? 28.610  180.833 37.666 1.00 51.98 ?  77  GLU J O   1 
ATOM   10460 C  CB  . GLU J  1 78  ? 29.345  177.920 36.382 1.00 54.66 ?  77  GLU J CB  1 
ATOM   10461 C  CG  . GLU J  1 78  ? 28.800  178.798 35.250 1.00 67.17 ?  77  GLU J CG  1 
ATOM   10462 C  CD  . GLU J  1 78  ? 28.319  178.005 34.033 1.00 80.38 ?  77  GLU J CD  1 
ATOM   10463 O  OE1 . GLU J  1 78  ? 28.184  178.617 32.945 1.00 76.20 ?  77  GLU J OE1 1 
ATOM   10464 O  OE2 . GLU J  1 78  ? 28.073  176.780 34.164 1.00 82.39 ?  77  GLU J OE2 1 
ATOM   10465 N  N   . GLU J  1 79  ? 27.657  179.129 38.797 1.00 43.42 ?  78  GLU J N   1 
ATOM   10466 C  CA  . GLU J  1 79  ? 26.603  179.944 39.396 1.00 47.62 ?  78  GLU J CA  1 
ATOM   10467 C  C   . GLU J  1 79  ? 27.175  180.581 40.651 1.00 45.15 ?  78  GLU J C   1 
ATOM   10468 O  O   . GLU J  1 79  ? 27.228  179.956 41.712 1.00 46.43 ?  78  GLU J O   1 
ATOM   10469 C  CB  . GLU J  1 79  ? 25.370  179.105 39.709 1.00 48.77 ?  78  GLU J CB  1 
ATOM   10470 C  CG  . GLU J  1 79  ? 24.173  179.902 40.246 1.00 52.91 ?  78  GLU J CG  1 
ATOM   10471 C  CD  . GLU J  1 79  ? 23.485  180.752 39.175 1.00 56.15 ?  78  GLU J CD  1 
ATOM   10472 O  OE1 . GLU J  1 79  ? 23.954  180.755 38.012 1.00 63.88 ?  78  GLU J OE1 1 
ATOM   10473 O  OE2 . GLU J  1 79  ? 22.473  181.419 39.495 1.00 54.27 ?  78  GLU J OE2 1 
ATOM   10474 N  N   . ARG J  1 80  ? 27.629  181.825 40.522 1.00 45.64 ?  79  ARG J N   1 
ATOM   10475 C  CA  . ARG J  1 80  ? 28.184  182.556 41.653 1.00 41.85 ?  79  ARG J CA  1 
ATOM   10476 C  C   . ARG J  1 80  ? 28.011  184.044 41.401 1.00 45.99 ?  79  ARG J C   1 
ATOM   10477 O  O   . ARG J  1 80  ? 27.883  184.487 40.255 1.00 43.32 ?  79  ARG J O   1 
ATOM   10478 C  CB  . ARG J  1 80  ? 29.657  182.228 41.856 1.00 39.20 ?  79  ARG J CB  1 
ATOM   10479 C  CG  . ARG J  1 80  ? 30.534  182.727 40.726 1.00 39.13 ?  79  ARG J CG  1 
ATOM   10480 C  CD  . ARG J  1 80  ? 31.996  182.578 41.066 1.00 36.40 ?  79  ARG J CD  1 
ATOM   10481 N  NE  . ARG J  1 80  ? 32.556  183.842 41.511 1.00 34.99 ?  79  ARG J NE  1 
ATOM   10482 C  CZ  . ARG J  1 80  ? 33.849  184.080 41.663 1.00 40.54 ?  79  ARG J CZ  1 
ATOM   10483 N  NH1 . ARG J  1 80  ? 34.755  183.140 41.447 1.00 36.00 ?  79  ARG J NH1 1 
ATOM   10484 N  NH2 . ARG J  1 80  ? 34.247  185.297 42.037 1.00 36.53 ?  79  ARG J NH2 1 
ATOM   10485 N  N   . HIS J  1 81  ? 28.005  184.809 42.487 1.00 41.09 ?  80  HIS J N   1 
ATOM   10486 C  CA  . HIS J  1 81  ? 28.164  186.248 42.376 1.00 39.70 ?  80  HIS J CA  1 
ATOM   10487 C  C   . HIS J  1 81  ? 29.599  186.555 41.962 1.00 40.08 ?  80  HIS J C   1 
ATOM   10488 O  O   . HIS J  1 81  ? 30.526  185.800 42.267 1.00 39.74 ?  80  HIS J O   1 
ATOM   10489 C  CB  . HIS J  1 81  ? 27.842  186.932 43.709 1.00 35.36 ?  80  HIS J CB  1 
ATOM   10490 C  CG  . HIS J  1 81  ? 26.438  186.719 44.195 1.00 36.89 ?  80  HIS J CG  1 
ATOM   10491 N  ND1 . HIS J  1 81  ? 26.118  186.654 45.536 1.00 33.41 ?  80  HIS J ND1 1 
ATOM   10492 C  CD2 . HIS J  1 81  ? 25.271  186.574 43.526 1.00 37.12 ?  80  HIS J CD2 1 
ATOM   10493 C  CE1 . HIS J  1 81  ? 24.819  186.466 45.671 1.00 31.49 ?  80  HIS J CE1 1 
ATOM   10494 N  NE2 . HIS J  1 81  ? 24.279  186.419 44.467 1.00 38.54 ?  80  HIS J NE2 1 
ATOM   10495 N  N   . VAL J  1 82  ? 29.788  187.675 41.257 1.00 39.34 ?  81  VAL J N   1 
ATOM   10496 C  CA  . VAL J  1 82  ? 31.149  188.093 40.929 1.00 32.75 ?  81  VAL J CA  1 
ATOM   10497 C  C   . VAL J  1 82  ? 31.972  188.274 42.206 1.00 35.55 ?  81  VAL J C   1 
ATOM   10498 O  O   . VAL J  1 82  ? 33.144  187.883 42.272 1.00 37.52 ?  81  VAL J O   1 
ATOM   10499 C  CB  . VAL J  1 82  ? 31.131  189.371 40.063 1.00 40.67 ?  81  VAL J CB  1 
ATOM   10500 C  CG1 . VAL J  1 82  ? 32.535  189.895 39.871 1.00 40.81 ?  81  VAL J CG1 1 
ATOM   10501 C  CG2 . VAL J  1 82  ? 30.492  189.092 38.702 1.00 40.68 ?  81  VAL J CG2 1 
ATOM   10502 N  N   . GLY J  1 83  ? 31.373  188.841 43.247 1.00 32.19 ?  82  GLY J N   1 
ATOM   10503 C  CA  . GLY J  1 83  ? 32.147  189.067 44.461 1.00 36.62 ?  82  GLY J CA  1 
ATOM   10504 C  C   . GLY J  1 83  ? 32.326  187.876 45.393 1.00 35.05 ?  82  GLY J C   1 
ATOM   10505 O  O   . GLY J  1 83  ? 32.918  188.029 46.468 1.00 37.66 ?  82  GLY J O   1 
ATOM   10506 N  N   . ASP J  1 84  ? 31.843  186.692 45.019 1.00 35.29 ?  83  ASP J N   1 
ATOM   10507 C  CA  . ASP J  1 84  ? 31.932  185.516 45.882 1.00 38.24 ?  83  ASP J CA  1 
ATOM   10508 C  C   . ASP J  1 84  ? 33.336  184.933 45.898 1.00 39.61 ?  83  ASP J C   1 
ATOM   10509 O  O   . ASP J  1 84  ? 33.652  184.065 45.081 1.00 40.96 ?  83  ASP J O   1 
ATOM   10510 C  CB  . ASP J  1 84  ? 30.958  184.440 45.403 1.00 35.29 ?  83  ASP J CB  1 
ATOM   10511 C  CG  . ASP J  1 84  ? 29.531  184.792 45.679 1.00 37.29 ?  83  ASP J CG  1 
ATOM   10512 O  OD1 . ASP J  1 84  ? 29.277  185.730 46.489 1.00 36.72 ?  83  ASP J OD1 1 
ATOM   10513 O  OD2 . ASP J  1 84  ? 28.651  184.127 45.088 1.00 35.85 ?  83  ASP J OD2 1 
ATOM   10514 N  N   . LEU J  1 85  ? 34.189  185.364 46.817 1.00 35.86 ?  84  LEU J N   1 
ATOM   10515 C  CA  . LEU J  1 85  ? 35.532  184.817 46.858 1.00 32.67 ?  84  LEU J CA  1 
ATOM   10516 C  C   . LEU J  1 85  ? 35.660  183.638 47.810 1.00 38.14 ?  84  LEU J C   1 
ATOM   10517 O  O   . LEU J  1 85  ? 36.778  183.172 48.046 1.00 41.52 ?  84  LEU J O   1 
ATOM   10518 C  CB  . LEU J  1 85  ? 36.532  185.905 47.241 1.00 31.33 ?  84  LEU J CB  1 
ATOM   10519 C  CG  . LEU J  1 85  ? 36.643  187.028 46.208 1.00 35.48 ?  84  LEU J CG  1 
ATOM   10520 C  CD1 . LEU J  1 85  ? 37.684  188.054 46.646 1.00 36.45 ?  84  LEU J CD1 1 
ATOM   10521 C  CD2 . LEU J  1 85  ? 36.934  186.472 44.796 1.00 36.55 ?  84  LEU J CD2 1 
ATOM   10522 N  N   . GLY J  1 86  ? 34.556  183.149 48.360 1.00 35.60 ?  85  GLY J N   1 
ATOM   10523 C  CA  . GLY J  1 86  ? 34.611  181.968 49.216 1.00 35.19 ?  85  GLY J CA  1 
ATOM   10524 C  C   . GLY J  1 86  ? 34.940  182.311 50.657 1.00 42.16 ?  85  GLY J C   1 
ATOM   10525 O  O   . GLY J  1 86  ? 34.398  183.273 51.230 1.00 37.73 ?  85  GLY J O   1 
ATOM   10526 N  N   . ASN J  1 87  ? 35.830  181.517 51.256 1.00 36.53 ?  86  ASN J N   1 
ATOM   10527 C  CA  . ASN J  1 87  ? 36.236  181.673 52.647 1.00 33.87 ?  86  ASN J CA  1 
ATOM   10528 C  C   . ASN J  1 87  ? 37.729  181.925 52.751 1.00 35.77 ?  86  ASN J C   1 
ATOM   10529 O  O   . ASN J  1 87  ? 38.509  181.515 51.886 1.00 39.27 ?  86  ASN J O   1 
ATOM   10530 C  CB  . ASN J  1 87  ? 35.930  180.425 53.471 1.00 34.52 ?  86  ASN J CB  1 
ATOM   10531 C  CG  . ASN J  1 87  ? 34.471  180.222 53.701 1.00 37.03 ?  86  ASN J CG  1 
ATOM   10532 O  OD1 . ASN J  1 87  ? 33.837  180.986 54.431 1.00 33.31 ?  86  ASN J OD1 1 
ATOM   10533 N  ND2 . ASN J  1 87  ? 33.922  179.165 53.106 1.00 35.18 ?  86  ASN J ND2 1 
ATOM   10534 N  N   . VAL J  1 88  ? 38.114  182.590 53.833 1.00 33.78 ?  87  VAL J N   1 
ATOM   10535 C  CA  . VAL J  1 88  ? 39.491  182.640 54.294 1.00 34.89 ?  87  VAL J CA  1 
ATOM   10536 C  C   . VAL J  1 88  ? 39.532  181.922 55.639 1.00 34.02 ?  87  VAL J C   1 
ATOM   10537 O  O   . VAL J  1 88  ? 38.509  181.761 56.310 1.00 41.22 ?  87  VAL J O   1 
ATOM   10538 C  CB  . VAL J  1 88  ? 40.016  184.084 54.413 1.00 35.91 ?  87  VAL J CB  1 
ATOM   10539 C  CG1 . VAL J  1 88  ? 39.953  184.769 53.056 1.00 36.22 ?  87  VAL J CG1 1 
ATOM   10540 C  CG2 . VAL J  1 88  ? 39.192  184.845 55.426 1.00 34.66 ?  87  VAL J CG2 1 
ATOM   10541 N  N   . THR J  1 89  ? 40.719  181.463 56.024 1.00 37.84 ?  88  THR J N   1 
ATOM   10542 C  CA  . THR J  1 89  ? 40.869  180.652 57.229 1.00 35.96 ?  88  THR J CA  1 
ATOM   10543 C  C   . THR J  1 89  ? 41.783  181.346 58.224 1.00 40.71 ?  88  THR J C   1 
ATOM   10544 O  O   . THR J  1 89  ? 42.916  181.704 57.893 1.00 40.46 ?  88  THR J O   1 
ATOM   10545 C  CB  . THR J  1 89  ? 41.425  179.251 56.912 1.00 43.65 ?  88  THR J CB  1 
ATOM   10546 O  OG1 . THR J  1 89  ? 40.586  178.605 55.946 1.00 38.95 ?  88  THR J OG1 1 
ATOM   10547 C  CG2 . THR J  1 89  ? 41.460  178.396 58.184 1.00 39.35 ?  88  THR J CG2 1 
ATOM   10548 N  N   . ALA J  1 90  ? 41.288  181.521 59.442 1.00 40.48 ?  89  ALA J N   1 
ATOM   10549 C  CA  . ALA J  1 90  ? 42.077  182.052 60.540 1.00 45.50 ?  89  ALA J CA  1 
ATOM   10550 C  C   . ALA J  1 90  ? 42.662  180.890 61.334 1.00 47.73 ?  89  ALA J C   1 
ATOM   10551 O  O   . ALA J  1 90  ? 41.964  179.912 61.615 1.00 48.26 ?  89  ALA J O   1 
ATOM   10552 C  CB  . ALA J  1 90  ? 41.214  182.936 61.441 1.00 43.01 ?  89  ALA J CB  1 
ATOM   10553 N  N   . ASP J  1 91  ? 43.948  180.986 61.671 1.00 51.29 ?  90  ASP J N   1 
ATOM   10554 C  CA  . ASP J  1 91  ? 44.580  179.969 62.502 1.00 51.73 ?  90  ASP J CA  1 
ATOM   10555 C  C   . ASP J  1 91  ? 44.233  180.212 63.969 1.00 49.28 ?  90  ASP J C   1 
ATOM   10556 O  O   . ASP J  1 91  ? 43.443  181.097 64.309 1.00 52.77 ?  90  ASP J O   1 
ATOM   10557 C  CB  . ASP J  1 91  ? 46.089  179.939 62.255 1.00 50.75 ?  90  ASP J CB  1 
ATOM   10558 C  CG  . ASP J  1 91  ? 46.778  181.255 62.588 1.00 56.03 ?  90  ASP J CG  1 
ATOM   10559 O  OD1 . ASP J  1 91  ? 47.750  181.599 61.877 1.00 59.03 ?  90  ASP J OD1 1 
ATOM   10560 O  OD2 . ASP J  1 91  ? 46.382  181.932 63.569 1.00 58.38 ?  90  ASP J OD2 1 
ATOM   10561 N  N   . LYS J  1 92  ? 44.821  179.415 64.864 1.00 54.35 ?  91  LYS J N   1 
ATOM   10562 C  CA  . LYS J  1 92  ? 44.457  179.522 66.275 1.00 50.96 ?  91  LYS J CA  1 
ATOM   10563 C  C   . LYS J  1 92  ? 44.889  180.855 66.880 1.00 53.43 ?  91  LYS J C   1 
ATOM   10564 O  O   . LYS J  1 92  ? 44.354  181.256 67.922 1.00 52.66 ?  91  LYS J O   1 
ATOM   10565 C  CB  . LYS J  1 92  ? 45.049  178.349 67.068 1.00 57.24 ?  91  LYS J CB  1 
ATOM   10566 C  CG  . LYS J  1 92  ? 46.562  178.161 66.921 1.00 57.22 ?  91  LYS J CG  1 
ATOM   10567 C  CD  . LYS J  1 92  ? 47.015  176.822 67.537 1.00 65.38 ?  91  LYS J CD  1 
ATOM   10568 C  CE  . LYS J  1 92  ? 48.266  176.981 68.421 1.00 65.39 ?  91  LYS J CE  1 
ATOM   10569 N  NZ  . LYS J  1 92  ? 48.249  176.100 69.647 1.00 63.96 ?  91  LYS J NZ  1 
ATOM   10570 N  N   . ASP J  1 93  ? 45.830  181.551 66.248 1.00 53.56 ?  92  ASP J N   1 
ATOM   10571 C  CA  . ASP J  1 93  ? 46.203  182.902 66.648 1.00 57.71 ?  92  ASP J CA  1 
ATOM   10572 C  C   . ASP J  1 93  ? 45.251  183.967 66.105 1.00 60.32 ?  92  ASP J C   1 
ATOM   10573 O  O   . ASP J  1 93  ? 45.461  185.158 66.365 1.00 55.59 ?  92  ASP J O   1 
ATOM   10574 C  CB  . ASP J  1 93  ? 47.631  183.208 66.178 1.00 59.21 ?  92  ASP J CB  1 
ATOM   10575 C  CG  . ASP J  1 93  ? 48.677  182.385 66.915 1.00 68.19 ?  92  ASP J CG  1 
ATOM   10576 O  OD1 . ASP J  1 93  ? 48.630  182.345 68.167 1.00 57.01 ?  92  ASP J OD1 1 
ATOM   10577 O  OD2 . ASP J  1 93  ? 49.536  181.772 66.239 1.00 70.25 ?  92  ASP J OD2 1 
ATOM   10578 N  N   . GLY J  1 94  ? 44.230  183.578 65.349 1.00 54.38 ?  93  GLY J N   1 
ATOM   10579 C  CA  . GLY J  1 94  ? 43.325  184.545 64.773 1.00 46.77 ?  93  GLY J CA  1 
ATOM   10580 C  C   . GLY J  1 94  ? 43.806  185.202 63.502 1.00 50.86 ?  93  GLY J C   1 
ATOM   10581 O  O   . GLY J  1 94  ? 43.193  186.183 63.064 1.00 50.85 ?  93  GLY J O   1 
ATOM   10582 N  N   . VAL J  1 95  ? 44.871  184.693 62.884 1.00 47.97 ?  94  VAL J N   1 
ATOM   10583 C  CA  . VAL J  1 95  ? 45.431  185.281 61.672 1.00 44.32 ?  94  VAL J CA  1 
ATOM   10584 C  C   . VAL J  1 95  ? 44.978  184.471 60.469 1.00 44.61 ?  94  VAL J C   1 
ATOM   10585 O  O   . VAL J  1 95  ? 45.033  183.235 60.483 1.00 49.62 ?  94  VAL J O   1 
ATOM   10586 C  CB  . VAL J  1 95  ? 46.966  185.343 61.736 1.00 44.45 ?  94  VAL J CB  1 
ATOM   10587 C  CG1 . VAL J  1 95  ? 47.547  185.658 60.353 1.00 49.26 ?  94  VAL J CG1 1 
ATOM   10588 C  CG2 . VAL J  1 95  ? 47.406  186.375 62.755 1.00 50.65 ?  94  VAL J CG2 1 
ATOM   10589 N  N   . ALA J  1 96  ? 44.530  185.165 59.431 1.00 41.62 ?  95  ALA J N   1 
ATOM   10590 C  CA  . ALA J  1 96  ? 44.224  184.563 58.139 1.00 47.43 ?  95  ALA J CA  1 
ATOM   10591 C  C   . ALA J  1 96  ? 45.260  185.057 57.139 1.00 48.20 ?  95  ALA J C   1 
ATOM   10592 O  O   . ALA J  1 96  ? 45.302  186.251 56.827 1.00 46.19 ?  95  ALA J O   1 
ATOM   10593 C  CB  . ALA J  1 96  ? 42.809  184.909 57.678 1.00 41.77 ?  95  ALA J CB  1 
ATOM   10594 N  N   . ASP J  1 97  ? 46.095  184.143 56.633 1.00 46.04 ?  96  ASP J N   1 
ATOM   10595 C  CA  . ASP J  1 97  ? 47.053  184.485 55.582 1.00 42.56 ?  96  ASP J CA  1 
ATOM   10596 C  C   . ASP J  1 97  ? 46.381  184.242 54.242 1.00 48.37 ?  96  ASP J C   1 
ATOM   10597 O  O   . ASP J  1 97  ? 46.462  183.153 53.683 1.00 56.08 ?  96  ASP J O   1 
ATOM   10598 C  CB  . ASP J  1 97  ? 48.338  183.676 55.712 1.00 47.13 ?  96  ASP J CB  1 
ATOM   10599 C  CG  . ASP J  1 97  ? 49.128  184.035 56.948 1.00 52.41 ?  96  ASP J CG  1 
ATOM   10600 O  OD1 . ASP J  1 97  ? 49.712  185.147 56.980 1.00 57.54 ?  96  ASP J OD1 1 
ATOM   10601 O  OD2 . ASP J  1 97  ? 49.162  183.201 57.887 1.00 59.55 ?  96  ASP J OD2 1 
ATOM   10602 N  N   . VAL J  1 98  ? 45.765  185.261 53.697 1.00 42.46 ?  97  VAL J N   1 
ATOM   10603 C  CA  . VAL J  1 98  ? 44.927  185.086 52.523 1.00 41.98 ?  97  VAL J CA  1 
ATOM   10604 C  C   . VAL J  1 98  ? 45.800  184.862 51.297 1.00 43.16 ?  97  VAL J C   1 
ATOM   10605 O  O   . VAL J  1 98  ? 46.830  185.522 51.114 1.00 43.04 ?  97  VAL J O   1 
ATOM   10606 C  CB  . VAL J  1 98  ? 44.013  186.312 52.354 1.00 39.37 ?  97  VAL J CB  1 
ATOM   10607 C  CG1 . VAL J  1 98  ? 43.255  186.230 51.048 1.00 38.95 ?  97  VAL J CG1 1 
ATOM   10608 C  CG2 . VAL J  1 98  ? 43.070  186.388 53.525 1.00 37.43 ?  97  VAL J CG2 1 
ATOM   10609 N  N   . SER J  1 99  ? 45.397  183.910 50.460 1.00 42.60 ?  98  SER J N   1 
ATOM   10610 C  CA  . SER J  1 99  ? 46.036  183.719 49.165 1.00 42.71 ?  98  SER J CA  1 
ATOM   10611 C  C   . SER J  1 99  ? 45.020  183.039 48.264 1.00 41.98 ?  98  SER J C   1 
ATOM   10612 O  O   . SER J  1 99  ? 44.706  181.861 48.443 1.00 48.24 ?  98  SER J O   1 
ATOM   10613 C  CB  . SER J  1 99  ? 47.314  182.899 49.282 1.00 48.91 ?  98  SER J CB  1 
ATOM   10614 O  OG  . SER J  1 99  ? 48.176  183.212 48.204 1.00 57.55 ?  98  SER J OG  1 
ATOM   10615 N  N   . ILE J  1 100 ? 44.502  183.788 47.308 1.00 41.97 ?  99  ILE J N   1 
ATOM   10616 C  CA  . ILE J  1 100 ? 43.411  183.339 46.462 1.00 39.69 ?  99  ILE J CA  1 
ATOM   10617 C  C   . ILE J  1 100 ? 43.750  183.770 45.048 1.00 42.17 ?  99  ILE J C   1 
ATOM   10618 O  O   . ILE J  1 100 ? 44.406  184.795 44.837 1.00 42.74 ?  99  ILE J O   1 
ATOM   10619 C  CB  . ILE J  1 100 ? 42.041  183.924 46.930 1.00 47.70 ?  99  ILE J CB  1 
ATOM   10620 C  CG1 . ILE J  1 100 ? 41.572  183.249 48.225 1.00 46.65 ?  99  ILE J CG1 1 
ATOM   10621 C  CG2 . ILE J  1 100 ? 40.963  183.751 45.877 1.00 46.02 ?  99  ILE J CG2 1 
ATOM   10622 C  CD1 . ILE J  1 100 ? 40.890  184.178 49.220 1.00 46.21 ?  99  ILE J CD1 1 
ATOM   10623 N  N   . GLU J  1 101 ? 43.333  182.966 44.076 1.00 42.67 ?  100 GLU J N   1 
ATOM   10624 C  CA  . GLU J  1 101 ? 43.398  183.353 42.677 1.00 42.13 ?  100 GLU J CA  1 
ATOM   10625 C  C   . GLU J  1 101 ? 41.994  183.254 42.111 1.00 41.85 ?  100 GLU J C   1 
ATOM   10626 O  O   . GLU J  1 101 ? 41.309  182.250 42.320 1.00 45.06 ?  100 GLU J O   1 
ATOM   10627 C  CB  . GLU J  1 101 ? 44.364  182.459 41.895 1.00 51.28 ?  100 GLU J CB  1 
ATOM   10628 C  CG  . GLU J  1 101 ? 44.775  183.030 40.552 1.00 53.55 ?  100 GLU J CG  1 
ATOM   10629 C  CD  . GLU J  1 101 ? 46.046  182.393 39.999 1.00 70.28 ?  100 GLU J CD  1 
ATOM   10630 O  OE1 . GLU J  1 101 ? 45.928  181.600 39.039 1.00 74.59 ?  100 GLU J OE1 1 
ATOM   10631 O  OE2 . GLU J  1 101 ? 47.152  182.683 40.521 1.00 67.93 ?  100 GLU J OE2 1 
ATOM   10632 N  N   . ASP J  1 102 ? 41.547  184.299 41.427 1.00 39.23 ?  101 ASP J N   1 
ATOM   10633 C  CA  . ASP J  1 102 ? 40.191  184.285 40.905 1.00 41.69 ?  101 ASP J CA  1 
ATOM   10634 C  C   . ASP J  1 102 ? 40.185  184.939 39.533 1.00 47.63 ?  101 ASP J C   1 
ATOM   10635 O  O   . ASP J  1 102 ? 40.872  185.940 39.303 1.00 52.34 ?  101 ASP J O   1 
ATOM   10636 C  CB  . ASP J  1 102 ? 39.214  184.996 41.870 1.00 43.86 ?  101 ASP J CB  1 
ATOM   10637 C  CG  . ASP J  1 102 ? 37.751  184.768 41.505 1.00 44.75 ?  101 ASP J CG  1 
ATOM   10638 O  OD1 . ASP J  1 102 ? 37.185  183.716 41.878 1.00 48.90 ?  101 ASP J OD1 1 
ATOM   10639 O  OD2 . ASP J  1 102 ? 37.153  185.643 40.839 1.00 46.32 ?  101 ASP J OD2 1 
ATOM   10640 N  N   . SER J  1 103 ? 39.418  184.366 38.619 1.00 47.89 ?  102 SER J N   1 
ATOM   10641 C  CA  . SER J  1 103 ? 39.369  184.877 37.263 1.00 52.52 ?  102 SER J CA  1 
ATOM   10642 C  C   . SER J  1 103 ? 38.058  185.579 36.959 1.00 54.51 ?  102 SER J C   1 
ATOM   10643 O  O   . SER J  1 103 ? 37.898  186.097 35.844 1.00 56.64 ?  102 SER J O   1 
ATOM   10644 C  CB  . SER J  1 103 ? 39.600  183.740 36.260 1.00 56.84 ?  102 SER J CB  1 
ATOM   10645 O  OG  . SER J  1 103 ? 38.679  182.681 36.493 1.00 65.17 ?  102 SER J OG  1 
ATOM   10646 N  N   . VAL J  1 104 ? 37.127  185.623 37.914 1.00 45.65 ?  103 VAL J N   1 
ATOM   10647 C  CA  . VAL J  1 104 ? 35.835  186.273 37.691 1.00 48.00 ?  103 VAL J CA  1 
ATOM   10648 C  C   . VAL J  1 104 ? 35.879  187.744 38.072 1.00 49.11 ?  103 VAL J C   1 
ATOM   10649 O  O   . VAL J  1 104 ? 35.431  188.613 37.316 1.00 46.82 ?  103 VAL J O   1 
ATOM   10650 C  CB  . VAL J  1 104 ? 34.724  185.535 38.458 1.00 46.20 ?  103 VAL J CB  1 
ATOM   10651 C  CG1 . VAL J  1 104 ? 33.378  186.092 38.037 1.00 48.20 ?  103 VAL J CG1 1 
ATOM   10652 C  CG2 . VAL J  1 104 ? 34.799  184.045 38.177 1.00 49.83 ?  103 VAL J CG2 1 
ATOM   10653 N  N   . ILE J  1 105 ? 36.396  188.054 39.261 1.00 45.68 ?  104 ILE J N   1 
ATOM   10654 C  CA  . ILE J  1 105 ? 36.658  189.444 39.554 1.00 44.60 ?  104 ILE J CA  1 
ATOM   10655 C  C   . ILE J  1 105 ? 37.679  189.961 38.543 1.00 46.30 ?  104 ILE J C   1 
ATOM   10656 O  O   . ILE J  1 105 ? 38.405  189.193 37.902 1.00 45.15 ?  104 ILE J O   1 
ATOM   10657 C  CB  . ILE J  1 105 ? 37.162  189.641 40.991 1.00 40.32 ?  104 ILE J CB  1 
ATOM   10658 C  CG1 . ILE J  1 105 ? 38.411  188.800 41.250 1.00 39.38 ?  104 ILE J CG1 1 
ATOM   10659 C  CG2 . ILE J  1 105 ? 36.068  189.300 42.005 1.00 43.46 ?  104 ILE J CG2 1 
ATOM   10660 C  CD1 . ILE J  1 105 ? 39.139  189.215 42.518 1.00 38.43 ?  104 ILE J CD1 1 
ATOM   10661 N  N   . SER J  1 106 ? 37.730  191.284 38.401 1.00 46.80 ?  105 SER J N   1 
ATOM   10662 C  CA  . SER J  1 106 ? 38.728  191.910 37.553 1.00 47.23 ?  105 SER J CA  1 
ATOM   10663 C  C   . SER J  1 106 ? 39.066  193.282 38.120 1.00 48.77 ?  105 SER J C   1 
ATOM   10664 O  O   . SER J  1 106 ? 38.281  193.875 38.862 1.00 45.39 ?  105 SER J O   1 
ATOM   10665 C  CB  . SER J  1 106 ? 38.232  192.018 36.103 1.00 49.35 ?  105 SER J CB  1 
ATOM   10666 O  OG  . SER J  1 106 ? 39.219  192.608 35.270 1.00 57.51 ?  105 SER J OG  1 
ATOM   10667 N  N   . LEU J  1 107 ? 40.256  193.775 37.772 1.00 51.67 ?  106 LEU J N   1 
ATOM   10668 C  CA  . LEU J  1 107 ? 40.670  195.133 38.098 1.00 48.12 ?  106 LEU J CA  1 
ATOM   10669 C  C   . LEU J  1 107 ? 40.382  196.129 36.964 1.00 50.11 ?  106 LEU J C   1 
ATOM   10670 O  O   . LEU J  1 107 ? 40.957  197.225 36.950 1.00 51.26 ?  106 LEU J O   1 
ATOM   10671 C  CB  . LEU J  1 107 ? 42.155  195.153 38.470 1.00 47.06 ?  106 LEU J CB  1 
ATOM   10672 C  CG  . LEU J  1 107 ? 42.556  194.342 39.707 1.00 47.90 ?  106 LEU J CG  1 
ATOM   10673 C  CD1 . LEU J  1 107 ? 44.005  194.622 40.093 1.00 41.62 ?  106 LEU J CD1 1 
ATOM   10674 C  CD2 . LEU J  1 107 ? 41.624  194.611 40.892 1.00 46.83 ?  106 LEU J CD2 1 
ATOM   10675 N  N   . SER J  1 108 ? 39.508  195.769 36.025 1.00 43.47 ?  107 SER J N   1 
ATOM   10676 C  CA  . SER J  1 108 ? 38.979  196.669 35.010 1.00 51.10 ?  107 SER J CA  1 
ATOM   10677 C  C   . SER J  1 108 ? 37.808  195.964 34.336 1.00 50.94 ?  107 SER J C   1 
ATOM   10678 O  O   . SER J  1 108 ? 37.654  194.745 34.450 1.00 57.01 ?  107 SER J O   1 
ATOM   10679 C  CB  . SER J  1 108 ? 40.051  197.051 33.984 1.00 53.71 ?  107 SER J CB  1 
ATOM   10680 O  OG  . SER J  1 108 ? 40.717  195.890 33.517 1.00 60.26 ?  107 SER J OG  1 
ATOM   10681 N  N   . GLY J  1 109 ? 36.979  196.735 33.645 1.00 49.65 ?  108 GLY J N   1 
ATOM   10682 C  CA  . GLY J  1 109 ? 35.874  196.151 32.892 1.00 51.87 ?  108 GLY J CA  1 
ATOM   10683 C  C   . GLY J  1 109 ? 34.574  196.084 33.673 1.00 56.00 ?  108 GLY J C   1 
ATOM   10684 O  O   . GLY J  1 109 ? 34.396  196.740 34.705 1.00 53.15 ?  108 GLY J O   1 
ATOM   10685 N  N   . ASP J  1 110 ? 33.644  195.261 33.161 1.00 62.52 ?  109 ASP J N   1 
ATOM   10686 C  CA  . ASP J  1 110 ? 32.324  195.133 33.787 1.00 61.20 ?  109 ASP J CA  1 
ATOM   10687 C  C   . ASP J  1 110 ? 32.411  194.565 35.196 1.00 63.25 ?  109 ASP J C   1 
ATOM   10688 O  O   . ASP J  1 110 ? 31.540  194.842 36.032 1.00 60.73 ?  109 ASP J O   1 
ATOM   10689 C  CB  . ASP J  1 110 ? 31.398  194.229 32.961 1.00 64.88 ?  109 ASP J CB  1 
ATOM   10690 C  CG  . ASP J  1 110 ? 31.617  194.360 31.465 1.00 77.33 ?  109 ASP J CG  1 
ATOM   10691 O  OD1 . ASP J  1 110 ? 32.177  193.411 30.864 1.00 81.67 ?  109 ASP J OD1 1 
ATOM   10692 O  OD2 . ASP J  1 110 ? 31.212  195.400 30.888 1.00 79.75 ?  109 ASP J OD2 1 
ATOM   10693 N  N   . HIS J  1 111 ? 33.416  193.729 35.462 1.00 56.58 ?  110 HIS J N   1 
ATOM   10694 C  CA  . HIS J  1 111 ? 33.590  193.107 36.766 1.00 54.69 ?  110 HIS J CA  1 
ATOM   10695 C  C   . HIS J  1 111 ? 34.634  193.820 37.599 1.00 51.53 ?  110 HIS J C   1 
ATOM   10696 O  O   . HIS J  1 111 ? 35.162  193.233 38.556 1.00 46.37 ?  110 HIS J O   1 
ATOM   10697 C  CB  . HIS J  1 111 ? 33.973  191.633 36.618 1.00 48.74 ?  110 HIS J CB  1 
ATOM   10698 C  CG  . HIS J  1 111 ? 32.986  190.834 35.834 1.00 56.11 ?  110 HIS J CG  1 
ATOM   10699 N  ND1 . HIS J  1 111 ? 33.182  189.504 35.525 1.00 57.50 ?  110 HIS J ND1 1 
ATOM   10700 C  CD2 . HIS J  1 111 ? 31.793  191.177 35.290 1.00 58.50 ?  110 HIS J CD2 1 
ATOM   10701 C  CE1 . HIS J  1 111 ? 32.152  189.062 34.824 1.00 55.83 ?  110 HIS J CE1 1 
ATOM   10702 N  NE2 . HIS J  1 111 ? 31.295  190.057 34.669 1.00 58.58 ?  110 HIS J NE2 1 
ATOM   10703 N  N   . CYS J  1 112 ? 34.967  195.056 37.238 1.00 48.37 ?  111 CYS J N   1 
ATOM   10704 C  CA  . CYS J  1 112 ? 35.948  195.791 38.014 1.00 43.41 ?  111 CYS J CA  1 
ATOM   10705 C  C   . CYS J  1 112 ? 35.491  195.899 39.463 1.00 44.03 ?  111 CYS J C   1 
ATOM   10706 O  O   . CYS J  1 112 ? 34.317  196.152 39.750 1.00 43.79 ?  111 CYS J O   1 
ATOM   10707 C  CB  . CYS J  1 112 ? 36.168  197.179 37.422 1.00 42.22 ?  111 CYS J CB  1 
ATOM   10708 S  SG  . CYS J  1 112 ? 37.588  197.990 38.158 1.00 47.31 ?  111 CYS J SG  1 
ATOM   10709 N  N   . ILE J  1 113 ? 36.419  195.667 40.385 1.00 43.38 ?  112 ILE J N   1 
ATOM   10710 C  CA  . ILE J  1 113 ? 36.125  195.780 41.806 1.00 46.41 ?  112 ILE J CA  1 
ATOM   10711 C  C   . ILE J  1 113 ? 36.785  196.991 42.424 1.00 38.91 ?  112 ILE J C   1 
ATOM   10712 O  O   . ILE J  1 113 ? 36.642  197.211 43.638 1.00 41.54 ?  112 ILE J O   1 
ATOM   10713 C  CB  . ILE J  1 113 ? 36.527  194.503 42.564 1.00 40.40 ?  112 ILE J CB  1 
ATOM   10714 C  CG1 . ILE J  1 113 ? 38.042  194.331 42.520 1.00 39.98 ?  112 ILE J CG1 1 
ATOM   10715 C  CG2 . ILE J  1 113 ? 35.826  193.298 41.969 1.00 39.24 ?  112 ILE J CG2 1 
ATOM   10716 C  CD1 . ILE J  1 113 ? 38.521  193.130 43.334 1.00 41.66 ?  112 ILE J CD1 1 
ATOM   10717 N  N   . ILE J  1 114 ? 37.520  197.779 41.632 1.00 43.78 ?  113 ILE J N   1 
ATOM   10718 C  CA  . ILE J  1 114 ? 38.077  199.033 42.123 1.00 43.45 ?  113 ILE J CA  1 
ATOM   10719 C  C   . ILE J  1 114 ? 36.930  199.921 42.571 1.00 41.36 ?  113 ILE J C   1 
ATOM   10720 O  O   . ILE J  1 114 ? 35.934  200.085 41.854 1.00 43.27 ?  113 ILE J O   1 
ATOM   10721 C  CB  . ILE J  1 114 ? 38.911  199.720 41.031 1.00 49.56 ?  113 ILE J CB  1 
ATOM   10722 C  CG1 . ILE J  1 114 ? 40.112  198.860 40.629 1.00 51.46 ?  113 ILE J CG1 1 
ATOM   10723 C  CG2 . ILE J  1 114 ? 39.426  201.066 41.530 1.00 44.73 ?  113 ILE J CG2 1 
ATOM   10724 C  CD1 . ILE J  1 114 ? 40.954  198.428 41.804 1.00 49.80 ?  113 ILE J CD1 1 
ATOM   10725 N  N   . GLY J  1 115 ? 37.050  200.478 43.766 1.00 38.56 ?  114 GLY J N   1 
ATOM   10726 C  CA  . GLY J  1 115 ? 36.008  201.330 44.285 1.00 41.39 ?  114 GLY J CA  1 
ATOM   10727 C  C   . GLY J  1 115 ? 34.897  200.600 44.997 1.00 41.74 ?  114 GLY J C   1 
ATOM   10728 O  O   . GLY J  1 115 ? 34.006  201.253 45.562 1.00 36.64 ?  114 GLY J O   1 
ATOM   10729 N  N   . ARG J  1 116 ? 34.908  199.273 44.988 1.00 37.45 ?  115 ARG J N   1 
ATOM   10730 C  CA  . ARG J  1 116 ? 33.912  198.527 45.732 1.00 36.66 ?  115 ARG J CA  1 
ATOM   10731 C  C   . ARG J  1 116 ? 34.508  198.164 47.088 1.00 30.34 ?  115 ARG J C   1 
ATOM   10732 O  O   . ARG J  1 116 ? 35.586  198.637 47.452 1.00 35.36 ?  115 ARG J O   1 
ATOM   10733 C  CB  . ARG J  1 116 ? 33.435  197.347 44.895 1.00 35.99 ?  115 ARG J CB  1 
ATOM   10734 C  CG  . ARG J  1 116 ? 32.858  197.836 43.558 1.00 39.30 ?  115 ARG J CG  1 
ATOM   10735 C  CD  . ARG J  1 116 ? 32.210  196.729 42.741 1.00 42.87 ?  115 ARG J CD  1 
ATOM   10736 N  NE  . ARG J  1 116 ? 31.916  197.172 41.379 1.00 42.01 ?  115 ARG J NE  1 
ATOM   10737 C  CZ  . ARG J  1 116 ? 30.831  197.853 41.028 1.00 45.12 ?  115 ARG J CZ  1 
ATOM   10738 N  NH1 . ARG J  1 116 ? 29.891  198.166 41.910 1.00 41.91 ?  115 ARG J NH1 1 
ATOM   10739 N  NH2 . ARG J  1 116 ? 30.677  198.218 39.758 1.00 45.43 ?  115 ARG J NH2 1 
ATOM   10740 N  N   . THR J  1 117 ? 33.791  197.365 47.872 1.00 34.14 ?  116 THR J N   1 
ATOM   10741 C  CA  . THR J  1 117 ? 34.185  197.085 49.249 1.00 40.90 ?  116 THR J CA  1 
ATOM   10742 C  C   . THR J  1 117 ? 34.488  195.596 49.411 1.00 38.35 ?  116 THR J C   1 
ATOM   10743 O  O   . THR J  1 117 ? 33.761  194.740 48.901 1.00 38.37 ?  116 THR J O   1 
ATOM   10744 C  CB  . THR J  1 117 ? 33.094  197.526 50.250 1.00 39.91 ?  116 THR J CB  1 
ATOM   10745 O  OG1 . THR J  1 117 ? 33.098  198.958 50.371 1.00 42.47 ?  116 THR J OG1 1 
ATOM   10746 C  CG2 . THR J  1 117 ? 33.356  196.959 51.625 1.00 36.80 ?  116 THR J CG2 1 
ATOM   10747 N  N   . LEU J  1 118 ? 35.574  195.297 50.112 1.00 39.50 ?  117 LEU J N   1 
ATOM   10748 C  CA  . LEU J  1 118 ? 35.913  193.935 50.487 1.00 36.57 ?  117 LEU J CA  1 
ATOM   10749 C  C   . LEU J  1 118 ? 35.522  193.720 51.947 1.00 34.60 ?  117 LEU J C   1 
ATOM   10750 O  O   . LEU J  1 118 ? 35.897  194.512 52.809 1.00 33.71 ?  117 LEU J O   1 
ATOM   10751 C  CB  . LEU J  1 118 ? 37.404  193.689 50.282 1.00 37.93 ?  117 LEU J CB  1 
ATOM   10752 C  CG  . LEU J  1 118 ? 37.887  192.285 50.620 1.00 38.86 ?  117 LEU J CG  1 
ATOM   10753 C  CD1 . LEU J  1 118 ? 37.553  191.359 49.454 1.00 33.94 ?  117 LEU J CD1 1 
ATOM   10754 C  CD2 . LEU J  1 118 ? 39.386  192.299 50.896 1.00 39.79 ?  117 LEU J CD2 1 
ATOM   10755 N  N   . VAL J  1 119 ? 34.774  192.651 52.218 1.00 34.40 ?  118 VAL J N   1 
ATOM   10756 C  CA  . VAL J  1 119 ? 34.214  192.384 53.540 1.00 34.45 ?  118 VAL J CA  1 
ATOM   10757 C  C   . VAL J  1 119 ? 34.614  190.982 53.986 1.00 35.03 ?  118 VAL J C   1 
ATOM   10758 O  O   . VAL J  1 119 ? 34.400  190.014 53.250 1.00 34.38 ?  118 VAL J O   1 
ATOM   10759 C  CB  . VAL J  1 119 ? 32.677  192.501 53.524 1.00 33.62 ?  118 VAL J CB  1 
ATOM   10760 C  CG1 . VAL J  1 119 ? 32.113  192.182 54.893 1.00 35.64 ?  118 VAL J CG1 1 
ATOM   10761 C  CG2 . VAL J  1 119 ? 32.258  193.874 53.049 1.00 40.81 ?  118 VAL J CG2 1 
ATOM   10762 N  N   . VAL J  1 120 ? 35.156  190.867 55.196 1.00 33.10 ?  119 VAL J N   1 
ATOM   10763 C  CA  . VAL J  1 120 ? 35.372  189.573 55.841 1.00 34.37 ?  119 VAL J CA  1 
ATOM   10764 C  C   . VAL J  1 120 ? 34.262  189.366 56.865 1.00 36.27 ?  119 VAL J C   1 
ATOM   10765 O  O   . VAL J  1 120 ? 33.981  190.250 57.686 1.00 37.21 ?  119 VAL J O   1 
ATOM   10766 C  CB  . VAL J  1 120 ? 36.776  189.483 56.480 1.00 32.19 ?  119 VAL J CB  1 
ATOM   10767 C  CG1 . VAL J  1 120 ? 37.032  190.632 57.452 1.00 34.94 ?  119 VAL J CG1 1 
ATOM   10768 C  CG2 . VAL J  1 120 ? 36.948  188.163 57.194 1.00 38.03 ?  119 VAL J CG2 1 
ATOM   10769 N  N   . HIS J  1 121 ? 33.619  188.211 56.812 1.00 33.04 ?  120 HIS J N   1 
ATOM   10770 C  CA  . HIS J  1 121 ? 32.373  187.985 57.532 1.00 32.76 ?  120 HIS J CA  1 
ATOM   10771 C  C   . HIS J  1 121 ? 32.584  187.195 58.819 1.00 39.32 ?  120 HIS J C   1 
ATOM   10772 O  O   . HIS J  1 121 ? 33.660  186.648 59.087 1.00 37.65 ?  120 HIS J O   1 
ATOM   10773 C  CB  . HIS J  1 121 ? 31.376  187.245 56.641 1.00 32.79 ?  120 HIS J CB  1 
ATOM   10774 C  CG  . HIS J  1 121 ? 30.695  188.129 55.649 1.00 33.75 ?  120 HIS J CG  1 
ATOM   10775 N  ND1 . HIS J  1 121 ? 29.426  188.628 55.848 1.00 42.89 ?  120 HIS J ND1 1 
ATOM   10776 C  CD2 . HIS J  1 121 ? 31.102  188.598 54.447 1.00 34.94 ?  120 HIS J CD2 1 
ATOM   10777 C  CE1 . HIS J  1 121 ? 29.085  189.381 54.815 1.00 39.62 ?  120 HIS J CE1 1 
ATOM   10778 N  NE2 . HIS J  1 121 ? 30.081  189.372 53.947 1.00 37.55 ?  120 HIS J NE2 1 
ATOM   10779 N  N   . GLU J  1 122 ? 31.493  187.089 59.586 1.00 38.25 ?  121 GLU J N   1 
ATOM   10780 C  CA  . GLU J  1 122 ? 31.530  186.540 60.936 1.00 35.53 ?  121 GLU J CA  1 
ATOM   10781 C  C   . GLU J  1 122 ? 31.652  185.021 60.943 1.00 41.53 ?  121 GLU J C   1 
ATOM   10782 O  O   . GLU J  1 122 ? 32.356  184.467 61.793 1.00 36.08 ?  121 GLU J O   1 
ATOM   10783 C  CB  . GLU J  1 122 ? 30.274  186.973 61.697 1.00 35.89 ?  121 GLU J CB  1 
ATOM   10784 C  CG  . GLU J  1 122 ? 29.974  186.176 62.957 1.00 44.66 ?  121 GLU J CG  1 
ATOM   10785 C  CD  . GLU J  1 122 ? 28.533  186.358 63.444 1.00 51.00 ?  121 GLU J CD  1 
ATOM   10786 O  OE1 . GLU J  1 122 ? 27.629  186.613 62.611 1.00 48.11 ?  121 GLU J OE1 1 
ATOM   10787 O  OE2 . GLU J  1 122 ? 28.303  186.241 64.666 1.00 60.78 ?  121 GLU J OE2 1 
ATOM   10788 N  N   . LYS J  1 123 ? 30.967  184.338 60.018 1.00 40.57 ?  122 LYS J N   1 
ATOM   10789 C  CA  . LYS J  1 123 ? 30.873  182.882 59.951 1.00 40.83 ?  122 LYS J CA  1 
ATOM   10790 C  C   . LYS J  1 123 ? 31.405  182.362 58.614 1.00 39.62 ?  122 LYS J C   1 
ATOM   10791 O  O   . LYS J  1 123 ? 31.728  183.123 57.695 1.00 37.64 ?  122 LYS J O   1 
ATOM   10792 C  CB  . LYS J  1 123 ? 29.426  182.415 60.120 1.00 36.82 ?  122 LYS J CB  1 
ATOM   10793 C  CG  . LYS J  1 123 ? 28.751  182.855 61.386 1.00 47.56 ?  122 LYS J CG  1 
ATOM   10794 C  CD  . LYS J  1 123 ? 27.379  182.218 61.461 1.00 51.94 ?  122 LYS J CD  1 
ATOM   10795 C  CE  . LYS J  1 123 ? 26.303  183.165 60.982 1.00 47.90 ?  122 LYS J CE  1 
ATOM   10796 N  NZ  . LYS J  1 123 ? 25.534  183.653 62.158 1.00 61.89 ?  122 LYS J NZ  1 
ATOM   10797 N  N   . ALA J  1 124 ? 31.461  181.038 58.499 1.00 37.12 ?  123 ALA J N   1 
ATOM   10798 C  CA  . ALA J  1 124 ? 31.802  180.421 57.226 1.00 35.32 ?  123 ALA J CA  1 
ATOM   10799 C  C   . ALA J  1 124 ? 30.737  180.727 56.180 1.00 34.82 ?  123 ALA J C   1 
ATOM   10800 O  O   . ALA J  1 124 ? 29.535  180.673 56.447 1.00 32.15 ?  123 ALA J O   1 
ATOM   10801 C  CB  . ALA J  1 124 ? 31.943  178.903 57.386 1.00 28.80 ?  123 ALA J CB  1 
ATOM   10802 N  N   . ASP J  1 125 ? 31.192  181.075 54.985 1.00 31.82 ?  124 ASP J N   1 
ATOM   10803 C  CA  . ASP J  1 125 ? 30.347  181.016 53.802 1.00 31.31 ?  124 ASP J CA  1 
ATOM   10804 C  C   . ASP J  1 125 ? 30.069  179.553 53.481 1.00 35.24 ?  124 ASP J C   1 
ATOM   10805 O  O   . ASP J  1 125 ? 31.006  178.764 53.330 1.00 33.37 ?  124 ASP J O   1 
ATOM   10806 C  CB  . ASP J  1 125 ? 31.069  181.721 52.647 1.00 31.50 ?  124 ASP J CB  1 
ATOM   10807 C  CG  . ASP J  1 125 ? 30.244  181.822 51.383 1.00 34.52 ?  124 ASP J CG  1 
ATOM   10808 O  OD1 . ASP J  1 125 ? 29.265  181.059 51.200 1.00 33.95 ?  124 ASP J OD1 1 
ATOM   10809 O  OD2 . ASP J  1 125 ? 30.605  182.675 50.544 1.00 33.11 ?  124 ASP J OD2 1 
ATOM   10810 N  N   . ASP J  1 126 ? 28.788  179.177 53.373 1.00 30.87 ?  125 ASP J N   1 
ATOM   10811 C  CA  . ASP J  1 126 ? 28.459  177.801 52.999 1.00 33.46 ?  125 ASP J CA  1 
ATOM   10812 C  C   . ASP J  1 126 ? 28.460  177.581 51.484 1.00 36.04 ?  125 ASP J C   1 
ATOM   10813 O  O   . ASP J  1 126 ? 28.000  176.526 51.020 1.00 34.44 ?  125 ASP J O   1 
ATOM   10814 C  CB  . ASP J  1 126 ? 27.114  177.371 53.621 1.00 31.46 ?  125 ASP J CB  1 
ATOM   10815 C  CG  . ASP J  1 126 ? 25.884  178.054 52.992 1.00 37.98 ?  125 ASP J CG  1 
ATOM   10816 O  OD1 . ASP J  1 126 ? 25.962  178.614 51.882 1.00 33.54 ?  125 ASP J OD1 1 
ATOM   10817 O  OD2 . ASP J  1 126 ? 24.802  178.013 53.635 1.00 35.02 ?  125 ASP J OD2 1 
ATOM   10818 N  N   . LEU J  1 127 ? 28.956  178.561 50.718 1.00 35.78 ?  126 LEU J N   1 
ATOM   10819 C  CA  . LEU J  1 127 ? 29.122  178.451 49.257 1.00 38.38 ?  126 LEU J CA  1 
ATOM   10820 C  C   . LEU J  1 127 ? 27.835  178.028 48.552 1.00 37.49 ?  126 LEU J C   1 
ATOM   10821 O  O   . LEU J  1 127 ? 27.873  177.377 47.507 1.00 39.74 ?  126 LEU J O   1 
ATOM   10822 C  CB  . LEU J  1 127 ? 30.257  177.488 48.897 1.00 33.29 ?  126 LEU J CB  1 
ATOM   10823 C  CG  . LEU J  1 127 ? 31.438  177.506 49.877 1.00 34.60 ?  126 LEU J CG  1 
ATOM   10824 C  CD1 . LEU J  1 127 ? 32.465  176.452 49.512 1.00 38.60 ?  126 LEU J CD1 1 
ATOM   10825 C  CD2 . LEU J  1 127 ? 32.084  178.878 49.931 1.00 36.85 ?  126 LEU J CD2 1 
ATOM   10826 N  N   . GLY J  1 128 ? 26.683  178.410 49.100 1.00 34.62 ?  127 GLY J N   1 
ATOM   10827 C  CA  . GLY J  1 128 ? 25.426  178.149 48.428 1.00 33.87 ?  127 GLY J CA  1 
ATOM   10828 C  C   . GLY J  1 128 ? 24.858  176.767 48.656 1.00 33.42 ?  127 GLY J C   1 
ATOM   10829 O  O   . GLY J  1 128 ? 23.850  176.422 48.035 1.00 33.14 ?  127 GLY J O   1 
ATOM   10830 N  N   . LYS J  1 129 ? 25.440  175.982 49.564 1.00 34.16 ?  128 LYS J N   1 
ATOM   10831 C  CA  . LYS J  1 129 ? 25.016  174.603 49.797 1.00 39.82 ?  128 LYS J CA  1 
ATOM   10832 C  C   . LYS J  1 129 ? 24.183  174.431 51.066 1.00 39.52 ?  128 LYS J C   1 
ATOM   10833 O  O   . LYS J  1 129 ? 23.978  173.295 51.507 1.00 34.04 ?  128 LYS J O   1 
ATOM   10834 C  CB  . LYS J  1 129 ? 26.245  173.692 49.850 1.00 39.54 ?  128 LYS J CB  1 
ATOM   10835 C  CG  . LYS J  1 129 ? 27.000  173.631 48.523 1.00 40.34 ?  128 LYS J CG  1 
ATOM   10836 C  CD  . LYS J  1 129 ? 28.427  173.131 48.725 1.00 50.99 ?  128 LYS J CD  1 
ATOM   10837 C  CE  . LYS J  1 129 ? 28.505  171.604 48.600 1.00 47.81 ?  128 LYS J CE  1 
ATOM   10838 N  NZ  . LYS J  1 129 ? 29.001  171.191 47.251 1.00 64.24 ?  128 LYS J NZ  1 
ATOM   10839 N  N   . GLY J  1 130 ? 23.694  175.523 51.657 1.00 34.07 ?  129 GLY J N   1 
ATOM   10840 C  CA  . GLY J  1 130 ? 23.021  175.478 52.942 1.00 32.98 ?  129 GLY J CA  1 
ATOM   10841 C  C   . GLY J  1 130 ? 21.581  175.015 52.916 1.00 32.82 ?  129 GLY J C   1 
ATOM   10842 O  O   . GLY J  1 130 ? 21.044  174.663 53.971 1.00 33.21 ?  129 GLY J O   1 
ATOM   10843 N  N   . GLY J  1 131 ? 20.937  175.016 51.753 1.00 30.63 ?  130 GLY J N   1 
ATOM   10844 C  CA  . GLY J  1 131 ? 19.593  174.484 51.636 1.00 30.18 ?  130 GLY J CA  1 
ATOM   10845 C  C   . GLY J  1 131 ? 18.482  175.416 52.076 1.00 28.33 ?  130 GLY J C   1 
ATOM   10846 O  O   . GLY J  1 131 ? 17.307  175.049 51.946 1.00 31.81 ?  130 GLY J O   1 
ATOM   10847 N  N   . ASN J  1 132 ? 18.809  176.592 52.603 1.00 32.94 ?  131 ASN J N   1 
ATOM   10848 C  CA  . ASN J  1 132 ? 17.820  177.596 52.985 1.00 42.80 ?  131 ASN J CA  1 
ATOM   10849 C  C   . ASN J  1 132 ? 17.916  178.775 52.027 1.00 38.00 ?  131 ASN J C   1 
ATOM   10850 O  O   . ASN J  1 132 ? 18.863  178.880 51.241 1.00 40.30 ?  131 ASN J O   1 
ATOM   10851 C  CB  . ASN J  1 132 ? 17.993  178.046 54.452 1.00 32.72 ?  131 ASN J CB  1 
ATOM   10852 C  CG  . ASN J  1 132 ? 19.271  178.886 54.698 1.00 39.86 ?  131 ASN J CG  1 
ATOM   10853 O  OD1 . ASN J  1 132 ? 20.194  178.925 53.875 1.00 33.97 ?  131 ASN J OD1 1 
ATOM   10854 N  ND2 . ASN J  1 132 ? 19.320  179.550 55.864 1.00 35.36 ?  131 ASN J ND2 1 
ATOM   10855 N  N   . GLU J  1 133 ? 16.914  179.658 52.085 1.00 40.67 ?  132 GLU J N   1 
ATOM   10856 C  CA  . GLU J  1 133 ? 16.874  180.781 51.148 1.00 40.29 ?  132 GLU J CA  1 
ATOM   10857 C  C   . GLU J  1 133 ? 18.130  181.633 51.271 1.00 40.15 ?  132 GLU J C   1 
ATOM   10858 O  O   . GLU J  1 133 ? 18.700  182.073 50.264 1.00 44.49 ?  132 GLU J O   1 
ATOM   10859 C  CB  . GLU J  1 133 ? 15.626  181.637 51.385 1.00 44.26 ?  132 GLU J CB  1 
ATOM   10860 C  CG  . GLU J  1 133 ? 14.420  180.895 52.014 1.00 49.55 ?  132 GLU J CG  1 
ATOM   10861 C  CD  . GLU J  1 133 ? 13.137  181.751 52.026 1.00 56.12 ?  132 GLU J CD  1 
ATOM   10862 O  OE1 . GLU J  1 133 ? 13.248  182.990 52.031 1.00 62.34 ?  132 GLU J OE1 1 
ATOM   10863 O  OE2 . GLU J  1 133 ? 12.016  181.195 52.018 1.00 61.62 ?  132 GLU J OE2 1 
ATOM   10864 N  N   . GLU J  1 134 ? 18.592  181.844 52.503 1.00 40.16 ?  133 GLU J N   1 
ATOM   10865 C  CA  . GLU J  1 134 ? 19.743  182.701 52.752 1.00 41.55 ?  133 GLU J CA  1 
ATOM   10866 C  C   . GLU J  1 134 ? 21.015  182.169 52.092 1.00 39.14 ?  133 GLU J C   1 
ATOM   10867 O  O   . GLU J  1 134 ? 21.883  182.958 51.696 1.00 38.97 ?  133 GLU J O   1 
ATOM   10868 C  CB  . GLU J  1 134 ? 19.935  182.844 54.264 1.00 35.29 ?  133 GLU J CB  1 
ATOM   10869 C  CG  . GLU J  1 134 ? 20.939  183.900 54.644 1.00 43.21 ?  133 GLU J CG  1 
ATOM   10870 C  CD  . GLU J  1 134 ? 20.456  185.298 54.277 1.00 51.59 ?  133 GLU J CD  1 
ATOM   10871 O  OE1 . GLU J  1 134 ? 19.266  185.604 54.507 1.00 56.14 ?  133 GLU J OE1 1 
ATOM   10872 O  OE2 . GLU J  1 134 ? 21.257  186.078 53.725 1.00 46.60 ?  133 GLU J OE2 1 
ATOM   10873 N  N   . SER J  1 135 ? 21.141  180.842 51.957 1.00 38.79 ?  134 SER J N   1 
ATOM   10874 C  CA  . SER J  1 135 ? 22.360  180.269 51.382 1.00 38.20 ?  134 SER J CA  1 
ATOM   10875 C  C   . SER J  1 135 ? 22.654  180.833 49.996 1.00 35.27 ?  134 SER J C   1 
ATOM   10876 O  O   . SER J  1 135 ? 23.811  181.137 49.679 1.00 38.63 ?  134 SER J O   1 
ATOM   10877 C  CB  . SER J  1 135 ? 22.261  178.746 51.308 1.00 34.71 ?  134 SER J CB  1 
ATOM   10878 O  OG  . SER J  1 135 ? 23.525  178.212 50.957 1.00 35.80 ?  134 SER J OG  1 
ATOM   10879 N  N   . THR J  1 136 ? 21.624  180.996 49.159 1.00 35.36 ?  135 THR J N   1 
ATOM   10880 C  CA  . THR J  1 136 ? 21.842  181.457 47.792 1.00 39.96 ?  135 THR J CA  1 
ATOM   10881 C  C   . THR J  1 136 ? 21.881  182.976 47.664 1.00 43.00 ?  135 THR J C   1 
ATOM   10882 O  O   . THR J  1 136 ? 21.955  183.478 46.532 1.00 39.68 ?  135 THR J O   1 
ATOM   10883 C  CB  . THR J  1 136 ? 20.770  180.893 46.857 1.00 42.62 ?  135 THR J CB  1 
ATOM   10884 O  OG1 . THR J  1 136 ? 19.481  181.052 47.455 1.00 50.54 ?  135 THR J OG1 1 
ATOM   10885 C  CG2 . THR J  1 136 ? 21.025  179.410 46.634 1.00 45.92 ?  135 THR J CG2 1 
ATOM   10886 N  N   . LYS J  1 137 ? 21.836  183.711 48.778 1.00 39.23 ?  136 LYS J N   1 
ATOM   10887 C  CA  . LYS J  1 137 ? 22.076  185.152 48.783 1.00 38.80 ?  136 LYS J CA  1 
ATOM   10888 C  C   . LYS J  1 137 ? 23.388  185.525 49.458 1.00 38.65 ?  136 LYS J C   1 
ATOM   10889 O  O   . LYS J  1 137 ? 24.203  186.246 48.873 1.00 39.05 ?  136 LYS J O   1 
ATOM   10890 C  CB  . LYS J  1 137 ? 20.911  185.879 49.472 1.00 43.14 ?  136 LYS J CB  1 
ATOM   10891 C  CG  . LYS J  1 137 ? 19.553  185.260 49.186 1.00 45.21 ?  136 LYS J CG  1 
ATOM   10892 C  CD  . LYS J  1 137 ? 18.448  186.293 49.292 1.00 50.85 ?  136 LYS J CD  1 
ATOM   10893 C  CE  . LYS J  1 137 ? 17.753  186.224 50.644 1.00 59.80 ?  136 LYS J CE  1 
ATOM   10894 N  NZ  . LYS J  1 137 ? 16.391  186.833 50.600 1.00 70.13 ?  136 LYS J NZ  1 
ATOM   10895 N  N   . THR J  1 138 ? 23.628  185.034 50.677 1.00 37.62 ?  137 THR J N   1 
ATOM   10896 C  CA  . THR J  1 138 ? 24.815  185.403 51.429 1.00 36.30 ?  137 THR J CA  1 
ATOM   10897 C  C   . THR J  1 138 ? 25.691  184.228 51.841 1.00 39.10 ?  137 THR J C   1 
ATOM   10898 O  O   . THR J  1 138 ? 26.715  184.452 52.500 1.00 33.77 ?  137 THR J O   1 
ATOM   10899 C  CB  . THR J  1 138 ? 24.425  186.143 52.706 1.00 45.69 ?  137 THR J CB  1 
ATOM   10900 O  OG1 . THR J  1 138 ? 23.587  185.290 53.509 1.00 38.58 ?  137 THR J OG1 1 
ATOM   10901 C  CG2 . THR J  1 138 ? 23.698  187.437 52.367 1.00 42.04 ?  137 THR J CG2 1 
ATOM   10902 N  N   . GLY J  1 139 ? 25.300  182.991 51.532 1.00 35.43 ?  138 GLY J N   1 
ATOM   10903 C  CA  . GLY J  1 139 ? 26.007  181.845 52.074 1.00 35.23 ?  138 GLY J CA  1 
ATOM   10904 C  C   . GLY J  1 139 ? 25.950  181.720 53.584 1.00 36.12 ?  138 GLY J C   1 
ATOM   10905 O  O   . GLY J  1 139 ? 26.758  180.993 54.163 1.00 33.85 ?  138 GLY J O   1 
ATOM   10906 N  N   . ASN J  1 140 ? 25.020  182.417 54.241 1.00 36.36 ?  139 ASN J N   1 
ATOM   10907 C  CA  . ASN J  1 140 ? 24.841  182.337 55.696 1.00 34.96 ?  139 ASN J CA  1 
ATOM   10908 C  C   . ASN J  1 140 ? 26.110  182.720 56.442 1.00 34.11 ?  139 ASN J C   1 
ATOM   10909 O  O   . ASN J  1 140 ? 26.352  182.224 57.544 1.00 34.09 ?  139 ASN J O   1 
ATOM   10910 C  CB  . ASN J  1 140 ? 24.389  180.937 56.136 1.00 33.81 ?  139 ASN J CB  1 
ATOM   10911 C  CG  . ASN J  1 140 ? 22.954  180.640 55.754 1.00 36.21 ?  139 ASN J CG  1 
ATOM   10912 O  OD1 . ASN J  1 140 ? 22.016  181.223 56.307 1.00 40.25 ?  139 ASN J OD1 1 
ATOM   10913 N  ND2 . ASN J  1 140 ? 22.771  179.717 54.817 1.00 34.33 ?  139 ASN J ND2 1 
ATOM   10914 N  N   . ALA J  1 141 ? 26.937  183.592 55.846 1.00 29.71 ?  140 ALA J N   1 
ATOM   10915 C  CA  . ALA J  1 141 ? 28.201  183.991 56.463 1.00 33.32 ?  140 ALA J CA  1 
ATOM   10916 C  C   . ALA J  1 141 ? 28.027  184.998 57.599 1.00 34.72 ?  140 ALA J C   1 
ATOM   10917 O  O   . ALA J  1 141 ? 29.006  185.325 58.276 1.00 35.78 ?  140 ALA J O   1 
ATOM   10918 C  CB  . ALA J  1 141 ? 29.160  184.557 55.405 1.00 34.23 ?  140 ALA J CB  1 
ATOM   10919 N  N   . GLY J  1 142 ? 26.821  185.485 57.844 1.00 37.76 ?  141 GLY J N   1 
ATOM   10920 C  CA  . GLY J  1 142 ? 26.612  186.309 59.016 1.00 37.92 ?  141 GLY J CA  1 
ATOM   10921 C  C   . GLY J  1 142 ? 27.155  187.718 58.844 1.00 40.07 ?  141 GLY J C   1 
ATOM   10922 O  O   . GLY J  1 142 ? 27.298  188.228 57.730 1.00 38.77 ?  141 GLY J O   1 
ATOM   10923 N  N   . SER J  1 143 ? 27.494  188.338 59.974 1.00 38.08 ?  142 SER J N   1 
ATOM   10924 C  CA  . SER J  1 143 ? 27.688  189.779 60.000 1.00 40.27 ?  142 SER J CA  1 
ATOM   10925 C  C   . SER J  1 143 ? 29.048  190.157 59.424 1.00 40.73 ?  142 SER J C   1 
ATOM   10926 O  O   . SER J  1 143 ? 29.898  189.311 59.133 1.00 37.16 ?  142 SER J O   1 
ATOM   10927 C  CB  . SER J  1 143 ? 27.552  190.316 61.422 1.00 39.98 ?  142 SER J CB  1 
ATOM   10928 O  OG  . SER J  1 143 ? 28.349  189.576 62.321 1.00 48.32 ?  142 SER J OG  1 
ATOM   10929 N  N   . ARG J  1 144 ? 29.248  191.457 59.274 1.00 38.58 ?  143 ARG J N   1 
ATOM   10930 C  CA  . ARG J  1 144 ? 30.426  192.003 58.621 1.00 35.52 ?  143 ARG J CA  1 
ATOM   10931 C  C   . ARG J  1 144 ? 31.382  192.465 59.707 1.00 40.96 ?  143 ARG J C   1 
ATOM   10932 O  O   . ARG J  1 144 ? 31.086  193.417 60.434 1.00 42.79 ?  143 ARG J O   1 
ATOM   10933 C  CB  . ARG J  1 144 ? 30.016  193.141 57.689 1.00 36.31 ?  143 ARG J CB  1 
ATOM   10934 C  CG  . ARG J  1 144 ? 28.728  192.804 56.960 1.00 37.15 ?  143 ARG J CG  1 
ATOM   10935 C  CD  . ARG J  1 144 ? 28.304  193.859 55.951 1.00 35.00 ?  143 ARG J CD  1 
ATOM   10936 N  NE  . ARG J  1 144 ? 27.198  193.348 55.149 1.00 32.55 ?  143 ARG J NE  1 
ATOM   10937 C  CZ  . ARG J  1 144 ? 26.788  193.892 54.013 1.00 40.98 ?  143 ARG J CZ  1 
ATOM   10938 N  NH1 . ARG J  1 144 ? 27.336  195.001 53.545 1.00 34.10 ?  143 ARG J NH1 1 
ATOM   10939 N  NH2 . ARG J  1 144 ? 25.809  193.308 53.327 1.00 35.95 ?  143 ARG J NH2 1 
ATOM   10940 N  N   . LEU J  1 145 ? 32.523  191.784 59.824 1.00 39.22 ?  144 LEU J N   1 
ATOM   10941 C  CA  . LEU J  1 145 ? 33.483  192.064 60.886 1.00 36.64 ?  144 LEU J CA  1 
ATOM   10942 C  C   . LEU J  1 145 ? 34.423  193.201 60.539 1.00 37.64 ?  144 LEU J C   1 
ATOM   10943 O  O   . LEU J  1 145 ? 34.802  193.976 61.423 1.00 37.14 ?  144 LEU J O   1 
ATOM   10944 C  CB  . LEU J  1 145 ? 34.314  190.817 61.204 1.00 38.51 ?  144 LEU J CB  1 
ATOM   10945 C  CG  . LEU J  1 145 ? 33.520  189.577 61.602 1.00 42.75 ?  144 LEU J CG  1 
ATOM   10946 C  CD1 . LEU J  1 145 ? 34.463  188.488 62.093 1.00 39.64 ?  144 LEU J CD1 1 
ATOM   10947 C  CD2 . LEU J  1 145 ? 32.471  189.915 62.672 1.00 34.38 ?  144 LEU J CD2 1 
ATOM   10948 N  N   . ALA J  1 146 ? 34.849  193.289 59.283 1.00 33.00 ?  145 ALA J N   1 
ATOM   10949 C  CA  . ALA J  1 146 ? 35.721  194.372 58.857 1.00 37.32 ?  145 ALA J CA  1 
ATOM   10950 C  C   . ALA J  1 146 ? 35.581  194.529 57.354 1.00 35.34 ?  145 ALA J C   1 
ATOM   10951 O  O   . ALA J  1 146 ? 35.178  193.599 56.650 1.00 37.64 ?  145 ALA J O   1 
ATOM   10952 C  CB  . ALA J  1 146 ? 37.182  194.120 59.243 1.00 33.98 ?  145 ALA J CB  1 
ATOM   10953 N  N   . CYS J  1 147 ? 35.913  195.718 56.870 1.00 33.51 ?  146 CYS J N   1 
ATOM   10954 C  CA  . CYS J  1 147 ? 35.788  196.008 55.450 1.00 35.21 ?  146 CYS J CA  1 
ATOM   10955 C  C   . CYS J  1 147 ? 36.696  197.174 55.107 1.00 32.45 ?  146 CYS J C   1 
ATOM   10956 O  O   . CYS J  1 147 ? 37.240  197.846 55.985 1.00 40.02 ?  146 CYS J O   1 
ATOM   10957 C  CB  . CYS J  1 147 ? 34.344  196.333 55.050 1.00 42.95 ?  146 CYS J CB  1 
ATOM   10958 S  SG  . CYS J  1 147 ? 33.583  197.675 56.010 1.00 42.04 ?  146 CYS J SG  1 
ATOM   10959 N  N   . GLY J  1 148 ? 36.852  197.395 53.810 1.00 36.88 ?  147 GLY J N   1 
ATOM   10960 C  CA  . GLY J  1 148 ? 37.582  198.540 53.304 1.00 36.46 ?  147 GLY J CA  1 
ATOM   10961 C  C   . GLY J  1 148 ? 37.236  198.715 51.850 1.00 37.18 ?  147 GLY J C   1 
ATOM   10962 O  O   . GLY J  1 148 ? 36.786  197.772 51.184 1.00 33.10 ?  147 GLY J O   1 
ATOM   10963 N  N   . VAL J  1 149 ? 37.431  199.947 51.356 1.00 35.09 ?  148 VAL J N   1 
ATOM   10964 C  CA  . VAL J  1 149 ? 37.226  200.235 49.942 1.00 38.07 ?  148 VAL J CA  1 
ATOM   10965 C  C   . VAL J  1 149 ? 38.441  199.745 49.162 1.00 36.67 ?  148 VAL J C   1 
ATOM   10966 O  O   . VAL J  1 149 ? 39.586  199.918 49.597 1.00 39.29 ?  148 VAL J O   1 
ATOM   10967 C  CB  . VAL J  1 149 ? 36.983  201.744 49.732 1.00 38.69 ?  148 VAL J CB  1 
ATOM   10968 C  CG1 . VAL J  1 149 ? 36.623  202.019 48.293 1.00 36.23 ?  148 VAL J CG1 1 
ATOM   10969 C  CG2 . VAL J  1 149 ? 35.880  202.239 50.660 1.00 37.12 ?  148 VAL J CG2 1 
ATOM   10970 N  N   . ILE J  1 150 ? 38.207  199.131 48.005 1.00 39.47 ?  149 ILE J N   1 
ATOM   10971 C  CA  . ILE J  1 150 ? 39.301  198.601 47.198 1.00 35.79 ?  149 ILE J CA  1 
ATOM   10972 C  C   . ILE J  1 150 ? 39.884  199.746 46.378 1.00 43.87 ?  149 ILE J C   1 
ATOM   10973 O  O   . ILE J  1 150 ? 39.232  200.266 45.466 1.00 41.47 ?  149 ILE J O   1 
ATOM   10974 C  CB  . ILE J  1 150 ? 38.838  197.455 46.299 1.00 38.80 ?  149 ILE J CB  1 
ATOM   10975 C  CG1 . ILE J  1 150 ? 38.372  196.279 47.154 1.00 37.60 ?  149 ILE J CG1 1 
ATOM   10976 C  CG2 . ILE J  1 150 ? 39.962  197.030 45.392 1.00 41.72 ?  149 ILE J CG2 1 
ATOM   10977 C  CD1 . ILE J  1 150 ? 37.379  195.373 46.448 1.00 33.32 ?  149 ILE J CD1 1 
ATOM   10978 N  N   . GLY J  1 151 ? 41.114  200.146 46.704 1.00 40.94 ?  150 GLY J N   1 
ATOM   10979 C  CA  . GLY J  1 151 ? 41.742  201.268 46.032 1.00 43.51 ?  150 GLY J CA  1 
ATOM   10980 C  C   . GLY J  1 151 ? 42.850  200.892 45.063 1.00 51.85 ?  150 GLY J C   1 
ATOM   10981 O  O   . GLY J  1 151 ? 43.433  199.811 45.156 1.00 43.62 ?  150 GLY J O   1 
ATOM   10982 N  N   . ILE J  1 152 ? 43.140  201.799 44.127 1.00 45.62 ?  151 ILE J N   1 
ATOM   10983 C  CA  . ILE J  1 152 ? 44.202  201.574 43.153 1.00 47.67 ?  151 ILE J CA  1 
ATOM   10984 C  C   . ILE J  1 152 ? 45.552  201.714 43.841 1.00 48.78 ?  151 ILE J C   1 
ATOM   10985 O  O   . ILE J  1 152 ? 45.790  202.675 44.590 1.00 46.27 ?  151 ILE J O   1 
ATOM   10986 C  CB  . ILE J  1 152 ? 44.070  202.558 41.985 1.00 46.28 ?  151 ILE J CB  1 
ATOM   10987 C  CG1 . ILE J  1 152 ? 42.843  202.210 41.148 1.00 47.70 ?  151 ILE J CG1 1 
ATOM   10988 C  CG2 . ILE J  1 152 ? 45.333  202.529 41.117 1.00 53.67 ?  151 ILE J CG2 1 
ATOM   10989 C  CD1 . ILE J  1 152 ? 42.461  203.285 40.133 1.00 49.39 ?  151 ILE J CD1 1 
ATOM   10990 N  N   . ALA J  1 153 ? 46.443  200.756 43.599 1.00 48.51 ?  152 ALA J N   1 
ATOM   10991 C  CA  . ALA J  1 153 ? 47.736  200.731 44.268 1.00 50.90 ?  152 ALA J CA  1 
ATOM   10992 C  C   . ALA J  1 153 ? 48.863  200.899 43.256 1.00 56.31 ?  152 ALA J C   1 
ATOM   10993 O  O   . ALA J  1 153 ? 48.683  200.694 42.046 1.00 50.68 ?  152 ALA J O   1 
ATOM   10994 C  CB  . ALA J  1 153 ? 47.932  199.434 45.064 1.00 51.71 ?  152 ALA J CB  1 
ATOM   10995 N  N   . GLN J  1 154 ? 50.028  201.286 43.770 1.00 50.69 ?  153 GLN J N   1 
ATOM   10996 C  CA  . GLN J  1 154 ? 51.168  201.585 42.907 1.00 57.74 ?  153 GLN J CA  1 
ATOM   10997 C  C   . GLN J  1 154 ? 51.710  200.328 42.241 1.00 67.88 ?  153 GLN J C   1 
ATOM   10998 O  O   . GLN J  1 154 ? 52.117  199.397 42.945 1.00 66.22 ?  153 GLN J O   1 
ATOM   10999 C  CB  . GLN J  1 154 ? 52.286  202.258 43.691 1.00 54.35 ?  153 GLN J CB  1 
ATOM   11000 C  CG  . GLN J  1 154 ? 53.452  202.648 42.807 1.00 57.81 ?  153 GLN J CG  1 
ATOM   11001 C  CD  . GLN J  1 154 ? 54.253  203.777 43.388 1.00 62.10 ?  153 GLN J CD  1 
ATOM   11002 O  OE1 . GLN J  1 154 ? 54.632  203.741 44.565 1.00 64.25 ?  153 GLN J OE1 1 
ATOM   11003 N  NE2 . GLN J  1 154 ? 54.523  204.797 42.571 1.00 57.34 ?  153 GLN J NE2 1 
ATOM   11004 O  OXT . GLN J  1 154 ? 51.757  200.232 41.007 1.00 64.97 ?  153 GLN J OXT 1 
HETATM 11005 ZN ZN  . ZN  K  5 .   ? 34.422  268.629 23.187 1.00 41.81 ?  201 ZN  A ZN  1 
HETATM 11006 C  C1  . GOL L  6 .   ? 28.602  270.106 13.424 1.00 52.50 ?  202 GOL A C1  1 
HETATM 11007 O  O1  . GOL L  6 .   ? 28.947  270.633 12.164 1.00 69.46 ?  202 GOL A O1  1 
HETATM 11008 C  C2  . GOL L  6 .   ? 29.900  270.156 14.295 1.00 55.77 ?  202 GOL A C2  1 
HETATM 11009 O  O2  . GOL L  6 .   ? 30.602  271.353 14.139 1.00 63.65 ?  202 GOL A O2  1 
HETATM 11010 C  C3  . GOL L  6 .   ? 29.424  269.991 15.733 1.00 50.31 ?  202 GOL A C3  1 
HETATM 11011 O  O3  . GOL L  6 .   ? 30.424  269.269 16.408 1.00 51.20 ?  202 GOL A O3  1 
HETATM 11012 ZN ZN  . ZN  M  5 .   ? 15.240  234.522 20.587 1.00 34.03 ?  201 ZN  B ZN  1 
HETATM 11013 C  C1  . GOL N  6 .   ? 19.725  235.070 12.138 1.00 48.40 ?  202 GOL B C1  1 
HETATM 11014 O  O1  . GOL N  6 .   ? 20.317  234.111 12.945 1.00 56.57 ?  202 GOL B O1  1 
HETATM 11015 C  C2  . GOL N  6 .   ? 20.010  234.698 10.678 1.00 53.69 ?  202 GOL B C2  1 
HETATM 11016 O  O2  . GOL N  6 .   ? 21.248  235.171 10.215 1.00 55.31 ?  202 GOL B O2  1 
HETATM 11017 C  C3  . GOL N  6 .   ? 19.874  233.167 10.638 1.00 53.03 ?  202 GOL B C3  1 
HETATM 11018 O  O3  . GOL N  6 .   ? 19.804  232.832 9.278  1.00 61.62 ?  202 GOL B O3  1 
HETATM 11019 ZN ZN  . ZN  O  5 .   ? 15.422  182.346 23.025 1.00 46.70 ?  201 ZN  C ZN  1 
HETATM 11020 C  C1  . GOL P  6 .   ? 20.022  186.115 13.281 1.00 50.37 ?  202 GOL C C1  1 
HETATM 11021 O  O1  . GOL P  6 .   ? 20.129  187.504 13.121 1.00 59.88 ?  202 GOL C O1  1 
HETATM 11022 C  C2  . GOL P  6 .   ? 20.068  185.811 14.817 1.00 55.51 ?  202 GOL C C2  1 
HETATM 11023 O  O2  . GOL P  6 .   ? 21.002  186.600 15.506 1.00 61.96 ?  202 GOL C O2  1 
HETATM 11024 C  C3  . GOL P  6 .   ? 18.621  186.040 15.315 1.00 47.96 ?  202 GOL C C3  1 
HETATM 11025 O  O3  . GOL P  6 .   ? 18.527  185.529 16.623 1.00 49.82 ?  202 GOL C O3  1 
HETATM 11026 ZN ZN  . ZN  Q  5 .   ? -4.547  216.116 20.649 1.00 30.44 ?  201 ZN  D ZN  1 
HETATM 11027 C  C1  . GOL R  6 .   ? -6.089  212.732 12.755 1.00 39.08 ?  202 GOL D C1  1 
HETATM 11028 O  O1  . GOL R  6 .   ? -6.123  212.468 14.129 1.00 44.82 ?  202 GOL D O1  1 
HETATM 11029 C  C2  . GOL R  6 .   ? -7.098  211.860 11.993 1.00 46.61 ?  202 GOL D C2  1 
HETATM 11030 O  O2  . GOL R  6 .   ? -8.369  211.849 12.572 1.00 57.17 ?  202 GOL D O2  1 
HETATM 11031 C  C3  . GOL R  6 .   ? -7.088  212.394 10.537 1.00 41.53 ?  202 GOL D C3  1 
HETATM 11032 O  O3  . GOL R  6 .   ? -6.855  211.262 9.749  1.00 49.52 ?  202 GOL D O3  1 
HETATM 11033 ZN ZN  . ZN  S  5 .   ? 49.586  241.832 48.852 1.00 56.54 ?  201 ZN  E ZN  1 
HETATM 11034 C  C1  . GOL T  6 .   ? 49.133  238.075 55.806 1.00 60.10 ?  202 GOL E C1  1 
HETATM 11035 O  O1  . GOL T  6 .   ? 49.022  239.061 54.783 1.00 62.77 ?  202 GOL E O1  1 
HETATM 11036 C  C2  . GOL T  6 .   ? 48.202  236.914 55.411 1.00 55.23 ?  202 GOL E C2  1 
HETATM 11037 O  O2  . GOL T  6 .   ? 48.225  236.635 54.016 1.00 63.37 ?  202 GOL E O2  1 
HETATM 11038 C  C3  . GOL T  6 .   ? 48.627  235.695 56.313 1.00 55.26 ?  202 GOL E C3  1 
HETATM 11039 O  O3  . GOL T  6 .   ? 48.291  236.039 57.645 1.00 59.72 ?  202 GOL E O3  1 
HETATM 11040 ZN ZN  . ZN  U  5 .   ? 10.427  242.731 51.772 1.00 34.89 ?  201 ZN  F ZN  1 
HETATM 11041 C  C1  . GOL V  6 .   ? 12.725  246.785 60.150 1.00 46.46 ?  202 GOL F C1  1 
HETATM 11042 O  O1  . GOL V  6 .   ? 12.942  245.646 59.322 1.00 49.20 ?  202 GOL F O1  1 
HETATM 11043 C  C2  . GOL V  6 .   ? 12.995  246.326 61.634 1.00 50.18 ?  202 GOL F C2  1 
HETATM 11044 O  O2  . GOL V  6 .   ? 14.028  247.041 62.273 1.00 52.74 ?  202 GOL F O2  1 
HETATM 11045 C  C3  . GOL V  6 .   ? 11.627  246.511 62.373 1.00 57.12 ?  202 GOL F C3  1 
HETATM 11046 O  O3  . GOL V  6 .   ? 11.849  246.215 63.724 1.00 58.83 ?  202 GOL F O3  1 
HETATM 11047 ZN ZN  . ZN  W  5 .   ? -22.161 159.141 21.099 1.00 45.00 ?  201 ZN  H ZN  1 
HETATM 11048 C  C1  . K4I X  7 .   ? -11.638 185.302 12.984 0.80 58.86 ?  202 K4I H C1  1 
HETATM 11049 C  C2  . K4I X  7 .   ? -12.278 184.315 14.970 0.80 57.38 ?  202 K4I H C2  1 
HETATM 11050 C  C3  . K4I X  7 .   ? -11.024 183.839 15.235 0.80 55.77 ?  202 K4I H C3  1 
HETATM 11051 C  C4  . K4I X  7 .   ? -10.655 183.021 16.441 1.00 53.00 ?  202 K4I H C4  1 
HETATM 11052 C  C5  . K4I X  7 .   ? -9.986  183.857 17.521 1.00 52.87 ?  202 K4I H C5  1 
HETATM 11053 N  N1  . K4I X  7 .   ? -12.587 185.065 13.833 0.80 55.83 ?  202 K4I H N1  1 
HETATM 11054 O  O1  . K4I X  7 .   ? -5.672  180.434 23.204 0.50 44.98 ?  202 K4I H O1  1 
HETATM 11055 O  O2  . K4I X  7 .   ? -13.195 185.431 11.144 1.00 65.96 ?  202 K4I H O2  1 
HETATM 11056 N  N   . K4I X  7 .   ? -10.330 184.846 13.178 0.50 55.34 ?  202 K4I H N   1 
HETATM 11057 C  C   . K4I X  7 .   ? -9.961  184.103 14.306 0.50 55.37 ?  202 K4I H C   1 
HETATM 11058 O  O   . K4I X  7 .   ? -8.812  183.701 14.444 1.00 56.37 ?  202 K4I H O   1 
HETATM 11059 C  C10 . K4I X  7 .   ? -6.923  180.113 23.622 1.00 49.79 ?  202 K4I H C10 1 
HETATM 11060 C  C11 . K4I X  7 .   ? -7.240  179.380 24.746 1.00 49.00 ?  202 K4I H C11 1 
HETATM 11061 C  C12 . K4I X  7 .   ? -8.586  179.151 24.942 1.00 49.24 ?  202 K4I H C12 1 
HETATM 11062 C  C13 . K4I X  7 .   ? -9.577  179.635 24.113 1.00 52.32 ?  202 K4I H C13 1 
HETATM 11063 C  C14 . K4I X  7 .   ? -9.209  180.372 22.998 1.00 53.64 ?  202 K4I H C14 1 
HETATM 11064 C  C15 . K4I X  7 .   ? -7.862  180.617 22.737 1.00 49.64 ?  202 K4I H C15 1 
HETATM 11065 C  C16 . K4I X  7 .   ? -8.084  181.211 19.427 1.00 50.36 ?  202 K4I H C16 1 
HETATM 11066 C  C17 . K4I X  7 .   ? -8.505  182.098 18.260 1.00 49.51 ?  202 K4I H C17 1 
HETATM 11067 C  C18 . K4I X  7 .   ? -13.462 184.054 15.843 1.00 54.69 ?  202 K4I H C18 1 
HETATM 11068 C  C19 . K4I X  7 .   ? -12.069 186.068 11.752 1.00 66.57 ?  202 K4I H C19 1 
HETATM 11069 C  C20 . K4I X  7 .   ? -10.947 186.251 10.737 1.00 62.47 ?  202 K4I H C20 1 
HETATM 11070 C  C21 . K4I X  7 .   ? -9.926  185.115 10.813 1.00 62.61 ?  202 K4I H C21 1 
HETATM 11071 C  C22 . K4I X  7 .   ? -9.270  185.073 12.179 1.00 55.80 ?  202 K4I H C22 1 
HETATM 11072 C  C6  . K4I X  7 .   ? -8.998  183.930 19.727 1.00 46.29 ?  202 K4I H C6  1 
HETATM 11073 C  C7  . K4I X  7 .   ? -8.593  183.119 20.951 1.00 46.39 ?  202 K4I H C7  1 
HETATM 11074 C  C8  . K4I X  7 .   ? -7.531  182.092 20.552 1.00 48.41 ?  202 K4I H C8  1 
HETATM 11075 C  C9  . K4I X  7 .   ? -7.059  181.290 21.735 0.50 47.12 ?  202 K4I H C9  1 
HETATM 11076 F  F   . K4I X  7 .   ? -8.950  178.350 25.980 1.00 56.81 ?  202 K4I H F   1 
HETATM 11077 N  N2  . K4I X  7 .   ? -9.537  183.062 18.670 1.00 50.35 ?  202 K4I H N2  1 
HETATM 11078 N  N3  . K4I X  7 .   ? -5.798  181.184 21.987 0.80 46.49 ?  202 K4I H N3  1 
HETATM 11079 ZN ZN  . ZN  Y  5 .   ? 48.212  219.508 43.029 1.00 59.98 ?  201 ZN  I ZN  1 
HETATM 11080 ZN ZN  . ZN  Z  5 .   ? 27.563  185.980 47.017 1.00 46.03 ?  201 ZN  J ZN  1 
HETATM 11081 O  O   . HOH AA 8 .   ? 44.045  272.178 25.256 1.00 49.96 ?  301 HOH A O   1 
HETATM 11082 O  O   . HOH AA 8 .   ? 48.005  258.250 20.132 1.00 56.24 ?  302 HOH A O   1 
HETATM 11083 O  O   . HOH AA 8 .   ? 45.839  266.959 18.060 1.00 42.96 ?  303 HOH A O   1 
HETATM 11084 O  O   . HOH AA 8 .   ? 33.450  268.830 17.108 1.00 41.33 ?  304 HOH A O   1 
HETATM 11085 O  O   . HOH AA 8 .   ? 37.074  262.739 2.970  1.00 40.05 ?  305 HOH A O   1 
HETATM 11086 O  O   . HOH AA 8 .   ? 37.205  245.478 35.599 1.00 44.17 ?  306 HOH A O   1 
HETATM 11087 O  O   . HOH AA 8 .   ? 35.947  246.537 31.868 1.00 48.54 ?  307 HOH A O   1 
HETATM 11088 O  O   . HOH AA 8 .   ? 27.326  257.692 39.910 1.00 50.67 ?  308 HOH A O   1 
HETATM 11089 O  O   . HOH AA 8 .   ? 19.583  264.568 18.683 1.00 40.12 ?  309 HOH A O   1 
HETATM 11090 O  O   . HOH AA 8 .   ? 40.523  279.262 23.354 1.00 43.36 ?  310 HOH A O   1 
HETATM 11091 O  O   . HOH AA 8 .   ? 34.005  248.775 31.731 1.00 37.67 ?  311 HOH A O   1 
HETATM 11092 O  O   . HOH AA 8 .   ? 34.863  250.212 38.205 1.00 32.20 ?  312 HOH A O   1 
HETATM 11093 O  O   . HOH AA 8 .   ? 34.515  266.025 31.505 1.00 41.68 ?  313 HOH A O   1 
HETATM 11094 O  O   . HOH AA 8 .   ? 43.407  260.254 25.505 1.00 47.49 ?  314 HOH A O   1 
HETATM 11095 O  O   . HOH AA 8 .   ? 18.155  262.165 20.071 1.00 36.06 ?  315 HOH A O   1 
HETATM 11096 O  O   . HOH AA 8 .   ? 32.074  255.968 34.022 1.00 44.39 ?  316 HOH A O   1 
HETATM 11097 O  O   . HOH AA 8 .   ? 30.809  256.509 4.305  1.00 39.82 ?  317 HOH A O   1 
HETATM 11098 O  O   . HOH AA 8 .   ? 28.998  262.606 6.059  1.00 47.88 ?  318 HOH A O   1 
HETATM 11099 O  O   . HOH AA 8 .   ? 28.310  268.136 9.769  1.00 45.93 ?  319 HOH A O   1 
HETATM 11100 O  O   . HOH AA 8 .   ? 39.396  266.977 22.005 1.00 33.50 ?  320 HOH A O   1 
HETATM 11101 O  O   . HOH AA 8 .   ? 48.519  255.670 8.595  1.00 42.48 ?  321 HOH A O   1 
HETATM 11102 O  O   . HOH AA 8 .   ? 38.237  267.096 5.567  1.00 45.83 ?  322 HOH A O   1 
HETATM 11103 O  O   . HOH AA 8 .   ? 26.504  265.311 27.191 1.00 40.80 ?  323 HOH A O   1 
HETATM 11104 O  O   . HOH AA 8 .   ? 38.825  255.162 31.620 1.00 35.69 ?  324 HOH A O   1 
HETATM 11105 O  O   . HOH AA 8 .   ? 27.300  253.322 11.141 1.00 41.01 ?  325 HOH A O   1 
HETATM 11106 O  O   . HOH AA 8 .   ? 41.221  254.276 38.408 1.00 41.47 ?  326 HOH A O   1 
HETATM 11107 O  O   . HOH AA 8 .   ? 22.629  261.924 27.491 1.00 45.97 ?  327 HOH A O   1 
HETATM 11108 O  O   . HOH AA 8 .   ? 33.153  273.457 14.571 1.00 47.83 ?  328 HOH A O   1 
HETATM 11109 O  O   . HOH AA 8 .   ? 31.174  273.145 26.020 1.00 47.44 ?  329 HOH A O   1 
HETATM 11110 O  O   . HOH AA 8 .   ? 29.149  269.652 18.807 1.00 45.87 ?  330 HOH A O   1 
HETATM 11111 O  O   . HOH AA 8 .   ? 43.941  262.105 19.935 1.00 38.83 ?  331 HOH A O   1 
HETATM 11112 O  O   . HOH AA 8 .   ? 35.817  245.785 19.005 1.00 37.20 ?  332 HOH A O   1 
HETATM 11113 O  O   . HOH AA 8 .   ? 30.159  270.117 21.756 1.00 31.85 ?  333 HOH A O   1 
HETATM 11114 O  O   . HOH AA 8 .   ? 45.032  271.321 16.334 1.00 50.16 ?  334 HOH A O   1 
HETATM 11115 O  O   . HOH AA 8 .   ? 15.066  260.769 17.618 1.00 46.69 ?  335 HOH A O   1 
HETATM 11116 O  O   . HOH AA 8 .   ? 39.904  273.195 27.877 1.00 44.78 ?  336 HOH A O   1 
HETATM 11117 O  O   . HOH AA 8 .   ? 22.373  254.289 10.279 1.00 52.20 ?  337 HOH A O   1 
HETATM 11118 O  O   . HOH AA 8 .   ? 40.258  273.645 12.953 1.00 42.00 ?  338 HOH A O   1 
HETATM 11119 O  O   . HOH AA 8 .   ? 32.014  266.079 30.605 1.00 34.17 ?  339 HOH A O   1 
HETATM 11120 O  O   . HOH AA 8 .   ? 20.545  255.922 15.805 1.00 27.62 ?  340 HOH A O   1 
HETATM 11121 O  O   . HOH AA 8 .   ? 50.476  274.802 24.961 1.00 55.16 ?  341 HOH A O   1 
HETATM 11122 O  O   . HOH AA 8 .   ? 47.403  257.273 10.352 1.00 41.25 ?  342 HOH A O   1 
HETATM 11123 O  O   . HOH AA 8 .   ? 36.313  244.763 14.861 1.00 43.54 ?  343 HOH A O   1 
HETATM 11124 O  O   . HOH AA 8 .   ? 41.446  256.147 1.824  1.00 46.74 ?  344 HOH A O   1 
HETATM 11125 O  O   . HOH AA 8 .   ? 29.175  257.119 0.702  1.00 51.14 ?  345 HOH A O   1 
HETATM 11126 O  O   . HOH AA 8 .   ? 41.213  249.191 31.491 1.00 39.82 ?  346 HOH A O   1 
HETATM 11127 O  O   . HOH AA 8 .   ? 37.332  246.239 20.628 1.00 55.49 ?  347 HOH A O   1 
HETATM 11128 O  O   . HOH AA 8 .   ? 49.619  262.897 7.859  1.00 54.79 ?  348 HOH A O   1 
HETATM 11129 O  O   . HOH AA 8 .   ? 20.464  257.592 8.751  1.00 47.04 ?  349 HOH A O   1 
HETATM 11130 O  O   . HOH AA 8 .   ? 32.016  260.841 4.424  1.00 40.74 ?  350 HOH A O   1 
HETATM 11131 O  O   . HOH AA 8 .   ? 26.936  257.286 30.200 1.00 44.68 ?  351 HOH A O   1 
HETATM 11132 O  O   . HOH AA 8 .   ? 28.518  250.935 14.714 1.00 29.23 ?  352 HOH A O   1 
HETATM 11133 O  O   . HOH AA 8 .   ? 44.890  254.177 1.024  1.00 53.25 ?  353 HOH A O   1 
HETATM 11134 O  O   . HOH AA 8 .   ? 38.086  280.340 23.253 1.00 54.53 ?  354 HOH A O   1 
HETATM 11135 O  O   . HOH AA 8 .   ? 45.329  256.652 29.577 1.00 44.62 ?  355 HOH A O   1 
HETATM 11136 O  O   . HOH AA 8 .   ? 42.143  274.139 26.226 1.00 49.73 ?  356 HOH A O   1 
HETATM 11137 O  O   . HOH AA 8 .   ? 45.076  270.057 32.365 1.00 52.27 ?  357 HOH A O   1 
HETATM 11138 O  O   . HOH AA 8 .   ? 16.458  263.311 16.778 1.00 45.14 ?  358 HOH A O   1 
HETATM 11139 O  O   . HOH AA 8 .   ? 25.998  252.809 13.742 1.00 33.64 ?  359 HOH A O   1 
HETATM 11140 O  O   . HOH AA 8 .   ? 38.435  264.563 4.801  1.00 46.82 ?  360 HOH A O   1 
HETATM 11141 O  O   . HOH AA 8 .   ? 26.249  255.986 10.291 1.00 46.53 ?  361 HOH A O   1 
HETATM 11142 O  O   . HOH AA 8 .   ? 27.144  264.022 8.073  1.00 60.57 ?  362 HOH A O   1 
HETATM 11143 O  O   . HOH AA 8 .   ? 45.395  280.150 22.557 1.00 51.19 ?  363 HOH A O   1 
HETATM 11144 O  O   . HOH AA 8 .   ? 25.104  258.178 8.834  1.00 54.47 ?  364 HOH A O   1 
HETATM 11145 O  O   . HOH AA 8 .   ? 39.453  246.405 13.278 1.00 49.32 ?  365 HOH A O   1 
HETATM 11146 O  O   . HOH AA 8 .   ? 42.050  271.490 9.691  1.00 47.43 ?  366 HOH A O   1 
HETATM 11147 O  O   . HOH AA 8 .   ? 43.708  262.125 1.000  1.00 57.05 ?  367 HOH A O   1 
HETATM 11148 O  O   . HOH AA 8 .   ? 25.333  261.984 8.010  1.00 48.30 ?  368 HOH A O   1 
HETATM 11149 O  O   . HOH AA 8 .   ? 32.001  243.722 26.018 1.00 44.15 ?  369 HOH A O   1 
HETATM 11150 O  O   . HOH AA 8 .   ? 33.238  241.404 25.472 1.00 53.27 ?  370 HOH A O   1 
HETATM 11151 O  O   . HOH AA 8 .   ? 44.742  250.257 7.583  1.00 58.44 ?  371 HOH A O   1 
HETATM 11152 O  O   . HOH AA 8 .   ? 42.776  271.845 32.072 1.00 44.79 ?  372 HOH A O   1 
HETATM 11153 O  O   . HOH AA 8 .   ? 46.270  258.627 23.481 1.00 39.95 ?  373 HOH A O   1 
HETATM 11154 O  O   . HOH AA 8 .   ? 29.468  273.739 28.527 1.00 60.72 ?  374 HOH A O   1 
HETATM 11155 O  O   . HOH AA 8 .   ? 27.234  250.606 32.831 1.00 50.82 ?  375 HOH A O   1 
HETATM 11156 O  O   . HOH AA 8 .   ? 51.878  260.512 5.398  1.00 56.73 ?  376 HOH A O   1 
HETATM 11157 O  O   . HOH AA 8 .   ? 45.400  267.111 24.574 1.00 41.11 ?  377 HOH A O   1 
HETATM 11158 O  O   . HOH AA 8 .   ? 44.435  264.847 0.776  1.00 56.45 ?  378 HOH A O   1 
HETATM 11159 O  O   . HOH AA 8 .   ? 25.005  269.456 18.204 1.00 41.20 ?  379 HOH A O   1 
HETATM 11160 O  O   . HOH AA 8 .   ? 28.342  269.642 25.436 1.00 51.32 ?  380 HOH A O   1 
HETATM 11161 O  O   . HOH AA 8 .   ? 25.591  253.401 31.728 1.00 57.64 ?  381 HOH A O   1 
HETATM 11162 O  O   . HOH AA 8 .   ? 45.823  270.145 24.753 1.00 52.01 ?  382 HOH A O   1 
HETATM 11163 O  O   . HOH AA 8 .   ? 36.311  264.798 32.836 1.00 47.43 ?  383 HOH A O   1 
HETATM 11164 O  O   . HOH AA 8 .   ? 33.475  280.585 15.442 1.00 62.69 ?  384 HOH A O   1 
HETATM 11165 O  O   . HOH AA 8 .   ? 25.711  268.507 26.472 1.00 55.31 ?  385 HOH A O   1 
HETATM 11166 O  O   . HOH AA 8 .   ? 30.383  242.081 34.207 1.00 66.78 ?  386 HOH A O   1 
HETATM 11167 O  O   . HOH AA 8 .   ? 35.993  250.023 6.530  1.00 49.27 ?  387 HOH A O   1 
HETATM 11168 O  O   . HOH AA 8 .   ? 19.053  266.799 14.429 1.00 50.35 ?  388 HOH A O   1 
HETATM 11169 O  O   . HOH AA 8 .   ? 25.587  259.690 7.431  1.00 59.83 ?  389 HOH A O   1 
HETATM 11170 O  O   . HOH AA 8 .   ? 49.359  267.044 6.969  1.00 60.00 ?  390 HOH A O   1 
HETATM 11171 O  O   . HOH AA 8 .   ? 48.221  276.081 19.817 1.00 58.35 ?  391 HOH A O   1 
HETATM 11172 O  O   . HOH AA 8 .   ? 42.203  280.544 24.493 1.00 52.47 ?  392 HOH A O   1 
HETATM 11173 O  O   . HOH AA 8 .   ? 45.901  265.527 22.723 1.00 48.07 ?  393 HOH A O   1 
HETATM 11174 O  O   . HOH AA 8 .   ? 33.926  263.261 3.254  1.00 45.60 ?  394 HOH A O   1 
HETATM 11175 O  O   . HOH AA 8 .   ? 43.084  275.157 14.436 1.00 52.97 ?  395 HOH A O   1 
HETATM 11176 O  O   . HOH AA 8 .   ? 12.134  259.850 13.436 1.00 49.38 ?  396 HOH A O   1 
HETATM 11177 O  O   . HOH BA 8 .   ? 16.147  226.979 29.341 1.00 49.90 ?  301 HOH B O   1 
HETATM 11178 O  O   . HOH BA 8 .   ? 11.636  229.783 32.021 1.00 48.59 ?  302 HOH B O   1 
HETATM 11179 O  O   . HOH BA 8 .   ? 21.816  251.645 10.936 1.00 40.40 ?  303 HOH B O   1 
HETATM 11180 O  O   . HOH BA 8 .   ? 4.112   252.823 15.067 1.00 40.57 ?  304 HOH B O   1 
HETATM 11181 O  O   . HOH BA 8 .   ? 17.291  230.707 33.131 1.00 52.37 ?  305 HOH B O   1 
HETATM 11182 O  O   . HOH BA 8 .   ? 25.709  240.405 7.065  1.00 54.39 ?  306 HOH B O   1 
HETATM 11183 O  O   . HOH BA 8 .   ? 25.653  235.762 13.267 1.00 40.66 ?  307 HOH B O   1 
HETATM 11184 O  O   . HOH BA 8 .   ? 1.321   245.396 19.141 1.00 44.30 ?  308 HOH B O   1 
HETATM 11185 O  O   . HOH BA 8 .   ? 18.323  249.158 3.789  1.00 38.60 ?  309 HOH B O   1 
HETATM 11186 O  O   . HOH BA 8 .   ? 8.885   231.222 9.986  1.00 39.52 ?  310 HOH B O   1 
HETATM 11187 O  O   . HOH BA 8 .   ? 4.932   245.305 28.976 1.00 45.57 ?  311 HOH B O   1 
HETATM 11188 O  O   . HOH BA 8 .   ? 19.145  219.530 15.534 1.00 50.08 ?  312 HOH B O   1 
HETATM 11189 O  O   . HOH BA 8 .   ? 17.901  235.588 28.149 1.00 32.70 ?  313 HOH B O   1 
HETATM 11190 O  O   . HOH BA 8 .   ? 22.742  244.620 28.891 1.00 40.17 ?  314 HOH B O   1 
HETATM 11191 O  O   . HOH BA 8 .   ? 15.811  252.552 32.324 1.00 46.91 ?  315 HOH B O   1 
HETATM 11192 O  O   . HOH BA 8 .   ? 0.878   249.710 8.572  1.00 47.93 ?  316 HOH B O   1 
HETATM 11193 O  O   . HOH BA 8 .   ? 6.591   238.326 4.202  1.00 44.98 ?  317 HOH B O   1 
HETATM 11194 O  O   . HOH BA 8 .   ? 0.868   252.003 4.904  1.00 48.56 ?  318 HOH B O   1 
HETATM 11195 O  O   . HOH BA 8 .   ? 6.608   237.003 6.214  1.00 47.76 ?  319 HOH B O   1 
HETATM 11196 O  O   . HOH BA 8 .   ? 8.294   227.029 12.254 1.00 24.18 ?  320 HOH B O   1 
HETATM 11197 O  O   . HOH BA 8 .   ? 12.146  243.352 1.562  1.00 33.83 ?  321 HOH B O   1 
HETATM 11198 O  O   . HOH BA 8 .   ? -1.888  250.202 6.381  1.00 46.93 ?  322 HOH B O   1 
HETATM 11199 O  O   . HOH BA 8 .   ? 9.873   229.233 24.865 1.00 39.11 ?  323 HOH B O   1 
HETATM 11200 O  O   . HOH BA 8 .   ? 3.582   225.514 16.472 1.00 33.07 ?  324 HOH B O   1 
HETATM 11201 O  O   . HOH BA 8 .   ? 28.959  248.284 15.198 1.00 29.60 ?  325 HOH B O   1 
HETATM 11202 O  O   . HOH BA 8 .   ? 31.522  241.404 18.270 1.00 40.29 ?  326 HOH B O   1 
HETATM 11203 O  O   . HOH BA 8 .   ? 17.059  245.038 3.297  1.00 32.84 ?  327 HOH B O   1 
HETATM 11204 O  O   . HOH BA 8 .   ? 5.586   244.954 0.241  1.00 46.32 ?  328 HOH B O   1 
HETATM 11205 O  O   . HOH BA 8 .   ? 23.437  241.199 31.161 1.00 49.88 ?  329 HOH B O   1 
HETATM 11206 O  O   . HOH BA 8 .   ? 16.915  233.935 12.077 1.00 45.40 ?  330 HOH B O   1 
HETATM 11207 O  O   . HOH BA 8 .   ? 30.140  239.455 16.707 1.00 45.64 ?  331 HOH B O   1 
HETATM 11208 O  O   . HOH BA 8 .   ? 11.873  227.310 21.810 1.00 36.94 ?  332 HOH B O   1 
HETATM 11209 O  O   . HOH BA 8 .   ? 27.509  235.151 22.312 1.00 53.55 ?  333 HOH B O   1 
HETATM 11210 O  O   . HOH BA 8 .   ? 20.738  233.641 22.029 1.00 42.79 ?  334 HOH B O   1 
HETATM 11211 O  O   . HOH BA 8 .   ? 13.888  225.808 9.194  1.00 53.94 ?  335 HOH B O   1 
HETATM 11212 O  O   . HOH BA 8 .   ? 5.650   241.498 18.672 1.00 30.09 ?  336 HOH B O   1 
HETATM 11213 O  O   . HOH BA 8 .   ? 22.983  249.009 9.963  1.00 43.13 ?  337 HOH B O   1 
HETATM 11214 O  O   . HOH BA 8 .   ? 15.961  248.020 34.481 1.00 44.33 ?  338 HOH B O   1 
HETATM 11215 O  O   . HOH BA 8 .   ? 9.354   224.113 19.500 1.00 29.51 ?  339 HOH B O   1 
HETATM 11216 O  O   . HOH BA 8 .   ? 10.446  236.475 19.719 1.00 27.61 ?  340 HOH B O   1 
HETATM 11217 O  O   . HOH BA 8 .   ? 4.457   223.276 18.698 1.00 33.83 ?  341 HOH B O   1 
HETATM 11218 O  O   . HOH BA 8 .   ? 6.082   242.345 24.704 1.00 39.33 ?  342 HOH B O   1 
HETATM 11219 O  O   . HOH BA 8 .   ? 19.473  233.332 18.811 1.00 31.29 ?  343 HOH B O   1 
HETATM 11220 O  O   . HOH BA 8 .   ? 13.712  257.735 20.188 1.00 40.13 ?  344 HOH B O   1 
HETATM 11221 O  O   . HOH BA 8 .   ? 7.043   234.048 7.228  1.00 45.32 ?  345 HOH B O   1 
HETATM 11222 O  O   . HOH BA 8 .   ? -0.255  242.430 6.593  1.00 41.76 ?  346 HOH B O   1 
HETATM 11223 O  O   . HOH BA 8 .   ? 20.951  253.281 14.998 1.00 29.41 ?  347 HOH B O   1 
HETATM 11224 O  O   . HOH BA 8 .   ? 15.906  235.081 14.422 1.00 33.71 ?  348 HOH B O   1 
HETATM 11225 O  O   . HOH BA 8 .   ? 15.417  235.867 29.303 1.00 35.57 ?  349 HOH B O   1 
HETATM 11226 O  O   . HOH BA 8 .   ? 10.751  241.695 3.171  1.00 29.99 ?  350 HOH B O   1 
HETATM 11227 O  O   . HOH BA 8 .   ? 23.033  238.620 7.776  1.00 58.97 ?  351 HOH B O   1 
HETATM 11228 O  O   . HOH BA 8 .   ? 7.369   230.093 28.667 1.00 48.05 ?  352 HOH B O   1 
HETATM 11229 O  O   . HOH BA 8 .   ? 20.048  224.389 13.643 1.00 57.74 ?  353 HOH B O   1 
HETATM 11230 O  O   . HOH BA 8 .   ? 1.934   247.699 10.163 1.00 32.23 ?  354 HOH B O   1 
HETATM 11231 O  O   . HOH BA 8 .   ? 23.882  243.463 6.734  1.00 46.86 ?  355 HOH B O   1 
HETATM 11232 O  O   . HOH BA 8 .   ? 22.626  250.243 33.338 1.00 47.35 ?  356 HOH B O   1 
HETATM 11233 O  O   . HOH BA 8 .   ? 18.476  229.590 22.437 1.00 38.77 ?  357 HOH B O   1 
HETATM 11234 O  O   . HOH BA 8 .   ? 17.716  245.291 33.501 1.00 33.25 ?  358 HOH B O   1 
HETATM 11235 O  O   . HOH BA 8 .   ? 3.305   236.791 16.064 1.00 36.40 ?  359 HOH B O   1 
HETATM 11236 O  O   . HOH BA 8 .   ? 18.403  235.336 14.636 1.00 44.27 ?  360 HOH B O   1 
HETATM 11237 O  O   . HOH BA 8 .   ? 23.585  251.479 13.655 1.00 33.21 ?  361 HOH B O   1 
HETATM 11238 O  O   . HOH BA 8 .   ? 20.206  249.501 0.961  1.00 49.64 ?  362 HOH B O   1 
HETATM 11239 O  O   . HOH BA 8 .   ? 13.567  254.869 37.366 1.00 57.08 ?  363 HOH B O   1 
HETATM 11240 O  O   . HOH BA 8 .   ? 23.345  237.074 24.926 1.00 39.80 ?  364 HOH B O   1 
HETATM 11241 O  O   . HOH BA 8 .   ? 32.803  240.648 14.846 1.00 46.49 ?  365 HOH B O   1 
HETATM 11242 O  O   . HOH BA 8 .   ? -0.036  233.349 23.439 1.00 57.18 ?  366 HOH B O   1 
HETATM 11243 O  O   . HOH BA 8 .   ? 21.216  237.159 7.332  1.00 39.60 ?  367 HOH B O   1 
HETATM 11244 O  O   . HOH BA 8 .   ? 13.444  259.348 16.192 1.00 43.34 ?  368 HOH B O   1 
HETATM 11245 O  O   . HOH BA 8 .   ? 24.076  233.517 26.873 1.00 46.32 ?  369 HOH B O   1 
HETATM 11246 O  O   . HOH BA 8 .   ? 10.967  239.006 3.487  1.00 38.50 ?  370 HOH B O   1 
HETATM 11247 O  O   . HOH BA 8 .   ? 18.614  230.494 11.442 1.00 62.28 ?  371 HOH B O   1 
HETATM 11248 O  O   . HOH BA 8 .   ? 17.529  258.836 27.289 1.00 38.67 ?  372 HOH B O   1 
HETATM 11249 O  O   . HOH BA 8 .   ? 1.947   253.415 2.854  1.00 58.06 ?  373 HOH B O   1 
HETATM 11250 O  O   . HOH BA 8 .   ? 16.302  231.100 11.180 1.00 40.79 ?  374 HOH B O   1 
HETATM 11251 O  O   . HOH BA 8 .   ? 4.501   232.510 13.609 1.00 47.70 ?  375 HOH B O   1 
HETATM 11252 O  O   . HOH BA 8 .   ? 16.237  261.367 27.746 1.00 54.83 ?  376 HOH B O   1 
HETATM 11253 O  O   . HOH BA 8 .   ? 27.041  240.702 25.701 1.00 39.52 ?  377 HOH B O   1 
HETATM 11254 O  O   . HOH BA 8 .   ? 2.576   243.933 25.439 1.00 44.73 ?  378 HOH B O   1 
HETATM 11255 O  O   . HOH BA 8 .   ? 3.040   236.413 7.361  1.00 41.92 ?  379 HOH B O   1 
HETATM 11256 O  O   . HOH BA 8 .   ? 7.573   228.894 23.073 1.00 35.03 ?  380 HOH B O   1 
HETATM 11257 O  O   . HOH BA 8 .   ? 8.736   252.403 32.296 1.00 42.99 ?  381 HOH B O   1 
HETATM 11258 O  O   . HOH BA 8 .   ? 7.523   250.152 1.523  1.00 41.20 ?  382 HOH B O   1 
HETATM 11259 O  O   . HOH BA 8 .   ? 4.444   254.064 12.959 1.00 47.62 ?  383 HOH B O   1 
HETATM 11260 O  O   . HOH BA 8 .   ? 24.472  248.626 27.647 1.00 40.98 ?  384 HOH B O   1 
HETATM 11261 O  O   . HOH BA 8 .   ? 14.169  254.616 32.954 1.00 45.64 ?  385 HOH B O   1 
HETATM 11262 O  O   . HOH BA 8 .   ? -0.120  254.643 1.628  1.00 58.29 ?  386 HOH B O   1 
HETATM 11263 O  O   . HOH BA 8 .   ? 6.484   242.025 28.140 1.00 43.33 ?  387 HOH B O   1 
HETATM 11264 O  O   . HOH BA 8 .   ? 1.196   248.814 21.883 1.00 55.85 ?  388 HOH B O   1 
HETATM 11265 O  O   . HOH BA 8 .   ? 21.300  242.794 5.220  1.00 45.75 ?  389 HOH B O   1 
HETATM 11266 O  O   . HOH BA 8 .   ? 2.228   243.527 -0.782 1.00 56.67 ?  390 HOH B O   1 
HETATM 11267 O  O   . HOH BA 8 .   ? 34.742  243.313 15.980 1.00 53.07 ?  391 HOH B O   1 
HETATM 11268 O  O   . HOH BA 8 .   ? 21.776  252.940 30.348 1.00 51.66 ?  392 HOH B O   1 
HETATM 11269 O  O   . HOH BA 8 .   ? -0.074  227.280 22.475 1.00 44.05 ?  393 HOH B O   1 
HETATM 11270 O  O   . HOH BA 8 .   ? 7.993   226.112 23.114 1.00 36.06 ?  394 HOH B O   1 
HETATM 11271 O  O   . HOH BA 8 .   ? 2.240   245.444 21.648 1.00 57.41 ?  395 HOH B O   1 
HETATM 11272 O  O   . HOH BA 8 .   ? 10.293  258.193 14.505 1.00 45.88 ?  396 HOH B O   1 
HETATM 11273 O  O   . HOH BA 8 .   ? 4.050   251.080 22.345 1.00 49.85 ?  397 HOH B O   1 
HETATM 11274 O  O   . HOH BA 8 .   ? 7.615   253.659 29.226 1.00 50.76 ?  398 HOH B O   1 
HETATM 11275 O  O   . HOH BA 8 .   ? 4.523   242.697 -0.445 1.00 48.96 ?  399 HOH B O   1 
HETATM 11276 O  O   . HOH BA 8 .   ? 12.642  222.256 22.815 1.00 52.19 ?  400 HOH B O   1 
HETATM 11277 O  O   . HOH BA 8 .   ? -1.822  242.745 -1.297 1.00 53.33 ?  401 HOH B O   1 
HETATM 11278 O  O   . HOH BA 8 .   ? 9.578   256.098 12.726 1.00 39.83 ?  402 HOH B O   1 
HETATM 11279 O  O   . HOH BA 8 .   ? 22.325  232.329 23.240 1.00 46.38 ?  403 HOH B O   1 
HETATM 11280 O  O   . HOH BA 8 .   ? 3.495   244.093 22.950 1.00 38.58 ?  404 HOH B O   1 
HETATM 11281 O  O   . HOH BA 8 .   ? 20.356  234.315 16.137 1.00 43.65 ?  405 HOH B O   1 
HETATM 11282 O  O   . HOH BA 8 .   ? 9.522   253.703 39.988 1.00 60.56 ?  406 HOH B O   1 
HETATM 11283 O  O   . HOH BA 8 .   ? 23.558  246.378 7.728  1.00 54.78 ?  407 HOH B O   1 
HETATM 11284 O  O   . HOH BA 8 .   ? 24.636  234.467 15.245 1.00 41.97 ?  408 HOH B O   1 
HETATM 11285 O  O   . HOH BA 8 .   ? 15.331  229.793 9.228  1.00 48.27 ?  409 HOH B O   1 
HETATM 11286 O  O   . HOH BA 8 .   ? 21.704  226.918 29.278 1.00 54.85 ?  410 HOH B O   1 
HETATM 11287 O  O   . HOH BA 8 .   ? 13.223  236.586 30.840 1.00 45.36 ?  411 HOH B O   1 
HETATM 11288 O  O   . HOH BA 8 .   ? 22.829  240.879 7.045  1.00 52.52 ?  412 HOH B O   1 
HETATM 11289 O  O   . HOH BA 8 .   ? 15.767  223.986 9.992  1.00 40.27 ?  413 HOH B O   1 
HETATM 11290 O  O   . HOH BA 8 .   ? 10.926  255.519 8.913  1.00 54.25 ?  414 HOH B O   1 
HETATM 11291 O  O   . HOH BA 8 .   ? 22.583  232.998 15.631 1.00 51.07 ?  415 HOH B O   1 
HETATM 11292 O  O   . HOH BA 8 .   ? 23.472  231.176 25.422 1.00 58.06 ?  416 HOH B O   1 
HETATM 11293 O  O   . HOH BA 8 .   ? 6.598   256.219 13.007 1.00 49.26 ?  417 HOH B O   1 
HETATM 11294 O  O   . HOH BA 8 .   ? 1.293   236.882 4.513  1.00 60.21 ?  418 HOH B O   1 
HETATM 11295 O  O   . HOH BA 8 .   ? 24.302  248.429 6.641  1.00 51.98 ?  419 HOH B O   1 
HETATM 11296 O  O   . HOH BA 8 .   ? 7.648   222.298 20.597 1.00 34.13 ?  420 HOH B O   1 
HETATM 11297 O  O   . HOH BA 8 .   ? 6.938   252.959 1.898  1.00 51.04 ?  421 HOH B O   1 
HETATM 11298 O  O   . HOH BA 8 .   ? 15.671  242.758 1.662  1.00 44.08 ?  422 HOH B O   1 
HETATM 11299 O  O   . HOH BA 8 .   ? 9.239   227.969 9.859  1.00 43.97 ?  423 HOH B O   1 
HETATM 11300 O  O   . HOH BA 8 .   ? 6.244   228.517 11.543 1.00 43.94 ?  424 HOH B O   1 
HETATM 11301 O  O   . HOH BA 8 .   ? 6.228   224.156 22.485 1.00 34.22 ?  425 HOH B O   1 
HETATM 11302 O  O   . HOH BA 8 .   ? 4.084   256.077 21.876 1.00 55.38 ?  426 HOH B O   1 
HETATM 11303 O  O   . HOH BA 8 .   ? 21.528  231.280 17.301 1.00 52.07 ?  427 HOH B O   1 
HETATM 11304 O  O   . HOH BA 8 .   ? 3.971   233.914 8.082  1.00 46.48 ?  428 HOH B O   1 
HETATM 11305 O  O   . HOH BA 8 .   ? 22.189  216.991 15.150 1.00 59.53 ?  429 HOH B O   1 
HETATM 11306 O  O   . HOH BA 8 .   ? 3.047   259.588 23.840 1.00 63.78 ?  430 HOH B O   1 
HETATM 11307 O  O   . HOH BA 8 .   ? 3.677   232.469 10.602 1.00 55.58 ?  431 HOH B O   1 
HETATM 11308 O  O   . HOH BA 8 .   ? -0.050  230.819 14.612 1.00 51.65 ?  432 HOH B O   1 
HETATM 11309 O  O   . HOH BA 8 .   ? 2.070   229.755 12.255 1.00 54.67 ?  433 HOH B O   1 
HETATM 11310 O  O   . HOH CA 8 .   ? 2.953   194.505 3.965  1.00 59.27 ?  301 HOH C O   1 
HETATM 11311 O  O   . HOH CA 8 .   ? 18.571  188.845 34.634 1.00 51.95 ?  302 HOH C O   1 
HETATM 11312 O  O   . HOH CA 8 .   ? 21.034  187.336 17.806 1.00 54.43 ?  303 HOH C O   1 
HETATM 11313 O  O   . HOH CA 8 .   ? 19.018  186.408 18.843 1.00 42.94 ?  304 HOH C O   1 
HETATM 11314 O  O   . HOH CA 8 .   ? 4.641   178.032 19.932 1.00 41.49 ?  305 HOH C O   1 
HETATM 11315 O  O   . HOH CA 8 .   ? 0.025   176.782 10.460 1.00 40.62 ?  306 HOH C O   1 
HETATM 11316 O  O   . HOH CA 8 .   ? 6.572   179.614 0.296  1.00 40.70 ?  307 HOH C O   1 
HETATM 11317 O  O   . HOH CA 8 .   ? 1.043   190.928 34.124 1.00 28.76 ?  308 HOH C O   1 
HETATM 11318 O  O   . HOH CA 8 .   ? 9.413   191.140 37.864 1.00 56.30 ?  309 HOH C O   1 
HETATM 11319 O  O   . HOH CA 8 .   ? 3.783   188.683 0.708  1.00 38.65 ?  310 HOH C O   1 
HETATM 11320 O  O   . HOH CA 8 .   ? 18.391  190.869 10.438 1.00 49.77 ?  311 HOH C O   1 
HETATM 11321 O  O   . HOH CA 8 .   ? -3.152  177.763 2.838  1.00 53.49 ?  312 HOH C O   1 
HETATM 11322 O  O   . HOH CA 8 .   ? 20.075  172.571 15.722 1.00 48.30 ?  313 HOH C O   1 
HETATM 11323 O  O   . HOH CA 8 .   ? 6.025   196.271 10.915 1.00 36.23 ?  314 HOH C O   1 
HETATM 11324 O  O   . HOH CA 8 .   ? 18.915  194.399 8.840  1.00 53.80 ?  315 HOH C O   1 
HETATM 11325 O  O   . HOH CA 8 .   ? 16.268  175.366 27.738 1.00 49.64 ?  316 HOH C O   1 
HETATM 11326 O  O   . HOH CA 8 .   ? 18.659  182.979 14.752 1.00 52.40 ?  317 HOH C O   1 
HETATM 11327 O  O   . HOH CA 8 .   ? -5.065  192.553 18.162 1.00 35.51 ?  318 HOH C O   1 
HETATM 11328 O  O   . HOH CA 8 .   ? 18.065  203.275 17.852 1.00 48.59 ?  319 HOH C O   1 
HETATM 11329 O  O   . HOH CA 8 .   ? 10.026  183.395 2.599  1.00 36.16 ?  320 HOH C O   1 
HETATM 11330 O  O   . HOH CA 8 .   ? 14.220  185.455 30.385 1.00 31.90 ?  321 HOH C O   1 
HETATM 11331 O  O   . HOH CA 8 .   ? -1.117  183.420 37.987 1.00 47.99 ?  322 HOH C O   1 
HETATM 11332 O  O   . HOH CA 8 .   ? 1.170   185.387 31.287 1.00 31.17 ?  323 HOH C O   1 
HETATM 11333 O  O   . HOH CA 8 .   ? 9.312   200.067 10.003 1.00 52.03 ?  324 HOH C O   1 
HETATM 11334 O  O   . HOH CA 8 .   ? -5.641  192.590 14.098 1.00 35.78 ?  325 HOH C O   1 
HETATM 11335 O  O   . HOH CA 8 .   ? 9.221   194.584 29.672 1.00 33.72 ?  326 HOH C O   1 
HETATM 11336 O  O   . HOH CA 8 .   ? 3.359   196.385 14.539 1.00 22.07 ?  327 HOH C O   1 
HETATM 11337 O  O   . HOH CA 8 .   ? -4.695  191.774 31.476 1.00 37.08 ?  328 HOH C O   1 
HETATM 11338 O  O   . HOH CA 8 .   ? 8.820   195.760 4.042  1.00 60.07 ?  329 HOH C O   1 
HETATM 11339 O  O   . HOH CA 8 .   ? 11.425  179.058 21.318 1.00 33.51 ?  330 HOH C O   1 
HETATM 11340 O  O   . HOH CA 8 .   ? 19.324  189.524 29.710 1.00 49.58 ?  331 HOH C O   1 
HETATM 11341 O  O   . HOH CA 8 .   ? 7.698   191.677 3.933  1.00 37.84 ?  332 HOH C O   1 
HETATM 11342 O  O   . HOH CA 8 .   ? 11.478  200.940 15.843 1.00 29.02 ?  333 HOH C O   1 
HETATM 11343 O  O   . HOH CA 8 .   ? 7.773   177.742 30.911 1.00 46.64 ?  334 HOH C O   1 
HETATM 11344 O  O   . HOH CA 8 .   ? 13.575  190.328 5.756  1.00 41.37 ?  335 HOH C O   1 
HETATM 11345 O  O   . HOH CA 8 .   ? -8.757  187.668 14.933 1.00 52.99 ?  336 HOH C O   1 
HETATM 11346 O  O   . HOH CA 8 .   ? 0.611   172.031 3.630  1.00 53.51 ?  337 HOH C O   1 
HETATM 11347 O  O   . HOH CA 8 .   ? 16.616  182.927 16.850 1.00 35.84 ?  338 HOH C O   1 
HETATM 11348 O  O   . HOH CA 8 .   ? 5.242   190.728 33.552 1.00 42.85 ?  339 HOH C O   1 
HETATM 11349 O  O   . HOH CA 8 .   ? 3.219   172.400 6.895  1.00 53.69 ?  340 HOH C O   1 
HETATM 11350 O  O   . HOH CA 8 .   ? 16.673  190.579 27.171 1.00 39.81 ?  341 HOH C O   1 
HETATM 11351 O  O   . HOH CA 8 .   ? 8.487   173.893 24.098 1.00 41.18 ?  342 HOH C O   1 
HETATM 11352 O  O   . HOH CA 8 .   ? 9.621   179.156 32.186 1.00 51.32 ?  343 HOH C O   1 
HETATM 11353 O  O   . HOH CA 8 .   ? 2.630   192.971 6.738  1.00 41.24 ?  344 HOH C O   1 
HETATM 11354 O  O   . HOH CA 8 .   ? 6.310   174.182 -0.446 1.00 52.43 ?  345 HOH C O   1 
HETATM 11355 O  O   . HOH CA 8 .   ? 12.985  180.374 5.227  1.00 43.00 ?  346 HOH C O   1 
HETATM 11356 O  O   . HOH CA 8 .   ? -5.822  184.893 36.652 1.00 54.33 ?  347 HOH C O   1 
HETATM 11357 O  O   . HOH CA 8 .   ? -11.071 202.806 22.802 1.00 52.31 ?  348 HOH C O   1 
HETATM 11358 O  O   . HOH CA 8 .   ? 3.373   178.711 24.786 1.00 37.43 ?  349 HOH C O   1 
HETATM 11359 O  O   . HOH CA 8 .   ? 12.905  183.635 31.363 1.00 36.20 ?  350 HOH C O   1 
HETATM 11360 O  O   . HOH CA 8 .   ? 12.106  175.066 8.250  1.00 47.28 ?  351 HOH C O   1 
HETATM 11361 O  O   . HOH CA 8 .   ? 17.970  199.714 20.129 1.00 33.73 ?  352 HOH C O   1 
HETATM 11362 O  O   . HOH CA 8 .   ? 18.630  188.224 9.605  1.00 41.18 ?  353 HOH C O   1 
HETATM 11363 O  O   . HOH CA 8 .   ? -5.071  186.167 30.915 1.00 35.39 ?  354 HOH C O   1 
HETATM 11364 O  O   . HOH CA 8 .   ? 15.059  195.920 27.525 1.00 37.48 ?  355 HOH C O   1 
HETATM 11365 O  O   . HOH CA 8 .   ? 2.339   182.474 1.285  1.00 33.70 ?  356 HOH C O   1 
HETATM 11366 O  O   . HOH CA 8 .   ? 17.292  191.787 33.551 1.00 56.75 ?  357 HOH C O   1 
HETATM 11367 O  O   . HOH CA 8 .   ? 19.267  197.707 19.131 1.00 38.84 ?  358 HOH C O   1 
HETATM 11368 O  O   . HOH CA 8 .   ? 1.855   177.603 13.364 1.00 34.43 ?  359 HOH C O   1 
HETATM 11369 O  O   . HOH CA 8 .   ? 3.169   177.579 17.653 1.00 45.02 ?  360 HOH C O   1 
HETATM 11370 O  O   . HOH CA 8 .   ? 20.060  187.389 26.853 1.00 58.19 ?  361 HOH C O   1 
HETATM 11371 O  O   . HOH CA 8 .   ? 20.992  191.661 16.281 1.00 50.87 ?  362 HOH C O   1 
HETATM 11372 O  O   . HOH CA 8 .   ? 10.597  188.651 4.155  1.00 33.16 ?  363 HOH C O   1 
HETATM 11373 O  O   . HOH CA 8 .   ? 20.443  181.053 14.301 1.00 47.26 ?  364 HOH C O   1 
HETATM 11374 O  O   . HOH CA 8 .   ? 7.208   197.424 27.762 1.00 43.23 ?  365 HOH C O   1 
HETATM 11375 O  O   . HOH CA 8 .   ? 10.187  174.345 2.370  1.00 54.59 ?  366 HOH C O   1 
HETATM 11376 O  O   . HOH CA 8 .   ? 10.582  181.486 4.556  1.00 37.34 ?  367 HOH C O   1 
HETATM 11377 O  O   . HOH CA 8 .   ? -6.987  178.299 17.276 1.00 42.45 ?  368 HOH C O   1 
HETATM 11378 O  O   . HOH CA 8 .   ? 6.119   197.680 13.538 1.00 28.57 ?  369 HOH C O   1 
HETATM 11379 O  O   . HOH CA 8 .   ? 18.918  185.443 21.701 1.00 40.56 ?  370 HOH C O   1 
HETATM 11380 O  O   . HOH CA 8 .   ? 8.767   196.106 10.350 1.00 41.12 ?  371 HOH C O   1 
HETATM 11381 O  O   . HOH CA 8 .   ? -0.043  175.983 20.380 1.00 48.27 ?  372 HOH C O   1 
HETATM 11382 O  O   . HOH CA 8 .   ? 19.969  200.526 16.822 1.00 44.24 ?  373 HOH C O   1 
HETATM 11383 O  O   . HOH CA 8 .   ? 18.718  186.564 24.794 1.00 50.21 ?  374 HOH C O   1 
HETATM 11384 O  O   . HOH CA 8 .   ? 10.602  172.612 8.589  1.00 43.04 ?  375 HOH C O   1 
HETATM 11385 O  O   . HOH CA 8 .   ? 19.804  175.734 25.266 1.00 48.92 ?  376 HOH C O   1 
HETATM 11386 O  O   . HOH CA 8 .   ? 6.540   191.546 36.578 1.00 40.65 ?  377 HOH C O   1 
HETATM 11387 O  O   . HOH CA 8 .   ? -4.092  187.830 11.272 1.00 43.65 ?  378 HOH C O   1 
HETATM 11388 O  O   . HOH CA 8 .   ? 1.815   180.317 -2.277 1.00 49.51 ?  379 HOH C O   1 
HETATM 11389 O  O   . HOH CA 8 .   ? 6.312   175.625 19.172 1.00 46.94 ?  380 HOH C O   1 
HETATM 11390 O  O   . HOH CA 8 .   ? -5.690  189.731 12.577 1.00 45.32 ?  381 HOH C O   1 
HETATM 11391 O  O   . HOH CA 8 .   ? -6.598  185.950 27.665 1.00 44.34 ?  382 HOH C O   1 
HETATM 11392 O  O   . HOH CA 8 .   ? 20.944  182.489 26.256 1.00 49.58 ?  383 HOH C O   1 
HETATM 11393 O  O   . HOH CA 8 .   ? 8.012   176.244 0.319  1.00 45.10 ?  384 HOH C O   1 
HETATM 11394 O  O   . HOH CA 8 .   ? 3.634   178.934 28.478 1.00 42.69 ?  385 HOH C O   1 
HETATM 11395 O  O   . HOH CA 8 .   ? 0.960   178.276 16.148 1.00 35.90 ?  386 HOH C O   1 
HETATM 11396 O  O   . HOH CA 8 .   ? 27.485  176.837 18.460 1.00 51.23 ?  387 HOH C O   1 
HETATM 11397 O  O   . HOH CA 8 .   ? 28.892  172.117 20.906 1.00 59.70 ?  388 HOH C O   1 
HETATM 11398 O  O   . HOH CA 8 .   ? -5.000  181.462 13.610 1.00 44.30 ?  389 HOH C O   1 
HETATM 11399 O  O   . HOH CA 8 .   ? -8.158  196.318 17.634 1.00 57.55 ?  390 HOH C O   1 
HETATM 11400 O  O   . HOH CA 8 .   ? -2.609  182.054 36.447 1.00 58.08 ?  391 HOH C O   1 
HETATM 11401 O  O   . HOH CA 8 .   ? -1.710  175.238 18.046 1.00 51.89 ?  392 HOH C O   1 
HETATM 11402 O  O   . HOH CA 8 .   ? -5.012  196.971 25.420 1.00 32.10 ?  393 HOH C O   1 
HETATM 11403 O  O   . HOH CA 8 .   ? 2.695   197.462 32.869 1.00 47.52 ?  394 HOH C O   1 
HETATM 11404 O  O   . HOH CA 8 .   ? 14.328  174.341 9.188  1.00 45.50 ?  395 HOH C O   1 
HETATM 11405 O  O   . HOH CA 8 .   ? -0.535  178.668 28.754 1.00 47.14 ?  396 HOH C O   1 
HETATM 11406 O  O   . HOH CA 8 .   ? -1.262  176.600 8.257  1.00 51.75 ?  397 HOH C O   1 
HETATM 11407 O  O   . HOH CA 8 .   ? 5.329   177.640 29.972 1.00 50.54 ?  398 HOH C O   1 
HETATM 11408 O  O   . HOH CA 8 .   ? 0.578   177.108 22.792 1.00 36.37 ?  399 HOH C O   1 
HETATM 11409 O  O   . HOH CA 8 .   ? -7.652  197.030 25.266 1.00 50.69 ?  400 HOH C O   1 
HETATM 11410 O  O   . HOH CA 8 .   ? 11.597  196.159 14.745 1.00 42.59 ?  401 HOH C O   1 
HETATM 11411 O  O   . HOH CA 8 .   ? 7.686   173.678 18.119 1.00 45.35 ?  402 HOH C O   1 
HETATM 11412 O  O   . HOH CA 8 .   ? 2.698   191.828 -1.496 1.00 36.19 ?  403 HOH C O   1 
HETATM 11413 O  O   . HOH CA 8 .   ? 14.267  190.505 -0.517 1.00 39.34 ?  404 HOH C O   1 
HETATM 11414 O  O   . HOH CA 8 .   ? -9.596  202.926 16.940 1.00 51.20 ?  405 HOH C O   1 
HETATM 11415 O  O   . HOH CA 8 .   ? -6.369  193.220 33.181 1.00 51.93 ?  406 HOH C O   1 
HETATM 11416 O  O   . HOH CA 8 .   ? 22.436  179.366 13.009 1.00 55.03 ?  407 HOH C O   1 
HETATM 11417 O  O   . HOH CA 8 .   ? 21.138  190.361 18.448 1.00 39.10 ?  408 HOH C O   1 
HETATM 11418 O  O   . HOH CA 8 .   ? 9.890   196.004 1.858  1.00 46.61 ?  409 HOH C O   1 
HETATM 11419 O  O   . HOH CA 8 .   ? 9.054   197.283 12.893 1.00 45.63 ?  410 HOH C O   1 
HETATM 11420 O  O   . HOH CA 8 .   ? 25.788  176.394 15.032 1.00 53.09 ?  411 HOH C O   1 
HETATM 11421 O  O   . HOH CA 8 .   ? -1.160  182.209 33.940 1.00 56.27 ?  412 HOH C O   1 
HETATM 11422 O  O   . HOH CA 8 .   ? 10.735  196.335 5.785  1.00 52.51 ?  413 HOH C O   1 
HETATM 11423 O  O   . HOH CA 8 .   ? 14.704  198.530 6.913  1.00 53.25 ?  414 HOH C O   1 
HETATM 11424 O  O   . HOH CA 8 .   ? 4.323   197.707 12.160 1.00 55.43 ?  415 HOH C O   1 
HETATM 11425 O  O   . HOH CA 8 .   ? 22.067  185.202 29.819 1.00 57.96 ?  416 HOH C O   1 
HETATM 11426 O  O   . HOH CA 8 .   ? 6.166   194.076 3.830  1.00 37.36 ?  417 HOH C O   1 
HETATM 11427 O  O   . HOH CA 8 .   ? 8.460   198.078 8.092  1.00 55.73 ?  418 HOH C O   1 
HETATM 11428 O  O   . HOH CA 8 .   ? 12.222  186.736 3.312  1.00 43.73 ?  419 HOH C O   1 
HETATM 11429 O  O   . HOH CA 8 .   ? -1.238  175.544 25.184 1.00 52.66 ?  420 HOH C O   1 
HETATM 11430 O  O   . HOH CA 8 .   ? 8.319   200.181 12.877 1.00 41.03 ?  421 HOH C O   1 
HETATM 11431 O  O   . HOH CA 8 .   ? -1.116  189.875 6.282  1.00 51.17 ?  422 HOH C O   1 
HETATM 11432 O  O   . HOH CA 8 .   ? 21.857  197.007 14.720 1.00 53.07 ?  423 HOH C O   1 
HETATM 11433 O  O   . HOH CA 8 .   ? -8.203  179.018 8.886  1.00 55.34 ?  424 HOH C O   1 
HETATM 11434 O  O   . HOH CA 8 .   ? -6.058  198.549 35.277 1.00 66.14 ?  425 HOH C O   1 
HETATM 11435 O  O   . HOH CA 8 .   ? -6.898  184.038 31.775 1.00 46.33 ?  426 HOH C O   1 
HETATM 11436 O  O   . HOH CA 8 .   ? 3.321   177.382 22.409 1.00 43.11 ?  427 HOH C O   1 
HETATM 11437 O  O   . HOH CA 8 .   ? 3.772   174.272 22.508 1.00 50.58 ?  428 HOH C O   1 
HETATM 11438 O  O   . HOH CA 8 .   ? 26.847  185.336 19.198 1.00 58.65 ?  429 HOH C O   1 
HETATM 11439 O  O   . HOH CA 8 .   ? -4.730  176.168 14.448 1.00 43.62 ?  430 HOH C O   1 
HETATM 11440 O  O   . HOH CA 8 .   ? 21.296  203.126 17.988 1.00 56.41 ?  431 HOH C O   1 
HETATM 11441 O  O   . HOH CA 8 .   ? 12.501  171.798 10.186 1.00 54.27 ?  432 HOH C O   1 
HETATM 11442 O  O   . HOH CA 8 .   ? -3.045  184.258 2.916  1.00 52.47 ?  433 HOH C O   1 
HETATM 11443 O  O   . HOH CA 8 .   ? -7.349  199.758 33.452 1.00 63.49 ?  434 HOH C O   1 
HETATM 11444 O  O   . HOH DA 8 .   ? -2.587  226.295 22.514 1.00 33.88 ?  301 HOH D O   1 
HETATM 11445 O  O   . HOH DA 8 .   ? -11.352 221.314 9.791  1.00 51.61 ?  302 HOH D O   1 
HETATM 11446 O  O   . HOH DA 8 .   ? 0.801   220.774 29.891 1.00 43.30 ?  303 HOH D O   1 
HETATM 11447 O  O   . HOH DA 8 .   ? -7.179  211.815 16.267 1.00 40.72 ?  304 HOH D O   1 
HETATM 11448 O  O   . HOH DA 8 .   ? -11.803 214.141 14.523 1.00 45.11 ?  305 HOH D O   1 
HETATM 11449 O  O   . HOH DA 8 .   ? -2.615  205.235 30.348 1.00 41.56 ?  306 HOH D O   1 
HETATM 11450 O  O   . HOH DA 8 .   ? 11.694  222.692 19.636 1.00 42.25 ?  307 HOH D O   1 
HETATM 11451 O  O   . HOH DA 8 .   ? 3.318   222.738 4.603  1.00 47.81 ?  308 HOH D O   1 
HETATM 11452 O  O   . HOH DA 8 .   ? -9.093  211.098 14.920 1.00 50.87 ?  309 HOH D O   1 
HETATM 11453 O  O   . HOH DA 8 .   ? -11.450 216.821 31.463 1.00 49.58 ?  310 HOH D O   1 
HETATM 11454 O  O   . HOH DA 8 .   ? -8.301  217.760 6.955  1.00 55.97 ?  311 HOH D O   1 
HETATM 11455 O  O   . HOH DA 8 .   ? 6.204   202.952 2.587  1.00 53.28 ?  312 HOH D O   1 
HETATM 11456 O  O   . HOH DA 8 .   ? -4.834  212.961 28.244 1.00 27.17 ?  313 HOH D O   1 
HETATM 11457 O  O   . HOH DA 8 .   ? 17.133  216.794 15.433 1.00 39.38 ?  314 HOH D O   1 
HETATM 11458 O  O   . HOH DA 8 .   ? 6.925   220.181 24.967 1.00 35.81 ?  315 HOH D O   1 
HETATM 11459 O  O   . HOH DA 8 .   ? -17.072 219.438 12.791 1.00 42.99 ?  316 HOH D O   1 
HETATM 11460 O  O   . HOH DA 8 .   ? -3.743  215.143 29.332 1.00 29.69 ?  317 HOH D O   1 
HETATM 11461 O  O   . HOH DA 8 .   ? 1.901   221.490 6.546  1.00 49.62 ?  318 HOH D O   1 
HETATM 11462 O  O   . HOH DA 8 .   ? 6.832   208.586 34.337 1.00 37.03 ?  319 HOH D O   1 
HETATM 11463 O  O   . HOH DA 8 .   ? 1.772   223.563 7.134  1.00 43.21 ?  320 HOH D O   1 
HETATM 11464 O  O   . HOH DA 8 .   ? 15.877  221.356 8.990  1.00 37.62 ?  321 HOH D O   1 
HETATM 11465 O  O   . HOH DA 8 .   ? 0.500   204.290 28.638 1.00 38.13 ?  322 HOH D O   1 
HETATM 11466 O  O   . HOH DA 8 .   ? -1.981  227.656 28.093 1.00 50.78 ?  323 HOH D O   1 
HETATM 11467 O  O   . HOH DA 8 .   ? 11.203  206.414 32.073 1.00 41.72 ?  324 HOH D O   1 
HETATM 11468 O  O   . HOH DA 8 .   ? 12.029  227.306 5.518  1.00 58.07 ?  325 HOH D O   1 
HETATM 11469 O  O   . HOH DA 8 .   ? -4.123  215.263 14.531 1.00 30.99 ?  326 HOH D O   1 
HETATM 11470 O  O   . HOH DA 8 .   ? -10.494 226.567 19.662 1.00 25.27 ?  327 HOH D O   1 
HETATM 11471 O  O   . HOH DA 8 .   ? 9.966   219.709 29.227 1.00 46.37 ?  328 HOH D O   1 
HETATM 11472 O  O   . HOH DA 8 .   ? 16.484  205.938 20.092 1.00 39.79 ?  329 HOH D O   1 
HETATM 11473 O  O   . HOH DA 8 .   ? -4.277  223.455 10.139 1.00 30.89 ?  330 HOH D O   1 
HETATM 11474 O  O   . HOH DA 8 .   ? 6.121   221.008 18.888 1.00 26.35 ?  331 HOH D O   1 
HETATM 11475 O  O   . HOH DA 8 .   ? 6.008   219.719 28.707 1.00 42.08 ?  332 HOH D O   1 
HETATM 11476 O  O   . HOH DA 8 .   ? 7.008   206.543 3.559  1.00 41.64 ?  333 HOH D O   1 
HETATM 11477 O  O   . HOH DA 8 .   ? 3.510   208.240 33.273 1.00 32.26 ?  334 HOH D O   1 
HETATM 11478 O  O   . HOH DA 8 .   ? -2.882  228.075 16.507 1.00 38.02 ?  335 HOH D O   1 
HETATM 11479 O  O   . HOH DA 8 .   ? 4.531   215.007 1.824  1.00 24.34 ?  336 HOH D O   1 
HETATM 11480 O  O   . HOH DA 8 .   ? 4.202   198.145 9.699  1.00 43.38 ?  337 HOH D O   1 
HETATM 11481 O  O   . HOH DA 8 .   ? -7.593  196.943 11.116 1.00 51.95 ?  338 HOH D O   1 
HETATM 11482 O  O   . HOH DA 8 .   ? 0.814   207.866 4.038  1.00 37.66 ?  339 HOH D O   1 
HETATM 11483 O  O   . HOH DA 8 .   ? 9.474   201.280 31.150 1.00 53.81 ?  340 HOH D O   1 
HETATM 11484 O  O   . HOH DA 8 .   ? 20.570  210.621 17.268 1.00 54.80 ?  341 HOH D O   1 
HETATM 11485 O  O   . HOH DA 8 .   ? -0.471  219.565 19.928 1.00 28.71 ?  342 HOH D O   1 
HETATM 11486 O  O   . HOH DA 8 .   ? 0.899   197.419 14.860 1.00 26.00 ?  343 HOH D O   1 
HETATM 11487 O  O   . HOH DA 8 .   ? -10.123 205.094 21.544 1.00 46.38 ?  344 HOH D O   1 
HETATM 11488 O  O   . HOH DA 8 .   ? -7.579  200.789 16.281 1.00 37.40 ?  345 HOH D O   1 
HETATM 11489 O  O   . HOH DA 8 .   ? 17.730  220.394 4.349  1.00 48.79 ?  346 HOH D O   1 
HETATM 11490 O  O   . HOH DA 8 .   ? 7.270   201.804 10.759 1.00 40.45 ?  347 HOH D O   1 
HETATM 11491 O  O   . HOH DA 8 .   ? 7.479   212.968 31.657 1.00 40.16 ?  348 HOH D O   1 
HETATM 11492 O  O   . HOH DA 8 .   ? -9.654  219.299 32.178 1.00 52.85 ?  349 HOH D O   1 
HETATM 11493 O  O   . HOH DA 8 .   ? 5.807   205.262 0.183  1.00 53.71 ?  350 HOH D O   1 
HETATM 11494 O  O   . HOH DA 8 .   ? -6.384  195.103 15.702 1.00 43.83 ?  351 HOH D O   1 
HETATM 11495 O  O   . HOH DA 8 .   ? 12.523  215.873 1.827  1.00 28.56 ?  352 HOH D O   1 
HETATM 11496 O  O   . HOH DA 8 .   ? 9.078   201.893 14.822 1.00 26.75 ?  353 HOH D O   1 
HETATM 11497 O  O   . HOH DA 8 .   ? -6.697  198.613 17.750 1.00 38.44 ?  354 HOH D O   1 
HETATM 11498 O  O   . HOH DA 8 .   ? 18.129  205.600 16.258 1.00 43.48 ?  355 HOH D O   1 
HETATM 11499 O  O   . HOH DA 8 .   ? 14.162  226.226 4.892  1.00 38.79 ?  356 HOH D O   1 
HETATM 11500 O  O   . HOH DA 8 .   ? -8.752  231.359 18.745 1.00 31.21 ?  357 HOH D O   1 
HETATM 11501 O  O   . HOH DA 8 .   ? 3.851   216.992 3.601  1.00 28.25 ?  358 HOH D O   1 
HETATM 11502 O  O   . HOH DA 8 .   ? -7.717  217.370 11.251 1.00 39.59 ?  359 HOH D O   1 
HETATM 11503 O  O   . HOH DA 8 .   ? 5.941   200.512 13.387 1.00 29.54 ?  360 HOH D O   1 
HETATM 11504 O  O   . HOH DA 8 .   ? -7.510  197.582 13.924 1.00 55.78 ?  361 HOH D O   1 
HETATM 11505 O  O   . HOH DA 8 .   ? -6.263  230.950 16.301 1.00 28.85 ?  362 HOH D O   1 
HETATM 11506 O  O   . HOH DA 8 .   ? -6.273  207.566 24.634 1.00 34.55 ?  363 HOH D O   1 
HETATM 11507 O  O   . HOH DA 8 .   ? 14.332  212.874 32.088 1.00 32.87 ?  364 HOH D O   1 
HETATM 11508 O  O   . HOH DA 8 .   ? 10.016  218.815 33.956 1.00 54.38 ?  365 HOH D O   1 
HETATM 11509 O  O   . HOH DA 8 .   ? 16.672  210.362 12.649 1.00 33.32 ?  366 HOH D O   1 
HETATM 11510 O  O   . HOH DA 8 .   ? -5.187  210.012 7.380  1.00 34.04 ?  367 HOH D O   1 
HETATM 11511 O  O   . HOH DA 8 .   ? -14.877 221.140 12.891 1.00 36.35 ?  368 HOH D O   1 
HETATM 11512 O  O   . HOH DA 8 .   ? -13.901 218.183 10.154 1.00 51.64 ?  369 HOH D O   1 
HETATM 11513 O  O   . HOH DA 8 .   ? -0.526  226.537 14.199 1.00 50.80 ?  370 HOH D O   1 
HETATM 11514 O  O   . HOH DA 8 .   ? -10.509 215.736 22.637 1.00 36.08 ?  371 HOH D O   1 
HETATM 11515 O  O   . HOH DA 8 .   ? 13.486  207.023 33.034 1.00 42.19 ?  372 HOH D O   1 
HETATM 11516 O  O   . HOH DA 8 .   ? -8.471  206.880 13.098 1.00 48.31 ?  373 HOH D O   1 
HETATM 11517 O  O   . HOH DA 8 .   ? -0.712  207.081 5.611  1.00 50.84 ?  374 HOH D O   1 
HETATM 11518 O  O   . HOH DA 8 .   ? 13.735  221.382 10.447 1.00 32.96 ?  375 HOH D O   1 
HETATM 11519 O  O   . HOH DA 8 .   ? 15.154  217.336 22.255 1.00 45.86 ?  376 HOH D O   1 
HETATM 11520 O  O   . HOH DA 8 .   ? -5.911  215.504 12.188 1.00 44.05 ?  377 HOH D O   1 
HETATM 11521 O  O   . HOH DA 8 .   ? -7.144  206.471 31.461 1.00 53.93 ?  378 HOH D O   1 
HETATM 11522 O  O   . HOH DA 8 .   ? -7.785  213.045 18.599 1.00 32.16 ?  379 HOH D O   1 
HETATM 11523 O  O   . HOH DA 8 .   ? 4.795   202.237 9.681  1.00 44.83 ?  380 HOH D O   1 
HETATM 11524 O  O   . HOH DA 8 .   ? 18.334  217.874 19.351 1.00 51.16 ?  381 HOH D O   1 
HETATM 11525 O  O   . HOH DA 8 .   ? 13.895  217.918 -1.475 1.00 47.30 ?  382 HOH D O   1 
HETATM 11526 O  O   . HOH DA 8 .   ? 7.541   222.223 0.236  1.00 31.65 ?  383 HOH D O   1 
HETATM 11527 O  O   . HOH DA 8 .   ? -6.771  223.188 24.907 1.00 39.23 ?  384 HOH D O   1 
HETATM 11528 O  O   . HOH DA 8 .   ? -3.241  233.199 22.298 1.00 43.27 ?  385 HOH D O   1 
HETATM 11529 O  O   . HOH DA 8 .   ? 1.591   218.108 3.635  1.00 32.57 ?  386 HOH D O   1 
HETATM 11530 O  O   . HOH DA 8 .   ? 17.838  202.016 27.715 1.00 55.89 ?  387 HOH D O   1 
HETATM 11531 O  O   . HOH DA 8 .   ? -4.988  214.407 2.550  1.00 55.22 ?  388 HOH D O   1 
HETATM 11532 O  O   . HOH DA 8 .   ? 4.002   209.705 3.089  1.00 33.13 ?  389 HOH D O   1 
HETATM 11533 O  O   . HOH DA 8 .   ? -1.108  218.663 30.736 1.00 42.25 ?  390 HOH D O   1 
HETATM 11534 O  O   . HOH DA 8 .   ? 20.087  220.608 0.564  1.00 55.98 ?  391 HOH D O   1 
HETATM 11535 O  O   . HOH DA 8 .   ? 15.317  201.907 27.231 1.00 41.56 ?  392 HOH D O   1 
HETATM 11536 O  O   . HOH DA 8 .   ? 11.270  228.406 0.497  1.00 56.64 ?  393 HOH D O   1 
HETATM 11537 O  O   . HOH DA 8 .   ? -10.902 210.020 26.072 1.00 57.10 ?  394 HOH D O   1 
HETATM 11538 O  O   . HOH DA 8 .   ? -5.211  202.604 25.505 1.00 40.01 ?  395 HOH D O   1 
HETATM 11539 O  O   . HOH DA 8 .   ? 10.507  226.237 7.092  1.00 40.15 ?  396 HOH D O   1 
HETATM 11540 O  O   . HOH DA 8 .   ? -5.571  225.663 23.384 1.00 38.99 ?  397 HOH D O   1 
HETATM 11541 O  O   . HOH DA 8 .   ? -6.309  205.856 26.715 1.00 44.93 ?  398 HOH D O   1 
HETATM 11542 O  O   . HOH DA 8 .   ? 9.850   221.374 22.938 1.00 41.74 ?  399 HOH D O   1 
HETATM 11543 O  O   . HOH DA 8 .   ? 3.241   201.221 27.493 1.00 40.60 ?  400 HOH D O   1 
HETATM 11544 O  O   . HOH DA 8 .   ? -0.091  197.776 7.194  1.00 49.02 ?  401 HOH D O   1 
HETATM 11545 O  O   . HOH DA 8 .   ? -2.296  226.405 30.143 1.00 48.89 ?  402 HOH D O   1 
HETATM 11546 O  O   . HOH DA 8 .   ? 18.281  208.910 14.392 1.00 50.94 ?  403 HOH D O   1 
HETATM 11547 O  O   . HOH DA 8 .   ? -0.928  223.838 7.260  1.00 44.55 ?  404 HOH D O   1 
HETATM 11548 O  O   . HOH DA 8 .   ? 3.125   226.257 8.053  1.00 33.53 ?  405 HOH D O   1 
HETATM 11549 O  O   . HOH DA 8 .   ? 3.925   200.882 11.757 1.00 47.84 ?  406 HOH D O   1 
HETATM 11550 O  O   . HOH DA 8 .   ? 17.854  215.786 13.361 1.00 44.30 ?  407 HOH D O   1 
HETATM 11551 O  O   . HOH DA 8 .   ? 1.965   224.866 22.956 1.00 29.09 ?  408 HOH D O   1 
HETATM 11552 O  O   . HOH DA 8 .   ? -4.471  225.219 29.342 1.00 37.92 ?  409 HOH D O   1 
HETATM 11553 O  O   . HOH DA 8 .   ? -7.563  211.702 6.785  1.00 56.82 ?  410 HOH D O   1 
HETATM 11554 O  O   . HOH DA 8 .   ? -0.664  204.706 6.398  1.00 46.18 ?  411 HOH D O   1 
HETATM 11555 O  O   . HOH DA 8 .   ? 4.133   203.373 -1.398 1.00 49.04 ?  412 HOH D O   1 
HETATM 11556 O  O   . HOH DA 8 .   ? -21.745 219.799 13.583 1.00 51.69 ?  413 HOH D O   1 
HETATM 11557 O  O   . HOH DA 8 .   ? -9.040  208.232 15.052 1.00 36.08 ?  414 HOH D O   1 
HETATM 11558 O  O   . HOH DA 8 .   ? -2.694  212.001 2.585  1.00 50.20 ?  415 HOH D O   1 
HETATM 11559 O  O   . HOH DA 8 .   ? -19.877 219.226 12.202 1.00 61.70 ?  416 HOH D O   1 
HETATM 11560 O  O   . HOH DA 8 .   ? -8.187  226.863 23.413 1.00 40.39 ?  417 HOH D O   1 
HETATM 11561 O  O   . HOH DA 8 .   ? 1.162   202.103 13.494 1.00 37.75 ?  418 HOH D O   1 
HETATM 11562 O  O   . HOH DA 8 .   ? 5.404   201.351 32.285 1.00 56.23 ?  419 HOH D O   1 
HETATM 11563 O  O   . HOH DA 8 .   ? 6.844   208.639 -2.577 1.00 42.13 ?  420 HOH D O   1 
HETATM 11564 O  O   . HOH DA 8 .   ? 1.677   203.151 7.583  1.00 51.23 ?  421 HOH D O   1 
HETATM 11565 O  O   . HOH DA 8 .   ? -9.057  208.504 23.558 1.00 45.04 ?  422 HOH D O   1 
HETATM 11566 O  O   . HOH DA 8 .   ? -10.841 206.495 23.123 1.00 58.86 ?  423 HOH D O   1 
HETATM 11567 O  O   . HOH DA 8 .   ? -12.148 213.809 25.704 1.00 56.51 ?  424 HOH D O   1 
HETATM 11568 O  O   . HOH DA 8 .   ? -13.824 220.699 10.355 1.00 34.72 ?  425 HOH D O   1 
HETATM 11569 O  O   . HOH DA 8 .   ? -14.690 211.150 28.798 1.00 55.79 ?  426 HOH D O   1 
HETATM 11570 O  O   . HOH DA 8 .   ? -1.805  216.317 31.029 1.00 42.40 ?  427 HOH D O   1 
HETATM 11571 O  O   A HOH DA 8 .   ? -9.660  210.768 22.772 0.50 34.01 ?  428 HOH D O   1 
HETATM 11572 O  O   B HOH DA 8 .   ? -8.086  211.787 21.797 0.50 25.92 ?  428 HOH D O   1 
HETATM 11573 O  O   . HOH DA 8 .   ? 2.339   211.127 2.236  1.00 50.26 ?  429 HOH D O   1 
HETATM 11574 O  O   . HOH DA 8 .   ? -8.874  201.295 11.566 1.00 48.22 ?  430 HOH D O   1 
HETATM 11575 O  O   . HOH DA 8 .   ? -4.673  204.514 28.882 1.00 48.64 ?  431 HOH D O   1 
HETATM 11576 O  O   . HOH DA 8 .   ? -9.920  213.190 20.426 1.00 43.63 ?  432 HOH D O   1 
HETATM 11577 O  O   . HOH DA 8 .   ? -8.385  199.024 12.069 1.00 55.74 ?  433 HOH D O   1 
HETATM 11578 O  O   . HOH DA 8 .   ? 1.949   227.384 16.448 1.00 44.57 ?  434 HOH D O   1 
HETATM 11579 O  O   . HOH DA 8 .   ? -4.869  205.863 32.409 1.00 50.46 ?  435 HOH D O   1 
HETATM 11580 O  O   . HOH DA 8 .   ? 20.909  215.405 16.880 1.00 54.27 ?  436 HOH D O   1 
HETATM 11581 O  O   . HOH DA 8 .   ? -11.158 228.929 20.917 1.00 30.22 ?  437 HOH D O   1 
HETATM 11582 O  O   . HOH DA 8 .   ? -0.156  210.202 2.063  1.00 49.76 ?  438 HOH D O   1 
HETATM 11583 O  O   . HOH DA 8 .   ? -8.965  195.403 15.095 1.00 58.56 ?  439 HOH D O   1 
HETATM 11584 O  O   . HOH DA 8 .   ? -7.161  231.026 21.143 1.00 31.32 ?  440 HOH D O   1 
HETATM 11585 O  O   . HOH DA 8 .   ? 3.896   224.643 21.177 1.00 30.23 ?  441 HOH D O   1 
HETATM 11586 O  O   . HOH DA 8 .   ? -8.950  229.378 22.532 1.00 34.71 ?  442 HOH D O   1 
HETATM 11587 O  O   . HOH DA 8 .   ? -10.566 206.217 28.460 1.00 64.26 ?  443 HOH D O   1 
HETATM 11588 O  O   . HOH DA 8 .   ? -2.432  221.159 -0.698 1.00 56.73 ?  444 HOH D O   1 
HETATM 11589 O  O   . HOH DA 8 .   ? 4.251   230.103 6.114  1.00 60.31 ?  445 HOH D O   1 
HETATM 11590 O  O   . HOH EA 8 .   ? 53.156  244.183 37.024 1.00 60.23 ?  301 HOH E O   1 
HETATM 11591 O  O   . HOH EA 8 .   ? 56.986  251.499 45.967 1.00 64.02 ?  302 HOH E O   1 
HETATM 11592 O  O   . HOH EA 8 .   ? 19.000  255.040 50.035 1.00 53.26 ?  303 HOH E O   1 
HETATM 11593 O  O   . HOH EA 8 .   ? 47.832  254.488 54.648 1.00 47.92 ?  304 HOH E O   1 
HETATM 11594 O  O   . HOH EA 8 .   ? 54.779  250.017 69.202 1.00 51.38 ?  305 HOH E O   1 
HETATM 11595 O  O   . HOH EA 8 .   ? 42.775  232.319 46.125 1.00 47.91 ?  306 HOH E O   1 
HETATM 11596 O  O   . HOH EA 8 .   ? 41.673  236.884 37.175 1.00 53.79 ?  307 HOH E O   1 
HETATM 11597 O  O   . HOH EA 8 .   ? 46.330  256.594 75.375 1.00 64.21 ?  308 HOH E O   1 
HETATM 11598 O  O   . HOH EA 8 .   ? 32.210  252.122 41.568 1.00 35.95 ?  309 HOH E O   1 
HETATM 11599 O  O   . HOH EA 8 .   ? 33.816  252.169 34.452 1.00 32.13 ?  310 HOH E O   1 
HETATM 11600 O  O   . HOH EA 8 .   ? 39.097  248.985 71.364 1.00 45.61 ?  311 HOH E O   1 
HETATM 11601 O  O   . HOH EA 8 .   ? 43.640  232.653 55.188 1.00 53.63 ?  312 HOH E O   1 
HETATM 11602 O  O   . HOH EA 8 .   ? 39.832  253.190 40.990 1.00 39.80 ?  313 HOH E O   1 
HETATM 11603 O  O   . HOH EA 8 .   ? 30.771  254.642 54.273 1.00 45.02 ?  314 HOH E O   1 
HETATM 11604 O  O   . HOH EA 8 .   ? 57.953  246.164 46.184 1.00 59.46 ?  315 HOH E O   1 
HETATM 11605 O  O   . HOH EA 8 .   ? 40.430  233.350 63.397 1.00 48.85 ?  316 HOH E O   1 
HETATM 11606 O  O   . HOH EA 8 .   ? 31.534  245.329 57.611 1.00 30.96 ?  317 HOH E O   1 
HETATM 11607 O  O   . HOH EA 8 .   ? 37.618  243.845 68.062 1.00 42.20 ?  318 HOH E O   1 
HETATM 11608 O  O   . HOH EA 8 .   ? 46.190  241.623 41.620 1.00 42.43 ?  319 HOH E O   1 
HETATM 11609 O  O   . HOH EA 8 .   ? 24.616  253.003 54.656 1.00 39.16 ?  320 HOH E O   1 
HETATM 11610 O  O   . HOH EA 8 .   ? 49.981  251.611 41.844 1.00 56.80 ?  321 HOH E O   1 
HETATM 11611 O  O   . HOH EA 8 .   ? 36.150  237.914 57.215 1.00 41.34 ?  322 HOH E O   1 
HETATM 11612 O  O   . HOH EA 8 .   ? 46.261  245.588 69.213 1.00 37.19 ?  323 HOH E O   1 
HETATM 11613 O  O   . HOH EA 8 .   ? 48.250  251.091 72.025 1.00 43.06 ?  324 HOH E O   1 
HETATM 11614 O  O   . HOH EA 8 .   ? 30.347  255.341 58.388 1.00 39.88 ?  325 HOH E O   1 
HETATM 11615 O  O   . HOH EA 8 .   ? 45.141  235.954 36.820 1.00 54.19 ?  326 HOH E O   1 
HETATM 11616 O  O   . HOH EA 8 .   ? 35.412  231.127 51.578 1.00 36.17 ?  327 HOH E O   1 
HETATM 11617 O  O   . HOH EA 8 .   ? 32.585  243.363 61.428 1.00 41.16 ?  328 HOH E O   1 
HETATM 11618 O  O   . HOH EA 8 .   ? 31.491  236.144 55.954 1.00 28.56 ?  329 HOH E O   1 
HETATM 11619 O  O   . HOH EA 8 .   ? 50.620  247.111 50.454 1.00 49.62 ?  330 HOH E O   1 
HETATM 11620 O  O   . HOH EA 8 .   ? 33.078  228.942 54.423 1.00 42.26 ?  331 HOH E O   1 
HETATM 11621 O  O   . HOH EA 8 .   ? 46.243  259.685 57.899 1.00 51.60 ?  332 HOH E O   1 
HETATM 11622 O  O   . HOH EA 8 .   ? 35.783  241.663 42.247 1.00 46.13 ?  333 HOH E O   1 
HETATM 11623 O  O   . HOH EA 8 .   ? 42.086  242.591 67.910 1.00 38.58 ?  334 HOH E O   1 
HETATM 11624 O  O   . HOH EA 8 .   ? 34.217  245.903 68.923 1.00 65.15 ?  335 HOH E O   1 
HETATM 11625 O  O   . HOH EA 8 .   ? 31.496  254.907 40.863 1.00 35.77 ?  336 HOH E O   1 
HETATM 11626 O  O   . HOH EA 8 .   ? 33.610  227.807 56.965 1.00 38.65 ?  337 HOH E O   1 
HETATM 11627 O  O   . HOH EA 8 .   ? 47.151  255.849 59.005 1.00 45.38 ?  338 HOH E O   1 
HETATM 11628 O  O   . HOH EA 8 .   ? 43.452  236.632 45.063 1.00 48.41 ?  339 HOH E O   1 
HETATM 11629 O  O   . HOH EA 8 .   ? 51.726  253.730 72.940 1.00 50.99 ?  340 HOH E O   1 
HETATM 11630 O  O   . HOH EA 8 .   ? 30.752  256.580 36.967 1.00 39.89 ?  341 HOH E O   1 
HETATM 11631 O  O   . HOH EA 8 .   ? 31.828  232.033 62.981 1.00 46.27 ?  342 HOH E O   1 
HETATM 11632 O  O   . HOH EA 8 .   ? 53.941  256.837 59.916 1.00 55.08 ?  343 HOH E O   1 
HETATM 11633 O  O   . HOH EA 8 .   ? 37.439  235.677 44.440 1.00 43.02 ?  344 HOH E O   1 
HETATM 11634 O  O   . HOH EA 8 .   ? 56.095  246.442 62.502 1.00 51.16 ?  345 HOH E O   1 
HETATM 11635 O  O   . HOH EA 8 .   ? 40.629  255.632 34.415 1.00 45.66 ?  346 HOH E O   1 
HETATM 11636 O  O   . HOH EA 8 .   ? 47.331  243.459 40.330 1.00 48.06 ?  347 HOH E O   1 
HETATM 11637 O  O   . HOH EA 8 .   ? 36.112  258.210 41.539 1.00 33.39 ?  348 HOH E O   1 
HETATM 11638 O  O   . HOH EA 8 .   ? 48.640  237.187 50.208 1.00 45.42 ?  349 HOH E O   1 
HETATM 11639 O  O   . HOH EA 8 .   ? 30.438  245.356 39.414 1.00 49.14 ?  350 HOH E O   1 
HETATM 11640 O  O   . HOH EA 8 .   ? 51.382  259.841 68.671 1.00 46.83 ?  351 HOH E O   1 
HETATM 11641 O  O   . HOH EA 8 .   ? 46.068  235.835 62.099 1.00 44.50 ?  352 HOH E O   1 
HETATM 11642 O  O   . HOH EA 8 .   ? 28.336  259.690 41.154 1.00 52.42 ?  353 HOH E O   1 
HETATM 11643 O  O   . HOH EA 8 .   ? 50.555  244.938 66.893 1.00 50.73 ?  354 HOH E O   1 
HETATM 11644 O  O   . HOH EA 8 .   ? 53.830  252.149 47.768 1.00 56.93 ?  355 HOH E O   1 
HETATM 11645 O  O   . HOH EA 8 .   ? 35.387  259.520 45.007 1.00 45.43 ?  356 HOH E O   1 
HETATM 11646 O  O   . HOH EA 8 .   ? 48.350  246.086 67.558 1.00 40.60 ?  357 HOH E O   1 
HETATM 11647 O  O   . HOH EA 8 .   ? 51.985  236.794 45.893 1.00 52.75 ?  358 HOH E O   1 
HETATM 11648 O  O   . HOH EA 8 .   ? 36.679  259.744 34.609 1.00 51.25 ?  359 HOH E O   1 
HETATM 11649 O  O   . HOH EA 8 .   ? 47.487  258.695 55.240 1.00 53.49 ?  360 HOH E O   1 
HETATM 11650 O  O   . HOH EA 8 .   ? 39.502  236.988 63.735 1.00 47.68 ?  361 HOH E O   1 
HETATM 11651 O  O   . HOH EA 8 .   ? 53.591  237.959 57.441 1.00 54.26 ?  362 HOH E O   1 
HETATM 11652 O  O   . HOH EA 8 .   ? 33.562  256.734 60.179 1.00 50.51 ?  363 HOH E O   1 
HETATM 11653 O  O   . HOH EA 8 .   ? 42.864  252.965 71.232 1.00 47.00 ?  364 HOH E O   1 
HETATM 11654 O  O   . HOH EA 8 .   ? 56.202  250.825 63.225 1.00 48.09 ?  365 HOH E O   1 
HETATM 11655 O  O   . HOH EA 8 .   ? 26.810  252.840 46.951 1.00 40.19 ?  366 HOH E O   1 
HETATM 11656 O  O   . HOH EA 8 .   ? 31.767  242.321 58.676 1.00 39.46 ?  367 HOH E O   1 
HETATM 11657 O  O   . HOH EA 8 .   ? 51.219  251.252 71.988 1.00 39.53 ?  368 HOH E O   1 
HETATM 11658 O  O   . HOH EA 8 .   ? 46.182  256.329 55.992 1.00 41.06 ?  369 HOH E O   1 
HETATM 11659 O  O   . HOH EA 8 .   ? 32.367  242.111 41.063 1.00 56.97 ?  370 HOH E O   1 
HETATM 11660 O  O   . HOH EA 8 .   ? 35.988  236.385 42.521 1.00 56.12 ?  371 HOH E O   1 
HETATM 11661 O  O   . HOH EA 8 .   ? 35.728  239.418 62.536 1.00 51.97 ?  372 HOH E O   1 
HETATM 11662 O  O   . HOH EA 8 .   ? 53.309  256.515 65.127 1.00 59.42 ?  373 HOH E O   1 
HETATM 11663 O  O   . HOH EA 8 .   ? 38.275  254.479 66.159 1.00 52.28 ?  374 HOH E O   1 
HETATM 11664 O  O   . HOH EA 8 .   ? 17.054  253.676 52.677 1.00 51.40 ?  375 HOH E O   1 
HETATM 11665 O  O   . HOH EA 8 .   ? 41.630  256.746 37.878 1.00 51.52 ?  376 HOH E O   1 
HETATM 11666 O  O   . HOH EA 8 .   ? 39.747  261.876 54.162 1.00 47.92 ?  377 HOH E O   1 
HETATM 11667 O  O   . HOH EA 8 .   ? 29.359  256.030 39.496 1.00 48.83 ?  378 HOH E O   1 
HETATM 11668 O  O   . HOH EA 8 .   ? 45.467  232.653 53.489 1.00 39.00 ?  379 HOH E O   1 
HETATM 11669 O  O   . HOH EA 8 .   ? 38.672  237.362 41.583 1.00 52.18 ?  380 HOH E O   1 
HETATM 11670 O  O   . HOH EA 8 .   ? 45.789  232.860 58.410 1.00 48.94 ?  381 HOH E O   1 
HETATM 11671 O  O   . HOH EA 8 .   ? 45.543  233.456 45.426 1.00 57.91 ?  382 HOH E O   1 
HETATM 11672 O  O   . HOH EA 8 .   ? 44.928  242.681 69.277 1.00 49.43 ?  383 HOH E O   1 
HETATM 11673 O  O   . HOH EA 8 .   ? 46.210  231.118 51.323 1.00 52.10 ?  384 HOH E O   1 
HETATM 11674 O  O   . HOH EA 8 .   ? 44.772  240.127 68.420 1.00 59.21 ?  385 HOH E O   1 
HETATM 11675 O  O   . HOH FA 8 .   ? 2.736   236.073 49.690 1.00 38.90 ?  301 HOH F O   1 
HETATM 11676 O  O   . HOH FA 8 .   ? 9.675   239.015 70.711 1.00 53.78 ?  302 HOH F O   1 
HETATM 11677 O  O   . HOH FA 8 .   ? 9.221   234.742 66.473 1.00 52.96 ?  303 HOH F O   1 
HETATM 11678 O  O   . HOH FA 8 .   ? 4.313   247.735 43.100 1.00 47.75 ?  304 HOH F O   1 
HETATM 11679 O  O   . HOH FA 8 .   ? 8.900   235.843 42.142 1.00 48.68 ?  305 HOH F O   1 
HETATM 11680 O  O   . HOH FA 8 .   ? 12.572  230.873 46.929 1.00 44.23 ?  306 HOH F O   1 
HETATM 11681 O  O   . HOH FA 8 .   ? 24.708  224.037 43.984 1.00 66.89 ?  307 HOH F O   1 
HETATM 11682 O  O   . HOH FA 8 .   ? 24.576  236.999 68.140 1.00 40.83 ?  308 HOH F O   1 
HETATM 11683 O  O   . HOH FA 8 .   ? 19.434  226.946 69.783 1.00 34.27 ?  309 HOH F O   1 
HETATM 11684 O  O   . HOH FA 8 .   ? 12.566  231.901 42.947 1.00 43.11 ?  310 HOH F O   1 
HETATM 11685 O  O   . HOH FA 8 .   ? 12.764  225.094 52.607 1.00 36.58 ?  311 HOH F O   1 
HETATM 11686 O  O   . HOH FA 8 .   ? 7.819   233.251 65.323 1.00 40.24 ?  312 HOH F O   1 
HETATM 11687 O  O   . HOH FA 8 .   ? 33.791  229.953 44.195 1.00 55.52 ?  313 HOH F O   1 
HETATM 11688 O  O   . HOH FA 8 .   ? 14.748  228.590 71.596 1.00 39.29 ?  314 HOH F O   1 
HETATM 11689 O  O   . HOH FA 8 .   ? 18.253  228.641 31.630 1.00 59.06 ?  315 HOH F O   1 
HETATM 11690 O  O   . HOH FA 8 .   ? 18.228  220.812 66.564 1.00 42.44 ?  316 HOH F O   1 
HETATM 11691 O  O   . HOH FA 8 .   ? 23.207  244.772 43.529 1.00 41.96 ?  317 HOH F O   1 
HETATM 11692 O  O   . HOH FA 8 .   ? 19.647  220.670 63.788 1.00 46.43 ?  318 HOH F O   1 
HETATM 11693 O  O   . HOH FA 8 .   ? 9.210   244.300 67.204 1.00 55.15 ?  319 HOH F O   1 
HETATM 11694 O  O   . HOH FA 8 .   ? 16.216  221.784 62.797 1.00 34.79 ?  320 HOH F O   1 
HETATM 11695 O  O   . HOH FA 8 .   ? 9.606   237.507 52.372 1.00 23.22 ?  321 HOH F O   1 
HETATM 11696 O  O   . HOH FA 8 .   ? -4.699  238.814 53.511 1.00 37.14 ?  322 HOH F O   1 
HETATM 11697 O  O   . HOH FA 8 .   ? 6.537   248.539 41.210 1.00 50.60 ?  323 HOH F O   1 
HETATM 11698 O  O   . HOH FA 8 .   ? 11.377  242.680 57.883 1.00 32.03 ?  324 HOH F O   1 
HETATM 11699 O  O   . HOH FA 8 .   ? 8.893   232.184 67.671 1.00 40.65 ?  325 HOH F O   1 
HETATM 11700 O  O   . HOH FA 8 .   ? 16.228  234.478 70.234 1.00 39.23 ?  326 HOH F O   1 
HETATM 11701 O  O   . HOH FA 8 .   ? 29.576  237.700 57.015 1.00 28.89 ?  327 HOH F O   1 
HETATM 11702 O  O   . HOH FA 8 .   ? 24.814  254.045 58.390 1.00 38.62 ?  328 HOH F O   1 
HETATM 11703 O  O   . HOH FA 8 .   ? 11.683  242.764 42.991 1.00 32.20 ?  329 HOH F O   1 
HETATM 11704 O  O   . HOH FA 8 .   ? 0.450   240.129 59.920 1.00 27.64 ?  330 HOH F O   1 
HETATM 11705 O  O   . HOH FA 8 .   ? 29.461  247.167 57.520 1.00 32.75 ?  331 HOH F O   1 
HETATM 11706 O  O   . HOH FA 8 .   ? 9.529   238.727 41.503 1.00 47.22 ?  332 HOH F O   1 
HETATM 11707 O  O   . HOH FA 8 .   ? 22.248  252.739 56.213 1.00 39.72 ?  333 HOH F O   1 
HETATM 11708 O  O   . HOH FA 8 .   ? 30.854  225.657 51.199 1.00 46.30 ?  334 HOH F O   1 
HETATM 11709 O  O   . HOH FA 8 .   ? 29.769  229.219 51.504 1.00 45.90 ?  335 HOH F O   1 
HETATM 11710 O  O   . HOH FA 8 .   ? 12.925  244.647 44.161 1.00 31.38 ?  336 HOH F O   1 
HETATM 11711 O  O   . HOH FA 8 .   ? 3.228   240.853 47.377 1.00 41.14 ?  337 HOH F O   1 
HETATM 11712 O  O   . HOH FA 8 .   ? 4.071   238.401 61.945 1.00 40.20 ?  338 HOH F O   1 
HETATM 11713 O  O   . HOH FA 8 .   ? -1.519  242.813 52.809 1.00 24.54 ?  339 HOH F O   1 
HETATM 11714 O  O   . HOH FA 8 .   ? 7.360   226.055 59.621 1.00 29.20 ?  340 HOH F O   1 
HETATM 11715 O  O   . HOH FA 8 .   ? 11.449  230.856 53.012 1.00 29.12 ?  341 HOH F O   1 
HETATM 11716 O  O   . HOH FA 8 .   ? 32.791  234.653 63.312 1.00 50.10 ?  342 HOH F O   1 
HETATM 11717 O  O   . HOH FA 8 .   ? 20.677  223.421 56.209 1.00 36.09 ?  343 HOH F O   1 
HETATM 11718 O  O   . HOH FA 8 .   ? 11.312  220.795 66.843 1.00 38.91 ?  344 HOH F O   1 
HETATM 11719 O  O   . HOH FA 8 .   ? 2.661   238.592 42.993 1.00 45.91 ?  345 HOH F O   1 
HETATM 11720 O  O   . HOH FA 8 .   ? 12.470  248.035 50.522 1.00 44.06 ?  346 HOH F O   1 
HETATM 11721 O  O   . HOH FA 8 .   ? 30.693  227.747 55.398 1.00 46.30 ?  347 HOH F O   1 
HETATM 11722 O  O   . HOH FA 8 .   ? 17.226  250.321 41.182 1.00 54.03 ?  348 HOH F O   1 
HETATM 11723 O  O   . HOH FA 8 .   ? 10.791  244.095 60.233 1.00 45.19 ?  349 HOH F O   1 
HETATM 11724 O  O   . HOH FA 8 .   ? 16.833  248.669 47.632 1.00 35.24 ?  350 HOH F O   1 
HETATM 11725 O  O   . HOH FA 8 .   ? 19.174  234.249 40.017 1.00 45.11 ?  351 HOH F O   1 
HETATM 11726 O  O   . HOH FA 8 .   ? 21.003  239.998 38.784 1.00 34.35 ?  352 HOH F O   1 
HETATM 11727 O  O   . HOH FA 8 .   ? 12.147  227.267 45.782 1.00 48.62 ?  353 HOH F O   1 
HETATM 11728 O  O   . HOH FA 8 .   ? 2.494   232.967 46.992 1.00 55.11 ?  354 HOH F O   1 
HETATM 11729 O  O   . HOH FA 8 .   ? 1.017   234.956 55.603 1.00 35.59 ?  355 HOH F O   1 
HETATM 11730 O  O   . HOH FA 8 .   ? 28.969  239.219 61.177 1.00 44.54 ?  356 HOH F O   1 
HETATM 11731 O  O   . HOH FA 8 .   ? 7.894   222.411 71.150 1.00 56.47 ?  357 HOH F O   1 
HETATM 11732 O  O   . HOH FA 8 .   ? 20.439  237.844 68.873 1.00 30.25 ?  358 HOH F O   1 
HETATM 11733 O  O   . HOH FA 8 .   ? 7.830   244.692 61.165 1.00 35.50 ?  359 HOH F O   1 
HETATM 11734 O  O   . HOH FA 8 .   ? 12.905  250.942 40.891 1.00 54.57 ?  360 HOH F O   1 
HETATM 11735 O  O   . HOH FA 8 .   ? 15.135  223.900 61.235 1.00 31.36 ?  361 HOH F O   1 
HETATM 11736 O  O   . HOH FA 8 .   ? 21.704  236.730 37.327 1.00 51.44 ?  362 HOH F O   1 
HETATM 11737 O  O   . HOH FA 8 .   ? 2.033   229.964 48.588 1.00 51.98 ?  363 HOH F O   1 
HETATM 11738 O  O   . HOH FA 8 .   ? 26.916  241.440 62.241 1.00 41.67 ?  364 HOH F O   1 
HETATM 11739 O  O   . HOH FA 8 .   ? 17.315  233.082 38.259 1.00 52.38 ?  365 HOH F O   1 
HETATM 11740 O  O   . HOH FA 8 .   ? 5.802   235.263 64.797 1.00 40.71 ?  366 HOH F O   1 
HETATM 11741 O  O   . HOH FA 8 .   ? 16.515  250.384 60.058 1.00 48.28 ?  367 HOH F O   1 
HETATM 11742 O  O   . HOH FA 8 .   ? 7.784   248.157 50.131 1.00 34.92 ?  368 HOH F O   1 
HETATM 11743 O  O   . HOH FA 8 .   ? 11.743  228.347 71.672 1.00 40.16 ?  369 HOH F O   1 
HETATM 11744 O  O   . HOH FA 8 .   ? 21.932  250.162 46.953 1.00 40.47 ?  370 HOH F O   1 
HETATM 11745 O  O   . HOH FA 8 .   ? 28.188  254.390 56.853 1.00 51.94 ?  371 HOH F O   1 
HETATM 11746 O  O   . HOH FA 8 .   ? 2.288   243.553 50.429 1.00 45.23 ?  372 HOH F O   1 
HETATM 11747 O  O   . HOH FA 8 .   ? 13.936  228.862 42.582 1.00 48.09 ?  373 HOH F O   1 
HETATM 11748 O  O   . HOH FA 8 .   ? 11.640  246.950 53.925 1.00 30.82 ?  374 HOH F O   1 
HETATM 11749 O  O   . HOH FA 8 .   ? 22.379  228.297 39.588 1.00 41.01 ?  375 HOH F O   1 
HETATM 11750 O  O   . HOH FA 8 .   ? 22.836  244.579 65.727 1.00 48.34 ?  376 HOH F O   1 
HETATM 11751 O  O   . HOH FA 8 .   ? 14.321  234.412 68.505 1.00 29.79 ?  377 HOH F O   1 
HETATM 11752 O  O   . HOH FA 8 .   ? 26.948  243.863 44.832 1.00 48.07 ?  378 HOH F O   1 
HETATM 11753 O  O   . HOH FA 8 .   ? 5.775   230.309 64.134 1.00 37.03 ?  379 HOH F O   1 
HETATM 11754 O  O   . HOH FA 8 .   ? 17.593  237.181 39.316 1.00 43.62 ?  380 HOH F O   1 
HETATM 11755 O  O   . HOH FA 8 .   ? -3.331  233.008 49.784 1.00 46.74 ?  381 HOH F O   1 
HETATM 11756 O  O   . HOH FA 8 .   ? 17.973  247.945 36.394 1.00 54.49 ?  382 HOH F O   1 
HETATM 11757 O  O   . HOH FA 8 .   ? 16.916  223.061 73.409 1.00 45.55 ?  383 HOH F O   1 
HETATM 11758 O  O   . HOH FA 8 .   ? 4.538   246.118 40.348 1.00 55.71 ?  384 HOH F O   1 
HETATM 11759 O  O   . HOH FA 8 .   ? 29.482  240.686 58.600 1.00 39.37 ?  385 HOH F O   1 
HETATM 11760 O  O   . HOH FA 8 .   ? 15.009  219.002 64.816 1.00 51.29 ?  386 HOH F O   1 
HETATM 11761 O  O   . HOH FA 8 .   ? 25.957  226.597 58.837 1.00 36.39 ?  387 HOH F O   1 
HETATM 11762 O  O   . HOH FA 8 .   ? 12.115  235.919 68.645 1.00 32.20 ?  388 HOH F O   1 
HETATM 11763 O  O   . HOH FA 8 .   ? 6.090   232.959 49.300 1.00 30.12 ?  389 HOH F O   1 
HETATM 11764 O  O   . HOH FA 8 .   ? 32.617  232.534 44.507 1.00 43.86 ?  390 HOH F O   1 
HETATM 11765 O  O   . HOH FA 8 .   ? 3.280   234.049 58.491 1.00 48.48 ?  391 HOH F O   1 
HETATM 11766 O  O   . HOH FA 8 .   ? 15.640  245.903 65.169 1.00 36.35 ?  392 HOH F O   1 
HETATM 11767 O  O   . HOH FA 8 .   ? 15.565  223.444 49.400 1.00 48.70 ?  393 HOH F O   1 
HETATM 11768 O  O   . HOH FA 8 .   ? 39.568  226.707 46.328 1.00 44.44 ?  394 HOH F O   1 
HETATM 11769 O  O   . HOH FA 8 .   ? 18.451  249.422 45.579 1.00 47.41 ?  395 HOH F O   1 
HETATM 11770 O  O   . HOH FA 8 .   ? 25.452  243.179 64.295 1.00 48.54 ?  396 HOH F O   1 
HETATM 11771 O  O   . HOH FA 8 .   ? 1.629   238.929 49.027 1.00 43.65 ?  397 HOH F O   1 
HETATM 11772 O  O   . HOH FA 8 .   ? 0.883   249.066 59.673 1.00 39.17 ?  398 HOH F O   1 
HETATM 11773 O  O   . HOH FA 8 .   ? 1.366   245.210 63.075 1.00 48.42 ?  399 HOH F O   1 
HETATM 11774 O  O   . HOH FA 8 .   ? 22.605  249.488 44.776 1.00 53.90 ?  400 HOH F O   1 
HETATM 11775 O  O   . HOH FA 8 .   ? 21.921  223.051 58.364 1.00 43.31 ?  401 HOH F O   1 
HETATM 11776 O  O   . HOH FA 8 .   ? 12.749  227.774 48.735 1.00 33.60 ?  402 HOH F O   1 
HETATM 11777 O  O   . HOH FA 8 .   ? 30.597  227.239 40.423 1.00 58.07 ?  403 HOH F O   1 
HETATM 11778 O  O   . HOH FA 8 .   ? 10.873  225.565 72.514 1.00 46.54 ?  404 HOH F O   1 
HETATM 11779 O  O   . HOH FA 8 .   ? 20.626  247.249 42.522 1.00 48.31 ?  405 HOH F O   1 
HETATM 11780 O  O   . HOH FA 8 .   ? -0.700  240.725 48.936 1.00 45.87 ?  406 HOH F O   1 
HETATM 11781 O  O   . HOH FA 8 .   ? 26.344  248.454 67.163 1.00 55.18 ?  407 HOH F O   1 
HETATM 11782 O  O   . HOH FA 8 .   ? 42.949  230.903 48.439 1.00 42.24 ?  408 HOH F O   1 
HETATM 11783 O  O   . HOH FA 8 .   ? 12.365  243.080 70.364 1.00 57.88 ?  409 HOH F O   1 
HETATM 11784 O  O   . HOH FA 8 .   ? 15.318  250.522 57.549 1.00 38.48 ?  410 HOH F O   1 
HETATM 11785 O  O   . HOH FA 8 .   ? 22.682  226.536 42.738 1.00 47.63 ?  411 HOH F O   1 
HETATM 11786 O  O   . HOH FA 8 .   ? 3.157   236.848 60.472 1.00 52.30 ?  412 HOH F O   1 
HETATM 11787 O  O   . HOH FA 8 .   ? 1.405   248.404 62.035 1.00 42.23 ?  413 HOH F O   1 
HETATM 11788 O  O   . HOH FA 8 .   ? 12.807  246.905 56.151 1.00 39.74 ?  414 HOH F O   1 
HETATM 11789 O  O   . HOH FA 8 .   ? 13.035  249.242 57.275 1.00 49.53 ?  415 HOH F O   1 
HETATM 11790 O  O   . HOH FA 8 .   ? 28.064  229.740 64.125 1.00 58.84 ?  416 HOH F O   1 
HETATM 11791 O  O   . HOH FA 8 .   ? -2.593  254.426 53.960 1.00 57.33 ?  417 HOH F O   1 
HETATM 11792 O  O   . HOH FA 8 .   ? 24.976  223.761 58.729 1.00 52.10 ?  418 HOH F O   1 
HETATM 11793 O  O   . HOH FA 8 .   ? 12.835  240.271 39.107 1.00 55.22 ?  419 HOH F O   1 
HETATM 11794 O  O   . HOH FA 8 .   ? 17.542  251.431 43.589 1.00 55.11 ?  420 HOH F O   1 
HETATM 11795 O  O   . HOH FA 8 .   ? 10.291  229.917 47.287 1.00 46.29 ?  421 HOH F O   1 
HETATM 11796 O  O   . HOH FA 8 .   ? -3.711  242.030 51.567 1.00 36.66 ?  422 HOH F O   1 
HETATM 11797 O  O   . HOH FA 8 .   ? 12.293  246.573 68.432 1.00 54.61 ?  423 HOH F O   1 
HETATM 11798 O  O   . HOH FA 8 .   ? 11.641  240.820 41.198 1.00 47.68 ?  424 HOH F O   1 
HETATM 11799 O  O   . HOH FA 8 .   ? 4.925   227.943 63.164 1.00 46.75 ?  425 HOH F O   1 
HETATM 11800 O  O   . HOH FA 8 .   ? 39.747  228.059 43.982 1.00 52.33 ?  426 HOH F O   1 
HETATM 11801 O  O   . HOH FA 8 .   ? 19.188  248.311 39.821 1.00 50.46 ?  427 HOH F O   1 
HETATM 11802 O  O   . HOH FA 8 .   ? 0.438   237.255 60.184 1.00 42.68 ?  428 HOH F O   1 
HETATM 11803 O  O   . HOH FA 8 .   ? 13.146  237.609 70.662 1.00 49.35 ?  429 HOH F O   1 
HETATM 11804 O  O   . HOH GA 8 .   ? 3.126   141.418 26.656 1.00 64.50 ?  201 HOH G O   1 
HETATM 11805 O  O   . HOH GA 8 .   ? 0.234   159.173 12.102 1.00 42.76 ?  202 HOH G O   1 
HETATM 11806 O  O   . HOH GA 8 .   ? 5.439   160.098 5.116  1.00 39.65 ?  203 HOH G O   1 
HETATM 11807 O  O   . HOH GA 8 .   ? 37.255  156.948 28.763 1.00 50.90 ?  204 HOH G O   1 
HETATM 11808 O  O   . HOH GA 8 .   ? -2.441  147.284 12.403 1.00 51.95 ?  205 HOH G O   1 
HETATM 11809 O  O   . HOH GA 8 .   ? 3.947   156.971 30.745 1.00 50.12 ?  206 HOH G O   1 
HETATM 11810 O  O   . HOH GA 8 .   ? 33.629  152.055 20.070 1.00 47.54 ?  207 HOH G O   1 
HETATM 11811 O  O   . HOH GA 8 .   ? 19.834  146.570 5.171  1.00 54.22 ?  208 HOH G O   1 
HETATM 11812 O  O   . HOH GA 8 .   ? 17.704  146.524 13.202 1.00 52.43 ?  209 HOH G O   1 
HETATM 11813 O  O   . HOH GA 8 .   ? 13.904  158.169 3.725  1.00 36.48 ?  210 HOH G O   1 
HETATM 11814 O  O   . HOH GA 8 .   ? -0.827  156.874 14.934 1.00 35.15 ?  211 HOH G O   1 
HETATM 11815 O  O   . HOH GA 8 .   ? 15.430  153.251 -0.291 1.00 42.67 ?  212 HOH G O   1 
HETATM 11816 O  O   . HOH GA 8 .   ? 5.527   163.742 1.793  1.00 58.95 ?  213 HOH G O   1 
HETATM 11817 O  O   . HOH GA 8 .   ? 15.858  157.196 5.162  1.00 41.97 ?  214 HOH G O   1 
HETATM 11818 O  O   . HOH GA 8 .   ? 10.559  151.626 0.429  1.00 42.95 ?  215 HOH G O   1 
HETATM 11819 O  O   . HOH GA 8 .   ? 21.837  153.772 2.356  1.00 52.95 ?  216 HOH G O   1 
HETATM 11820 O  O   . HOH GA 8 .   ? -0.767  165.467 18.011 1.00 35.24 ?  217 HOH G O   1 
HETATM 11821 O  O   . HOH GA 8 .   ? 18.619  144.121 1.652  1.00 43.95 ?  218 HOH G O   1 
HETATM 11822 O  O   . HOH GA 8 .   ? 15.850  165.072 16.880 1.00 50.76 ?  219 HOH G O   1 
HETATM 11823 O  O   . HOH GA 8 .   ? -0.693  160.083 14.688 1.00 46.48 ?  220 HOH G O   1 
HETATM 11824 O  O   . HOH GA 8 .   ? 9.827   161.139 5.381  1.00 41.93 ?  221 HOH G O   1 
HETATM 11825 O  O   . HOH GA 8 .   ? 17.916  149.059 23.711 1.00 61.21 ?  222 HOH G O   1 
HETATM 11826 O  O   . HOH GA 8 .   ? 18.774  153.416 0.032  1.00 44.96 ?  223 HOH G O   1 
HETATM 11827 O  O   . HOH GA 8 .   ? 13.642  166.819 12.323 1.00 50.12 ?  224 HOH G O   1 
HETATM 11828 O  O   . HOH GA 8 .   ? 5.774   167.708 2.869  1.00 54.16 ?  225 HOH G O   1 
HETATM 11829 O  O   . HOH GA 8 .   ? 4.413   151.920 -1.369 1.00 50.12 ?  226 HOH G O   1 
HETATM 11830 O  O   . HOH GA 8 .   ? 19.556  150.595 -1.901 1.00 53.83 ?  227 HOH G O   1 
HETATM 11831 O  O   . HOH GA 8 .   ? 3.305   163.347 16.845 1.00 46.26 ?  228 HOH G O   1 
HETATM 11832 O  O   . HOH GA 8 .   ? 23.643  151.874 8.445  1.00 47.18 ?  229 HOH G O   1 
HETATM 11833 O  O   . HOH GA 8 .   ? 4.477   164.581 10.886 1.00 51.91 ?  230 HOH G O   1 
HETATM 11834 O  O   . HOH GA 8 .   ? 16.093  163.400 18.930 1.00 53.79 ?  231 HOH G O   1 
HETATM 11835 O  O   . HOH GA 8 .   ? 31.991  158.802 22.205 1.00 58.40 ?  232 HOH G O   1 
HETATM 11836 O  O   . HOH GA 8 .   ? 21.576  152.208 -0.499 1.00 58.94 ?  233 HOH G O   1 
HETATM 11837 O  O   . HOH GA 8 .   ? 9.286   153.422 -0.757 1.00 51.99 ?  234 HOH G O   1 
HETATM 11838 O  O   . HOH GA 8 .   ? 4.947   170.264 9.893  1.00 56.13 ?  235 HOH G O   1 
HETATM 11839 O  O   . HOH GA 8 .   ? 12.127  161.798 4.576  1.00 50.05 ?  236 HOH G O   1 
HETATM 11840 O  O   . HOH GA 8 .   ? -8.637  151.042 31.000 1.00 59.82 ?  237 HOH G O   1 
HETATM 11841 O  O   . HOH GA 8 .   ? 21.442  147.258 -4.412 1.00 52.29 ?  238 HOH G O   1 
HETATM 11842 O  O   . HOH GA 8 .   ? 23.374  160.265 18.511 1.00 62.10 ?  239 HOH G O   1 
HETATM 11843 O  O   . HOH HA 8 .   ? -3.354  174.769 5.471  1.00 46.37 ?  301 HOH H O   1 
HETATM 11844 O  O   . HOH HA 8 .   ? -9.858  161.836 36.112 1.00 55.08 ?  302 HOH H O   1 
HETATM 11845 O  O   . HOH HA 8 .   ? -27.979 165.170 11.981 1.00 44.39 ?  303 HOH H O   1 
HETATM 11846 O  O   . HOH HA 8 .   ? -6.666  183.570 13.279 1.00 49.90 ?  304 HOH H O   1 
HETATM 11847 O  O   . HOH HA 8 .   ? -29.511 165.874 24.078 1.00 55.00 ?  305 HOH H O   1 
HETATM 11848 O  O   . HOH HA 8 .   ? -24.327 170.742 9.298  1.00 45.84 ?  306 HOH H O   1 
HETATM 11849 O  O   . HOH HA 8 .   ? -36.398 150.096 14.688 1.00 39.68 ?  307 HOH H O   1 
HETATM 11850 O  O   . HOH HA 8 .   ? -13.110 165.160 34.109 1.00 59.20 ?  308 HOH H O   1 
HETATM 11851 O  O   . HOH HA 8 .   ? -4.048  163.308 12.274 1.00 47.62 ?  309 HOH H O   1 
HETATM 11852 O  O   . HOH HA 8 .   ? -20.695 171.038 21.619 1.00 33.32 ?  310 HOH H O   1 
HETATM 11853 O  O   . HOH HA 8 .   ? -33.871 159.545 20.134 1.00 37.63 ?  311 HOH H O   1 
HETATM 11854 O  O   . HOH HA 8 .   ? -24.084 153.380 33.247 1.00 54.46 ?  312 HOH H O   1 
HETATM 11855 O  O   . HOH HA 8 .   ? -24.505 176.851 15.915 1.00 35.09 ?  313 HOH H O   1 
HETATM 11856 O  O   . HOH HA 8 .   ? -15.469 181.407 13.704 1.00 46.70 ?  314 HOH H O   1 
HETATM 11857 O  O   . HOH HA 8 .   ? -8.847  156.545 12.801 1.00 51.22 ?  315 HOH H O   1 
HETATM 11858 O  O   . HOH HA 8 .   ? -24.747 158.811 11.568 1.00 46.39 ?  316 HOH H O   1 
HETATM 11859 O  O   . HOH HA 8 .   ? -10.550 170.697 35.582 1.00 47.64 ?  317 HOH H O   1 
HETATM 11860 O  O   . HOH HA 8 .   ? -24.974 153.850 21.784 1.00 43.49 ?  318 HOH H O   1 
HETATM 11861 O  O   . HOH HA 8 .   ? -12.242 177.158 5.885  1.00 33.35 ?  319 HOH H O   1 
HETATM 11862 O  O   . HOH HA 8 .   ? 1.453   168.035 30.341 1.00 58.48 ?  320 HOH H O   1 
HETATM 11863 O  O   . HOH HA 8 .   ? -7.865  148.328 12.672 1.00 48.35 ?  321 HOH H O   1 
HETATM 11864 O  O   . HOH HA 8 .   ? -13.657 182.959 9.815  1.00 49.41 ?  322 HOH H O   1 
HETATM 11865 O  O   . HOH HA 8 .   ? -20.996 160.172 14.936 1.00 37.99 ?  323 HOH H O   1 
HETATM 11866 O  O   . HOH HA 8 .   ? -20.186 155.710 28.181 1.00 44.06 ?  324 HOH H O   1 
HETATM 11867 O  O   . HOH HA 8 .   ? -7.317  166.838 5.847  1.00 46.48 ?  325 HOH H O   1 
HETATM 11868 O  O   . HOH HA 8 .   ? -9.726  155.569 29.220 1.00 50.90 ?  326 HOH H O   1 
HETATM 11869 O  O   . HOH HA 8 .   ? -26.040 173.226 10.709 1.00 41.13 ?  327 HOH H O   1 
HETATM 11870 O  O   . HOH HA 8 .   ? -2.761  171.548 23.823 1.00 45.86 ?  328 HOH H O   1 
HETATM 11871 O  O   . HOH HA 8 .   ? -32.019 163.341 13.432 1.00 38.35 ?  329 HOH H O   1 
HETATM 11872 O  O   . HOH HA 8 .   ? -3.334  155.113 14.651 1.00 41.39 ?  330 HOH H O   1 
HETATM 11873 O  O   . HOH HA 8 .   ? -5.968  161.244 10.721 1.00 50.80 ?  331 HOH H O   1 
HETATM 11874 O  O   . HOH HA 8 .   ? -21.800 159.092 12.456 1.00 46.83 ?  332 HOH H O   1 
HETATM 11875 O  O   . HOH HA 8 .   ? -20.192 168.349 5.598  1.00 37.97 ?  333 HOH H O   1 
HETATM 11876 O  O   . HOH HA 8 .   ? -11.042 150.657 24.916 1.00 45.54 ?  334 HOH H O   1 
HETATM 11877 O  O   . HOH HA 8 .   ? -2.827  164.162 16.782 1.00 32.38 ?  335 HOH H O   1 
HETATM 11878 O  O   . HOH HA 8 .   ? -15.995 170.150 3.824  1.00 39.14 ?  336 HOH H O   1 
HETATM 11879 O  O   . HOH HA 8 .   ? -1.385  173.495 20.047 1.00 43.28 ?  337 HOH H O   1 
HETATM 11880 O  O   . HOH HA 8 .   ? -20.340 183.148 9.586  1.00 42.70 ?  338 HOH H O   1 
HETATM 11881 O  O   . HOH HA 8 .   ? -17.865 169.913 5.838  1.00 38.37 ?  339 HOH H O   1 
HETATM 11882 O  O   . HOH HA 8 .   ? -22.814 164.439 21.410 1.00 35.74 ?  340 HOH H O   1 
HETATM 11883 O  O   . HOH HA 8 .   ? -37.011 163.693 20.132 1.00 49.47 ?  341 HOH H O   1 
HETATM 11884 O  O   . HOH HA 8 .   ? -2.190  172.820 7.048  1.00 61.28 ?  342 HOH H O   1 
HETATM 11885 O  O   . HOH HA 8 .   ? -16.647 158.034 7.392  1.00 41.36 ?  343 HOH H O   1 
HETATM 11886 O  O   . HOH HA 8 .   ? -28.985 169.017 16.483 1.00 50.92 ?  344 HOH H O   1 
HETATM 11887 O  O   . HOH HA 8 .   ? -5.574  156.463 27.922 1.00 51.64 ?  345 HOH H O   1 
HETATM 11888 O  O   . HOH HA 8 .   ? -3.151  161.305 14.726 1.00 42.95 ?  346 HOH H O   1 
HETATM 11889 O  O   . HOH HA 8 .   ? -20.890 155.067 18.150 1.00 42.07 ?  347 HOH H O   1 
HETATM 11890 O  O   . HOH HA 8 .   ? -11.856 166.209 5.051  1.00 38.65 ?  348 HOH H O   1 
HETATM 11891 O  O   . HOH HA 8 .   ? -10.329 149.482 15.297 1.00 51.74 ?  349 HOH H O   1 
HETATM 11892 O  O   . HOH HA 8 .   ? -19.247 173.325 26.560 1.00 44.77 ?  350 HOH H O   1 
HETATM 11893 O  O   . HOH HA 8 .   ? -13.507 173.304 40.759 1.00 45.94 ?  351 HOH H O   1 
HETATM 11894 O  O   . HOH HA 8 .   ? -20.928 179.131 3.543  1.00 50.17 ?  352 HOH H O   1 
HETATM 11895 O  O   . HOH HA 8 .   ? -23.925 174.721 4.848  1.00 41.34 ?  353 HOH H O   1 
HETATM 11896 O  O   . HOH HA 8 .   ? -17.264 176.234 3.643  1.00 42.67 ?  354 HOH H O   1 
HETATM 11897 O  O   . HOH HA 8 .   ? -4.051  175.512 18.593 1.00 40.22 ?  355 HOH H O   1 
HETATM 11898 O  O   . HOH HA 8 .   ? -14.696 181.633 2.619  1.00 38.23 ?  356 HOH H O   1 
HETATM 11899 O  O   . HOH HA 8 .   ? -15.921 152.240 24.303 1.00 50.09 ?  357 HOH H O   1 
HETATM 11900 O  O   . HOH HA 8 .   ? -31.745 154.303 12.312 1.00 48.51 ?  358 HOH H O   1 
HETATM 11901 O  O   . HOH HA 8 .   ? -9.764  179.111 17.441 1.00 44.38 ?  359 HOH H O   1 
HETATM 11902 O  O   . HOH HA 8 .   ? -16.710 179.077 14.665 1.00 30.77 ?  360 HOH H O   1 
HETATM 11903 O  O   . HOH HA 8 .   ? -26.435 168.742 9.422  1.00 47.69 ?  361 HOH H O   1 
HETATM 11904 O  O   . HOH HA 8 .   ? -3.715  172.207 25.799 1.00 55.38 ?  362 HOH H O   1 
HETATM 11905 O  O   . HOH HA 8 .   ? -9.885  181.348 13.017 1.00 55.39 ?  363 HOH H O   1 
HETATM 11906 O  O   . HOH HA 8 .   ? -6.283  174.704 12.487 1.00 50.60 ?  364 HOH H O   1 
HETATM 11907 O  O   . HOH HA 8 .   ? -30.239 158.187 21.942 1.00 51.13 ?  365 HOH H O   1 
HETATM 11908 O  O   . HOH HA 8 .   ? -9.525  159.134 6.960  1.00 49.81 ?  366 HOH H O   1 
HETATM 11909 O  O   . HOH HA 8 .   ? -4.223  165.547 41.953 1.00 59.92 ?  367 HOH H O   1 
HETATM 11910 O  O   . HOH HA 8 .   ? -19.528 153.770 14.798 1.00 55.33 ?  368 HOH H O   1 
HETATM 11911 O  O   . HOH HA 8 .   ? -22.924 179.259 11.266 1.00 43.14 ?  369 HOH H O   1 
HETATM 11912 O  O   . HOH HA 8 .   ? -7.515  177.081 11.101 1.00 54.00 ?  370 HOH H O   1 
HETATM 11913 O  O   . HOH HA 8 .   ? -6.290  155.736 5.051  1.00 57.04 ?  371 HOH H O   1 
HETATM 11914 O  O   . HOH HA 8 .   ? -17.515 152.129 14.357 1.00 43.41 ?  372 HOH H O   1 
HETATM 11915 O  O   . HOH HA 8 .   ? -5.848  175.709 16.833 1.00 39.30 ?  373 HOH H O   1 
HETATM 11916 O  O   . HOH HA 8 .   ? -26.456 168.643 25.148 1.00 34.12 ?  374 HOH H O   1 
HETATM 11917 O  O   . HOH HA 8 .   ? -19.262 156.995 10.281 1.00 50.63 ?  375 HOH H O   1 
HETATM 11918 O  O   . HOH HA 8 .   ? -12.358 179.167 2.955  1.00 49.61 ?  376 HOH H O   1 
HETATM 11919 O  O   . HOH HA 8 .   ? -7.610  160.217 8.437  1.00 54.35 ?  377 HOH H O   1 
HETATM 11920 O  O   . HOH HA 8 .   ? -3.875  170.997 10.906 1.00 44.72 ?  378 HOH H O   1 
HETATM 11921 O  O   . HOH HA 8 .   ? -4.565  160.040 12.847 1.00 52.01 ?  379 HOH H O   1 
HETATM 11922 O  O   . HOH HA 8 .   ? -4.952  167.854 41.114 1.00 54.43 ?  380 HOH H O   1 
HETATM 11923 O  O   . HOH HA 8 .   ? -19.932 157.209 13.125 1.00 46.92 ?  381 HOH H O   1 
HETATM 11924 O  O   . HOH HA 8 .   ? -14.187 173.519 1.850  1.00 50.29 ?  382 HOH H O   1 
HETATM 11925 O  O   . HOH HA 8 .   ? -6.315  179.043 13.771 1.00 52.54 ?  383 HOH H O   1 
HETATM 11926 O  O   . HOH HA 8 .   ? -16.068 148.353 19.351 1.00 52.93 ?  384 HOH H O   1 
HETATM 11927 O  O   . HOH HA 8 .   ? -11.304 182.671 7.606  1.00 51.23 ?  385 HOH H O   1 
HETATM 11928 O  O   . HOH HA 8 .   ? -11.150 181.420 5.400  1.00 56.30 ?  386 HOH H O   1 
HETATM 11929 O  O   . HOH HA 8 .   ? -29.865 167.037 13.562 1.00 55.16 ?  387 HOH H O   1 
HETATM 11930 O  O   . HOH HA 8 .   ? -14.149 166.455 3.427  1.00 46.98 ?  388 HOH H O   1 
HETATM 11931 O  O   . HOH HA 8 .   ? 1.433   168.755 7.380  1.00 62.02 ?  389 HOH H O   1 
HETATM 11932 O  O   . HOH HA 8 .   ? -30.689 163.690 11.193 1.00 47.93 ?  390 HOH H O   1 
HETATM 11933 O  O   . HOH HA 8 .   ? -10.041 179.082 6.607  1.00 53.71 ?  391 HOH H O   1 
HETATM 11934 O  O   . HOH HA 8 .   ? -36.159 160.080 21.714 1.00 46.78 ?  392 HOH H O   1 
HETATM 11935 O  O   . HOH HA 8 .   ? -23.161 173.270 2.688  1.00 56.53 ?  393 HOH H O   1 
HETATM 11936 O  O   . HOH HA 8 .   ? -7.472  145.712 12.967 1.00 59.90 ?  394 HOH H O   1 
HETATM 11937 O  O   . HOH HA 8 .   ? -18.716 166.695 3.166  1.00 47.97 ?  395 HOH H O   1 
HETATM 11938 O  O   . HOH HA 8 .   ? -16.106 167.771 2.561  1.00 50.32 ?  396 HOH H O   1 
HETATM 11939 O  O   . HOH IA 8 .   ? 44.534  222.851 44.632 1.00 48.95 ?  301 HOH I O   1 
HETATM 11940 O  O   . HOH IA 8 .   ? 27.977  226.147 56.981 1.00 35.44 ?  302 HOH I O   1 
HETATM 11941 O  O   . HOH IA 8 .   ? 53.341  219.036 39.743 1.00 58.83 ?  303 HOH I O   1 
HETATM 11942 O  O   . HOH IA 8 .   ? 43.544  213.776 61.822 1.00 53.02 ?  304 HOH I O   1 
HETATM 11943 O  O   . HOH IA 8 .   ? 43.971  201.537 50.617 1.00 45.80 ?  305 HOH I O   1 
HETATM 11944 O  O   . HOH IA 8 .   ? 40.209  210.902 62.382 1.00 47.13 ?  306 HOH I O   1 
HETATM 11945 O  O   . HOH IA 8 .   ? 25.902  203.737 48.611 1.00 48.57 ?  307 HOH I O   1 
HETATM 11946 O  O   . HOH IA 8 .   ? 37.822  230.852 52.662 1.00 38.64 ?  308 HOH I O   1 
HETATM 11947 O  O   . HOH IA 8 .   ? 45.740  218.248 34.505 1.00 52.37 ?  309 HOH I O   1 
HETATM 11948 O  O   . HOH IA 8 .   ? 38.484  206.166 55.663 1.00 50.43 ?  310 HOH I O   1 
HETATM 11949 O  O   . HOH IA 8 .   ? 43.693  218.710 32.143 1.00 65.81 ?  311 HOH I O   1 
HETATM 11950 O  O   . HOH IA 8 .   ? 34.174  215.712 34.125 1.00 56.50 ?  312 HOH I O   1 
HETATM 11951 O  O   . HOH IA 8 .   ? 29.789  224.692 62.660 1.00 50.22 ?  313 HOH I O   1 
HETATM 11952 O  O   . HOH IA 8 .   ? 33.840  222.428 67.785 1.00 55.37 ?  314 HOH I O   1 
HETATM 11953 O  O   . HOH IA 8 .   ? 35.824  206.011 52.001 1.00 38.52 ?  315 HOH I O   1 
HETATM 11954 O  O   . HOH IA 8 .   ? 45.826  221.892 60.535 1.00 50.29 ?  316 HOH I O   1 
HETATM 11955 O  O   . HOH IA 8 .   ? 27.282  209.545 48.119 1.00 42.90 ?  317 HOH I O   1 
HETATM 11956 O  O   . HOH IA 8 .   ? 34.980  220.374 64.620 1.00 40.01 ?  318 HOH I O   1 
HETATM 11957 O  O   . HOH IA 8 .   ? 37.609  224.413 46.026 1.00 44.66 ?  319 HOH I O   1 
HETATM 11958 O  O   . HOH IA 8 .   ? 38.925  204.596 52.860 1.00 40.40 ?  320 HOH I O   1 
HETATM 11959 O  O   . HOH IA 8 .   ? 29.925  226.335 58.806 1.00 50.43 ?  321 HOH I O   1 
HETATM 11960 O  O   . HOH IA 8 .   ? 41.442  227.960 41.618 1.00 55.24 ?  322 HOH I O   1 
HETATM 11961 O  O   . HOH IA 8 .   ? 30.368  227.691 63.498 1.00 46.48 ?  323 HOH I O   1 
HETATM 11962 O  O   . HOH IA 8 .   ? 43.732  229.576 56.945 1.00 44.04 ?  324 HOH I O   1 
HETATM 11963 O  O   . HOH IA 8 .   ? 45.627  230.233 48.965 1.00 47.71 ?  325 HOH I O   1 
HETATM 11964 O  O   . HOH IA 8 .   ? 46.749  216.011 35.574 1.00 56.30 ?  326 HOH I O   1 
HETATM 11965 O  O   . HOH IA 8 .   ? 36.450  223.341 41.031 1.00 48.50 ?  327 HOH I O   1 
HETATM 11966 O  O   . HOH IA 8 .   ? 56.562  217.428 47.009 1.00 61.77 ?  328 HOH I O   1 
HETATM 11967 O  O   . HOH IA 8 .   ? 43.356  220.785 61.460 1.00 41.63 ?  329 HOH I O   1 
HETATM 11968 O  O   . HOH IA 8 .   ? 49.464  209.437 33.636 1.00 54.77 ?  330 HOH I O   1 
HETATM 11969 O  O   . HOH IA 8 .   ? 33.055  225.038 42.870 1.00 47.50 ?  331 HOH I O   1 
HETATM 11970 O  O   . HOH IA 8 .   ? 53.899  216.876 36.156 1.00 67.09 ?  332 HOH I O   1 
HETATM 11971 O  O   . HOH IA 8 .   ? 51.290  234.601 46.818 1.00 69.32 ?  333 HOH I O   1 
HETATM 11972 O  O   . HOH IA 8 .   ? 41.373  207.574 35.886 1.00 54.63 ?  334 HOH I O   1 
HETATM 11973 O  O   . HOH IA 8 .   ? 24.750  205.472 40.643 1.00 59.53 ?  335 HOH I O   1 
HETATM 11974 O  O   . HOH IA 8 .   ? 27.502  205.307 40.816 1.00 52.93 ?  336 HOH I O   1 
HETATM 11975 O  O   . HOH IA 8 .   ? 32.786  226.021 54.601 1.00 46.91 ?  337 HOH I O   1 
HETATM 11976 O  O   . HOH IA 8 .   ? 35.879  225.001 48.167 1.00 44.27 ?  338 HOH I O   1 
HETATM 11977 O  O   . HOH IA 8 .   ? 23.959  218.163 46.125 1.00 52.27 ?  339 HOH I O   1 
HETATM 11978 O  O   . HOH IA 8 .   ? 34.670  225.124 52.342 1.00 37.95 ?  340 HOH I O   1 
HETATM 11979 O  O   . HOH IA 8 .   ? 51.337  213.582 56.368 1.00 49.74 ?  341 HOH I O   1 
HETATM 11980 O  O   . HOH IA 8 .   ? 26.494  209.704 52.246 1.00 50.21 ?  342 HOH I O   1 
HETATM 11981 O  O   . HOH IA 8 .   ? 33.220  225.760 40.060 1.00 51.13 ?  343 HOH I O   1 
HETATM 11982 O  O   . HOH IA 8 .   ? 31.799  225.705 57.319 1.00 48.22 ?  344 HOH I O   1 
HETATM 11983 O  O   . HOH IA 8 .   ? 47.547  205.579 38.622 1.00 48.13 ?  345 HOH I O   1 
HETATM 11984 O  O   . HOH IA 8 .   ? 28.581  214.735 54.574 1.00 54.33 ?  346 HOH I O   1 
HETATM 11985 O  O   . HOH IA 8 .   ? 50.652  198.448 48.873 1.00 50.34 ?  347 HOH I O   1 
HETATM 11986 O  O   . HOH IA 8 .   ? 47.101  231.848 46.840 1.00 51.22 ?  348 HOH I O   1 
HETATM 11987 O  O   . HOH IA 8 .   ? 33.841  223.985 49.867 1.00 36.87 ?  349 HOH I O   1 
HETATM 11988 O  O   . HOH IA 8 .   ? 32.061  229.316 63.618 1.00 54.38 ?  350 HOH I O   1 
HETATM 11989 O  O   . HOH IA 8 .   ? 53.684  211.896 47.227 1.00 51.29 ?  351 HOH I O   1 
HETATM 11990 O  O   . HOH IA 8 .   ? 43.228  219.257 63.516 1.00 48.80 ?  352 HOH I O   1 
HETATM 11991 O  O   . HOH IA 8 .   ? 30.918  217.288 60.297 1.00 55.77 ?  353 HOH I O   1 
HETATM 11992 O  O   . HOH IA 8 .   ? 51.220  216.173 49.736 1.00 48.90 ?  354 HOH I O   1 
HETATM 11993 O  O   . HOH IA 8 .   ? 24.707  214.075 27.786 1.00 61.17 ?  355 HOH I O   1 
HETATM 11994 O  O   . HOH IA 8 .   ? 26.932  213.079 53.920 1.00 48.36 ?  356 HOH I O   1 
HETATM 11995 O  O   . HOH IA 8 .   ? 52.490  215.517 52.263 1.00 58.43 ?  357 HOH I O   1 
HETATM 11996 O  O   . HOH IA 8 .   ? 36.798  204.779 56.858 1.00 49.65 ?  358 HOH I O   1 
HETATM 11997 O  O   . HOH IA 8 .   ? 25.012  221.961 49.193 1.00 57.26 ?  359 HOH I O   1 
HETATM 11998 O  O   . HOH IA 8 .   ? 23.425  218.869 48.367 1.00 53.61 ?  360 HOH I O   1 
HETATM 11999 O  O   . HOH IA 8 .   ? 40.745  218.321 31.414 1.00 56.68 ?  361 HOH I O   1 
HETATM 12000 O  O   . HOH IA 8 .   ? 23.270  216.219 44.541 1.00 58.62 ?  362 HOH I O   1 
HETATM 12001 O  O   . HOH IA 8 .   ? 53.221  198.345 47.744 1.00 58.90 ?  363 HOH I O   1 
HETATM 12002 O  O   . HOH IA 8 .   ? 46.877  220.026 62.978 1.00 59.45 ?  364 HOH I O   1 
HETATM 12003 O  O   . HOH JA 8 .   ? 47.894  200.045 40.110 1.00 57.78 ?  301 HOH J O   1 
HETATM 12004 O  O   . HOH JA 8 .   ? 36.831  201.626 55.014 1.00 59.28 ?  302 HOH J O   1 
HETATM 12005 O  O   . HOH JA 8 .   ? 21.803  175.443 48.965 1.00 31.10 ?  303 HOH J O   1 
HETATM 12006 O  O   . HOH JA 8 .   ? 38.240  186.513 33.439 1.00 57.91 ?  304 HOH J O   1 
HETATM 12007 O  O   . HOH JA 8 .   ? 29.331  175.392 45.931 1.00 46.51 ?  305 HOH J O   1 
HETATM 12008 O  O   . HOH JA 8 .   ? 32.733  196.963 37.962 1.00 52.84 ?  306 HOH J O   1 
HETATM 12009 O  O   . HOH JA 8 .   ? 39.447  188.488 35.566 1.00 62.62 ?  307 HOH J O   1 
HETATM 12010 O  O   . HOH JA 8 .   ? 38.880  181.698 43.017 1.00 50.32 ?  308 HOH J O   1 
HETATM 12011 O  O   . HOH JA 8 .   ? 41.123  200.445 51.617 1.00 33.41 ?  309 HOH J O   1 
HETATM 12012 O  O   . HOH JA 8 .   ? 33.096  205.057 51.490 1.00 36.76 ?  310 HOH J O   1 
HETATM 12013 O  O   . HOH JA 8 .   ? 38.760  196.861 63.535 1.00 50.96 ?  311 HOH J O   1 
HETATM 12014 O  O   . HOH JA 8 .   ? 27.313  188.643 39.202 1.00 45.60 ?  312 HOH J O   1 
HETATM 12015 O  O   . HOH JA 8 .   ? 26.179  187.620 55.417 1.00 48.92 ?  313 HOH J O   1 
HETATM 12016 O  O   . HOH JA 8 .   ? 28.184  186.270 38.325 1.00 44.68 ?  314 HOH J O   1 
HETATM 12017 O  O   . HOH JA 8 .   ? 27.948  179.411 58.167 1.00 45.75 ?  315 HOH J O   1 
HETATM 12018 O  O   . HOH JA 8 .   ? 21.771  185.915 45.227 1.00 52.00 ?  316 HOH J O   1 
HETATM 12019 O  O   . HOH JA 8 .   ? 35.884  193.829 63.860 1.00 46.52 ?  317 HOH J O   1 
HETATM 12020 O  O   . HOH JA 8 .   ? 38.748  201.765 52.804 1.00 45.98 ?  318 HOH J O   1 
HETATM 12021 O  O   . HOH JA 8 .   ? 27.891  187.185 53.075 1.00 45.10 ?  319 HOH J O   1 
HETATM 12022 O  O   . HOH JA 8 .   ? 26.368  207.448 51.013 1.00 53.18 ?  320 HOH J O   1 
HETATM 12023 O  O   . HOH JA 8 .   ? 31.671  182.709 48.052 1.00 32.33 ?  321 HOH J O   1 
HETATM 12024 O  O   . HOH JA 8 .   ? 38.406  181.259 49.181 1.00 43.69 ?  322 HOH J O   1 
HETATM 12025 O  O   . HOH JA 8 .   ? 11.211  178.610 52.284 1.00 43.51 ?  323 HOH J O   1 
HETATM 12026 O  O   . HOH JA 8 .   ? 35.266  177.104 51.924 1.00 49.96 ?  324 HOH J O   1 
HETATM 12027 O  O   . HOH JA 8 .   ? 20.448  182.142 58.355 1.00 53.72 ?  325 HOH J O   1 
HETATM 12028 O  O   . HOH JA 8 .   ? 25.624  193.917 42.293 1.00 46.37 ?  326 HOH J O   1 
HETATM 12029 O  O   . HOH JA 8 .   ? 35.136  180.054 38.801 1.00 54.11 ?  327 HOH J O   1 
HETATM 12030 O  O   . HOH JA 8 .   ? 49.391  185.720 52.226 1.00 51.48 ?  328 HOH J O   1 
HETATM 12031 O  O   . HOH JA 8 .   ? 39.324  200.796 56.190 1.00 48.39 ?  329 HOH J O   1 
HETATM 12032 O  O   . HOH JA 8 .   ? 45.642  181.447 57.264 1.00 45.46 ?  330 HOH J O   1 
HETATM 12033 O  O   . HOH JA 8 .   ? 40.530  175.817 56.310 1.00 37.78 ?  331 HOH J O   1 
HETATM 12034 O  O   . HOH JA 8 .   ? 27.409  199.074 40.921 1.00 49.53 ?  332 HOH J O   1 
HETATM 12035 O  O   . HOH JA 8 .   ? 29.734  174.635 52.227 1.00 46.32 ?  333 HOH J O   1 
HETATM 12036 O  O   . HOH JA 8 .   ? 25.360  178.483 43.269 1.00 47.53 ?  334 HOH J O   1 
HETATM 12037 O  O   . HOH JA 8 .   ? 29.310  168.363 47.285 1.00 54.84 ?  335 HOH J O   1 
HETATM 12038 O  O   . HOH JA 8 .   ? 25.817  171.487 52.781 1.00 42.03 ?  336 HOH J O   1 
HETATM 12039 O  O   . HOH JA 8 .   ? 24.134  185.650 56.310 1.00 48.52 ?  337 HOH J O   1 
HETATM 12040 O  O   . HOH JA 8 .   ? 23.457  170.661 50.462 1.00 39.80 ?  338 HOH J O   1 
HETATM 12041 O  O   . HOH JA 8 .   ? 24.643  206.138 54.849 1.00 57.14 ?  339 HOH J O   1 
HETATM 12042 O  O   . HOH JA 8 .   ? 27.700  176.308 39.410 1.00 50.02 ?  340 HOH J O   1 
HETATM 12043 O  O   . HOH JA 8 .   ? 45.824  202.138 58.635 1.00 61.45 ?  341 HOH J O   1 
HETATM 12044 O  O   . HOH JA 8 .   ? 38.095  192.035 32.657 1.00 60.52 ?  342 HOH J O   1 
HETATM 12045 O  O   . HOH JA 8 .   ? 24.280  189.150 48.582 1.00 39.70 ?  343 HOH J O   1 
HETATM 12046 O  O   . HOH JA 8 .   ? 36.021  186.600 64.077 1.00 45.90 ?  344 HOH J O   1 
HETATM 12047 O  O   . HOH JA 8 .   ? 36.591  200.495 57.157 1.00 47.04 ?  345 HOH J O   1 
HETATM 12048 O  O   . HOH JA 8 .   ? 42.417  176.954 61.595 1.00 52.89 ?  346 HOH J O   1 
HETATM 12049 O  O   . HOH JA 8 .   ? 45.303  188.102 65.676 1.00 56.99 ?  347 HOH J O   1 
HETATM 12050 O  O   . HOH JA 8 .   ? 33.950  177.073 45.472 1.00 40.10 ?  348 HOH J O   1 
HETATM 12051 O  O   . HOH JA 8 .   ? 23.362  193.707 43.734 1.00 56.21 ?  349 HOH J O   1 
HETATM 12052 O  O   . HOH JA 8 .   ? 16.819  181.408 54.978 1.00 43.28 ?  350 HOH J O   1 
HETATM 12053 O  O   . HOH JA 8 .   ? 38.286  199.163 66.056 1.00 56.28 ?  351 HOH J O   1 
HETATM 12054 O  O   . HOH JA 8 .   ? 31.829  198.825 60.388 1.00 51.93 ?  352 HOH J O   1 
HETATM 12055 O  O   . HOH JA 8 .   ? 24.485  201.534 49.865 1.00 50.72 ?  353 HOH J O   1 
HETATM 12056 O  O   . HOH JA 8 .   ? 25.577  190.723 55.673 1.00 54.68 ?  354 HOH J O   1 
HETATM 12057 O  O   . HOH JA 8 .   ? 22.395  181.850 35.486 1.00 62.70 ?  355 HOH J O   1 
HETATM 12058 O  O   . HOH JA 8 .   ? 27.125  193.756 59.874 1.00 41.94 ?  356 HOH J O   1 
HETATM 12059 O  O   . HOH JA 8 .   ? 23.198  194.470 51.893 1.00 48.57 ?  357 HOH J O   1 
HETATM 12060 O  O   . HOH JA 8 .   ? 32.216  175.144 45.653 1.00 57.56 ?  358 HOH J O   1 
HETATM 12061 O  O   . HOH JA 8 .   ? 34.130  199.789 58.836 1.00 51.26 ?  359 HOH J O   1 
HETATM 12062 O  O   . HOH JA 8 .   ? 31.155  202.617 61.293 1.00 56.17 ?  360 HOH J O   1 
HETATM 12063 O  O   . HOH JA 8 .   ? 17.960  182.310 57.338 1.00 50.15 ?  361 HOH J O   1 
HETATM 12064 O  O   . HOH JA 8 .   ? 29.514  178.984 60.458 1.00 48.37 ?  362 HOH J O   1 
HETATM 12065 O  O   . HOH JA 8 .   ? 36.493  204.333 54.083 1.00 48.77 ?  363 HOH J O   1 
HETATM 12066 O  O   . HOH JA 8 .   ? 26.142  189.872 53.496 1.00 50.00 ?  364 HOH J O   1 
HETATM 12067 O  O   . HOH JA 8 .   ? 28.755  196.253 59.874 1.00 51.76 ?  365 HOH J O   1 
HETATM 12068 O  O   . HOH JA 8 .   ? 24.815  190.407 50.889 1.00 44.23 ?  366 HOH J O   1 
HETATM 12069 O  O   . HOH JA 8 .   ? 22.855  191.536 52.209 1.00 55.73 ?  367 HOH J O   1 
HETATM 12070 O  O   . HOH JA 8 .   ? 37.978  178.316 46.732 1.00 66.58 ?  368 HOH J O   1 
HETATM 12071 O  O   . HOH JA 8 .   ? 25.129  170.538 48.032 1.00 46.79 ?  369 HOH J O   1 
HETATM 12072 O  O   . HOH JA 8 .   ? 21.203  172.795 48.202 1.00 42.10 ?  370 HOH J O   1 
# 
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   MET 1   0   0   MET MET A . n 
A 1 2   ALA 2   1   1   ALA ALA A . n 
A 1 3   THR 3   2   2   THR THR A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   ALA 5   4   4   ALA ALA A . n 
A 1 6   VAL 6   5   5   VAL VAL A . n 
A 1 7   CYS 7   6   6   CYS CYS A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  ASP 12  11  11  ASP ASP A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLN 16  15  15  GLN GLN A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  ILE 18  17  17  ILE ILE A . n 
A 1 19  ILE 19  18  18  ILE ILE A . n 
A 1 20  ASN 20  19  19  ASN ASN A . n 
A 1 21  PHE 21  20  20  PHE PHE A . n 
A 1 22  GLU 22  21  21  GLU GLU A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LYS 24  23  23  LYS LYS A . n 
A 1 25  GLU 25  24  24  GLU GLU A . n 
A 1 26  SER 26  25  25  SER SER A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  GLY 28  27  27  GLY GLY A . n 
A 1 29  PRO 29  28  28  PRO PRO A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  LYS 31  30  30  LYS LYS A . n 
A 1 32  VAL 32  31  31  VAL VAL A . n 
A 1 33  TRP 33  32  32  TRP TRP A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  SER 35  34  34  SER SER A . n 
A 1 36  ILE 36  35  35  ILE ILE A . n 
A 1 37  LYS 37  36  36  LYS LYS A . n 
A 1 38  GLY 38  37  37  GLY GLY A . n 
A 1 39  LEU 39  38  38  LEU LEU A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  GLU 41  40  40  GLU GLU A . n 
A 1 42  GLY 42  41  41  GLY GLY A . n 
A 1 43  LEU 43  42  42  LEU LEU A . n 
A 1 44  HIS 44  43  43  HIS HIS A . n 
A 1 45  GLY 45  44  44  GLY GLY A . n 
A 1 46  PHE 46  45  45  PHE PHE A . n 
A 1 47  HIS 47  46  46  HIS HIS A . n 
A 1 48  VAL 48  47  47  VAL VAL A . n 
A 1 49  HIS 49  48  48  HIS HIS A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  PHE 51  50  50  PHE PHE A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  ASP 53  52  52  ASP ASP A . n 
A 1 54  ASN 54  53  53  ASN ASN A . n 
A 1 55  THR 55  54  54  THR THR A . n 
A 1 56  ALA 56  55  55  ALA ALA A . n 
A 1 57  GLY 57  56  56  GLY GLY A . n 
A 1 58  CYS 58  57  57  CYS CYS A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  SER 60  59  59  SER SER A . n 
A 1 61  ALA 61  60  60  ALA ALA A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  PRO 63  62  62  PRO PRO A . n 
A 1 64  HIS 64  63  63  HIS HIS A . n 
A 1 65  PHE 65  64  64  PHE PHE A . n 
A 1 66  ASN 66  65  65  ASN ASN A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  LEU 68  67  67  LEU LEU A . n 
A 1 69  SER 69  68  68  SER SER A . n 
A 1 70  ARG 70  69  69  ARG ARG A . n 
A 1 71  LYS 71  70  70  LYS LYS A . n 
A 1 72  HIS 72  71  71  HIS HIS A . n 
A 1 73  GLY 73  72  72  GLY GLY A . n 
A 1 74  GLY 74  73  73  GLY GLY A . n 
A 1 75  PRO 75  74  74  PRO PRO A . n 
A 1 76  LYS 76  75  75  LYS LYS A . n 
A 1 77  ASP 77  76  76  ASP ASP A . n 
A 1 78  GLU 78  77  77  GLU GLU A . n 
A 1 79  GLU 79  78  78  GLU GLU A . n 
A 1 80  ARG 80  79  79  ARG ARG A . n 
A 1 81  HIS 81  80  80  HIS HIS A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  GLY 83  82  82  GLY GLY A . n 
A 1 84  ASP 84  83  83  ASP ASP A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  GLY 86  85  85  GLY GLY A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  THR 89  88  88  THR THR A . n 
A 1 90  ALA 90  89  89  ALA ALA A . n 
A 1 91  ASP 91  90  90  ASP ASP A . n 
A 1 92  LYS 92  91  91  LYS LYS A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  GLY 94  93  93  GLY GLY A . n 
A 1 95  VAL 95  94  94  VAL VAL A . n 
A 1 96  ALA 96  95  95  ALA ALA A . n 
A 1 97  ASP 97  96  96  ASP ASP A . n 
A 1 98  VAL 98  97  97  VAL VAL A . n 
A 1 99  SER 99  98  98  SER SER A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 GLU 101 100 100 GLU GLU A . n 
A 1 102 ASP 102 101 101 ASP ASP A . n 
A 1 103 SER 103 102 102 SER SER A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 ILE 105 104 104 ILE ILE A . n 
A 1 106 SER 106 105 105 SER SER A . n 
A 1 107 LEU 107 106 106 LEU LEU A . n 
A 1 108 SER 108 107 107 SER SER A . n 
A 1 109 GLY 109 108 108 GLY GLY A . n 
A 1 110 ASP 110 109 109 ASP ASP A . n 
A 1 111 HIS 111 110 110 HIS HIS A . n 
A 1 112 CYS 112 111 111 CYS CYS A . n 
A 1 113 ILE 113 112 112 ILE ILE A . n 
A 1 114 ILE 114 113 113 ILE ILE A . n 
A 1 115 GLY 115 114 114 GLY GLY A . n 
A 1 116 ARG 116 115 115 ARG ARG A . n 
A 1 117 THR 117 116 116 THR THR A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 VAL 119 118 118 VAL VAL A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 HIS 121 120 120 HIS HIS A . n 
A 1 122 GLU 122 121 121 GLU GLU A . n 
A 1 123 LYS 123 122 122 LYS LYS A . n 
A 1 124 ALA 124 123 123 ALA ALA A . n 
A 1 125 ASP 125 124 124 ASP ASP A . n 
A 1 126 ASP 126 125 125 ASP ASP A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 GLY 128 127 127 GLY GLY A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 GLY 131 130 130 GLY GLY A . n 
A 1 132 ASN 132 131 131 ASN ASN A . n 
A 1 133 GLU 133 132 132 GLU GLU A . n 
A 1 134 GLU 134 133 133 GLU GLU A . n 
A 1 135 SER 135 134 134 SER SER A . n 
A 1 136 THR 136 135 135 THR THR A . n 
A 1 137 LYS 137 136 136 LYS LYS A . n 
A 1 138 THR 138 137 137 THR THR A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 ASN 140 139 139 ASN ASN A . n 
A 1 141 ALA 141 140 140 ALA ALA A . n 
A 1 142 GLY 142 141 141 GLY GLY A . n 
A 1 143 SER 143 142 142 SER SER A . n 
A 1 144 ARG 144 143 143 ARG ARG A . n 
A 1 145 LEU 145 144 144 LEU LEU A . n 
A 1 146 ALA 146 145 145 ALA ALA A . n 
A 1 147 CYS 147 146 146 CYS CYS A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 VAL 149 148 148 VAL VAL A . n 
A 1 150 ILE 150 149 149 ILE ILE A . n 
A 1 151 GLY 151 150 150 GLY GLY A . n 
A 1 152 ILE 152 151 151 ILE ILE A . n 
A 1 153 ALA 153 152 152 ALA ALA A . n 
A 1 154 GLN 154 153 153 GLN GLN A . n 
B 1 1   MET 1   0   0   MET MET B . n 
B 1 2   ALA 2   1   1   ALA ALA B . n 
B 1 3   THR 3   2   2   THR THR B . n 
B 1 4   LYS 4   3   3   LYS LYS B . n 
B 1 5   ALA 5   4   4   ALA ALA B . n 
B 1 6   VAL 6   5   5   VAL VAL B . n 
B 1 7   CYS 7   6   6   CYS CYS B . n 
B 1 8   VAL 8   7   7   VAL VAL B . n 
B 1 9   LEU 9   8   8   LEU LEU B . n 
B 1 10  LYS 10  9   9   LYS LYS B . n 
B 1 11  GLY 11  10  10  GLY GLY B . n 
B 1 12  ASP 12  11  11  ASP ASP B . n 
B 1 13  GLY 13  12  12  GLY GLY B . n 
B 1 14  PRO 14  13  13  PRO PRO B . n 
B 1 15  VAL 15  14  14  VAL VAL B . n 
B 1 16  GLN 16  15  15  GLN GLN B . n 
B 1 17  GLY 17  16  16  GLY GLY B . n 
B 1 18  ILE 18  17  17  ILE ILE B . n 
B 1 19  ILE 19  18  18  ILE ILE B . n 
B 1 20  ASN 20  19  19  ASN ASN B . n 
B 1 21  PHE 21  20  20  PHE PHE B . n 
B 1 22  GLU 22  21  21  GLU GLU B . n 
B 1 23  GLN 23  22  22  GLN GLN B . n 
B 1 24  LYS 24  23  23  LYS LYS B . n 
B 1 25  GLU 25  24  24  GLU GLU B . n 
B 1 26  SER 26  25  25  SER SER B . n 
B 1 27  ASN 27  26  26  ASN ASN B . n 
B 1 28  GLY 28  27  27  GLY GLY B . n 
B 1 29  PRO 29  28  28  PRO PRO B . n 
B 1 30  VAL 30  29  29  VAL VAL B . n 
B 1 31  LYS 31  30  30  LYS LYS B . n 
B 1 32  VAL 32  31  31  VAL VAL B . n 
B 1 33  TRP 33  32  32  TRP TRP B . n 
B 1 34  GLY 34  33  33  GLY GLY B . n 
B 1 35  SER 35  34  34  SER SER B . n 
B 1 36  ILE 36  35  35  ILE ILE B . n 
B 1 37  LYS 37  36  36  LYS LYS B . n 
B 1 38  GLY 38  37  37  GLY GLY B . n 
B 1 39  LEU 39  38  38  LEU LEU B . n 
B 1 40  THR 40  39  39  THR THR B . n 
B 1 41  GLU 41  40  40  GLU GLU B . n 
B 1 42  GLY 42  41  41  GLY GLY B . n 
B 1 43  LEU 43  42  42  LEU LEU B . n 
B 1 44  HIS 44  43  43  HIS HIS B . n 
B 1 45  GLY 45  44  44  GLY GLY B . n 
B 1 46  PHE 46  45  45  PHE PHE B . n 
B 1 47  HIS 47  46  46  HIS HIS B . n 
B 1 48  VAL 48  47  47  VAL VAL B . n 
B 1 49  HIS 49  48  48  HIS HIS B . n 
B 1 50  GLU 50  49  49  GLU GLU B . n 
B 1 51  PHE 51  50  50  PHE PHE B . n 
B 1 52  GLY 52  51  51  GLY GLY B . n 
B 1 53  ASP 53  52  52  ASP ASP B . n 
B 1 54  ASN 54  53  53  ASN ASN B . n 
B 1 55  THR 55  54  54  THR THR B . n 
B 1 56  ALA 56  55  55  ALA ALA B . n 
B 1 57  GLY 57  56  56  GLY GLY B . n 
B 1 58  CYS 58  57  57  CYS CYS B . n 
B 1 59  THR 59  58  58  THR THR B . n 
B 1 60  SER 60  59  59  SER SER B . n 
B 1 61  ALA 61  60  60  ALA ALA B . n 
B 1 62  GLY 62  61  61  GLY GLY B . n 
B 1 63  PRO 63  62  62  PRO PRO B . n 
B 1 64  HIS 64  63  63  HIS HIS B . n 
B 1 65  PHE 65  64  64  PHE PHE B . n 
B 1 66  ASN 66  65  65  ASN ASN B . n 
B 1 67  PRO 67  66  66  PRO PRO B . n 
B 1 68  LEU 68  67  67  LEU LEU B . n 
B 1 69  SER 69  68  68  SER SER B . n 
B 1 70  ARG 70  69  69  ARG ARG B . n 
B 1 71  LYS 71  70  70  LYS LYS B . n 
B 1 72  HIS 72  71  71  HIS HIS B . n 
B 1 73  GLY 73  72  72  GLY GLY B . n 
B 1 74  GLY 74  73  73  GLY GLY B . n 
B 1 75  PRO 75  74  74  PRO PRO B . n 
B 1 76  LYS 76  75  75  LYS LYS B . n 
B 1 77  ASP 77  76  76  ASP ASP B . n 
B 1 78  GLU 78  77  77  GLU GLU B . n 
B 1 79  GLU 79  78  78  GLU GLU B . n 
B 1 80  ARG 80  79  79  ARG ARG B . n 
B 1 81  HIS 81  80  80  HIS HIS B . n 
B 1 82  VAL 82  81  81  VAL VAL B . n 
B 1 83  GLY 83  82  82  GLY GLY B . n 
B 1 84  ASP 84  83  83  ASP ASP B . n 
B 1 85  LEU 85  84  84  LEU LEU B . n 
B 1 86  GLY 86  85  85  GLY GLY B . n 
B 1 87  ASN 87  86  86  ASN ASN B . n 
B 1 88  VAL 88  87  87  VAL VAL B . n 
B 1 89  THR 89  88  88  THR THR B . n 
B 1 90  ALA 90  89  89  ALA ALA B . n 
B 1 91  ASP 91  90  90  ASP ASP B . n 
B 1 92  LYS 92  91  91  LYS LYS B . n 
B 1 93  ASP 93  92  92  ASP ASP B . n 
B 1 94  GLY 94  93  93  GLY GLY B . n 
B 1 95  VAL 95  94  94  VAL VAL B . n 
B 1 96  ALA 96  95  95  ALA ALA B . n 
B 1 97  ASP 97  96  96  ASP ASP B . n 
B 1 98  VAL 98  97  97  VAL VAL B . n 
B 1 99  SER 99  98  98  SER SER B . n 
B 1 100 ILE 100 99  99  ILE ILE B . n 
B 1 101 GLU 101 100 100 GLU GLU B . n 
B 1 102 ASP 102 101 101 ASP ASP B . n 
B 1 103 SER 103 102 102 SER SER B . n 
B 1 104 VAL 104 103 103 VAL VAL B . n 
B 1 105 ILE 105 104 104 ILE ILE B . n 
B 1 106 SER 106 105 105 SER SER B . n 
B 1 107 LEU 107 106 106 LEU LEU B . n 
B 1 108 SER 108 107 107 SER SER B . n 
B 1 109 GLY 109 108 108 GLY GLY B . n 
B 1 110 ASP 110 109 109 ASP ASP B . n 
B 1 111 HIS 111 110 110 HIS HIS B . n 
B 1 112 CYS 112 111 111 CYS CYS B . n 
B 1 113 ILE 113 112 112 ILE ILE B . n 
B 1 114 ILE 114 113 113 ILE ILE B . n 
B 1 115 GLY 115 114 114 GLY GLY B . n 
B 1 116 ARG 116 115 115 ARG ARG B . n 
B 1 117 THR 117 116 116 THR THR B . n 
B 1 118 LEU 118 117 117 LEU LEU B . n 
B 1 119 VAL 119 118 118 VAL VAL B . n 
B 1 120 VAL 120 119 119 VAL VAL B . n 
B 1 121 HIS 121 120 120 HIS HIS B . n 
B 1 122 GLU 122 121 121 GLU GLU B . n 
B 1 123 LYS 123 122 122 LYS LYS B . n 
B 1 124 ALA 124 123 123 ALA ALA B . n 
B 1 125 ASP 125 124 124 ASP ASP B . n 
B 1 126 ASP 126 125 125 ASP ASP B . n 
B 1 127 LEU 127 126 126 LEU LEU B . n 
B 1 128 GLY 128 127 127 GLY GLY B . n 
B 1 129 LYS 129 128 128 LYS LYS B . n 
B 1 130 GLY 130 129 129 GLY GLY B . n 
B 1 131 GLY 131 130 130 GLY GLY B . n 
B 1 132 ASN 132 131 131 ASN ASN B . n 
B 1 133 GLU 133 132 132 GLU GLU B . n 
B 1 134 GLU 134 133 133 GLU GLU B . n 
B 1 135 SER 135 134 134 SER SER B . n 
B 1 136 THR 136 135 135 THR THR B . n 
B 1 137 LYS 137 136 136 LYS LYS B . n 
B 1 138 THR 138 137 137 THR THR B . n 
B 1 139 GLY 139 138 138 GLY GLY B . n 
B 1 140 ASN 140 139 139 ASN ASN B . n 
B 1 141 ALA 141 140 140 ALA ALA B . n 
B 1 142 GLY 142 141 141 GLY GLY B . n 
B 1 143 SER 143 142 142 SER SER B . n 
B 1 144 ARG 144 143 143 ARG ARG B . n 
B 1 145 LEU 145 144 144 LEU LEU B . n 
B 1 146 ALA 146 145 145 ALA ALA B . n 
B 1 147 CYS 147 146 146 CYS CYS B . n 
B 1 148 GLY 148 147 147 GLY GLY B . n 
B 1 149 VAL 149 148 148 VAL VAL B . n 
B 1 150 ILE 150 149 149 ILE ILE B . n 
B 1 151 GLY 151 150 150 GLY GLY B . n 
B 1 152 ILE 152 151 151 ILE ILE B . n 
B 1 153 ALA 153 152 152 ALA ALA B . n 
B 1 154 GLN 154 153 153 GLN GLN B . n 
C 2 1   ALA 1   -1  -1  ALA ALA C . n 
C 2 2   MET 2   0   0   MET MET C . n 
C 2 3   ALA 3   1   1   ALA ALA C . n 
C 2 4   THR 4   2   2   THR THR C . n 
C 2 5   LYS 5   3   3   LYS LYS C . n 
C 2 6   ALA 6   4   4   ALA ALA C . n 
C 2 7   VAL 7   5   5   VAL VAL C . n 
C 2 8   CYS 8   6   6   CYS CYS C . n 
C 2 9   VAL 9   7   7   VAL VAL C . n 
C 2 10  LEU 10  8   8   LEU LEU C . n 
C 2 11  LYS 11  9   9   LYS LYS C . n 
C 2 12  GLY 12  10  10  GLY GLY C . n 
C 2 13  ASP 13  11  11  ASP ASP C . n 
C 2 14  GLY 14  12  12  GLY GLY C . n 
C 2 15  PRO 15  13  13  PRO PRO C . n 
C 2 16  VAL 16  14  14  VAL VAL C . n 
C 2 17  GLN 17  15  15  GLN GLN C . n 
C 2 18  GLY 18  16  16  GLY GLY C . n 
C 2 19  ILE 19  17  17  ILE ILE C . n 
C 2 20  ILE 20  18  18  ILE ILE C . n 
C 2 21  ASN 21  19  19  ASN ASN C . n 
C 2 22  PHE 22  20  20  PHE PHE C . n 
C 2 23  GLU 23  21  21  GLU GLU C . n 
C 2 24  GLN 24  22  22  GLN GLN C . n 
C 2 25  LYS 25  23  23  LYS LYS C . n 
C 2 26  GLU 26  24  24  GLU GLU C . n 
C 2 27  SER 27  25  25  SER SER C . n 
C 2 28  ASN 28  26  26  ASN ASN C . n 
C 2 29  GLY 29  27  27  GLY GLY C . n 
C 2 30  PRO 30  28  28  PRO PRO C . n 
C 2 31  VAL 31  29  29  VAL VAL C . n 
C 2 32  LYS 32  30  30  LYS LYS C . n 
C 2 33  VAL 33  31  31  VAL VAL C . n 
C 2 34  TRP 34  32  32  TRP TRP C . n 
C 2 35  GLY 35  33  33  GLY GLY C . n 
C 2 36  SER 36  34  34  SER SER C . n 
C 2 37  ILE 37  35  35  ILE ILE C . n 
C 2 38  LYS 38  36  36  LYS LYS C . n 
C 2 39  GLY 39  37  37  GLY GLY C . n 
C 2 40  LEU 40  38  38  LEU LEU C . n 
C 2 41  THR 41  39  39  THR THR C . n 
C 2 42  GLU 42  40  40  GLU GLU C . n 
C 2 43  GLY 43  41  41  GLY GLY C . n 
C 2 44  LEU 44  42  42  LEU LEU C . n 
C 2 45  HIS 45  43  43  HIS HIS C . n 
C 2 46  GLY 46  44  44  GLY GLY C . n 
C 2 47  PHE 47  45  45  PHE PHE C . n 
C 2 48  HIS 48  46  46  HIS HIS C . n 
C 2 49  VAL 49  47  47  VAL VAL C . n 
C 2 50  HIS 50  48  48  HIS HIS C . n 
C 2 51  GLU 51  49  49  GLU GLU C . n 
C 2 52  PHE 52  50  50  PHE PHE C . n 
C 2 53  GLY 53  51  51  GLY GLY C . n 
C 2 54  ASP 54  52  52  ASP ASP C . n 
C 2 55  ASN 55  53  53  ASN ASN C . n 
C 2 56  THR 56  54  54  THR THR C . n 
C 2 57  ALA 57  55  55  ALA ALA C . n 
C 2 58  GLY 58  56  56  GLY GLY C . n 
C 2 59  CYS 59  57  57  CYS CYS C . n 
C 2 60  THR 60  58  58  THR THR C . n 
C 2 61  SER 61  59  59  SER SER C . n 
C 2 62  ALA 62  60  60  ALA ALA C . n 
C 2 63  GLY 63  61  61  GLY GLY C . n 
C 2 64  PRO 64  62  62  PRO PRO C . n 
C 2 65  HIS 65  63  63  HIS HIS C . n 
C 2 66  PHE 66  64  64  PHE PHE C . n 
C 2 67  ASN 67  65  65  ASN ASN C . n 
C 2 68  PRO 68  66  66  PRO PRO C . n 
C 2 69  LEU 69  67  67  LEU LEU C . n 
C 2 70  SER 70  68  68  SER SER C . n 
C 2 71  ARG 71  69  69  ARG ARG C . n 
C 2 72  LYS 72  70  70  LYS LYS C . n 
C 2 73  HIS 73  71  71  HIS HIS C . n 
C 2 74  GLY 74  72  72  GLY GLY C . n 
C 2 75  GLY 75  73  73  GLY GLY C . n 
C 2 76  PRO 76  74  74  PRO PRO C . n 
C 2 77  LYS 77  75  75  LYS LYS C . n 
C 2 78  ASP 78  76  76  ASP ASP C . n 
C 2 79  GLU 79  77  77  GLU GLU C . n 
C 2 80  GLU 80  78  78  GLU GLU C . n 
C 2 81  ARG 81  79  79  ARG ARG C . n 
C 2 82  HIS 82  80  80  HIS HIS C . n 
C 2 83  VAL 83  81  81  VAL VAL C . n 
C 2 84  GLY 84  82  82  GLY GLY C . n 
C 2 85  ASP 85  83  83  ASP ASP C . n 
C 2 86  LEU 86  84  84  LEU LEU C . n 
C 2 87  GLY 87  85  85  GLY GLY C . n 
C 2 88  ASN 88  86  86  ASN ASN C . n 
C 2 89  VAL 89  87  87  VAL VAL C . n 
C 2 90  THR 90  88  88  THR THR C . n 
C 2 91  ALA 91  89  89  ALA ALA C . n 
C 2 92  ASP 92  90  90  ASP ASP C . n 
C 2 93  LYS 93  91  91  LYS LYS C . n 
C 2 94  ASP 94  92  92  ASP ASP C . n 
C 2 95  GLY 95  93  93  GLY GLY C . n 
C 2 96  VAL 96  94  94  VAL VAL C . n 
C 2 97  ALA 97  95  95  ALA ALA C . n 
C 2 98  ASP 98  96  96  ASP ASP C . n 
C 2 99  VAL 99  97  97  VAL VAL C . n 
C 2 100 SER 100 98  98  SER SER C . n 
C 2 101 ILE 101 99  99  ILE ILE C . n 
C 2 102 GLU 102 100 100 GLU GLU C . n 
C 2 103 ASP 103 101 101 ASP ASP C . n 
C 2 104 SER 104 102 102 SER SER C . n 
C 2 105 VAL 105 103 103 VAL VAL C . n 
C 2 106 ILE 106 104 104 ILE ILE C . n 
C 2 107 SER 107 105 105 SER SER C . n 
C 2 108 LEU 108 106 106 LEU LEU C . n 
C 2 109 SER 109 107 107 SER SER C . n 
C 2 110 GLY 110 108 108 GLY GLY C . n 
C 2 111 ASP 111 109 109 ASP ASP C . n 
C 2 112 HIS 112 110 110 HIS HIS C . n 
C 2 113 CYS 113 111 111 CYS CYS C . n 
C 2 114 ILE 114 112 112 ILE ILE C . n 
C 2 115 ILE 115 113 113 ILE ILE C . n 
C 2 116 GLY 116 114 114 GLY GLY C . n 
C 2 117 ARG 117 115 115 ARG ARG C . n 
C 2 118 THR 118 116 116 THR THR C . n 
C 2 119 LEU 119 117 117 LEU LEU C . n 
C 2 120 VAL 120 118 118 VAL VAL C . n 
C 2 121 VAL 121 119 119 VAL VAL C . n 
C 2 122 HIS 122 120 120 HIS HIS C . n 
C 2 123 GLU 123 121 121 GLU GLU C . n 
C 2 124 LYS 124 122 122 LYS LYS C . n 
C 2 125 ALA 125 123 123 ALA ALA C . n 
C 2 126 ASP 126 124 124 ASP ASP C . n 
C 2 127 ASP 127 125 125 ASP ASP C . n 
C 2 128 LEU 128 126 126 LEU LEU C . n 
C 2 129 GLY 129 127 127 GLY GLY C . n 
C 2 130 LYS 130 128 128 LYS LYS C . n 
C 2 131 GLY 131 129 129 GLY GLY C . n 
C 2 132 GLY 132 130 130 GLY GLY C . n 
C 2 133 ASN 133 131 131 ASN ASN C . n 
C 2 134 GLU 134 132 132 GLU GLU C . n 
C 2 135 GLU 135 133 133 GLU GLU C . n 
C 2 136 SER 136 134 134 SER SER C . n 
C 2 137 THR 137 135 135 THR THR C . n 
C 2 138 LYS 138 136 136 LYS LYS C . n 
C 2 139 THR 139 137 137 THR THR C . n 
C 2 140 GLY 140 138 138 GLY GLY C . n 
C 2 141 ASN 141 139 139 ASN ASN C . n 
C 2 142 ALA 142 140 140 ALA ALA C . n 
C 2 143 GLY 143 141 141 GLY GLY C . n 
C 2 144 SER 144 142 142 SER SER C . n 
C 2 145 ARG 145 143 143 ARG ARG C . n 
C 2 146 LEU 146 144 144 LEU LEU C . n 
C 2 147 ALA 147 145 145 ALA ALA C . n 
C 2 148 CYS 148 146 146 CYS CYS C . n 
C 2 149 GLY 149 147 147 GLY GLY C . n 
C 2 150 VAL 150 148 148 VAL VAL C . n 
C 2 151 ILE 151 149 149 ILE ILE C . n 
C 2 152 GLY 152 150 150 GLY GLY C . n 
C 2 153 ILE 153 151 151 ILE ILE C . n 
C 2 154 ALA 154 152 152 ALA ALA C . n 
C 2 155 GLN 155 153 153 GLN GLN C . n 
D 1 1   MET 1   0   0   MET MET D . n 
D 1 2   ALA 2   1   1   ALA ALA D . n 
D 1 3   THR 3   2   2   THR THR D . n 
D 1 4   LYS 4   3   3   LYS LYS D . n 
D 1 5   ALA 5   4   4   ALA ALA D . n 
D 1 6   VAL 6   5   5   VAL VAL D . n 
D 1 7   CYS 7   6   6   CYS CYS D . n 
D 1 8   VAL 8   7   7   VAL VAL D . n 
D 1 9   LEU 9   8   8   LEU LEU D . n 
D 1 10  LYS 10  9   9   LYS LYS D . n 
D 1 11  GLY 11  10  10  GLY GLY D . n 
D 1 12  ASP 12  11  11  ASP ASP D . n 
D 1 13  GLY 13  12  12  GLY GLY D . n 
D 1 14  PRO 14  13  13  PRO PRO D . n 
D 1 15  VAL 15  14  14  VAL VAL D . n 
D 1 16  GLN 16  15  15  GLN GLN D . n 
D 1 17  GLY 17  16  16  GLY GLY D . n 
D 1 18  ILE 18  17  17  ILE ILE D . n 
D 1 19  ILE 19  18  18  ILE ILE D . n 
D 1 20  ASN 20  19  19  ASN ASN D . n 
D 1 21  PHE 21  20  20  PHE PHE D . n 
D 1 22  GLU 22  21  21  GLU GLU D . n 
D 1 23  GLN 23  22  22  GLN GLN D . n 
D 1 24  LYS 24  23  23  LYS LYS D . n 
D 1 25  GLU 25  24  24  GLU GLU D . n 
D 1 26  SER 26  25  25  SER SER D . n 
D 1 27  ASN 27  26  26  ASN ASN D . n 
D 1 28  GLY 28  27  27  GLY GLY D . n 
D 1 29  PRO 29  28  28  PRO PRO D . n 
D 1 30  VAL 30  29  29  VAL VAL D . n 
D 1 31  LYS 31  30  30  LYS LYS D . n 
D 1 32  VAL 32  31  31  VAL VAL D . n 
D 1 33  TRP 33  32  32  TRP TRP D . n 
D 1 34  GLY 34  33  33  GLY GLY D . n 
D 1 35  SER 35  34  34  SER SER D . n 
D 1 36  ILE 36  35  35  ILE ILE D . n 
D 1 37  LYS 37  36  36  LYS LYS D . n 
D 1 38  GLY 38  37  37  GLY GLY D . n 
D 1 39  LEU 39  38  38  LEU LEU D . n 
D 1 40  THR 40  39  39  THR THR D . n 
D 1 41  GLU 41  40  40  GLU GLU D . n 
D 1 42  GLY 42  41  41  GLY GLY D . n 
D 1 43  LEU 43  42  42  LEU LEU D . n 
D 1 44  HIS 44  43  43  HIS HIS D . n 
D 1 45  GLY 45  44  44  GLY GLY D . n 
D 1 46  PHE 46  45  45  PHE PHE D . n 
D 1 47  HIS 47  46  46  HIS HIS D . n 
D 1 48  VAL 48  47  47  VAL VAL D . n 
D 1 49  HIS 49  48  48  HIS HIS D . n 
D 1 50  GLU 50  49  49  GLU GLU D . n 
D 1 51  PHE 51  50  50  PHE PHE D . n 
D 1 52  GLY 52  51  51  GLY GLY D . n 
D 1 53  ASP 53  52  52  ASP ASP D . n 
D 1 54  ASN 54  53  53  ASN ASN D . n 
D 1 55  THR 55  54  54  THR THR D . n 
D 1 56  ALA 56  55  55  ALA ALA D . n 
D 1 57  GLY 57  56  56  GLY GLY D . n 
D 1 58  CYS 58  57  57  CYS CYS D . n 
D 1 59  THR 59  58  58  THR THR D . n 
D 1 60  SER 60  59  59  SER SER D . n 
D 1 61  ALA 61  60  60  ALA ALA D . n 
D 1 62  GLY 62  61  61  GLY GLY D . n 
D 1 63  PRO 63  62  62  PRO PRO D . n 
D 1 64  HIS 64  63  63  HIS HIS D . n 
D 1 65  PHE 65  64  64  PHE PHE D . n 
D 1 66  ASN 66  65  65  ASN ASN D . n 
D 1 67  PRO 67  66  66  PRO PRO D . n 
D 1 68  LEU 68  67  67  LEU LEU D . n 
D 1 69  SER 69  68  68  SER SER D . n 
D 1 70  ARG 70  69  69  ARG ARG D . n 
D 1 71  LYS 71  70  70  LYS LYS D . n 
D 1 72  HIS 72  71  71  HIS HIS D . n 
D 1 73  GLY 73  72  72  GLY GLY D . n 
D 1 74  GLY 74  73  73  GLY GLY D . n 
D 1 75  PRO 75  74  74  PRO PRO D . n 
D 1 76  LYS 76  75  75  LYS LYS D . n 
D 1 77  ASP 77  76  76  ASP ASP D . n 
D 1 78  GLU 78  77  77  GLU GLU D . n 
D 1 79  GLU 79  78  78  GLU GLU D . n 
D 1 80  ARG 80  79  79  ARG ARG D . n 
D 1 81  HIS 81  80  80  HIS HIS D . n 
D 1 82  VAL 82  81  81  VAL VAL D . n 
D 1 83  GLY 83  82  82  GLY GLY D . n 
D 1 84  ASP 84  83  83  ASP ASP D . n 
D 1 85  LEU 85  84  84  LEU LEU D . n 
D 1 86  GLY 86  85  85  GLY GLY D . n 
D 1 87  ASN 87  86  86  ASN ASN D . n 
D 1 88  VAL 88  87  87  VAL VAL D . n 
D 1 89  THR 89  88  88  THR THR D . n 
D 1 90  ALA 90  89  89  ALA ALA D . n 
D 1 91  ASP 91  90  90  ASP ASP D . n 
D 1 92  LYS 92  91  91  LYS LYS D . n 
D 1 93  ASP 93  92  92  ASP ASP D . n 
D 1 94  GLY 94  93  93  GLY GLY D . n 
D 1 95  VAL 95  94  94  VAL VAL D . n 
D 1 96  ALA 96  95  95  ALA ALA D . n 
D 1 97  ASP 97  96  96  ASP ASP D . n 
D 1 98  VAL 98  97  97  VAL VAL D . n 
D 1 99  SER 99  98  98  SER SER D . n 
D 1 100 ILE 100 99  99  ILE ILE D . n 
D 1 101 GLU 101 100 100 GLU GLU D . n 
D 1 102 ASP 102 101 101 ASP ASP D . n 
D 1 103 SER 103 102 102 SER SER D . n 
D 1 104 VAL 104 103 103 VAL VAL D . n 
D 1 105 ILE 105 104 104 ILE ILE D . n 
D 1 106 SER 106 105 105 SER SER D . n 
D 1 107 LEU 107 106 106 LEU LEU D . n 
D 1 108 SER 108 107 107 SER SER D . n 
D 1 109 GLY 109 108 108 GLY GLY D . n 
D 1 110 ASP 110 109 109 ASP ASP D . n 
D 1 111 HIS 111 110 110 HIS HIS D . n 
D 1 112 CYS 112 111 111 CYS CYS D . n 
D 1 113 ILE 113 112 112 ILE ILE D . n 
D 1 114 ILE 114 113 113 ILE ILE D . n 
D 1 115 GLY 115 114 114 GLY GLY D . n 
D 1 116 ARG 116 115 115 ARG ARG D . n 
D 1 117 THR 117 116 116 THR THR D . n 
D 1 118 LEU 118 117 117 LEU LEU D . n 
D 1 119 VAL 119 118 118 VAL VAL D . n 
D 1 120 VAL 120 119 119 VAL VAL D . n 
D 1 121 HIS 121 120 120 HIS HIS D . n 
D 1 122 GLU 122 121 121 GLU GLU D . n 
D 1 123 LYS 123 122 122 LYS LYS D . n 
D 1 124 ALA 124 123 123 ALA ALA D . n 
D 1 125 ASP 125 124 124 ASP ASP D . n 
D 1 126 ASP 126 125 125 ASP ASP D . n 
D 1 127 LEU 127 126 126 LEU LEU D . n 
D 1 128 GLY 128 127 127 GLY GLY D . n 
D 1 129 LYS 129 128 128 LYS LYS D . n 
D 1 130 GLY 130 129 129 GLY GLY D . n 
D 1 131 GLY 131 130 130 GLY GLY D . n 
D 1 132 ASN 132 131 131 ASN ASN D . n 
D 1 133 GLU 133 132 132 GLU GLU D . n 
D 1 134 GLU 134 133 133 GLU GLU D . n 
D 1 135 SER 135 134 134 SER SER D . n 
D 1 136 THR 136 135 135 THR THR D . n 
D 1 137 LYS 137 136 136 LYS LYS D . n 
D 1 138 THR 138 137 137 THR THR D . n 
D 1 139 GLY 139 138 138 GLY GLY D . n 
D 1 140 ASN 140 139 139 ASN ASN D . n 
D 1 141 ALA 141 140 140 ALA ALA D . n 
D 1 142 GLY 142 141 141 GLY GLY D . n 
D 1 143 SER 143 142 142 SER SER D . n 
D 1 144 ARG 144 143 143 ARG ARG D . n 
D 1 145 LEU 145 144 144 LEU LEU D . n 
D 1 146 ALA 146 145 145 ALA ALA D . n 
D 1 147 CYS 147 146 146 CYS CYS D . n 
D 1 148 GLY 148 147 147 GLY GLY D . n 
D 1 149 VAL 149 148 148 VAL VAL D . n 
D 1 150 ILE 150 149 149 ILE ILE D . n 
D 1 151 GLY 151 150 150 GLY GLY D . n 
D 1 152 ILE 152 151 151 ILE ILE D . n 
D 1 153 ALA 153 152 152 ALA ALA D . n 
D 1 154 GLN 154 153 153 GLN GLN D . n 
E 3 1   ALA 1   0   0   ALA ALA E . n 
E 3 2   ALA 2   1   1   ALA ALA E . n 
E 3 3   THR 3   2   2   THR THR E . n 
E 3 4   LYS 4   3   3   LYS LYS E . n 
E 3 5   ALA 5   4   4   ALA ALA E . n 
E 3 6   VAL 6   5   5   VAL VAL E . n 
E 3 7   CYS 7   6   6   CYS CYS E . n 
E 3 8   VAL 8   7   7   VAL VAL E . n 
E 3 9   LEU 9   8   8   LEU LEU E . n 
E 3 10  LYS 10  9   9   LYS LYS E . n 
E 3 11  GLY 11  10  10  GLY GLY E . n 
E 3 12  ASP 12  11  11  ASP ASP E . n 
E 3 13  GLY 13  12  12  GLY GLY E . n 
E 3 14  PRO 14  13  13  PRO PRO E . n 
E 3 15  VAL 15  14  14  VAL VAL E . n 
E 3 16  GLN 16  15  15  GLN GLN E . n 
E 3 17  GLY 17  16  16  GLY GLY E . n 
E 3 18  ILE 18  17  17  ILE ILE E . n 
E 3 19  ILE 19  18  18  ILE ILE E . n 
E 3 20  ASN 20  19  19  ASN ASN E . n 
E 3 21  PHE 21  20  20  PHE PHE E . n 
E 3 22  GLU 22  21  21  GLU GLU E . n 
E 3 23  GLN 23  22  22  GLN GLN E . n 
E 3 24  LYS 24  23  23  LYS LYS E . n 
E 3 25  GLU 25  24  24  GLU GLU E . n 
E 3 26  SER 26  25  25  SER SER E . n 
E 3 27  ASN 27  26  26  ASN ASN E . n 
E 3 28  GLY 28  27  27  GLY GLY E . n 
E 3 29  PRO 29  28  28  PRO PRO E . n 
E 3 30  VAL 30  29  29  VAL VAL E . n 
E 3 31  LYS 31  30  30  LYS LYS E . n 
E 3 32  VAL 32  31  31  VAL VAL E . n 
E 3 33  TRP 33  32  32  TRP TRP E . n 
E 3 34  GLY 34  33  33  GLY GLY E . n 
E 3 35  SER 35  34  34  SER SER E . n 
E 3 36  ILE 36  35  35  ILE ILE E . n 
E 3 37  LYS 37  36  36  LYS LYS E . n 
E 3 38  GLY 38  37  37  GLY GLY E . n 
E 3 39  LEU 39  38  38  LEU LEU E . n 
E 3 40  THR 40  39  39  THR THR E . n 
E 3 41  GLU 41  40  40  GLU GLU E . n 
E 3 42  GLY 42  41  41  GLY GLY E . n 
E 3 43  LEU 43  42  42  LEU LEU E . n 
E 3 44  HIS 44  43  43  HIS HIS E . n 
E 3 45  GLY 45  44  44  GLY GLY E . n 
E 3 46  PHE 46  45  45  PHE PHE E . n 
E 3 47  HIS 47  46  46  HIS HIS E . n 
E 3 48  VAL 48  47  47  VAL VAL E . n 
E 3 49  HIS 49  48  48  HIS HIS E . n 
E 3 50  GLU 50  49  49  GLU GLU E . n 
E 3 51  PHE 51  50  50  PHE PHE E . n 
E 3 52  GLY 52  51  51  GLY GLY E . n 
E 3 53  ASP 53  52  52  ASP ASP E . n 
E 3 54  ASN 54  53  53  ASN ASN E . n 
E 3 55  THR 55  54  54  THR THR E . n 
E 3 56  ALA 56  55  55  ALA ALA E . n 
E 3 57  GLY 57  56  56  GLY GLY E . n 
E 3 58  CYS 58  57  57  CYS CYS E . n 
E 3 59  THR 59  58  58  THR THR E . n 
E 3 60  SER 60  59  59  SER SER E . n 
E 3 61  ALA 61  60  60  ALA ALA E . n 
E 3 62  GLY 62  61  61  GLY GLY E . n 
E 3 63  PRO 63  62  62  PRO PRO E . n 
E 3 64  HIS 64  63  63  HIS HIS E . n 
E 3 65  PHE 65  64  64  PHE PHE E . n 
E 3 66  ASN 66  65  65  ASN ASN E . n 
E 3 67  PRO 67  66  66  PRO PRO E . n 
E 3 68  LEU 68  67  67  LEU LEU E . n 
E 3 69  SER 69  68  68  SER SER E . n 
E 3 70  ARG 70  69  69  ARG ARG E . n 
E 3 71  LYS 71  70  70  LYS LYS E . n 
E 3 72  HIS 72  71  71  HIS HIS E . n 
E 3 73  GLY 73  72  72  GLY GLY E . n 
E 3 74  GLY 74  73  73  GLY GLY E . n 
E 3 75  PRO 75  74  74  PRO PRO E . n 
E 3 76  LYS 76  75  75  LYS LYS E . n 
E 3 77  ASP 77  76  76  ASP ASP E . n 
E 3 78  ALA 78  77  77  ALA ALA E . n 
E 3 79  GLU 79  78  78  GLU GLU E . n 
E 3 80  ARG 80  79  79  ARG ARG E . n 
E 3 81  HIS 81  80  80  HIS HIS E . n 
E 3 82  VAL 82  81  81  VAL VAL E . n 
E 3 83  GLY 83  82  82  GLY GLY E . n 
E 3 84  ASP 84  83  83  ASP ASP E . n 
E 3 85  LEU 85  84  84  LEU LEU E . n 
E 3 86  GLY 86  85  85  GLY GLY E . n 
E 3 87  ASN 87  86  86  ASN ASN E . n 
E 3 88  VAL 88  87  87  VAL VAL E . n 
E 3 89  THR 89  88  88  THR THR E . n 
E 3 90  ALA 90  89  89  ALA ALA E . n 
E 3 91  ASP 91  90  90  ASP ASP E . n 
E 3 92  LYS 92  91  91  LYS LYS E . n 
E 3 93  ASP 93  92  92  ASP ASP E . n 
E 3 94  GLY 94  93  93  GLY GLY E . n 
E 3 95  VAL 95  94  94  VAL VAL E . n 
E 3 96  ALA 96  95  95  ALA ALA E . n 
E 3 97  ASP 97  96  96  ASP ASP E . n 
E 3 98  VAL 98  97  97  VAL VAL E . n 
E 3 99  SER 99  98  98  SER SER E . n 
E 3 100 ILE 100 99  99  ILE ILE E . n 
E 3 101 GLU 101 100 100 GLU GLU E . n 
E 3 102 ASP 102 101 101 ASP ASP E . n 
E 3 103 SER 103 102 102 SER SER E . n 
E 3 104 VAL 104 103 103 VAL VAL E . n 
E 3 105 ILE 105 104 104 ILE ILE E . n 
E 3 106 SER 106 105 105 SER SER E . n 
E 3 107 LEU 107 106 106 LEU LEU E . n 
E 3 108 SER 108 107 107 SER SER E . n 
E 3 109 GLY 109 108 108 GLY GLY E . n 
E 3 110 ASP 110 109 109 ASP ASP E . n 
E 3 111 HIS 111 110 110 HIS HIS E . n 
E 3 112 CYS 112 111 111 CYS CYS E . n 
E 3 113 ILE 113 112 112 ILE ILE E . n 
E 3 114 ILE 114 113 113 ILE ILE E . n 
E 3 115 GLY 115 114 114 GLY GLY E . n 
E 3 116 ARG 116 115 115 ARG ARG E . n 
E 3 117 THR 117 116 116 THR THR E . n 
E 3 118 LEU 118 117 117 LEU LEU E . n 
E 3 119 VAL 119 118 118 VAL VAL E . n 
E 3 120 VAL 120 119 119 VAL VAL E . n 
E 3 121 HIS 121 120 120 HIS HIS E . n 
E 3 122 GLU 122 121 121 GLU GLU E . n 
E 3 123 LYS 123 122 122 LYS LYS E . n 
E 3 124 ALA 124 123 123 ALA ALA E . n 
E 3 125 ASP 125 124 124 ASP ASP E . n 
E 3 126 ASP 126 125 125 ASP ASP E . n 
E 3 127 LEU 127 126 126 LEU LEU E . n 
E 3 128 GLY 128 127 127 GLY GLY E . n 
E 3 129 LYS 129 128 128 LYS LYS E . n 
E 3 130 GLY 130 129 129 GLY GLY E . n 
E 3 131 GLY 131 130 130 GLY GLY E . n 
E 3 132 ASN 132 131 131 ASN ASN E . n 
E 3 133 GLU 133 132 132 GLU GLU E . n 
E 3 134 GLU 134 133 133 GLU GLU E . n 
E 3 135 SER 135 134 134 SER SER E . n 
E 3 136 THR 136 135 135 THR THR E . n 
E 3 137 LYS 137 136 136 LYS LYS E . n 
E 3 138 THR 138 137 137 THR THR E . n 
E 3 139 GLY 139 138 138 GLY GLY E . n 
E 3 140 ASN 140 139 139 ASN ASN E . n 
E 3 141 ALA 141 140 140 ALA ALA E . n 
E 3 142 GLY 142 141 141 GLY GLY E . n 
E 3 143 SER 143 142 142 SER SER E . n 
E 3 144 ARG 144 143 143 ARG ARG E . n 
E 3 145 LEU 145 144 144 LEU LEU E . n 
E 3 146 ALA 146 145 145 ALA ALA E . n 
E 3 147 CYS 147 146 146 CYS CYS E . n 
E 3 148 GLY 148 147 147 GLY GLY E . n 
E 3 149 VAL 149 148 148 VAL VAL E . n 
E 3 150 ILE 150 149 149 ILE ILE E . n 
E 3 151 GLY 151 150 150 GLY GLY E . n 
E 3 152 ILE 152 151 151 ILE ILE E . n 
E 3 153 ALA 153 152 152 ALA ALA E . n 
E 3 154 GLN 154 153 153 GLN GLN E . n 
F 1 1   MET 1   0   0   MET MET F . n 
F 1 2   ALA 2   1   1   ALA ALA F . n 
F 1 3   THR 3   2   2   THR THR F . n 
F 1 4   LYS 4   3   3   LYS LYS F . n 
F 1 5   ALA 5   4   4   ALA ALA F . n 
F 1 6   VAL 6   5   5   VAL VAL F . n 
F 1 7   CYS 7   6   6   CYS CYS F . n 
F 1 8   VAL 8   7   7   VAL VAL F . n 
F 1 9   LEU 9   8   8   LEU LEU F . n 
F 1 10  LYS 10  9   9   LYS LYS F . n 
F 1 11  GLY 11  10  10  GLY GLY F . n 
F 1 12  ASP 12  11  11  ASP ASP F . n 
F 1 13  GLY 13  12  12  GLY GLY F . n 
F 1 14  PRO 14  13  13  PRO PRO F . n 
F 1 15  VAL 15  14  14  VAL VAL F . n 
F 1 16  GLN 16  15  15  GLN GLN F . n 
F 1 17  GLY 17  16  16  GLY GLY F . n 
F 1 18  ILE 18  17  17  ILE ILE F . n 
F 1 19  ILE 19  18  18  ILE ILE F . n 
F 1 20  ASN 20  19  19  ASN ASN F . n 
F 1 21  PHE 21  20  20  PHE PHE F . n 
F 1 22  GLU 22  21  21  GLU GLU F . n 
F 1 23  GLN 23  22  22  GLN GLN F . n 
F 1 24  LYS 24  23  23  LYS LYS F . n 
F 1 25  GLU 25  24  24  GLU GLU F . n 
F 1 26  SER 26  25  25  SER SER F . n 
F 1 27  ASN 27  26  26  ASN ASN F . n 
F 1 28  GLY 28  27  27  GLY GLY F . n 
F 1 29  PRO 29  28  28  PRO PRO F . n 
F 1 30  VAL 30  29  29  VAL VAL F . n 
F 1 31  LYS 31  30  30  LYS LYS F . n 
F 1 32  VAL 32  31  31  VAL VAL F . n 
F 1 33  TRP 33  32  32  TRP TRP F . n 
F 1 34  GLY 34  33  33  GLY GLY F . n 
F 1 35  SER 35  34  34  SER SER F . n 
F 1 36  ILE 36  35  35  ILE ILE F . n 
F 1 37  LYS 37  36  36  LYS LYS F . n 
F 1 38  GLY 38  37  37  GLY GLY F . n 
F 1 39  LEU 39  38  38  LEU LEU F . n 
F 1 40  THR 40  39  39  THR THR F . n 
F 1 41  GLU 41  40  40  GLU GLU F . n 
F 1 42  GLY 42  41  41  GLY GLY F . n 
F 1 43  LEU 43  42  42  LEU LEU F . n 
F 1 44  HIS 44  43  43  HIS HIS F . n 
F 1 45  GLY 45  44  44  GLY GLY F . n 
F 1 46  PHE 46  45  45  PHE PHE F . n 
F 1 47  HIS 47  46  46  HIS HIS F . n 
F 1 48  VAL 48  47  47  VAL VAL F . n 
F 1 49  HIS 49  48  48  HIS HIS F . n 
F 1 50  GLU 50  49  49  GLU GLU F . n 
F 1 51  PHE 51  50  50  PHE PHE F . n 
F 1 52  GLY 52  51  51  GLY GLY F . n 
F 1 53  ASP 53  52  52  ASP ASP F . n 
F 1 54  ASN 54  53  53  ASN ASN F . n 
F 1 55  THR 55  54  54  THR THR F . n 
F 1 56  ALA 56  55  55  ALA ALA F . n 
F 1 57  GLY 57  56  56  GLY GLY F . n 
F 1 58  CYS 58  57  57  CYS CYS F . n 
F 1 59  THR 59  58  58  THR THR F . n 
F 1 60  SER 60  59  59  SER SER F . n 
F 1 61  ALA 61  60  60  ALA ALA F . n 
F 1 62  GLY 62  61  61  GLY GLY F . n 
F 1 63  PRO 63  62  62  PRO PRO F . n 
F 1 64  HIS 64  63  63  HIS HIS F . n 
F 1 65  PHE 65  64  64  PHE PHE F . n 
F 1 66  ASN 66  65  65  ASN ASN F . n 
F 1 67  PRO 67  66  66  PRO PRO F . n 
F 1 68  LEU 68  67  67  LEU LEU F . n 
F 1 69  SER 69  68  68  SER SER F . n 
F 1 70  ARG 70  69  69  ARG ARG F . n 
F 1 71  LYS 71  70  70  LYS LYS F . n 
F 1 72  HIS 72  71  71  HIS HIS F . n 
F 1 73  GLY 73  72  72  GLY GLY F . n 
F 1 74  GLY 74  73  73  GLY GLY F . n 
F 1 75  PRO 75  74  74  PRO PRO F . n 
F 1 76  LYS 76  75  75  LYS LYS F . n 
F 1 77  ASP 77  76  76  ASP ASP F . n 
F 1 78  GLU 78  77  77  GLU GLU F . n 
F 1 79  GLU 79  78  78  GLU GLU F . n 
F 1 80  ARG 80  79  79  ARG ARG F . n 
F 1 81  HIS 81  80  80  HIS HIS F . n 
F 1 82  VAL 82  81  81  VAL VAL F . n 
F 1 83  GLY 83  82  82  GLY GLY F . n 
F 1 84  ASP 84  83  83  ASP ASP F . n 
F 1 85  LEU 85  84  84  LEU LEU F . n 
F 1 86  GLY 86  85  85  GLY GLY F . n 
F 1 87  ASN 87  86  86  ASN ASN F . n 
F 1 88  VAL 88  87  87  VAL VAL F . n 
F 1 89  THR 89  88  88  THR THR F . n 
F 1 90  ALA 90  89  89  ALA ALA F . n 
F 1 91  ASP 91  90  90  ASP ASP F . n 
F 1 92  LYS 92  91  91  LYS LYS F . n 
F 1 93  ASP 93  92  92  ASP ASP F . n 
F 1 94  GLY 94  93  93  GLY GLY F . n 
F 1 95  VAL 95  94  94  VAL VAL F . n 
F 1 96  ALA 96  95  95  ALA ALA F . n 
F 1 97  ASP 97  96  96  ASP ASP F . n 
F 1 98  VAL 98  97  97  VAL VAL F . n 
F 1 99  SER 99  98  98  SER SER F . n 
F 1 100 ILE 100 99  99  ILE ILE F . n 
F 1 101 GLU 101 100 100 GLU GLU F . n 
F 1 102 ASP 102 101 101 ASP ASP F . n 
F 1 103 SER 103 102 102 SER SER F . n 
F 1 104 VAL 104 103 103 VAL VAL F . n 
F 1 105 ILE 105 104 104 ILE ILE F . n 
F 1 106 SER 106 105 105 SER SER F . n 
F 1 107 LEU 107 106 106 LEU LEU F . n 
F 1 108 SER 108 107 107 SER SER F . n 
F 1 109 GLY 109 108 108 GLY GLY F . n 
F 1 110 ASP 110 109 109 ASP ASP F . n 
F 1 111 HIS 111 110 110 HIS HIS F . n 
F 1 112 CYS 112 111 111 CYS CYS F . n 
F 1 113 ILE 113 112 112 ILE ILE F . n 
F 1 114 ILE 114 113 113 ILE ILE F . n 
F 1 115 GLY 115 114 114 GLY GLY F . n 
F 1 116 ARG 116 115 115 ARG ARG F . n 
F 1 117 THR 117 116 116 THR THR F . n 
F 1 118 LEU 118 117 117 LEU LEU F . n 
F 1 119 VAL 119 118 118 VAL VAL F . n 
F 1 120 VAL 120 119 119 VAL VAL F . n 
F 1 121 HIS 121 120 120 HIS HIS F . n 
F 1 122 GLU 122 121 121 GLU GLU F . n 
F 1 123 LYS 123 122 122 LYS LYS F . n 
F 1 124 ALA 124 123 123 ALA ALA F . n 
F 1 125 ASP 125 124 124 ASP ASP F . n 
F 1 126 ASP 126 125 125 ASP ASP F . n 
F 1 127 LEU 127 126 126 LEU LEU F . n 
F 1 128 GLY 128 127 127 GLY GLY F . n 
F 1 129 LYS 129 128 128 LYS LYS F . n 
F 1 130 GLY 130 129 129 GLY GLY F . n 
F 1 131 GLY 131 130 130 GLY GLY F . n 
F 1 132 ASN 132 131 131 ASN ASN F . n 
F 1 133 GLU 133 132 132 GLU GLU F . n 
F 1 134 GLU 134 133 133 GLU GLU F . n 
F 1 135 SER 135 134 134 SER SER F . n 
F 1 136 THR 136 135 135 THR THR F . n 
F 1 137 LYS 137 136 136 LYS LYS F . n 
F 1 138 THR 138 137 137 THR THR F . n 
F 1 139 GLY 139 138 138 GLY GLY F . n 
F 1 140 ASN 140 139 139 ASN ASN F . n 
F 1 141 ALA 141 140 140 ALA ALA F . n 
F 1 142 GLY 142 141 141 GLY GLY F . n 
F 1 143 SER 143 142 142 SER SER F . n 
F 1 144 ARG 144 143 143 ARG ARG F . n 
F 1 145 LEU 145 144 144 LEU LEU F . n 
F 1 146 ALA 146 145 145 ALA ALA F . n 
F 1 147 CYS 147 146 146 CYS CYS F . n 
F 1 148 GLY 148 147 147 GLY GLY F . n 
F 1 149 VAL 149 148 148 VAL VAL F . n 
F 1 150 ILE 150 149 149 ILE ILE F . n 
F 1 151 GLY 151 150 150 GLY GLY F . n 
F 1 152 ILE 152 151 151 ILE ILE F . n 
F 1 153 ALA 153 152 152 ALA ALA F . n 
F 1 154 GLN 154 153 153 GLN GLN F . n 
G 3 1   ALA 1   0   ?   ?   ?   G . n 
G 3 2   ALA 2   1   1   ALA ALA G . n 
G 3 3   THR 3   2   2   THR THR G . n 
G 3 4   LYS 4   3   3   LYS LYS G . n 
G 3 5   ALA 5   4   4   ALA ALA G . n 
G 3 6   VAL 6   5   5   VAL VAL G . n 
G 3 7   CYS 7   6   6   CYS CYS G . n 
G 3 8   VAL 8   7   7   VAL VAL G . n 
G 3 9   LEU 9   8   8   LEU LEU G . n 
G 3 10  LYS 10  9   9   LYS LYS G . n 
G 3 11  GLY 11  10  10  GLY GLY G . n 
G 3 12  ASP 12  11  11  ASP ASP G . n 
G 3 13  GLY 13  12  12  GLY GLY G . n 
G 3 14  PRO 14  13  13  PRO PRO G . n 
G 3 15  VAL 15  14  14  VAL VAL G . n 
G 3 16  GLN 16  15  15  GLN GLN G . n 
G 3 17  GLY 17  16  16  GLY GLY G . n 
G 3 18  ILE 18  17  17  ILE ILE G . n 
G 3 19  ILE 19  18  18  ILE ILE G . n 
G 3 20  ASN 20  19  19  ASN ASN G . n 
G 3 21  PHE 21  20  20  PHE PHE G . n 
G 3 22  GLU 22  21  21  GLU GLU G . n 
G 3 23  GLN 23  22  22  GLN GLN G . n 
G 3 24  LYS 24  23  23  LYS LYS G . n 
G 3 25  GLU 25  24  24  GLU GLU G . n 
G 3 26  SER 26  25  25  SER SER G . n 
G 3 27  ASN 27  26  26  ASN ASN G . n 
G 3 28  GLY 28  27  27  GLY GLY G . n 
G 3 29  PRO 29  28  28  PRO PRO G . n 
G 3 30  VAL 30  29  29  VAL VAL G . n 
G 3 31  LYS 31  30  30  LYS LYS G . n 
G 3 32  VAL 32  31  31  VAL VAL G . n 
G 3 33  TRP 33  32  32  TRP TRP G . n 
G 3 34  GLY 34  33  33  GLY GLY G . n 
G 3 35  SER 35  34  34  SER SER G . n 
G 3 36  ILE 36  35  35  ILE ILE G . n 
G 3 37  LYS 37  36  36  LYS LYS G . n 
G 3 38  GLY 38  37  37  GLY GLY G . n 
G 3 39  LEU 39  38  38  LEU LEU G . n 
G 3 40  THR 40  39  39  THR THR G . n 
G 3 41  GLU 41  40  40  GLU GLU G . n 
G 3 42  GLY 42  41  41  GLY GLY G . n 
G 3 43  LEU 43  42  42  LEU LEU G . n 
G 3 44  HIS 44  43  43  HIS HIS G . n 
G 3 45  GLY 45  44  44  GLY GLY G . n 
G 3 46  PHE 46  45  45  PHE PHE G . n 
G 3 47  HIS 47  46  46  HIS HIS G . n 
G 3 48  VAL 48  47  47  VAL VAL G . n 
G 3 49  HIS 49  48  48  HIS HIS G . n 
G 3 50  GLU 50  49  49  GLU GLU G . n 
G 3 51  PHE 51  50  50  PHE PHE G . n 
G 3 52  GLY 52  51  51  GLY GLY G . n 
G 3 53  ASP 53  52  52  ASP ASP G . n 
G 3 54  ASN 54  53  53  ASN ASN G . n 
G 3 55  THR 55  54  54  THR THR G . n 
G 3 56  ALA 56  55  55  ALA ALA G . n 
G 3 57  GLY 57  56  56  GLY GLY G . n 
G 3 58  CYS 58  57  57  CYS CYS G . n 
G 3 59  THR 59  58  58  THR THR G . n 
G 3 60  SER 60  59  59  SER SER G . n 
G 3 61  ALA 61  60  60  ALA ALA G . n 
G 3 62  GLY 62  61  61  GLY GLY G . n 
G 3 63  PRO 63  62  62  PRO PRO G . n 
G 3 64  HIS 64  63  63  HIS HIS G . n 
G 3 65  PHE 65  64  64  PHE PHE G . n 
G 3 66  ASN 66  65  65  ASN ASN G . n 
G 3 67  PRO 67  66  66  PRO PRO G . n 
G 3 68  LEU 68  67  67  LEU ALA G . n 
G 3 69  SER 69  68  ?   ?   ?   G . n 
G 3 70  ARG 70  69  ?   ?   ?   G . n 
G 3 71  LYS 71  70  ?   ?   ?   G . n 
G 3 72  HIS 72  71  ?   ?   ?   G . n 
G 3 73  GLY 73  72  ?   ?   ?   G . n 
G 3 74  GLY 74  73  ?   ?   ?   G . n 
G 3 75  PRO 75  74  ?   ?   ?   G . n 
G 3 76  LYS 76  75  ?   ?   ?   G . n 
G 3 77  ASP 77  76  ?   ?   ?   G . n 
G 3 78  ALA 78  77  ?   ?   ?   G . n 
G 3 79  GLU 79  78  ?   ?   ?   G . n 
G 3 80  ARG 80  79  79  ARG ARG G . n 
G 3 81  HIS 81  80  80  HIS HIS G . n 
G 3 82  VAL 82  81  81  VAL VAL G . n 
G 3 83  GLY 83  82  82  GLY GLY G . n 
G 3 84  ASP 84  83  83  ASP ASP G . n 
G 3 85  LEU 85  84  84  LEU LEU G . n 
G 3 86  GLY 86  85  85  GLY GLY G . n 
G 3 87  ASN 87  86  86  ASN ASN G . n 
G 3 88  VAL 88  87  87  VAL VAL G . n 
G 3 89  THR 89  88  88  THR THR G . n 
G 3 90  ALA 90  89  89  ALA ALA G . n 
G 3 91  ASP 91  90  90  ASP ASP G . n 
G 3 92  LYS 92  91  91  LYS LYS G . n 
G 3 93  ASP 93  92  92  ASP ASP G . n 
G 3 94  GLY 94  93  93  GLY GLY G . n 
G 3 95  VAL 95  94  94  VAL VAL G . n 
G 3 96  ALA 96  95  95  ALA ALA G . n 
G 3 97  ASP 97  96  96  ASP ASP G . n 
G 3 98  VAL 98  97  97  VAL VAL G . n 
G 3 99  SER 99  98  98  SER SER G . n 
G 3 100 ILE 100 99  99  ILE ILE G . n 
G 3 101 GLU 101 100 100 GLU GLU G . n 
G 3 102 ASP 102 101 101 ASP ASP G . n 
G 3 103 SER 103 102 102 SER SER G . n 
G 3 104 VAL 104 103 103 VAL VAL G . n 
G 3 105 ILE 105 104 104 ILE ILE G . n 
G 3 106 SER 106 105 105 SER SER G . n 
G 3 107 LEU 107 106 106 LEU LEU G . n 
G 3 108 SER 108 107 107 SER SER G . n 
G 3 109 GLY 109 108 108 GLY GLY G . n 
G 3 110 ASP 110 109 109 ASP ASP G . n 
G 3 111 HIS 111 110 110 HIS HIS G . n 
G 3 112 CYS 112 111 111 CYS CYS G . n 
G 3 113 ILE 113 112 112 ILE ILE G . n 
G 3 114 ILE 114 113 113 ILE ILE G . n 
G 3 115 GLY 115 114 114 GLY GLY G . n 
G 3 116 ARG 116 115 115 ARG ARG G . n 
G 3 117 THR 117 116 116 THR THR G . n 
G 3 118 LEU 118 117 117 LEU LEU G . n 
G 3 119 VAL 119 118 118 VAL VAL G . n 
G 3 120 VAL 120 119 119 VAL VAL G . n 
G 3 121 HIS 121 120 120 HIS HIS G . n 
G 3 122 GLU 122 121 121 GLU GLU G . n 
G 3 123 LYS 123 122 122 LYS LYS G . n 
G 3 124 ALA 124 123 123 ALA ALA G . n 
G 3 125 ASP 125 124 124 ASP ASP G . n 
G 3 126 ASP 126 125 125 ASP ALA G . n 
G 3 127 LEU 127 126 126 LEU ALA G . n 
G 3 128 GLY 128 127 127 GLY GLY G . n 
G 3 129 LYS 129 128 128 LYS ALA G . n 
G 3 130 GLY 130 129 129 GLY ALA G . n 
G 3 131 GLY 131 130 130 GLY ALA G . n 
G 3 132 ASN 132 131 131 ASN ALA G . n 
G 3 133 GLU 133 132 ?   ?   ?   G . n 
G 3 134 GLU 134 133 ?   ?   ?   G . n 
G 3 135 SER 135 134 ?   ?   ?   G . n 
G 3 136 THR 136 135 ?   ?   ?   G . n 
G 3 137 LYS 137 136 ?   ?   ?   G . n 
G 3 138 THR 138 137 ?   ?   ?   G . n 
G 3 139 GLY 139 138 ?   ?   ?   G . n 
G 3 140 ASN 140 139 ?   ?   ?   G . n 
G 3 141 ALA 141 140 ?   ?   ?   G . n 
G 3 142 GLY 142 141 141 GLY GLY G . n 
G 3 143 SER 143 142 142 SER SER G . n 
G 3 144 ARG 144 143 143 ARG ARG G . n 
G 3 145 LEU 145 144 144 LEU LEU G . n 
G 3 146 ALA 146 145 145 ALA ALA G . n 
G 3 147 CYS 147 146 146 CYS CYS G . n 
G 3 148 GLY 148 147 147 GLY GLY G . n 
G 3 149 VAL 149 148 148 VAL VAL G . n 
G 3 150 ILE 150 149 149 ILE ILE G . n 
G 3 151 GLY 151 150 150 GLY GLY G . n 
G 3 152 ILE 152 151 151 ILE ILE G . n 
G 3 153 ALA 153 152 152 ALA ALA G . n 
G 3 154 GLN 154 153 153 GLN GLN G . n 
H 4 1   ALA 1   1   1   ALA ALA H . n 
H 4 2   THR 2   2   2   THR THR H . n 
H 4 3   LYS 3   3   3   LYS LYS H . n 
H 4 4   ALA 4   4   4   ALA ALA H . n 
H 4 5   VAL 5   5   5   VAL VAL H . n 
H 4 6   CYS 6   6   6   CYS CYS H . n 
H 4 7   VAL 7   7   7   VAL VAL H . n 
H 4 8   LEU 8   8   8   LEU LEU H . n 
H 4 9   LYS 9   9   9   LYS LYS H . n 
H 4 10  GLY 10  10  10  GLY GLY H . n 
H 4 11  ASP 11  11  11  ASP ASP H . n 
H 4 12  GLY 12  12  12  GLY GLY H . n 
H 4 13  PRO 13  13  13  PRO PRO H . n 
H 4 14  VAL 14  14  14  VAL VAL H . n 
H 4 15  GLN 15  15  15  GLN GLN H . n 
H 4 16  GLY 16  16  16  GLY GLY H . n 
H 4 17  ILE 17  17  17  ILE ILE H . n 
H 4 18  ILE 18  18  18  ILE ILE H . n 
H 4 19  ASN 19  19  19  ASN ASN H . n 
H 4 20  PHE 20  20  20  PHE PHE H . n 
H 4 21  GLU 21  21  21  GLU GLU H . n 
H 4 22  GLN 22  22  22  GLN GLN H . n 
H 4 23  LYS 23  23  23  LYS LYS H . n 
H 4 24  GLU 24  24  24  GLU GLU H . n 
H 4 25  SER 25  25  25  SER SER H . n 
H 4 26  ASN 26  26  26  ASN ASN H . n 
H 4 27  GLY 27  27  27  GLY GLY H . n 
H 4 28  PRO 28  28  28  PRO PRO H . n 
H 4 29  VAL 29  29  29  VAL VAL H . n 
H 4 30  LYS 30  30  30  LYS LYS H . n 
H 4 31  VAL 31  31  31  VAL VAL H . n 
H 4 32  TRP 32  32  32  TRP TRP H . n 
H 4 33  GLY 33  33  33  GLY GLY H . n 
H 4 34  SER 34  34  34  SER SER H . n 
H 4 35  ILE 35  35  35  ILE ILE H . n 
H 4 36  LYS 36  36  36  LYS LYS H . n 
H 4 37  GLY 37  37  37  GLY GLY H . n 
H 4 38  LEU 38  38  38  LEU LEU H . n 
H 4 39  THR 39  39  39  THR THR H . n 
H 4 40  GLU 40  40  40  GLU GLU H . n 
H 4 41  GLY 41  41  41  GLY GLY H . n 
H 4 42  LEU 42  42  42  LEU LEU H . n 
H 4 43  HIS 43  43  43  HIS HIS H . n 
H 4 44  GLY 44  44  44  GLY GLY H . n 
H 4 45  PHE 45  45  45  PHE PHE H . n 
H 4 46  HIS 46  46  46  HIS HIS H . n 
H 4 47  VAL 47  47  47  VAL VAL H . n 
H 4 48  HIS 48  48  48  HIS HIS H . n 
H 4 49  GLU 49  49  49  GLU GLU H . n 
H 4 50  PHE 50  50  50  PHE PHE H . n 
H 4 51  GLY 51  51  51  GLY GLY H . n 
H 4 52  ASP 52  52  52  ASP ASP H . n 
H 4 53  ASN 53  53  53  ASN ASN H . n 
H 4 54  THR 54  54  54  THR THR H . n 
H 4 55  ALA 55  55  55  ALA ALA H . n 
H 4 56  GLY 56  56  56  GLY GLY H . n 
H 4 57  CYS 57  57  57  CYS CYS H . n 
H 4 58  THR 58  58  58  THR THR H . n 
H 4 59  SER 59  59  59  SER SER H . n 
H 4 60  ALA 60  60  60  ALA ALA H . n 
H 4 61  GLY 61  61  61  GLY GLY H . n 
H 4 62  PRO 62  62  62  PRO PRO H . n 
H 4 63  HIS 63  63  63  HIS HIS H . n 
H 4 64  PHE 64  64  64  PHE PHE H . n 
H 4 65  ASN 65  65  65  ASN ASN H . n 
H 4 66  PRO 66  66  66  PRO PRO H . n 
H 4 67  LEU 67  67  67  LEU LEU H . n 
H 4 68  SER 68  68  68  SER SER H . n 
H 4 69  ARG 69  69  69  ARG ARG H . n 
H 4 70  LYS 70  70  70  LYS LYS H . n 
H 4 71  HIS 71  71  71  HIS HIS H . n 
H 4 72  GLY 72  72  72  GLY GLY H . n 
H 4 73  GLY 73  73  73  GLY GLY H . n 
H 4 74  PRO 74  74  74  PRO PRO H . n 
H 4 75  LYS 75  75  75  LYS LYS H . n 
H 4 76  ASP 76  76  76  ASP ASP H . n 
H 4 77  GLU 77  77  77  GLU GLU H . n 
H 4 78  GLU 78  78  78  GLU GLU H . n 
H 4 79  ARG 79  79  79  ARG ARG H . n 
H 4 80  HIS 80  80  80  HIS HIS H . n 
H 4 81  VAL 81  81  81  VAL VAL H . n 
H 4 82  GLY 82  82  82  GLY GLY H . n 
H 4 83  ASP 83  83  83  ASP ASP H . n 
H 4 84  LEU 84  84  84  LEU LEU H . n 
H 4 85  GLY 85  85  85  GLY GLY H . n 
H 4 86  ASN 86  86  86  ASN ASN H . n 
H 4 87  VAL 87  87  87  VAL VAL H . n 
H 4 88  THR 88  88  88  THR THR H . n 
H 4 89  ALA 89  89  89  ALA ALA H . n 
H 4 90  ASP 90  90  90  ASP ASP H . n 
H 4 91  LYS 91  91  91  LYS LYS H . n 
H 4 92  ASP 92  92  92  ASP ASP H . n 
H 4 93  GLY 93  93  93  GLY GLY H . n 
H 4 94  VAL 94  94  94  VAL VAL H . n 
H 4 95  ALA 95  95  95  ALA ALA H . n 
H 4 96  ASP 96  96  96  ASP ASP H . n 
H 4 97  VAL 97  97  97  VAL VAL H . n 
H 4 98  SER 98  98  98  SER SER H . n 
H 4 99  ILE 99  99  99  ILE ILE H . n 
H 4 100 GLU 100 100 100 GLU GLU H . n 
H 4 101 ASP 101 101 101 ASP ASP H . n 
H 4 102 SER 102 102 102 SER SER H . n 
H 4 103 VAL 103 103 103 VAL VAL H . n 
H 4 104 ILE 104 104 104 ILE ILE H . n 
H 4 105 SER 105 105 105 SER SER H . n 
H 4 106 LEU 106 106 106 LEU LEU H . n 
H 4 107 SER 107 107 107 SER SER H . n 
H 4 108 GLY 108 108 108 GLY GLY H . n 
H 4 109 ASP 109 109 109 ASP ASP H . n 
H 4 110 HIS 110 110 110 HIS HIS H . n 
H 4 111 CYS 111 111 111 CYS CYS H . n 
H 4 112 ILE 112 112 112 ILE ILE H . n 
H 4 113 ILE 113 113 113 ILE ILE H . n 
H 4 114 GLY 114 114 114 GLY GLY H . n 
H 4 115 ARG 115 115 115 ARG ARG H . n 
H 4 116 THR 116 116 116 THR THR H . n 
H 4 117 LEU 117 117 117 LEU LEU H . n 
H 4 118 VAL 118 118 118 VAL VAL H . n 
H 4 119 VAL 119 119 119 VAL VAL H . n 
H 4 120 HIS 120 120 120 HIS HIS H . n 
H 4 121 GLU 121 121 121 GLU GLU H . n 
H 4 122 LYS 122 122 122 LYS LYS H . n 
H 4 123 ALA 123 123 123 ALA ALA H . n 
H 4 124 ASP 124 124 124 ASP ASP H . n 
H 4 125 ASP 125 125 125 ASP ASP H . n 
H 4 126 LEU 126 126 126 LEU LEU H . n 
H 4 127 GLY 127 127 127 GLY GLY H . n 
H 4 128 LYS 128 128 128 LYS LYS H . n 
H 4 129 GLY 129 129 129 GLY GLY H . n 
H 4 130 GLY 130 130 130 GLY GLY H . n 
H 4 131 ASN 131 131 131 ASN ASN H . n 
H 4 132 GLU 132 132 132 GLU GLU H . n 
H 4 133 GLU 133 133 133 GLU GLU H . n 
H 4 134 SER 134 134 134 SER SER H . n 
H 4 135 THR 135 135 135 THR THR H . n 
H 4 136 LYS 136 136 136 LYS LYS H . n 
H 4 137 THR 137 137 137 THR THR H . n 
H 4 138 GLY 138 138 138 GLY GLY H . n 
H 4 139 ASN 139 139 139 ASN ASN H . n 
H 4 140 ALA 140 140 140 ALA ALA H . n 
H 4 141 GLY 141 141 141 GLY GLY H . n 
H 4 142 SER 142 142 142 SER SER H . n 
H 4 143 ARG 143 143 143 ARG ARG H . n 
H 4 144 LEU 144 144 144 LEU LEU H . n 
H 4 145 ALA 145 145 145 ALA ALA H . n 
H 4 146 CYS 146 146 146 CYS CYS H . n 
H 4 147 GLY 147 147 147 GLY GLY H . n 
H 4 148 VAL 148 148 148 VAL VAL H . n 
H 4 149 ILE 149 149 149 ILE ILE H . n 
H 4 150 GLY 150 150 150 GLY GLY H . n 
H 4 151 ILE 151 151 151 ILE ILE H . n 
H 4 152 ALA 152 152 152 ALA ALA H . n 
H 4 153 ALA 153 153 153 ALA ALA H . n 
I 1 1   MET 1   0   0   MET MET I . n 
I 1 2   ALA 2   1   1   ALA ALA I . n 
I 1 3   THR 3   2   2   THR THR I . n 
I 1 4   LYS 4   3   3   LYS LYS I . n 
I 1 5   ALA 5   4   4   ALA ALA I . n 
I 1 6   VAL 6   5   5   VAL VAL I . n 
I 1 7   CYS 7   6   6   CYS CYS I . n 
I 1 8   VAL 8   7   7   VAL VAL I . n 
I 1 9   LEU 9   8   8   LEU LEU I . n 
I 1 10  LYS 10  9   9   LYS LYS I . n 
I 1 11  GLY 11  10  10  GLY GLY I . n 
I 1 12  ASP 12  11  11  ASP ASP I . n 
I 1 13  GLY 13  12  12  GLY GLY I . n 
I 1 14  PRO 14  13  13  PRO PRO I . n 
I 1 15  VAL 15  14  14  VAL VAL I . n 
I 1 16  GLN 16  15  15  GLN GLN I . n 
I 1 17  GLY 17  16  16  GLY GLY I . n 
I 1 18  ILE 18  17  17  ILE ILE I . n 
I 1 19  ILE 19  18  18  ILE ILE I . n 
I 1 20  ASN 20  19  19  ASN ASN I . n 
I 1 21  PHE 21  20  20  PHE PHE I . n 
I 1 22  GLU 22  21  21  GLU GLU I . n 
I 1 23  GLN 23  22  22  GLN GLN I . n 
I 1 24  LYS 24  23  23  LYS LYS I . n 
I 1 25  GLU 25  24  24  GLU GLU I . n 
I 1 26  SER 26  25  25  SER SER I . n 
I 1 27  ASN 27  26  26  ASN ASN I . n 
I 1 28  GLY 28  27  27  GLY GLY I . n 
I 1 29  PRO 29  28  28  PRO PRO I . n 
I 1 30  VAL 30  29  29  VAL VAL I . n 
I 1 31  LYS 31  30  30  LYS LYS I . n 
I 1 32  VAL 32  31  31  VAL VAL I . n 
I 1 33  TRP 33  32  32  TRP TRP I . n 
I 1 34  GLY 34  33  33  GLY GLY I . n 
I 1 35  SER 35  34  34  SER SER I . n 
I 1 36  ILE 36  35  35  ILE ILE I . n 
I 1 37  LYS 37  36  36  LYS LYS I . n 
I 1 38  GLY 38  37  37  GLY GLY I . n 
I 1 39  LEU 39  38  38  LEU LEU I . n 
I 1 40  THR 40  39  39  THR THR I . n 
I 1 41  GLU 41  40  40  GLU GLU I . n 
I 1 42  GLY 42  41  41  GLY GLY I . n 
I 1 43  LEU 43  42  42  LEU LEU I . n 
I 1 44  HIS 44  43  43  HIS HIS I . n 
I 1 45  GLY 45  44  44  GLY GLY I . n 
I 1 46  PHE 46  45  45  PHE PHE I . n 
I 1 47  HIS 47  46  46  HIS HIS I . n 
I 1 48  VAL 48  47  47  VAL VAL I . n 
I 1 49  HIS 49  48  48  HIS HIS I . n 
I 1 50  GLU 50  49  49  GLU GLU I . n 
I 1 51  PHE 51  50  50  PHE PHE I . n 
I 1 52  GLY 52  51  51  GLY GLY I . n 
I 1 53  ASP 53  52  52  ASP ASP I . n 
I 1 54  ASN 54  53  53  ASN ASN I . n 
I 1 55  THR 55  54  54  THR THR I . n 
I 1 56  ALA 56  55  55  ALA ALA I . n 
I 1 57  GLY 57  56  56  GLY GLY I . n 
I 1 58  CYS 58  57  57  CYS CYS I . n 
I 1 59  THR 59  58  58  THR THR I . n 
I 1 60  SER 60  59  59  SER SER I . n 
I 1 61  ALA 61  60  60  ALA ALA I . n 
I 1 62  GLY 62  61  61  GLY GLY I . n 
I 1 63  PRO 63  62  62  PRO PRO I . n 
I 1 64  HIS 64  63  63  HIS HIS I . n 
I 1 65  PHE 65  64  64  PHE PHE I . n 
I 1 66  ASN 66  65  65  ASN ASN I . n 
I 1 67  PRO 67  66  66  PRO PRO I . n 
I 1 68  LEU 68  67  67  LEU LEU I . n 
I 1 69  SER 69  68  68  SER SER I . n 
I 1 70  ARG 70  69  69  ARG ARG I . n 
I 1 71  LYS 71  70  70  LYS LYS I . n 
I 1 72  HIS 72  71  71  HIS HIS I . n 
I 1 73  GLY 73  72  72  GLY GLY I . n 
I 1 74  GLY 74  73  73  GLY GLY I . n 
I 1 75  PRO 75  74  74  PRO PRO I . n 
I 1 76  LYS 76  75  75  LYS LYS I . n 
I 1 77  ASP 77  76  76  ASP ASP I . n 
I 1 78  GLU 78  77  77  GLU GLU I . n 
I 1 79  GLU 79  78  78  GLU GLU I . n 
I 1 80  ARG 80  79  79  ARG ARG I . n 
I 1 81  HIS 81  80  80  HIS HIS I . n 
I 1 82  VAL 82  81  81  VAL VAL I . n 
I 1 83  GLY 83  82  82  GLY GLY I . n 
I 1 84  ASP 84  83  83  ASP ASP I . n 
I 1 85  LEU 85  84  84  LEU LEU I . n 
I 1 86  GLY 86  85  85  GLY GLY I . n 
I 1 87  ASN 87  86  86  ASN ASN I . n 
I 1 88  VAL 88  87  87  VAL VAL I . n 
I 1 89  THR 89  88  88  THR THR I . n 
I 1 90  ALA 90  89  89  ALA ALA I . n 
I 1 91  ASP 91  90  90  ASP ASP I . n 
I 1 92  LYS 92  91  91  LYS LYS I . n 
I 1 93  ASP 93  92  92  ASP ASP I . n 
I 1 94  GLY 94  93  93  GLY GLY I . n 
I 1 95  VAL 95  94  94  VAL VAL I . n 
I 1 96  ALA 96  95  95  ALA ALA I . n 
I 1 97  ASP 97  96  96  ASP ASP I . n 
I 1 98  VAL 98  97  97  VAL VAL I . n 
I 1 99  SER 99  98  98  SER SER I . n 
I 1 100 ILE 100 99  99  ILE ILE I . n 
I 1 101 GLU 101 100 100 GLU GLU I . n 
I 1 102 ASP 102 101 101 ASP ASP I . n 
I 1 103 SER 103 102 102 SER SER I . n 
I 1 104 VAL 104 103 103 VAL VAL I . n 
I 1 105 ILE 105 104 104 ILE ILE I . n 
I 1 106 SER 106 105 105 SER SER I . n 
I 1 107 LEU 107 106 106 LEU LEU I . n 
I 1 108 SER 108 107 107 SER SER I . n 
I 1 109 GLY 109 108 108 GLY GLY I . n 
I 1 110 ASP 110 109 109 ASP ASP I . n 
I 1 111 HIS 111 110 110 HIS HIS I . n 
I 1 112 CYS 112 111 111 CYS CYS I . n 
I 1 113 ILE 113 112 112 ILE ILE I . n 
I 1 114 ILE 114 113 113 ILE ILE I . n 
I 1 115 GLY 115 114 114 GLY GLY I . n 
I 1 116 ARG 116 115 115 ARG ARG I . n 
I 1 117 THR 117 116 116 THR THR I . n 
I 1 118 LEU 118 117 117 LEU LEU I . n 
I 1 119 VAL 119 118 118 VAL VAL I . n 
I 1 120 VAL 120 119 119 VAL VAL I . n 
I 1 121 HIS 121 120 120 HIS HIS I . n 
I 1 122 GLU 122 121 121 GLU GLU I . n 
I 1 123 LYS 123 122 122 LYS LYS I . n 
I 1 124 ALA 124 123 123 ALA ALA I . n 
I 1 125 ASP 125 124 124 ASP ASP I . n 
I 1 126 ASP 126 125 125 ASP ASP I . n 
I 1 127 LEU 127 126 126 LEU LEU I . n 
I 1 128 GLY 128 127 127 GLY GLY I . n 
I 1 129 LYS 129 128 128 LYS LYS I . n 
I 1 130 GLY 130 129 129 GLY GLY I . n 
I 1 131 GLY 131 130 130 GLY GLY I . n 
I 1 132 ASN 132 131 131 ASN ASN I . n 
I 1 133 GLU 133 132 132 GLU GLU I . n 
I 1 134 GLU 134 133 133 GLU GLU I . n 
I 1 135 SER 135 134 134 SER SER I . n 
I 1 136 THR 136 135 135 THR THR I . n 
I 1 137 LYS 137 136 136 LYS LYS I . n 
I 1 138 THR 138 137 137 THR THR I . n 
I 1 139 GLY 139 138 138 GLY GLY I . n 
I 1 140 ASN 140 139 139 ASN ASN I . n 
I 1 141 ALA 141 140 140 ALA ALA I . n 
I 1 142 GLY 142 141 141 GLY GLY I . n 
I 1 143 SER 143 142 142 SER SER I . n 
I 1 144 ARG 144 143 143 ARG ARG I . n 
I 1 145 LEU 145 144 144 LEU LEU I . n 
I 1 146 ALA 146 145 145 ALA ALA I . n 
I 1 147 CYS 147 146 146 CYS CYS I . n 
I 1 148 GLY 148 147 147 GLY GLY I . n 
I 1 149 VAL 149 148 148 VAL VAL I . n 
I 1 150 ILE 150 149 149 ILE ILE I . n 
I 1 151 GLY 151 150 150 GLY GLY I . n 
I 1 152 ILE 152 151 151 ILE ILE I . n 
I 1 153 ALA 153 152 152 ALA ALA I . n 
I 1 154 GLN 154 153 153 GLN GLN I . n 
J 1 1   MET 1   0   0   MET MET J . n 
J 1 2   ALA 2   1   1   ALA ALA J . n 
J 1 3   THR 3   2   2   THR THR J . n 
J 1 4   LYS 4   3   3   LYS LYS J . n 
J 1 5   ALA 5   4   4   ALA ALA J . n 
J 1 6   VAL 6   5   5   VAL VAL J . n 
J 1 7   CYS 7   6   6   CYS CYS J . n 
J 1 8   VAL 8   7   7   VAL VAL J . n 
J 1 9   LEU 9   8   8   LEU LEU J . n 
J 1 10  LYS 10  9   9   LYS LYS J . n 
J 1 11  GLY 11  10  10  GLY GLY J . n 
J 1 12  ASP 12  11  11  ASP ASP J . n 
J 1 13  GLY 13  12  12  GLY GLY J . n 
J 1 14  PRO 14  13  13  PRO PRO J . n 
J 1 15  VAL 15  14  14  VAL VAL J . n 
J 1 16  GLN 16  15  15  GLN GLN J . n 
J 1 17  GLY 17  16  16  GLY GLY J . n 
J 1 18  ILE 18  17  17  ILE ILE J . n 
J 1 19  ILE 19  18  18  ILE ILE J . n 
J 1 20  ASN 20  19  19  ASN ASN J . n 
J 1 21  PHE 21  20  20  PHE PHE J . n 
J 1 22  GLU 22  21  21  GLU GLU J . n 
J 1 23  GLN 23  22  22  GLN GLN J . n 
J 1 24  LYS 24  23  23  LYS LYS J . n 
J 1 25  GLU 25  24  24  GLU GLU J . n 
J 1 26  SER 26  25  25  SER SER J . n 
J 1 27  ASN 27  26  26  ASN ASN J . n 
J 1 28  GLY 28  27  27  GLY GLY J . n 
J 1 29  PRO 29  28  28  PRO PRO J . n 
J 1 30  VAL 30  29  29  VAL VAL J . n 
J 1 31  LYS 31  30  30  LYS LYS J . n 
J 1 32  VAL 32  31  31  VAL VAL J . n 
J 1 33  TRP 33  32  32  TRP TRP J . n 
J 1 34  GLY 34  33  33  GLY GLY J . n 
J 1 35  SER 35  34  34  SER SER J . n 
J 1 36  ILE 36  35  35  ILE ILE J . n 
J 1 37  LYS 37  36  36  LYS LYS J . n 
J 1 38  GLY 38  37  37  GLY GLY J . n 
J 1 39  LEU 39  38  38  LEU LEU J . n 
J 1 40  THR 40  39  39  THR THR J . n 
J 1 41  GLU 41  40  40  GLU GLU J . n 
J 1 42  GLY 42  41  41  GLY GLY J . n 
J 1 43  LEU 43  42  42  LEU LEU J . n 
J 1 44  HIS 44  43  43  HIS HIS J . n 
J 1 45  GLY 45  44  44  GLY GLY J . n 
J 1 46  PHE 46  45  45  PHE PHE J . n 
J 1 47  HIS 47  46  46  HIS HIS J . n 
J 1 48  VAL 48  47  47  VAL VAL J . n 
J 1 49  HIS 49  48  48  HIS HIS J . n 
J 1 50  GLU 50  49  49  GLU GLU J . n 
J 1 51  PHE 51  50  50  PHE PHE J . n 
J 1 52  GLY 52  51  51  GLY GLY J . n 
J 1 53  ASP 53  52  52  ASP ASP J . n 
J 1 54  ASN 54  53  53  ASN ASN J . n 
J 1 55  THR 55  54  54  THR THR J . n 
J 1 56  ALA 56  55  55  ALA ALA J . n 
J 1 57  GLY 57  56  56  GLY GLY J . n 
J 1 58  CYS 58  57  57  CYS CYS J . n 
J 1 59  THR 59  58  58  THR THR J . n 
J 1 60  SER 60  59  59  SER SER J . n 
J 1 61  ALA 61  60  60  ALA ALA J . n 
J 1 62  GLY 62  61  61  GLY GLY J . n 
J 1 63  PRO 63  62  62  PRO PRO J . n 
J 1 64  HIS 64  63  63  HIS HIS J . n 
J 1 65  PHE 65  64  64  PHE PHE J . n 
J 1 66  ASN 66  65  65  ASN ASN J . n 
J 1 67  PRO 67  66  66  PRO PRO J . n 
J 1 68  LEU 68  67  67  LEU LEU J . n 
J 1 69  SER 69  68  68  SER SER J . n 
J 1 70  ARG 70  69  69  ARG ARG J . n 
J 1 71  LYS 71  70  70  LYS LYS J . n 
J 1 72  HIS 72  71  71  HIS HIS J . n 
J 1 73  GLY 73  72  72  GLY GLY J . n 
J 1 74  GLY 74  73  73  GLY GLY J . n 
J 1 75  PRO 75  74  74  PRO PRO J . n 
J 1 76  LYS 76  75  75  LYS LYS J . n 
J 1 77  ASP 77  76  76  ASP ASP J . n 
J 1 78  GLU 78  77  77  GLU GLU J . n 
J 1 79  GLU 79  78  78  GLU GLU J . n 
J 1 80  ARG 80  79  79  ARG ARG J . n 
J 1 81  HIS 81  80  80  HIS HIS J . n 
J 1 82  VAL 82  81  81  VAL VAL J . n 
J 1 83  GLY 83  82  82  GLY GLY J . n 
J 1 84  ASP 84  83  83  ASP ASP J . n 
J 1 85  LEU 85  84  84  LEU LEU J . n 
J 1 86  GLY 86  85  85  GLY GLY J . n 
J 1 87  ASN 87  86  86  ASN ASN J . n 
J 1 88  VAL 88  87  87  VAL VAL J . n 
J 1 89  THR 89  88  88  THR THR J . n 
J 1 90  ALA 90  89  89  ALA ALA J . n 
J 1 91  ASP 91  90  90  ASP ASP J . n 
J 1 92  LYS 92  91  91  LYS LYS J . n 
J 1 93  ASP 93  92  92  ASP ASP J . n 
J 1 94  GLY 94  93  93  GLY GLY J . n 
J 1 95  VAL 95  94  94  VAL VAL J . n 
J 1 96  ALA 96  95  95  ALA ALA J . n 
J 1 97  ASP 97  96  96  ASP ASP J . n 
J 1 98  VAL 98  97  97  VAL VAL J . n 
J 1 99  SER 99  98  98  SER SER J . n 
J 1 100 ILE 100 99  99  ILE ILE J . n 
J 1 101 GLU 101 100 100 GLU GLU J . n 
J 1 102 ASP 102 101 101 ASP ASP J . n 
J 1 103 SER 103 102 102 SER SER J . n 
J 1 104 VAL 104 103 103 VAL VAL J . n 
J 1 105 ILE 105 104 104 ILE ILE J . n 
J 1 106 SER 106 105 105 SER SER J . n 
J 1 107 LEU 107 106 106 LEU LEU J . n 
J 1 108 SER 108 107 107 SER SER J . n 
J 1 109 GLY 109 108 108 GLY GLY J . n 
J 1 110 ASP 110 109 109 ASP ASP J . n 
J 1 111 HIS 111 110 110 HIS HIS J . n 
J 1 112 CYS 112 111 111 CYS CYS J . n 
J 1 113 ILE 113 112 112 ILE ILE J . n 
J 1 114 ILE 114 113 113 ILE ILE J . n 
J 1 115 GLY 115 114 114 GLY GLY J . n 
J 1 116 ARG 116 115 115 ARG ARG J . n 
J 1 117 THR 117 116 116 THR THR J . n 
J 1 118 LEU 118 117 117 LEU LEU J . n 
J 1 119 VAL 119 118 118 VAL VAL J . n 
J 1 120 VAL 120 119 119 VAL VAL J . n 
J 1 121 HIS 121 120 120 HIS HIS J . n 
J 1 122 GLU 122 121 121 GLU GLU J . n 
J 1 123 LYS 123 122 122 LYS LYS J . n 
J 1 124 ALA 124 123 123 ALA ALA J . n 
J 1 125 ASP 125 124 124 ASP ASP J . n 
J 1 126 ASP 126 125 125 ASP ASP J . n 
J 1 127 LEU 127 126 126 LEU LEU J . n 
J 1 128 GLY 128 127 127 GLY GLY J . n 
J 1 129 LYS 129 128 128 LYS LYS J . n 
J 1 130 GLY 130 129 129 GLY GLY J . n 
J 1 131 GLY 131 130 130 GLY GLY J . n 
J 1 132 ASN 132 131 131 ASN ASN J . n 
J 1 133 GLU 133 132 132 GLU GLU J . n 
J 1 134 GLU 134 133 133 GLU GLU J . n 
J 1 135 SER 135 134 134 SER SER J . n 
J 1 136 THR 136 135 135 THR THR J . n 
J 1 137 LYS 137 136 136 LYS LYS J . n 
J 1 138 THR 138 137 137 THR THR J . n 
J 1 139 GLY 139 138 138 GLY GLY J . n 
J 1 140 ASN 140 139 139 ASN ASN J . n 
J 1 141 ALA 141 140 140 ALA ALA J . n 
J 1 142 GLY 142 141 141 GLY GLY J . n 
J 1 143 SER 143 142 142 SER SER J . n 
J 1 144 ARG 144 143 143 ARG ARG J . n 
J 1 145 LEU 145 144 144 LEU LEU J . n 
J 1 146 ALA 146 145 145 ALA ALA J . n 
J 1 147 CYS 147 146 146 CYS CYS J . n 
J 1 148 GLY 148 147 147 GLY GLY J . n 
J 1 149 VAL 149 148 148 VAL VAL J . n 
J 1 150 ILE 150 149 149 ILE ILE J . n 
J 1 151 GLY 151 150 150 GLY GLY J . n 
J 1 152 ILE 152 151 151 ILE ILE J . n 
J 1 153 ALA 153 152 152 ALA ALA J . n 
J 1 154 GLN 154 153 153 GLN GLN J . n 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              balapaddy@gmail.com 
_pdbx_contact_author.name_first         Balasundaram 
_pdbx_contact_author.name_last          Padmanabhan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8434-828X 
# 
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 
K  5 ZN  1   201 201 ZN  ZN  A . 
L  6 GOL 1   202 203 GOL GOL A . 
M  5 ZN  1   201 201 ZN  ZN  B . 
N  6 GOL 1   202 301 GOL GOL B . 
O  5 ZN  1   201 201 ZN  ZN  C . 
P  6 GOL 1   202 202 GOL GOL C . 
Q  5 ZN  1   201 201 ZN  ZN  D . 
R  6 GOL 1   202 301 GOL GOL D . 
S  5 ZN  1   201 201 ZN  ZN  E . 
T  6 GOL 1   202 301 GOL GOL E . 
U  5 ZN  1   201 201 ZN  ZN  F . 
V  6 GOL 1   202 301 GOL GOL F . 
W  5 ZN  1   201 201 ZN  ZN  H . 
X  7 K4I 1   202 301 K4I PLE H . 
Y  5 ZN  1   201 201 ZN  ZN  I . 
Z  5 ZN  1   201 201 ZN  ZN  J . 
AA 8 HOH 1   301 471 HOH HOH A . 
AA 8 HOH 2   302 748 HOH HOH A . 
AA 8 HOH 3   303 161 HOH HOH A . 
AA 8 HOH 4   304 221 HOH HOH A . 
AA 8 HOH 5   305 440 HOH HOH A . 
AA 8 HOH 6   306 457 HOH HOH A . 
AA 8 HOH 7   307 236 HOH HOH A . 
AA 8 HOH 8   308 259 HOH HOH A . 
AA 8 HOH 9   309 502 HOH HOH A . 
AA 8 HOH 10  310 275 HOH HOH A . 
AA 8 HOH 11  311 75  HOH HOH A . 
AA 8 HOH 12  312 213 HOH HOH A . 
AA 8 HOH 13  313 190 HOH HOH A . 
AA 8 HOH 14  314 132 HOH HOH A . 
AA 8 HOH 15  315 52  HOH HOH A . 
AA 8 HOH 16  316 752 HOH HOH A . 
AA 8 HOH 17  317 356 HOH HOH A . 
AA 8 HOH 18  318 777 HOH HOH A . 
AA 8 HOH 19  319 363 HOH HOH A . 
AA 8 HOH 20  320 40  HOH HOH A . 
AA 8 HOH 21  321 268 HOH HOH A . 
AA 8 HOH 22  322 205 HOH HOH A . 
AA 8 HOH 23  323 453 HOH HOH A . 
AA 8 HOH 24  324 50  HOH HOH A . 
AA 8 HOH 25  325 702 HOH HOH A . 
AA 8 HOH 26  326 151 HOH HOH A . 
AA 8 HOH 27  327 178 HOH HOH A . 
AA 8 HOH 28  328 61  HOH HOH A . 
AA 8 HOH 29  329 322 HOH HOH A . 
AA 8 HOH 30  330 326 HOH HOH A . 
AA 8 HOH 31  331 309 HOH HOH A . 
AA 8 HOH 32  332 307 HOH HOH A . 
AA 8 HOH 33  333 412 HOH HOH A . 
AA 8 HOH 34  334 289 HOH HOH A . 
AA 8 HOH 35  335 462 HOH HOH A . 
AA 8 HOH 36  336 95  HOH HOH A . 
AA 8 HOH 37  337 871 HOH HOH A . 
AA 8 HOH 38  338 146 HOH HOH A . 
AA 8 HOH 39  339 35  HOH HOH A . 
AA 8 HOH 40  340 22  HOH HOH A . 
AA 8 HOH 41  341 397 HOH HOH A . 
AA 8 HOH 42  342 76  HOH HOH A . 
AA 8 HOH 43  343 446 HOH HOH A . 
AA 8 HOH 44  344 137 HOH HOH A . 
AA 8 HOH 45  345 750 HOH HOH A . 
AA 8 HOH 46  346 317 HOH HOH A . 
AA 8 HOH 47  347 755 HOH HOH A . 
AA 8 HOH 48  348 390 HOH HOH A . 
AA 8 HOH 49  349 181 HOH HOH A . 
AA 8 HOH 50  350 108 HOH HOH A . 
AA 8 HOH 51  351 231 HOH HOH A . 
AA 8 HOH 52  352 9   HOH HOH A . 
AA 8 HOH 53  353 743 HOH HOH A . 
AA 8 HOH 54  354 714 HOH HOH A . 
AA 8 HOH 55  355 747 HOH HOH A . 
AA 8 HOH 56  356 546 HOH HOH A . 
AA 8 HOH 57  357 793 HOH HOH A . 
AA 8 HOH 58  358 552 HOH HOH A . 
AA 8 HOH 59  359 55  HOH HOH A . 
AA 8 HOH 60  360 162 HOH HOH A . 
AA 8 HOH 61  361 210 HOH HOH A . 
AA 8 HOH 62  362 856 HOH HOH A . 
AA 8 HOH 63  363 712 HOH HOH A . 
AA 8 HOH 64  364 489 HOH HOH A . 
AA 8 HOH 65  365 851 HOH HOH A . 
AA 8 HOH 66  366 479 HOH HOH A . 
AA 8 HOH 67  367 806 HOH HOH A . 
AA 8 HOH 68  368 481 HOH HOH A . 
AA 8 HOH 69  369 185 HOH HOH A . 
AA 8 HOH 70  370 241 HOH HOH A . 
AA 8 HOH 71  371 395 HOH HOH A . 
AA 8 HOH 72  372 284 HOH HOH A . 
AA 8 HOH 73  373 451 HOH HOH A . 
AA 8 HOH 74  374 809 HOH HOH A . 
AA 8 HOH 75  375 477 HOH HOH A . 
AA 8 HOH 76  376 727 HOH HOH A . 
AA 8 HOH 77  377 354 HOH HOH A . 
AA 8 HOH 78  378 298 HOH HOH A . 
AA 8 HOH 79  379 609 HOH HOH A . 
AA 8 HOH 80  380 544 HOH HOH A . 
AA 8 HOH 81  381 819 HOH HOH A . 
AA 8 HOH 82  382 872 HOH HOH A . 
AA 8 HOH 83  383 776 HOH HOH A . 
AA 8 HOH 84  384 731 HOH HOH A . 
AA 8 HOH 85  385 823 HOH HOH A . 
AA 8 HOH 86  386 709 HOH HOH A . 
AA 8 HOH 87  387 784 HOH HOH A . 
AA 8 HOH 88  388 815 HOH HOH A . 
AA 8 HOH 89  389 857 HOH HOH A . 
AA 8 HOH 90  390 890 HOH HOH A . 
AA 8 HOH 91  391 549 HOH HOH A . 
AA 8 HOH 92  392 386 HOH HOH A . 
AA 8 HOH 93  393 373 HOH HOH A . 
AA 8 HOH 94  394 524 HOH HOH A . 
AA 8 HOH 95  395 545 HOH HOH A . 
AA 8 HOH 96  396 244 HOH HOH A . 
BA 8 HOH 1   301 182 HOH HOH B . 
BA 8 HOH 2   302 285 HOH HOH B . 
BA 8 HOH 3   303 312 HOH HOH B . 
BA 8 HOH 4   304 488 HOH HOH B . 
BA 8 HOH 5   305 474 HOH HOH B . 
BA 8 HOH 6   306 240 HOH HOH B . 
BA 8 HOH 7   307 379 HOH HOH B . 
BA 8 HOH 8   308 349 HOH HOH B . 
BA 8 HOH 9   309 218 HOH HOH B . 
BA 8 HOH 10  310 645 HOH HOH B . 
BA 8 HOH 11  311 672 HOH HOH B . 
BA 8 HOH 12  312 643 HOH HOH B . 
BA 8 HOH 13  313 41  HOH HOH B . 
BA 8 HOH 14  314 124 HOH HOH B . 
BA 8 HOH 15  315 739 HOH HOH B . 
BA 8 HOH 16  316 224 HOH HOH B . 
BA 8 HOH 17  317 458 HOH HOH B . 
BA 8 HOH 18  318 255 HOH HOH B . 
BA 8 HOH 19  319 718 HOH HOH B . 
BA 8 HOH 20  320 13  HOH HOH B . 
BA 8 HOH 21  321 308 HOH HOH B . 
BA 8 HOH 22  322 211 HOH HOH B . 
BA 8 HOH 23  323 105 HOH HOH B . 
BA 8 HOH 24  324 768 HOH HOH B . 
BA 8 HOH 25  325 24  HOH HOH B . 
BA 8 HOH 26  326 67  HOH HOH B . 
BA 8 HOH 27  327 413 HOH HOH B . 
BA 8 HOH 28  328 279 HOH HOH B . 
BA 8 HOH 29  329 636 HOH HOH B . 
BA 8 HOH 30  330 668 HOH HOH B . 
BA 8 HOH 31  331 128 HOH HOH B . 
BA 8 HOH 32  332 665 HOH HOH B . 
BA 8 HOH 33  333 837 HOH HOH B . 
BA 8 HOH 34  334 749 HOH HOH B . 
BA 8 HOH 35  335 873 HOH HOH B . 
BA 8 HOH 36  336 12  HOH HOH B . 
BA 8 HOH 37  337 706 HOH HOH B . 
BA 8 HOH 38  338 442 HOH HOH B . 
BA 8 HOH 39  339 18  HOH HOH B . 
BA 8 HOH 40  340 5   HOH HOH B . 
BA 8 HOH 41  341 85  HOH HOH B . 
BA 8 HOH 42  342 96  HOH HOH B . 
BA 8 HOH 43  343 43  HOH HOH B . 
BA 8 HOH 44  344 265 HOH HOH B . 
BA 8 HOH 45  345 646 HOH HOH B . 
BA 8 HOH 46  346 184 HOH HOH B . 
BA 8 HOH 47  347 676 HOH HOH B . 
BA 8 HOH 48  348 34  HOH HOH B . 
BA 8 HOH 49  349 94  HOH HOH B . 
BA 8 HOH 50  350 53  HOH HOH B . 
BA 8 HOH 51  351 762 HOH HOH B . 
BA 8 HOH 52  352 681 HOH HOH B . 
BA 8 HOH 53  353 666 HOH HOH B . 
BA 8 HOH 54  354 29  HOH HOH B . 
BA 8 HOH 55  355 153 HOH HOH B . 
BA 8 HOH 56  356 697 HOH HOH B . 
BA 8 HOH 57  357 171 HOH HOH B . 
BA 8 HOH 58  358 98  HOH HOH B . 
BA 8 HOH 59  359 711 HOH HOH B . 
BA 8 HOH 60  360 669 HOH HOH B . 
BA 8 HOH 61  361 704 HOH HOH B . 
BA 8 HOH 62  362 527 HOH HOH B . 
BA 8 HOH 63  363 775 HOH HOH B . 
BA 8 HOH 64  364 637 HOH HOH B . 
BA 8 HOH 65  365 372 HOH HOH B . 
BA 8 HOH 66  366 484 HOH HOH B . 
BA 8 HOH 67  367 431 HOH HOH B . 
BA 8 HOH 68  368 119 HOH HOH B . 
BA 8 HOH 69  369 384 HOH HOH B . 
BA 8 HOH 70  370 141 HOH HOH B . 
BA 8 HOH 71  371 902 HOH HOH B . 
BA 8 HOH 72  372 439 HOH HOH B . 
BA 8 HOH 73  373 772 HOH HOH B . 
BA 8 HOH 74  374 642 HOH HOH B . 
BA 8 HOH 75  375 651 HOH HOH B . 
BA 8 HOH 76  376 554 HOH HOH B . 
BA 8 HOH 77  377 682 HOH HOH B . 
BA 8 HOH 78  378 499 HOH HOH B . 
BA 8 HOH 79  379 647 HOH HOH B . 
BA 8 HOH 80  380 123 HOH HOH B . 
BA 8 HOH 81  381 168 HOH HOH B . 
BA 8 HOH 82  382 460 HOH HOH B . 
BA 8 HOH 83  383 603 HOH HOH B . 
BA 8 HOH 84  384 482 HOH HOH B . 
BA 8 HOH 85  385 848 HOH HOH B . 
BA 8 HOH 86  386 916 HOH HOH B . 
BA 8 HOH 87  387 671 HOH HOH B . 
BA 8 HOH 88  388 402 HOH HOH B . 
BA 8 HOH 89  389 798 HOH HOH B . 
BA 8 HOH 90  390 774 HOH HOH B . 
BA 8 HOH 91  391 396 HOH HOH B . 
BA 8 HOH 92  392 560 HOH HOH B . 
BA 8 HOH 93  393 445 HOH HOH B . 
BA 8 HOH 94  394 351 HOH HOH B . 
BA 8 HOH 95  395 845 HOH HOH B . 
BA 8 HOH 96  396 177 HOH HOH B . 
BA 8 HOH 97  397 515 HOH HOH B . 
BA 8 HOH 98  398 710 HOH HOH B . 
BA 8 HOH 99  399 514 HOH HOH B . 
BA 8 HOH 100 400 879 HOH HOH B . 
BA 8 HOH 101 401 839 HOH HOH B . 
BA 8 HOH 102 402 207 HOH HOH B . 
BA 8 HOH 103 403 852 HOH HOH B . 
BA 8 HOH 104 404 432 HOH HOH B . 
BA 8 HOH 105 405 367 HOH HOH B . 
BA 8 HOH 106 406 896 HOH HOH B . 
BA 8 HOH 107 407 371 HOH HOH B . 
BA 8 HOH 108 408 449 HOH HOH B . 
BA 8 HOH 109 409 667 HOH HOH B . 
BA 8 HOH 110 410 903 HOH HOH B . 
BA 8 HOH 111 411 670 HOH HOH B . 
BA 8 HOH 112 412 508 HOH HOH B . 
BA 8 HOH 113 413 644 HOH HOH B . 
BA 8 HOH 114 414 864 HOH HOH B . 
BA 8 HOH 115 415 429 HOH HOH B . 
BA 8 HOH 116 416 880 HOH HOH B . 
BA 8 HOH 117 417 405 HOH HOH B . 
BA 8 HOH 118 418 652 HOH HOH B . 
BA 8 HOH 119 419 370 HOH HOH B . 
BA 8 HOH 120 420 352 HOH HOH B . 
BA 8 HOH 121 421 561 HOH HOH B . 
BA 8 HOH 122 422 653 HOH HOH B . 
BA 8 HOH 123 423 364 HOH HOH B . 
BA 8 HOH 124 424 365 HOH HOH B . 
BA 8 HOH 125 425 106 HOH HOH B . 
BA 8 HOH 126 426 600 HOH HOH B . 
BA 8 HOH 127 427 641 HOH HOH B . 
BA 8 HOH 128 428 648 HOH HOH B . 
BA 8 HOH 129 429 393 HOH HOH B . 
BA 8 HOH 130 430 601 HOH HOH B . 
BA 8 HOH 131 431 650 HOH HOH B . 
BA 8 HOH 132 432 209 HOH HOH B . 
BA 8 HOH 133 433 165 HOH HOH B . 
CA 8 HOH 1   301 577 HOH HOH C . 
CA 8 HOH 2   302 701 HOH HOH C . 
CA 8 HOH 3   303 795 HOH HOH C . 
CA 8 HOH 4   304 574 HOH HOH C . 
CA 8 HOH 5   305 223 HOH HOH C . 
CA 8 HOH 6   306 269 HOH HOH C . 
CA 8 HOH 7   307 509 HOH HOH C . 
CA 8 HOH 8   308 3   HOH HOH C . 
CA 8 HOH 9   309 818 HOH HOH C . 
CA 8 HOH 10  310 261 HOH HOH C . 
CA 8 HOH 11  311 882 HOH HOH C . 
CA 8 HOH 12  312 382 HOH HOH C . 
CA 8 HOH 13  313 328 HOH HOH C . 
CA 8 HOH 14  314 567 HOH HOH C . 
CA 8 HOH 15  315 573 HOH HOH C . 
CA 8 HOH 16  316 495 HOH HOH C . 
CA 8 HOH 17  317 610 HOH HOH C . 
CA 8 HOH 18  318 310 HOH HOH C . 
CA 8 HOH 19  319 794 HOH HOH C . 
CA 8 HOH 20  320 220 HOH HOH C . 
CA 8 HOH 21  321 36  HOH HOH C . 
CA 8 HOH 22  322 329 HOH HOH C . 
CA 8 HOH 23  323 350 HOH HOH C . 
CA 8 HOH 24  324 568 HOH HOH C . 
CA 8 HOH 25  325 624 HOH HOH C . 
CA 8 HOH 26  326 424 HOH HOH C . 
CA 8 HOH 27  327 15  HOH HOH C . 
CA 8 HOH 28  328 126 HOH HOH C . 
CA 8 HOH 29  329 751 HOH HOH C . 
CA 8 HOH 30  330 416 HOH HOH C . 
CA 8 HOH 31  331 331 HOH HOH C . 
CA 8 HOH 32  332 65  HOH HOH C . 
CA 8 HOH 33  333 4   HOH HOH C . 
CA 8 HOH 34  334 375 HOH HOH C . 
CA 8 HOH 35  335 588 HOH HOH C . 
CA 8 HOH 36  336 572 HOH HOH C . 
CA 8 HOH 37  337 707 HOH HOH C . 
CA 8 HOH 38  338 47  HOH HOH C . 
CA 8 HOH 39  339 696 HOH HOH C . 
CA 8 HOH 40  340 900 HOH HOH C . 
CA 8 HOH 41  341 466 HOH HOH C . 
CA 8 HOH 42  342 673 HOH HOH C . 
CA 8 HOH 43  343 737 HOH HOH C . 
CA 8 HOH 44  344 359 HOH HOH C . 
CA 8 HOH 45  345 847 HOH HOH C . 
CA 8 HOH 46  346 579 HOH HOH C . 
CA 8 HOH 47  347 518 HOH HOH C . 
CA 8 HOH 48  348 294 HOH HOH C . 
CA 8 HOH 49  349 133 HOH HOH C . 
CA 8 HOH 50  350 127 HOH HOH C . 
CA 8 HOH 51  351 580 HOH HOH C . 
CA 8 HOH 52  352 72  HOH HOH C . 
CA 8 HOH 53  353 582 HOH HOH C . 
CA 8 HOH 54  354 69  HOH HOH C . 
CA 8 HOH 55  355 435 HOH HOH C . 
CA 8 HOH 56  356 575 HOH HOH C . 
CA 8 HOH 57  357 407 HOH HOH C . 
CA 8 HOH 58  358 612 HOH HOH C . 
CA 8 HOH 59  359 62  HOH HOH C . 
CA 8 HOH 60  360 450 HOH HOH C . 
CA 8 HOH 61  361 583 HOH HOH C . 
CA 8 HOH 62  362 247 HOH HOH C . 
CA 8 HOH 63  363 80  HOH HOH C . 
CA 8 HOH 64  364 103 HOH HOH C . 
CA 8 HOH 65  365 516 HOH HOH C . 
CA 8 HOH 66  366 565 HOH HOH C . 
CA 8 HOH 67  367 433 HOH HOH C . 
CA 8 HOH 68  368 139 HOH HOH C . 
CA 8 HOH 69  369 570 HOH HOH C . 
CA 8 HOH 70  370 91  HOH HOH C . 
CA 8 HOH 71  371 166 HOH HOH C . 
CA 8 HOH 72  372 861 HOH HOH C . 
CA 8 HOH 73  373 277 HOH HOH C . 
CA 8 HOH 74  374 854 HOH HOH C . 
CA 8 HOH 75  375 318 HOH HOH C . 
CA 8 HOH 76  376 700 HOH HOH C . 
CA 8 HOH 77  377 79  HOH HOH C . 
CA 8 HOH 78  378 556 HOH HOH C . 
CA 8 HOH 79  379 708 HOH HOH C . 
CA 8 HOH 80  380 188 HOH HOH C . 
CA 8 HOH 81  381 483 HOH HOH C . 
CA 8 HOH 82  382 571 HOH HOH C . 
CA 8 HOH 83  383 585 HOH HOH C . 
CA 8 HOH 84  384 537 HOH HOH C . 
CA 8 HOH 85  385 533 HOH HOH C . 
CA 8 HOH 86  386 92  HOH HOH C . 
CA 8 HOH 87  387 203 HOH HOH C . 
CA 8 HOH 88  388 905 HOH HOH C . 
CA 8 HOH 89  389 239 HOH HOH C . 
CA 8 HOH 90  390 746 HOH HOH C . 
CA 8 HOH 91  391 530 HOH HOH C . 
CA 8 HOH 92  392 598 HOH HOH C . 
CA 8 HOH 93  393 566 HOH HOH C . 
CA 8 HOH 94  394 842 HOH HOH C . 
CA 8 HOH 95  395 581 HOH HOH C . 
CA 8 HOH 96  396 519 HOH HOH C . 
CA 8 HOH 97  397 888 HOH HOH C . 
CA 8 HOH 98  398 773 HOH HOH C . 
CA 8 HOH 99  399 101 HOH HOH C . 
CA 8 HOH 100 400 780 HOH HOH C . 
CA 8 HOH 101 401 569 HOH HOH C . 
CA 8 HOH 102 402 174 HOH HOH C . 
CA 8 HOH 103 403 417 HOH HOH C . 
CA 8 HOH 104 404 191 HOH HOH C . 
CA 8 HOH 105 405 621 HOH HOH C . 
CA 8 HOH 106 406 186 HOH HOH C . 
CA 8 HOH 107 407 243 HOH HOH C . 
CA 8 HOH 108 408 419 HOH HOH C . 
CA 8 HOH 109 409 528 HOH HOH C . 
CA 8 HOH 110 410 183 HOH HOH C . 
CA 8 HOH 111 411 786 HOH HOH C . 
CA 8 HOH 112 412 816 HOH HOH C . 
CA 8 HOH 113 413 576 HOH HOH C . 
CA 8 HOH 114 414 587 HOH HOH C . 
CA 8 HOH 115 415 909 HOH HOH C . 
CA 8 HOH 116 416 584 HOH HOH C . 
CA 8 HOH 117 417 144 HOH HOH C . 
CA 8 HOH 118 418 291 HOH HOH C . 
CA 8 HOH 119 419 558 HOH HOH C . 
CA 8 HOH 120 420 597 HOH HOH C . 
CA 8 HOH 121 421 229 HOH HOH C . 
CA 8 HOH 122 422 578 HOH HOH C . 
CA 8 HOH 123 423 611 HOH HOH C . 
CA 8 HOH 124 424 978 HOH HOH C . 
CA 8 HOH 125 425 344 HOH HOH C . 
CA 8 HOH 126 426 253 HOH HOH C . 
CA 8 HOH 127 427 199 HOH HOH C . 
CA 8 HOH 128 428 249 HOH HOH C . 
CA 8 HOH 129 429 822 HOH HOH C . 
CA 8 HOH 130 430 157 HOH HOH C . 
CA 8 HOH 131 431 529 HOH HOH C . 
CA 8 HOH 132 432 381 HOH HOH C . 
CA 8 HOH 133 433 254 HOH HOH C . 
CA 8 HOH 134 434 336 HOH HOH C . 
DA 8 HOH 1   301 215 HOH HOH D . 
DA 8 HOH 2   302 830 HOH HOH D . 
DA 8 HOH 3   303 754 HOH HOH D . 
DA 8 HOH 4   304 176 HOH HOH D . 
DA 8 HOH 5   305 201 HOH HOH D . 
DA 8 HOH 6   306 522 HOH HOH D . 
DA 8 HOH 7   307 110 HOH HOH D . 
DA 8 HOH 8   308 843 HOH HOH D . 
DA 8 HOH 9   309 715 HOH HOH D . 
DA 8 HOH 10  310 212 HOH HOH D . 
DA 8 HOH 11  311 391 HOH HOH D . 
DA 8 HOH 12  312 517 HOH HOH D . 
DA 8 HOH 13  313 25  HOH HOH D . 
DA 8 HOH 14  314 260 HOH HOH D . 
DA 8 HOH 15  315 327 HOH HOH D . 
DA 8 HOH 16  316 629 HOH HOH D . 
DA 8 HOH 17  317 409 HOH HOH D . 
DA 8 HOH 18  318 767 HOH HOH D . 
DA 8 HOH 19  319 266 HOH HOH D . 
DA 8 HOH 20  320 378 HOH HOH D . 
DA 8 HOH 21  321 430 HOH HOH D . 
DA 8 HOH 22  322 121 HOH HOH D . 
DA 8 HOH 23  323 788 HOH HOH D . 
DA 8 HOH 24  324 614 HOH HOH D . 
DA 8 HOH 25  325 661 HOH HOH D . 
DA 8 HOH 26  326 31  HOH HOH D . 
DA 8 HOH 27  327 2   HOH HOH D . 
DA 8 HOH 28  328 886 HOH HOH D . 
DA 8 HOH 29  329 156 HOH HOH D . 
DA 8 HOH 30  330 420 HOH HOH D . 
DA 8 HOH 31  331 6   HOH HOH D . 
DA 8 HOH 32  332 228 HOH HOH D . 
DA 8 HOH 33  333 523 HOH HOH D . 
DA 8 HOH 34  334 263 HOH HOH D . 
DA 8 HOH 35  335 377 HOH HOH D . 
DA 8 HOH 36  336 44  HOH HOH D . 
DA 8 HOH 37  337 154 HOH HOH D . 
DA 8 HOH 38  338 292 HOH HOH D . 
DA 8 HOH 39  339 626 HOH HOH D . 
DA 8 HOH 40  340 734 HOH HOH D . 
DA 8 HOH 41  341 781 HOH HOH D . 
DA 8 HOH 42  342 27  HOH HOH D . 
DA 8 HOH 43  343 32  HOH HOH D . 
DA 8 HOH 44  344 492 HOH HOH D . 
DA 8 HOH 45  345 313 HOH HOH D . 
DA 8 HOH 46  346 134 HOH HOH D . 
DA 8 HOH 47  347 487 HOH HOH D . 
DA 8 HOH 48  348 713 HOH HOH D . 
DA 8 HOH 49  349 838 HOH HOH D . 
DA 8 HOH 50  350 758 HOH HOH D . 
DA 8 HOH 51  351 361 HOH HOH D . 
DA 8 HOH 52  352 21  HOH HOH D . 
DA 8 HOH 53  353 20  HOH HOH D . 
DA 8 HOH 54  354 71  HOH HOH D . 
DA 8 HOH 55  355 472 HOH HOH D . 
DA 8 HOH 56  356 272 HOH HOH D . 
DA 8 HOH 57  357 64  HOH HOH D . 
DA 8 HOH 58  358 30  HOH HOH D . 
DA 8 HOH 59  359 428 HOH HOH D . 
DA 8 HOH 60  360 217 HOH HOH D . 
DA 8 HOH 61  361 692 HOH HOH D . 
DA 8 HOH 62  362 19  HOH HOH D . 
DA 8 HOH 63  363 270 HOH HOH D . 
DA 8 HOH 64  364 63  HOH HOH D . 
DA 8 HOH 65  365 400 HOH HOH D . 
DA 8 HOH 66  366 114 HOH HOH D . 
DA 8 HOH 67  367 70  HOH HOH D . 
DA 8 HOH 68  368 118 HOH HOH D . 
DA 8 HOH 69  369 235 HOH HOH D . 
DA 8 HOH 70  370 789 HOH HOH D . 
DA 8 HOH 71  371 630 HOH HOH D . 
DA 8 HOH 72  372 290 HOH HOH D . 
DA 8 HOH 73  373 855 HOH HOH D . 
DA 8 HOH 74  374 831 HOH HOH D . 
DA 8 HOH 75  375 418 HOH HOH D . 
DA 8 HOH 76  376 202 HOH HOH D . 
DA 8 HOH 77  377 726 HOH HOH D . 
DA 8 HOH 78  378 779 HOH HOH D . 
DA 8 HOH 79  379 304 HOH HOH D . 
DA 8 HOH 80  380 782 HOH HOH D . 
DA 8 HOH 81  381 801 HOH HOH D . 
DA 8 HOH 82  382 541 HOH HOH D . 
DA 8 HOH 83  383 49  HOH HOH D . 
DA 8 HOH 84  384 99  HOH HOH D . 
DA 8 HOH 85  385 366 HOH HOH D . 
DA 8 HOH 86  386 93  HOH HOH D . 
DA 8 HOH 87  387 811 HOH HOH D . 
DA 8 HOH 88  388 559 HOH HOH D . 
DA 8 HOH 89  389 426 HOH HOH D . 
DA 8 HOH 90  390 163 HOH HOH D . 
DA 8 HOH 91  391 248 HOH HOH D . 
DA 8 HOH 92  392 613 HOH HOH D . 
DA 8 HOH 93  393 258 HOH HOH D . 
DA 8 HOH 94  394 633 HOH HOH D . 
DA 8 HOH 95  395 465 HOH HOH D . 
DA 8 HOH 96  396 357 HOH HOH D . 
DA 8 HOH 97  397 131 HOH HOH D . 
DA 8 HOH 98  398 404 HOH HOH D . 
DA 8 HOH 99  399 721 HOH HOH D . 
DA 8 HOH 100 400 454 HOH HOH D . 
DA 8 HOH 101 401 376 HOH HOH D . 
DA 8 HOH 102 402 878 HOH HOH D . 
DA 8 HOH 103 403 778 HOH HOH D . 
DA 8 HOH 104 404 742 HOH HOH D . 
DA 8 HOH 105 405 437 HOH HOH D . 
DA 8 HOH 106 406 732 HOH HOH D . 
DA 8 HOH 107 407 262 HOH HOH D . 
DA 8 HOH 108 408 16  HOH HOH D . 
DA 8 HOH 109 409 360 HOH HOH D . 
DA 8 HOH 110 410 295 HOH HOH D . 
DA 8 HOH 111 411 374 HOH HOH D . 
DA 8 HOH 112 412 766 HOH HOH D . 
DA 8 HOH 113 413 532 HOH HOH D . 
DA 8 HOH 114 414 620 HOH HOH D . 
DA 8 HOH 115 415 250 HOH HOH D . 
DA 8 HOH 116 416 893 HOH HOH D . 
DA 8 HOH 117 417 738 HOH HOH D . 
DA 8 HOH 118 418 628 HOH HOH D . 
DA 8 HOH 119 419 394 HOH HOH D . 
DA 8 HOH 120 420 468 HOH HOH D . 
DA 8 HOH 121 421 627 HOH HOH D . 
DA 8 HOH 122 422 334 HOH HOH D . 
DA 8 HOH 123 423 804 HOH HOH D . 
DA 8 HOH 124 424 632 HOH HOH D . 
DA 8 HOH 125 425 314 HOH HOH D . 
DA 8 HOH 126 426 398 HOH HOH D . 
DA 8 HOH 127 427 192 HOH HOH D . 
DA 8 HOH 128 428 634 HOH HOH D . 
DA 8 HOH 129 429 625 HOH HOH D . 
DA 8 HOH 130 430 622 HOH HOH D . 
DA 8 HOH 131 431 539 HOH HOH D . 
DA 8 HOH 132 432 631 HOH HOH D . 
DA 8 HOH 133 433 908 HOH HOH D . 
DA 8 HOH 134 434 874 HOH HOH D . 
DA 8 HOH 135 435 531 HOH HOH D . 
DA 8 HOH 136 436 380 HOH HOH D . 
DA 8 HOH 137 437 303 HOH HOH D . 
DA 8 HOH 138 438 335 HOH HOH D . 
DA 8 HOH 139 439 623 HOH HOH D . 
DA 8 HOH 140 440 39  HOH HOH D . 
DA 8 HOH 141 441 104 HOH HOH D . 
DA 8 HOH 142 442 82  HOH HOH D . 
DA 8 HOH 143 443 635 HOH HOH D . 
DA 8 HOH 144 444 251 HOH HOH D . 
DA 8 HOH 145 445 649 HOH HOH D . 
EA 8 HOH 1   301 281 HOH HOH E . 
EA 8 HOH 2   302 897 HOH HOH E . 
EA 8 HOH 3   303 469 HOH HOH E . 
EA 8 HOH 4   304 447 HOH HOH E . 
EA 8 HOH 5   305 343 HOH HOH E . 
EA 8 HOH 6   306 683 HOH HOH E . 
EA 8 HOH 7   307 799 HOH HOH E . 
EA 8 HOH 8   308 866 HOH HOH E . 
EA 8 HOH 9   309 45  HOH HOH E . 
EA 8 HOH 10  310 408 HOH HOH E . 
EA 8 HOH 11  311 233 HOH HOH E . 
EA 8 HOH 12  312 688 HOH HOH E . 
EA 8 HOH 13  313 57  HOH HOH E . 
EA 8 HOH 14  314 129 HOH HOH E . 
EA 8 HOH 15  315 764 HOH HOH E . 
EA 8 HOH 16  316 695 HOH HOH E . 
EA 8 HOH 17  317 26  HOH HOH E . 
EA 8 HOH 18  318 698 HOH HOH E . 
EA 8 HOH 19  319 83  HOH HOH E . 
EA 8 HOH 20  320 88  HOH HOH E . 
EA 8 HOH 21  321 867 HOH HOH E . 
EA 8 HOH 22  322 689 HOH HOH E . 
EA 8 HOH 23  323 107 HOH HOH E . 
EA 8 HOH 24  324 534 HOH HOH E . 
EA 8 HOH 25  325 150 HOH HOH E . 
EA 8 HOH 26  326 716 HOH HOH E . 
EA 8 HOH 27  327 60  HOH HOH E . 
EA 8 HOH 28  328 699 HOH HOH E . 
EA 8 HOH 29  329 8   HOH HOH E . 
EA 8 HOH 30  330 155 HOH HOH E . 
EA 8 HOH 31  331 656 HOH HOH E . 
EA 8 HOH 32  332 884 HOH HOH E . 
EA 8 HOH 33  333 149 HOH HOH E . 
EA 8 HOH 34  334 112 HOH HOH E . 
EA 8 HOH 35  335 834 HOH HOH E . 
EA 8 HOH 36  336 54  HOH HOH E . 
EA 8 HOH 37  337 109 HOH HOH E . 
EA 8 HOH 38  338 142 HOH HOH E . 
EA 8 HOH 39  339 342 HOH HOH E . 
EA 8 HOH 40  340 195 HOH HOH E . 
EA 8 HOH 41  341 348 HOH HOH E . 
EA 8 HOH 42  342 197 HOH HOH E . 
EA 8 HOH 43  343 825 HOH HOH E . 
EA 8 HOH 44  344 355 HOH HOH E . 
EA 8 HOH 45  345 300 HOH HOH E . 
EA 8 HOH 46  346 136 HOH HOH E . 
EA 8 HOH 47  347 271 HOH HOH E . 
EA 8 HOH 48  348 78  HOH HOH E . 
EA 8 HOH 49  349 172 HOH HOH E . 
EA 8 HOH 50  350 753 HOH HOH E . 
EA 8 HOH 51  351 759 HOH HOH E . 
EA 8 HOH 52  352 459 HOH HOH E . 
EA 8 HOH 53  353 296 HOH HOH E . 
EA 8 HOH 54  354 538 HOH HOH E . 
EA 8 HOH 55  355 840 HOH HOH E . 
EA 8 HOH 56  356 288 HOH HOH E . 
EA 8 HOH 57  357 443 HOH HOH E . 
EA 8 HOH 58  358 245 HOH HOH E . 
EA 8 HOH 59  359 814 HOH HOH E . 
EA 8 HOH 60  360 849 HOH HOH E . 
EA 8 HOH 61  361 526 HOH HOH E . 
EA 8 HOH 62  362 503 HOH HOH E . 
EA 8 HOH 63  363 769 HOH HOH E . 
EA 8 HOH 64  364 678 HOH HOH E . 
EA 8 HOH 65  365 493 HOH HOH E . 
EA 8 HOH 66  366 175 HOH HOH E . 
EA 8 HOH 67  367 684 HOH HOH E . 
EA 8 HOH 68  368 115 HOH HOH E . 
EA 8 HOH 69  369 227 HOH HOH E . 
EA 8 HOH 70  370 883 HOH HOH E . 
EA 8 HOH 71  371 403 HOH HOH E . 
EA 8 HOH 72  372 771 HOH HOH E . 
EA 8 HOH 73  373 189 HOH HOH E . 
EA 8 HOH 74  374 895 HOH HOH E . 
EA 8 HOH 75  375 891 HOH HOH E . 
EA 8 HOH 76  376 785 HOH HOH E . 
EA 8 HOH 77  377 506 HOH HOH E . 
EA 8 HOH 78  378 234 HOH HOH E . 
EA 8 HOH 79  379 306 HOH HOH E . 
EA 8 HOH 80  380 640 HOH HOH E . 
EA 8 HOH 81  381 441 HOH HOH E . 
EA 8 HOH 82  382 557 HOH HOH E . 
EA 8 HOH 83  383 333 HOH HOH E . 
EA 8 HOH 84  384 330 HOH HOH E . 
EA 8 HOH 85  385 346 HOH HOH E . 
FA 8 HOH 1   301 844 HOH HOH F . 
FA 8 HOH 2   302 860 HOH HOH F . 
FA 8 HOH 3   303 796 HOH HOH F . 
FA 8 HOH 4   304 159 HOH HOH F . 
FA 8 HOH 5   305 278 HOH HOH F . 
FA 8 HOH 6   306 494 HOH HOH F . 
FA 8 HOH 7   307 817 HOH HOH F . 
FA 8 HOH 8   308 267 HOH HOH F . 
FA 8 HOH 9   309 427 HOH HOH F . 
FA 8 HOH 10  310 500 HOH HOH F . 
FA 8 HOH 11  311 415 HOH HOH F . 
FA 8 HOH 12  312 464 HOH HOH F . 
FA 8 HOH 13  313 332 HOH HOH F . 
FA 8 HOH 14  314 456 HOH HOH F . 
FA 8 HOH 15  315 876 HOH HOH F . 
FA 8 HOH 16  316 438 HOH HOH F . 
FA 8 HOH 17  317 208 HOH HOH F . 
FA 8 HOH 18  318 345 HOH HOH F . 
FA 8 HOH 19  319 383 HOH HOH F . 
FA 8 HOH 20  320 219 HOH HOH F . 
FA 8 HOH 21  321 1   HOH HOH F . 
FA 8 HOH 22  322 353 HOH HOH F . 
FA 8 HOH 23  323 719 HOH HOH F . 
FA 8 HOH 24  324 46  HOH HOH F . 
FA 8 HOH 25  325 180 HOH HOH F . 
FA 8 HOH 26  326 319 HOH HOH F . 
FA 8 HOH 27  327 10  HOH HOH F . 
FA 8 HOH 28  328 339 HOH HOH F . 
FA 8 HOH 29  329 122 HOH HOH F . 
FA 8 HOH 30  330 28  HOH HOH F . 
FA 8 HOH 31  331 33  HOH HOH F . 
FA 8 HOH 32  332 187 HOH HOH F . 
FA 8 HOH 33  333 120 HOH HOH F . 
FA 8 HOH 34  334 657 HOH HOH F . 
FA 8 HOH 35  335 510 HOH HOH F . 
FA 8 HOH 36  336 14  HOH HOH F . 
FA 8 HOH 37  337 222 HOH HOH F . 
FA 8 HOH 38  338 452 HOH HOH F . 
FA 8 HOH 39  339 11  HOH HOH F . 
FA 8 HOH 40  340 302 HOH HOH F . 
FA 8 HOH 41  341 23  HOH HOH F . 
FA 8 HOH 42  342 414 HOH HOH F . 
FA 8 HOH 43  343 423 HOH HOH F . 
FA 8 HOH 44  344 448 HOH HOH F . 
FA 8 HOH 45  345 723 HOH HOH F . 
FA 8 HOH 46  346 827 HOH HOH F . 
FA 8 HOH 47  347 654 HOH HOH F . 
FA 8 HOH 48  348 299 HOH HOH F . 
FA 8 HOH 49  349 761 HOH HOH F . 
FA 8 HOH 50  350 606 HOH HOH F . 
FA 8 HOH 51  351 730 HOH HOH F . 
FA 8 HOH 52  352 90  HOH HOH F . 
FA 8 HOH 53  353 548 HOH HOH F . 
FA 8 HOH 54  354 805 HOH HOH F . 
FA 8 HOH 55  355 73  HOH HOH F . 
FA 8 HOH 56  356 722 HOH HOH F . 
FA 8 HOH 57  357 246 HOH HOH F . 
FA 8 HOH 58  358 691 HOH HOH F . 
FA 8 HOH 59  359 84  HOH HOH F . 
FA 8 HOH 60  360 297 HOH HOH F . 
FA 8 HOH 61  361 7   HOH HOH F . 
FA 8 HOH 62  362 486 HOH HOH F . 
FA 8 HOH 63  363 703 HOH HOH F . 
FA 8 HOH 64  364 179 HOH HOH F . 
FA 8 HOH 65  365 859 HOH HOH F . 
FA 8 HOH 66  366 320 HOH HOH F . 
FA 8 HOH 67  367 196 HOH HOH F . 
FA 8 HOH 68  368 274 HOH HOH F . 
FA 8 HOH 69  369 717 HOH HOH F . 
FA 8 HOH 70  370 608 HOH HOH F . 
FA 8 HOH 71  371 790 HOH HOH F . 
FA 8 HOH 72  372 757 HOH HOH F . 
FA 8 HOH 73  373 535 HOH HOH F . 
FA 8 HOH 74  374 66  HOH HOH F . 
FA 8 HOH 75  375 116 HOH HOH F . 
FA 8 HOH 76  376 498 HOH HOH F . 
FA 8 HOH 77  377 17  HOH HOH F . 
FA 8 HOH 78  378 736 HOH HOH F . 
FA 8 HOH 79  379 705 HOH HOH F . 
FA 8 HOH 80  380 745 HOH HOH F . 
FA 8 HOH 81  381 555 HOH HOH F . 
FA 8 HOH 82  382 841 HOH HOH F . 
FA 8 HOH 83  383 520 HOH HOH F . 
FA 8 HOH 84  384 875 HOH HOH F . 
FA 8 HOH 85  385 316 HOH HOH F . 
FA 8 HOH 86  386 338 HOH HOH F . 
FA 8 HOH 87  387 111 HOH HOH F . 
FA 8 HOH 88  388 56  HOH HOH F . 
FA 8 HOH 89  389 42  HOH HOH F . 
FA 8 HOH 90  390 87  HOH HOH F . 
FA 8 HOH 91  391 167 HOH HOH F . 
FA 8 HOH 92  392 311 HOH HOH F . 
FA 8 HOH 93  393 194 HOH HOH F . 
FA 8 HOH 94  394 315 HOH HOH F . 
FA 8 HOH 95  395 607 HOH HOH F . 
FA 8 HOH 96  396 497 HOH HOH F . 
FA 8 HOH 97  397 125 HOH HOH F . 
FA 8 HOH 98  398 86  HOH HOH F . 
FA 8 HOH 99  399 820 HOH HOH F . 
FA 8 HOH 100 400 797 HOH HOH F . 
FA 8 HOH 101 401 480 HOH HOH F . 
FA 8 HOH 102 402 305 HOH HOH F . 
FA 8 HOH 103 403 808 HOH HOH F . 
FA 8 HOH 104 404 337 HOH HOH F . 
FA 8 HOH 105 405 877 HOH HOH F . 
FA 8 HOH 106 406 496 HOH HOH F . 
FA 8 HOH 107 407 906 HOH HOH F . 
FA 8 HOH 108 408 230 HOH HOH F . 
FA 8 HOH 109 409 807 HOH HOH F . 
FA 8 HOH 110 410 421 HOH HOH F . 
FA 8 HOH 111 411 803 HOH HOH F . 
FA 8 HOH 112 412 870 HOH HOH F . 
FA 8 HOH 113 413 321 HOH HOH F . 
FA 8 HOH 114 414 615 HOH HOH F . 
FA 8 HOH 115 415 756 HOH HOH F . 
FA 8 HOH 116 416 660 HOH HOH F . 
FA 8 HOH 117 417 602 HOH HOH F . 
FA 8 HOH 118 418 389 HOH HOH F . 
FA 8 HOH 119 419 256 HOH HOH F . 
FA 8 HOH 120 420 340 HOH HOH F . 
FA 8 HOH 121 421 543 HOH HOH F . 
FA 8 HOH 122 422 434 HOH HOH F . 
FA 8 HOH 123 423 616 HOH HOH F . 
FA 8 HOH 124 424 237 HOH HOH F . 
FA 8 HOH 125 425 889 HOH HOH F . 
FA 8 HOH 126 426 392 HOH HOH F . 
FA 8 HOH 127 427 564 HOH HOH F . 
FA 8 HOH 128 428 501 HOH HOH F . 
FA 8 HOH 129 429 562 HOH HOH F . 
GA 8 HOH 1   201 824 HOH HOH G . 
GA 8 HOH 2   202 935 HOH HOH G . 
GA 8 HOH 3   203 694 HOH HOH G . 
GA 8 HOH 4   204 436 HOH HOH G . 
GA 8 HOH 5   205 912 HOH HOH G . 
GA 8 HOH 6   206 991 HOH HOH G . 
GA 8 HOH 7   207 674 HOH HOH G . 
GA 8 HOH 8   208 919 HOH HOH G . 
GA 8 HOH 9   209 920 HOH HOH G . 
GA 8 HOH 10  210 927 HOH HOH G . 
GA 8 HOH 11  211 936 HOH HOH G . 
GA 8 HOH 12  212 934 HOH HOH G . 
GA 8 HOH 13  213 728 HOH HOH G . 
GA 8 HOH 14  214 928 HOH HOH G . 
GA 8 HOH 15  215 917 HOH HOH G . 
GA 8 HOH 16  216 929 HOH HOH G . 
GA 8 HOH 17  217 944 HOH HOH G . 
GA 8 HOH 18  218 918 HOH HOH G . 
GA 8 HOH 19  219 923 HOH HOH G . 
GA 8 HOH 20  220 938 HOH HOH G . 
GA 8 HOH 21  221 926 HOH HOH G . 
GA 8 HOH 22  222 921 HOH HOH G . 
GA 8 HOH 23  223 933 HOH HOH G . 
GA 8 HOH 24  224 924 HOH HOH G . 
GA 8 HOH 25  225 491 HOH HOH G . 
GA 8 HOH 26  226 551 HOH HOH G . 
GA 8 HOH 27  227 932 HOH HOH G . 
GA 8 HOH 28  228 593 HOH HOH G . 
GA 8 HOH 29  229 930 HOH HOH G . 
GA 8 HOH 30  230 590 HOH HOH G . 
GA 8 HOH 31  231 922 HOH HOH G . 
GA 8 HOH 32  232 680 HOH HOH G . 
GA 8 HOH 33  233 931 HOH HOH G . 
GA 8 HOH 34  234 885 HOH HOH G . 
GA 8 HOH 35  235 592 HOH HOH G . 
GA 8 HOH 36  236 925 HOH HOH G . 
GA 8 HOH 37  237 973 HOH HOH G . 
GA 8 HOH 38  238 863 HOH HOH G . 
GA 8 HOH 39  239 787 HOH HOH G . 
HA 8 HOH 1   301 586 HOH HOH H . 
HA 8 HOH 2   302 974 HOH HOH H . 
HA 8 HOH 3   303 955 HOH HOH H . 
HA 8 HOH 4   304 858 HOH HOH H . 
HA 8 HOH 5   305 599 HOH HOH H . 
HA 8 HOH 6   306 959 HOH HOH H . 
HA 8 HOH 7   307 693 HOH HOH H . 
HA 8 HOH 8   308 595 HOH HOH H . 
HA 8 HOH 9   309 589 HOH HOH H . 
HA 8 HOH 10  310 58  HOH HOH H . 
HA 8 HOH 11  311 216 HOH HOH H . 
HA 8 HOH 12  312 204 HOH HOH H . 
HA 8 HOH 13  313 988 HOH HOH H . 
HA 8 HOH 14  314 140 HOH HOH H . 
HA 8 HOH 15  315 833 HOH HOH H . 
HA 8 HOH 16  316 954 HOH HOH H . 
HA 8 HOH 17  317 975 HOH HOH H . 
HA 8 HOH 18  318 951 HOH HOH H . 
HA 8 HOH 19  319 981 HOH HOH H . 
HA 8 HOH 20  320 812 HOH HOH H . 
HA 8 HOH 21  321 913 HOH HOH H . 
HA 8 HOH 22  322 663 HOH HOH H . 
HA 8 HOH 23  323 950 HOH HOH H . 
HA 8 HOH 24  324 675 HOH HOH H . 
HA 8 HOH 25  325 967 HOH HOH H . 
HA 8 HOH 26  326 490 HOH HOH H . 
HA 8 HOH 27  327 987 HOH HOH H . 
HA 8 HOH 28  328 143 HOH HOH H . 
HA 8 HOH 29  329 956 HOH HOH H . 
HA 8 HOH 30  330 937 HOH HOH H . 
HA 8 HOH 31  331 942 HOH HOH H . 
HA 8 HOH 32  332 948 HOH HOH H . 
HA 8 HOH 33  333 960 HOH HOH H . 
HA 8 HOH 34  334 915 HOH HOH H . 
HA 8 HOH 35  335 940 HOH HOH H . 
HA 8 HOH 36  336 962 HOH HOH H . 
HA 8 HOH 37  337 729 HOH HOH H . 
HA 8 HOH 38  338 463 HOH HOH H . 
HA 8 HOH 39  339 961 HOH HOH H . 
HA 8 HOH 40  340 48  HOH HOH H . 
HA 8 HOH 41  341 273 HOH HOH H . 
HA 8 HOH 42  342 969 HOH HOH H . 
HA 8 HOH 43  343 945 HOH HOH H . 
HA 8 HOH 44  344 989 HOH HOH H . 
HA 8 HOH 45  345 972 HOH HOH H . 
HA 8 HOH 46  346 939 HOH HOH H . 
HA 8 HOH 47  347 949 HOH HOH H . 
HA 8 HOH 48  348 966 HOH HOH H . 
HA 8 HOH 49  349 971 HOH HOH H . 
HA 8 HOH 50  350 276 HOH HOH H . 
HA 8 HOH 51  351 478 HOH HOH H . 
HA 8 HOH 52  352 984 HOH HOH H . 
HA 8 HOH 53  353 985 HOH HOH H . 
HA 8 HOH 54  354 741 HOH HOH H . 
HA 8 HOH 55  355 425 HOH HOH H . 
HA 8 HOH 56  356 983 HOH HOH H . 
HA 8 HOH 57  357 952 HOH HOH H . 
HA 8 HOH 58  358 953 HOH HOH H . 
HA 8 HOH 59  359 282 HOH HOH H . 
HA 8 HOH 60  360 51  HOH HOH H . 
HA 8 HOH 61  361 958 HOH HOH H . 
HA 8 HOH 62  362 826 HOH HOH H . 
HA 8 HOH 63  363 662 HOH HOH H . 
HA 8 HOH 64  364 594 HOH HOH H . 
HA 8 HOH 65  365 735 HOH HOH H . 
HA 8 HOH 66  366 169 HOH HOH H . 
HA 8 HOH 67  367 810 HOH HOH H . 
HA 8 HOH 68  368 910 HOH HOH H . 
HA 8 HOH 69  369 685 HOH HOH H . 
HA 8 HOH 70  370 977 HOH HOH H . 
HA 8 HOH 71  371 970 HOH HOH H . 
HA 8 HOH 72  372 596 HOH HOH H . 
HA 8 HOH 73  373 158 HOH HOH H . 
HA 8 HOH 74  374 37  HOH HOH H . 
HA 8 HOH 75  375 946 HOH HOH H . 
HA 8 HOH 76  376 982 HOH HOH H . 
HA 8 HOH 77  377 943 HOH HOH H . 
HA 8 HOH 78  378 968 HOH HOH H . 
HA 8 HOH 79  379 941 HOH HOH H . 
HA 8 HOH 80  380 829 HOH HOH H . 
HA 8 HOH 81  381 947 HOH HOH H . 
HA 8 HOH 82  382 347 HOH HOH H . 
HA 8 HOH 83  383 664 HOH HOH H . 
HA 8 HOH 84  384 914 HOH HOH H . 
HA 8 HOH 85  385 979 HOH HOH H . 
HA 8 HOH 86  386 540 HOH HOH H . 
HA 8 HOH 87  387 990 HOH HOH H . 
HA 8 HOH 88  388 963 HOH HOH H . 
HA 8 HOH 89  389 591 HOH HOH H . 
HA 8 HOH 90  390 957 HOH HOH H . 
HA 8 HOH 91  391 980 HOH HOH H . 
HA 8 HOH 92  392 507 HOH HOH H . 
HA 8 HOH 93  393 986 HOH HOH H . 
HA 8 HOH 94  394 911 HOH HOH H . 
HA 8 HOH 95  395 965 HOH HOH H . 
HA 8 HOH 96  396 964 HOH HOH H . 
IA 8 HOH 1   301 638 HOH HOH I . 
IA 8 HOH 2   302 264 HOH HOH I . 
IA 8 HOH 3   303 242 HOH HOH I . 
IA 8 HOH 4   304 821 HOH HOH I . 
IA 8 HOH 5   305 81  HOH HOH I . 
IA 8 HOH 6   306 97  HOH HOH I . 
IA 8 HOH 7   307 369 HOH HOH I . 
IA 8 HOH 8   308 77  HOH HOH I . 
IA 8 HOH 9   309 862 HOH HOH I . 
IA 8 HOH 10  310 828 HOH HOH I . 
IA 8 HOH 11  311 898 HOH HOH I . 
IA 8 HOH 12  312 686 HOH HOH I . 
IA 8 HOH 13  313 659 HOH HOH I . 
IA 8 HOH 14  314 301 HOH HOH I . 
IA 8 HOH 15  315 68  HOH HOH I . 
IA 8 HOH 16  316 232 HOH HOH I . 
IA 8 HOH 17  317 724 HOH HOH I . 
IA 8 HOH 18  318 117 HOH HOH I . 
IA 8 HOH 19  319 138 HOH HOH I . 
IA 8 HOH 20  320 130 HOH HOH I . 
IA 8 HOH 21  321 658 HOH HOH I . 
IA 8 HOH 22  322 387 HOH HOH I . 
IA 8 HOH 23  323 385 HOH HOH I . 
IA 8 HOH 24  324 135 HOH HOH I . 
IA 8 HOH 25  325 325 HOH HOH I . 
IA 8 HOH 26  326 725 HOH HOH I . 
IA 8 HOH 27  327 238 HOH HOH I . 
IA 8 HOH 28  328 791 HOH HOH I . 
IA 8 HOH 29  329 89  HOH HOH I . 
IA 8 HOH 30  330 257 HOH HOH I . 
IA 8 HOH 31  331 639 HOH HOH I . 
IA 8 HOH 32  332 901 HOH HOH I . 
IA 8 HOH 33  333 881 HOH HOH I . 
IA 8 HOH 34  334 865 HOH HOH I . 
IA 8 HOH 35  335 783 HOH HOH I . 
IA 8 HOH 36  336 206 HOH HOH I . 
IA 8 HOH 37  337 655 HOH HOH I . 
IA 8 HOH 38  338 100 HOH HOH I . 
IA 8 HOH 39  339 605 HOH HOH I . 
IA 8 HOH 40  340 147 HOH HOH I . 
IA 8 HOH 41  341 160 HOH HOH I . 
IA 8 HOH 42  342 521 HOH HOH I . 
IA 8 HOH 43  343 200 HOH HOH I . 
IA 8 HOH 44  344 687 HOH HOH I . 
IA 8 HOH 45  345 547 HOH HOH I . 
IA 8 HOH 46  346 832 HOH HOH I . 
IA 8 HOH 47  347 800 HOH HOH I . 
IA 8 HOH 48  348 553 HOH HOH I . 
IA 8 HOH 49  349 677 HOH HOH I . 
IA 8 HOH 50  350 765 HOH HOH I . 
IA 8 HOH 51  351 733 HOH HOH I . 
IA 8 HOH 52  352 536 HOH HOH I . 
IA 8 HOH 53  353 899 HOH HOH I . 
IA 8 HOH 54  354 467 HOH HOH I . 
IA 8 HOH 55  355 853 HOH HOH I . 
IA 8 HOH 56  356 461 HOH HOH I . 
IA 8 HOH 57  357 513 HOH HOH I . 
IA 8 HOH 58  358 505 HOH HOH I . 
IA 8 HOH 59  359 690 HOH HOH I . 
IA 8 HOH 60  360 604 HOH HOH I . 
IA 8 HOH 61  361 835 HOH HOH I . 
IA 8 HOH 62  362 763 HOH HOH I . 
IA 8 HOH 63  363 869 HOH HOH I . 
IA 8 HOH 64  364 286 HOH HOH I . 
JA 8 HOH 1   301 720 HOH HOH J . 
JA 8 HOH 2   302 323 HOH HOH J . 
JA 8 HOH 3   303 214 HOH HOH J . 
JA 8 HOH 4   304 813 HOH HOH J . 
JA 8 HOH 5   305 362 HOH HOH J . 
JA 8 HOH 6   306 252 HOH HOH J . 
JA 8 HOH 7   307 770 HOH HOH J . 
JA 8 HOH 8   308 198 HOH HOH J . 
JA 8 HOH 9   309 38  HOH HOH J . 
JA 8 HOH 10  310 74  HOH HOH J . 
JA 8 HOH 11  311 113 HOH HOH J . 
JA 8 HOH 12  312 470 HOH HOH J . 
JA 8 HOH 13  313 512 HOH HOH J . 
JA 8 HOH 14  314 525 HOH HOH J . 
JA 8 HOH 15  315 145 HOH HOH J . 
JA 8 HOH 16  316 850 HOH HOH J . 
JA 8 HOH 17  317 473 HOH HOH J . 
JA 8 HOH 18  318 226 HOH HOH J . 
JA 8 HOH 19  319 102 HOH HOH J . 
JA 8 HOH 20  320 887 HOH HOH J . 
JA 8 HOH 21  321 59  HOH HOH J . 
JA 8 HOH 22  322 485 HOH HOH J . 
JA 8 HOH 23  323 976 HOH HOH J . 
JA 8 HOH 24  324 170 HOH HOH J . 
JA 8 HOH 25  325 904 HOH HOH J . 
JA 8 HOH 26  326 476 HOH HOH J . 
JA 8 HOH 27  327 287 HOH HOH J . 
JA 8 HOH 28  328 401 HOH HOH J . 
JA 8 HOH 29  329 293 HOH HOH J . 
JA 8 HOH 30  330 152 HOH HOH J . 
JA 8 HOH 31  331 422 HOH HOH J . 
JA 8 HOH 32  332 504 HOH HOH J . 
JA 8 HOH 33  333 164 HOH HOH J . 
JA 8 HOH 34  334 324 HOH HOH J . 
JA 8 HOH 35  335 399 HOH HOH J . 
JA 8 HOH 36  336 280 HOH HOH J . 
JA 8 HOH 37  337 802 HOH HOH J . 
JA 8 HOH 38  338 358 HOH HOH J . 
JA 8 HOH 39  339 907 HOH HOH J . 
JA 8 HOH 40  340 550 HOH HOH J . 
JA 8 HOH 41  341 563 HOH HOH J . 
JA 8 HOH 42  342 868 HOH HOH J . 
JA 8 HOH 43  343 455 HOH HOH J . 
JA 8 HOH 44  344 679 HOH HOH J . 
JA 8 HOH 45  345 193 HOH HOH J . 
JA 8 HOH 46  346 846 HOH HOH J . 
JA 8 HOH 47  347 148 HOH HOH J . 
JA 8 HOH 48  348 411 HOH HOH J . 
JA 8 HOH 49  349 836 HOH HOH J . 
JA 8 HOH 50  350 368 HOH HOH J . 
JA 8 HOH 51  351 740 HOH HOH J . 
JA 8 HOH 52  352 894 HOH HOH J . 
JA 8 HOH 53  353 792 HOH HOH J . 
JA 8 HOH 54  354 618 HOH HOH J . 
JA 8 HOH 55  355 892 HOH HOH J . 
JA 8 HOH 56  356 444 HOH HOH J . 
JA 8 HOH 57  357 410 HOH HOH J . 
JA 8 HOH 58  358 406 HOH HOH J . 
JA 8 HOH 59  359 283 HOH HOH J . 
JA 8 HOH 60  360 744 HOH HOH J . 
JA 8 HOH 61  361 388 HOH HOH J . 
JA 8 HOH 62  362 511 HOH HOH J . 
JA 8 HOH 63  363 341 HOH HOH J . 
JA 8 HOH 64  364 617 HOH HOH J . 
JA 8 HOH 65  365 619 HOH HOH J . 
JA 8 HOH 66  366 475 HOH HOH J . 
JA 8 HOH 67  367 542 HOH HOH J . 
JA 8 HOH 68  368 760 HOH HOH J . 
JA 8 HOH 69  369 225 HOH HOH J . 
JA 8 HOH 70  370 173 HOH HOH J . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
3 author_and_software_defined_assembly PISA dimeric 2 
4 author_and_software_defined_assembly PISA dimeric 2 
5 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,K,L,M,N,AA,BA 
2 1 C,D,O,P,Q,R,CA,DA 
3 1 E,F,S,T,U,V,EA,FA 
4 1 G,H,W,X,GA,HA     
5 1 I,J,Y,Z,IA,JA     
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1410  ? 
1 MORE         -12   ? 
1 'SSA (A^2)'  13890 ? 
2 'ABSA (A^2)' 1420  ? 
2 MORE         -12   ? 
2 'SSA (A^2)'  13890 ? 
3 'ABSA (A^2)' 1410  ? 
3 MORE         -11   ? 
3 'SSA (A^2)'  13890 ? 
4 'ABSA (A^2)' 1350  ? 
4 MORE         -11   ? 
4 'SSA (A^2)'  13460 ? 
5 'ABSA (A^2)' 1360  ? 
5 MORE         -12   ? 
5 'SSA (A^2)'  13840 ? 
# 
_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_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? K ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 72 ? A HIS 71 ? 1_555 103.0 ? 
2  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? K ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 81 ? A HIS 80 ? 1_555 114.5 ? 
3  ND1 ? A HIS 72 ? A HIS 71 ? 1_555 ZN ? K ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 81 ? A HIS 80 ? 1_555 124.8 ? 
4  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? K ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 84 ? A ASP 83 ? 1_555 107.0 ? 
5  ND1 ? A HIS 72 ? A HIS 71 ? 1_555 ZN ? K ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 84 ? A ASP 83 ? 1_555 87.7  ? 
6  ND1 ? A HIS 81 ? A HIS 80 ? 1_555 ZN ? K ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 84 ? A ASP 83 ? 1_555 116.0 ? 
7  ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? M ZN . ? B ZN 201 ? 1_555 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 102.2 ? 
8  ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? M ZN . ? B ZN 201 ? 1_555 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 111.2 ? 
9  ND1 ? B HIS 72 ? B HIS 71 ? 1_555 ZN ? M ZN . ? B ZN 201 ? 1_555 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 126.5 ? 
10 ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? M ZN . ? B ZN 201 ? 1_555 OD1 ? B ASP 84 ? B ASP 83 ? 1_555 106.4 ? 
11 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 ZN ? M ZN . ? B ZN 201 ? 1_555 OD1 ? B ASP 84 ? B ASP 83 ? 1_555 93.9  ? 
12 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 ZN ? M ZN . ? B ZN 201 ? 1_555 OD1 ? B ASP 84 ? B ASP 83 ? 1_555 114.1 ? 
13 ND1 ? C HIS 65 ? C HIS 63 ? 1_555 ZN ? O ZN . ? C ZN 201 ? 1_555 ND1 ? C HIS 73 ? C HIS 71 ? 1_555 102.3 ? 
14 ND1 ? C HIS 65 ? C HIS 63 ? 1_555 ZN ? O ZN . ? C ZN 201 ? 1_555 ND1 ? C HIS 82 ? C HIS 80 ? 1_555 113.4 ? 
15 ND1 ? C HIS 73 ? C HIS 71 ? 1_555 ZN ? O ZN . ? C ZN 201 ? 1_555 ND1 ? C HIS 82 ? C HIS 80 ? 1_555 127.9 ? 
16 ND1 ? C HIS 65 ? C HIS 63 ? 1_555 ZN ? O ZN . ? C ZN 201 ? 1_555 OD1 ? C ASP 85 ? C ASP 83 ? 1_555 99.6  ? 
17 ND1 ? C HIS 73 ? C HIS 71 ? 1_555 ZN ? O ZN . ? C ZN 201 ? 1_555 OD1 ? C ASP 85 ? C ASP 83 ? 1_555 87.0  ? 
18 ND1 ? C HIS 82 ? C HIS 80 ? 1_555 ZN ? O ZN . ? C ZN 201 ? 1_555 OD1 ? C ASP 85 ? C ASP 83 ? 1_555 120.8 ? 
19 ND1 ? D HIS 64 ? D HIS 63 ? 1_555 ZN ? Q ZN . ? D ZN 201 ? 1_555 ND1 ? D HIS 72 ? D HIS 71 ? 1_555 107.6 ? 
20 ND1 ? D HIS 64 ? D HIS 63 ? 1_555 ZN ? Q ZN . ? D ZN 201 ? 1_555 ND1 ? D HIS 81 ? D HIS 80 ? 1_555 110.8 ? 
21 ND1 ? D HIS 72 ? D HIS 71 ? 1_555 ZN ? Q ZN . ? D ZN 201 ? 1_555 ND1 ? D HIS 81 ? D HIS 80 ? 1_555 124.9 ? 
22 ND1 ? D HIS 64 ? D HIS 63 ? 1_555 ZN ? Q ZN . ? D ZN 201 ? 1_555 OD1 ? D ASP 84 ? D ASP 83 ? 1_555 103.8 ? 
23 ND1 ? D HIS 72 ? D HIS 71 ? 1_555 ZN ? Q ZN . ? D ZN 201 ? 1_555 OD1 ? D ASP 84 ? D ASP 83 ? 1_555 94.5  ? 
24 ND1 ? D HIS 81 ? D HIS 80 ? 1_555 ZN ? Q ZN . ? D ZN 201 ? 1_555 OD1 ? D ASP 84 ? D ASP 83 ? 1_555 112.4 ? 
25 ND1 ? E HIS 64 ? E HIS 63 ? 1_555 ZN ? S ZN . ? E ZN 201 ? 1_555 ND1 ? E HIS 72 ? E HIS 71 ? 1_555 103.6 ? 
26 ND1 ? E HIS 64 ? E HIS 63 ? 1_555 ZN ? S ZN . ? E ZN 201 ? 1_555 ND1 ? E HIS 81 ? E HIS 80 ? 1_555 115.0 ? 
27 ND1 ? E HIS 72 ? E HIS 71 ? 1_555 ZN ? S ZN . ? E ZN 201 ? 1_555 ND1 ? E HIS 81 ? E HIS 80 ? 1_555 121.2 ? 
28 ND1 ? E HIS 64 ? E HIS 63 ? 1_555 ZN ? S ZN . ? E ZN 201 ? 1_555 OD1 ? E ASP 84 ? E ASP 83 ? 1_555 105.3 ? 
29 ND1 ? E HIS 72 ? E HIS 71 ? 1_555 ZN ? S ZN . ? E ZN 201 ? 1_555 OD1 ? E ASP 84 ? E ASP 83 ? 1_555 88.5  ? 
30 ND1 ? E HIS 81 ? E HIS 80 ? 1_555 ZN ? S ZN . ? E ZN 201 ? 1_555 OD1 ? E ASP 84 ? E ASP 83 ? 1_555 119.3 ? 
31 ND1 ? F HIS 64 ? F HIS 63 ? 1_555 ZN ? U ZN . ? F ZN 201 ? 1_555 ND1 ? F HIS 72 ? F HIS 71 ? 1_555 106.7 ? 
32 ND1 ? F HIS 64 ? F HIS 63 ? 1_555 ZN ? U ZN . ? F ZN 201 ? 1_555 ND1 ? F HIS 81 ? F HIS 80 ? 1_555 107.4 ? 
33 ND1 ? F HIS 72 ? F HIS 71 ? 1_555 ZN ? U ZN . ? F ZN 201 ? 1_555 ND1 ? F HIS 81 ? F HIS 80 ? 1_555 127.5 ? 
34 ND1 ? F HIS 64 ? F HIS 63 ? 1_555 ZN ? U ZN . ? F ZN 201 ? 1_555 OD1 ? F ASP 84 ? F ASP 83 ? 1_555 105.0 ? 
35 ND1 ? F HIS 72 ? F HIS 71 ? 1_555 ZN ? U ZN . ? F ZN 201 ? 1_555 OD1 ? F ASP 84 ? F ASP 83 ? 1_555 95.9  ? 
36 ND1 ? F HIS 81 ? F HIS 80 ? 1_555 ZN ? U ZN . ? F ZN 201 ? 1_555 OD1 ? F ASP 84 ? F ASP 83 ? 1_555 112.2 ? 
37 ND1 ? H HIS 63 ? H HIS 63 ? 1_555 ZN ? W ZN . ? H ZN 201 ? 1_555 ND1 ? H HIS 71 ? H HIS 71 ? 1_555 102.0 ? 
38 ND1 ? H HIS 63 ? H HIS 63 ? 1_555 ZN ? W ZN . ? H ZN 201 ? 1_555 ND1 ? H HIS 80 ? H HIS 80 ? 1_555 107.0 ? 
39 ND1 ? H HIS 71 ? H HIS 71 ? 1_555 ZN ? W ZN . ? H ZN 201 ? 1_555 ND1 ? H HIS 80 ? H HIS 80 ? 1_555 130.1 ? 
40 ND1 ? H HIS 63 ? H HIS 63 ? 1_555 ZN ? W ZN . ? H ZN 201 ? 1_555 OD1 ? H ASP 83 ? H ASP 83 ? 1_555 110.2 ? 
41 ND1 ? H HIS 71 ? H HIS 71 ? 1_555 ZN ? W ZN . ? H ZN 201 ? 1_555 OD1 ? H ASP 83 ? H ASP 83 ? 1_555 97.7  ? 
42 ND1 ? H HIS 80 ? H HIS 80 ? 1_555 ZN ? W ZN . ? H ZN 201 ? 1_555 OD1 ? H ASP 83 ? H ASP 83 ? 1_555 108.9 ? 
43 ND1 ? I HIS 64 ? I HIS 63 ? 1_555 ZN ? Y ZN . ? I ZN 201 ? 1_555 ND1 ? I HIS 72 ? I HIS 71 ? 1_555 104.5 ? 
44 ND1 ? I HIS 64 ? I HIS 63 ? 1_555 ZN ? Y ZN . ? I ZN 201 ? 1_555 ND1 ? I HIS 81 ? I HIS 80 ? 1_555 106.7 ? 
45 ND1 ? I HIS 72 ? I HIS 71 ? 1_555 ZN ? Y ZN . ? I ZN 201 ? 1_555 ND1 ? I HIS 81 ? I HIS 80 ? 1_555 124.3 ? 
46 ND1 ? I HIS 64 ? I HIS 63 ? 1_555 ZN ? Y ZN . ? I ZN 201 ? 1_555 OD1 ? I ASP 84 ? I ASP 83 ? 1_555 116.4 ? 
47 ND1 ? I HIS 72 ? I HIS 71 ? 1_555 ZN ? Y ZN . ? I ZN 201 ? 1_555 OD1 ? I ASP 84 ? I ASP 83 ? 1_555 105.9 ? 
48 ND1 ? I HIS 81 ? I HIS 80 ? 1_555 ZN ? Y ZN . ? I ZN 201 ? 1_555 OD1 ? I ASP 84 ? I ASP 83 ? 1_555 100.0 ? 
49 ND1 ? J HIS 64 ? J HIS 63 ? 1_555 ZN ? Z ZN . ? J ZN 201 ? 1_555 ND1 ? J HIS 72 ? J HIS 71 ? 1_555 105.7 ? 
50 ND1 ? J HIS 64 ? J HIS 63 ? 1_555 ZN ? Z ZN . ? J ZN 201 ? 1_555 ND1 ? J HIS 81 ? J HIS 80 ? 1_555 108.6 ? 
51 ND1 ? J HIS 72 ? J HIS 71 ? 1_555 ZN ? Z ZN . ? J ZN 201 ? 1_555 ND1 ? J HIS 81 ? J HIS 80 ? 1_555 121.0 ? 
52 ND1 ? J HIS 64 ? J HIS 63 ? 1_555 ZN ? Z ZN . ? J ZN 201 ? 1_555 OD1 ? J ASP 84 ? J ASP 83 ? 1_555 108.5 ? 
53 ND1 ? J HIS 72 ? J HIS 71 ? 1_555 ZN ? Z ZN . ? J ZN 201 ? 1_555 OD1 ? J ASP 84 ? J ASP 83 ? 1_555 93.3  ? 
54 ND1 ? J HIS 81 ? J HIS 80 ? 1_555 ZN ? Z ZN . ? J ZN 201 ? 1_555 OD1 ? J ASP 84 ? J ASP 83 ? 1_555 118.2 ? 
# 
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 
1 'Structure model' 1 0 2023-06-14 
2 'Structure model' 1 1 2023-09-20 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'      
2 2 'Structure model' 'Derived calculations' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom            
2 2 'Structure model' chem_comp_bond            
3 2 'Structure model' pdbx_struct_assembly_gen  
4 2 'Structure model' pdbx_struct_assembly_prop 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_pdbx_struct_assembly_gen.asym_id_list' 
2 2 'Structure model' '_pdbx_struct_assembly_prop.value'       
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z+1/2         
4 -x,-y,z+1/2         
5 x+1/2,y+1/2,z       
6 x+1/2,-y+1/2,-z     
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? v1.1.7               2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? v1.1.7               3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_pdbx_entry_details.entry_id                 8GSQ 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.has_ligand_of_interest   Y 
# 
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   A HOH 364 ? ? O A HOH 389 ? ? 2.12 
2 1 OE2 E GLU 78  ? ? O E HOH 301 ? ? 2.14 
3 1 O   D HOH 318 ? ? O D HOH 320 ? ? 2.16 
4 1 O   G PRO 28  ? ? O G HOH 201 ? ? 2.18 
5 1 O   J ALA 152 ? ? O J HOH 301 ? ? 2.19 
6 1 O   G VAL 7   ? ? O G HOH 202 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O C HOH 403 ? ? 1_555 O D HOH 429 ? ? 4_575 2.12 
2 1 O A HOH 392 ? ? 1_555 O J HOH 368 ? ? 7_555 2.13 
# 
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 MET C 0   ? ? -52.65  -100.82 
2  1 ASN E 131 ? ? 175.15  165.87  
3  1 ASN F 26  ? ? -69.40  2.61    
4  1 SER G 25  ? ? -34.59  -28.10  
5  1 ASN G 26  ? ? -146.70 34.10   
6  1 ASN G 65  ? ? 55.46   70.39   
7  1 ASP G 124 ? ? -111.06 -160.60 
8  1 ASP G 125 ? ? -9.60   88.51   
9  1 LEU G 126 ? ? -109.76 -99.19  
10 1 LYS G 128 ? ? -144.53 31.94   
11 1 ALA I 55  ? ? -101.85 52.72   
12 1 ASN I 65  ? ? -145.32 59.86   
13 1 LYS I 128 ? ? -84.65  31.58   
14 1 ALA J 55  ? ? -106.69 43.38   
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? B HOH 432 ? 6.38 . 
2 1 O ? B HOH 433 ? 6.67 . 
3 1 O ? D HOH 445 ? 6.46 . 
# 
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 MET 0   ? CG  ? A MET 1   CG  
2  1 Y 1 A MET 0   ? SD  ? A MET 1   SD  
3  1 Y 1 A MET 0   ? CE  ? A MET 1   CE  
4  1 Y 1 B MET 0   ? CG  ? B MET 1   CG  
5  1 Y 1 B MET 0   ? SD  ? B MET 1   SD  
6  1 Y 1 B MET 0   ? CE  ? B MET 1   CE  
7  1 Y 1 D MET 0   ? CG  ? D MET 1   CG  
8  1 Y 1 D MET 0   ? SD  ? D MET 1   SD  
9  1 Y 1 D MET 0   ? CE  ? D MET 1   CE  
10 1 Y 1 E LYS 128 ? CG  ? E LYS 129 CG  
11 1 Y 1 E LYS 128 ? CD  ? E LYS 129 CD  
12 1 Y 1 E LYS 128 ? CE  ? E LYS 129 CE  
13 1 Y 1 E LYS 128 ? NZ  ? E LYS 129 NZ  
14 1 Y 1 F MET 0   ? CG  ? F MET 1   CG  
15 1 Y 1 F MET 0   ? SD  ? F MET 1   SD  
16 1 Y 1 F MET 0   ? CE  ? F MET 1   CE  
17 1 Y 1 G LYS 23  ? CG  ? G LYS 24  CG  
18 1 Y 1 G LYS 23  ? CD  ? G LYS 24  CD  
19 1 Y 1 G LYS 23  ? CE  ? G LYS 24  CE  
20 1 Y 1 G LYS 23  ? NZ  ? G LYS 24  NZ  
21 1 Y 1 G LEU 67  ? CG  ? G LEU 68  CG  
22 1 Y 1 G LEU 67  ? CD1 ? G LEU 68  CD1 
23 1 Y 1 G LEU 67  ? CD2 ? G LEU 68  CD2 
24 1 Y 1 G ASP 125 ? CG  ? G ASP 126 CG  
25 1 Y 1 G ASP 125 ? OD1 ? G ASP 126 OD1 
26 1 Y 1 G ASP 125 ? OD2 ? G ASP 126 OD2 
27 1 Y 1 G LEU 126 ? CG  ? G LEU 127 CG  
28 1 Y 1 G LEU 126 ? CD1 ? G LEU 127 CD1 
29 1 Y 1 G LEU 126 ? CD2 ? G LEU 127 CD2 
30 1 Y 1 G LYS 128 ? CG  ? G LYS 129 CG  
31 1 Y 1 G LYS 128 ? CD  ? G LYS 129 CD  
32 1 Y 1 G LYS 128 ? CE  ? G LYS 129 CE  
33 1 Y 1 G LYS 128 ? NZ  ? G LYS 129 NZ  
34 1 Y 1 G ASN 131 ? CG  ? G ASN 132 CG  
35 1 Y 1 G ASN 131 ? OD1 ? G ASN 132 OD1 
36 1 Y 1 G ASN 131 ? ND2 ? G ASN 132 ND2 
37 1 Y 1 I MET 0   ? CG  ? I MET 1   CG  
38 1 Y 1 I MET 0   ? SD  ? I MET 1   SD  
39 1 Y 1 I MET 0   ? CE  ? I MET 1   CE  
40 1 Y 0 I LYS 9   ? CD  ? I LYS 10  CD  
41 1 Y 0 I LYS 9   ? CE  ? I LYS 10  CE  
42 1 Y 0 I LYS 9   ? NZ  ? I LYS 10  NZ  
43 1 Y 1 I GLU 132 ? CG  ? I GLU 133 CG  
44 1 Y 1 I GLU 132 ? CD  ? I GLU 133 CD  
45 1 Y 1 I GLU 132 ? OE1 ? I GLU 133 OE1 
46 1 Y 1 I GLU 132 ? OE2 ? I GLU 133 OE2 
47 1 Y 1 J MET 0   ? CG  ? J MET 1   CG  
48 1 Y 1 J MET 0   ? SD  ? J MET 1   SD  
49 1 Y 1 J MET 0   ? CE  ? J MET 1   CE  
# 
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 G ALA 0   ? G ALA 1   
2  1 Y 1 G SER 68  ? G SER 69  
3  1 Y 1 G ARG 69  ? G ARG 70  
4  1 Y 1 G LYS 70  ? G LYS 71  
5  1 Y 1 G HIS 71  ? G HIS 72  
6  1 Y 1 G GLY 72  ? G GLY 73  
7  1 Y 1 G GLY 73  ? G GLY 74  
8  1 Y 1 G PRO 74  ? G PRO 75  
9  1 Y 1 G LYS 75  ? G LYS 76  
10 1 Y 1 G ASP 76  ? G ASP 77  
11 1 Y 1 G ALA 77  ? G ALA 78  
12 1 Y 1 G GLU 78  ? G GLU 79  
13 1 Y 1 G GLU 132 ? G GLU 133 
14 1 Y 1 G GLU 133 ? G GLU 134 
15 1 Y 1 G SER 134 ? G SER 135 
16 1 Y 1 G THR 135 ? G THR 136 
17 1 Y 1 G LYS 136 ? G LYS 137 
18 1 Y 1 G THR 137 ? G THR 138 
19 1 Y 1 G GLY 138 ? G GLY 139 
20 1 Y 1 G ASN 139 ? G ASN 140 
21 1 Y 1 G ALA 140 ? G ALA 141 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
GOL C1   C  N N 137 
GOL O1   O  N N 138 
GOL C2   C  N N 139 
GOL O2   O  N N 140 
GOL C3   C  N N 141 
GOL O3   O  N N 142 
GOL H11  H  N N 143 
GOL H12  H  N N 144 
GOL HO1  H  N N 145 
GOL H2   H  N N 146 
GOL HO2  H  N N 147 
GOL H31  H  N N 148 
GOL H32  H  N N 149 
GOL HO3  H  N N 150 
HIS N    N  N N 151 
HIS CA   C  N S 152 
HIS C    C  N N 153 
HIS O    O  N N 154 
HIS CB   C  N N 155 
HIS CG   C  Y N 156 
HIS ND1  N  Y N 157 
HIS CD2  C  Y N 158 
HIS CE1  C  Y N 159 
HIS NE2  N  Y N 160 
HIS OXT  O  N N 161 
HIS H    H  N N 162 
HIS H2   H  N N 163 
HIS HA   H  N N 164 
HIS HB2  H  N N 165 
HIS HB3  H  N N 166 
HIS HD1  H  N N 167 
HIS HD2  H  N N 168 
HIS HE1  H  N N 169 
HIS HE2  H  N N 170 
HIS HXT  H  N N 171 
HOH O    O  N N 172 
HOH H1   H  N N 173 
HOH H2   H  N N 174 
ILE N    N  N N 175 
ILE CA   C  N S 176 
ILE C    C  N N 177 
ILE O    O  N N 178 
ILE CB   C  N S 179 
ILE CG1  C  N N 180 
ILE CG2  C  N N 181 
ILE CD1  C  N N 182 
ILE OXT  O  N N 183 
ILE H    H  N N 184 
ILE H2   H  N N 185 
ILE HA   H  N N 186 
ILE HB   H  N N 187 
ILE HG12 H  N N 188 
ILE HG13 H  N N 189 
ILE HG21 H  N N 190 
ILE HG22 H  N N 191 
ILE HG23 H  N N 192 
ILE HD11 H  N N 193 
ILE HD12 H  N N 194 
ILE HD13 H  N N 195 
ILE HXT  H  N N 196 
K4I C1   C  N N 197 
K4I C2   C  N N 198 
K4I C3   C  N N 199 
K4I C4   C  N N 200 
K4I C5   C  N N 201 
K4I N1   N  N N 202 
K4I O1   O  Y N 203 
K4I O2   O  N N 204 
K4I N    N  N N 205 
K4I C    C  N N 206 
K4I O    O  N N 207 
K4I C10  C  Y N 208 
K4I C11  C  Y N 209 
K4I C12  C  Y N 210 
K4I C13  C  Y N 211 
K4I C14  C  Y N 212 
K4I C15  C  Y N 213 
K4I C16  C  N N 214 
K4I C17  C  N N 215 
K4I C18  C  N N 216 
K4I C19  C  N R 217 
K4I C20  C  N N 218 
K4I C21  C  N N 219 
K4I C22  C  N N 220 
K4I C6   C  N N 221 
K4I C7   C  N N 222 
K4I C8   C  N N 223 
K4I C9   C  Y N 224 
K4I F    F  N N 225 
K4I N2   N  N N 226 
K4I N3   N  Y N 227 
K4I H1   H  N N 228 
K4I H2   H  N N 229 
K4I H3   H  N N 230 
K4I H4   H  N N 231 
K4I H5   H  N N 232 
K4I H6   H  N N 233 
K4I H7   H  N N 234 
K4I H8   H  N N 235 
K4I H9   H  N N 236 
K4I H10  H  N N 237 
K4I H11  H  N N 238 
K4I H12  H  N N 239 
K4I H13  H  N N 240 
K4I H14  H  N N 241 
K4I H15  H  N N 242 
K4I H16  H  N N 243 
K4I H17  H  N N 244 
K4I H18  H  N N 245 
K4I H19  H  N N 246 
K4I H20  H  N N 247 
K4I H21  H  N N 248 
K4I H22  H  N N 249 
K4I H23  H  N N 250 
K4I H24  H  N N 251 
K4I H25  H  N N 252 
K4I H26  H  N N 253 
K4I H27  H  N N 254 
LEU N    N  N N 255 
LEU CA   C  N S 256 
LEU C    C  N N 257 
LEU O    O  N N 258 
LEU CB   C  N N 259 
LEU CG   C  N N 260 
LEU CD1  C  N N 261 
LEU CD2  C  N N 262 
LEU OXT  O  N N 263 
LEU H    H  N N 264 
LEU H2   H  N N 265 
LEU HA   H  N N 266 
LEU HB2  H  N N 267 
LEU HB3  H  N N 268 
LEU HG   H  N N 269 
LEU HD11 H  N N 270 
LEU HD12 H  N N 271 
LEU HD13 H  N N 272 
LEU HD21 H  N N 273 
LEU HD22 H  N N 274 
LEU HD23 H  N N 275 
LEU HXT  H  N N 276 
LYS N    N  N N 277 
LYS CA   C  N S 278 
LYS C    C  N N 279 
LYS O    O  N N 280 
LYS CB   C  N N 281 
LYS CG   C  N N 282 
LYS CD   C  N N 283 
LYS CE   C  N N 284 
LYS NZ   N  N N 285 
LYS OXT  O  N N 286 
LYS H    H  N N 287 
LYS H2   H  N N 288 
LYS HA   H  N N 289 
LYS HB2  H  N N 290 
LYS HB3  H  N N 291 
LYS HG2  H  N N 292 
LYS HG3  H  N N 293 
LYS HD2  H  N N 294 
LYS HD3  H  N N 295 
LYS HE2  H  N N 296 
LYS HE3  H  N N 297 
LYS HZ1  H  N N 298 
LYS HZ2  H  N N 299 
LYS HZ3  H  N N 300 
LYS HXT  H  N N 301 
MET N    N  N N 302 
MET CA   C  N S 303 
MET C    C  N N 304 
MET O    O  N N 305 
MET CB   C  N N 306 
MET CG   C  N N 307 
MET SD   S  N N 308 
MET CE   C  N N 309 
MET OXT  O  N N 310 
MET H    H  N N 311 
MET H2   H  N N 312 
MET HA   H  N N 313 
MET HB2  H  N N 314 
MET HB3  H  N N 315 
MET HG2  H  N N 316 
MET HG3  H  N N 317 
MET HE1  H  N N 318 
MET HE2  H  N N 319 
MET HE3  H  N N 320 
MET HXT  H  N N 321 
PHE N    N  N N 322 
PHE CA   C  N S 323 
PHE C    C  N N 324 
PHE O    O  N N 325 
PHE CB   C  N N 326 
PHE CG   C  Y N 327 
PHE CD1  C  Y N 328 
PHE CD2  C  Y N 329 
PHE CE1  C  Y N 330 
PHE CE2  C  Y N 331 
PHE CZ   C  Y N 332 
PHE OXT  O  N N 333 
PHE H    H  N N 334 
PHE H2   H  N N 335 
PHE HA   H  N N 336 
PHE HB2  H  N N 337 
PHE HB3  H  N N 338 
PHE HD1  H  N N 339 
PHE HD2  H  N N 340 
PHE HE1  H  N N 341 
PHE HE2  H  N N 342 
PHE HZ   H  N N 343 
PHE HXT  H  N N 344 
PRO N    N  N N 345 
PRO CA   C  N S 346 
PRO C    C  N N 347 
PRO O    O  N N 348 
PRO CB   C  N N 349 
PRO CG   C  N N 350 
PRO CD   C  N N 351 
PRO OXT  O  N N 352 
PRO H    H  N N 353 
PRO HA   H  N N 354 
PRO HB2  H  N N 355 
PRO HB3  H  N N 356 
PRO HG2  H  N N 357 
PRO HG3  H  N N 358 
PRO HD2  H  N N 359 
PRO HD3  H  N N 360 
PRO HXT  H  N N 361 
SER N    N  N N 362 
SER CA   C  N S 363 
SER C    C  N N 364 
SER O    O  N N 365 
SER CB   C  N N 366 
SER OG   O  N N 367 
SER OXT  O  N N 368 
SER H    H  N N 369 
SER H2   H  N N 370 
SER HA   H  N N 371 
SER HB2  H  N N 372 
SER HB3  H  N N 373 
SER HG   H  N N 374 
SER HXT  H  N N 375 
THR N    N  N N 376 
THR CA   C  N S 377 
THR C    C  N N 378 
THR O    O  N N 379 
THR CB   C  N R 380 
THR OG1  O  N N 381 
THR CG2  C  N N 382 
THR OXT  O  N N 383 
THR H    H  N N 384 
THR H2   H  N N 385 
THR HA   H  N N 386 
THR HB   H  N N 387 
THR HG1  H  N N 388 
THR HG21 H  N N 389 
THR HG22 H  N N 390 
THR HG23 H  N N 391 
THR HXT  H  N N 392 
TRP N    N  N N 393 
TRP CA   C  N S 394 
TRP C    C  N N 395 
TRP O    O  N N 396 
TRP CB   C  N N 397 
TRP CG   C  Y N 398 
TRP CD1  C  Y N 399 
TRP CD2  C  Y N 400 
TRP NE1  N  Y N 401 
TRP CE2  C  Y N 402 
TRP CE3  C  Y N 403 
TRP CZ2  C  Y N 404 
TRP CZ3  C  Y N 405 
TRP CH2  C  Y N 406 
TRP OXT  O  N N 407 
TRP H    H  N N 408 
TRP H2   H  N N 409 
TRP HA   H  N N 410 
TRP HB2  H  N N 411 
TRP HB3  H  N N 412 
TRP HD1  H  N N 413 
TRP HE1  H  N N 414 
TRP HE3  H  N N 415 
TRP HZ2  H  N N 416 
TRP HZ3  H  N N 417 
TRP HH2  H  N N 418 
TRP HXT  H  N N 419 
VAL N    N  N N 420 
VAL CA   C  N S 421 
VAL C    C  N N 422 
VAL O    O  N N 423 
VAL CB   C  N N 424 
VAL CG1  C  N N 425 
VAL CG2  C  N N 426 
VAL OXT  O  N N 427 
VAL H    H  N N 428 
VAL H2   H  N N 429 
VAL HA   H  N N 430 
VAL HB   H  N N 431 
VAL HG11 H  N N 432 
VAL HG12 H  N N 433 
VAL HG13 H  N N 434 
VAL HG21 H  N N 435 
VAL HG22 H  N N 436 
VAL HG23 H  N N 437 
VAL HXT  H  N N 438 
ZN  ZN   ZN N N 439 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
K4I C20 C21  sing N N 186 
K4I C20 C19  sing N N 187 
K4I C21 C22  sing N N 188 
K4I O2  C19  sing N N 189 
K4I C19 C1   sing N N 190 
K4I C22 N    sing N N 191 
K4I C1  N    sing N N 192 
K4I C1  N1   doub N N 193 
K4I N   C    sing N N 194 
K4I N1  C2   sing N N 195 
K4I C   O    doub N N 196 
K4I C   C3   sing N N 197 
K4I C2  C3   doub N N 198 
K4I C2  C18  sing N N 199 
K4I C3  C4   sing N N 200 
K4I C4  C5   sing N N 201 
K4I C5  N2   sing N N 202 
K4I C17 N2   sing N N 203 
K4I C17 C16  sing N N 204 
K4I N2  C6   sing N N 205 
K4I C16 C8   sing N N 206 
K4I C6  C7   sing N N 207 
K4I C8  C7   sing N N 208 
K4I C8  C9   sing N N 209 
K4I C9  N3   doub Y N 210 
K4I C9  C15  sing Y N 211 
K4I N3  O1   sing Y N 212 
K4I C15 C14  sing Y N 213 
K4I C15 C10  doub Y N 214 
K4I C14 C13  doub Y N 215 
K4I O1  C10  sing Y N 216 
K4I C10 C11  sing Y N 217 
K4I C13 C12  sing Y N 218 
K4I C11 C12  doub Y N 219 
K4I C12 F    sing N N 220 
K4I C4  H1   sing N N 221 
K4I C4  H2   sing N N 222 
K4I C5  H3   sing N N 223 
K4I C5  H4   sing N N 224 
K4I O2  H5   sing N N 225 
K4I C11 H6   sing N N 226 
K4I C13 H7   sing N N 227 
K4I C14 H8   sing N N 228 
K4I C16 H9   sing N N 229 
K4I C16 H10  sing N N 230 
K4I C17 H11  sing N N 231 
K4I C17 H12  sing N N 232 
K4I C18 H13  sing N N 233 
K4I C18 H14  sing N N 234 
K4I C18 H15  sing N N 235 
K4I C19 H16  sing N N 236 
K4I C20 H17  sing N N 237 
K4I C20 H18  sing N N 238 
K4I C21 H19  sing N N 239 
K4I C21 H20  sing N N 240 
K4I C22 H21  sing N N 241 
K4I C22 H22  sing N N 242 
K4I C6  H23  sing N N 243 
K4I C6  H24  sing N N 244 
K4I C7  H25  sing N N 245 
K4I C7  H26  sing N N 246 
K4I C8  H27  sing N N 247 
LEU N   CA   sing N N 248 
LEU N   H    sing N N 249 
LEU N   H2   sing N N 250 
LEU CA  C    sing N N 251 
LEU CA  CB   sing N N 252 
LEU CA  HA   sing N N 253 
LEU C   O    doub N N 254 
LEU C   OXT  sing N N 255 
LEU CB  CG   sing N N 256 
LEU CB  HB2  sing N N 257 
LEU CB  HB3  sing N N 258 
LEU CG  CD1  sing N N 259 
LEU CG  CD2  sing N N 260 
LEU CG  HG   sing N N 261 
LEU CD1 HD11 sing N N 262 
LEU CD1 HD12 sing N N 263 
LEU CD1 HD13 sing N N 264 
LEU CD2 HD21 sing N N 265 
LEU CD2 HD22 sing N N 266 
LEU CD2 HD23 sing N N 267 
LEU OXT HXT  sing N N 268 
LYS N   CA   sing N N 269 
LYS N   H    sing N N 270 
LYS N   H2   sing N N 271 
LYS CA  C    sing N N 272 
LYS CA  CB   sing N N 273 
LYS CA  HA   sing N N 274 
LYS C   O    doub N N 275 
LYS C   OXT  sing N N 276 
LYS CB  CG   sing N N 277 
LYS CB  HB2  sing N N 278 
LYS CB  HB3  sing N N 279 
LYS CG  CD   sing N N 280 
LYS CG  HG2  sing N N 281 
LYS CG  HG3  sing N N 282 
LYS CD  CE   sing N N 283 
LYS CD  HD2  sing N N 284 
LYS CD  HD3  sing N N 285 
LYS CE  NZ   sing N N 286 
LYS CE  HE2  sing N N 287 
LYS CE  HE3  sing N N 288 
LYS NZ  HZ1  sing N N 289 
LYS NZ  HZ2  sing N N 290 
LYS NZ  HZ3  sing N N 291 
LYS OXT HXT  sing N N 292 
MET N   CA   sing N N 293 
MET N   H    sing N N 294 
MET N   H2   sing N N 295 
MET CA  C    sing N N 296 
MET CA  CB   sing N N 297 
MET CA  HA   sing N N 298 
MET C   O    doub N N 299 
MET C   OXT  sing N N 300 
MET CB  CG   sing N N 301 
MET CB  HB2  sing N N 302 
MET CB  HB3  sing N N 303 
MET CG  SD   sing N N 304 
MET CG  HG2  sing N N 305 
MET CG  HG3  sing N N 306 
MET SD  CE   sing N N 307 
MET CE  HE1  sing N N 308 
MET CE  HE2  sing N N 309 
MET CE  HE3  sing N N 310 
MET OXT HXT  sing N N 311 
PHE N   CA   sing N N 312 
PHE N   H    sing N N 313 
PHE N   H2   sing N N 314 
PHE CA  C    sing N N 315 
PHE CA  CB   sing N N 316 
PHE CA  HA   sing N N 317 
PHE C   O    doub N N 318 
PHE C   OXT  sing N N 319 
PHE CB  CG   sing N N 320 
PHE CB  HB2  sing N N 321 
PHE CB  HB3  sing N N 322 
PHE CG  CD1  doub Y N 323 
PHE CG  CD2  sing Y N 324 
PHE CD1 CE1  sing Y N 325 
PHE CD1 HD1  sing N N 326 
PHE CD2 CE2  doub Y N 327 
PHE CD2 HD2  sing N N 328 
PHE CE1 CZ   doub Y N 329 
PHE CE1 HE1  sing N N 330 
PHE CE2 CZ   sing Y N 331 
PHE CE2 HE2  sing N N 332 
PHE CZ  HZ   sing N N 333 
PHE OXT HXT  sing N N 334 
PRO N   CA   sing N N 335 
PRO N   CD   sing N N 336 
PRO N   H    sing N N 337 
PRO CA  C    sing N N 338 
PRO CA  CB   sing N N 339 
PRO CA  HA   sing N N 340 
PRO C   O    doub N N 341 
PRO C   OXT  sing N N 342 
PRO CB  CG   sing N N 343 
PRO CB  HB2  sing N N 344 
PRO CB  HB3  sing N N 345 
PRO CG  CD   sing N N 346 
PRO CG  HG2  sing N N 347 
PRO CG  HG3  sing N N 348 
PRO CD  HD2  sing N N 349 
PRO CD  HD3  sing N N 350 
PRO OXT HXT  sing N N 351 
SER N   CA   sing N N 352 
SER N   H    sing N N 353 
SER N   H2   sing N N 354 
SER CA  C    sing N N 355 
SER CA  CB   sing N N 356 
SER CA  HA   sing N N 357 
SER C   O    doub N N 358 
SER C   OXT  sing N N 359 
SER CB  OG   sing N N 360 
SER CB  HB2  sing N N 361 
SER CB  HB3  sing N N 362 
SER OG  HG   sing N N 363 
SER OXT HXT  sing N N 364 
THR N   CA   sing N N 365 
THR N   H    sing N N 366 
THR N   H2   sing N N 367 
THR CA  C    sing N N 368 
THR CA  CB   sing N N 369 
THR CA  HA   sing N N 370 
THR C   O    doub N N 371 
THR C   OXT  sing N N 372 
THR CB  OG1  sing N N 373 
THR CB  CG2  sing N N 374 
THR CB  HB   sing N N 375 
THR OG1 HG1  sing N N 376 
THR CG2 HG21 sing N N 377 
THR CG2 HG22 sing N N 378 
THR CG2 HG23 sing N N 379 
THR OXT HXT  sing N N 380 
TRP N   CA   sing N N 381 
TRP N   H    sing N N 382 
TRP N   H2   sing N N 383 
TRP CA  C    sing N N 384 
TRP CA  CB   sing N N 385 
TRP CA  HA   sing N N 386 
TRP C   O    doub N N 387 
TRP C   OXT  sing N N 388 
TRP CB  CG   sing N N 389 
TRP CB  HB2  sing N N 390 
TRP CB  HB3  sing N N 391 
TRP CG  CD1  doub Y N 392 
TRP CG  CD2  sing Y N 393 
TRP CD1 NE1  sing Y N 394 
TRP CD1 HD1  sing N N 395 
TRP CD2 CE2  doub Y N 396 
TRP CD2 CE3  sing Y N 397 
TRP NE1 CE2  sing Y N 398 
TRP NE1 HE1  sing N N 399 
TRP CE2 CZ2  sing Y N 400 
TRP CE3 CZ3  doub Y N 401 
TRP CE3 HE3  sing N N 402 
TRP CZ2 CH2  doub Y N 403 
TRP CZ2 HZ2  sing N N 404 
TRP CZ3 CH2  sing Y N 405 
TRP CZ3 HZ3  sing N N 406 
TRP CH2 HH2  sing N N 407 
TRP OXT HXT  sing N N 408 
VAL N   CA   sing N N 409 
VAL N   H    sing N N 410 
VAL N   H2   sing N N 411 
VAL CA  C    sing N N 412 
VAL CA  CB   sing N N 413 
VAL CA  HA   sing N N 414 
VAL C   O    doub N N 415 
VAL C   OXT  sing N N 416 
VAL CB  CG1  sing N N 417 
VAL CB  CG2  sing N N 418 
VAL CB  HB   sing N N 419 
VAL CG1 HG11 sing N N 420 
VAL CG1 HG12 sing N N 421 
VAL CG1 HG13 sing N N 422 
VAL CG2 HG21 sing N N 423 
VAL CG2 HG22 sing N N 424 
VAL CG2 HG23 sing N N 425 
VAL OXT HXT  sing N N 426 
# 
_pdbx_audit_support.funding_organization   'Indian Council of Medical Research' 
_pdbx_audit_support.country                India 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        K4I 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   K4I 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
5 'ZINC ION' ZN  
6 GLYCEROL GOL 
7 
;(9~{R})-3-[2-[4-(6-fluoranyl-1,2-benzoxazol-3-yl)piperidin-1-yl]ethyl]-2-methyl-9-oxidanyl-6,7,8,9-tetrahydropyrido[1,2-a]pyrimidin-4-one
;
K4I 
8 water HOH 
# 
_pdbx_initial_refinement_model.accession_code   6a9o 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_space_group.name_H-M_alt     'C 2 2 21' 
_space_group.name_Hall        'C 2c 2' 
_space_group.IT_number        20 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
